HEADER    SIGNALING PROTEIN                       09-MAY-11   3AYM              
TITLE     CRYSTAL STRUCTURE OF THE BATHO INTERMEDIATE OF SQUID RHODOPSIN        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHODOPSIN;                                                 
COMPND   3 CHAIN: A, B                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TODARODES PACIFICUS;                            
SOURCE   3 ORGANISM_COMMON: JAPANESE FLYING SQUID;                              
SOURCE   4 ORGANISM_TAXID: 6637                                                 
KEYWDS    TRANSMEMBRANE PROTEIN, PHOTORECEPTOR, CHROMOPHORE, GLYCOPROTEIN,      
KEYWDS   2 LIPOPROTEIN, GQ-TYPE G-PROTEIN, PHOSPHORYLATION, MEMBRANE, SIGNALING 
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MURAKAMI,T.KOUYAMA                                                  
REVDAT   4   29-JUL-20 3AYM    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   11-OCT-17 3AYM    1       REMARK                                   
REVDAT   2   26-OCT-11 3AYM    1       JRNL                                     
REVDAT   1   17-AUG-11 3AYM    0                                                
JRNL        AUTH   M.MURAKAMI,T.KOUYAMA                                         
JRNL        TITL   CRYSTALLOGRAPHIC ANALYSIS OF THE PRIMARY PHOTOCHEMICAL       
JRNL        TITL 2 REACTION OF SQUID RHODOPSIN                                  
JRNL        REF    J.MOL.BIOL.                   V. 413   615 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21906602                                                     
JRNL        DOI    10.1016/J.JMB.2011.08.044                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2354525.720                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 67.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22229                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.295                           
REMARK   3   FREE R VALUE                     : 0.345                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1080                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3377                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5340                       
REMARK   3   BIN FREE R VALUE                    : 0.5470                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 178                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.041                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5542                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 141                                     
REMARK   3   SOLVENT ATOMS            : 59                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -10.27200                                            
REMARK   3    B22 (A**2) : -10.27200                                            
REMARK   3    B33 (A**2) : 20.54500                                             
REMARK   3    B12 (A**2) : -14.46900                                            
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.61                            
REMARK   3   ESD FROM SIGMAA              (A) : 1.02                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.64                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.06                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.821 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.048 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.639 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.100 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 59.19                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : RET-TRANS.PARAM                                
REMARK   3  PARAMETER FILE  5  : BOG.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3AYM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000029857.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW14A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31468                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 88.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2Z73                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2M AMMONIUM SULFATE, 20MM MES, 75MM    
REMARK 280  EDTA, 10MM BETA-MERCAPTOETHANOL, PH 6.6, VAPOR DIFFUSION,           
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.48000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       52.74000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      105.48000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       52.74000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     SER A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 465     ASP A   361                                                      
REMARK 465     ALA A   362                                                      
REMARK 465     ALA A   363                                                      
REMARK 465     PRO A   364                                                      
REMARK 465     SER A   365                                                      
REMARK 465     ALA A   366                                                      
REMARK 465     ASP A   367                                                      
REMARK 465     ALA A   368                                                      
REMARK 465     ALA A   369                                                      
REMARK 465     GLN A   370                                                      
REMARK 465     MET A   371                                                      
REMARK 465     LYS A   372                                                      
REMARK 465     GLU A   373                                                      
REMARK 465     MET A   374                                                      
REMARK 465     MET A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     MET A   377                                                      
REMARK 465     MET A   378                                                      
REMARK 465     GLN A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     MET A   381                                                      
REMARK 465     GLN A   382                                                      
REMARK 465     GLN A   383                                                      
REMARK 465     GLN A   384                                                      
REMARK 465     GLN A   385                                                      
REMARK 465     ALA A   386                                                      
REMARK 465     ALA A   387                                                      
REMARK 465     TYR A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     PRO A   390                                                      
REMARK 465     GLN A   391                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     TYR A   393                                                      
REMARK 465     ALA A   394                                                      
REMARK 465     PRO A   395                                                      
REMARK 465     PRO A   396                                                      
REMARK 465     PRO A   397                                                      
REMARK 465     GLN A   398                                                      
REMARK 465     GLY A   399                                                      
REMARK 465     TYR A   400                                                      
REMARK 465     PRO A   401                                                      
REMARK 465     PRO A   402                                                      
REMARK 465     GLN A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     TYR A   405                                                      
REMARK 465     PRO A   406                                                      
REMARK 465     PRO A   407                                                      
REMARK 465     GLN A   408                                                      
REMARK 465     GLY A   409                                                      
REMARK 465     TYR A   410                                                      
REMARK 465     PRO A   411                                                      
REMARK 465     PRO A   412                                                      
REMARK 465     GLN A   413                                                      
REMARK 465     GLY A   414                                                      
REMARK 465     TYR A   415                                                      
REMARK 465     PRO A   416                                                      
REMARK 465     PRO A   417                                                      
REMARK 465     GLN A   418                                                      
REMARK 465     GLY A   419                                                      
REMARK 465     TYR A   420                                                      
REMARK 465     PRO A   421                                                      
REMARK 465     PRO A   422                                                      
REMARK 465     PRO A   423                                                      
REMARK 465     PRO A   424                                                      
REMARK 465     GLN A   425                                                      
REMARK 465     GLY A   426                                                      
REMARK 465     ALA A   427                                                      
REMARK 465     PRO A   428                                                      
REMARK 465     PRO A   429                                                      
REMARK 465     GLN A   430                                                      
REMARK 465     GLY A   431                                                      
REMARK 465     ALA A   432                                                      
REMARK 465     PRO A   433                                                      
REMARK 465     PRO A   434                                                      
REMARK 465     ALA A   435                                                      
REMARK 465     ALA A   436                                                      
REMARK 465     PRO A   437                                                      
REMARK 465     PRO A   438                                                      
REMARK 465     GLN A   439                                                      
REMARK 465     GLY A   440                                                      
REMARK 465     VAL A   441                                                      
REMARK 465     ASP A   442                                                      
REMARK 465     ASN A   443                                                      
REMARK 465     GLN A   444                                                      
REMARK 465     ALA A   445                                                      
REMARK 465     TYR A   446                                                      
REMARK 465     GLN A   447                                                      
REMARK 465     ALA A   448                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     ALA B   356                                                      
REMARK 465     GLY B   357                                                      
REMARK 465     GLU B   358                                                      
REMARK 465     SER B   359                                                      
REMARK 465     SER B   360                                                      
REMARK 465     ASP B   361                                                      
REMARK 465     ALA B   362                                                      
REMARK 465     ALA B   363                                                      
REMARK 465     PRO B   364                                                      
REMARK 465     SER B   365                                                      
REMARK 465     ALA B   366                                                      
REMARK 465     ASP B   367                                                      
REMARK 465     ALA B   368                                                      
REMARK 465     ALA B   369                                                      
REMARK 465     GLN B   370                                                      
REMARK 465     MET B   371                                                      
REMARK 465     LYS B   372                                                      
REMARK 465     GLU B   373                                                      
REMARK 465     MET B   374                                                      
REMARK 465     MET B   375                                                      
REMARK 465     ALA B   376                                                      
REMARK 465     MET B   377                                                      
REMARK 465     MET B   378                                                      
REMARK 465     GLN B   379                                                      
REMARK 465     LYS B   380                                                      
REMARK 465     MET B   381                                                      
REMARK 465     GLN B   382                                                      
REMARK 465     GLN B   383                                                      
REMARK 465     GLN B   384                                                      
REMARK 465     GLN B   385                                                      
REMARK 465     ALA B   386                                                      
REMARK 465     ALA B   387                                                      
REMARK 465     TYR B   388                                                      
REMARK 465     PRO B   389                                                      
REMARK 465     PRO B   390                                                      
REMARK 465     GLN B   391                                                      
REMARK 465     GLY B   392                                                      
REMARK 465     TYR B   393                                                      
REMARK 465     ALA B   394                                                      
REMARK 465     PRO B   395                                                      
REMARK 465     PRO B   396                                                      
REMARK 465     PRO B   397                                                      
REMARK 465     GLN B   398                                                      
REMARK 465     GLY B   399                                                      
REMARK 465     TYR B   400                                                      
REMARK 465     PRO B   401                                                      
REMARK 465     PRO B   402                                                      
REMARK 465     GLN B   403                                                      
REMARK 465     GLY B   404                                                      
REMARK 465     TYR B   405                                                      
REMARK 465     PRO B   406                                                      
REMARK 465     PRO B   407                                                      
REMARK 465     GLN B   408                                                      
REMARK 465     GLY B   409                                                      
REMARK 465     TYR B   410                                                      
REMARK 465     PRO B   411                                                      
REMARK 465     PRO B   412                                                      
REMARK 465     GLN B   413                                                      
REMARK 465     GLY B   414                                                      
REMARK 465     TYR B   415                                                      
REMARK 465     PRO B   416                                                      
REMARK 465     PRO B   417                                                      
REMARK 465     GLN B   418                                                      
REMARK 465     GLY B   419                                                      
REMARK 465     TYR B   420                                                      
REMARK 465     PRO B   421                                                      
REMARK 465     PRO B   422                                                      
REMARK 465     PRO B   423                                                      
REMARK 465     PRO B   424                                                      
REMARK 465     GLN B   425                                                      
REMARK 465     GLY B   426                                                      
REMARK 465     ALA B   427                                                      
REMARK 465     PRO B   428                                                      
REMARK 465     PRO B   429                                                      
REMARK 465     GLN B   430                                                      
REMARK 465     GLY B   431                                                      
REMARK 465     ALA B   432                                                      
REMARK 465     PRO B   433                                                      
REMARK 465     PRO B   434                                                      
REMARK 465     ALA B   435                                                      
REMARK 465     ALA B   436                                                      
REMARK 465     PRO B   437                                                      
REMARK 465     PRO B   438                                                      
REMARK 465     GLN B   439                                                      
REMARK 465     GLY B   440                                                      
REMARK 465     VAL B   441                                                      
REMARK 465     ASP B   442                                                      
REMARK 465     ASN B   443                                                      
REMARK 465     GLN B   444                                                      
REMARK 465     ALA B   445                                                      
REMARK 465     TYR B   446                                                      
REMARK 465     GLN B   447                                                      
REMARK 465     ALA B   448                                                      
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   OD1  ASN A   185     O    HOH A   500              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  27   CB  -  CG  -  OD2 ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    PRO A 331   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    PRO A 331   C   -  N   -  CD  ANGL. DEV. = -14.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  65       38.95    -90.22                                   
REMARK 500    LYS A 100      131.50    178.27                                   
REMARK 500    MET A 141      -36.87    -33.92                                   
REMARK 500    ALA A 176      144.47   -173.61                                   
REMARK 500    PHE A 209      -69.65    -99.84                                   
REMARK 500    MET A 225       41.37    -78.58                                   
REMARK 500    SER A 226       -1.38   -159.25                                   
REMARK 500    LEU A 241       28.42     31.39                                   
REMARK 500    ALA A 243     -171.52    -48.97                                   
REMARK 500    PRO A 288       91.48    -69.09                                   
REMARK 500    VAL A 292       79.37    -56.07                                   
REMARK 500    ALA A 308        3.34    -66.22                                   
REMARK 500    SER A 318       -7.02   -140.72                                   
REMARK 500    PRO A 331      -12.50    -43.45                                   
REMARK 500    THR A 335      -75.09    -52.74                                   
REMARK 500    GLN A 338      134.74    -37.83                                   
REMARK 500    THR A 352       77.78    -62.65                                   
REMARK 500    ALA A 356       68.08     61.53                                   
REMARK 500    PHE B  26     -145.16    -84.55                                   
REMARK 500    ASP B  31      -38.74    -38.70                                   
REMARK 500    THR B  62      106.71    -54.69                                   
REMARK 500    LYS B 100      136.42   -175.67                                   
REMARK 500    ILE B 223      -73.21    -60.27                                   
REMARK 500    SER B 226      -13.31   -165.32                                   
REMARK 500    ALA B 236        6.14    -68.16                                   
REMARK 500    ALA B 243      -92.68   -101.20                                   
REMARK 500    SER B 318      -25.81   -151.74                                   
REMARK 500    THR B 329      -45.94   -138.46                                   
REMARK 500    THR B 352      106.30    -57.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PLM A 1001                                                       
REMARK 610     PC1 B 1004                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2Z73   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3AYN   RELATED DB: PDB                                   
DBREF  3AYM A    1   448  UNP    P31356   OPSD_TODPA       1    448             
DBREF  3AYM B    1   448  UNP    P31356   OPSD_TODPA       1    448             
SEQRES   1 A  448  MET GLY ARG ASP LEU ARG ASP ASN GLU THR TRP TRP TYR          
SEQRES   2 A  448  ASN PRO SER ILE VAL VAL HIS PRO HIS TRP ARG GLU PHE          
SEQRES   3 A  448  ASP GLN VAL PRO ASP ALA VAL TYR TYR SER LEU GLY ILE          
SEQRES   4 A  448  PHE ILE GLY ILE CYS GLY ILE ILE GLY CYS GLY GLY ASN          
SEQRES   5 A  448  GLY ILE VAL ILE TYR LEU PHE THR LYS THR LYS SER LEU          
SEQRES   6 A  448  GLN THR PRO ALA ASN MET PHE ILE ILE ASN LEU ALA PHE          
SEQRES   7 A  448  SER ASP PHE THR PHE SER LEU VAL ASN GLY PHE PRO LEU          
SEQRES   8 A  448  MET THR ILE SER CYS PHE LEU LYS LYS TRP ILE PHE GLY          
SEQRES   9 A  448  PHE ALA ALA CYS LYS VAL TYR GLY PHE ILE GLY GLY ILE          
SEQRES  10 A  448  PHE GLY PHE MET SER ILE MET THR MET ALA MET ILE SER          
SEQRES  11 A  448  ILE ASP ARG TYR ASN VAL ILE GLY ARG PRO MET ALA ALA          
SEQRES  12 A  448  SER LYS LYS MET SER HIS ARG ARG ALA PHE ILE MET ILE          
SEQRES  13 A  448  ILE PHE VAL TRP LEU TRP SER VAL LEU TRP ALA ILE GLY          
SEQRES  14 A  448  PRO ILE PHE GLY TRP GLY ALA TYR THR LEU GLU GLY VAL          
SEQRES  15 A  448  LEU CYS ASN CYS SER PHE ASP TYR ILE SER ARG ASP SER          
SEQRES  16 A  448  THR THR ARG SER ASN ILE LEU CYS MET PHE ILE LEU GLY          
SEQRES  17 A  448  PHE PHE GLY PRO ILE LEU ILE ILE PHE PHE CYS TYR PHE          
SEQRES  18 A  448  ASN ILE VAL MET SER VAL SER ASN HIS GLU LYS GLU MET          
SEQRES  19 A  448  ALA ALA MET ALA LYS ARG LEU ASN ALA LYS GLU LEU ARG          
SEQRES  20 A  448  LYS ALA GLN ALA GLY ALA ASN ALA GLU MET ARG LEU ALA          
SEQRES  21 A  448  LYS ILE SER ILE VAL ILE VAL SER GLN PHE LEU LEU SER          
SEQRES  22 A  448  TRP SER PRO TYR ALA VAL VAL ALA LEU LEU ALA GLN PHE          
SEQRES  23 A  448  GLY PRO LEU GLU TRP VAL THR PRO TYR ALA ALA GLN LEU          
SEQRES  24 A  448  PRO VAL MET PHE ALA LYS ALA SER ALA ILE HIS ASN PRO          
SEQRES  25 A  448  MET ILE TYR SER VAL SER HIS PRO LYS PHE ARG GLU ALA          
SEQRES  26 A  448  ILE SER GLN THR PHE PRO TRP VAL LEU THR CYS CYS GLN          
SEQRES  27 A  448  PHE ASP ASP LYS GLU THR GLU ASP ASP LYS ASP ALA GLU          
SEQRES  28 A  448  THR GLU ILE PRO ALA GLY GLU SER SER ASP ALA ALA PRO          
SEQRES  29 A  448  SER ALA ASP ALA ALA GLN MET LYS GLU MET MET ALA MET          
SEQRES  30 A  448  MET GLN LYS MET GLN GLN GLN GLN ALA ALA TYR PRO PRO          
SEQRES  31 A  448  GLN GLY TYR ALA PRO PRO PRO GLN GLY TYR PRO PRO GLN          
SEQRES  32 A  448  GLY TYR PRO PRO GLN GLY TYR PRO PRO GLN GLY TYR PRO          
SEQRES  33 A  448  PRO GLN GLY TYR PRO PRO PRO PRO GLN GLY ALA PRO PRO          
SEQRES  34 A  448  GLN GLY ALA PRO PRO ALA ALA PRO PRO GLN GLY VAL ASP          
SEQRES  35 A  448  ASN GLN ALA TYR GLN ALA                                      
SEQRES   1 B  448  MET GLY ARG ASP LEU ARG ASP ASN GLU THR TRP TRP TYR          
SEQRES   2 B  448  ASN PRO SER ILE VAL VAL HIS PRO HIS TRP ARG GLU PHE          
SEQRES   3 B  448  ASP GLN VAL PRO ASP ALA VAL TYR TYR SER LEU GLY ILE          
SEQRES   4 B  448  PHE ILE GLY ILE CYS GLY ILE ILE GLY CYS GLY GLY ASN          
SEQRES   5 B  448  GLY ILE VAL ILE TYR LEU PHE THR LYS THR LYS SER LEU          
SEQRES   6 B  448  GLN THR PRO ALA ASN MET PHE ILE ILE ASN LEU ALA PHE          
SEQRES   7 B  448  SER ASP PHE THR PHE SER LEU VAL ASN GLY PHE PRO LEU          
SEQRES   8 B  448  MET THR ILE SER CYS PHE LEU LYS LYS TRP ILE PHE GLY          
SEQRES   9 B  448  PHE ALA ALA CYS LYS VAL TYR GLY PHE ILE GLY GLY ILE          
SEQRES  10 B  448  PHE GLY PHE MET SER ILE MET THR MET ALA MET ILE SER          
SEQRES  11 B  448  ILE ASP ARG TYR ASN VAL ILE GLY ARG PRO MET ALA ALA          
SEQRES  12 B  448  SER LYS LYS MET SER HIS ARG ARG ALA PHE ILE MET ILE          
SEQRES  13 B  448  ILE PHE VAL TRP LEU TRP SER VAL LEU TRP ALA ILE GLY          
SEQRES  14 B  448  PRO ILE PHE GLY TRP GLY ALA TYR THR LEU GLU GLY VAL          
SEQRES  15 B  448  LEU CYS ASN CYS SER PHE ASP TYR ILE SER ARG ASP SER          
SEQRES  16 B  448  THR THR ARG SER ASN ILE LEU CYS MET PHE ILE LEU GLY          
SEQRES  17 B  448  PHE PHE GLY PRO ILE LEU ILE ILE PHE PHE CYS TYR PHE          
SEQRES  18 B  448  ASN ILE VAL MET SER VAL SER ASN HIS GLU LYS GLU MET          
SEQRES  19 B  448  ALA ALA MET ALA LYS ARG LEU ASN ALA LYS GLU LEU ARG          
SEQRES  20 B  448  LYS ALA GLN ALA GLY ALA ASN ALA GLU MET ARG LEU ALA          
SEQRES  21 B  448  LYS ILE SER ILE VAL ILE VAL SER GLN PHE LEU LEU SER          
SEQRES  22 B  448  TRP SER PRO TYR ALA VAL VAL ALA LEU LEU ALA GLN PHE          
SEQRES  23 B  448  GLY PRO LEU GLU TRP VAL THR PRO TYR ALA ALA GLN LEU          
SEQRES  24 B  448  PRO VAL MET PHE ALA LYS ALA SER ALA ILE HIS ASN PRO          
SEQRES  25 B  448  MET ILE TYR SER VAL SER HIS PRO LYS PHE ARG GLU ALA          
SEQRES  26 B  448  ILE SER GLN THR PHE PRO TRP VAL LEU THR CYS CYS GLN          
SEQRES  27 B  448  PHE ASP ASP LYS GLU THR GLU ASP ASP LYS ASP ALA GLU          
SEQRES  28 B  448  THR GLU ILE PRO ALA GLY GLU SER SER ASP ALA ALA PRO          
SEQRES  29 B  448  SER ALA ASP ALA ALA GLN MET LYS GLU MET MET ALA MET          
SEQRES  30 B  448  MET GLN LYS MET GLN GLN GLN GLN ALA ALA TYR PRO PRO          
SEQRES  31 B  448  GLN GLY TYR ALA PRO PRO PRO GLN GLY TYR PRO PRO GLN          
SEQRES  32 B  448  GLY TYR PRO PRO GLN GLY TYR PRO PRO GLN GLY TYR PRO          
SEQRES  33 B  448  PRO GLN GLY TYR PRO PRO PRO PRO GLN GLY ALA PRO PRO          
SEQRES  34 B  448  GLN GLY ALA PRO PRO ALA ALA PRO PRO GLN GLY VAL ASP          
SEQRES  35 B  448  ASN GLN ALA TYR GLN ALA                                      
HET    PLM  A1001      17                                                       
HET    BOG  A1005      20                                                       
HET    RET  A1000      20                                                       
HET    SO4  B 449       5                                                       
HET    PC1  B1004      39                                                       
HET    BOG  B1005      20                                                       
HET    RET  B1000      20                                                       
HETNAM     PLM PALMITIC ACID                                                    
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE                                     
HETNAM     RET RETINAL                                                          
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE                           
HETSYN     PC1 3-SN-PHOSPHATIDYLCHOLINE                                         
FORMUL   3  PLM    C16 H32 O2                                                   
FORMUL   4  BOG    2(C14 H28 O6)                                                
FORMUL   5  RET    2(C20 H28 O)                                                 
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  PC1    C44 H88 N O8 P                                               
FORMUL  10  HOH   *59(H2 O)                                                     
HELIX    1   1 HIS A   20  GLU A   25  1                                   6    
HELIX    2   2 PRO A   30  THR A   62  1                                  33    
HELIX    3   3 ALA A   69  GLY A   88  1                                  20    
HELIX    4   4 PRO A   90  LEU A   98  1                                   9    
HELIX    5   5 PHE A  103  ILE A  137  1                                  35    
HELIX    6   6 SER A  148  TRP A  166  1                                  19    
HELIX    7   7 ILE A  168  PHE A  172  5                                   5    
HELIX    8   8 ASP A  194  GLY A  208  1                                  15    
HELIX    9   9 PHE A  209  MET A  225  1                                  17    
HELIX   10  10 SER A  226  LYS A  239  1                                  14    
HELIX   11  11 GLU A  245  GLY A  287  1                                  43    
HELIX   12  12 THR A  293  SER A  307  1                                  15    
HELIX   13  13 HIS A  310  HIS A  319  1                                  10    
HELIX   14  14 HIS A  319  PHE A  330  1                                  12    
HELIX   15  15 ASP A  340  GLU A  343  5                                   4    
HELIX   16  16 THR A  344  THR A  352  1                                   9    
HELIX   17  17 HIS B   20  GLU B   25  1                                   6    
HELIX   18  18 PRO B   30  THR B   62  1                                  33    
HELIX   19  19 LYS B   63  GLN B   66  5                                   4    
HELIX   20  20 THR B   67  PRO B   68  5                                   2    
HELIX   21  21 ALA B   69  GLY B   88  1                                  20    
HELIX   22  22 PRO B   90  LEU B   98  1                                   9    
HELIX   23  23 PHE B  103  ILE B  137  1                                  35    
HELIX   24  24 SER B  148  GLY B  169  1                                  22    
HELIX   25  25 PRO B  170  GLY B  173  5                                   4    
HELIX   26  26 ASP B  194  PHE B  209  1                                  16    
HELIX   27  27 PHE B  209  MET B  225  1                                  17    
HELIX   28  28 SER B  226  LYS B  239  1                                  14    
HELIX   29  29 LYS B  244  GLY B  287  1                                  44    
HELIX   30  30 THR B  293  SER B  307  1                                  15    
HELIX   31  31 ILE B  309  VAL B  317  1                                   9    
HELIX   32  32 HIS B  319  GLN B  328  1                                  10    
HELIX   33  33 PHE B  330  GLN B  338  5                                   9    
HELIX   34  34 ASP B  340  GLU B  343  5                                   4    
HELIX   35  35 THR B  344  THR B  352  1                                   9    
SHEET    1   A 2 TYR A 177  LEU A 179  0                                        
SHEET    2   A 2 CYS A 186  PHE A 188 -1  O  SER A 187   N  THR A 178           
SHEET    1   B 2 TYR B 177  LEU B 179  0                                        
SHEET    2   B 2 CYS B 186  PHE B 188 -1  O  SER B 187   N  THR B 178           
SSBOND   1 CYS A  108    CYS A  186                          1555   1555  2.05  
SSBOND   2 CYS B  108    CYS B  186                          1555   1555  2.02  
LINK         NZ  LYS A 305                 C15 RET A1000     1555   1555  1.27  
LINK         NZ  LYS B 305                 C15 RET B1000     1555   1555  1.29  
CISPEP   1 PHE A   89    PRO A   90          0         0.47                     
CISPEP   2 PHE B   89    PRO B   90          0         1.25                     
CRYST1  122.360  122.360  158.220  90.00  90.00 120.00 P 62         12          
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      0.008173  0.004718  0.000000        0.00000                         
SCALE2      0.000000  0.009437  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006320        0.00000                         
ATOM      1  N   GLU A   9       5.549  31.180  31.831  1.00 59.74           N  
ATOM      2  CA  GLU A   9       6.766  31.904  31.379  1.00 62.95           C  
ATOM      3  C   GLU A   9       7.804  32.082  32.512  1.00 62.24           C  
ATOM      4  O   GLU A   9       9.026  32.033  32.283  1.00 62.70           O  
ATOM      5  CB  GLU A   9       6.362  33.258  30.810  1.00 65.62           C  
ATOM      6  CG  GLU A   9       7.119  33.630  29.536  1.00 74.18           C  
ATOM      7  CD  GLU A   9       6.930  32.617  28.385  1.00 78.93           C  
ATOM      8  OE1 GLU A   9       5.796  32.497  27.840  1.00 80.57           O  
ATOM      9  OE2 GLU A   9       7.927  31.941  28.021  1.00 81.63           O  
ATOM     10  N   THR A  10       7.302  32.315  33.726  1.00 59.97           N  
ATOM     11  CA  THR A  10       8.131  32.452  34.917  1.00 55.02           C  
ATOM     12  C   THR A  10       7.346  31.901  36.111  1.00 52.80           C  
ATOM     13  O   THR A  10       6.116  31.845  36.094  1.00 48.63           O  
ATOM     14  CB  THR A  10       8.557  33.907  35.163  1.00 54.32           C  
ATOM     15  OG1 THR A  10       7.406  34.749  35.263  1.00 54.28           O  
ATOM     16  CG2 THR A  10       9.431  34.381  34.021  1.00 52.66           C  
ATOM     17  N   TRP A  11       8.095  31.441  37.105  1.00 52.01           N  
ATOM     18  CA  TRP A  11       7.568  30.856  38.319  1.00 52.68           C  
ATOM     19  C   TRP A  11       7.711  31.833  39.467  1.00 55.99           C  
ATOM     20  O   TRP A  11       7.431  31.476  40.626  1.00 60.79           O  
ATOM     21  CB  TRP A  11       8.327  29.577  38.703  1.00 49.45           C  
ATOM     22  CG  TRP A  11       9.785  29.850  38.934  1.00 50.38           C  
ATOM     23  CD1 TRP A  11      10.808  29.708  38.011  1.00 51.88           C  
ATOM     24  CD2 TRP A  11      10.393  30.444  40.103  1.00 51.49           C  
ATOM     25  NE1 TRP A  11      12.004  30.185  38.533  1.00 52.27           N  
ATOM     26  CE2 TRP A  11      11.780  30.640  39.808  1.00 51.94           C  
ATOM     27  CE3 TRP A  11       9.906  30.837  41.366  1.00 52.70           C  
ATOM     28  CZ2 TRP A  11      12.673  31.207  40.727  1.00 52.89           C  
ATOM     29  CZ3 TRP A  11      10.801  31.411  42.297  1.00 52.50           C  
ATOM     30  CH2 TRP A  11      12.169  31.588  41.968  1.00 53.74           C  
ATOM     31  N   TRP A  12       8.152  33.058  39.185  1.00 57.20           N  
ATOM     32  CA  TRP A  12       8.313  34.030  40.278  1.00 58.26           C  
ATOM     33  C   TRP A  12       7.484  35.309  40.124  1.00 57.36           C  
ATOM     34  O   TRP A  12       7.338  36.070  41.101  1.00 57.33           O  
ATOM     35  CB  TRP A  12       9.788  34.409  40.431  1.00 60.62           C  
ATOM     36  CG  TRP A  12      10.356  34.762  39.118  1.00 62.84           C  
ATOM     37  CD1 TRP A  12      10.950  33.919  38.245  1.00 63.34           C  
ATOM     38  CD2 TRP A  12      10.261  36.027  38.456  1.00 64.11           C  
ATOM     39  NE1 TRP A  12      11.231  34.566  37.070  1.00 65.25           N  
ATOM     40  CE2 TRP A  12      10.821  35.867  37.173  1.00 64.08           C  
ATOM     41  CE3 TRP A  12       9.758  37.273  38.820  1.00 63.41           C  
ATOM     42  CZ2 TRP A  12      10.889  36.910  36.245  1.00 64.17           C  
ATOM     43  CZ3 TRP A  12       9.825  38.303  37.894  1.00 65.64           C  
ATOM     44  CH2 TRP A  12      10.389  38.113  36.619  1.00 62.70           C  
ATOM     45  N   TYR A  13       6.925  35.539  38.928  1.00 55.41           N  
ATOM     46  CA  TYR A  13       6.128  36.758  38.684  1.00 54.19           C  
ATOM     47  C   TYR A  13       5.030  37.139  39.653  1.00 50.89           C  
ATOM     48  O   TYR A  13       4.126  36.358  39.934  1.00 49.68           O  
ATOM     49  CB  TYR A  13       5.464  36.777  37.295  1.00 57.33           C  
ATOM     50  CG  TYR A  13       4.907  38.171  36.922  1.00 60.35           C  
ATOM     51  CD1 TYR A  13       3.558  38.351  36.580  1.00 60.42           C  
ATOM     52  CD2 TYR A  13       5.753  39.312  36.936  1.00 62.40           C  
ATOM     53  CE1 TYR A  13       3.056  39.623  36.262  1.00 63.10           C  
ATOM     54  CE2 TYR A  13       5.279  40.586  36.627  1.00 62.76           C  
ATOM     55  CZ  TYR A  13       3.928  40.744  36.290  1.00 65.65           C  
ATOM     56  OH  TYR A  13       3.457  42.027  36.012  1.00 66.73           O  
ATOM     57  N   ASN A  14       5.110  38.372  40.126  1.00 48.06           N  
ATOM     58  CA  ASN A  14       4.103  38.894  41.003  1.00 45.88           C  
ATOM     59  C   ASN A  14       3.487  40.119  40.383  1.00 44.82           C  
ATOM     60  O   ASN A  14       4.136  41.162  40.197  1.00 41.81           O  
ATOM     61  CB  ASN A  14       4.649  39.277  42.359  1.00 47.43           C  
ATOM     62  CG  ASN A  14       3.531  39.478  43.349  1.00 49.02           C  
ATOM     63  OD1 ASN A  14       2.452  39.981  42.963  1.00 48.34           O  
ATOM     64  ND2 ASN A  14       3.746  39.069  44.621  1.00 48.20           N  
ATOM     65  N   PRO A  15       2.206  40.020  40.060  1.00 46.51           N  
ATOM     66  CA  PRO A  15       1.537  41.166  39.446  1.00 46.87           C  
ATOM     67  C   PRO A  15       1.333  42.345  40.365  1.00 46.36           C  
ATOM     68  O   PRO A  15       0.820  43.356  39.910  1.00 48.30           O  
ATOM     69  CB  PRO A  15       0.226  40.582  38.986  1.00 46.64           C  
ATOM     70  CG  PRO A  15      -0.051  39.583  40.102  1.00 48.82           C  
ATOM     71  CD  PRO A  15       1.278  38.891  40.238  1.00 46.09           C  
ATOM     72  N   SER A  16       1.729  42.231  41.637  1.00 46.05           N  
ATOM     73  CA  SER A  16       1.552  43.332  42.596  1.00 45.50           C  
ATOM     74  C   SER A  16       2.871  43.903  43.098  1.00 45.93           C  
ATOM     75  O   SER A  16       2.896  44.973  43.703  1.00 46.43           O  
ATOM     76  CB  SER A  16       0.748  42.881  43.829  1.00 44.94           C  
ATOM     77  OG  SER A  16      -0.230  41.889  43.527  1.00 44.02           O  
ATOM     78  N   ILE A  17       3.963  43.184  42.854  1.00 48.15           N  
ATOM     79  CA  ILE A  17       5.303  43.580  43.330  1.00 49.21           C  
ATOM     80  C   ILE A  17       6.425  43.222  42.286  1.00 50.05           C  
ATOM     81  O   ILE A  17       6.540  42.060  41.860  1.00 51.32           O  
ATOM     82  CB  ILE A  17       5.596  42.847  44.745  1.00 47.99           C  
ATOM     83  CG1 ILE A  17       4.468  43.115  45.738  1.00 43.93           C  
ATOM     84  CG2 ILE A  17       6.886  43.364  45.416  1.00 50.65           C  
ATOM     85  CD1 ILE A  17       4.826  42.705  47.148  1.00 42.83           C  
ATOM     86  N   VAL A  18       7.237  44.199  41.872  1.00 49.08           N  
ATOM     87  CA  VAL A  18       8.325  43.914  40.921  1.00 48.87           C  
ATOM     88  C   VAL A  18       9.500  43.197  41.628  1.00 47.56           C  
ATOM     89  O   VAL A  18      10.225  43.819  42.396  1.00 46.58           O  
ATOM     90  CB  VAL A  18       8.854  45.250  40.227  1.00 50.15           C  
ATOM     91  CG1 VAL A  18      10.192  45.032  39.542  1.00 47.61           C  
ATOM     92  CG2 VAL A  18       7.853  45.733  39.174  1.00 51.69           C  
ATOM     93  N   VAL A  19       9.673  41.894  41.375  1.00 48.55           N  
ATOM     94  CA  VAL A  19      10.759  41.077  41.979  1.00 49.44           C  
ATOM     95  C   VAL A  19      12.127  41.538  41.461  1.00 50.73           C  
ATOM     96  O   VAL A  19      12.352  41.616  40.254  1.00 52.25           O  
ATOM     97  CB  VAL A  19      10.570  39.522  41.634  1.00 47.85           C  
ATOM     98  CG1 VAL A  19      11.857  38.712  41.883  1.00 44.87           C  
ATOM     99  CG2 VAL A  19       9.461  38.951  42.469  1.00 44.90           C  
ATOM    100  N   HIS A  20      13.043  41.852  42.362  1.00 52.13           N  
ATOM    101  CA  HIS A  20      14.368  42.274  41.921  1.00 54.35           C  
ATOM    102  C   HIS A  20      14.956  41.146  41.084  1.00 57.02           C  
ATOM    103  O   HIS A  20      14.953  40.005  41.533  1.00 60.12           O  
ATOM    104  CB  HIS A  20      15.252  42.500  43.101  1.00 53.64           C  
ATOM    105  CG  HIS A  20      16.487  43.233  42.753  1.00 54.16           C  
ATOM    106  ND1 HIS A  20      17.345  42.804  41.769  1.00 52.73           N  
ATOM    107  CD2 HIS A  20      17.038  44.355  43.280  1.00 54.49           C  
ATOM    108  CE1 HIS A  20      18.380  43.625  41.709  1.00 53.23           C  
ATOM    109  NE2 HIS A  20      18.218  44.576  42.617  1.00 51.80           N  
ATOM    110  N   PRO A  21      15.512  41.452  39.881  1.00 57.74           N  
ATOM    111  CA  PRO A  21      16.110  40.473  38.931  1.00 55.74           C  
ATOM    112  C   PRO A  21      16.986  39.395  39.567  1.00 53.01           C  
ATOM    113  O   PRO A  21      17.056  38.279  39.055  1.00 52.35           O  
ATOM    114  CB  PRO A  21      16.932  41.345  37.965  1.00 57.33           C  
ATOM    115  CG  PRO A  21      16.312  42.686  38.070  1.00 58.98           C  
ATOM    116  CD  PRO A  21      15.959  42.819  39.555  1.00 57.66           C  
ATOM    117  N   HIS A  22      17.648  39.765  40.663  1.00 48.80           N  
ATOM    118  CA  HIS A  22      18.520  38.885  41.405  1.00 48.05           C  
ATOM    119  C   HIS A  22      17.841  37.646  41.926  1.00 47.69           C  
ATOM    120  O   HIS A  22      18.450  36.580  41.969  1.00 49.05           O  
ATOM    121  CB  HIS A  22      19.134  39.599  42.617  1.00 50.04           C  
ATOM    122  CG  HIS A  22      19.797  38.659  43.585  1.00 49.39           C  
ATOM    123  ND1 HIS A  22      20.874  37.875  43.231  1.00 49.39           N  
ATOM    124  CD2 HIS A  22      19.458  38.285  44.842  1.00 50.44           C  
ATOM    125  CE1 HIS A  22      21.162  37.052  44.221  1.00 49.55           C  
ATOM    126  NE2 HIS A  22      20.316  37.278  45.210  1.00 50.62           N  
ATOM    127  N   TRP A  23      16.605  37.789  42.396  1.00 47.06           N  
ATOM    128  CA  TRP A  23      15.850  36.641  42.927  1.00 44.72           C  
ATOM    129  C   TRP A  23      15.141  35.957  41.749  1.00 43.52           C  
ATOM    130  O   TRP A  23      14.508  34.938  41.916  1.00 45.40           O  
ATOM    131  CB  TRP A  23      14.782  37.071  43.975  1.00 41.57           C  
ATOM    132  CG  TRP A  23      15.291  37.767  45.196  1.00 39.02           C  
ATOM    133  CD1 TRP A  23      15.026  39.058  45.574  1.00 42.32           C  
ATOM    134  CD2 TRP A  23      16.176  37.248  46.165  1.00 37.81           C  
ATOM    135  NE1 TRP A  23      15.701  39.383  46.729  1.00 41.18           N  
ATOM    136  CE2 TRP A  23      16.427  38.289  47.110  1.00 41.55           C  
ATOM    137  CE3 TRP A  23      16.795  36.018  46.336  1.00 37.38           C  
ATOM    138  CZ2 TRP A  23      17.280  38.123  48.216  1.00 42.91           C  
ATOM    139  CZ3 TRP A  23      17.638  35.845  47.432  1.00 43.26           C  
ATOM    140  CH2 TRP A  23      17.879  36.901  48.362  1.00 44.20           C  
ATOM    141  N   ARG A  24      15.245  36.514  40.560  1.00 43.35           N  
ATOM    142  CA  ARG A  24      14.563  35.897  39.468  1.00 44.48           C  
ATOM    143  C   ARG A  24      15.433  34.994  38.700  1.00 46.60           C  
ATOM    144  O   ARG A  24      14.922  34.146  37.998  1.00 50.46           O  
ATOM    145  CB  ARG A  24      14.007  36.928  38.529  1.00 45.21           C  
ATOM    146  CG  ARG A  24      13.063  37.837  39.239  1.00 50.44           C  
ATOM    147  CD  ARG A  24      13.336  39.260  38.850  1.00 47.57           C  
ATOM    148  NE  ARG A  24      12.894  39.458  37.492  1.00 45.72           N  
ATOM    149  CZ  ARG A  24      12.621  40.640  36.983  1.00 44.97           C  
ATOM    150  NH1 ARG A  24      12.756  41.731  37.732  1.00 44.85           N  
ATOM    151  NH2 ARG A  24      12.187  40.714  35.731  1.00 47.70           N  
ATOM    152  N   GLU A  25      16.744  35.134  38.793  1.00 47.12           N  
ATOM    153  CA  GLU A  25      17.562  34.248  37.987  1.00 45.47           C  
ATOM    154  C   GLU A  25      17.582  32.844  38.515  1.00 47.05           C  
ATOM    155  O   GLU A  25      18.027  31.935  37.812  1.00 50.00           O  
ATOM    156  CB  GLU A  25      18.982  34.742  37.899  1.00 41.88           C  
ATOM    157  CG  GLU A  25      19.697  34.766  39.183  1.00 39.44           C  
ATOM    158  CD  GLU A  25      21.045  35.369  39.017  1.00 40.97           C  
ATOM    159  OE1 GLU A  25      22.015  34.614  38.836  1.00 41.40           O  
ATOM    160  OE2 GLU A  25      21.128  36.612  39.037  1.00 42.93           O  
ATOM    161  N   PHE A  26      17.089  32.631  39.726  1.00 45.11           N  
ATOM    162  CA  PHE A  26      17.156  31.280  40.241  1.00 49.35           C  
ATOM    163  C   PHE A  26      16.021  30.394  39.777  1.00 51.56           C  
ATOM    164  O   PHE A  26      15.121  30.860  39.060  1.00 49.72           O  
ATOM    165  CB  PHE A  26      17.196  31.297  41.763  1.00 48.97           C  
ATOM    166  CG  PHE A  26      18.324  32.100  42.314  1.00 47.36           C  
ATOM    167  CD1 PHE A  26      19.595  31.554  42.402  1.00 47.07           C  
ATOM    168  CD2 PHE A  26      18.126  33.427  42.704  1.00 46.12           C  
ATOM    169  CE1 PHE A  26      20.685  32.335  42.876  1.00 48.15           C  
ATOM    170  CE2 PHE A  26      19.189  34.220  43.179  1.00 44.02           C  
ATOM    171  CZ  PHE A  26      20.468  33.676  43.263  1.00 47.05           C  
ATOM    172  N   ASP A  27      16.100  29.095  40.144  1.00 52.91           N  
ATOM    173  CA  ASP A  27      14.979  28.138  39.823  1.00 55.82           C  
ATOM    174  C   ASP A  27      14.117  28.128  41.118  1.00 55.62           C  
ATOM    175  O   ASP A  27      14.602  28.476  42.224  1.00 56.94           O  
ATOM    176  CB  ASP A  27      15.438  26.662  39.564  1.00 56.95           C  
ATOM    177  CG  ASP A  27      16.499  26.535  38.441  1.00 57.83           C  
ATOM    178  OD1 ASP A  27      16.256  26.926  37.167  1.00 52.90           O  
ATOM    179  OD2 ASP A  27      17.576  25.977  38.911  1.00 55.15           O  
ATOM    180  N   GLN A  28      12.875  27.680  40.954  1.00 58.48           N  
ATOM    181  CA  GLN A  28      11.936  27.629  42.048  1.00 60.05           C  
ATOM    182  C   GLN A  28      12.162  26.446  42.961  1.00 59.64           C  
ATOM    183  O   GLN A  28      12.043  25.283  42.526  1.00 60.69           O  
ATOM    184  CB  GLN A  28      10.518  27.557  41.512  1.00 64.22           C  
ATOM    185  CG  GLN A  28       9.465  27.707  42.597  1.00 69.93           C  
ATOM    186  CD  GLN A  28       8.087  27.825  41.986  1.00 73.51           C  
ATOM    187  OE1 GLN A  28       7.862  27.311  40.863  1.00 77.52           O  
ATOM    188  NE2 GLN A  28       7.149  28.500  42.701  1.00 73.14           N  
ATOM    189  N   VAL A  29      12.458  26.760  44.233  1.00 59.09           N  
ATOM    190  CA  VAL A  29      12.694  25.773  45.294  1.00 55.56           C  
ATOM    191  C   VAL A  29      11.519  24.760  45.296  1.00 58.61           C  
ATOM    192  O   VAL A  29      10.395  25.108  44.942  1.00 59.30           O  
ATOM    193  CB  VAL A  29      12.792  26.493  46.666  1.00 52.04           C  
ATOM    194  CG1 VAL A  29      13.959  27.465  46.658  1.00 49.13           C  
ATOM    195  CG2 VAL A  29      11.519  27.243  46.947  1.00 48.19           C  
ATOM    196  N   PRO A  30      11.767  23.491  45.673  1.00 59.85           N  
ATOM    197  CA  PRO A  30      10.718  22.437  45.713  1.00 59.74           C  
ATOM    198  C   PRO A  30       9.499  22.747  46.606  1.00 60.02           C  
ATOM    199  O   PRO A  30       9.608  23.480  47.601  1.00 60.83           O  
ATOM    200  CB  PRO A  30      11.464  21.210  46.237  1.00 58.90           C  
ATOM    201  CG  PRO A  30      12.906  21.488  45.887  1.00 60.06           C  
ATOM    202  CD  PRO A  30      13.084  22.971  46.088  1.00 59.23           C  
ATOM    203  N   ASP A  31       8.350  22.157  46.281  1.00 60.87           N  
ATOM    204  CA  ASP A  31       7.124  22.363  47.078  1.00 60.76           C  
ATOM    205  C   ASP A  31       7.365  22.136  48.574  1.00 57.69           C  
ATOM    206  O   ASP A  31       7.027  22.974  49.410  1.00 58.57           O  
ATOM    207  CB  ASP A  31       6.015  21.409  46.615  1.00 66.54           C  
ATOM    208  CG  ASP A  31       5.607  21.633  45.147  1.00 71.59           C  
ATOM    209  OD1 ASP A  31       6.290  22.430  44.445  1.00 74.20           O  
ATOM    210  OD2 ASP A  31       4.608  21.004  44.706  1.00 71.11           O  
ATOM    211  N   ALA A  32       7.943  20.994  48.901  1.00 52.86           N  
ATOM    212  CA  ALA A  32       8.230  20.678  50.279  1.00 50.20           C  
ATOM    213  C   ALA A  32       8.906  21.829  51.033  1.00 48.10           C  
ATOM    214  O   ALA A  32       8.680  22.017  52.224  1.00 47.72           O  
ATOM    215  CB  ALA A  32       9.096  19.444  50.334  1.00 50.40           C  
ATOM    216  N   VAL A  33       9.744  22.592  50.345  1.00 45.28           N  
ATOM    217  CA  VAL A  33      10.438  23.691  50.986  1.00 43.92           C  
ATOM    218  C   VAL A  33       9.466  24.815  51.300  1.00 44.55           C  
ATOM    219  O   VAL A  33       9.540  25.428  52.362  1.00 44.82           O  
ATOM    220  CB  VAL A  33      11.562  24.223  50.088  1.00 42.31           C  
ATOM    221  CG1 VAL A  33      12.269  25.385  50.739  1.00 41.85           C  
ATOM    222  CG2 VAL A  33      12.529  23.123  49.810  1.00 42.89           C  
ATOM    223  N   TYR A  34       8.545  25.083  50.384  1.00 44.46           N  
ATOM    224  CA  TYR A  34       7.579  26.145  50.608  1.00 45.56           C  
ATOM    225  C   TYR A  34       6.681  25.769  51.751  1.00 47.78           C  
ATOM    226  O   TYR A  34       6.431  26.587  52.643  1.00 48.30           O  
ATOM    227  CB  TYR A  34       6.720  26.395  49.371  1.00 42.88           C  
ATOM    228  CG  TYR A  34       7.397  27.184  48.260  1.00 41.06           C  
ATOM    229  CD1 TYR A  34       7.760  26.557  47.064  1.00 40.14           C  
ATOM    230  CD2 TYR A  34       7.596  28.568  48.370  1.00 38.67           C  
ATOM    231  CE1 TYR A  34       8.287  27.274  46.003  1.00 40.21           C  
ATOM    232  CE2 TYR A  34       8.129  29.300  47.312  1.00 39.79           C  
ATOM    233  CZ  TYR A  34       8.467  28.630  46.124  1.00 41.41           C  
ATOM    234  OH  TYR A  34       8.961  29.290  45.035  1.00 38.90           O  
ATOM    235  N   TYR A  35       6.204  24.527  51.725  1.00 50.20           N  
ATOM    236  CA  TYR A  35       5.309  24.001  52.773  1.00 55.02           C  
ATOM    237  C   TYR A  35       5.942  24.015  54.148  1.00 53.45           C  
ATOM    238  O   TYR A  35       5.296  24.382  55.125  1.00 53.45           O  
ATOM    239  CB  TYR A  35       4.852  22.582  52.431  1.00 61.87           C  
ATOM    240  CG  TYR A  35       4.124  22.557  51.109  1.00 73.70           C  
ATOM    241  CD1 TYR A  35       4.073  21.393  50.316  1.00 76.33           C  
ATOM    242  CD2 TYR A  35       3.530  23.736  50.614  1.00 78.45           C  
ATOM    243  CE1 TYR A  35       3.452  21.414  49.052  1.00 82.42           C  
ATOM    244  CE2 TYR A  35       2.907  23.776  49.358  1.00 83.55           C  
ATOM    245  CZ  TYR A  35       2.869  22.623  48.573  1.00 85.20           C  
ATOM    246  OH  TYR A  35       2.283  22.704  47.309  1.00 88.64           O  
ATOM    247  N   SER A  36       7.208  23.621  54.215  1.00 50.96           N  
ATOM    248  CA  SER A  36       7.908  23.619  55.468  1.00 47.07           C  
ATOM    249  C   SER A  36       8.047  25.057  55.925  1.00 44.71           C  
ATOM    250  O   SER A  36       7.814  25.371  57.080  1.00 45.12           O  
ATOM    251  CB  SER A  36       9.279  22.967  55.301  1.00 48.48           C  
ATOM    252  OG  SER A  36       9.150  21.621  54.884  1.00 48.17           O  
ATOM    253  N   LEU A  37       8.406  25.948  55.018  1.00 43.20           N  
ATOM    254  CA  LEU A  37       8.580  27.347  55.413  1.00 42.95           C  
ATOM    255  C   LEU A  37       7.294  27.897  56.036  1.00 45.49           C  
ATOM    256  O   LEU A  37       7.334  28.569  57.082  1.00 44.84           O  
ATOM    257  CB  LEU A  37       9.018  28.215  54.209  1.00 35.61           C  
ATOM    258  CG  LEU A  37      10.479  28.102  53.790  1.00 28.98           C  
ATOM    259  CD1 LEU A  37      10.748  28.895  52.557  1.00 26.67           C  
ATOM    260  CD2 LEU A  37      11.339  28.567  54.915  1.00 21.85           C  
ATOM    261  N   GLY A  38       6.160  27.587  55.397  1.00 46.84           N  
ATOM    262  CA  GLY A  38       4.869  28.062  55.877  1.00 47.56           C  
ATOM    263  C   GLY A  38       4.529  27.522  57.251  1.00 46.35           C  
ATOM    264  O   GLY A  38       4.129  28.260  58.157  1.00 46.45           O  
ATOM    265  N   ILE A  39       4.697  26.216  57.399  1.00 44.60           N  
ATOM    266  CA  ILE A  39       4.433  25.548  58.661  1.00 40.44           C  
ATOM    267  C   ILE A  39       5.335  26.121  59.724  1.00 42.10           C  
ATOM    268  O   ILE A  39       4.905  26.375  60.849  1.00 43.38           O  
ATOM    269  CB  ILE A  39       4.695  24.044  58.550  1.00 37.94           C  
ATOM    270  CG1 ILE A  39       3.598  23.404  57.691  1.00 37.35           C  
ATOM    271  CG2 ILE A  39       4.790  23.428  59.922  1.00 32.69           C  
ATOM    272  CD1 ILE A  39       3.874  21.975  57.315  1.00 40.03           C  
ATOM    273  N   PHE A  40       6.592  26.347  59.353  1.00 43.92           N  
ATOM    274  CA  PHE A  40       7.585  26.873  60.280  1.00 43.30           C  
ATOM    275  C   PHE A  40       7.180  28.215  60.875  1.00 44.65           C  
ATOM    276  O   PHE A  40       7.003  28.350  62.096  1.00 44.60           O  
ATOM    277  CB  PHE A  40       8.947  27.021  59.597  1.00 42.12           C  
ATOM    278  CG  PHE A  40      10.002  27.547  60.513  1.00 43.55           C  
ATOM    279  CD1 PHE A  40      10.689  26.689  61.355  1.00 44.13           C  
ATOM    280  CD2 PHE A  40      10.255  28.924  60.606  1.00 45.49           C  
ATOM    281  CE1 PHE A  40      11.607  27.181  62.281  1.00 46.03           C  
ATOM    282  CE2 PHE A  40      11.174  29.430  61.534  1.00 45.95           C  
ATOM    283  CZ  PHE A  40      11.851  28.560  62.373  1.00 45.75           C  
ATOM    284  N   ILE A  41       7.030  29.213  60.007  1.00 45.37           N  
ATOM    285  CA  ILE A  41       6.669  30.565  60.450  1.00 45.59           C  
ATOM    286  C   ILE A  41       5.299  30.575  61.132  1.00 44.69           C  
ATOM    287  O   ILE A  41       5.052  31.364  62.054  1.00 44.23           O  
ATOM    288  CB  ILE A  41       6.676  31.570  59.245  1.00 47.01           C  
ATOM    289  CG1 ILE A  41       6.926  32.995  59.754  1.00 47.83           C  
ATOM    290  CG2 ILE A  41       5.383  31.457  58.435  1.00 46.78           C  
ATOM    291  CD1 ILE A  41       8.254  33.151  60.522  1.00 45.09           C  
ATOM    292  N   GLY A  42       4.418  29.687  60.678  1.00 42.03           N  
ATOM    293  CA  GLY A  42       3.106  29.603  61.276  1.00 41.91           C  
ATOM    294  C   GLY A  42       3.244  29.210  62.732  1.00 42.98           C  
ATOM    295  O   GLY A  42       2.544  29.749  63.599  1.00 45.30           O  
ATOM    296  N   ILE A  43       4.155  28.275  63.014  1.00 41.48           N  
ATOM    297  CA  ILE A  43       4.369  27.831  64.373  1.00 37.64           C  
ATOM    298  C   ILE A  43       5.072  28.927  65.179  1.00 37.60           C  
ATOM    299  O   ILE A  43       5.022  28.918  66.397  1.00 36.61           O  
ATOM    300  CB  ILE A  43       5.162  26.510  64.385  1.00 35.91           C  
ATOM    301  CG1 ILE A  43       4.333  25.423  63.740  1.00 28.64           C  
ATOM    302  CG2 ILE A  43       5.540  26.103  65.834  1.00 38.61           C  
ATOM    303  CD1 ILE A  43       4.917  24.071  63.928  1.00 26.35           C  
ATOM    304  N   CYS A  44       5.722  29.874  64.517  1.00 38.67           N  
ATOM    305  CA  CYS A  44       6.345  30.955  65.280  1.00 41.50           C  
ATOM    306  C   CYS A  44       5.206  31.900  65.639  1.00 39.16           C  
ATOM    307  O   CYS A  44       5.206  32.559  66.687  1.00 37.90           O  
ATOM    308  CB  CYS A  44       7.421  31.691  64.466  1.00 44.74           C  
ATOM    309  SG  CYS A  44       9.018  30.813  64.359  1.00 47.47           S  
ATOM    310  N   GLY A  45       4.217  31.934  64.757  1.00 38.06           N  
ATOM    311  CA  GLY A  45       3.049  32.764  64.984  1.00 36.27           C  
ATOM    312  C   GLY A  45       2.342  32.290  66.239  1.00 34.02           C  
ATOM    313  O   GLY A  45       2.023  33.091  67.129  1.00 35.92           O  
ATOM    314  N   ILE A  46       2.095  30.989  66.311  1.00 28.30           N  
ATOM    315  CA  ILE A  46       1.445  30.435  67.470  1.00 27.81           C  
ATOM    316  C   ILE A  46       2.247  30.621  68.783  1.00 29.55           C  
ATOM    317  O   ILE A  46       1.766  31.249  69.750  1.00 31.83           O  
ATOM    318  CB  ILE A  46       1.167  28.968  67.277  1.00 25.28           C  
ATOM    319  CG1 ILE A  46       0.201  28.756  66.128  1.00 26.40           C  
ATOM    320  CG2 ILE A  46       0.463  28.459  68.474  1.00 25.26           C  
ATOM    321  CD1 ILE A  46       0.049  27.306  65.745  1.00 29.73           C  
ATOM    322  N   ILE A  47       3.462  30.085  68.831  1.00 29.81           N  
ATOM    323  CA  ILE A  47       4.290  30.197  70.023  1.00 28.24           C  
ATOM    324  C   ILE A  47       4.488  31.659  70.371  1.00 31.42           C  
ATOM    325  O   ILE A  47       4.234  32.059  71.505  1.00 29.32           O  
ATOM    326  CB  ILE A  47       5.644  29.505  69.809  1.00 27.17           C  
ATOM    327  CG1 ILE A  47       5.420  28.012  69.598  1.00 25.10           C  
ATOM    328  CG2 ILE A  47       6.537  29.736  70.971  1.00 26.16           C  
ATOM    329  CD1 ILE A  47       6.657  27.210  69.414  1.00 24.63           C  
ATOM    330  N   GLY A  48       4.922  32.457  69.382  1.00 34.83           N  
ATOM    331  CA  GLY A  48       5.138  33.894  69.584  1.00 38.17           C  
ATOM    332  C   GLY A  48       3.951  34.659  70.189  1.00 41.23           C  
ATOM    333  O   GLY A  48       4.068  35.291  71.260  1.00 39.76           O  
ATOM    334  N   CYS A  49       2.799  34.605  69.508  1.00 43.31           N  
ATOM    335  CA  CYS A  49       1.596  35.288  70.003  1.00 45.86           C  
ATOM    336  C   CYS A  49       1.171  34.670  71.313  1.00 45.99           C  
ATOM    337  O   CYS A  49       0.797  35.389  72.237  1.00 45.85           O  
ATOM    338  CB  CYS A  49       0.435  35.203  69.001  1.00 47.96           C  
ATOM    339  SG  CYS A  49       0.753  36.015  67.402  1.00 48.49           S  
ATOM    340  N   GLY A  50       1.226  33.343  71.392  1.00 46.98           N  
ATOM    341  CA  GLY A  50       0.852  32.690  72.634  1.00 50.78           C  
ATOM    342  C   GLY A  50       1.738  33.095  73.826  1.00 51.55           C  
ATOM    343  O   GLY A  50       1.279  33.607  74.868  1.00 53.43           O  
ATOM    344  N   GLY A  51       3.034  32.868  73.673  1.00 50.76           N  
ATOM    345  CA  GLY A  51       3.952  33.200  74.745  1.00 47.00           C  
ATOM    346  C   GLY A  51       4.021  34.670  75.064  1.00 45.36           C  
ATOM    347  O   GLY A  51       4.110  35.003  76.216  1.00 46.07           O  
ATOM    348  N   ASN A  52       3.997  35.563  74.086  1.00 45.21           N  
ATOM    349  CA  ASN A  52       4.078  36.975  74.448  1.00 46.97           C  
ATOM    350  C   ASN A  52       2.786  37.503  75.056  1.00 46.10           C  
ATOM    351  O   ASN A  52       2.772  38.492  75.824  1.00 42.53           O  
ATOM    352  CB  ASN A  52       4.447  37.814  73.239  1.00 51.19           C  
ATOM    353  CG  ASN A  52       5.913  37.667  72.862  1.00 54.63           C  
ATOM    354  OD1 ASN A  52       6.825  38.008  73.648  1.00 48.01           O  
ATOM    355  ND2 ASN A  52       6.152  37.152  71.635  1.00 60.84           N  
ATOM    356  N   GLY A  53       1.701  36.835  74.679  1.00 45.52           N  
ATOM    357  CA  GLY A  53       0.397  37.198  75.177  1.00 43.36           C  
ATOM    358  C   GLY A  53       0.454  36.936  76.650  1.00 41.26           C  
ATOM    359  O   GLY A  53       0.144  37.826  77.453  1.00 43.47           O  
ATOM    360  N   ILE A  54       0.883  35.721  76.999  1.00 37.73           N  
ATOM    361  CA  ILE A  54       1.007  35.314  78.390  1.00 35.58           C  
ATOM    362  C   ILE A  54       1.825  36.312  79.235  1.00 36.34           C  
ATOM    363  O   ILE A  54       1.355  36.752  80.280  1.00 37.97           O  
ATOM    364  CB  ILE A  54       1.596  33.888  78.479  1.00 32.73           C  
ATOM    365  CG1 ILE A  54       0.683  32.913  77.721  1.00 25.08           C  
ATOM    366  CG2 ILE A  54       1.772  33.492  79.958  1.00 32.74           C  
ATOM    367  CD1 ILE A  54       1.068  31.493  77.898  1.00 24.99           C  
ATOM    368  N   VAL A  55       3.024  36.684  78.788  1.00 38.07           N  
ATOM    369  CA  VAL A  55       3.833  37.670  79.518  1.00 38.47           C  
ATOM    370  C   VAL A  55       3.076  39.016  79.632  1.00 39.84           C  
ATOM    371  O   VAL A  55       3.058  39.623  80.709  1.00 41.26           O  
ATOM    372  CB  VAL A  55       5.264  37.879  78.876  1.00 34.79           C  
ATOM    373  CG1 VAL A  55       5.208  37.735  77.385  1.00 36.65           C  
ATOM    374  CG2 VAL A  55       5.795  39.236  79.240  1.00 34.01           C  
ATOM    375  N   ILE A  56       2.431  39.473  78.554  1.00 40.58           N  
ATOM    376  CA  ILE A  56       1.670  40.718  78.635  1.00 41.04           C  
ATOM    377  C   ILE A  56       0.503  40.607  79.625  1.00 42.19           C  
ATOM    378  O   ILE A  56       0.241  41.537  80.398  1.00 42.47           O  
ATOM    379  CB  ILE A  56       1.095  41.133  77.275  1.00 40.87           C  
ATOM    380  CG1 ILE A  56       2.233  41.458  76.305  1.00 40.16           C  
ATOM    381  CG2 ILE A  56       0.154  42.329  77.463  1.00 38.84           C  
ATOM    382  CD1 ILE A  56       1.788  42.024  75.004  1.00 38.70           C  
ATOM    383  N   TYR A  57      -0.179  39.462  79.606  1.00 42.50           N  
ATOM    384  CA  TYR A  57      -1.322  39.209  80.491  1.00 42.59           C  
ATOM    385  C   TYR A  57      -0.893  39.172  81.947  1.00 40.18           C  
ATOM    386  O   TYR A  57      -1.369  39.971  82.753  1.00 38.22           O  
ATOM    387  CB  TYR A  57      -2.030  37.891  80.080  1.00 45.66           C  
ATOM    388  CG  TYR A  57      -3.224  37.508  80.911  1.00 49.55           C  
ATOM    389  CD1 TYR A  57      -3.170  36.386  81.725  1.00 50.94           C  
ATOM    390  CD2 TYR A  57      -4.383  38.304  80.930  1.00 52.01           C  
ATOM    391  CE1 TYR A  57      -4.226  36.058  82.553  1.00 59.35           C  
ATOM    392  CE2 TYR A  57      -5.464  37.997  81.759  1.00 57.72           C  
ATOM    393  CZ  TYR A  57      -5.387  36.867  82.579  1.00 61.06           C  
ATOM    394  OH  TYR A  57      -6.438  36.533  83.441  1.00 63.05           O  
ATOM    395  N   LEU A  58       0.026  38.261  82.267  1.00 41.60           N  
ATOM    396  CA  LEU A  58       0.549  38.072  83.638  1.00 41.47           C  
ATOM    397  C   LEU A  58       1.256  39.287  84.212  1.00 43.51           C  
ATOM    398  O   LEU A  58       1.036  39.617  85.375  1.00 45.50           O  
ATOM    399  CB  LEU A  58       1.494  36.859  83.715  1.00 34.27           C  
ATOM    400  CG  LEU A  58       0.906  35.530  84.200  1.00 32.09           C  
ATOM    401  CD1 LEU A  58      -0.547  35.409  83.850  1.00 32.88           C  
ATOM    402  CD2 LEU A  58       1.639  34.386  83.560  1.00 31.27           C  
ATOM    403  N   PHE A  59       2.106  39.949  83.427  1.00 44.33           N  
ATOM    404  CA  PHE A  59       2.788  41.123  83.942  1.00 44.45           C  
ATOM    405  C   PHE A  59       1.862  42.292  84.207  1.00 47.13           C  
ATOM    406  O   PHE A  59       1.976  42.933  85.238  1.00 48.37           O  
ATOM    407  CB  PHE A  59       3.937  41.562  83.035  1.00 42.07           C  
ATOM    408  CG  PHE A  59       5.240  40.913  83.387  1.00 41.31           C  
ATOM    409  CD1 PHE A  59       5.475  39.566  83.078  1.00 37.24           C  
ATOM    410  CD2 PHE A  59       6.219  41.628  84.074  1.00 40.12           C  
ATOM    411  CE1 PHE A  59       6.659  38.941  83.448  1.00 35.12           C  
ATOM    412  CE2 PHE A  59       7.408  41.003  84.448  1.00 40.05           C  
ATOM    413  CZ  PHE A  59       7.628  39.646  84.132  1.00 35.53           C  
ATOM    414  N   THR A  60       0.932  42.588  83.315  1.00 50.36           N  
ATOM    415  CA  THR A  60       0.044  43.714  83.594  1.00 53.99           C  
ATOM    416  C   THR A  60      -0.949  43.414  84.727  1.00 57.00           C  
ATOM    417  O   THR A  60      -1.447  44.345  85.376  1.00 60.35           O  
ATOM    418  CB  THR A  60      -0.783  44.154  82.343  1.00 53.37           C  
ATOM    419  OG1 THR A  60      -1.358  43.012  81.683  1.00 56.27           O  
ATOM    420  CG2 THR A  60       0.085  44.887  81.378  1.00 54.95           C  
ATOM    421  N   LYS A  61      -1.213  42.132  84.996  1.00 56.72           N  
ATOM    422  CA  LYS A  61      -2.203  41.780  85.995  1.00 55.61           C  
ATOM    423  C   LYS A  61      -1.713  41.185  87.293  1.00 56.42           C  
ATOM    424  O   LYS A  61      -2.463  41.141  88.278  1.00 59.95           O  
ATOM    425  CB  LYS A  61      -3.244  40.853  85.356  1.00 57.23           C  
ATOM    426  CG  LYS A  61      -4.049  41.504  84.204  1.00 57.23           C  
ATOM    427  CD  LYS A  61      -4.835  42.725  84.689  1.00 53.41           C  
ATOM    428  CE  LYS A  61      -5.355  43.522  83.533  1.00 51.68           C  
ATOM    429  NZ  LYS A  61      -5.948  44.770  84.016  1.00 53.86           N  
ATOM    430  N   THR A  62      -0.483  40.685  87.316  1.00 55.50           N  
ATOM    431  CA  THR A  62       0.013  40.125  88.573  1.00 52.55           C  
ATOM    432  C   THR A  62       0.488  41.295  89.451  1.00 53.54           C  
ATOM    433  O   THR A  62       1.018  42.302  88.955  1.00 52.54           O  
ATOM    434  CB  THR A  62       1.175  39.128  88.374  1.00 49.35           C  
ATOM    435  OG1 THR A  62       0.749  38.009  87.575  1.00 43.90           O  
ATOM    436  CG2 THR A  62       1.638  38.656  89.728  1.00 44.96           C  
ATOM    437  N   LYS A  63       0.279  41.161  90.752  1.00 52.59           N  
ATOM    438  CA  LYS A  63       0.653  42.207  91.675  1.00 52.04           C  
ATOM    439  C   LYS A  63       2.137  42.241  91.859  1.00 52.56           C  
ATOM    440  O   LYS A  63       2.749  43.301  91.947  1.00 52.84           O  
ATOM    441  CB  LYS A  63       0.007  41.965  93.035  1.00 51.83           C  
ATOM    442  CG  LYS A  63       0.469  42.912  94.148  1.00 52.36           C  
ATOM    443  CD  LYS A  63       1.099  42.148  95.317  1.00 51.95           C  
ATOM    444  CE  LYS A  63       0.695  42.709  96.676  1.00 53.06           C  
ATOM    445  NZ  LYS A  63      -0.622  42.161  97.103  1.00 52.85           N  
ATOM    446  N   SER A  64       2.716  41.058  91.921  1.00 52.86           N  
ATOM    447  CA  SER A  64       4.139  40.920  92.153  1.00 54.77           C  
ATOM    448  C   SER A  64       5.041  41.580  91.105  1.00 57.38           C  
ATOM    449  O   SER A  64       6.084  42.173  91.430  1.00 59.14           O  
ATOM    450  CB  SER A  64       4.451  39.445  92.232  1.00 53.10           C  
ATOM    451  OG  SER A  64       3.859  38.811  91.134  1.00 48.57           O  
ATOM    452  N   LEU A  65       4.630  41.452  89.850  1.00 57.97           N  
ATOM    453  CA  LEU A  65       5.352  41.991  88.719  1.00 59.41           C  
ATOM    454  C   LEU A  65       4.851  43.447  88.427  1.00 62.35           C  
ATOM    455  O   LEU A  65       4.741  43.872  87.270  1.00 63.70           O  
ATOM    456  CB  LEU A  65       5.111  41.035  87.517  1.00 58.46           C  
ATOM    457  CG  LEU A  65       4.773  39.525  87.740  1.00 56.69           C  
ATOM    458  CD1 LEU A  65       4.212  38.898  86.459  1.00 57.98           C  
ATOM    459  CD2 LEU A  65       5.993  38.718  88.178  1.00 55.97           C  
ATOM    460  N   GLN A  66       4.581  44.229  89.470  1.00 65.05           N  
ATOM    461  CA  GLN A  66       4.051  45.584  89.266  1.00 68.20           C  
ATOM    462  C   GLN A  66       5.019  46.787  89.321  1.00 70.91           C  
ATOM    463  O   GLN A  66       4.546  47.934  89.509  1.00 75.39           O  
ATOM    464  CB  GLN A  66       2.906  45.858  90.270  1.00 68.14           C  
ATOM    465  CG  GLN A  66       1.681  46.544  89.686  1.00 64.08           C  
ATOM    466  CD  GLN A  66       1.162  45.774  88.521  1.00 64.86           C  
ATOM    467  OE1 GLN A  66       1.661  45.916  87.408  1.00 66.24           O  
ATOM    468  NE2 GLN A  66       0.176  44.921  88.764  1.00 66.01           N  
ATOM    469  N   THR A  67       6.333  46.579  89.161  1.00 68.75           N  
ATOM    470  CA  THR A  67       7.285  47.709  89.218  1.00 65.83           C  
ATOM    471  C   THR A  67       7.466  48.323  87.845  1.00 63.20           C  
ATOM    472  O   THR A  67       7.329  47.613  86.859  1.00 63.90           O  
ATOM    473  CB  THR A  67       8.636  47.268  89.688  1.00 67.17           C  
ATOM    474  OG1 THR A  67       9.204  46.426  88.682  1.00 69.82           O  
ATOM    475  CG2 THR A  67       8.519  46.505  91.009  1.00 69.00           C  
ATOM    476  N   PRO A  68       7.804  49.639  87.766  1.00 61.13           N  
ATOM    477  CA  PRO A  68       8.007  50.395  86.519  1.00 60.60           C  
ATOM    478  C   PRO A  68       8.877  49.748  85.426  1.00 61.30           C  
ATOM    479  O   PRO A  68       8.514  49.746  84.231  1.00 59.69           O  
ATOM    480  CB  PRO A  68       8.579  51.727  87.013  1.00 57.83           C  
ATOM    481  CG  PRO A  68       7.916  51.916  88.265  1.00 58.12           C  
ATOM    482  CD  PRO A  68       8.040  50.536  88.911  1.00 60.60           C  
ATOM    483  N   ALA A  69      10.030  49.213  85.831  1.00 62.50           N  
ATOM    484  CA  ALA A  69      10.951  48.558  84.892  1.00 63.43           C  
ATOM    485  C   ALA A  69      10.262  47.426  84.097  1.00 64.51           C  
ATOM    486  O   ALA A  69      10.557  47.225  82.906  1.00 66.81           O  
ATOM    487  CB  ALA A  69      12.164  48.012  85.642  1.00 61.66           C  
ATOM    488  N   ASN A  70       9.354  46.691  84.751  1.00 63.03           N  
ATOM    489  CA  ASN A  70       8.615  45.613  84.091  1.00 60.94           C  
ATOM    490  C   ASN A  70       7.822  46.089  82.860  1.00 59.00           C  
ATOM    491  O   ASN A  70       7.452  45.278  81.988  1.00 57.87           O  
ATOM    492  CB  ASN A  70       7.682  44.935  85.093  1.00 63.73           C  
ATOM    493  CG  ASN A  70       8.395  43.876  85.900  1.00 65.97           C  
ATOM    494  OD1 ASN A  70       7.846  43.292  86.842  1.00 66.44           O  
ATOM    495  ND2 ASN A  70       9.644  43.613  85.525  1.00 68.23           N  
ATOM    496  N   MET A  71       7.547  47.398  82.811  1.00 55.41           N  
ATOM    497  CA  MET A  71       6.863  47.996  81.680  1.00 54.08           C  
ATOM    498  C   MET A  71       7.702  47.669  80.401  1.00 55.20           C  
ATOM    499  O   MET A  71       7.161  47.327  79.330  1.00 55.74           O  
ATOM    500  CB  MET A  71       6.740  49.509  81.894  1.00 51.48           C  
ATOM    501  CG  MET A  71       5.715  49.936  82.943  1.00 49.67           C  
ATOM    502  SD  MET A  71       5.680  51.775  83.285  1.00 52.77           S  
ATOM    503  CE  MET A  71       5.388  52.484  81.577  1.00 47.06           C  
ATOM    504  N   PHE A  72       9.030  47.749  80.524  1.00 55.57           N  
ATOM    505  CA  PHE A  72       9.937  47.440  79.409  1.00 52.63           C  
ATOM    506  C   PHE A  72       9.621  46.048  78.906  1.00 52.50           C  
ATOM    507  O   PHE A  72       9.429  45.852  77.704  1.00 50.05           O  
ATOM    508  CB  PHE A  72      11.411  47.514  79.854  1.00 47.48           C  
ATOM    509  CG  PHE A  72      11.841  48.884  80.292  1.00 43.93           C  
ATOM    510  CD1 PHE A  72      11.358  50.027  79.638  1.00 43.25           C  
ATOM    511  CD2 PHE A  72      12.709  49.038  81.358  1.00 41.69           C  
ATOM    512  CE1 PHE A  72      11.728  51.298  80.045  1.00 44.09           C  
ATOM    513  CE2 PHE A  72      13.087  50.307  81.777  1.00 44.21           C  
ATOM    514  CZ  PHE A  72      12.595  51.445  81.121  1.00 44.29           C  
ATOM    515  N   ILE A  73       9.552  45.101  79.846  1.00 54.94           N  
ATOM    516  CA  ILE A  73       9.248  43.695  79.529  1.00 58.17           C  
ATOM    517  C   ILE A  73       7.948  43.560  78.752  1.00 57.66           C  
ATOM    518  O   ILE A  73       7.879  42.801  77.762  1.00 57.69           O  
ATOM    519  CB  ILE A  73       9.115  42.816  80.804  1.00 62.38           C  
ATOM    520  CG1 ILE A  73      10.521  42.508  81.379  1.00 65.95           C  
ATOM    521  CG2 ILE A  73       8.358  41.512  80.470  1.00 61.10           C  
ATOM    522  CD1 ILE A  73      10.503  41.625  82.660  1.00 68.48           C  
ATOM    523  N   ILE A  74       6.917  44.280  79.218  1.00 54.40           N  
ATOM    524  CA  ILE A  74       5.611  44.269  78.562  1.00 47.94           C  
ATOM    525  C   ILE A  74       5.773  44.818  77.143  1.00 47.22           C  
ATOM    526  O   ILE A  74       5.262  44.224  76.178  1.00 43.32           O  
ATOM    527  CB  ILE A  74       4.592  45.115  79.370  1.00 44.36           C  
ATOM    528  CG1 ILE A  74       4.296  44.404  80.701  1.00 43.06           C  
ATOM    529  CG2 ILE A  74       3.343  45.328  78.559  1.00 41.93           C  
ATOM    530  CD1 ILE A  74       3.403  45.137  81.634  1.00 41.25           C  
ATOM    531  N   ASN A  75       6.531  45.928  77.038  1.00 48.04           N  
ATOM    532  CA  ASN A  75       6.786  46.613  75.773  1.00 47.99           C  
ATOM    533  C   ASN A  75       7.484  45.686  74.801  1.00 46.18           C  
ATOM    534  O   ASN A  75       7.199  45.680  73.602  1.00 46.84           O  
ATOM    535  CB  ASN A  75       7.629  47.859  75.995  1.00 49.53           C  
ATOM    536  CG  ASN A  75       7.769  48.677  74.728  1.00 55.66           C  
ATOM    537  OD1 ASN A  75       6.808  49.287  74.225  1.00 56.77           O  
ATOM    538  ND2 ASN A  75       8.974  48.680  74.180  1.00 62.46           N  
ATOM    539  N   LEU A  76       8.396  44.890  75.338  1.00 44.85           N  
ATOM    540  CA  LEU A  76       9.149  43.914  74.552  1.00 40.84           C  
ATOM    541  C   LEU A  76       8.196  42.815  74.023  1.00 38.21           C  
ATOM    542  O   LEU A  76       8.242  42.425  72.828  1.00 33.61           O  
ATOM    543  CB  LEU A  76      10.252  43.296  75.433  1.00 40.34           C  
ATOM    544  CG  LEU A  76      11.631  42.956  74.822  1.00 38.35           C  
ATOM    545  CD1 LEU A  76      12.331  42.005  75.738  1.00 40.48           C  
ATOM    546  CD2 LEU A  76      11.515  42.281  73.483  1.00 37.42           C  
ATOM    547  N   ALA A  77       7.331  42.326  74.916  1.00 37.99           N  
ATOM    548  CA  ALA A  77       6.333  41.297  74.556  1.00 37.84           C  
ATOM    549  C   ALA A  77       5.328  41.799  73.529  1.00 36.62           C  
ATOM    550  O   ALA A  77       4.934  41.031  72.657  1.00 36.26           O  
ATOM    551  CB  ALA A  77       5.591  40.825  75.774  1.00 39.10           C  
ATOM    552  N   PHE A  78       4.902  43.065  73.650  1.00 33.72           N  
ATOM    553  CA  PHE A  78       3.988  43.643  72.691  1.00 33.50           C  
ATOM    554  C   PHE A  78       4.693  43.653  71.346  1.00 35.33           C  
ATOM    555  O   PHE A  78       4.088  43.382  70.305  1.00 34.88           O  
ATOM    556  CB  PHE A  78       3.642  45.082  73.036  1.00 34.72           C  
ATOM    557  CG  PHE A  78       2.667  45.700  72.069  1.00 39.04           C  
ATOM    558  CD1 PHE A  78       1.293  45.761  72.369  1.00 40.98           C  
ATOM    559  CD2 PHE A  78       3.090  46.118  70.814  1.00 39.29           C  
ATOM    560  CE1 PHE A  78       0.347  46.221  71.427  1.00 39.26           C  
ATOM    561  CE2 PHE A  78       2.167  46.573  69.877  1.00 43.65           C  
ATOM    562  CZ  PHE A  78       0.776  46.622  70.187  1.00 43.16           C  
ATOM    563  N   SER A  79       5.978  44.001  71.379  1.00 38.23           N  
ATOM    564  CA  SER A  79       6.833  44.067  70.185  1.00 38.92           C  
ATOM    565  C   SER A  79       6.950  42.708  69.515  1.00 39.62           C  
ATOM    566  O   SER A  79       6.702  42.558  68.295  1.00 37.02           O  
ATOM    567  CB  SER A  79       8.231  44.541  70.570  1.00 41.46           C  
ATOM    568  OG  SER A  79       9.054  44.713  69.419  1.00 42.59           O  
ATOM    569  N   ASP A  80       7.357  41.718  70.312  1.00 40.37           N  
ATOM    570  CA  ASP A  80       7.480  40.358  69.796  1.00 42.74           C  
ATOM    571  C   ASP A  80       6.146  39.717  69.416  1.00 42.50           C  
ATOM    572  O   ASP A  80       6.102  38.909  68.493  1.00 41.76           O  
ATOM    573  CB  ASP A  80       8.186  39.513  70.811  1.00 47.31           C  
ATOM    574  CG  ASP A  80       9.575  39.978  71.023  1.00 52.91           C  
ATOM    575  OD1 ASP A  80      10.213  39.499  71.986  1.00 61.64           O  
ATOM    576  OD2 ASP A  80      10.032  40.831  70.227  1.00 50.14           O  
ATOM    577  N   PHE A  81       5.067  40.058  70.136  1.00 41.07           N  
ATOM    578  CA  PHE A  81       3.748  39.535  69.821  1.00 37.13           C  
ATOM    579  C   PHE A  81       3.393  39.969  68.385  1.00 38.89           C  
ATOM    580  O   PHE A  81       3.089  39.129  67.535  1.00 37.97           O  
ATOM    581  CB  PHE A  81       2.710  40.096  70.806  1.00 36.12           C  
ATOM    582  CG  PHE A  81       1.279  39.687  70.492  1.00 37.03           C  
ATOM    583  CD1 PHE A  81       0.820  38.418  70.839  1.00 34.76           C  
ATOM    584  CD2 PHE A  81       0.438  40.529  69.736  1.00 35.86           C  
ATOM    585  CE1 PHE A  81      -0.406  37.989  70.439  1.00 29.97           C  
ATOM    586  CE2 PHE A  81      -0.798  40.104  69.326  1.00 32.07           C  
ATOM    587  CZ  PHE A  81      -1.218  38.828  69.675  1.00 33.31           C  
ATOM    588  N   THR A  82       3.451  41.279  68.130  1.00 38.67           N  
ATOM    589  CA  THR A  82       3.097  41.856  66.843  1.00 41.01           C  
ATOM    590  C   THR A  82       3.997  41.326  65.736  1.00 44.04           C  
ATOM    591  O   THR A  82       3.537  41.094  64.604  1.00 47.39           O  
ATOM    592  CB  THR A  82       3.199  43.431  66.864  1.00 43.49           C  
ATOM    593  OG1 THR A  82       2.680  43.955  68.100  1.00 39.52           O  
ATOM    594  CG2 THR A  82       2.418  44.046  65.685  1.00 43.26           C  
ATOM    595  N   PHE A  83       5.283  41.143  66.038  1.00 43.18           N  
ATOM    596  CA  PHE A  83       6.189  40.637  65.016  1.00 40.34           C  
ATOM    597  C   PHE A  83       5.713  39.260  64.566  1.00 37.87           C  
ATOM    598  O   PHE A  83       5.512  39.011  63.393  1.00 35.28           O  
ATOM    599  CB  PHE A  83       7.607  40.536  65.566  1.00 39.78           C  
ATOM    600  CG  PHE A  83       8.629  40.231  64.518  1.00 40.02           C  
ATOM    601  CD1 PHE A  83       9.407  41.253  63.994  1.00 39.67           C  
ATOM    602  CD2 PHE A  83       8.802  38.919  64.032  1.00 41.71           C  
ATOM    603  CE1 PHE A  83      10.354  40.992  63.001  1.00 42.15           C  
ATOM    604  CE2 PHE A  83       9.746  38.633  63.036  1.00 42.76           C  
ATOM    605  CZ  PHE A  83      10.531  39.675  62.516  1.00 43.64           C  
ATOM    606  N   SER A  84       5.504  38.387  65.535  1.00 38.00           N  
ATOM    607  CA  SER A  84       5.089  37.031  65.279  1.00 39.01           C  
ATOM    608  C   SER A  84       3.752  36.980  64.560  1.00 41.28           C  
ATOM    609  O   SER A  84       3.569  36.139  63.658  1.00 42.69           O  
ATOM    610  CB  SER A  84       5.004  36.271  66.601  1.00 42.55           C  
ATOM    611  OG  SER A  84       6.233  36.354  67.358  1.00 43.49           O  
ATOM    612  N   LEU A  85       2.816  37.861  64.952  1.00 41.50           N  
ATOM    613  CA  LEU A  85       1.481  37.915  64.324  1.00 39.88           C  
ATOM    614  C   LEU A  85       1.597  38.303  62.838  1.00 41.18           C  
ATOM    615  O   LEU A  85       1.231  37.538  61.918  1.00 43.13           O  
ATOM    616  CB  LEU A  85       0.590  38.958  65.017  1.00 35.87           C  
ATOM    617  CG  LEU A  85      -0.959  38.801  64.998  1.00 35.22           C  
ATOM    618  CD1 LEU A  85      -1.564  40.211  64.832  1.00 34.25           C  
ATOM    619  CD2 LEU A  85      -1.490  37.890  63.885  1.00 29.17           C  
ATOM    620  N   VAL A  86       2.120  39.498  62.604  1.00 40.31           N  
ATOM    621  CA  VAL A  86       2.243  39.996  61.251  1.00 41.60           C  
ATOM    622  C   VAL A  86       3.199  39.201  60.356  1.00 43.75           C  
ATOM    623  O   VAL A  86       2.922  38.976  59.186  1.00 46.27           O  
ATOM    624  CB  VAL A  86       2.637  41.522  61.251  1.00 39.60           C  
ATOM    625  CG1 VAL A  86       2.723  42.049  59.809  1.00 36.52           C  
ATOM    626  CG2 VAL A  86       1.600  42.353  62.018  1.00 35.31           C  
ATOM    627  N   ASN A  87       4.316  38.752  60.898  1.00 46.56           N  
ATOM    628  CA  ASN A  87       5.290  38.016  60.081  1.00 47.87           C  
ATOM    629  C   ASN A  87       5.050  36.519  59.848  1.00 46.39           C  
ATOM    630  O   ASN A  87       5.730  35.908  59.023  1.00 46.60           O  
ATOM    631  CB  ASN A  87       6.684  38.226  60.667  1.00 49.27           C  
ATOM    632  CG  ASN A  87       7.151  39.637  60.488  1.00 51.53           C  
ATOM    633  OD1 ASN A  87       7.499  40.026  59.376  1.00 55.01           O  
ATOM    634  ND2 ASN A  87       7.136  40.429  61.564  1.00 52.58           N  
ATOM    635  N   GLY A  88       4.092  35.935  60.565  1.00 45.30           N  
ATOM    636  CA  GLY A  88       3.812  34.511  60.421  1.00 42.83           C  
ATOM    637  C   GLY A  88       2.541  34.224  59.645  1.00 42.29           C  
ATOM    638  O   GLY A  88       2.540  34.226  58.398  1.00 42.42           O  
ATOM    639  N   PHE A  89       1.461  33.954  60.383  1.00 39.57           N  
ATOM    640  CA  PHE A  89       0.149  33.698  59.788  1.00 38.64           C  
ATOM    641  C   PHE A  89      -0.705  34.971  59.829  1.00 37.70           C  
ATOM    642  O   PHE A  89      -0.758  35.657  60.842  1.00 37.28           O  
ATOM    643  CB  PHE A  89      -0.568  32.576  60.518  1.00 37.32           C  
ATOM    644  CG  PHE A  89      -1.952  32.334  60.006  1.00 39.40           C  
ATOM    645  CD1 PHE A  89      -3.030  33.051  60.500  1.00 39.64           C  
ATOM    646  CD2 PHE A  89      -2.183  31.428  58.989  1.00 41.67           C  
ATOM    647  CE1 PHE A  89      -4.313  32.870  59.987  1.00 38.28           C  
ATOM    648  CE2 PHE A  89      -3.480  31.246  58.472  1.00 42.16           C  
ATOM    649  CZ  PHE A  89      -4.537  31.969  58.975  1.00 38.74           C  
ATOM    650  N   PRO A  90      -1.400  35.288  58.730  1.00 36.89           N  
ATOM    651  CA  PRO A  90      -1.465  34.556  57.456  1.00 38.39           C  
ATOM    652  C   PRO A  90      -0.614  35.070  56.256  1.00 38.74           C  
ATOM    653  O   PRO A  90      -0.472  34.375  55.227  1.00 34.81           O  
ATOM    654  CB  PRO A  90      -2.943  34.630  57.133  1.00 39.78           C  
ATOM    655  CG  PRO A  90      -3.234  36.088  57.485  1.00 41.55           C  
ATOM    656  CD  PRO A  90      -2.468  36.301  58.801  1.00 37.90           C  
ATOM    657  N   LEU A  91      -0.063  36.282  56.385  1.00 38.28           N  
ATOM    658  CA  LEU A  91       0.714  36.874  55.299  1.00 38.57           C  
ATOM    659  C   LEU A  91       1.783  35.960  54.688  1.00 39.18           C  
ATOM    660  O   LEU A  91       1.845  35.770  53.464  1.00 35.67           O  
ATOM    661  CB  LEU A  91       1.336  38.213  55.761  1.00 35.86           C  
ATOM    662  CG  LEU A  91       0.312  39.321  55.980  1.00 35.13           C  
ATOM    663  CD1 LEU A  91       1.015  40.571  56.402  1.00 34.52           C  
ATOM    664  CD2 LEU A  91      -0.478  39.580  54.692  1.00 33.62           C  
ATOM    665  N   MET A  92       2.621  35.375  55.532  1.00 41.12           N  
ATOM    666  CA  MET A  92       3.671  34.531  54.997  1.00 43.61           C  
ATOM    667  C   MET A  92       3.206  33.091  54.808  1.00 43.79           C  
ATOM    668  O   MET A  92       3.290  32.521  53.713  1.00 42.79           O  
ATOM    669  CB  MET A  92       4.914  34.568  55.904  1.00 44.80           C  
ATOM    670  CG  MET A  92       6.118  33.877  55.253  1.00 46.49           C  
ATOM    671  SD  MET A  92       7.710  33.867  56.132  1.00 45.01           S  
ATOM    672  CE  MET A  92       8.699  32.978  54.894  1.00 41.25           C  
ATOM    673  N   THR A  93       2.699  32.515  55.883  1.00 43.93           N  
ATOM    674  CA  THR A  93       2.234  31.144  55.841  1.00 47.59           C  
ATOM    675  C   THR A  93       1.360  30.872  54.618  1.00 49.59           C  
ATOM    676  O   THR A  93       1.569  29.879  53.905  1.00 52.00           O  
ATOM    677  CB  THR A  93       1.433  30.786  57.115  1.00 47.78           C  
ATOM    678  OG1 THR A  93       2.251  31.022  58.265  1.00 50.41           O  
ATOM    679  CG2 THR A  93       1.016  29.333  57.095  1.00 45.82           C  
ATOM    680  N   ILE A  94       0.366  31.736  54.373  1.00 49.48           N  
ATOM    681  CA  ILE A  94      -0.530  31.553  53.206  1.00 46.28           C  
ATOM    682  C   ILE A  94       0.248  31.741  51.890  1.00 44.25           C  
ATOM    683  O   ILE A  94       0.028  31.018  50.930  1.00 42.96           O  
ATOM    684  CB  ILE A  94      -1.750  32.526  53.267  1.00 43.06           C  
ATOM    685  CG1 ILE A  94      -2.687  32.079  54.386  1.00 43.91           C  
ATOM    686  CG2 ILE A  94      -2.538  32.504  51.965  1.00 42.92           C  
ATOM    687  CD1 ILE A  94      -3.300  30.692  54.163  1.00 37.39           C  
ATOM    688  N   SER A  95       1.165  32.703  51.870  1.00 42.94           N  
ATOM    689  CA  SER A  95       1.956  32.966  50.699  1.00 39.79           C  
ATOM    690  C   SER A  95       2.715  31.720  50.391  1.00 38.95           C  
ATOM    691  O   SER A  95       2.768  31.293  49.244  1.00 40.19           O  
ATOM    692  CB  SER A  95       2.946  34.088  50.956  1.00 40.34           C  
ATOM    693  OG  SER A  95       2.354  35.351  50.790  1.00 43.33           O  
ATOM    694  N   CYS A  96       3.312  31.119  51.409  1.00 39.19           N  
ATOM    695  CA  CYS A  96       4.079  29.895  51.168  1.00 41.28           C  
ATOM    696  C   CYS A  96       3.227  28.778  50.513  1.00 41.30           C  
ATOM    697  O   CYS A  96       3.511  28.323  49.391  1.00 41.17           O  
ATOM    698  CB  CYS A  96       4.721  29.383  52.477  1.00 39.15           C  
ATOM    699  SG  CYS A  96       6.037  30.429  53.170  1.00 35.67           S  
ATOM    700  N   PHE A  97       2.171  28.367  51.197  1.00 41.31           N  
ATOM    701  CA  PHE A  97       1.320  27.314  50.676  1.00 42.88           C  
ATOM    702  C   PHE A  97       0.809  27.516  49.264  1.00 41.33           C  
ATOM    703  O   PHE A  97       0.280  26.584  48.679  1.00 43.73           O  
ATOM    704  CB  PHE A  97       0.126  27.058  51.608  1.00 47.46           C  
ATOM    705  CG  PHE A  97       0.517  26.644  53.012  1.00 49.79           C  
ATOM    706  CD1 PHE A  97       1.619  25.803  53.232  1.00 51.34           C  
ATOM    707  CD2 PHE A  97      -0.199  27.117  54.113  1.00 50.52           C  
ATOM    708  CE1 PHE A  97       2.022  25.441  54.546  1.00 52.34           C  
ATOM    709  CE2 PHE A  97       0.186  26.759  55.428  1.00 52.68           C  
ATOM    710  CZ  PHE A  97       1.306  25.919  55.647  1.00 50.65           C  
ATOM    711  N   LEU A  98       0.945  28.716  48.714  1.00 40.80           N  
ATOM    712  CA  LEU A  98       0.500  28.985  47.336  1.00 41.20           C  
ATOM    713  C   LEU A  98       1.718  29.276  46.490  1.00 43.15           C  
ATOM    714  O   LEU A  98       1.618  29.418  45.276  1.00 43.23           O  
ATOM    715  CB  LEU A  98      -0.433  30.198  47.275  1.00 37.30           C  
ATOM    716  CG  LEU A  98      -1.772  30.112  47.982  1.00 32.90           C  
ATOM    717  CD1 LEU A  98      -2.399  31.475  48.047  1.00 29.38           C  
ATOM    718  CD2 LEU A  98      -2.637  29.138  47.249  1.00 29.94           C  
ATOM    719  N   LYS A  99       2.865  29.398  47.165  1.00 45.67           N  
ATOM    720  CA  LYS A  99       4.140  29.694  46.510  1.00 46.36           C  
ATOM    721  C   LYS A  99       4.068  31.043  45.802  1.00 44.77           C  
ATOM    722  O   LYS A  99       4.497  31.157  44.644  1.00 44.29           O  
ATOM    723  CB  LYS A  99       4.453  28.569  45.515  1.00 48.42           C  
ATOM    724  CG  LYS A  99       4.542  27.225  46.202  1.00 48.77           C  
ATOM    725  CD  LYS A  99       3.887  26.158  45.400  1.00 51.62           C  
ATOM    726  CE  LYS A  99       4.601  25.971  44.085  1.00 53.26           C  
ATOM    727  NZ  LYS A  99       4.274  24.600  43.560  1.00 58.52           N  
ATOM    728  N   LYS A 100       3.521  32.041  46.513  1.00 44.95           N  
ATOM    729  CA  LYS A 100       3.323  33.418  46.012  1.00 47.01           C  
ATOM    730  C   LYS A 100       2.631  34.363  47.023  1.00 47.14           C  
ATOM    731  O   LYS A 100       1.595  34.012  47.604  1.00 49.34           O  
ATOM    732  CB  LYS A 100       2.485  33.405  44.725  1.00 48.62           C  
ATOM    733  CG  LYS A 100       2.645  34.641  43.856  1.00 52.41           C  
ATOM    734  CD  LYS A 100       2.268  34.369  42.364  1.00 56.05           C  
ATOM    735  CE  LYS A 100       3.149  33.286  41.641  1.00 56.19           C  
ATOM    736  NZ  LYS A 100       4.658  33.457  41.724  1.00 56.86           N  
ATOM    737  N   TRP A 101       3.207  35.559  47.218  1.00 46.26           N  
ATOM    738  CA  TRP A 101       2.691  36.592  48.137  1.00 42.17           C  
ATOM    739  C   TRP A 101       1.548  37.224  47.396  1.00 41.85           C  
ATOM    740  O   TRP A 101       1.754  38.093  46.547  1.00 43.57           O  
ATOM    741  CB  TRP A 101       3.781  37.632  48.426  1.00 41.22           C  
ATOM    742  CG  TRP A 101       3.318  38.851  49.172  1.00 40.55           C  
ATOM    743  CD1 TRP A 101       2.786  39.998  48.628  1.00 41.44           C  
ATOM    744  CD2 TRP A 101       3.326  39.053  50.608  1.00 38.65           C  
ATOM    745  NE1 TRP A 101       2.466  40.895  49.638  1.00 42.22           N  
ATOM    746  CE2 TRP A 101       2.787  40.337  50.857  1.00 38.70           C  
ATOM    747  CE3 TRP A 101       3.734  38.277  51.698  1.00 36.79           C  
ATOM    748  CZ2 TRP A 101       2.647  40.854  52.164  1.00 37.69           C  
ATOM    749  CZ3 TRP A 101       3.590  38.806  52.999  1.00 35.00           C  
ATOM    750  CH2 TRP A 101       3.053  40.071  53.211  1.00 33.65           C  
ATOM    751  N   ILE A 102       0.349  36.771  47.738  1.00 41.16           N  
ATOM    752  CA  ILE A 102      -0.888  37.189  47.096  1.00 42.55           C  
ATOM    753  C   ILE A 102      -1.543  38.409  47.679  1.00 42.29           C  
ATOM    754  O   ILE A 102      -2.615  38.817  47.192  1.00 44.36           O  
ATOM    755  CB  ILE A 102      -1.943  36.045  47.146  1.00 43.99           C  
ATOM    756  CG1 ILE A 102      -2.202  35.622  48.620  1.00 46.74           C  
ATOM    757  CG2 ILE A 102      -1.431  34.873  46.353  1.00 43.65           C  
ATOM    758  CD1 ILE A 102      -3.470  34.761  48.902  1.00 44.57           C  
ATOM    759  N   PHE A 103      -0.904  38.981  48.703  1.00 40.10           N  
ATOM    760  CA  PHE A 103      -1.425  40.150  49.425  1.00 38.84           C  
ATOM    761  C   PHE A 103      -1.011  41.545  48.953  1.00 36.90           C  
ATOM    762  O   PHE A 103      -1.129  42.541  49.671  1.00 33.32           O  
ATOM    763  CB  PHE A 103      -1.121  39.959  50.912  1.00 40.18           C  
ATOM    764  CG  PHE A 103      -1.571  38.626  51.436  1.00 43.48           C  
ATOM    765  CD1 PHE A 103      -2.919  38.352  51.605  1.00 45.98           C  
ATOM    766  CD2 PHE A 103      -0.653  37.605  51.652  1.00 46.55           C  
ATOM    767  CE1 PHE A 103      -3.346  37.062  51.969  1.00 48.63           C  
ATOM    768  CE2 PHE A 103      -1.061  36.308  52.020  1.00 47.15           C  
ATOM    769  CZ  PHE A 103      -2.405  36.038  52.174  1.00 49.06           C  
ATOM    770  N   GLY A 104      -0.513  41.589  47.733  1.00 37.40           N  
ATOM    771  CA  GLY A 104      -0.119  42.844  47.134  1.00 40.16           C  
ATOM    772  C   GLY A 104       0.985  43.686  47.740  1.00 40.71           C  
ATOM    773  O   GLY A 104       1.510  43.432  48.847  1.00 39.97           O  
ATOM    774  N   PHE A 105       1.312  44.744  47.005  1.00 41.40           N  
ATOM    775  CA  PHE A 105       2.388  45.624  47.434  1.00 44.18           C  
ATOM    776  C   PHE A 105       2.182  46.332  48.785  1.00 44.04           C  
ATOM    777  O   PHE A 105       3.080  46.325  49.643  1.00 46.87           O  
ATOM    778  CB  PHE A 105       2.692  46.666  46.355  1.00 45.74           C  
ATOM    779  CG  PHE A 105       4.129  47.106  46.332  1.00 46.99           C  
ATOM    780  CD1 PHE A 105       4.495  48.275  45.703  1.00 45.81           C  
ATOM    781  CD2 PHE A 105       5.128  46.308  46.896  1.00 51.09           C  
ATOM    782  CE1 PHE A 105       5.816  48.646  45.627  1.00 48.38           C  
ATOM    783  CE2 PHE A 105       6.478  46.674  46.827  1.00 52.29           C  
ATOM    784  CZ  PHE A 105       6.814  47.842  46.191  1.00 52.11           C  
ATOM    785  N   ALA A 106       1.016  46.932  48.998  1.00 41.88           N  
ATOM    786  CA  ALA A 106       0.796  47.623  50.250  1.00 37.74           C  
ATOM    787  C   ALA A 106       0.995  46.665  51.429  1.00 36.81           C  
ATOM    788  O   ALA A 106       1.616  47.025  52.420  1.00 35.84           O  
ATOM    789  CB  ALA A 106      -0.560  48.206  50.256  1.00 37.38           C  
ATOM    790  N   ALA A 107       0.509  45.433  51.308  1.00 35.12           N  
ATOM    791  CA  ALA A 107       0.657  44.475  52.398  1.00 34.56           C  
ATOM    792  C   ALA A 107       2.127  44.228  52.639  1.00 35.80           C  
ATOM    793  O   ALA A 107       2.609  44.194  53.774  1.00 38.09           O  
ATOM    794  CB  ALA A 107      -0.038  43.188  52.049  1.00 30.30           C  
ATOM    795  N   CYS A 108       2.837  44.058  51.535  1.00 36.68           N  
ATOM    796  CA  CYS A 108       4.264  43.828  51.550  1.00 37.41           C  
ATOM    797  C   CYS A 108       4.960  44.939  52.321  1.00 37.57           C  
ATOM    798  O   CYS A 108       5.759  44.666  53.221  1.00 40.67           O  
ATOM    799  CB  CYS A 108       4.749  43.792  50.125  1.00 37.99           C  
ATOM    800  SG  CYS A 108       6.495  43.447  49.875  1.00 43.61           S  
ATOM    801  N   LYS A 109       4.652  46.188  51.987  1.00 35.61           N  
ATOM    802  CA  LYS A 109       5.263  47.313  52.677  1.00 36.01           C  
ATOM    803  C   LYS A 109       4.997  47.247  54.168  1.00 38.91           C  
ATOM    804  O   LYS A 109       5.937  47.371  54.987  1.00 40.92           O  
ATOM    805  CB  LYS A 109       4.724  48.607  52.122  1.00 30.65           C  
ATOM    806  CG  LYS A 109       4.967  48.678  50.678  1.00 34.40           C  
ATOM    807  CD  LYS A 109       4.536  49.981  50.137  1.00 41.58           C  
ATOM    808  CE  LYS A 109       4.687  50.021  48.614  1.00 47.91           C  
ATOM    809  NZ  LYS A 109       4.452  51.404  48.055  1.00 52.63           N  
ATOM    810  N   VAL A 110       3.714  47.050  54.511  1.00 39.44           N  
ATOM    811  CA  VAL A 110       3.277  46.958  55.904  1.00 38.29           C  
ATOM    812  C   VAL A 110       4.007  45.826  56.577  1.00 39.67           C  
ATOM    813  O   VAL A 110       4.497  45.974  57.691  1.00 41.35           O  
ATOM    814  CB  VAL A 110       1.776  46.706  56.019  1.00 37.15           C  
ATOM    815  CG1 VAL A 110       1.447  46.195  57.416  1.00 31.76           C  
ATOM    816  CG2 VAL A 110       1.033  47.990  55.732  1.00 33.57           C  
ATOM    817  N   TYR A 111       4.094  44.699  55.889  1.00 38.90           N  
ATOM    818  CA  TYR A 111       4.792  43.571  56.444  1.00 41.73           C  
ATOM    819  C   TYR A 111       6.272  43.912  56.758  1.00 43.83           C  
ATOM    820  O   TYR A 111       6.745  43.832  57.914  1.00 40.51           O  
ATOM    821  CB  TYR A 111       4.718  42.429  55.467  1.00 44.34           C  
ATOM    822  CG  TYR A 111       5.372  41.147  55.962  1.00 47.71           C  
ATOM    823  CD1 TYR A 111       4.584  40.016  56.260  1.00 46.63           C  
ATOM    824  CD2 TYR A 111       6.778  41.039  56.068  1.00 43.88           C  
ATOM    825  CE1 TYR A 111       5.168  38.820  56.639  1.00 44.57           C  
ATOM    826  CE2 TYR A 111       7.363  39.843  56.456  1.00 43.91           C  
ATOM    827  CZ  TYR A 111       6.542  38.743  56.738  1.00 43.43           C  
ATOM    828  OH  TYR A 111       7.069  37.560  57.139  1.00 41.90           O  
ATOM    829  N   GLY A 112       7.007  44.291  55.722  1.00 45.54           N  
ATOM    830  CA  GLY A 112       8.402  44.638  55.921  1.00 49.08           C  
ATOM    831  C   GLY A 112       8.625  45.699  56.994  1.00 51.81           C  
ATOM    832  O   GLY A 112       9.508  45.564  57.862  1.00 53.30           O  
ATOM    833  N   PHE A 113       7.821  46.767  56.919  1.00 52.86           N  
ATOM    834  CA  PHE A 113       7.880  47.903  57.852  1.00 51.44           C  
ATOM    835  C   PHE A 113       7.598  47.480  59.312  1.00 49.26           C  
ATOM    836  O   PHE A 113       8.217  47.950  60.265  1.00 44.88           O  
ATOM    837  CB  PHE A 113       6.877  48.980  57.371  1.00 51.77           C  
ATOM    838  CG  PHE A 113       6.779  50.181  58.280  1.00 52.27           C  
ATOM    839  CD1 PHE A 113       7.921  50.889  58.652  1.00 50.78           C  
ATOM    840  CD2 PHE A 113       5.539  50.624  58.747  1.00 51.81           C  
ATOM    841  CE1 PHE A 113       7.828  52.021  59.473  1.00 49.55           C  
ATOM    842  CE2 PHE A 113       5.450  51.757  59.569  1.00 49.67           C  
ATOM    843  CZ  PHE A 113       6.600  52.450  59.927  1.00 49.57           C  
ATOM    844  N   ILE A 114       6.652  46.572  59.469  1.00 51.66           N  
ATOM    845  CA  ILE A 114       6.285  46.093  60.799  1.00 54.89           C  
ATOM    846  C   ILE A 114       7.421  45.228  61.350  1.00 56.63           C  
ATOM    847  O   ILE A 114       7.740  45.277  62.575  1.00 56.42           O  
ATOM    848  CB  ILE A 114       4.966  45.264  60.746  1.00 52.78           C  
ATOM    849  CG1 ILE A 114       3.778  46.209  60.577  1.00 50.65           C  
ATOM    850  CG2 ILE A 114       4.808  44.434  62.008  1.00 54.09           C  
ATOM    851  CD1 ILE A 114       3.588  47.123  61.753  1.00 51.79           C  
ATOM    852  N   GLY A 115       8.013  44.437  60.433  1.00 57.11           N  
ATOM    853  CA  GLY A 115       9.123  43.550  60.782  1.00 55.57           C  
ATOM    854  C   GLY A 115      10.309  44.358  61.295  1.00 54.12           C  
ATOM    855  O   GLY A 115      10.880  44.048  62.347  1.00 52.96           O  
ATOM    856  N   GLY A 116      10.640  45.424  60.561  1.00 52.65           N  
ATOM    857  CA  GLY A 116      11.759  46.266  60.911  1.00 51.07           C  
ATOM    858  C   GLY A 116      11.471  47.107  62.121  1.00 53.19           C  
ATOM    859  O   GLY A 116      12.320  47.230  63.007  1.00 56.24           O  
ATOM    860  N   ILE A 117      10.269  47.677  62.188  1.00 53.48           N  
ATOM    861  CA  ILE A 117       9.873  48.537  63.321  1.00 52.91           C  
ATOM    862  C   ILE A 117       9.932  47.816  64.698  1.00 52.59           C  
ATOM    863  O   ILE A 117      10.368  48.397  65.718  1.00 51.70           O  
ATOM    864  CB  ILE A 117       8.448  49.118  63.083  1.00 53.18           C  
ATOM    865  CG1 ILE A 117       8.177  50.270  64.048  1.00 54.73           C  
ATOM    866  CG2 ILE A 117       7.416  48.025  63.240  1.00 52.57           C  
ATOM    867  CD1 ILE A 117       6.926  51.058  63.700  1.00 58.62           C  
ATOM    868  N   PHE A 118       9.512  46.550  64.731  1.00 52.12           N  
ATOM    869  CA  PHE A 118       9.551  45.815  65.988  1.00 51.97           C  
ATOM    870  C   PHE A 118      10.853  45.061  66.263  1.00 50.98           C  
ATOM    871  O   PHE A 118      11.120  44.636  67.395  1.00 51.16           O  
ATOM    872  CB  PHE A 118       8.340  44.890  66.099  1.00 51.52           C  
ATOM    873  CG  PHE A 118       7.066  45.627  66.304  1.00 50.04           C  
ATOM    874  CD1 PHE A 118       6.162  45.759  65.256  1.00 50.05           C  
ATOM    875  CD2 PHE A 118       6.816  46.268  67.523  1.00 50.25           C  
ATOM    876  CE1 PHE A 118       5.029  46.517  65.405  1.00 52.33           C  
ATOM    877  CE2 PHE A 118       5.685  47.040  67.699  1.00 53.37           C  
ATOM    878  CZ  PHE A 118       4.781  47.169  66.631  1.00 55.04           C  
ATOM    879  N   GLY A 119      11.660  44.885  65.226  1.00 51.13           N  
ATOM    880  CA  GLY A 119      12.946  44.246  65.412  1.00 47.80           C  
ATOM    881  C   GLY A 119      13.816  45.319  66.046  1.00 46.81           C  
ATOM    882  O   GLY A 119      14.607  45.031  66.927  1.00 45.35           O  
ATOM    883  N   PHE A 120      13.651  46.568  65.605  1.00 46.19           N  
ATOM    884  CA  PHE A 120      14.429  47.685  66.135  1.00 46.39           C  
ATOM    885  C   PHE A 120      13.949  47.971  67.530  1.00 47.41           C  
ATOM    886  O   PHE A 120      14.723  48.428  68.380  1.00 46.01           O  
ATOM    887  CB  PHE A 120      14.224  48.955  65.295  1.00 45.66           C  
ATOM    888  CG  PHE A 120      14.897  48.928  63.950  1.00 43.07           C  
ATOM    889  CD1 PHE A 120      14.291  49.552  62.858  1.00 40.38           C  
ATOM    890  CD2 PHE A 120      16.136  48.303  63.783  1.00 43.07           C  
ATOM    891  CE1 PHE A 120      14.887  49.561  61.616  1.00 41.93           C  
ATOM    892  CE2 PHE A 120      16.744  48.304  62.556  1.00 45.62           C  
ATOM    893  CZ  PHE A 120      16.109  48.941  61.448  1.00 46.03           C  
ATOM    894  N   MET A 121      12.656  47.705  67.750  1.00 50.31           N  
ATOM    895  CA  MET A 121      12.017  47.970  69.039  1.00 52.63           C  
ATOM    896  C   MET A 121      12.381  46.990  70.149  1.00 53.09           C  
ATOM    897  O   MET A 121      12.485  47.371  71.336  1.00 53.11           O  
ATOM    898  CB  MET A 121      10.496  48.029  68.894  1.00 53.98           C  
ATOM    899  CG  MET A 121       9.841  48.634  70.142  1.00 58.86           C  
ATOM    900  SD  MET A 121       8.168  49.198  69.850  1.00 57.76           S  
ATOM    901  CE  MET A 121       7.267  47.916  70.677  1.00 58.76           C  
ATOM    902  N   SER A 122      12.579  45.728  69.780  1.00 51.69           N  
ATOM    903  CA  SER A 122      12.960  44.738  70.784  1.00 49.71           C  
ATOM    904  C   SER A 122      14.408  44.928  71.333  1.00 48.10           C  
ATOM    905  O   SER A 122      14.652  44.703  72.521  1.00 48.81           O  
ATOM    906  CB  SER A 122      12.736  43.331  70.227  1.00 51.72           C  
ATOM    907  OG  SER A 122      11.335  43.060  70.074  1.00 46.71           O  
ATOM    908  N   ILE A 123      15.363  45.343  70.502  1.00 44.95           N  
ATOM    909  CA  ILE A 123      16.696  45.576  71.028  1.00 43.23           C  
ATOM    910  C   ILE A 123      16.694  46.888  71.823  1.00 44.59           C  
ATOM    911  O   ILE A 123      17.193  46.941  72.947  1.00 42.12           O  
ATOM    912  CB  ILE A 123      17.764  45.681  69.931  1.00 39.96           C  
ATOM    913  CG1 ILE A 123      17.104  45.703  68.563  1.00 38.76           C  
ATOM    914  CG2 ILE A 123      18.753  44.549  70.087  1.00 39.70           C  
ATOM    915  CD1 ILE A 123      18.028  46.057  67.428  1.00 39.54           C  
ATOM    916  N   MET A 124      16.122  47.948  71.253  1.00 46.27           N  
ATOM    917  CA  MET A 124      16.120  49.223  71.953  1.00 48.77           C  
ATOM    918  C   MET A 124      15.424  49.117  73.311  1.00 51.99           C  
ATOM    919  O   MET A 124      15.835  49.775  74.284  1.00 53.39           O  
ATOM    920  CB  MET A 124      15.477  50.308  71.109  1.00 46.75           C  
ATOM    921  CG  MET A 124      15.766  51.688  71.649  1.00 49.42           C  
ATOM    922  SD  MET A 124      17.543  51.891  71.960  1.00 55.02           S  
ATOM    923  CE  MET A 124      18.141  52.437  70.362  1.00 52.36           C  
ATOM    924  N   THR A 125      14.381  48.289  73.384  1.00 53.74           N  
ATOM    925  CA  THR A 125      13.667  48.095  74.636  1.00 54.61           C  
ATOM    926  C   THR A 125      14.631  47.383  75.562  1.00 55.64           C  
ATOM    927  O   THR A 125      14.712  47.697  76.749  1.00 54.46           O  
ATOM    928  CB  THR A 125      12.439  47.231  74.446  1.00 55.04           C  
ATOM    929  OG1 THR A 125      11.546  47.906  73.554  1.00 52.65           O  
ATOM    930  CG2 THR A 125      11.756  46.964  75.804  1.00 54.67           C  
ATOM    931  N   MET A 126      15.366  46.420  75.012  1.00 57.22           N  
ATOM    932  CA  MET A 126      16.357  45.709  75.821  1.00 60.62           C  
ATOM    933  C   MET A 126      17.425  46.730  76.300  1.00 61.84           C  
ATOM    934  O   MET A 126      17.964  46.654  77.433  1.00 61.17           O  
ATOM    935  CB  MET A 126      16.996  44.587  75.007  1.00 60.83           C  
ATOM    936  CG  MET A 126      16.089  43.364  74.837  1.00 61.77           C  
ATOM    937  SD  MET A 126      16.864  42.036  73.870  1.00 64.75           S  
ATOM    938  CE  MET A 126      15.541  41.494  72.822  1.00 67.24           C  
ATOM    939  N   ALA A 127      17.707  47.708  75.440  1.00 61.76           N  
ATOM    940  CA  ALA A 127      18.657  48.745  75.817  1.00 60.41           C  
ATOM    941  C   ALA A 127      18.137  49.457  77.074  1.00 60.85           C  
ATOM    942  O   ALA A 127      18.876  49.627  78.047  1.00 59.97           O  
ATOM    943  CB  ALA A 127      18.829  49.742  74.676  1.00 58.93           C  
ATOM    944  N   MET A 128      16.867  49.868  77.059  1.00 60.31           N  
ATOM    945  CA  MET A 128      16.285  50.540  78.217  1.00 58.23           C  
ATOM    946  C   MET A 128      16.316  49.609  79.421  1.00 56.90           C  
ATOM    947  O   MET A 128      16.401  50.057  80.555  1.00 55.84           O  
ATOM    948  CB  MET A 128      14.844  50.928  77.935  1.00 58.63           C  
ATOM    949  CG  MET A 128      14.673  51.827  76.765  1.00 58.13           C  
ATOM    950  SD  MET A 128      15.759  53.229  76.922  1.00 57.64           S  
ATOM    951  CE  MET A 128      16.208  53.382  75.205  1.00 59.02           C  
ATOM    952  N   ILE A 129      16.219  48.312  79.176  1.00 56.50           N  
ATOM    953  CA  ILE A 129      16.254  47.366  80.278  1.00 59.85           C  
ATOM    954  C   ILE A 129      17.681  47.261  80.823  1.00 61.77           C  
ATOM    955  O   ILE A 129      17.902  47.082  82.042  1.00 60.52           O  
ATOM    956  CB  ILE A 129      15.813  45.977  79.835  1.00 59.83           C  
ATOM    957  CG1 ILE A 129      14.366  46.037  79.367  1.00 61.66           C  
ATOM    958  CG2 ILE A 129      15.977  44.985  80.980  1.00 58.57           C  
ATOM    959  CD1 ILE A 129      13.868  44.723  78.796  1.00 64.16           C  
ATOM    960  N   SER A 130      18.652  47.376  79.915  1.00 62.38           N  
ATOM    961  CA  SER A 130      20.054  47.295  80.303  1.00 61.16           C  
ATOM    962  C   SER A 130      20.435  48.528  81.114  1.00 59.74           C  
ATOM    963  O   SER A 130      21.356  48.485  81.934  1.00 57.44           O  
ATOM    964  CB  SER A 130      20.948  47.205  79.065  1.00 61.19           C  
ATOM    965  OG  SER A 130      20.953  48.432  78.359  1.00 61.84           O  
ATOM    966  N   ILE A 131      19.720  49.633  80.867  1.00 56.69           N  
ATOM    967  CA  ILE A 131      19.949  50.889  81.580  1.00 53.33           C  
ATOM    968  C   ILE A 131      19.446  50.792  83.022  1.00 54.13           C  
ATOM    969  O   ILE A 131      20.134  51.201  83.978  1.00 54.06           O  
ATOM    970  CB  ILE A 131      19.265  52.045  80.847  1.00 49.44           C  
ATOM    971  CG1 ILE A 131      19.953  52.235  79.484  1.00 47.96           C  
ATOM    972  CG2 ILE A 131      19.309  53.289  81.678  1.00 42.85           C  
ATOM    973  CD1 ILE A 131      19.373  53.322  78.664  1.00 47.39           C  
ATOM    974  N   ASP A 132      18.251  50.220  83.169  1.00 55.01           N  
ATOM    975  CA  ASP A 132      17.643  50.022  84.485  1.00 55.26           C  
ATOM    976  C   ASP A 132      18.576  49.124  85.291  1.00 56.93           C  
ATOM    977  O   ASP A 132      18.846  49.370  86.478  1.00 55.84           O  
ATOM    978  CB  ASP A 132      16.273  49.341  84.350  1.00 53.54           C  
ATOM    979  CG  ASP A 132      15.749  48.827  85.686  1.00 52.90           C  
ATOM    980  OD1 ASP A 132      15.716  47.584  85.926  1.00 46.01           O  
ATOM    981  OD2 ASP A 132      15.384  49.690  86.518  1.00 55.90           O  
ATOM    982  N   ARG A 133      19.063  48.071  84.631  1.00 60.65           N  
ATOM    983  CA  ARG A 133      19.977  47.130  85.274  1.00 64.73           C  
ATOM    984  C   ARG A 133      21.206  47.880  85.805  1.00 67.67           C  
ATOM    985  O   ARG A 133      21.653  47.636  86.947  1.00 69.06           O  
ATOM    986  CB  ARG A 133      20.410  46.034  84.283  1.00 63.80           C  
ATOM    987  CG  ARG A 133      19.324  44.993  83.967  1.00 61.73           C  
ATOM    988  CD  ARG A 133      18.742  44.353  85.243  1.00 59.85           C  
ATOM    989  NE  ARG A 133      17.865  45.296  85.951  1.00 59.71           N  
ATOM    990  CZ  ARG A 133      17.326  45.076  87.143  1.00 59.49           C  
ATOM    991  NH1 ARG A 133      17.570  43.924  87.789  1.00 61.30           N  
ATOM    992  NH2 ARG A 133      16.547  46.008  87.688  1.00 57.16           N  
ATOM    993  N   TYR A 134      21.741  48.790  84.977  1.00 69.00           N  
ATOM    994  CA  TYR A 134      22.900  49.594  85.363  1.00 69.80           C  
ATOM    995  C   TYR A 134      22.608  50.509  86.574  1.00 69.99           C  
ATOM    996  O   TYR A 134      23.478  50.724  87.424  1.00 70.38           O  
ATOM    997  CB  TYR A 134      23.371  50.437  84.180  1.00 69.43           C  
ATOM    998  CG  TYR A 134      24.313  51.543  84.595  1.00 70.99           C  
ATOM    999  CD1 TYR A 134      23.906  52.887  84.538  1.00 70.83           C  
ATOM   1000  CD2 TYR A 134      25.606  51.245  85.072  1.00 71.80           C  
ATOM   1001  CE1 TYR A 134      24.756  53.925  84.941  1.00 73.42           C  
ATOM   1002  CE2 TYR A 134      26.474  52.266  85.482  1.00 74.97           C  
ATOM   1003  CZ  TYR A 134      26.041  53.613  85.415  1.00 75.53           C  
ATOM   1004  OH  TYR A 134      26.882  54.628  85.846  1.00 75.95           O  
ATOM   1005  N   ASN A 135      21.392  51.045  86.655  1.00 68.89           N  
ATOM   1006  CA  ASN A 135      21.041  51.904  87.783  1.00 68.10           C  
ATOM   1007  C   ASN A 135      20.826  51.155  89.098  1.00 68.09           C  
ATOM   1008  O   ASN A 135      21.067  51.706  90.177  1.00 68.54           O  
ATOM   1009  CB  ASN A 135      19.791  52.718  87.471  1.00 67.56           C  
ATOM   1010  CG  ASN A 135      20.095  53.899  86.598  1.00 67.73           C  
ATOM   1011  OD1 ASN A 135      20.987  54.693  86.910  1.00 68.41           O  
ATOM   1012  ND2 ASN A 135      19.363  54.037  85.500  1.00 67.10           N  
ATOM   1013  N   VAL A 136      20.368  49.908  89.018  1.00 66.64           N  
ATOM   1014  CA  VAL A 136      20.127  49.143  90.228  1.00 66.50           C  
ATOM   1015  C   VAL A 136      21.329  48.257  90.613  1.00 67.22           C  
ATOM   1016  O   VAL A 136      21.589  48.046  91.808  1.00 66.87           O  
ATOM   1017  CB  VAL A 136      18.851  48.275  90.075  1.00 66.85           C  
ATOM   1018  CG1 VAL A 136      18.987  47.401  88.838  1.00 69.13           C  
ATOM   1019  CG2 VAL A 136      18.612  47.410  91.338  1.00 64.77           C  
ATOM   1020  N   ILE A 137      22.065  47.761  89.612  1.00 66.40           N  
ATOM   1021  CA  ILE A 137      23.220  46.885  89.845  1.00 65.22           C  
ATOM   1022  C   ILE A 137      24.564  47.509  89.436  1.00 66.31           C  
ATOM   1023  O   ILE A 137      25.579  47.306  90.109  1.00 64.82           O  
ATOM   1024  CB  ILE A 137      23.032  45.529  89.102  1.00 64.60           C  
ATOM   1025  CG1 ILE A 137      21.854  44.784  89.699  1.00 63.87           C  
ATOM   1026  CG2 ILE A 137      24.251  44.649  89.262  1.00 66.28           C  
ATOM   1027  CD1 ILE A 137      22.065  44.449  91.148  1.00 67.10           C  
ATOM   1028  N   GLY A 138      24.571  48.273  88.339  1.00 67.82           N  
ATOM   1029  CA  GLY A 138      25.804  48.918  87.868  1.00 68.75           C  
ATOM   1030  C   GLY A 138      26.392  50.096  88.674  1.00 67.72           C  
ATOM   1031  O   GLY A 138      27.556  50.464  88.523  1.00 65.18           O  
ATOM   1032  N   ARG A 139      25.580  50.707  89.520  1.00 68.91           N  
ATOM   1033  CA  ARG A 139      26.037  51.817  90.329  1.00 70.42           C  
ATOM   1034  C   ARG A 139      26.254  51.267  91.725  1.00 71.84           C  
ATOM   1035  O   ARG A 139      25.804  50.166  92.026  1.00 73.13           O  
ATOM   1036  CB  ARG A 139      24.984  52.914  90.305  1.00 69.97           C  
ATOM   1037  CG  ARG A 139      24.589  53.230  88.873  1.00 71.41           C  
ATOM   1038  CD  ARG A 139      23.510  54.272  88.777  1.00 71.77           C  
ATOM   1039  NE  ARG A 139      23.980  55.541  89.295  1.00 71.31           N  
ATOM   1040  CZ  ARG A 139      23.559  56.714  88.852  1.00 72.16           C  
ATOM   1041  NH1 ARG A 139      22.656  56.779  87.874  1.00 70.59           N  
ATOM   1042  NH2 ARG A 139      24.052  57.820  89.385  1.00 73.34           N  
ATOM   1043  N   PRO A 140      26.975  52.004  92.587  1.00 72.61           N  
ATOM   1044  CA  PRO A 140      27.245  51.559  93.954  1.00 74.15           C  
ATOM   1045  C   PRO A 140      25.961  51.623  94.793  1.00 77.19           C  
ATOM   1046  O   PRO A 140      25.217  52.623  94.740  1.00 77.61           O  
ATOM   1047  CB  PRO A 140      28.282  52.554  94.421  1.00 72.27           C  
ATOM   1048  CG  PRO A 140      27.756  53.813  93.820  1.00 71.97           C  
ATOM   1049  CD  PRO A 140      27.460  53.380  92.397  1.00 72.06           C  
ATOM   1050  N   MET A 141      25.725  50.549  95.559  1.00 78.39           N  
ATOM   1051  CA  MET A 141      24.551  50.389  96.425  1.00 78.54           C  
ATOM   1052  C   MET A 141      24.062  51.690  97.038  1.00 77.83           C  
ATOM   1053  O   MET A 141      22.849  51.898  97.193  1.00 76.84           O  
ATOM   1054  CB  MET A 141      24.865  49.403  97.557  1.00 81.18           C  
ATOM   1055  CG  MET A 141      25.410  48.045  97.105  1.00 84.30           C  
ATOM   1056  SD  MET A 141      25.643  46.892  98.521  1.00 85.87           S  
ATOM   1057  CE  MET A 141      24.033  45.996  98.550  1.00 83.96           C  
ATOM   1058  N   ALA A 142      25.014  52.556  97.389  1.00 77.26           N  
ATOM   1059  CA  ALA A 142      24.692  53.844  98.003  1.00 76.30           C  
ATOM   1060  C   ALA A 142      23.950  54.758  97.025  1.00 74.75           C  
ATOM   1061  O   ALA A 142      23.113  55.558  97.442  1.00 72.79           O  
ATOM   1062  CB  ALA A 142      25.986  54.539  98.518  1.00 77.00           C  
ATOM   1063  N   ALA A 143      24.262  54.619  95.732  1.00 74.04           N  
ATOM   1064  CA  ALA A 143      23.651  55.428  94.683  1.00 74.12           C  
ATOM   1065  C   ALA A 143      22.616  54.671  93.838  1.00 73.74           C  
ATOM   1066  O   ALA A 143      22.038  55.220  92.883  1.00 71.84           O  
ATOM   1067  CB  ALA A 143      24.735  56.000  93.783  1.00 74.75           C  
ATOM   1068  N   SER A 144      22.383  53.413  94.200  1.00 74.17           N  
ATOM   1069  CA  SER A 144      21.424  52.563  93.503  1.00 74.36           C  
ATOM   1070  C   SER A 144      20.132  53.320  93.239  1.00 75.74           C  
ATOM   1071  O   SER A 144      19.579  53.944  94.137  1.00 75.28           O  
ATOM   1072  CB  SER A 144      21.121  51.323  94.338  1.00 73.40           C  
ATOM   1073  OG  SER A 144      20.084  50.570  93.746  1.00 70.86           O  
ATOM   1074  N   LYS A 145      19.650  53.253  92.002  1.00 78.76           N  
ATOM   1075  CA  LYS A 145      18.425  53.950  91.607  1.00 79.20           C  
ATOM   1076  C   LYS A 145      17.435  53.010  90.921  1.00 79.91           C  
ATOM   1077  O   LYS A 145      17.784  52.355  89.927  1.00 79.56           O  
ATOM   1078  CB  LYS A 145      18.771  55.101  90.652  1.00 77.38           C  
ATOM   1079  CG  LYS A 145      18.033  56.414  90.921  1.00 78.09           C  
ATOM   1080  CD  LYS A 145      16.528  56.309  90.707  1.00 80.18           C  
ATOM   1081  CE  LYS A 145      15.848  57.688  90.715  1.00 79.81           C  
ATOM   1082  NZ  LYS A 145      16.012  58.432  91.994  1.00 78.00           N  
ATOM   1083  N   LYS A 146      16.209  52.950  91.463  1.00 81.01           N  
ATOM   1084  CA  LYS A 146      15.120  52.130  90.907  1.00 80.91           C  
ATOM   1085  C   LYS A 146      14.348  52.893  89.806  1.00 80.60           C  
ATOM   1086  O   LYS A 146      14.284  54.135  89.811  1.00 81.74           O  
ATOM   1087  CB  LYS A 146      14.150  51.713  92.003  1.00 79.15           C  
ATOM   1088  CG  LYS A 146      14.056  50.234  92.134  1.00 81.43           C  
ATOM   1089  CD  LYS A 146      15.374  49.661  92.580  1.00 83.43           C  
ATOM   1090  CE  LYS A 146      15.253  48.159  92.776  1.00 87.42           C  
ATOM   1091  NZ  LYS A 146      16.451  47.614  93.502  1.00 88.94           N  
ATOM   1092  N   MET A 147      13.772  52.152  88.861  1.00 79.13           N  
ATOM   1093  CA  MET A 147      13.027  52.754  87.755  1.00 77.28           C  
ATOM   1094  C   MET A 147      11.699  53.383  88.200  1.00 78.56           C  
ATOM   1095  O   MET A 147      10.949  52.821  89.009  1.00 78.84           O  
ATOM   1096  CB  MET A 147      12.782  51.696  86.680  1.00 73.86           C  
ATOM   1097  CG  MET A 147      12.135  52.209  85.429  1.00 71.25           C  
ATOM   1098  SD  MET A 147      13.029  53.511  84.577  1.00 72.57           S  
ATOM   1099  CE  MET A 147      14.373  52.588  83.830  1.00 69.99           C  
ATOM   1100  N   SER A 148      11.410  54.560  87.670  1.00 80.14           N  
ATOM   1101  CA  SER A 148      10.179  55.251  88.020  1.00 82.31           C  
ATOM   1102  C   SER A 148       9.234  55.277  86.825  1.00 83.16           C  
ATOM   1103  O   SER A 148       9.677  55.349  85.674  1.00 81.70           O  
ATOM   1104  CB  SER A 148      10.492  56.687  88.435  1.00 84.64           C  
ATOM   1105  OG  SER A 148      10.953  57.451  87.321  1.00 84.52           O  
ATOM   1106  N   HIS A 149       7.935  55.232  87.102  1.00 84.57           N  
ATOM   1107  CA  HIS A 149       6.947  55.263  86.038  1.00 86.05           C  
ATOM   1108  C   HIS A 149       7.249  56.421  85.103  1.00 85.04           C  
ATOM   1109  O   HIS A 149       7.209  56.249  83.888  1.00 86.56           O  
ATOM   1110  CB  HIS A 149       5.538  55.417  86.617  1.00 89.88           C  
ATOM   1111  CG  HIS A 149       5.042  54.198  87.330  1.00 92.99           C  
ATOM   1112  ND1 HIS A 149       4.718  53.030  86.666  1.00 94.41           N  
ATOM   1113  CD2 HIS A 149       4.844  53.955  88.651  1.00 92.58           C  
ATOM   1114  CE1 HIS A 149       4.345  52.118  87.550  1.00 95.77           C  
ATOM   1115  NE2 HIS A 149       4.415  52.653  88.761  1.00 94.89           N  
ATOM   1116  N   ARG A 150       7.556  57.593  85.662  1.00 82.85           N  
ATOM   1117  CA  ARG A 150       7.867  58.756  84.836  1.00 80.53           C  
ATOM   1118  C   ARG A 150       8.954  58.399  83.851  1.00 77.48           C  
ATOM   1119  O   ARG A 150       8.720  58.410  82.647  1.00 77.38           O  
ATOM   1120  CB  ARG A 150       8.321  59.936  85.693  1.00 83.07           C  
ATOM   1121  CG  ARG A 150       7.181  60.814  86.200  1.00 88.26           C  
ATOM   1122  CD  ARG A 150       6.132  59.989  86.966  1.00 92.05           C  
ATOM   1123  NE  ARG A 150       6.732  59.241  88.071  1.00 93.34           N  
ATOM   1124  CZ  ARG A 150       6.076  58.359  88.814  1.00 93.07           C  
ATOM   1125  NH1 ARG A 150       6.701  57.719  89.804  1.00 93.20           N  
ATOM   1126  NH2 ARG A 150       4.797  58.117  88.556  1.00 91.45           N  
ATOM   1127  N   ARG A 151      10.141  58.071  84.360  1.00 75.44           N  
ATOM   1128  CA  ARG A 151      11.279  57.700  83.502  1.00 74.09           C  
ATOM   1129  C   ARG A 151      10.900  56.622  82.463  1.00 72.66           C  
ATOM   1130  O   ARG A 151      10.964  56.840  81.236  1.00 70.15           O  
ATOM   1131  CB  ARG A 151      12.442  57.208  84.371  1.00 74.14           C  
ATOM   1132  CG  ARG A 151      13.538  58.249  84.548  1.00 76.96           C  
ATOM   1133  CD  ARG A 151      13.018  59.525  85.240  1.00 80.76           C  
ATOM   1134  NE  ARG A 151      12.990  59.403  86.712  1.00 81.70           N  
ATOM   1135  CZ  ARG A 151      12.544  60.342  87.554  1.00 78.33           C  
ATOM   1136  NH1 ARG A 151      12.064  61.496  87.090  1.00 74.80           N  
ATOM   1137  NH2 ARG A 151      12.612  60.131  88.863  1.00 75.52           N  
ATOM   1138  N   ALA A 152      10.503  55.459  82.983  1.00 70.09           N  
ATOM   1139  CA  ALA A 152      10.082  54.336  82.168  1.00 66.12           C  
ATOM   1140  C   ALA A 152       9.218  54.819  81.005  1.00 65.99           C  
ATOM   1141  O   ALA A 152       9.569  54.636  79.849  1.00 65.95           O  
ATOM   1142  CB  ALA A 152       9.293  53.333  83.025  1.00 62.19           C  
ATOM   1143  N   PHE A 153       8.085  55.433  81.315  1.00 67.48           N  
ATOM   1144  CA  PHE A 153       7.172  55.916  80.288  1.00 68.41           C  
ATOM   1145  C   PHE A 153       7.877  56.766  79.210  1.00 66.28           C  
ATOM   1146  O   PHE A 153       7.623  56.591  78.008  1.00 65.13           O  
ATOM   1147  CB  PHE A 153       6.010  56.701  80.948  1.00 74.09           C  
ATOM   1148  CG  PHE A 153       5.015  57.289  79.954  1.00 80.53           C  
ATOM   1149  CD1 PHE A 153       4.334  56.457  79.049  1.00 82.83           C  
ATOM   1150  CD2 PHE A 153       4.798  58.684  79.886  1.00 80.76           C  
ATOM   1151  CE1 PHE A 153       3.461  57.006  78.089  1.00 81.91           C  
ATOM   1152  CE2 PHE A 153       3.927  59.232  78.933  1.00 79.45           C  
ATOM   1153  CZ  PHE A 153       3.259  58.392  78.033  1.00 80.39           C  
ATOM   1154  N   ILE A 154       8.756  57.673  79.624  1.00 63.83           N  
ATOM   1155  CA  ILE A 154       9.461  58.519  78.662  1.00 63.22           C  
ATOM   1156  C   ILE A 154      10.393  57.645  77.839  1.00 63.23           C  
ATOM   1157  O   ILE A 154      10.500  57.785  76.615  1.00 62.35           O  
ATOM   1158  CB  ILE A 154      10.303  59.594  79.359  1.00 62.89           C  
ATOM   1159  CG1 ILE A 154       9.406  60.436  80.263  1.00 64.75           C  
ATOM   1160  CG2 ILE A 154      10.923  60.517  78.337  1.00 60.60           C  
ATOM   1161  CD1 ILE A 154      10.163  61.296  81.279  1.00 65.38           C  
ATOM   1162  N   MET A 155      11.073  56.730  78.517  1.00 63.14           N  
ATOM   1163  CA  MET A 155      11.977  55.828  77.820  1.00 60.67           C  
ATOM   1164  C   MET A 155      11.260  55.041  76.705  1.00 62.02           C  
ATOM   1165  O   MET A 155      11.743  55.063  75.571  1.00 63.21           O  
ATOM   1166  CB  MET A 155      12.688  54.915  78.841  1.00 57.52           C  
ATOM   1167  CG  MET A 155      13.853  55.645  79.573  1.00 49.90           C  
ATOM   1168  SD  MET A 155      14.387  55.050  81.194  1.00 46.39           S  
ATOM   1169  CE  MET A 155      15.600  53.857  80.760  1.00 45.91           C  
ATOM   1170  N   ILE A 156      10.117  54.385  76.978  1.00 62.38           N  
ATOM   1171  CA  ILE A 156       9.429  53.655  75.904  1.00 61.70           C  
ATOM   1172  C   ILE A 156       8.980  54.628  74.791  1.00 62.00           C  
ATOM   1173  O   ILE A 156       8.980  54.274  73.595  1.00 64.33           O  
ATOM   1174  CB  ILE A 156       8.213  52.838  76.392  1.00 60.88           C  
ATOM   1175  CG1 ILE A 156       7.031  53.758  76.615  1.00 65.36           C  
ATOM   1176  CG2 ILE A 156       8.550  52.112  77.672  1.00 58.73           C  
ATOM   1177  CD1 ILE A 156       5.762  53.017  77.035  1.00 71.59           C  
ATOM   1178  N   ILE A 157       8.619  55.860  75.149  1.00 59.47           N  
ATOM   1179  CA  ILE A 157       8.226  56.817  74.105  1.00 57.99           C  
ATOM   1180  C   ILE A 157       9.390  56.999  73.159  1.00 56.70           C  
ATOM   1181  O   ILE A 157       9.192  57.102  71.943  1.00 56.49           O  
ATOM   1182  CB  ILE A 157       7.835  58.195  74.671  1.00 57.47           C  
ATOM   1183  CG1 ILE A 157       6.510  58.064  75.422  1.00 59.46           C  
ATOM   1184  CG2 ILE A 157       7.715  59.213  73.551  1.00 51.84           C  
ATOM   1185  CD1 ILE A 157       5.975  59.365  75.914  1.00 62.61           C  
ATOM   1186  N   PHE A 158      10.602  57.035  73.727  1.00 54.56           N  
ATOM   1187  CA  PHE A 158      11.816  57.183  72.922  1.00 52.28           C  
ATOM   1188  C   PHE A 158      11.924  55.932  72.060  1.00 50.18           C  
ATOM   1189  O   PHE A 158      12.163  56.003  70.847  1.00 49.27           O  
ATOM   1190  CB  PHE A 158      13.069  57.315  73.807  1.00 51.73           C  
ATOM   1191  CG  PHE A 158      14.363  57.035  73.075  1.00 52.54           C  
ATOM   1192  CD1 PHE A 158      14.797  57.869  72.054  1.00 52.19           C  
ATOM   1193  CD2 PHE A 158      15.113  55.883  73.360  1.00 54.12           C  
ATOM   1194  CE1 PHE A 158      15.960  57.557  71.314  1.00 52.89           C  
ATOM   1195  CE2 PHE A 158      16.280  55.564  72.624  1.00 53.61           C  
ATOM   1196  CZ  PHE A 158      16.698  56.399  71.603  1.00 51.83           C  
ATOM   1197  N   VAL A 159      11.723  54.791  72.699  1.00 47.31           N  
ATOM   1198  CA  VAL A 159      11.802  53.534  72.008  1.00 48.31           C  
ATOM   1199  C   VAL A 159      10.891  53.525  70.797  1.00 49.40           C  
ATOM   1200  O   VAL A 159      11.317  53.168  69.697  1.00 51.36           O  
ATOM   1201  CB  VAL A 159      11.409  52.378  72.920  1.00 47.18           C  
ATOM   1202  CG1 VAL A 159      11.404  51.058  72.137  1.00 48.65           C  
ATOM   1203  CG2 VAL A 159      12.363  52.321  74.088  1.00 45.24           C  
ATOM   1204  N   TRP A 160       9.641  53.916  70.984  1.00 48.51           N  
ATOM   1205  CA  TRP A 160       8.724  53.910  69.865  1.00 49.60           C  
ATOM   1206  C   TRP A 160       9.132  54.899  68.753  1.00 50.68           C  
ATOM   1207  O   TRP A 160       9.187  54.538  67.574  1.00 51.49           O  
ATOM   1208  CB  TRP A 160       7.303  54.180  70.353  1.00 49.55           C  
ATOM   1209  CG  TRP A 160       6.602  52.956  70.881  1.00 46.52           C  
ATOM   1210  CD1 TRP A 160       6.708  52.416  72.136  1.00 46.67           C  
ATOM   1211  CD2 TRP A 160       5.681  52.130  70.165  1.00 45.87           C  
ATOM   1212  NE1 TRP A 160       5.910  51.309  72.247  1.00 42.95           N  
ATOM   1213  CE2 TRP A 160       5.267  51.104  71.051  1.00 45.19           C  
ATOM   1214  CE3 TRP A 160       5.161  52.151  68.854  1.00 45.26           C  
ATOM   1215  CZ2 TRP A 160       4.354  50.095  70.665  1.00 46.26           C  
ATOM   1216  CZ3 TRP A 160       4.255  51.148  68.468  1.00 45.82           C  
ATOM   1217  CH2 TRP A 160       3.864  50.130  69.378  1.00 46.17           C  
ATOM   1218  N   LEU A 161       9.428  56.142  69.118  1.00 52.57           N  
ATOM   1219  CA  LEU A 161       9.852  57.131  68.132  1.00 52.01           C  
ATOM   1220  C   LEU A 161      11.056  56.592  67.381  1.00 53.38           C  
ATOM   1221  O   LEU A 161      11.068  56.535  66.142  1.00 51.82           O  
ATOM   1222  CB  LEU A 161      10.218  58.435  68.831  1.00 52.69           C  
ATOM   1223  CG  LEU A 161       9.028  59.384  68.882  1.00 57.06           C  
ATOM   1224  CD1 LEU A 161       8.458  59.467  67.452  1.00 61.43           C  
ATOM   1225  CD2 LEU A 161       7.948  58.894  69.830  1.00 58.36           C  
ATOM   1226  N   TRP A 162      12.072  56.187  68.143  1.00 54.08           N  
ATOM   1227  CA  TRP A 162      13.279  55.633  67.552  1.00 55.56           C  
ATOM   1228  C   TRP A 162      12.909  54.542  66.526  1.00 56.68           C  
ATOM   1229  O   TRP A 162      13.116  54.712  65.310  1.00 57.75           O  
ATOM   1230  CB  TRP A 162      14.176  55.065  68.647  1.00 56.34           C  
ATOM   1231  CG  TRP A 162      15.514  54.595  68.164  1.00 59.49           C  
ATOM   1232  CD1 TRP A 162      15.873  53.316  67.858  1.00 58.07           C  
ATOM   1233  CD2 TRP A 162      16.696  55.395  68.003  1.00 61.87           C  
ATOM   1234  NE1 TRP A 162      17.203  53.263  67.530  1.00 59.58           N  
ATOM   1235  CE2 TRP A 162      17.734  54.527  67.608  1.00 61.70           C  
ATOM   1236  CE3 TRP A 162      16.977  56.764  68.157  1.00 61.54           C  
ATOM   1237  CZ2 TRP A 162      19.038  54.982  67.368  1.00 61.16           C  
ATOM   1238  CZ3 TRP A 162      18.272  57.211  67.915  1.00 60.40           C  
ATOM   1239  CH2 TRP A 162      19.282  56.322  67.526  1.00 59.81           C  
ATOM   1240  N   SER A 163      12.318  53.451  67.011  1.00 55.23           N  
ATOM   1241  CA  SER A 163      11.937  52.326  66.162  1.00 54.06           C  
ATOM   1242  C   SER A 163      11.224  52.692  64.885  1.00 54.50           C  
ATOM   1243  O   SER A 163      11.545  52.159  63.822  1.00 54.21           O  
ATOM   1244  CB  SER A 163      11.055  51.367  66.934  1.00 53.78           C  
ATOM   1245  OG  SER A 163      11.687  50.967  68.136  1.00 57.24           O  
ATOM   1246  N   VAL A 164      10.239  53.577  64.978  1.00 55.51           N  
ATOM   1247  CA  VAL A 164       9.509  53.963  63.775  1.00 57.33           C  
ATOM   1248  C   VAL A 164      10.424  54.776  62.853  1.00 59.44           C  
ATOM   1249  O   VAL A 164      10.423  54.599  61.606  1.00 62.26           O  
ATOM   1250  CB  VAL A 164       8.282  54.817  64.088  1.00 56.14           C  
ATOM   1251  CG1 VAL A 164       7.508  55.090  62.811  1.00 55.18           C  
ATOM   1252  CG2 VAL A 164       7.425  54.111  65.083  1.00 56.45           C  
ATOM   1253  N   LEU A 165      11.220  55.655  63.460  1.00 57.72           N  
ATOM   1254  CA  LEU A 165      12.127  56.503  62.685  1.00 57.23           C  
ATOM   1255  C   LEU A 165      13.061  55.764  61.706  1.00 58.18           C  
ATOM   1256  O   LEU A 165      13.153  56.122  60.508  1.00 57.52           O  
ATOM   1257  CB  LEU A 165      12.989  57.360  63.628  1.00 56.10           C  
ATOM   1258  CG  LEU A 165      14.152  58.116  62.939  1.00 53.53           C  
ATOM   1259  CD1 LEU A 165      13.616  59.013  61.835  1.00 52.47           C  
ATOM   1260  CD2 LEU A 165      14.911  58.912  63.966  1.00 51.56           C  
ATOM   1261  N   TRP A 166      13.763  54.747  62.229  1.00 57.52           N  
ATOM   1262  CA  TRP A 166      14.719  53.995  61.430  1.00 54.34           C  
ATOM   1263  C   TRP A 166      14.089  52.904  60.624  1.00 52.98           C  
ATOM   1264  O   TRP A 166      14.787  52.191  59.919  1.00 56.08           O  
ATOM   1265  CB  TRP A 166      15.823  53.424  62.314  1.00 51.95           C  
ATOM   1266  CG  TRP A 166      16.510  54.492  63.039  1.00 54.27           C  
ATOM   1267  CD1 TRP A 166      16.670  54.601  64.396  1.00 55.76           C  
ATOM   1268  CD2 TRP A 166      17.054  55.677  62.470  1.00 57.35           C  
ATOM   1269  NE1 TRP A 166      17.280  55.789  64.708  1.00 58.28           N  
ATOM   1270  CE2 TRP A 166      17.525  56.472  63.541  1.00 59.73           C  
ATOM   1271  CE3 TRP A 166      17.187  56.156  61.156  1.00 59.00           C  
ATOM   1272  CZ2 TRP A 166      18.118  57.726  63.333  1.00 60.72           C  
ATOM   1273  CZ3 TRP A 166      17.773  57.396  60.949  1.00 58.46           C  
ATOM   1274  CH2 TRP A 166      18.232  58.168  62.034  1.00 60.00           C  
ATOM   1275  N   ALA A 167      12.774  52.768  60.692  1.00 50.07           N  
ATOM   1276  CA  ALA A 167      12.143  51.714  59.920  1.00 48.39           C  
ATOM   1277  C   ALA A 167      11.228  52.303  58.868  1.00 47.29           C  
ATOM   1278  O   ALA A 167      10.877  51.643  57.889  1.00 46.40           O  
ATOM   1279  CB  ALA A 167      11.367  50.790  60.848  1.00 44.35           C  
ATOM   1280  N   ILE A 168      10.876  53.568  59.050  1.00 45.89           N  
ATOM   1281  CA  ILE A 168       9.944  54.173  58.134  1.00 47.26           C  
ATOM   1282  C   ILE A 168      10.542  54.699  56.826  1.00 48.50           C  
ATOM   1283  O   ILE A 168       9.820  55.021  55.873  1.00 50.28           O  
ATOM   1284  CB  ILE A 168       9.162  55.260  58.857  1.00 44.57           C  
ATOM   1285  CG1 ILE A 168       7.836  55.487  58.142  1.00 45.36           C  
ATOM   1286  CG2 ILE A 168       9.995  56.519  58.913  1.00 46.29           C  
ATOM   1287  CD1 ILE A 168       6.859  56.243  58.944  1.00 47.03           C  
ATOM   1288  N   GLY A 169      11.862  54.760  56.761  1.00 48.97           N  
ATOM   1289  CA  GLY A 169      12.501  55.262  55.554  1.00 49.30           C  
ATOM   1290  C   GLY A 169      11.959  54.722  54.232  1.00 47.89           C  
ATOM   1291  O   GLY A 169      11.494  55.481  53.370  1.00 48.20           O  
ATOM   1292  N   PRO A 170      12.032  53.403  54.039  1.00 46.63           N  
ATOM   1293  CA  PRO A 170      11.545  52.779  52.813  1.00 49.46           C  
ATOM   1294  C   PRO A 170      10.081  53.106  52.511  1.00 50.93           C  
ATOM   1295  O   PRO A 170       9.599  52.911  51.375  1.00 47.54           O  
ATOM   1296  CB  PRO A 170      11.764  51.293  53.086  1.00 48.86           C  
ATOM   1297  CG  PRO A 170      13.007  51.332  53.908  1.00 47.17           C  
ATOM   1298  CD  PRO A 170      12.700  52.410  54.891  1.00 45.58           C  
ATOM   1299  N   ILE A 171       9.369  53.580  53.539  1.00 53.60           N  
ATOM   1300  CA  ILE A 171       7.961  53.956  53.368  1.00 55.85           C  
ATOM   1301  C   ILE A 171       7.843  55.247  52.582  1.00 56.27           C  
ATOM   1302  O   ILE A 171       6.824  55.499  51.938  1.00 54.03           O  
ATOM   1303  CB  ILE A 171       7.262  54.153  54.694  1.00 54.49           C  
ATOM   1304  CG1 ILE A 171       7.141  52.788  55.392  1.00 56.90           C  
ATOM   1305  CG2 ILE A 171       5.916  54.793  54.468  1.00 52.50           C  
ATOM   1306  CD1 ILE A 171       6.420  51.705  54.566  1.00 53.69           C  
ATOM   1307  N   PHE A 172       8.909  56.039  52.629  1.00 57.86           N  
ATOM   1308  CA  PHE A 172       8.952  57.297  51.920  1.00 59.01           C  
ATOM   1309  C   PHE A 172       9.934  57.400  50.747  1.00 57.70           C  
ATOM   1310  O   PHE A 172      10.164  58.475  50.202  1.00 56.02           O  
ATOM   1311  CB  PHE A 172       9.191  58.395  52.931  1.00 61.34           C  
ATOM   1312  CG  PHE A 172       8.000  58.657  53.805  1.00 64.68           C  
ATOM   1313  CD1 PHE A 172       6.746  58.923  53.241  1.00 66.29           C  
ATOM   1314  CD2 PHE A 172       8.120  58.655  55.189  1.00 66.99           C  
ATOM   1315  CE1 PHE A 172       5.624  59.187  54.054  1.00 66.95           C  
ATOM   1316  CE2 PHE A 172       7.003  58.917  56.020  1.00 67.97           C  
ATOM   1317  CZ  PHE A 172       5.758  59.183  55.448  1.00 67.05           C  
ATOM   1318  N   GLY A 173      10.496  56.271  50.351  1.00 58.94           N  
ATOM   1319  CA  GLY A 173      11.423  56.265  49.239  1.00 58.26           C  
ATOM   1320  C   GLY A 173      12.870  56.108  49.663  1.00 57.28           C  
ATOM   1321  O   GLY A 173      13.714  55.717  48.848  1.00 57.95           O  
ATOM   1322  N   TRP A 174      13.174  56.404  50.927  1.00 56.14           N  
ATOM   1323  CA  TRP A 174      14.558  56.303  51.392  1.00 55.19           C  
ATOM   1324  C   TRP A 174      14.846  54.847  51.757  1.00 55.26           C  
ATOM   1325  O   TRP A 174      15.135  54.508  52.907  1.00 56.53           O  
ATOM   1326  CB  TRP A 174      14.768  57.268  52.565  1.00 51.83           C  
ATOM   1327  CG  TRP A 174      16.111  57.228  53.135  1.00 48.02           C  
ATOM   1328  CD1 TRP A 174      17.284  57.038  52.470  1.00 47.84           C  
ATOM   1329  CD2 TRP A 174      16.444  57.396  54.504  1.00 45.80           C  
ATOM   1330  NE1 TRP A 174      18.340  57.076  53.357  1.00 48.58           N  
ATOM   1331  CE2 TRP A 174      17.839  57.296  54.612  1.00 47.19           C  
ATOM   1332  CE3 TRP A 174      15.695  57.618  55.653  1.00 44.97           C  
ATOM   1333  CZ2 TRP A 174      18.493  57.412  55.822  1.00 48.71           C  
ATOM   1334  CZ3 TRP A 174      16.338  57.736  56.857  1.00 48.72           C  
ATOM   1335  CH2 TRP A 174      17.726  57.632  56.941  1.00 49.49           C  
ATOM   1336  N   GLY A 175      14.772  54.006  50.722  1.00 55.33           N  
ATOM   1337  CA  GLY A 175      14.949  52.562  50.828  1.00 54.69           C  
ATOM   1338  C   GLY A 175      13.635  51.924  50.357  1.00 54.21           C  
ATOM   1339  O   GLY A 175      12.787  52.595  49.734  1.00 55.92           O  
ATOM   1340  N   ALA A 176      13.420  50.645  50.639  1.00 50.66           N  
ATOM   1341  CA  ALA A 176      12.171  50.045  50.192  1.00 46.43           C  
ATOM   1342  C   ALA A 176      12.050  48.674  50.729  1.00 43.84           C  
ATOM   1343  O   ALA A 176      13.047  48.004  50.869  1.00 44.92           O  
ATOM   1344  CB  ALA A 176      12.120  49.992  48.672  1.00 45.98           C  
ATOM   1345  N   TYR A 177      10.828  48.284  51.057  1.00 42.32           N  
ATOM   1346  CA  TYR A 177      10.528  46.950  51.536  1.00 39.91           C  
ATOM   1347  C   TYR A 177       9.997  46.267  50.302  1.00 39.82           C  
ATOM   1348  O   TYR A 177       9.110  46.794  49.647  1.00 41.70           O  
ATOM   1349  CB  TYR A 177       9.445  46.969  52.614  1.00 35.75           C  
ATOM   1350  CG  TYR A 177       9.948  47.508  53.929  1.00 34.92           C  
ATOM   1351  CD1 TYR A 177      10.870  46.780  54.685  1.00 33.99           C  
ATOM   1352  CD2 TYR A 177       9.544  48.772  54.413  1.00 30.28           C  
ATOM   1353  CE1 TYR A 177      11.383  47.293  55.886  1.00 29.62           C  
ATOM   1354  CE2 TYR A 177      10.057  49.274  55.604  1.00 27.31           C  
ATOM   1355  CZ  TYR A 177      10.977  48.521  56.318  1.00 26.10           C  
ATOM   1356  OH  TYR A 177      11.528  48.995  57.450  1.00 25.49           O  
ATOM   1357  N   THR A 178      10.560  45.117  49.969  1.00 39.19           N  
ATOM   1358  CA  THR A 178      10.110  44.357  48.821  1.00 40.71           C  
ATOM   1359  C   THR A 178      10.331  42.917  49.202  1.00 39.91           C  
ATOM   1360  O   THR A 178      10.651  42.635  50.357  1.00 39.07           O  
ATOM   1361  CB  THR A 178      10.920  44.684  47.555  1.00 43.12           C  
ATOM   1362  OG1 THR A 178      10.619  43.742  46.506  1.00 43.65           O  
ATOM   1363  CG2 THR A 178      12.416  44.661  47.879  1.00 44.47           C  
ATOM   1364  N   LEU A 179      10.152  42.020  48.233  1.00 40.46           N  
ATOM   1365  CA  LEU A 179      10.308  40.581  48.444  1.00 42.99           C  
ATOM   1366  C   LEU A 179      11.807  40.083  48.454  1.00 46.36           C  
ATOM   1367  O   LEU A 179      12.751  40.738  47.922  1.00 48.01           O  
ATOM   1368  CB  LEU A 179       9.460  39.838  47.375  1.00 39.02           C  
ATOM   1369  CG  LEU A 179       7.945  40.126  47.286  1.00 36.45           C  
ATOM   1370  CD1 LEU A 179       7.408  39.881  45.910  1.00 32.11           C  
ATOM   1371  CD2 LEU A 179       7.227  39.254  48.264  1.00 36.03           C  
ATOM   1372  N   GLU A 180      12.032  38.939  49.093  1.00 45.99           N  
ATOM   1373  CA  GLU A 180      13.366  38.365  49.145  1.00 45.97           C  
ATOM   1374  C   GLU A 180      13.284  36.840  49.040  1.00 46.72           C  
ATOM   1375  O   GLU A 180      12.188  36.255  49.010  1.00 47.90           O  
ATOM   1376  CB  GLU A 180      14.062  38.740  50.441  1.00 42.37           C  
ATOM   1377  CG  GLU A 180      13.237  38.482  51.637  1.00 41.10           C  
ATOM   1378  CD  GLU A 180      14.067  38.569  52.885  1.00 43.97           C  
ATOM   1379  OE1 GLU A 180      15.247  38.940  52.741  1.00 42.06           O  
ATOM   1380  OE2 GLU A 180      13.565  38.269  54.006  1.00 45.56           O  
ATOM   1381  N   GLY A 181      14.449  36.197  48.980  1.00 45.66           N  
ATOM   1382  CA  GLY A 181      14.497  34.750  48.897  1.00 40.38           C  
ATOM   1383  C   GLY A 181      13.498  34.141  47.949  1.00 37.59           C  
ATOM   1384  O   GLY A 181      13.484  34.476  46.760  1.00 34.31           O  
ATOM   1385  N   VAL A 182      12.670  33.246  48.483  1.00 37.08           N  
ATOM   1386  CA  VAL A 182      11.692  32.543  47.678  1.00 40.90           C  
ATOM   1387  C   VAL A 182      10.426  33.325  47.395  1.00 44.24           C  
ATOM   1388  O   VAL A 182       9.422  32.762  46.926  1.00 46.17           O  
ATOM   1389  CB  VAL A 182      11.344  31.196  48.286  1.00 40.37           C  
ATOM   1390  CG1 VAL A 182      12.542  30.280  48.163  1.00 40.21           C  
ATOM   1391  CG2 VAL A 182      10.956  31.363  49.717  1.00 40.21           C  
ATOM   1392  N   LEU A 183      10.497  34.630  47.686  1.00 46.47           N  
ATOM   1393  CA  LEU A 183       9.423  35.606  47.433  1.00 44.32           C  
ATOM   1394  C   LEU A 183       8.073  35.356  48.101  1.00 43.41           C  
ATOM   1395  O   LEU A 183       7.034  35.527  47.470  1.00 43.79           O  
ATOM   1396  CB  LEU A 183       9.222  35.727  45.921  1.00 44.62           C  
ATOM   1397  CG  LEU A 183      10.509  35.732  45.100  1.00 42.79           C  
ATOM   1398  CD1 LEU A 183      10.186  35.997  43.634  1.00 44.00           C  
ATOM   1399  CD2 LEU A 183      11.444  36.798  45.669  1.00 44.32           C  
ATOM   1400  N   CYS A 184       8.087  34.950  49.364  1.00 41.69           N  
ATOM   1401  CA  CYS A 184       6.849  34.711  50.082  1.00 41.10           C  
ATOM   1402  C   CYS A 184       6.822  35.466  51.379  1.00 40.02           C  
ATOM   1403  O   CYS A 184       6.081  35.122  52.285  1.00 42.74           O  
ATOM   1404  CB  CYS A 184       6.627  33.229  50.343  1.00 40.46           C  
ATOM   1405  SG  CYS A 184       6.209  32.455  48.821  1.00 51.91           S  
ATOM   1406  N   ASN A 185       7.655  36.481  51.480  1.00 38.04           N  
ATOM   1407  CA  ASN A 185       7.654  37.303  52.647  1.00 37.60           C  
ATOM   1408  C   ASN A 185       8.331  38.605  52.229  1.00 40.39           C  
ATOM   1409  O   ASN A 185       8.974  38.673  51.172  1.00 41.90           O  
ATOM   1410  CB  ASN A 185       8.343  36.603  53.821  1.00 35.95           C  
ATOM   1411  CG  ASN A 185       9.839  36.601  53.713  1.00 38.69           C  
ATOM   1412  OD1 ASN A 185      10.428  35.627  53.226  1.00 39.64           O  
ATOM   1413  ND2 ASN A 185      10.482  37.695  54.175  1.00 36.92           N  
ATOM   1414  N   CYS A 186       8.160  39.669  53.007  1.00 41.91           N  
ATOM   1415  CA  CYS A 186       8.774  40.918  52.601  1.00 40.57           C  
ATOM   1416  C   CYS A 186       9.890  41.315  53.537  1.00 37.58           C  
ATOM   1417  O   CYS A 186      10.017  40.769  54.625  1.00 32.66           O  
ATOM   1418  CB  CYS A 186       7.674  41.995  52.410  1.00 40.68           C  
ATOM   1419  SG  CYS A 186       6.805  41.658  50.820  1.00 42.93           S  
ATOM   1420  N   SER A 187      10.735  42.211  53.043  1.00 38.94           N  
ATOM   1421  CA  SER A 187      11.888  42.726  53.768  1.00 42.55           C  
ATOM   1422  C   SER A 187      12.339  44.051  53.138  1.00 43.76           C  
ATOM   1423  O   SER A 187      11.674  44.563  52.255  1.00 44.40           O  
ATOM   1424  CB  SER A 187      13.030  41.739  53.655  1.00 45.33           C  
ATOM   1425  OG  SER A 187      14.024  42.013  54.636  1.00 49.51           O  
ATOM   1426  N   PHE A 188      13.477  44.584  53.575  1.00 46.27           N  
ATOM   1427  CA  PHE A 188      14.014  45.824  53.023  1.00 49.09           C  
ATOM   1428  C   PHE A 188      14.997  45.461  51.911  1.00 53.25           C  
ATOM   1429  O   PHE A 188      15.798  44.526  52.076  1.00 54.18           O  
ATOM   1430  CB  PHE A 188      14.729  46.627  54.110  1.00 49.69           C  
ATOM   1431  CG  PHE A 188      16.009  46.006  54.608  1.00 48.49           C  
ATOM   1432  CD1 PHE A 188      17.239  46.487  54.181  1.00 49.80           C  
ATOM   1433  CD2 PHE A 188      15.981  44.939  55.482  1.00 47.61           C  
ATOM   1434  CE1 PHE A 188      18.418  45.912  54.608  1.00 47.69           C  
ATOM   1435  CE2 PHE A 188      17.158  44.362  55.910  1.00 48.27           C  
ATOM   1436  CZ  PHE A 188      18.378  44.852  55.466  1.00 47.65           C  
ATOM   1437  N   ASP A 189      14.956  46.193  50.789  1.00 56.46           N  
ATOM   1438  CA  ASP A 189      15.822  45.877  49.647  1.00 56.74           C  
ATOM   1439  C   ASP A 189      17.269  46.156  50.011  1.00 57.36           C  
ATOM   1440  O   ASP A 189      17.652  47.304  50.287  1.00 56.03           O  
ATOM   1441  CB  ASP A 189      15.402  46.666  48.402  1.00 56.84           C  
ATOM   1442  CG  ASP A 189      16.052  46.144  47.142  1.00 57.25           C  
ATOM   1443  OD1 ASP A 189      17.260  45.833  47.216  1.00 57.12           O  
ATOM   1444  OD2 ASP A 189      15.365  46.046  46.086  1.00 56.50           O  
ATOM   1445  N   TYR A 190      18.053  45.074  50.058  1.00 57.53           N  
ATOM   1446  CA  TYR A 190      19.472  45.139  50.410  1.00 56.08           C  
ATOM   1447  C   TYR A 190      20.307  44.856  49.189  1.00 55.71           C  
ATOM   1448  O   TYR A 190      21.539  44.894  49.236  1.00 57.99           O  
ATOM   1449  CB  TYR A 190      19.809  44.130  51.527  1.00 55.36           C  
ATOM   1450  CG  TYR A 190      19.196  42.738  51.393  1.00 53.00           C  
ATOM   1451  CD1 TYR A 190      18.347  42.225  52.395  1.00 48.65           C  
ATOM   1452  CD2 TYR A 190      19.452  41.940  50.264  1.00 51.84           C  
ATOM   1453  CE1 TYR A 190      17.770  40.967  52.271  1.00 44.38           C  
ATOM   1454  CE2 TYR A 190      18.871  40.679  50.138  1.00 50.28           C  
ATOM   1455  CZ  TYR A 190      18.028  40.205  51.139  1.00 46.53           C  
ATOM   1456  OH  TYR A 190      17.392  39.004  50.941  1.00 46.53           O  
ATOM   1457  N   ILE A 191      19.622  44.585  48.090  1.00 52.77           N  
ATOM   1458  CA  ILE A 191      20.306  44.287  46.873  1.00 50.49           C  
ATOM   1459  C   ILE A 191      20.730  45.568  46.197  1.00 51.87           C  
ATOM   1460  O   ILE A 191      21.924  45.862  46.166  1.00 50.01           O  
ATOM   1461  CB  ILE A 191      19.407  43.428  45.994  1.00 49.35           C  
ATOM   1462  CG1 ILE A 191      19.034  42.181  46.782  1.00 47.12           C  
ATOM   1463  CG2 ILE A 191      20.086  43.068  44.686  1.00 45.89           C  
ATOM   1464  CD1 ILE A 191      18.422  41.099  45.903  1.00 50.67           C  
ATOM   1465  N   SER A 192      19.757  46.329  45.683  1.00 55.58           N  
ATOM   1466  CA  SER A 192      19.999  47.599  44.976  1.00 58.91           C  
ATOM   1467  C   SER A 192      21.023  48.480  45.649  1.00 61.66           C  
ATOM   1468  O   SER A 192      20.801  48.885  46.803  1.00 65.36           O  
ATOM   1469  CB  SER A 192      18.717  48.377  44.855  1.00 56.49           C  
ATOM   1470  OG  SER A 192      18.167  48.048  43.602  1.00 61.78           O  
ATOM   1471  N   ARG A 193      22.103  48.835  44.930  1.00 61.07           N  
ATOM   1472  CA  ARG A 193      23.190  49.620  45.534  1.00 59.59           C  
ATOM   1473  C   ARG A 193      23.343  51.108  45.276  1.00 60.77           C  
ATOM   1474  O   ARG A 193      24.455  51.629  45.341  1.00 57.60           O  
ATOM   1475  CB  ARG A 193      24.508  48.922  45.251  1.00 55.86           C  
ATOM   1476  CG  ARG A 193      24.684  47.704  46.093  1.00 53.01           C  
ATOM   1477  CD  ARG A 193      25.194  46.580  45.260  1.00 51.85           C  
ATOM   1478  NE  ARG A 193      26.232  45.883  45.990  1.00 52.25           N  
ATOM   1479  CZ  ARG A 193      27.059  45.014  45.442  1.00 52.33           C  
ATOM   1480  NH1 ARG A 193      27.990  44.419  46.180  1.00 53.05           N  
ATOM   1481  NH2 ARG A 193      26.944  44.745  44.153  1.00 52.33           N  
ATOM   1482  N   ASP A 194      22.221  51.790  45.036  1.00 64.62           N  
ATOM   1483  CA  ASP A 194      22.203  53.235  44.770  1.00 66.99           C  
ATOM   1484  C   ASP A 194      22.457  54.045  46.038  1.00 67.42           C  
ATOM   1485  O   ASP A 194      22.412  53.503  47.141  1.00 68.18           O  
ATOM   1486  CB  ASP A 194      20.860  53.638  44.159  1.00 68.99           C  
ATOM   1487  CG  ASP A 194      19.686  53.182  44.995  1.00 71.13           C  
ATOM   1488  OD1 ASP A 194      19.187  52.040  44.780  1.00 70.51           O  
ATOM   1489  OD2 ASP A 194      19.285  53.978  45.883  1.00 73.49           O  
ATOM   1490  N   SER A 195      22.716  55.339  45.885  1.00 69.79           N  
ATOM   1491  CA  SER A 195      23.011  56.196  47.036  1.00 73.29           C  
ATOM   1492  C   SER A 195      21.916  56.111  48.104  1.00 75.21           C  
ATOM   1493  O   SER A 195      22.204  55.817  49.290  1.00 76.97           O  
ATOM   1494  CB  SER A 195      23.182  57.661  46.585  1.00 74.30           C  
ATOM   1495  OG  SER A 195      23.360  58.555  47.690  1.00 74.95           O  
ATOM   1496  N   THR A 196      20.668  56.370  47.680  1.00 73.54           N  
ATOM   1497  CA  THR A 196      19.503  56.333  48.575  1.00 70.02           C  
ATOM   1498  C   THR A 196      19.402  55.017  49.382  1.00 67.06           C  
ATOM   1499  O   THR A 196      19.499  55.000  50.626  1.00 65.79           O  
ATOM   1500  CB  THR A 196      18.212  56.529  47.770  1.00 70.68           C  
ATOM   1501  OG1 THR A 196      18.338  57.716  46.972  1.00 74.06           O  
ATOM   1502  CG2 THR A 196      17.007  56.677  48.716  1.00 71.75           C  
ATOM   1503  N   THR A 197      19.219  53.920  48.669  1.00 61.97           N  
ATOM   1504  CA  THR A 197      19.112  52.653  49.323  1.00 59.09           C  
ATOM   1505  C   THR A 197      20.263  52.410  50.271  1.00 59.82           C  
ATOM   1506  O   THR A 197      20.038  52.064  51.429  1.00 64.40           O  
ATOM   1507  CB  THR A 197      19.078  51.522  48.309  1.00 58.57           C  
ATOM   1508  OG1 THR A 197      17.964  51.714  47.430  1.00 58.36           O  
ATOM   1509  CG2 THR A 197      18.933  50.184  49.002  1.00 56.52           C  
ATOM   1510  N   ARG A 198      21.498  52.608  49.819  1.00 58.34           N  
ATOM   1511  CA  ARG A 198      22.651  52.326  50.682  1.00 56.07           C  
ATOM   1512  C   ARG A 198      22.732  53.149  51.966  1.00 54.41           C  
ATOM   1513  O   ARG A 198      23.210  52.657  52.990  1.00 52.01           O  
ATOM   1514  CB  ARG A 198      23.950  52.453  49.885  1.00 56.24           C  
ATOM   1515  CG  ARG A 198      25.186  52.123  50.698  1.00 58.20           C  
ATOM   1516  CD  ARG A 198      26.417  52.024  49.829  1.00 59.09           C  
ATOM   1517  NE  ARG A 198      26.463  50.736  49.172  1.00 63.06           N  
ATOM   1518  CZ  ARG A 198      27.356  50.395  48.243  1.00 65.82           C  
ATOM   1519  NH1 ARG A 198      28.298  51.264  47.861  1.00 64.75           N  
ATOM   1520  NH2 ARG A 198      27.284  49.183  47.681  1.00 63.91           N  
ATOM   1521  N   SER A 199      22.257  54.390  51.919  1.00 54.65           N  
ATOM   1522  CA  SER A 199      22.296  55.254  53.097  1.00 55.00           C  
ATOM   1523  C   SER A 199      21.291  54.754  54.105  1.00 53.75           C  
ATOM   1524  O   SER A 199      21.563  54.706  55.319  1.00 53.32           O  
ATOM   1525  CB  SER A 199      21.976  56.711  52.725  1.00 56.82           C  
ATOM   1526  OG  SER A 199      20.727  56.821  52.065  1.00 52.92           O  
ATOM   1527  N   ASN A 200      20.124  54.371  53.601  1.00 52.28           N  
ATOM   1528  CA  ASN A 200      19.081  53.861  54.492  1.00 52.02           C  
ATOM   1529  C   ASN A 200      19.561  52.588  55.163  1.00 51.12           C  
ATOM   1530  O   ASN A 200      19.332  52.405  56.359  1.00 49.43           O  
ATOM   1531  CB  ASN A 200      17.775  53.581  53.742  1.00 49.86           C  
ATOM   1532  CG  ASN A 200      16.634  53.186  54.686  1.00 45.91           C  
ATOM   1533  OD1 ASN A 200      16.173  52.044  54.672  1.00 39.17           O  
ATOM   1534  ND2 ASN A 200      16.190  54.136  55.516  1.00 41.68           N  
ATOM   1535  N   ILE A 201      20.214  51.716  54.388  1.00 50.34           N  
ATOM   1536  CA  ILE A 201      20.774  50.496  54.939  1.00 51.15           C  
ATOM   1537  C   ILE A 201      21.833  50.848  56.022  1.00 52.72           C  
ATOM   1538  O   ILE A 201      21.820  50.323  57.156  1.00 53.20           O  
ATOM   1539  CB  ILE A 201      21.447  49.657  53.866  1.00 48.29           C  
ATOM   1540  CG1 ILE A 201      20.410  49.114  52.915  1.00 46.95           C  
ATOM   1541  CG2 ILE A 201      22.176  48.501  54.516  1.00 49.22           C  
ATOM   1542  CD1 ILE A 201      21.007  48.262  51.838  1.00 49.92           C  
ATOM   1543  N   LEU A 202      22.753  51.742  55.672  1.00 52.89           N  
ATOM   1544  CA  LEU A 202      23.776  52.134  56.620  1.00 53.47           C  
ATOM   1545  C   LEU A 202      23.117  52.726  57.857  1.00 53.61           C  
ATOM   1546  O   LEU A 202      23.608  52.541  58.979  1.00 54.95           O  
ATOM   1547  CB  LEU A 202      24.724  53.134  55.989  1.00 52.18           C  
ATOM   1548  CG  LEU A 202      25.495  52.512  54.836  1.00 50.13           C  
ATOM   1549  CD1 LEU A 202      26.264  53.617  54.184  1.00 53.44           C  
ATOM   1550  CD2 LEU A 202      26.419  51.401  55.315  1.00 47.69           C  
ATOM   1551  N   CYS A 203      21.998  53.415  57.660  1.00 50.28           N  
ATOM   1552  CA  CYS A 203      21.294  53.996  58.789  1.00 50.77           C  
ATOM   1553  C   CYS A 203      20.661  52.919  59.678  1.00 50.56           C  
ATOM   1554  O   CYS A 203      20.718  52.989  60.927  1.00 48.19           O  
ATOM   1555  CB  CYS A 203      20.217  54.931  58.290  1.00 52.11           C  
ATOM   1556  SG  CYS A 203      20.796  56.571  58.148  1.00 54.55           S  
ATOM   1557  N   MET A 204      20.051  51.931  59.025  1.00 48.25           N  
ATOM   1558  CA  MET A 204      19.409  50.851  59.748  1.00 47.93           C  
ATOM   1559  C   MET A 204      20.428  50.102  60.590  1.00 48.88           C  
ATOM   1560  O   MET A 204      20.236  49.915  61.790  1.00 51.47           O  
ATOM   1561  CB  MET A 204      18.739  49.868  58.791  1.00 47.99           C  
ATOM   1562  CG  MET A 204      17.373  50.280  58.316  1.00 49.17           C  
ATOM   1563  SD  MET A 204      16.661  49.039  57.236  1.00 55.07           S  
ATOM   1564  CE  MET A 204      15.003  49.760  56.937  1.00 56.14           C  
ATOM   1565  N   PHE A 205      21.514  49.682  59.961  1.00 46.99           N  
ATOM   1566  CA  PHE A 205      22.518  48.937  60.662  1.00 46.85           C  
ATOM   1567  C   PHE A 205      23.182  49.704  61.791  1.00 50.25           C  
ATOM   1568  O   PHE A 205      23.383  49.164  62.891  1.00 52.61           O  
ATOM   1569  CB  PHE A 205      23.564  48.471  59.675  1.00 42.66           C  
ATOM   1570  CG  PHE A 205      23.244  47.169  59.037  1.00 38.11           C  
ATOM   1571  CD1 PHE A 205      23.608  45.975  59.639  1.00 39.24           C  
ATOM   1572  CD2 PHE A 205      22.581  47.125  57.840  1.00 35.02           C  
ATOM   1573  CE1 PHE A 205      23.310  44.734  59.041  1.00 36.64           C  
ATOM   1574  CE2 PHE A 205      22.279  45.901  57.235  1.00 34.35           C  
ATOM   1575  CZ  PHE A 205      22.646  44.707  57.838  1.00 34.04           C  
ATOM   1576  N   ILE A 206      23.504  50.969  61.551  1.00 51.85           N  
ATOM   1577  CA  ILE A 206      24.211  51.757  62.566  1.00 52.79           C  
ATOM   1578  C   ILE A 206      23.312  52.352  63.612  1.00 51.65           C  
ATOM   1579  O   ILE A 206      23.554  52.183  64.792  1.00 49.58           O  
ATOM   1580  CB  ILE A 206      25.039  52.869  61.903  1.00 55.06           C  
ATOM   1581  CG1 ILE A 206      26.065  52.253  60.938  1.00 57.14           C  
ATOM   1582  CG2 ILE A 206      25.759  53.655  62.937  1.00 54.64           C  
ATOM   1583  CD1 ILE A 206      26.598  53.215  59.897  1.00 56.89           C  
ATOM   1584  N   LEU A 207      22.273  53.053  63.186  1.00 53.84           N  
ATOM   1585  CA  LEU A 207      21.348  53.631  64.160  1.00 57.42           C  
ATOM   1586  C   LEU A 207      20.415  52.568  64.811  1.00 57.81           C  
ATOM   1587  O   LEU A 207      20.314  52.478  66.043  1.00 54.46           O  
ATOM   1588  CB  LEU A 207      20.508  54.751  63.504  1.00 57.51           C  
ATOM   1589  CG  LEU A 207      21.256  56.023  63.116  1.00 55.72           C  
ATOM   1590  CD1 LEU A 207      22.014  56.556  64.289  1.00 50.97           C  
ATOM   1591  CD2 LEU A 207      22.208  55.719  61.985  1.00 55.61           C  
ATOM   1592  N   GLY A 208      19.765  51.766  63.967  1.00 58.90           N  
ATOM   1593  CA  GLY A 208      18.834  50.764  64.433  1.00 60.16           C  
ATOM   1594  C   GLY A 208      19.452  49.606  65.173  1.00 63.12           C  
ATOM   1595  O   GLY A 208      18.914  49.180  66.203  1.00 67.19           O  
ATOM   1596  N   PHE A 209      20.581  49.102  64.683  1.00 62.28           N  
ATOM   1597  CA  PHE A 209      21.238  47.956  65.312  1.00 60.73           C  
ATOM   1598  C   PHE A 209      22.429  48.287  66.225  1.00 61.03           C  
ATOM   1599  O   PHE A 209      22.331  48.146  67.449  1.00 62.25           O  
ATOM   1600  CB  PHE A 209      21.650  46.963  64.222  1.00 60.22           C  
ATOM   1601  CG  PHE A 209      22.124  45.639  64.745  1.00 59.66           C  
ATOM   1602  CD1 PHE A 209      21.582  45.090  65.895  1.00 61.08           C  
ATOM   1603  CD2 PHE A 209      23.052  44.896  64.041  1.00 58.88           C  
ATOM   1604  CE1 PHE A 209      21.951  43.809  66.328  1.00 58.57           C  
ATOM   1605  CE2 PHE A 209      23.424  43.619  64.469  1.00 58.23           C  
ATOM   1606  CZ  PHE A 209      22.868  43.082  65.608  1.00 56.90           C  
ATOM   1607  N   PHE A 210      23.546  48.739  65.653  1.00 60.11           N  
ATOM   1608  CA  PHE A 210      24.733  49.062  66.456  1.00 58.77           C  
ATOM   1609  C   PHE A 210      24.449  49.981  67.624  1.00 58.90           C  
ATOM   1610  O   PHE A 210      25.022  49.838  68.707  1.00 58.83           O  
ATOM   1611  CB  PHE A 210      25.810  49.680  65.577  1.00 57.07           C  
ATOM   1612  CG  PHE A 210      26.229  48.796  64.449  1.00 58.42           C  
ATOM   1613  CD1 PHE A 210      26.438  47.425  64.657  1.00 58.95           C  
ATOM   1614  CD2 PHE A 210      26.413  49.307  63.176  1.00 60.03           C  
ATOM   1615  CE1 PHE A 210      26.823  46.565  63.613  1.00 55.39           C  
ATOM   1616  CE2 PHE A 210      26.798  48.460  62.119  1.00 58.29           C  
ATOM   1617  CZ  PHE A 210      27.000  47.083  62.351  1.00 56.39           C  
ATOM   1618  N   GLY A 211      23.546  50.923  67.391  1.00 61.56           N  
ATOM   1619  CA  GLY A 211      23.180  51.886  68.418  1.00 62.17           C  
ATOM   1620  C   GLY A 211      22.865  51.270  69.764  1.00 61.79           C  
ATOM   1621  O   GLY A 211      23.694  51.342  70.689  1.00 58.22           O  
ATOM   1622  N   PRO A 212      21.658  50.649  69.894  1.00 63.31           N  
ATOM   1623  CA  PRO A 212      21.220  50.011  71.146  1.00 62.36           C  
ATOM   1624  C   PRO A 212      22.251  49.017  71.667  1.00 60.83           C  
ATOM   1625  O   PRO A 212      22.315  48.749  72.879  1.00 60.80           O  
ATOM   1626  CB  PRO A 212      19.883  49.364  70.760  1.00 63.16           C  
ATOM   1627  CG  PRO A 212      19.981  49.158  69.282  1.00 61.38           C  
ATOM   1628  CD  PRO A 212      20.653  50.428  68.826  1.00 62.96           C  
ATOM   1629  N   ILE A 213      23.058  48.486  70.746  1.00 57.93           N  
ATOM   1630  CA  ILE A 213      24.121  47.559  71.114  1.00 55.16           C  
ATOM   1631  C   ILE A 213      25.150  48.251  72.003  1.00 55.21           C  
ATOM   1632  O   ILE A 213      25.589  47.701  73.020  1.00 54.16           O  
ATOM   1633  CB  ILE A 213      24.839  47.027  69.890  1.00 51.65           C  
ATOM   1634  CG1 ILE A 213      23.903  46.097  69.109  1.00 52.13           C  
ATOM   1635  CG2 ILE A 213      26.077  46.317  70.318  1.00 51.68           C  
ATOM   1636  CD1 ILE A 213      24.553  45.297  67.991  1.00 49.11           C  
ATOM   1637  N   LEU A 214      25.546  49.459  71.613  1.00 56.60           N  
ATOM   1638  CA  LEU A 214      26.505  50.204  72.411  1.00 58.82           C  
ATOM   1639  C   LEU A 214      25.925  50.445  73.807  1.00 60.21           C  
ATOM   1640  O   LEU A 214      26.595  50.237  74.818  1.00 59.12           O  
ATOM   1641  CB  LEU A 214      26.830  51.526  71.732  1.00 60.46           C  
ATOM   1642  CG  LEU A 214      27.565  51.403  70.403  1.00 62.79           C  
ATOM   1643  CD1 LEU A 214      27.614  52.750  69.704  1.00 67.03           C  
ATOM   1644  CD2 LEU A 214      28.965  50.911  70.665  1.00 64.23           C  
ATOM   1645  N   ILE A 215      24.663  50.867  73.859  1.00 62.09           N  
ATOM   1646  CA  ILE A 215      24.013  51.122  75.131  1.00 62.78           C  
ATOM   1647  C   ILE A 215      24.101  49.850  75.926  1.00 63.65           C  
ATOM   1648  O   ILE A 215      24.531  49.884  77.068  1.00 65.73           O  
ATOM   1649  CB  ILE A 215      22.525  51.513  74.967  1.00 63.27           C  
ATOM   1650  CG1 ILE A 215      22.419  52.842  74.216  1.00 63.13           C  
ATOM   1651  CG2 ILE A 215      21.875  51.665  76.340  1.00 63.41           C  
ATOM   1652  CD1 ILE A 215      21.018  53.267  73.907  1.00 61.88           C  
ATOM   1653  N   ILE A 216      23.707  48.727  75.321  1.00 63.48           N  
ATOM   1654  CA  ILE A 216      23.756  47.431  76.012  1.00 62.02           C  
ATOM   1655  C   ILE A 216      25.137  47.147  76.603  1.00 63.14           C  
ATOM   1656  O   ILE A 216      25.252  46.983  77.814  1.00 61.15           O  
ATOM   1657  CB  ILE A 216      23.378  46.271  75.074  1.00 59.56           C  
ATOM   1658  CG1 ILE A 216      21.900  46.344  74.719  1.00 56.61           C  
ATOM   1659  CG2 ILE A 216      23.680  44.943  75.742  1.00 56.77           C  
ATOM   1660  CD1 ILE A 216      21.558  45.562  73.470  1.00 57.06           C  
ATOM   1661  N   PHE A 217      26.173  47.093  75.749  1.00 66.76           N  
ATOM   1662  CA  PHE A 217      27.553  46.823  76.197  1.00 69.62           C  
ATOM   1663  C   PHE A 217      28.046  47.810  77.275  1.00 70.02           C  
ATOM   1664  O   PHE A 217      28.628  47.407  78.304  1.00 70.23           O  
ATOM   1665  CB  PHE A 217      28.525  46.821  74.998  1.00 70.32           C  
ATOM   1666  CG  PHE A 217      29.995  46.844  75.401  1.00 74.43           C  
ATOM   1667  CD1 PHE A 217      30.648  48.063  75.640  1.00 75.30           C  
ATOM   1668  CD2 PHE A 217      30.725  45.653  75.550  1.00 73.67           C  
ATOM   1669  CE1 PHE A 217      31.998  48.103  76.019  1.00 73.68           C  
ATOM   1670  CE2 PHE A 217      32.074  45.684  75.928  1.00 73.42           C  
ATOM   1671  CZ  PHE A 217      32.712  46.914  76.163  1.00 72.78           C  
ATOM   1672  N   PHE A 218      27.798  49.095  77.034  1.00 68.44           N  
ATOM   1673  CA  PHE A 218      28.198  50.132  77.956  1.00 66.34           C  
ATOM   1674  C   PHE A 218      27.548  49.923  79.302  1.00 67.21           C  
ATOM   1675  O   PHE A 218      28.115  50.306  80.298  1.00 69.90           O  
ATOM   1676  CB  PHE A 218      27.815  51.493  77.402  1.00 65.41           C  
ATOM   1677  CG  PHE A 218      27.991  52.610  78.373  1.00 65.59           C  
ATOM   1678  CD1 PHE A 218      27.037  52.849  79.389  1.00 65.25           C  
ATOM   1679  CD2 PHE A 218      29.103  53.433  78.281  1.00 66.22           C  
ATOM   1680  CE1 PHE A 218      27.185  53.901  80.311  1.00 64.62           C  
ATOM   1681  CE2 PHE A 218      29.268  54.487  79.189  1.00 69.12           C  
ATOM   1682  CZ  PHE A 218      28.298  54.725  80.218  1.00 67.14           C  
ATOM   1683  N   CYS A 219      26.364  49.315  79.338  1.00 68.51           N  
ATOM   1684  CA  CYS A 219      25.657  49.088  80.596  1.00 69.23           C  
ATOM   1685  C   CYS A 219      26.092  47.804  81.250  1.00 71.39           C  
ATOM   1686  O   CYS A 219      26.307  47.756  82.462  1.00 73.30           O  
ATOM   1687  CB  CYS A 219      24.130  49.049  80.391  1.00 67.88           C  
ATOM   1688  SG  CYS A 219      23.339  50.664  80.118  1.00 67.37           S  
ATOM   1689  N   TYR A 220      26.229  46.753  80.461  1.00 73.76           N  
ATOM   1690  CA  TYR A 220      26.602  45.491  81.047  1.00 77.76           C  
ATOM   1691  C   TYR A 220      28.054  45.485  81.339  1.00 78.70           C  
ATOM   1692  O   TYR A 220      28.459  45.005  82.394  1.00 78.92           O  
ATOM   1693  CB  TYR A 220      26.217  44.325  80.140  1.00 83.44           C  
ATOM   1694  CG  TYR A 220      24.718  44.100  80.114  1.00 89.52           C  
ATOM   1695  CD1 TYR A 220      24.003  43.857  81.304  1.00 90.04           C  
ATOM   1696  CD2 TYR A 220      23.999  44.239  78.921  1.00 92.95           C  
ATOM   1697  CE1 TYR A 220      22.608  43.774  81.311  1.00 93.42           C  
ATOM   1698  CE2 TYR A 220      22.599  44.157  78.912  1.00 96.35           C  
ATOM   1699  CZ  TYR A 220      21.906  43.931  80.112  1.00 96.25           C  
ATOM   1700  OH  TYR A 220      20.517  43.911  80.106  1.00 98.32           O  
ATOM   1701  N   PHE A 221      28.856  46.025  80.429  1.00 80.30           N  
ATOM   1702  CA  PHE A 221      30.287  46.057  80.708  1.00 82.87           C  
ATOM   1703  C   PHE A 221      30.520  46.939  81.964  1.00 82.26           C  
ATOM   1704  O   PHE A 221      31.525  46.803  82.693  1.00 83.29           O  
ATOM   1705  CB  PHE A 221      31.076  46.612  79.520  1.00 83.48           C  
ATOM   1706  CG  PHE A 221      32.559  46.605  79.743  1.00 85.98           C  
ATOM   1707  CD1 PHE A 221      33.243  45.394  79.886  1.00 87.00           C  
ATOM   1708  CD2 PHE A 221      33.267  47.802  79.849  1.00 85.96           C  
ATOM   1709  CE1 PHE A 221      34.612  45.374  80.129  1.00 87.95           C  
ATOM   1710  CE2 PHE A 221      34.630  47.796  80.091  1.00 86.66           C  
ATOM   1711  CZ  PHE A 221      35.309  46.575  80.231  1.00 87.67           C  
ATOM   1712  N   ASN A 222      29.562  47.828  82.212  1.00 79.51           N  
ATOM   1713  CA  ASN A 222      29.616  48.739  83.351  1.00 77.17           C  
ATOM   1714  C   ASN A 222      29.135  48.034  84.619  1.00 77.59           C  
ATOM   1715  O   ASN A 222      29.428  48.469  85.732  1.00 77.63           O  
ATOM   1716  CB  ASN A 222      28.728  49.954  83.089  1.00 74.39           C  
ATOM   1717  CG  ASN A 222      29.187  51.192  83.834  1.00 72.45           C  
ATOM   1718  OD1 ASN A 222      29.364  51.188  85.057  1.00 71.64           O  
ATOM   1719  ND2 ASN A 222      29.373  52.272  83.093  1.00 72.36           N  
ATOM   1720  N   ILE A 223      28.380  46.956  84.442  1.00 77.93           N  
ATOM   1721  CA  ILE A 223      27.866  46.197  85.564  1.00 77.60           C  
ATOM   1722  C   ILE A 223      28.922  45.183  85.966  1.00 79.39           C  
ATOM   1723  O   ILE A 223      28.975  44.752  87.115  1.00 78.17           O  
ATOM   1724  CB  ILE A 223      26.539  45.500  85.183  1.00 74.89           C  
ATOM   1725  CG1 ILE A 223      25.428  46.547  85.086  1.00 70.71           C  
ATOM   1726  CG2 ILE A 223      26.196  44.411  86.201  1.00 73.95           C  
ATOM   1727  CD1 ILE A 223      24.100  45.973  84.689  1.00 72.01           C  
ATOM   1728  N   VAL A 224      29.768  44.824  85.004  1.00 83.03           N  
ATOM   1729  CA  VAL A 224      30.858  43.869  85.230  1.00 88.24           C  
ATOM   1730  C   VAL A 224      32.006  44.615  85.937  1.00 91.70           C  
ATOM   1731  O   VAL A 224      32.558  44.130  86.954  1.00 93.99           O  
ATOM   1732  CB  VAL A 224      31.398  43.258  83.887  1.00 87.34           C  
ATOM   1733  CG1 VAL A 224      32.573  42.325  84.155  1.00 85.85           C  
ATOM   1734  CG2 VAL A 224      30.293  42.493  83.190  1.00 87.00           C  
ATOM   1735  N   MET A 225      32.357  45.792  85.401  1.00 92.27           N  
ATOM   1736  CA  MET A 225      33.421  46.631  85.974  1.00 91.05           C  
ATOM   1737  C   MET A 225      32.866  47.376  87.188  1.00 90.36           C  
ATOM   1738  O   MET A 225      33.149  48.552  87.397  1.00 88.18           O  
ATOM   1739  CB  MET A 225      33.921  47.642  84.939  1.00 91.02           C  
ATOM   1740  CG  MET A 225      34.490  47.037  83.672  1.00 91.12           C  
ATOM   1741  SD  MET A 225      36.080  46.289  83.946  1.00 89.71           S  
ATOM   1742  CE  MET A 225      35.691  44.557  83.701  1.00 91.33           C  
ATOM   1743  N   SER A 226      32.078  46.666  87.988  1.00 92.32           N  
ATOM   1744  CA  SER A 226      31.463  47.230  89.174  1.00 95.25           C  
ATOM   1745  C   SER A 226      31.087  46.088  90.094  1.00 98.07           C  
ATOM   1746  O   SER A 226      30.557  46.305  91.180  1.00 98.47           O  
ATOM   1747  CB  SER A 226      30.204  48.002  88.796  1.00 94.94           C  
ATOM   1748  OG  SER A 226      29.258  47.141  88.176  1.00 92.61           O  
ATOM   1749  N   VAL A 227      31.350  44.865  89.650  1.00101.32           N  
ATOM   1750  CA  VAL A 227      31.026  43.707  90.463  1.00105.85           C  
ATOM   1751  C   VAL A 227      31.928  43.765  91.674  1.00107.85           C  
ATOM   1752  O   VAL A 227      31.529  43.394  92.790  1.00108.26           O  
ATOM   1753  CB  VAL A 227      31.279  42.373  89.709  1.00106.73           C  
ATOM   1754  CG1 VAL A 227      30.750  41.197  90.547  1.00108.82           C  
ATOM   1755  CG2 VAL A 227      30.586  42.392  88.349  1.00106.67           C  
ATOM   1756  N   SER A 228      33.150  44.242  91.434  1.00110.38           N  
ATOM   1757  CA  SER A 228      34.157  44.380  92.483  1.00113.01           C  
ATOM   1758  C   SER A 228      33.939  45.678  93.254  1.00114.17           C  
ATOM   1759  O   SER A 228      34.116  45.727  94.479  1.00114.97           O  
ATOM   1760  CB  SER A 228      35.562  44.341  91.880  1.00112.40           C  
ATOM   1761  OG  SER A 228      35.863  43.031  91.422  1.00113.79           O  
ATOM   1762  N   ASN A 229      33.547  46.728  92.541  1.00115.07           N  
ATOM   1763  CA  ASN A 229      33.264  47.997  93.194  1.00116.88           C  
ATOM   1764  C   ASN A 229      32.243  47.678  94.305  1.00118.72           C  
ATOM   1765  O   ASN A 229      32.283  48.219  95.418  1.00118.94           O  
ATOM   1766  CB  ASN A 229      32.657  48.985  92.186  1.00115.90           C  
ATOM   1767  CG  ASN A 229      33.574  49.265  91.010  1.00115.20           C  
ATOM   1768  OD1 ASN A 229      33.230  50.036  90.112  1.00112.99           O  
ATOM   1769  ND2 ASN A 229      34.747  48.639  91.010  1.00114.91           N  
ATOM   1770  N   HIS A 230      31.338  46.764  93.971  1.00121.04           N  
ATOM   1771  CA  HIS A 230      30.276  46.304  94.857  1.00122.59           C  
ATOM   1772  C   HIS A 230      30.805  45.264  95.854  1.00122.30           C  
ATOM   1773  O   HIS A 230      30.402  45.244  97.014  1.00120.61           O  
ATOM   1774  CB  HIS A 230      29.145  45.723  93.987  1.00124.43           C  
ATOM   1775  CG  HIS A 230      28.229  44.793  94.712  1.00126.50           C  
ATOM   1776  ND1 HIS A 230      27.558  45.155  95.859  1.00127.57           N  
ATOM   1777  CD2 HIS A 230      27.865  43.514  94.448  1.00126.48           C  
ATOM   1778  CE1 HIS A 230      26.820  44.140  96.273  1.00127.90           C  
ATOM   1779  NE2 HIS A 230      26.989  43.132  95.434  1.00127.64           N  
ATOM   1780  N   GLU A 231      31.714  44.413  95.391  1.00122.76           N  
ATOM   1781  CA  GLU A 231      32.290  43.370  96.222  1.00123.79           C  
ATOM   1782  C   GLU A 231      32.850  43.980  97.491  1.00124.33           C  
ATOM   1783  O   GLU A 231      32.548  43.519  98.593  1.00124.07           O  
ATOM   1784  CB  GLU A 231      33.403  42.641  95.461  1.00124.45           C  
ATOM   1785  CG  GLU A 231      33.913  41.369  96.133  1.00125.98           C  
ATOM   1786  CD  GLU A 231      35.145  40.781  95.443  1.00126.71           C  
ATOM   1787  OE1 GLU A 231      35.106  40.597  94.208  1.00125.75           O  
ATOM   1788  OE2 GLU A 231      36.147  40.495  96.140  1.00126.82           O  
ATOM   1789  N   LYS A 232      33.663  45.021  97.333  1.00125.70           N  
ATOM   1790  CA  LYS A 232      34.271  45.699  98.477  1.00127.70           C  
ATOM   1791  C   LYS A 232      33.179  46.380  99.275  1.00128.35           C  
ATOM   1792  O   LYS A 232      32.995  46.100 100.461  1.00128.46           O  
ATOM   1793  CB  LYS A 232      35.287  46.755  98.019  1.00128.87           C  
ATOM   1794  CG  LYS A 232      36.605  46.204  97.478  1.00129.21           C  
ATOM   1795  CD  LYS A 232      37.491  45.668  98.587  1.00129.92           C  
ATOM   1796  CE  LYS A 232      38.858  45.264  98.042  1.00131.16           C  
ATOM   1797  NZ  LYS A 232      39.806  44.840  99.120  1.00132.20           N  
ATOM   1798  N   GLU A 233      32.454  47.270  98.603  1.00128.64           N  
ATOM   1799  CA  GLU A 233      31.370  48.017  99.222  1.00129.38           C  
ATOM   1800  C   GLU A 233      30.462  47.167 100.114  1.00129.94           C  
ATOM   1801  O   GLU A 233      30.048  47.611 101.190  1.00129.30           O  
ATOM   1802  CB  GLU A 233      30.536  48.691  98.140  1.00129.38           C  
ATOM   1803  CG  GLU A 233      29.313  49.405  98.674  1.00130.68           C  
ATOM   1804  CD  GLU A 233      28.491  50.038  97.573  1.00131.49           C  
ATOM   1805  OE1 GLU A 233      28.107  49.317  96.620  1.00130.43           O  
ATOM   1806  OE2 GLU A 233      28.231  51.259  97.668  1.00132.85           O  
ATOM   1807  N   MET A 234      30.154  45.953  99.659  1.00131.36           N  
ATOM   1808  CA  MET A 234      29.286  45.043 100.408  1.00132.35           C  
ATOM   1809  C   MET A 234      29.871  44.788 101.789  1.00132.63           C  
ATOM   1810  O   MET A 234      29.146  44.752 102.788  1.00132.62           O  
ATOM   1811  CB  MET A 234      29.133  43.711  99.663  1.00132.82           C  
ATOM   1812  CG  MET A 234      27.686  43.204  99.545  1.00133.35           C  
ATOM   1813  SD  MET A 234      26.812  42.933 101.129  1.00134.17           S  
ATOM   1814  CE  MET A 234      25.644  44.282 101.122  1.00132.84           C  
ATOM   1815  N   ALA A 235      31.189  44.615 101.835  1.00132.94           N  
ATOM   1816  CA  ALA A 235      31.890  44.360 103.089  1.00133.76           C  
ATOM   1817  C   ALA A 235      31.927  45.581 104.020  1.00134.32           C  
ATOM   1818  O   ALA A 235      31.585  45.473 105.207  1.00134.38           O  
ATOM   1819  CB  ALA A 235      33.308  43.879 102.800  1.00132.94           C  
ATOM   1820  N   ALA A 236      32.337  46.734 103.481  1.00134.45           N  
ATOM   1821  CA  ALA A 236      32.434  47.987 104.257  1.00133.66           C  
ATOM   1822  C   ALA A 236      31.176  48.283 105.060  1.00132.85           C  
ATOM   1823  O   ALA A 236      31.254  48.711 106.205  1.00131.95           O  
ATOM   1824  CB  ALA A 236      32.741  49.167 103.332  1.00133.08           C  
ATOM   1825  N   MET A 237      30.021  48.061 104.447  1.00132.83           N  
ATOM   1826  CA  MET A 237      28.754  48.285 105.114  1.00132.76           C  
ATOM   1827  C   MET A 237      28.397  47.062 105.956  1.00133.25           C  
ATOM   1828  O   MET A 237      27.708  47.170 106.972  1.00133.35           O  
ATOM   1829  CB  MET A 237      27.653  48.548 104.082  1.00132.61           C  
ATOM   1830  CG  MET A 237      27.468  47.439 103.056  1.00132.86           C  
ATOM   1831  SD  MET A 237      26.015  47.691 102.008  1.00132.63           S  
ATOM   1832  CE  MET A 237      26.661  48.855 100.774  1.00133.40           C  
ATOM   1833  N   ALA A 238      28.878  45.898 105.530  1.00133.62           N  
ATOM   1834  CA  ALA A 238      28.606  44.650 106.233  1.00134.75           C  
ATOM   1835  C   ALA A 238      29.094  44.708 107.679  1.00135.71           C  
ATOM   1836  O   ALA A 238      28.317  44.497 108.621  1.00135.64           O  
ATOM   1837  CB  ALA A 238      29.266  43.479 105.496  1.00134.17           C  
ATOM   1838  N   LYS A 239      30.383  44.997 107.855  1.00135.99           N  
ATOM   1839  CA  LYS A 239      30.959  45.075 109.192  1.00135.72           C  
ATOM   1840  C   LYS A 239      30.599  46.415 109.822  1.00135.45           C  
ATOM   1841  O   LYS A 239      31.071  46.739 110.913  1.00135.28           O  
ATOM   1842  CB  LYS A 239      32.484  44.902 109.142  1.00135.04           C  
ATOM   1843  CG  LYS A 239      33.253  46.101 108.622  1.00133.11           C  
ATOM   1844  CD  LYS A 239      34.747  45.858 108.706  1.00131.59           C  
ATOM   1845  CE  LYS A 239      35.514  47.133 108.448  1.00130.84           C  
ATOM   1846  NZ  LYS A 239      35.144  47.727 107.141  1.00129.76           N  
ATOM   1847  N   ARG A 240      29.749  47.176 109.127  1.00135.01           N  
ATOM   1848  CA  ARG A 240      29.284  48.482 109.600  1.00134.69           C  
ATOM   1849  C   ARG A 240      28.086  48.242 110.522  1.00134.28           C  
ATOM   1850  O   ARG A 240      26.945  48.576 110.174  1.00134.04           O  
ATOM   1851  CB  ARG A 240      28.861  49.371 108.416  1.00134.66           C  
ATOM   1852  CG  ARG A 240      28.700  50.868 108.741  1.00133.86           C  
ATOM   1853  CD  ARG A 240      30.040  51.545 109.065  1.00133.84           C  
ATOM   1854  NE  ARG A 240      30.664  50.995 110.272  1.00134.28           N  
ATOM   1855  CZ  ARG A 240      31.887  51.300 110.706  1.00134.13           C  
ATOM   1856  NH1 ARG A 240      32.355  50.741 111.817  1.00132.77           N  
ATOM   1857  NH2 ARG A 240      32.644  52.159 110.030  1.00134.51           N  
ATOM   1858  N   LEU A 241      28.372  47.660 111.694  1.00133.20           N  
ATOM   1859  CA  LEU A 241      27.372  47.315 112.713  1.00131.03           C  
ATOM   1860  C   LEU A 241      26.026  46.960 112.084  1.00130.71           C  
ATOM   1861  O   LEU A 241      24.977  47.135 112.698  1.00131.46           O  
ATOM   1862  CB  LEU A 241      27.202  48.453 113.736  1.00128.50           C  
ATOM   1863  CG  LEU A 241      28.224  48.571 114.875  1.00126.85           C  
ATOM   1864  CD1 LEU A 241      29.577  48.970 114.338  1.00126.35           C  
ATOM   1865  CD2 LEU A 241      27.757  49.600 115.875  1.00126.18           C  
ATOM   1866  N   ASN A 242      26.071  46.447 110.857  1.00129.43           N  
ATOM   1867  CA  ASN A 242      24.866  46.063 110.132  1.00127.17           C  
ATOM   1868  C   ASN A 242      24.456  44.639 110.541  1.00124.69           C  
ATOM   1869  O   ASN A 242      25.017  43.659 110.038  1.00125.13           O  
ATOM   1870  CB  ASN A 242      25.137  46.121 108.624  1.00129.00           C  
ATOM   1871  CG  ASN A 242      23.862  46.249 107.809  1.00130.42           C  
ATOM   1872  OD1 ASN A 242      23.843  45.981 106.599  1.00129.87           O  
ATOM   1873  ND2 ASN A 242      22.784  46.671 108.470  1.00130.92           N  
ATOM   1874  N   ALA A 243      23.478  44.534 111.441  1.00120.96           N  
ATOM   1875  CA  ALA A 243      23.001  43.243 111.948  1.00118.70           C  
ATOM   1876  C   ALA A 243      22.683  42.185 110.880  1.00117.11           C  
ATOM   1877  O   ALA A 243      22.999  42.362 109.699  1.00116.19           O  
ATOM   1878  CB  ALA A 243      21.778  43.462 112.835  1.00118.42           C  
ATOM   1879  N   LYS A 244      22.084  41.072 111.315  1.00115.63           N  
ATOM   1880  CA  LYS A 244      21.691  39.979 110.419  1.00114.78           C  
ATOM   1881  C   LYS A 244      20.788  40.542 109.299  1.00115.71           C  
ATOM   1882  O   LYS A 244      20.482  39.861 108.308  1.00115.44           O  
ATOM   1883  CB  LYS A 244      20.941  38.901 111.209  1.00111.98           C  
ATOM   1884  CG  LYS A 244      21.754  38.242 112.314  1.00110.07           C  
ATOM   1885  CD  LYS A 244      20.908  37.225 113.100  1.00109.70           C  
ATOM   1886  CE  LYS A 244      21.720  36.412 114.132  1.00106.94           C  
ATOM   1887  NZ  LYS A 244      22.210  37.215 115.291  1.00104.64           N  
ATOM   1888  N   GLU A 245      20.370  41.797 109.483  1.00116.10           N  
ATOM   1889  CA  GLU A 245      19.522  42.542 108.540  1.00114.52           C  
ATOM   1890  C   GLU A 245      20.296  42.834 107.259  1.00113.18           C  
ATOM   1891  O   GLU A 245      19.768  43.429 106.318  1.00112.64           O  
ATOM   1892  CB  GLU A 245      19.073  43.861 109.196  1.00115.67           C  
ATOM   1893  CG  GLU A 245      20.179  44.574 110.020  1.00116.57           C  
ATOM   1894  CD  GLU A 245      19.656  45.676 110.958  1.00115.96           C  
ATOM   1895  OE1 GLU A 245      19.220  46.741 110.466  1.00115.42           O  
ATOM   1896  OE2 GLU A 245      19.687  45.476 112.194  1.00114.96           O  
ATOM   1897  N   LEU A 246      21.559  42.412 107.249  1.00111.56           N  
ATOM   1898  CA  LEU A 246      22.447  42.594 106.111  1.00109.25           C  
ATOM   1899  C   LEU A 246      22.062  41.565 105.056  1.00107.40           C  
ATOM   1900  O   LEU A 246      22.233  41.786 103.858  1.00107.27           O  
ATOM   1901  CB  LEU A 246      23.906  42.382 106.547  1.00109.31           C  
ATOM   1902  CG  LEU A 246      24.989  42.329 105.458  1.00110.09           C  
ATOM   1903  CD1 LEU A 246      25.045  43.668 104.729  1.00109.67           C  
ATOM   1904  CD2 LEU A 246      26.348  41.978 106.082  1.00108.77           C  
ATOM   1905  N   ARG A 247      21.540  40.435 105.516  1.00105.60           N  
ATOM   1906  CA  ARG A 247      21.131  39.365 104.625  1.00105.47           C  
ATOM   1907  C   ARG A 247      20.092  39.905 103.650  1.00105.06           C  
ATOM   1908  O   ARG A 247      20.138  39.625 102.444  1.00104.85           O  
ATOM   1909  CB  ARG A 247      20.532  38.217 105.434  1.00107.13           C  
ATOM   1910  CG  ARG A 247      21.509  37.518 106.380  1.00107.23           C  
ATOM   1911  CD  ARG A 247      20.743  36.624 107.346  1.00106.32           C  
ATOM   1912  NE  ARG A 247      19.753  35.820 106.634  1.00107.81           N  
ATOM   1913  CZ  ARG A 247      18.711  35.221 107.207  1.00108.57           C  
ATOM   1914  NH1 ARG A 247      17.860  34.511 106.465  1.00108.54           N  
ATOM   1915  NH2 ARG A 247      18.515  35.333 108.518  1.00107.24           N  
ATOM   1916  N   LYS A 248      19.146  40.674 104.184  1.00104.30           N  
ATOM   1917  CA  LYS A 248      18.099  41.284 103.364  1.00102.65           C  
ATOM   1918  C   LYS A 248      18.751  41.893 102.125  1.00100.32           C  
ATOM   1919  O   LYS A 248      18.546  41.422 101.007  1.00 98.25           O  
ATOM   1920  CB  LYS A 248      17.388  42.377 104.169  1.00104.73           C  
ATOM   1921  CG  LYS A 248      16.419  43.238 103.360  1.00106.23           C  
ATOM   1922  CD  LYS A 248      15.893  44.391 104.224  1.00107.82           C  
ATOM   1923  CE  LYS A 248      15.042  45.371 103.421  1.00107.08           C  
ATOM   1924  NZ  LYS A 248      13.717  44.799 103.061  1.00108.11           N  
ATOM   1925  N   ALA A 249      19.555  42.935 102.352  1.00 99.44           N  
ATOM   1926  CA  ALA A 249      20.274  43.640 101.280  1.00 97.15           C  
ATOM   1927  C   ALA A 249      20.913  42.677 100.304  1.00 94.65           C  
ATOM   1928  O   ALA A 249      20.825  42.870  99.099  1.00 93.46           O  
ATOM   1929  CB  ALA A 249      21.358  44.568 101.871  1.00 97.20           C  
ATOM   1930  N   GLN A 250      21.550  41.638 100.830  1.00 94.19           N  
ATOM   1931  CA  GLN A 250      22.217  40.668  99.978  1.00 94.21           C  
ATOM   1932  C   GLN A 250      21.237  39.964  99.054  1.00 91.34           C  
ATOM   1933  O   GLN A 250      21.494  39.842  97.859  1.00 91.96           O  
ATOM   1934  CB  GLN A 250      22.983  39.630 100.815  1.00 96.90           C  
ATOM   1935  CG  GLN A 250      24.068  38.877 100.028  1.00 98.39           C  
ATOM   1936  CD  GLN A 250      25.274  39.761  99.675  1.00100.75           C  
ATOM   1937  OE1 GLN A 250      25.140  40.803  99.019  1.00101.60           O  
ATOM   1938  NE2 GLN A 250      26.461  39.341 100.111  1.00103.11           N  
ATOM   1939  N   ALA A 251      20.113  39.510  99.592  1.00 87.76           N  
ATOM   1940  CA  ALA A 251      19.117  38.818  98.770  1.00 85.03           C  
ATOM   1941  C   ALA A 251      18.671  39.691  97.612  1.00 83.39           C  
ATOM   1942  O   ALA A 251      18.503  39.211  96.492  1.00 80.68           O  
ATOM   1943  CB  ALA A 251      17.913  38.449  99.608  1.00 85.37           C  
ATOM   1944  N   GLY A 252      18.473  40.976  97.910  1.00 83.67           N  
ATOM   1945  CA  GLY A 252      18.046  41.943  96.910  1.00 82.12           C  
ATOM   1946  C   GLY A 252      19.001  42.010  95.738  1.00 81.28           C  
ATOM   1947  O   GLY A 252      18.578  42.000  94.588  1.00 81.07           O  
ATOM   1948  N   ALA A 253      20.293  42.083  96.035  1.00 81.80           N  
ATOM   1949  CA  ALA A 253      21.326  42.128  95.006  1.00 81.52           C  
ATOM   1950  C   ALA A 253      21.316  40.826  94.182  1.00 81.90           C  
ATOM   1951  O   ALA A 253      21.526  40.846  92.965  1.00 82.28           O  
ATOM   1952  CB  ALA A 253      22.673  42.329  95.648  1.00 81.53           C  
ATOM   1953  N   ASN A 254      21.086  39.693  94.842  1.00 81.56           N  
ATOM   1954  CA  ASN A 254      21.006  38.414  94.132  1.00 81.69           C  
ATOM   1955  C   ASN A 254      19.817  38.459  93.158  1.00 81.69           C  
ATOM   1956  O   ASN A 254      19.938  38.147  91.959  1.00 80.89           O  
ATOM   1957  CB  ASN A 254      20.779  37.255  95.118  1.00 81.89           C  
ATOM   1958  CG  ASN A 254      22.043  36.821  95.797  1.00 80.01           C  
ATOM   1959  OD1 ASN A 254      22.591  37.546  96.613  1.00 83.22           O  
ATOM   1960  ND2 ASN A 254      22.523  35.638  95.456  1.00 76.40           N  
ATOM   1961  N   ALA A 255      18.667  38.845  93.709  1.00 80.91           N  
ATOM   1962  CA  ALA A 255      17.430  38.940  92.952  1.00 80.43           C  
ATOM   1963  C   ALA A 255      17.592  39.826  91.710  1.00 79.30           C  
ATOM   1964  O   ALA A 255      17.194  39.439  90.607  1.00 79.64           O  
ATOM   1965  CB  ALA A 255      16.326  39.475  93.858  1.00 81.20           C  
ATOM   1966  N   GLU A 256      18.178  41.005  91.899  1.00 78.12           N  
ATOM   1967  CA  GLU A 256      18.406  41.940  90.799  1.00 77.32           C  
ATOM   1968  C   GLU A 256      19.417  41.350  89.823  1.00 75.60           C  
ATOM   1969  O   GLU A 256      19.241  41.420  88.598  1.00 73.54           O  
ATOM   1970  CB  GLU A 256      18.945  43.279  91.327  1.00 79.29           C  
ATOM   1971  CG  GLU A 256      18.023  43.972  92.295  1.00 83.92           C  
ATOM   1972  CD  GLU A 256      16.714  44.361  91.641  1.00 88.36           C  
ATOM   1973  OE1 GLU A 256      15.724  44.593  92.369  1.00 92.13           O  
ATOM   1974  OE2 GLU A 256      16.668  44.442  90.394  1.00 90.41           O  
ATOM   1975  N   MET A 257      20.477  40.769  90.379  1.00 75.00           N  
ATOM   1976  CA  MET A 257      21.527  40.173  89.571  1.00 75.36           C  
ATOM   1977  C   MET A 257      20.917  39.142  88.631  1.00 74.48           C  
ATOM   1978  O   MET A 257      21.216  39.141  87.429  1.00 74.39           O  
ATOM   1979  CB  MET A 257      22.583  39.515  90.470  1.00 76.56           C  
ATOM   1980  CG  MET A 257      23.785  38.927  89.714  1.00 78.97           C  
ATOM   1981  SD  MET A 257      24.721  40.168  88.759  1.00 82.75           S  
ATOM   1982  CE  MET A 257      24.628  39.470  87.082  1.00 78.91           C  
ATOM   1983  N   ARG A 258      20.053  38.281  89.178  1.00 73.30           N  
ATOM   1984  CA  ARG A 258      19.405  37.245  88.374  1.00 72.25           C  
ATOM   1985  C   ARG A 258      18.662  37.860  87.181  1.00 71.24           C  
ATOM   1986  O   ARG A 258      18.738  37.372  86.048  1.00 70.25           O  
ATOM   1987  CB  ARG A 258      18.422  36.430  89.213  1.00 71.94           C  
ATOM   1988  CG  ARG A 258      18.027  35.161  88.489  1.00 73.51           C  
ATOM   1989  CD  ARG A 258      16.978  34.374  89.246  1.00 76.77           C  
ATOM   1990  NE  ARG A 258      16.626  33.134  88.545  1.00 75.92           N  
ATOM   1991  CZ  ARG A 258      17.260  31.980  88.706  1.00 75.05           C  
ATOM   1992  NH1 ARG A 258      16.860  30.924  88.014  1.00 75.30           N  
ATOM   1993  NH2 ARG A 258      18.270  31.881  89.570  1.00 73.86           N  
ATOM   1994  N   LEU A 259      17.942  38.943  87.443  1.00 71.60           N  
ATOM   1995  CA  LEU A 259      17.194  39.615  86.398  1.00 71.60           C  
ATOM   1996  C   LEU A 259      18.158  40.158  85.361  1.00 71.26           C  
ATOM   1997  O   LEU A 259      17.903  40.046  84.146  1.00 73.06           O  
ATOM   1998  CB  LEU A 259      16.327  40.749  86.988  1.00 72.24           C  
ATOM   1999  CG  LEU A 259      14.914  40.423  87.552  1.00 72.25           C  
ATOM   2000  CD1 LEU A 259      14.090  39.658  86.485  1.00 74.82           C  
ATOM   2001  CD2 LEU A 259      14.991  39.581  88.823  1.00 69.34           C  
ATOM   2002  N   ALA A 260      19.267  40.735  85.832  1.00 68.57           N  
ATOM   2003  CA  ALA A 260      20.277  41.287  84.920  1.00 64.33           C  
ATOM   2004  C   ALA A 260      20.789  40.160  84.020  1.00 60.29           C  
ATOM   2005  O   ALA A 260      20.902  40.335  82.804  1.00 60.53           O  
ATOM   2006  CB  ALA A 260      21.420  41.898  85.708  1.00 65.08           C  
ATOM   2007  N   LYS A 261      21.082  39.010  84.618  1.00 55.11           N  
ATOM   2008  CA  LYS A 261      21.541  37.880  83.840  1.00 51.93           C  
ATOM   2009  C   LYS A 261      20.487  37.574  82.776  1.00 51.14           C  
ATOM   2010  O   LYS A 261      20.795  37.481  81.594  1.00 54.76           O  
ATOM   2011  CB  LYS A 261      21.748  36.656  84.721  1.00 51.69           C  
ATOM   2012  CG  LYS A 261      23.014  36.641  85.529  1.00 50.87           C  
ATOM   2013  CD  LYS A 261      22.943  35.493  86.537  1.00 54.85           C  
ATOM   2014  CE  LYS A 261      24.290  35.258  87.245  1.00 59.28           C  
ATOM   2015  NZ  LYS A 261      24.849  36.480  87.936  1.00 59.46           N  
ATOM   2016  N   ILE A 262      19.238  37.412  83.182  1.00 49.47           N  
ATOM   2017  CA  ILE A 262      18.174  37.140  82.209  1.00 47.35           C  
ATOM   2018  C   ILE A 262      18.332  38.096  81.003  1.00 46.76           C  
ATOM   2019  O   ILE A 262      18.451  37.658  79.847  1.00 44.61           O  
ATOM   2020  CB  ILE A 262      16.732  37.343  82.849  1.00 45.09           C  
ATOM   2021  CG1 ILE A 262      16.553  36.408  84.037  1.00 45.58           C  
ATOM   2022  CG2 ILE A 262      15.634  37.048  81.832  1.00 38.08           C  
ATOM   2023  CD1 ILE A 262      15.249  36.592  84.781  1.00 43.12           C  
ATOM   2024  N   SER A 263      18.355  39.397  81.302  1.00 47.14           N  
ATOM   2025  CA  SER A 263      18.438  40.442  80.290  1.00 49.39           C  
ATOM   2026  C   SER A 263      19.452  40.119  79.245  1.00 51.28           C  
ATOM   2027  O   SER A 263      19.212  40.303  78.051  1.00 55.04           O  
ATOM   2028  CB  SER A 263      18.821  41.780  80.908  1.00 47.71           C  
ATOM   2029  OG  SER A 263      17.892  42.183  81.868  1.00 53.53           O  
ATOM   2030  N   ILE A 264      20.612  39.671  79.706  1.00 53.20           N  
ATOM   2031  CA  ILE A 264      21.721  39.333  78.827  1.00 52.29           C  
ATOM   2032  C   ILE A 264      21.381  38.129  77.956  1.00 53.78           C  
ATOM   2033  O   ILE A 264      21.677  38.140  76.755  1.00 54.96           O  
ATOM   2034  CB  ILE A 264      22.999  39.088  79.652  1.00 50.22           C  
ATOM   2035  CG1 ILE A 264      23.726  40.397  79.804  1.00 47.30           C  
ATOM   2036  CG2 ILE A 264      23.875  38.040  79.011  1.00 52.31           C  
ATOM   2037  CD1 ILE A 264      24.874  40.284  80.706  1.00 54.24           C  
ATOM   2038  N   VAL A 265      20.752  37.100  78.528  1.00 52.87           N  
ATOM   2039  CA  VAL A 265      20.413  35.961  77.697  1.00 53.06           C  
ATOM   2040  C   VAL A 265      19.471  36.362  76.547  1.00 55.20           C  
ATOM   2041  O   VAL A 265      19.727  36.017  75.376  1.00 56.61           O  
ATOM   2042  CB  VAL A 265      19.794  34.833  78.507  1.00 50.71           C  
ATOM   2043  CG1 VAL A 265      19.460  33.644  77.584  1.00 44.76           C  
ATOM   2044  CG2 VAL A 265      20.780  34.427  79.588  1.00 49.79           C  
ATOM   2045  N   ILE A 266      18.407  37.120  76.843  1.00 55.32           N  
ATOM   2046  CA  ILE A 266      17.473  37.525  75.772  1.00 53.04           C  
ATOM   2047  C   ILE A 266      18.159  38.407  74.733  1.00 51.46           C  
ATOM   2048  O   ILE A 266      17.814  38.381  73.543  1.00 50.78           O  
ATOM   2049  CB  ILE A 266      16.210  38.247  76.332  1.00 52.41           C  
ATOM   2050  CG1 ILE A 266      16.597  39.548  77.020  1.00 53.76           C  
ATOM   2051  CG2 ILE A 266      15.475  37.322  77.315  1.00 52.32           C  
ATOM   2052  CD1 ILE A 266      15.430  40.266  77.671  1.00 55.59           C  
ATOM   2053  N   VAL A 267      19.150  39.165  75.188  1.00 50.49           N  
ATOM   2054  CA  VAL A 267      19.901  40.017  74.296  1.00 49.44           C  
ATOM   2055  C   VAL A 267      20.745  39.087  73.439  1.00 51.19           C  
ATOM   2056  O   VAL A 267      20.841  39.251  72.217  1.00 54.00           O  
ATOM   2057  CB  VAL A 267      20.835  40.968  75.058  1.00 46.65           C  
ATOM   2058  CG1 VAL A 267      21.815  41.593  74.087  1.00 47.47           C  
ATOM   2059  CG2 VAL A 267      20.040  42.058  75.747  1.00 45.75           C  
ATOM   2060  N   SER A 268      21.351  38.094  74.081  1.00 51.24           N  
ATOM   2061  CA  SER A 268      22.209  37.158  73.364  1.00 52.30           C  
ATOM   2062  C   SER A 268      21.402  36.449  72.303  1.00 53.87           C  
ATOM   2063  O   SER A 268      21.861  36.189  71.172  1.00 57.41           O  
ATOM   2064  CB  SER A 268      22.759  36.135  74.325  1.00 49.88           C  
ATOM   2065  OG  SER A 268      23.222  36.806  75.480  1.00 52.47           O  
ATOM   2066  N   GLN A 269      20.179  36.158  72.686  1.00 51.80           N  
ATOM   2067  CA  GLN A 269      19.242  35.456  71.821  1.00 48.17           C  
ATOM   2068  C   GLN A 269      18.973  36.294  70.569  1.00 46.71           C  
ATOM   2069  O   GLN A 269      19.054  35.804  69.433  1.00 44.94           O  
ATOM   2070  CB  GLN A 269      17.946  35.185  72.595  1.00 47.71           C  
ATOM   2071  CG  GLN A 269      16.821  34.625  71.763  1.00 51.38           C  
ATOM   2072  CD  GLN A 269      15.983  35.709  71.125  1.00 52.49           C  
ATOM   2073  OE1 GLN A 269      15.214  36.393  71.795  1.00 45.29           O  
ATOM   2074  NE2 GLN A 269      16.131  35.873  69.824  1.00 55.87           N  
ATOM   2075  N   PHE A 270      18.714  37.576  70.812  1.00 45.93           N  
ATOM   2076  CA  PHE A 270      18.431  38.504  69.738  1.00 46.03           C  
ATOM   2077  C   PHE A 270      19.565  38.550  68.782  1.00 44.69           C  
ATOM   2078  O   PHE A 270      19.372  38.311  67.609  1.00 45.68           O  
ATOM   2079  CB  PHE A 270      18.206  39.907  70.264  1.00 48.52           C  
ATOM   2080  CG  PHE A 270      17.798  40.883  69.203  1.00 49.58           C  
ATOM   2081  CD1 PHE A 270      18.735  41.516  68.424  1.00 48.38           C  
ATOM   2082  CD2 PHE A 270      16.446  41.124  68.948  1.00 53.93           C  
ATOM   2083  CE1 PHE A 270      18.330  42.377  67.399  1.00 50.81           C  
ATOM   2084  CE2 PHE A 270      16.034  41.984  67.918  1.00 53.81           C  
ATOM   2085  CZ  PHE A 270      16.976  42.609  67.146  1.00 51.49           C  
ATOM   2086  N   LEU A 271      20.746  38.878  69.290  1.00 44.57           N  
ATOM   2087  CA  LEU A 271      21.948  38.952  68.473  1.00 45.28           C  
ATOM   2088  C   LEU A 271      22.196  37.657  67.679  1.00 47.67           C  
ATOM   2089  O   LEU A 271      22.301  37.684  66.447  1.00 48.80           O  
ATOM   2090  CB  LEU A 271      23.129  39.260  69.371  1.00 42.76           C  
ATOM   2091  CG  LEU A 271      22.958  40.585  70.097  1.00 41.56           C  
ATOM   2092  CD1 LEU A 271      24.157  40.869  70.928  1.00 42.20           C  
ATOM   2093  CD2 LEU A 271      22.794  41.687  69.087  1.00 44.71           C  
ATOM   2094  N   LEU A 272      22.285  36.525  68.372  1.00 48.06           N  
ATOM   2095  CA  LEU A 272      22.488  35.255  67.686  1.00 48.94           C  
ATOM   2096  C   LEU A 272      21.421  35.020  66.613  1.00 49.03           C  
ATOM   2097  O   LEU A 272      21.687  34.386  65.597  1.00 51.99           O  
ATOM   2098  CB  LEU A 272      22.457  34.093  68.682  1.00 49.92           C  
ATOM   2099  CG  LEU A 272      23.628  34.011  69.655  1.00 50.20           C  
ATOM   2100  CD1 LEU A 272      23.299  33.080  70.798  1.00 52.60           C  
ATOM   2101  CD2 LEU A 272      24.841  33.535  68.899  1.00 51.35           C  
ATOM   2102  N   SER A 273      20.207  35.519  66.831  1.00 49.12           N  
ATOM   2103  CA  SER A 273      19.124  35.317  65.860  1.00 47.45           C  
ATOM   2104  C   SER A 273      19.205  36.213  64.603  1.00 49.01           C  
ATOM   2105  O   SER A 273      18.980  35.747  63.473  1.00 47.26           O  
ATOM   2106  CB  SER A 273      17.759  35.543  66.538  1.00 44.26           C  
ATOM   2107  OG  SER A 273      17.524  34.604  67.540  1.00 38.95           O  
ATOM   2108  N   TRP A 274      19.522  37.494  64.804  1.00 49.61           N  
ATOM   2109  CA  TRP A 274      19.566  38.431  63.701  1.00 51.42           C  
ATOM   2110  C   TRP A 274      20.902  38.579  62.969  1.00 53.07           C  
ATOM   2111  O   TRP A 274      20.930  38.723  61.723  1.00 53.66           O  
ATOM   2112  CB  TRP A 274      19.113  39.821  64.164  1.00 52.94           C  
ATOM   2113  CG  TRP A 274      17.634  39.938  64.445  1.00 54.90           C  
ATOM   2114  CD1 TRP A 274      16.998  39.708  65.639  1.00 54.47           C  
ATOM   2115  CD2 TRP A 274      16.606  40.281  63.504  1.00 55.09           C  
ATOM   2116  NE1 TRP A 274      15.646  39.889  65.495  1.00 54.60           N  
ATOM   2117  CE2 TRP A 274      15.375  40.234  64.196  1.00 55.15           C  
ATOM   2118  CE3 TRP A 274      16.605  40.623  62.141  1.00 54.77           C  
ATOM   2119  CZ2 TRP A 274      14.151  40.511  63.568  1.00 54.46           C  
ATOM   2120  CZ3 TRP A 274      15.394  40.902  61.518  1.00 51.04           C  
ATOM   2121  CH2 TRP A 274      14.184  40.842  62.233  1.00 53.30           C  
ATOM   2122  N   SER A 275      22.005  38.543  63.718  1.00 52.11           N  
ATOM   2123  CA  SER A 275      23.322  38.746  63.112  1.00 51.02           C  
ATOM   2124  C   SER A 275      23.564  37.950  61.824  1.00 50.36           C  
ATOM   2125  O   SER A 275      24.123  38.477  60.840  1.00 50.90           O  
ATOM   2126  CB  SER A 275      24.427  38.495  64.146  1.00 51.77           C  
ATOM   2127  OG  SER A 275      24.412  39.520  65.163  1.00 48.46           O  
ATOM   2128  N   PRO A 276      23.129  36.686  61.786  1.00 48.07           N  
ATOM   2129  CA  PRO A 276      23.356  35.920  60.543  1.00 48.92           C  
ATOM   2130  C   PRO A 276      22.747  36.631  59.318  1.00 47.91           C  
ATOM   2131  O   PRO A 276      23.450  37.019  58.358  1.00 46.57           O  
ATOM   2132  CB  PRO A 276      22.679  34.577  60.833  1.00 47.87           C  
ATOM   2133  CG  PRO A 276      22.905  34.416  62.316  1.00 47.57           C  
ATOM   2134  CD  PRO A 276      22.634  35.822  62.865  1.00 47.59           C  
ATOM   2135  N   TYR A 277      21.425  36.795  59.375  1.00 46.55           N  
ATOM   2136  CA  TYR A 277      20.668  37.478  58.320  1.00 43.73           C  
ATOM   2137  C   TYR A 277      21.305  38.835  58.013  1.00 43.64           C  
ATOM   2138  O   TYR A 277      21.493  39.183  56.835  1.00 42.94           O  
ATOM   2139  CB  TYR A 277      19.221  37.712  58.766  1.00 38.38           C  
ATOM   2140  CG  TYR A 277      18.340  38.339  57.707  1.00 30.31           C  
ATOM   2141  CD1 TYR A 277      17.859  39.630  57.867  1.00 24.70           C  
ATOM   2142  CD2 TYR A 277      17.968  37.614  56.567  1.00 26.50           C  
ATOM   2143  CE1 TYR A 277      17.031  40.173  56.926  1.00 28.01           C  
ATOM   2144  CE2 TYR A 277      17.146  38.145  55.614  1.00 23.93           C  
ATOM   2145  CZ  TYR A 277      16.676  39.414  55.782  1.00 28.21           C  
ATOM   2146  OH  TYR A 277      15.874  39.933  54.785  1.00 29.80           O  
ATOM   2147  N   ALA A 278      21.614  39.588  59.075  1.00 40.67           N  
ATOM   2148  CA  ALA A 278      22.221  40.893  58.918  1.00 39.82           C  
ATOM   2149  C   ALA A 278      23.412  40.740  58.019  1.00 42.45           C  
ATOM   2150  O   ALA A 278      23.583  41.513  57.063  1.00 45.40           O  
ATOM   2151  CB  ALA A 278      22.663  41.449  60.256  1.00 35.32           C  
ATOM   2152  N   VAL A 279      24.234  39.724  58.316  1.00 42.98           N  
ATOM   2153  CA  VAL A 279      25.447  39.479  57.544  1.00 41.57           C  
ATOM   2154  C   VAL A 279      25.126  39.212  56.070  1.00 42.57           C  
ATOM   2155  O   VAL A 279      25.639  39.907  55.182  1.00 40.00           O  
ATOM   2156  CB  VAL A 279      26.269  38.345  58.200  1.00 38.93           C  
ATOM   2157  CG1 VAL A 279      27.328  37.839  57.260  1.00 42.19           C  
ATOM   2158  CG2 VAL A 279      26.939  38.874  59.436  1.00 34.08           C  
ATOM   2159  N   VAL A 280      24.251  38.240  55.815  1.00 44.95           N  
ATOM   2160  CA  VAL A 280      23.855  37.917  54.447  1.00 48.16           C  
ATOM   2161  C   VAL A 280      23.372  39.149  53.695  1.00 49.96           C  
ATOM   2162  O   VAL A 280      23.621  39.287  52.494  1.00 54.48           O  
ATOM   2163  CB  VAL A 280      22.731  36.864  54.405  1.00 48.14           C  
ATOM   2164  CG1 VAL A 280      22.338  36.551  52.947  1.00 42.29           C  
ATOM   2165  CG2 VAL A 280      23.197  35.601  55.125  1.00 49.06           C  
ATOM   2166  N   ALA A 281      22.673  40.038  54.388  1.00 50.80           N  
ATOM   2167  CA  ALA A 281      22.186  41.268  53.766  1.00 51.08           C  
ATOM   2168  C   ALA A 281      23.366  42.128  53.305  1.00 52.31           C  
ATOM   2169  O   ALA A 281      23.398  42.565  52.149  1.00 51.93           O  
ATOM   2170  CB  ALA A 281      21.328  42.056  54.750  1.00 49.08           C  
ATOM   2171  N   LEU A 282      24.328  42.363  54.212  1.00 53.56           N  
ATOM   2172  CA  LEU A 282      25.532  43.171  53.925  1.00 51.69           C  
ATOM   2173  C   LEU A 282      26.355  42.626  52.745  1.00 51.59           C  
ATOM   2174  O   LEU A 282      26.901  43.413  51.976  1.00 51.32           O  
ATOM   2175  CB  LEU A 282      26.406  43.269  55.182  1.00 48.66           C  
ATOM   2176  CG  LEU A 282      25.909  44.265  56.212  1.00 44.51           C  
ATOM   2177  CD1 LEU A 282      26.789  44.226  57.390  1.00 43.07           C  
ATOM   2178  CD2 LEU A 282      25.896  45.642  55.620  1.00 42.37           C  
ATOM   2179  N   LEU A 283      26.441  41.296  52.618  1.00 50.31           N  
ATOM   2180  CA  LEU A 283      27.146  40.673  51.515  1.00 51.10           C  
ATOM   2181  C   LEU A 283      26.460  41.102  50.229  1.00 52.68           C  
ATOM   2182  O   LEU A 283      27.109  41.518  49.267  1.00 54.22           O  
ATOM   2183  CB  LEU A 283      27.087  39.157  51.631  1.00 49.94           C  
ATOM   2184  CG  LEU A 283      28.173  38.496  52.475  1.00 51.18           C  
ATOM   2185  CD1 LEU A 283      28.334  39.181  53.815  1.00 51.05           C  
ATOM   2186  CD2 LEU A 283      27.807  37.039  52.647  1.00 50.14           C  
ATOM   2187  N   ALA A 284      25.138  41.012  50.221  1.00 53.25           N  
ATOM   2188  CA  ALA A 284      24.354  41.398  49.046  1.00 54.79           C  
ATOM   2189  C   ALA A 284      24.495  42.885  48.656  1.00 53.90           C  
ATOM   2190  O   ALA A 284      24.414  43.250  47.484  1.00 52.19           O  
ATOM   2191  CB  ALA A 284      22.870  41.057  49.279  1.00 55.07           C  
ATOM   2192  N   GLN A 285      24.711  43.734  49.640  1.00 54.85           N  
ATOM   2193  CA  GLN A 285      24.827  45.154  49.397  1.00 58.30           C  
ATOM   2194  C   GLN A 285      26.267  45.624  49.233  1.00 61.16           C  
ATOM   2195  O   GLN A 285      26.505  46.721  48.705  1.00 62.77           O  
ATOM   2196  CB  GLN A 285      24.175  45.910  50.558  1.00 59.39           C  
ATOM   2197  CG  GLN A 285      24.405  47.415  50.583  1.00 61.56           C  
ATOM   2198  CD  GLN A 285      23.643  48.120  49.502  1.00 61.84           C  
ATOM   2199  OE1 GLN A 285      23.692  49.348  49.396  1.00 62.57           O  
ATOM   2200  NE2 GLN A 285      22.920  47.349  48.688  1.00 65.14           N  
ATOM   2201  N   PHE A 286      27.221  44.811  49.701  1.00 61.70           N  
ATOM   2202  CA  PHE A 286      28.649  45.156  49.634  1.00 61.41           C  
ATOM   2203  C   PHE A 286      29.583  44.063  49.110  1.00 62.16           C  
ATOM   2204  O   PHE A 286      30.710  44.367  48.694  1.00 66.63           O  
ATOM   2205  CB  PHE A 286      29.146  45.606  51.008  1.00 55.65           C  
ATOM   2206  CG  PHE A 286      28.520  46.864  51.481  1.00 54.43           C  
ATOM   2207  CD1 PHE A 286      27.941  46.925  52.719  1.00 55.02           C  
ATOM   2208  CD2 PHE A 286      28.555  48.021  50.706  1.00 56.59           C  
ATOM   2209  CE1 PHE A 286      27.404  48.136  53.205  1.00 57.86           C  
ATOM   2210  CE2 PHE A 286      28.015  49.245  51.181  1.00 57.57           C  
ATOM   2211  CZ  PHE A 286      27.445  49.301  52.430  1.00 56.33           C  
ATOM   2212  N   GLY A 287      29.124  42.815  49.101  1.00 59.98           N  
ATOM   2213  CA  GLY A 287      29.989  41.743  48.651  1.00 60.08           C  
ATOM   2214  C   GLY A 287      29.517  40.968  47.447  1.00 59.53           C  
ATOM   2215  O   GLY A 287      28.872  41.518  46.553  1.00 61.30           O  
ATOM   2216  N   PRO A 288      29.858  39.677  47.387  1.00 58.96           N  
ATOM   2217  CA  PRO A 288      29.470  38.789  46.280  1.00 59.81           C  
ATOM   2218  C   PRO A 288      27.964  38.484  46.247  1.00 59.90           C  
ATOM   2219  O   PRO A 288      27.507  37.518  46.869  1.00 61.56           O  
ATOM   2220  CB  PRO A 288      30.296  37.529  46.540  1.00 59.22           C  
ATOM   2221  CG  PRO A 288      31.494  38.048  47.318  1.00 60.82           C  
ATOM   2222  CD  PRO A 288      30.881  39.051  48.245  1.00 58.64           C  
ATOM   2223  N   LEU A 289      27.193  39.287  45.515  1.00 58.15           N  
ATOM   2224  CA  LEU A 289      25.766  39.046  45.450  1.00 58.01           C  
ATOM   2225  C   LEU A 289      25.537  37.597  45.063  1.00 59.74           C  
ATOM   2226  O   LEU A 289      24.488  37.025  45.368  1.00 60.33           O  
ATOM   2227  CB  LEU A 289      25.106  39.948  44.413  1.00 56.63           C  
ATOM   2228  CG  LEU A 289      23.599  39.753  44.202  1.00 53.88           C  
ATOM   2229  CD1 LEU A 289      22.883  40.198  45.452  1.00 55.49           C  
ATOM   2230  CD2 LEU A 289      23.114  40.562  43.021  1.00 52.07           C  
ATOM   2231  N   GLU A 290      26.533  37.000  44.409  1.00 62.13           N  
ATOM   2232  CA  GLU A 290      26.407  35.613  43.956  1.00 64.00           C  
ATOM   2233  C   GLU A 290      26.339  34.627  45.098  1.00 60.84           C  
ATOM   2234  O   GLU A 290      26.137  33.434  44.881  1.00 59.33           O  
ATOM   2235  CB  GLU A 290      27.524  35.211  42.926  1.00 68.67           C  
ATOM   2236  CG  GLU A 290      29.037  35.392  43.313  1.00 74.83           C  
ATOM   2237  CD  GLU A 290      29.638  36.765  42.924  1.00 77.74           C  
ATOM   2238  OE1 GLU A 290      30.835  37.033  43.241  1.00 76.29           O  
ATOM   2239  OE2 GLU A 290      28.908  37.580  42.300  1.00 80.80           O  
ATOM   2240  N   TRP A 291      26.487  35.130  46.314  1.00 58.85           N  
ATOM   2241  CA  TRP A 291      26.408  34.264  47.467  1.00 58.66           C  
ATOM   2242  C   TRP A 291      24.977  34.245  47.938  1.00 57.02           C  
ATOM   2243  O   TRP A 291      24.384  33.181  48.158  1.00 56.90           O  
ATOM   2244  CB  TRP A 291      27.279  34.772  48.599  1.00 62.57           C  
ATOM   2245  CG  TRP A 291      28.741  34.604  48.385  1.00 68.02           C  
ATOM   2246  CD1 TRP A 291      29.367  33.945  47.353  1.00 69.65           C  
ATOM   2247  CD2 TRP A 291      29.779  35.162  49.195  1.00 69.88           C  
ATOM   2248  NE1 TRP A 291      30.735  34.070  47.469  1.00 71.95           N  
ATOM   2249  CE2 TRP A 291      31.013  34.816  48.589  1.00 72.48           C  
ATOM   2250  CE3 TRP A 291      29.789  35.928  50.366  1.00 67.99           C  
ATOM   2251  CZ2 TRP A 291      32.243  35.220  49.124  1.00 73.67           C  
ATOM   2252  CZ3 TRP A 291      31.003  36.325  50.890  1.00 69.85           C  
ATOM   2253  CH2 TRP A 291      32.215  35.975  50.271  1.00 71.39           C  
ATOM   2254  N   VAL A 292      24.415  35.434  48.081  1.00 53.50           N  
ATOM   2255  CA  VAL A 292      23.060  35.531  48.547  1.00 49.39           C  
ATOM   2256  C   VAL A 292      22.094  34.735  47.675  1.00 49.55           C  
ATOM   2257  O   VAL A 292      21.428  35.292  46.827  1.00 50.03           O  
ATOM   2258  CB  VAL A 292      22.642  36.987  48.614  1.00 45.71           C  
ATOM   2259  CG1 VAL A 292      21.527  37.125  49.586  1.00 43.89           C  
ATOM   2260  CG2 VAL A 292      23.820  37.848  49.016  1.00 42.52           C  
ATOM   2261  N   THR A 293      22.032  33.423  47.864  1.00 49.97           N  
ATOM   2262  CA  THR A 293      21.110  32.570  47.098  1.00 53.82           C  
ATOM   2263  C   THR A 293      19.714  32.490  47.779  1.00 55.44           C  
ATOM   2264  O   THR A 293      19.504  33.036  48.892  1.00 58.20           O  
ATOM   2265  CB  THR A 293      21.647  31.128  47.002  1.00 55.01           C  
ATOM   2266  OG1 THR A 293      21.699  30.528  48.314  1.00 53.61           O  
ATOM   2267  CG2 THR A 293      23.027  31.129  46.396  1.00 56.93           C  
ATOM   2268  N   PRO A 294      18.746  31.808  47.138  1.00 52.52           N  
ATOM   2269  CA  PRO A 294      17.414  31.688  47.728  1.00 51.84           C  
ATOM   2270  C   PRO A 294      17.447  31.232  49.180  1.00 52.76           C  
ATOM   2271  O   PRO A 294      16.750  31.805  50.037  1.00 51.32           O  
ATOM   2272  CB  PRO A 294      16.759  30.676  46.826  1.00 53.02           C  
ATOM   2273  CG  PRO A 294      17.288  31.099  45.493  1.00 53.64           C  
ATOM   2274  CD  PRO A 294      18.761  31.250  45.781  1.00 51.76           C  
ATOM   2275  N   TYR A 295      18.253  30.189  49.439  1.00 53.88           N  
ATOM   2276  CA  TYR A 295      18.428  29.621  50.793  1.00 53.98           C  
ATOM   2277  C   TYR A 295      19.397  30.495  51.608  1.00 54.34           C  
ATOM   2278  O   TYR A 295      19.245  30.623  52.829  1.00 56.02           O  
ATOM   2279  CB  TYR A 295      18.992  28.178  50.760  1.00 52.78           C  
ATOM   2280  CG  TYR A 295      18.105  27.117  50.113  1.00 51.98           C  
ATOM   2281  CD1 TYR A 295      18.620  26.263  49.135  1.00 52.26           C  
ATOM   2282  CD2 TYR A 295      16.755  26.976  50.458  1.00 51.37           C  
ATOM   2283  CE1 TYR A 295      17.829  25.316  48.512  1.00 48.89           C  
ATOM   2284  CE2 TYR A 295      15.951  26.019  49.834  1.00 48.14           C  
ATOM   2285  CZ  TYR A 295      16.502  25.207  48.864  1.00 48.03           C  
ATOM   2286  OH  TYR A 295      15.723  24.311  48.197  1.00 48.86           O  
ATOM   2287  N   ALA A 296      20.394  31.087  50.950  1.00 52.39           N  
ATOM   2288  CA  ALA A 296      21.352  31.940  51.654  1.00 50.35           C  
ATOM   2289  C   ALA A 296      20.649  33.066  52.406  1.00 50.13           C  
ATOM   2290  O   ALA A 296      21.094  33.519  53.482  1.00 48.26           O  
ATOM   2291  CB  ALA A 296      22.327  32.516  50.674  1.00 52.97           C  
ATOM   2292  N   ALA A 297      19.549  33.533  51.815  1.00 48.86           N  
ATOM   2293  CA  ALA A 297      18.753  34.583  52.414  1.00 46.46           C  
ATOM   2294  C   ALA A 297      17.612  33.948  53.254  1.00 47.21           C  
ATOM   2295  O   ALA A 297      17.509  34.164  54.480  1.00 48.55           O  
ATOM   2296  CB  ALA A 297      18.202  35.469  51.320  1.00 41.03           C  
ATOM   2297  N   GLN A 298      16.794  33.114  52.613  1.00 46.61           N  
ATOM   2298  CA  GLN A 298      15.666  32.501  53.303  1.00 46.94           C  
ATOM   2299  C   GLN A 298      15.959  31.858  54.688  1.00 48.56           C  
ATOM   2300  O   GLN A 298      15.481  32.351  55.730  1.00 50.13           O  
ATOM   2301  CB  GLN A 298      14.981  31.490  52.382  1.00 45.17           C  
ATOM   2302  CG  GLN A 298      13.500  31.325  52.710  1.00 46.53           C  
ATOM   2303  CD  GLN A 298      12.728  32.615  52.525  1.00 46.59           C  
ATOM   2304  OE1 GLN A 298      12.552  33.046  51.397  1.00 51.03           O  
ATOM   2305  NE2 GLN A 298      12.279  33.243  53.622  1.00 41.12           N  
ATOM   2306  N   LEU A 299      16.731  30.772  54.717  1.00 49.19           N  
ATOM   2307  CA  LEU A 299      17.020  30.102  55.987  1.00 48.95           C  
ATOM   2308  C   LEU A 299      17.491  31.022  57.111  1.00 50.23           C  
ATOM   2309  O   LEU A 299      17.080  30.863  58.250  1.00 52.72           O  
ATOM   2310  CB  LEU A 299      18.022  28.951  55.799  1.00 46.72           C  
ATOM   2311  CG  LEU A 299      17.420  27.578  55.456  1.00 44.07           C  
ATOM   2312  CD1 LEU A 299      16.528  27.648  54.194  1.00 44.58           C  
ATOM   2313  CD2 LEU A 299      18.535  26.613  55.249  1.00 42.76           C  
ATOM   2314  N   PRO A 300      18.352  32.000  56.819  1.00 50.25           N  
ATOM   2315  CA  PRO A 300      18.806  32.887  57.906  1.00 48.74           C  
ATOM   2316  C   PRO A 300      17.760  33.883  58.313  1.00 48.11           C  
ATOM   2317  O   PRO A 300      17.842  34.392  59.430  1.00 47.99           O  
ATOM   2318  CB  PRO A 300      20.017  33.586  57.327  1.00 50.07           C  
ATOM   2319  CG  PRO A 300      20.534  32.580  56.373  1.00 53.53           C  
ATOM   2320  CD  PRO A 300      19.270  32.069  55.686  1.00 51.76           C  
ATOM   2321  N   VAL A 301      16.804  34.198  57.415  1.00 47.72           N  
ATOM   2322  CA  VAL A 301      15.705  35.130  57.777  1.00 47.08           C  
ATOM   2323  C   VAL A 301      14.679  34.417  58.703  1.00 46.90           C  
ATOM   2324  O   VAL A 301      14.149  35.045  59.641  1.00 47.37           O  
ATOM   2325  CB  VAL A 301      14.931  35.716  56.562  1.00 44.99           C  
ATOM   2326  CG1 VAL A 301      13.958  34.709  56.003  1.00 48.56           C  
ATOM   2327  CG2 VAL A 301      14.187  36.968  57.013  1.00 42.40           C  
ATOM   2328  N   MET A 302      14.416  33.127  58.449  1.00 42.41           N  
ATOM   2329  CA  MET A 302      13.522  32.372  59.315  1.00 45.03           C  
ATOM   2330  C   MET A 302      14.111  32.349  60.754  1.00 46.74           C  
ATOM   2331  O   MET A 302      13.426  32.609  61.749  1.00 47.61           O  
ATOM   2332  CB  MET A 302      13.353  30.936  58.805  1.00 46.13           C  
ATOM   2333  CG  MET A 302      12.965  30.832  57.348  1.00 47.28           C  
ATOM   2334  SD  MET A 302      11.583  31.853  56.966  1.00 47.84           S  
ATOM   2335  CE  MET A 302      10.201  30.665  56.990  1.00 41.94           C  
ATOM   2336  N   PHE A 303      15.395  32.043  60.861  1.00 48.17           N  
ATOM   2337  CA  PHE A 303      16.042  32.009  62.149  1.00 46.96           C  
ATOM   2338  C   PHE A 303      15.830  33.370  62.805  1.00 46.37           C  
ATOM   2339  O   PHE A 303      15.558  33.453  63.997  1.00 46.21           O  
ATOM   2340  CB  PHE A 303      17.525  31.721  61.963  1.00 47.62           C  
ATOM   2341  CG  PHE A 303      18.244  31.359  63.245  1.00 52.26           C  
ATOM   2342  CD1 PHE A 303      18.001  30.147  63.884  1.00 50.39           C  
ATOM   2343  CD2 PHE A 303      19.172  32.247  63.827  1.00 53.15           C  
ATOM   2344  CE1 PHE A 303      18.666  29.832  65.077  1.00 48.31           C  
ATOM   2345  CE2 PHE A 303      19.837  31.927  65.020  1.00 48.73           C  
ATOM   2346  CZ  PHE A 303      19.584  30.724  65.645  1.00 45.50           C  
ATOM   2347  N   ALA A 304      15.946  34.440  62.029  1.00 46.54           N  
ATOM   2348  CA  ALA A 304      15.759  35.779  62.584  1.00 48.15           C  
ATOM   2349  C   ALA A 304      14.322  35.982  63.058  1.00 48.02           C  
ATOM   2350  O   ALA A 304      14.086  36.454  64.180  1.00 47.67           O  
ATOM   2351  CB  ALA A 304      16.126  36.859  61.545  1.00 45.70           C  
ATOM   2352  N   LYS A 305      13.364  35.603  62.208  1.00 46.91           N  
ATOM   2353  CA  LYS A 305      11.932  35.780  62.522  1.00 44.28           C  
ATOM   2354  C   LYS A 305      11.486  35.100  63.790  1.00 42.32           C  
ATOM   2355  O   LYS A 305      10.682  35.632  64.530  1.00 42.83           O  
ATOM   2356  CB  LYS A 305      11.043  35.315  61.346  1.00 42.92           C  
ATOM   2357  CG  LYS A 305      11.141  36.192  60.078  1.00 40.43           C  
ATOM   2358  CD  LYS A 305      10.065  35.826  59.111  1.00 34.27           C  
ATOM   2359  CE  LYS A 305      10.263  36.512  57.793  1.00 34.41           C  
ATOM   2360  NZ  LYS A 305      10.007  37.928  57.917  1.00 31.09           N  
ATOM   2361  N   ALA A 306      12.008  33.917  64.033  1.00 41.82           N  
ATOM   2362  CA  ALA A 306      11.655  33.188  65.223  1.00 43.50           C  
ATOM   2363  C   ALA A 306      12.201  33.879  66.497  1.00 47.38           C  
ATOM   2364  O   ALA A 306      11.741  33.600  67.617  1.00 49.43           O  
ATOM   2365  CB  ALA A 306      12.179  31.776  65.116  1.00 42.58           C  
ATOM   2366  N   SER A 307      13.194  34.764  66.359  1.00 50.61           N  
ATOM   2367  CA  SER A 307      13.723  35.466  67.530  1.00 51.41           C  
ATOM   2368  C   SER A 307      12.617  35.993  68.420  1.00 52.50           C  
ATOM   2369  O   SER A 307      12.705  35.909  69.626  1.00 52.73           O  
ATOM   2370  CB  SER A 307      14.624  36.644  67.121  1.00 52.59           C  
ATOM   2371  OG  SER A 307      15.115  37.354  68.263  1.00 47.71           O  
ATOM   2372  N   ALA A 308      11.569  36.550  67.804  1.00 53.16           N  
ATOM   2373  CA  ALA A 308      10.465  37.119  68.595  1.00 53.34           C  
ATOM   2374  C   ALA A 308       9.639  36.131  69.408  1.00 51.79           C  
ATOM   2375  O   ALA A 308       8.677  36.547  70.033  1.00 52.45           O  
ATOM   2376  CB  ALA A 308       9.539  37.919  67.703  1.00 54.02           C  
ATOM   2377  N   ILE A 309      10.005  34.849  69.405  1.00 48.75           N  
ATOM   2378  CA  ILE A 309       9.259  33.861  70.170  1.00 46.19           C  
ATOM   2379  C   ILE A 309      10.097  33.271  71.283  1.00 46.86           C  
ATOM   2380  O   ILE A 309       9.698  32.278  71.867  1.00 50.94           O  
ATOM   2381  CB  ILE A 309       8.811  32.657  69.313  1.00 42.38           C  
ATOM   2382  CG1 ILE A 309      10.004  31.723  69.094  1.00 39.23           C  
ATOM   2383  CG2 ILE A 309       8.220  33.139  68.008  1.00 41.88           C  
ATOM   2384  CD1 ILE A 309       9.649  30.368  68.624  1.00 37.23           C  
ATOM   2385  N   HIS A 310      11.236  33.859  71.613  1.00 46.61           N  
ATOM   2386  CA  HIS A 310      12.063  33.209  72.623  1.00 45.18           C  
ATOM   2387  C   HIS A 310      11.968  33.746  74.023  1.00 46.18           C  
ATOM   2388  O   HIS A 310      11.871  32.986  74.973  1.00 44.99           O  
ATOM   2389  CB  HIS A 310      13.526  33.195  72.165  1.00 45.79           C  
ATOM   2390  CG  HIS A 310      13.789  32.282  70.998  1.00 49.32           C  
ATOM   2391  ND1 HIS A 310      14.515  32.669  69.878  1.00 48.20           N  
ATOM   2392  CD2 HIS A 310      13.375  31.008  70.750  1.00 51.48           C  
ATOM   2393  CE1 HIS A 310      14.531  31.682  68.994  1.00 47.32           C  
ATOM   2394  NE2 HIS A 310      13.846  30.663  69.497  1.00 51.70           N  
ATOM   2395  N   ASN A 311      11.967  35.054  74.171  1.00 48.79           N  
ATOM   2396  CA  ASN A 311      11.935  35.597  75.514  1.00 54.18           C  
ATOM   2397  C   ASN A 311      10.952  34.906  76.442  1.00 56.47           C  
ATOM   2398  O   ASN A 311      11.344  34.454  77.509  1.00 58.75           O  
ATOM   2399  CB  ASN A 311      11.660  37.106  75.488  1.00 58.30           C  
ATOM   2400  CG  ASN A 311      12.655  37.861  74.617  1.00 58.98           C  
ATOM   2401  OD1 ASN A 311      13.647  37.276  74.171  1.00 63.09           O  
ATOM   2402  ND2 ASN A 311      12.401  39.160  74.371  1.00 57.53           N  
ATOM   2403  N   PRO A 312       9.664  34.823  76.065  1.00 57.88           N  
ATOM   2404  CA  PRO A 312       8.689  34.164  76.936  1.00 59.23           C  
ATOM   2405  C   PRO A 312       9.164  32.783  77.453  1.00 60.16           C  
ATOM   2406  O   PRO A 312       9.023  32.434  78.657  1.00 59.24           O  
ATOM   2407  CB  PRO A 312       7.456  34.072  76.041  1.00 61.24           C  
ATOM   2408  CG  PRO A 312       7.546  35.343  75.256  1.00 59.83           C  
ATOM   2409  CD  PRO A 312       9.004  35.309  74.842  1.00 60.12           C  
ATOM   2410  N   MET A 313       9.738  31.981  76.560  1.00 60.56           N  
ATOM   2411  CA  MET A 313      10.241  30.668  77.008  1.00 60.22           C  
ATOM   2412  C   MET A 313      11.459  30.826  77.968  1.00 57.42           C  
ATOM   2413  O   MET A 313      11.595  30.066  78.934  1.00 56.60           O  
ATOM   2414  CB  MET A 313      10.593  29.786  75.784  1.00 60.96           C  
ATOM   2415  CG  MET A 313       9.418  29.580  74.797  1.00 61.69           C  
ATOM   2416  SD  MET A 313       9.617  28.251  73.516  1.00 60.87           S  
ATOM   2417  CE  MET A 313      10.539  29.173  72.176  1.00 61.05           C  
ATOM   2418  N   ILE A 314      12.315  31.823  77.703  1.00 53.46           N  
ATOM   2419  CA  ILE A 314      13.476  32.091  78.544  1.00 48.66           C  
ATOM   2420  C   ILE A 314      12.988  32.483  79.928  1.00 48.34           C  
ATOM   2421  O   ILE A 314      13.487  31.992  80.931  1.00 47.50           O  
ATOM   2422  CB  ILE A 314      14.322  33.237  77.984  1.00 46.72           C  
ATOM   2423  CG1 ILE A 314      14.848  32.885  76.603  1.00 48.37           C  
ATOM   2424  CG2 ILE A 314      15.492  33.494  78.866  1.00 45.00           C  
ATOM   2425  CD1 ILE A 314      15.608  34.032  75.938  1.00 47.38           C  
ATOM   2426  N   TYR A 315      12.001  33.366  79.973  1.00 49.50           N  
ATOM   2427  CA  TYR A 315      11.432  33.818  81.235  1.00 52.46           C  
ATOM   2428  C   TYR A 315      10.855  32.637  82.029  1.00 54.26           C  
ATOM   2429  O   TYR A 315      11.060  32.540  83.251  1.00 55.65           O  
ATOM   2430  CB  TYR A 315      10.285  34.818  81.018  1.00 53.77           C  
ATOM   2431  CG  TYR A 315      10.613  36.122  80.299  1.00 56.44           C  
ATOM   2432  CD1 TYR A 315       9.722  36.661  79.354  1.00 57.78           C  
ATOM   2433  CD2 TYR A 315      11.754  36.850  80.602  1.00 57.16           C  
ATOM   2434  CE1 TYR A 315       9.961  37.876  78.742  1.00 57.14           C  
ATOM   2435  CE2 TYR A 315      11.995  38.079  79.994  1.00 57.85           C  
ATOM   2436  CZ  TYR A 315      11.091  38.580  79.065  1.00 56.96           C  
ATOM   2437  OH  TYR A 315      11.302  39.790  78.458  1.00 53.93           O  
ATOM   2438  N   SER A 316      10.138  31.739  81.344  1.00 53.14           N  
ATOM   2439  CA  SER A 316       9.483  30.605  82.015  1.00 49.87           C  
ATOM   2440  C   SER A 316      10.386  29.611  82.680  1.00 49.12           C  
ATOM   2441  O   SER A 316       9.923  28.811  83.468  1.00 49.92           O  
ATOM   2442  CB  SER A 316       8.578  29.859  81.049  1.00 47.72           C  
ATOM   2443  OG  SER A 316       9.355  29.197  80.094  1.00 45.39           O  
ATOM   2444  N   VAL A 317      11.671  29.645  82.358  1.00 49.77           N  
ATOM   2445  CA  VAL A 317      12.614  28.722  82.975  1.00 50.65           C  
ATOM   2446  C   VAL A 317      13.631  29.424  83.914  1.00 54.48           C  
ATOM   2447  O   VAL A 317      14.432  28.754  84.582  1.00 56.49           O  
ATOM   2448  CB  VAL A 317      13.409  27.941  81.919  1.00 46.72           C  
ATOM   2449  CG1 VAL A 317      12.483  27.170  81.040  1.00 47.27           C  
ATOM   2450  CG2 VAL A 317      14.244  28.883  81.111  1.00 46.59           C  
ATOM   2451  N   SER A 318      13.588  30.759  83.999  1.00 55.70           N  
ATOM   2452  CA  SER A 318      14.546  31.506  84.834  1.00 54.90           C  
ATOM   2453  C   SER A 318      14.002  32.708  85.616  1.00 54.50           C  
ATOM   2454  O   SER A 318      14.730  33.309  86.409  1.00 53.25           O  
ATOM   2455  CB  SER A 318      15.684  32.021  83.952  1.00 57.74           C  
ATOM   2456  OG  SER A 318      15.240  33.132  83.193  1.00 54.77           O  
ATOM   2457  N   HIS A 319      12.745  33.075  85.374  1.00 53.64           N  
ATOM   2458  CA  HIS A 319      12.126  34.222  86.050  1.00 51.74           C  
ATOM   2459  C   HIS A 319      11.203  33.756  87.161  1.00 50.81           C  
ATOM   2460  O   HIS A 319      10.043  33.450  86.914  1.00 51.58           O  
ATOM   2461  CB  HIS A 319      11.309  35.061  85.056  1.00 50.13           C  
ATOM   2462  CG  HIS A 319      11.035  36.457  85.533  1.00 48.60           C  
ATOM   2463  ND1 HIS A 319      10.367  36.725  86.708  1.00 50.09           N  
ATOM   2464  CD2 HIS A 319      11.372  37.660  85.011  1.00 46.74           C  
ATOM   2465  CE1 HIS A 319      10.304  38.033  86.887  1.00 48.61           C  
ATOM   2466  NE2 HIS A 319      10.906  38.620  85.870  1.00 46.45           N  
ATOM   2467  N   PRO A 320      11.692  33.745  88.406  1.00 51.17           N  
ATOM   2468  CA  PRO A 320      10.924  33.308  89.585  1.00 51.37           C  
ATOM   2469  C   PRO A 320       9.516  33.881  89.740  1.00 51.52           C  
ATOM   2470  O   PRO A 320       8.535  33.128  89.715  1.00 50.14           O  
ATOM   2471  CB  PRO A 320      11.840  33.672  90.751  1.00 53.11           C  
ATOM   2472  CG  PRO A 320      12.554  34.900  90.227  1.00 54.14           C  
ATOM   2473  CD  PRO A 320      12.903  34.474  88.813  1.00 51.92           C  
ATOM   2474  N   LYS A 321       9.400  35.201  89.892  1.00 53.03           N  
ATOM   2475  CA  LYS A 321       8.083  35.793  90.069  1.00 54.00           C  
ATOM   2476  C   LYS A 321       7.182  35.387  88.932  1.00 52.97           C  
ATOM   2477  O   LYS A 321       6.063  34.918  89.141  1.00 54.03           O  
ATOM   2478  CB  LYS A 321       8.174  37.314  90.185  1.00 56.27           C  
ATOM   2479  CG  LYS A 321       8.486  37.791  91.620  1.00 58.78           C  
ATOM   2480  CD  LYS A 321       8.551  39.309  91.691  1.00 61.81           C  
ATOM   2481  CE  LYS A 321       8.880  39.815  93.102  1.00 66.93           C  
ATOM   2482  NZ  LYS A 321       8.924  41.329  93.199  1.00 68.48           N  
ATOM   2483  N   PHE A 322       7.685  35.537  87.725  1.00 52.12           N  
ATOM   2484  CA  PHE A 322       6.922  35.148  86.553  1.00 51.27           C  
ATOM   2485  C   PHE A 322       6.553  33.679  86.595  1.00 51.33           C  
ATOM   2486  O   PHE A 322       5.438  33.320  86.247  1.00 53.67           O  
ATOM   2487  CB  PHE A 322       7.737  35.404  85.288  1.00 51.40           C  
ATOM   2488  CG  PHE A 322       6.995  35.089  83.987  1.00 49.47           C  
ATOM   2489  CD1 PHE A 322       5.751  35.681  83.701  1.00 46.20           C  
ATOM   2490  CD2 PHE A 322       7.554  34.226  83.038  1.00 47.24           C  
ATOM   2491  CE1 PHE A 322       5.094  35.416  82.515  1.00 41.11           C  
ATOM   2492  CE2 PHE A 322       6.892  33.962  81.849  1.00 43.37           C  
ATOM   2493  CZ  PHE A 322       5.662  34.555  81.588  1.00 43.51           C  
ATOM   2494  N   ARG A 323       7.489  32.821  86.973  1.00 51.61           N  
ATOM   2495  CA  ARG A 323       7.200  31.393  87.036  1.00 53.65           C  
ATOM   2496  C   ARG A 323       6.149  31.132  88.108  1.00 54.50           C  
ATOM   2497  O   ARG A 323       5.349  30.188  87.996  1.00 54.30           O  
ATOM   2498  CB  ARG A 323       8.466  30.602  87.373  1.00 55.49           C  
ATOM   2499  CG  ARG A 323       9.360  30.315  86.193  1.00 56.89           C  
ATOM   2500  CD  ARG A 323      10.717  29.845  86.667  1.00 55.98           C  
ATOM   2501  NE  ARG A 323      10.631  28.648  87.484  1.00 55.29           N  
ATOM   2502  CZ  ARG A 323      10.327  27.443  87.016  1.00 57.51           C  
ATOM   2503  NH1 ARG A 323      10.068  27.249  85.715  1.00 55.12           N  
ATOM   2504  NH2 ARG A 323      10.295  26.423  87.868  1.00 60.96           N  
ATOM   2505  N   GLU A 324       6.166  31.957  89.158  1.00 54.06           N  
ATOM   2506  CA  GLU A 324       5.202  31.816  90.244  1.00 54.96           C  
ATOM   2507  C   GLU A 324       3.824  32.008  89.612  1.00 53.88           C  
ATOM   2508  O   GLU A 324       3.001  31.082  89.578  1.00 53.64           O  
ATOM   2509  CB  GLU A 324       5.444  32.894  91.269  1.00 58.90           C  
ATOM   2510  CG  GLU A 324       5.050  32.528  92.667  1.00 66.41           C  
ATOM   2511  CD  GLU A 324       5.118  33.739  93.579  1.00 73.00           C  
ATOM   2512  OE1 GLU A 324       5.168  33.553  94.824  1.00 76.91           O  
ATOM   2513  OE2 GLU A 324       5.115  34.889  93.042  1.00 76.13           O  
ATOM   2514  N   ALA A 325       3.608  33.219  89.083  1.00 50.57           N  
ATOM   2515  CA  ALA A 325       2.379  33.595  88.395  1.00 45.68           C  
ATOM   2516  C   ALA A 325       1.859  32.516  87.437  1.00 43.86           C  
ATOM   2517  O   ALA A 325       0.690  32.206  87.474  1.00 45.39           O  
ATOM   2518  CB  ALA A 325       2.606  34.886  87.646  1.00 43.59           C  
ATOM   2519  N   ILE A 326       2.707  31.964  86.575  1.00 42.66           N  
ATOM   2520  CA  ILE A 326       2.277  30.918  85.647  1.00 43.47           C  
ATOM   2521  C   ILE A 326       1.695  29.685  86.378  1.00 49.09           C  
ATOM   2522  O   ILE A 326       0.652  29.149  85.987  1.00 47.71           O  
ATOM   2523  CB  ILE A 326       3.443  30.431  84.753  1.00 37.56           C  
ATOM   2524  CG1 ILE A 326       3.978  31.575  83.919  1.00 31.86           C  
ATOM   2525  CG2 ILE A 326       2.979  29.277  83.872  1.00 32.48           C  
ATOM   2526  CD1 ILE A 326       4.932  31.121  82.842  1.00 32.87           C  
ATOM   2527  N   SER A 327       2.384  29.237  87.433  1.00 55.11           N  
ATOM   2528  CA  SER A 327       1.953  28.076  88.226  1.00 59.80           C  
ATOM   2529  C   SER A 327       0.545  28.311  88.808  1.00 62.15           C  
ATOM   2530  O   SER A 327      -0.263  27.367  88.953  1.00 63.03           O  
ATOM   2531  CB  SER A 327       2.958  27.816  89.369  1.00 61.25           C  
ATOM   2532  OG  SER A 327       2.980  28.865  90.338  1.00 60.39           O  
ATOM   2533  N   GLN A 328       0.278  29.583  89.129  1.00 62.82           N  
ATOM   2534  CA  GLN A 328      -0.996  30.028  89.679  1.00 64.16           C  
ATOM   2535  C   GLN A 328      -2.090  30.346  88.623  1.00 66.24           C  
ATOM   2536  O   GLN A 328      -3.253  30.502  89.011  1.00 70.81           O  
ATOM   2537  CB  GLN A 328      -0.794  31.282  90.534  1.00 64.27           C  
ATOM   2538  CG  GLN A 328      -0.175  31.060  91.885  1.00 66.75           C  
ATOM   2539  CD  GLN A 328       0.515  32.315  92.374  1.00 69.93           C  
ATOM   2540  OE1 GLN A 328       0.697  32.512  93.579  1.00 74.90           O  
ATOM   2541  NE2 GLN A 328       0.929  33.171  91.434  1.00 71.59           N  
ATOM   2542  N   THR A 329      -1.756  30.419  87.316  1.00 65.36           N  
ATOM   2543  CA  THR A 329      -2.735  30.771  86.263  1.00 61.80           C  
ATOM   2544  C   THR A 329      -2.872  29.881  84.996  1.00 62.54           C  
ATOM   2545  O   THR A 329      -3.991  29.616  84.573  1.00 63.70           O  
ATOM   2546  CB  THR A 329      -2.535  32.272  85.824  1.00 60.63           C  
ATOM   2547  OG1 THR A 329      -1.149  32.521  85.577  1.00 57.31           O  
ATOM   2548  CG2 THR A 329      -3.003  33.245  86.925  1.00 57.44           C  
ATOM   2549  N   PHE A 330      -1.756  29.462  84.382  1.00 63.38           N  
ATOM   2550  CA  PHE A 330      -1.715  28.555  83.176  1.00 64.43           C  
ATOM   2551  C   PHE A 330      -0.612  27.482  83.448  1.00 65.11           C  
ATOM   2552  O   PHE A 330       0.139  27.046  82.540  1.00 65.44           O  
ATOM   2553  CB  PHE A 330      -1.304  29.317  81.923  1.00 60.38           C  
ATOM   2554  CG  PHE A 330      -2.269  30.350  81.511  1.00 56.25           C  
ATOM   2555  CD1 PHE A 330      -3.495  29.995  81.028  1.00 56.24           C  
ATOM   2556  CD2 PHE A 330      -1.955  31.686  81.612  1.00 55.96           C  
ATOM   2557  CE1 PHE A 330      -4.402  30.956  80.653  1.00 55.05           C  
ATOM   2558  CE2 PHE A 330      -2.851  32.652  81.240  1.00 55.13           C  
ATOM   2559  CZ  PHE A 330      -4.079  32.284  80.760  1.00 55.27           C  
ATOM   2560  N   PRO A 331      -0.558  27.005  84.713  1.00 66.26           N  
ATOM   2561  CA  PRO A 331       0.380  26.019  85.310  1.00 66.92           C  
ATOM   2562  C   PRO A 331       0.700  24.764  84.470  1.00 66.29           C  
ATOM   2563  O   PRO A 331       1.653  24.015  84.792  1.00 66.10           O  
ATOM   2564  CB  PRO A 331      -0.281  25.729  86.706  1.00 66.79           C  
ATOM   2565  CG  PRO A 331      -1.793  25.729  86.330  1.00 62.01           C  
ATOM   2566  CD  PRO A 331      -1.896  26.936  85.389  1.00 63.48           C  
ATOM   2567  N   TRP A 332      -0.088  24.556  83.410  1.00 71.38           N  
ATOM   2568  CA  TRP A 332       0.144  23.417  82.555  1.00 76.28           C  
ATOM   2569  C   TRP A 332       1.491  23.599  81.873  1.00 77.04           C  
ATOM   2570  O   TRP A 332       2.223  22.625  81.704  1.00 78.89           O  
ATOM   2571  CB  TRP A 332      -0.957  23.240  81.505  1.00 79.63           C  
ATOM   2572  CG  TRP A 332      -0.874  24.161  80.380  1.00 83.76           C  
ATOM   2573  CD1 TRP A 332      -1.598  25.300  80.211  1.00 86.92           C  
ATOM   2574  CD2 TRP A 332      -0.032  24.033  79.216  1.00 86.35           C  
ATOM   2575  NE1 TRP A 332      -1.270  25.900  79.001  1.00 91.37           N  
ATOM   2576  CE2 TRP A 332      -0.311  25.142  78.371  1.00 88.91           C  
ATOM   2577  CE3 TRP A 332       0.925  23.094  78.804  1.00 85.14           C  
ATOM   2578  CZ2 TRP A 332       0.336  25.335  77.131  1.00 87.12           C  
ATOM   2579  CZ3 TRP A 332       1.569  23.283  77.569  1.00 84.64           C  
ATOM   2580  CH2 TRP A 332       1.267  24.398  76.751  1.00 85.69           C  
ATOM   2581  N   VAL A 333       1.821  24.850  81.519  1.00 79.04           N  
ATOM   2582  CA  VAL A 333       3.091  25.206  80.842  1.00 76.21           C  
ATOM   2583  C   VAL A 333       4.341  24.845  81.650  1.00 77.38           C  
ATOM   2584  O   VAL A 333       5.380  24.498  81.084  1.00 75.20           O  
ATOM   2585  CB  VAL A 333       3.188  26.721  80.536  1.00 75.81           C  
ATOM   2586  CG1 VAL A 333       4.448  26.991  79.758  1.00 75.00           C  
ATOM   2587  CG2 VAL A 333       1.971  27.197  79.755  1.00 74.55           C  
ATOM   2588  N   LEU A 334       4.219  24.956  82.973  1.00 77.90           N  
ATOM   2589  CA  LEU A 334       5.285  24.636  83.910  1.00 77.56           C  
ATOM   2590  C   LEU A 334       5.426  23.129  84.159  1.00 79.75           C  
ATOM   2591  O   LEU A 334       6.097  22.726  85.100  1.00 81.33           O  
ATOM   2592  CB  LEU A 334       5.040  25.337  85.246  1.00 73.86           C  
ATOM   2593  CG  LEU A 334       5.285  26.827  85.245  1.00 70.87           C  
ATOM   2594  CD1 LEU A 334       5.358  27.270  86.676  1.00 70.37           C  
ATOM   2595  CD2 LEU A 334       6.569  27.162  84.538  1.00 68.82           C  
ATOM   2596  N   THR A 335       4.787  22.286  83.350  1.00 82.04           N  
ATOM   2597  CA  THR A 335       4.928  20.842  83.559  1.00 83.66           C  
ATOM   2598  C   THR A 335       6.407  20.460  83.610  1.00 85.02           C  
ATOM   2599  O   THR A 335       6.947  20.207  84.684  1.00 87.23           O  
ATOM   2600  CB  THR A 335       4.283  20.016  82.445  1.00 81.94           C  
ATOM   2601  OG1 THR A 335       4.819  20.418  81.177  1.00 83.28           O  
ATOM   2602  CG2 THR A 335       2.796  20.191  82.470  1.00 80.34           C  
ATOM   2603  N   CYS A 336       7.070  20.435  82.458  1.00 85.36           N  
ATOM   2604  CA  CYS A 336       8.478  20.062  82.429  1.00 86.42           C  
ATOM   2605  C   CYS A 336       9.381  21.024  83.208  1.00 86.91           C  
ATOM   2606  O   CYS A 336      10.567  20.736  83.403  1.00 88.19           O  
ATOM   2607  CB  CYS A 336       8.979  19.987  80.990  1.00 86.00           C  
ATOM   2608  SG  CYS A 336       7.948  19.039  79.894  1.00 87.53           S  
ATOM   2609  N   CYS A 337       8.836  22.158  83.644  1.00 85.65           N  
ATOM   2610  CA  CYS A 337       9.630  23.145  84.373  1.00 85.26           C  
ATOM   2611  C   CYS A 337       8.970  23.386  85.715  1.00 85.01           C  
ATOM   2612  O   CYS A 337       8.782  24.542  86.080  1.00 86.94           O  
ATOM   2613  CB  CYS A 337       9.660  24.485  83.608  1.00 85.27           C  
ATOM   2614  SG  CYS A 337       9.474  24.414  81.786  1.00 87.31           S  
ATOM   2615  N   GLN A 338       8.640  22.322  86.453  1.00 82.88           N  
ATOM   2616  CA  GLN A 338       7.911  22.443  87.731  1.00 81.54           C  
ATOM   2617  C   GLN A 338       8.253  23.626  88.655  1.00 80.56           C  
ATOM   2618  O   GLN A 338       9.414  23.929  88.881  1.00 82.09           O  
ATOM   2619  CB  GLN A 338       8.007  21.118  88.506  1.00 82.38           C  
ATOM   2620  CG  GLN A 338       6.643  20.582  88.964  1.00 84.33           C  
ATOM   2621  CD  GLN A 338       5.641  20.484  87.809  1.00 83.70           C  
ATOM   2622  OE1 GLN A 338       5.488  19.432  87.191  1.00 81.77           O  
ATOM   2623  NE2 GLN A 338       4.968  21.593  87.510  1.00 83.55           N  
ATOM   2624  N   PHE A 339       7.254  24.307  89.201  1.00 78.26           N  
ATOM   2625  CA  PHE A 339       7.567  25.433  90.084  1.00 77.24           C  
ATOM   2626  C   PHE A 339       7.782  24.952  91.532  1.00 79.95           C  
ATOM   2627  O   PHE A 339       7.539  23.775  91.822  1.00 80.58           O  
ATOM   2628  CB  PHE A 339       6.428  26.450  90.028  1.00 73.27           C  
ATOM   2629  CG  PHE A 339       6.627  27.653  90.916  1.00 68.56           C  
ATOM   2630  CD1 PHE A 339       7.768  28.441  90.808  1.00 65.40           C  
ATOM   2631  CD2 PHE A 339       5.635  28.027  91.827  1.00 66.43           C  
ATOM   2632  CE1 PHE A 339       7.908  29.582  91.590  1.00 62.60           C  
ATOM   2633  CE2 PHE A 339       5.773  29.165  92.608  1.00 63.78           C  
ATOM   2634  CZ  PHE A 339       6.906  29.942  92.490  1.00 62.57           C  
ATOM   2635  N   ASP A 340       8.275  25.846  92.409  1.00 81.81           N  
ATOM   2636  CA  ASP A 340       8.502  25.603  93.868  1.00 82.63           C  
ATOM   2637  C   ASP A 340       8.662  26.916  94.633  1.00 84.49           C  
ATOM   2638  O   ASP A 340       9.162  27.908  94.101  1.00 86.24           O  
ATOM   2639  CB  ASP A 340       9.752  24.779  94.185  1.00 82.10           C  
ATOM   2640  CG  ASP A 340      10.080  24.784  95.693  1.00 81.65           C  
ATOM   2641  OD1 ASP A 340       9.276  24.245  96.478  1.00 81.60           O  
ATOM   2642  OD2 ASP A 340      11.126  25.335  96.104  1.00 81.37           O  
ATOM   2643  N   ASP A 341       8.294  26.911  95.903  1.00 85.76           N  
ATOM   2644  CA  ASP A 341       8.361  28.124  96.704  1.00 88.13           C  
ATOM   2645  C   ASP A 341       9.773  28.683  96.841  1.00 89.11           C  
ATOM   2646  O   ASP A 341       9.982  29.905  96.782  1.00 89.39           O  
ATOM   2647  CB  ASP A 341       7.781  27.855  98.086  1.00 90.77           C  
ATOM   2648  CG  ASP A 341       6.487  27.074  98.021  1.00 94.08           C  
ATOM   2649  OD1 ASP A 341       5.981  26.644  99.094  1.00 97.85           O  
ATOM   2650  OD2 ASP A 341       5.975  26.885  96.893  1.00 94.46           O  
ATOM   2651  N   LYS A 342      10.743  27.787  97.018  1.00 89.68           N  
ATOM   2652  CA  LYS A 342      12.132  28.206  97.194  1.00 89.45           C  
ATOM   2653  C   LYS A 342      12.648  29.171  96.104  1.00 88.96           C  
ATOM   2654  O   LYS A 342      13.609  29.911  96.332  1.00 89.21           O  
ATOM   2655  CB  LYS A 342      13.053  26.967  97.313  1.00 88.27           C  
ATOM   2656  CG  LYS A 342      13.099  26.336  98.698  1.00 84.40           C  
ATOM   2657  CD  LYS A 342      14.225  25.314  98.780  1.00 85.91           C  
ATOM   2658  CE  LYS A 342      14.593  24.933 100.236  1.00 85.02           C  
ATOM   2659  NZ  LYS A 342      13.492  24.235 101.007  1.00 83.43           N  
ATOM   2660  N   GLU A 343      12.003  29.189  94.941  1.00 88.05           N  
ATOM   2661  CA  GLU A 343      12.456  30.063  93.860  1.00 88.12           C  
ATOM   2662  C   GLU A 343      12.175  31.536  94.156  1.00 89.04           C  
ATOM   2663  O   GLU A 343      12.789  32.432  93.565  1.00 91.01           O  
ATOM   2664  CB  GLU A 343      11.791  29.690  92.532  1.00 86.09           C  
ATOM   2665  CG  GLU A 343      11.801  28.198  92.203  1.00 85.35           C  
ATOM   2666  CD  GLU A 343      11.127  27.887  90.861  1.00 86.01           C  
ATOM   2667  OE1 GLU A 343      10.904  26.690  90.547  1.00 83.91           O  
ATOM   2668  OE2 GLU A 343      10.822  28.848  90.114  1.00 86.45           O  
ATOM   2669  N   THR A 344      11.265  31.792  95.083  1.00 89.00           N  
ATOM   2670  CA  THR A 344      10.899  33.166  95.406  1.00 90.26           C  
ATOM   2671  C   THR A 344      11.477  33.706  96.727  1.00 91.58           C  
ATOM   2672  O   THR A 344      11.277  34.881  97.078  1.00 91.00           O  
ATOM   2673  CB  THR A 344       9.351  33.301  95.441  1.00 89.93           C  
ATOM   2674  OG1 THR A 344       8.794  32.257  96.257  1.00 89.80           O  
ATOM   2675  CG2 THR A 344       8.766  33.231  94.039  1.00 86.64           C  
ATOM   2676  N   GLU A 345      12.197  32.849  97.451  1.00 92.96           N  
ATOM   2677  CA  GLU A 345      12.810  33.218  98.743  1.00 92.62           C  
ATOM   2678  C   GLU A 345      13.627  34.529  98.728  1.00 91.79           C  
ATOM   2679  O   GLU A 345      13.390  35.418  99.544  1.00 90.02           O  
ATOM   2680  CB  GLU A 345      13.698  32.067  99.245  1.00 93.19           C  
ATOM   2681  CG  GLU A 345      12.957  30.751  99.414  1.00 92.99           C  
ATOM   2682  CD  GLU A 345      13.878  29.606  99.768  1.00 93.80           C  
ATOM   2683  OE1 GLU A 345      14.861  29.373  99.029  1.00 95.25           O  
ATOM   2684  OE2 GLU A 345      13.619  28.930 100.780  1.00 94.57           O  
ATOM   2685  N   ASP A 346      14.584  34.639  97.808  1.00 91.81           N  
ATOM   2686  CA  ASP A 346      15.405  35.836  97.719  1.00 92.99           C  
ATOM   2687  C   ASP A 346      14.598  37.115  97.532  1.00 94.86           C  
ATOM   2688  O   ASP A 346      15.074  38.205  97.866  1.00 94.73           O  
ATOM   2689  CB  ASP A 346      16.413  35.711  96.582  1.00 92.80           C  
ATOM   2690  CG  ASP A 346      17.630  34.891  96.965  1.00 92.07           C  
ATOM   2691  OD1 ASP A 346      17.469  33.663  97.181  1.00 89.87           O  
ATOM   2692  OD2 ASP A 346      18.738  35.490  97.047  1.00 91.45           O  
ATOM   2693  N   ASP A 347      13.397  36.995  96.970  1.00 97.16           N  
ATOM   2694  CA  ASP A 347      12.545  38.168  96.787  1.00 99.20           C  
ATOM   2695  C   ASP A 347      11.838  38.469  98.101  1.00100.70           C  
ATOM   2696  O   ASP A 347      11.557  39.631  98.401  1.00101.54           O  
ATOM   2697  CB  ASP A 347      11.491  37.949  95.696  1.00 99.53           C  
ATOM   2698  CG  ASP A 347      12.069  38.015  94.294  1.00100.53           C  
ATOM   2699  OD1 ASP A 347      12.658  36.995  93.856  1.00100.48           O  
ATOM   2700  OD2 ASP A 347      11.931  39.084  93.643  1.00 98.94           O  
ATOM   2701  N   LYS A 348      11.554  37.416  98.875  1.00101.97           N  
ATOM   2702  CA  LYS A 348      10.885  37.543 100.175  1.00102.01           C  
ATOM   2703  C   LYS A 348      11.732  38.384 101.141  1.00102.48           C  
ATOM   2704  O   LYS A 348      11.262  39.396 101.669  1.00103.05           O  
ATOM   2705  CB  LYS A 348      10.631  36.150 100.780  1.00101.89           C  
ATOM   2706  CG  LYS A 348       9.812  35.225  99.880  1.00102.81           C  
ATOM   2707  CD  LYS A 348       9.717  33.812 100.435  1.00103.21           C  
ATOM   2708  CE  LYS A 348       8.947  32.898  99.492  1.00100.78           C  
ATOM   2709  NZ  LYS A 348       8.928  31.495  99.985  1.00102.47           N  
ATOM   2710  N   ASP A 349      12.978  37.963 101.361  1.00102.53           N  
ATOM   2711  CA  ASP A 349      13.894  38.664 102.264  1.00102.79           C  
ATOM   2712  C   ASP A 349      14.217  40.067 101.772  1.00101.73           C  
ATOM   2713  O   ASP A 349      14.295  41.011 102.560  1.00101.17           O  
ATOM   2714  CB  ASP A 349      15.211  37.890 102.414  1.00105.19           C  
ATOM   2715  CG  ASP A 349      15.031  36.530 103.057  1.00107.96           C  
ATOM   2716  OD1 ASP A 349      14.279  35.689 102.487  1.00108.65           O  
ATOM   2717  OD2 ASP A 349      15.658  36.314 104.131  1.00109.33           O  
ATOM   2718  N   ALA A 350      14.421  40.192 100.465  1.00100.97           N  
ATOM   2719  CA  ALA A 350      14.748  41.470  99.856  1.00100.58           C  
ATOM   2720  C   ALA A 350      13.695  42.521 100.180  1.00101.44           C  
ATOM   2721  O   ALA A 350      13.991  43.712 100.201  1.00102.67           O  
ATOM   2722  CB  ALA A 350      14.889  41.303  98.351  1.00 98.94           C  
ATOM   2723  N   GLU A 351      12.470  42.086 100.457  1.00102.28           N  
ATOM   2724  CA  GLU A 351      11.402  43.018 100.793  1.00103.02           C  
ATOM   2725  C   GLU A 351      10.881  42.927 102.243  1.00104.14           C  
ATOM   2726  O   GLU A 351      10.329  43.899 102.759  1.00104.23           O  
ATOM   2727  CB  GLU A 351      10.270  42.852  99.800  1.00102.78           C  
ATOM   2728  CG  GLU A 351      10.689  43.222  98.414  1.00104.67           C  
ATOM   2729  CD  GLU A 351       9.844  42.527  97.375  1.00107.65           C  
ATOM   2730  OE1 GLU A 351       8.605  42.563  97.542  1.00107.43           O  
ATOM   2731  OE2 GLU A 351      10.409  41.950  96.399  1.00110.14           O  
ATOM   2732  N   THR A 352      11.055  41.781 102.908  1.00105.42           N  
ATOM   2733  CA  THR A 352      10.617  41.651 104.306  1.00106.21           C  
ATOM   2734  C   THR A 352      11.409  42.650 105.180  1.00108.10           C  
ATOM   2735  O   THR A 352      12.352  42.277 105.882  1.00108.48           O  
ATOM   2736  CB  THR A 352      10.805  40.186 104.867  1.00104.22           C  
ATOM   2737  OG1 THR A 352      12.118  39.705 104.569  1.00101.91           O  
ATOM   2738  CG2 THR A 352       9.771  39.237 104.276  1.00101.79           C  
ATOM   2739  N   GLU A 353      11.013  43.921 105.125  1.00109.77           N  
ATOM   2740  CA  GLU A 353      11.678  44.969 105.877  1.00111.40           C  
ATOM   2741  C   GLU A 353      11.777  44.684 107.371  1.00111.75           C  
ATOM   2742  O   GLU A 353      10.927  44.004 107.955  1.00111.84           O  
ATOM   2743  CB  GLU A 353      10.964  46.302 105.656  1.00112.53           C  
ATOM   2744  CG  GLU A 353      11.651  47.471 106.342  1.00116.55           C  
ATOM   2745  CD  GLU A 353      13.175  47.370 106.293  1.00118.19           C  
ATOM   2746  OE1 GLU A 353      13.708  47.011 105.221  1.00119.83           O  
ATOM   2747  OE2 GLU A 353      13.836  47.656 107.322  1.00118.63           O  
ATOM   2748  N   ILE A 354      12.831  45.224 107.977  1.00112.19           N  
ATOM   2749  CA  ILE A 354      13.102  45.073 109.402  1.00112.71           C  
ATOM   2750  C   ILE A 354      12.717  46.333 110.200  1.00113.97           C  
ATOM   2751  O   ILE A 354      13.252  47.418 109.973  1.00113.89           O  
ATOM   2752  CB  ILE A 354      14.590  44.726 109.598  1.00111.38           C  
ATOM   2753  CG1 ILE A 354      15.469  45.605 108.689  1.00110.62           C  
ATOM   2754  CG2 ILE A 354      14.813  43.241 109.278  1.00109.66           C  
ATOM   2755  CD1 ILE A 354      15.801  47.004 109.242  1.00108.95           C  
ATOM   2756  N   PRO A 355      11.781  46.193 111.153  1.00114.93           N  
ATOM   2757  CA  PRO A 355      11.272  47.277 112.014  1.00116.71           C  
ATOM   2758  C   PRO A 355      12.200  47.865 113.107  1.00118.47           C  
ATOM   2759  O   PRO A 355      12.113  47.446 114.271  1.00121.02           O  
ATOM   2760  CB  PRO A 355      10.029  46.645 112.637  1.00116.87           C  
ATOM   2761  CG  PRO A 355      10.452  45.206 112.804  1.00115.78           C  
ATOM   2762  CD  PRO A 355      11.124  44.909 111.477  1.00114.89           C  
ATOM   2763  N   ALA A 356      13.040  48.850 112.766  1.00117.82           N  
ATOM   2764  CA  ALA A 356      13.973  49.456 113.742  1.00116.69           C  
ATOM   2765  C   ALA A 356      14.966  48.407 114.289  1.00116.02           C  
ATOM   2766  O   ALA A 356      14.921  48.047 115.470  1.00115.64           O  
ATOM   2767  CB  ALA A 356      13.188  50.100 114.910  1.00116.64           C  
ATOM   2768  N   GLY A 357      15.861  47.929 113.426  1.00115.15           N  
ATOM   2769  CA  GLY A 357      16.821  46.916 113.821  1.00112.66           C  
ATOM   2770  C   GLY A 357      16.081  45.597 113.949  1.00111.56           C  
ATOM   2771  O   GLY A 357      16.687  44.535 114.008  1.00110.40           O  
ATOM   2772  N   GLU A 358      14.756  45.691 113.978  1.00111.72           N  
ATOM   2773  CA  GLU A 358      13.835  44.561 114.119  1.00113.00           C  
ATOM   2774  C   GLU A 358      13.444  44.393 115.604  1.00113.36           C  
ATOM   2775  O   GLU A 358      12.464  43.663 115.902  1.00113.17           O  
ATOM   2776  CB  GLU A 358      14.442  43.265 113.549  1.00113.36           C  
ATOM   2777  CG  GLU A 358      13.411  42.363 112.885  1.00113.97           C  
ATOM   2778  CD  GLU A 358      12.305  41.939 113.839  1.00114.03           C  
ATOM   2779  OE1 GLU A 358      12.498  40.948 114.568  1.00113.44           O  
ATOM   2780  OE2 GLU A 358      11.249  42.604 113.874  1.00113.54           O  
TER    2781      GLU A 358                                                      
ATOM   2782  N   GLU B   9      22.566  25.232  40.589  1.00 76.80           N  
ATOM   2783  CA  GLU B   9      21.193  25.433  41.157  1.00 78.21           C  
ATOM   2784  C   GLU B   9      20.293  26.179  40.192  1.00 77.28           C  
ATOM   2785  O   GLU B   9      19.152  26.508  40.551  1.00 78.15           O  
ATOM   2786  CB  GLU B   9      21.248  26.222  42.466  1.00 81.25           C  
ATOM   2787  CG  GLU B   9      21.832  25.461  43.637  1.00 87.37           C  
ATOM   2788  CD  GLU B   9      20.763  24.985  44.597  1.00 89.97           C  
ATOM   2789  OE1 GLU B   9      20.238  25.811  45.386  1.00 90.75           O  
ATOM   2790  OE2 GLU B   9      20.433  23.779  44.554  1.00 92.88           O  
ATOM   2791  N   THR B  10      20.824  26.477  38.995  1.00 75.06           N  
ATOM   2792  CA  THR B  10      20.072  27.172  37.931  1.00 70.11           C  
ATOM   2793  C   THR B  10      19.971  26.205  36.764  1.00 66.78           C  
ATOM   2794  O   THR B  10      20.356  25.037  36.900  1.00 66.54           O  
ATOM   2795  CB  THR B  10      20.765  28.510  37.435  1.00 70.24           C  
ATOM   2796  OG1 THR B  10      21.180  28.380  36.065  1.00 68.33           O  
ATOM   2797  CG2 THR B  10      21.976  28.874  38.319  1.00 71.08           C  
ATOM   2798  N   TRP B  11      19.452  26.679  35.634  1.00 62.42           N  
ATOM   2799  CA  TRP B  11      19.314  25.838  34.454  1.00 59.01           C  
ATOM   2800  C   TRP B  11      19.892  26.493  33.214  1.00 56.30           C  
ATOM   2801  O   TRP B  11      20.112  25.821  32.213  1.00 54.05           O  
ATOM   2802  CB  TRP B  11      17.849  25.547  34.177  1.00 61.64           C  
ATOM   2803  CG  TRP B  11      17.137  26.756  33.733  1.00 63.41           C  
ATOM   2804  CD1 TRP B  11      16.430  27.612  34.514  1.00 63.86           C  
ATOM   2805  CD2 TRP B  11      17.093  27.292  32.396  1.00 62.99           C  
ATOM   2806  NE1 TRP B  11      15.943  28.655  33.750  1.00 63.88           N  
ATOM   2807  CE2 TRP B  11      16.337  28.480  32.449  1.00 63.15           C  
ATOM   2808  CE3 TRP B  11      17.621  26.885  31.166  1.00 61.65           C  
ATOM   2809  CZ2 TRP B  11      16.088  29.264  31.313  1.00 64.53           C  
ATOM   2810  CZ3 TRP B  11      17.371  27.665  30.034  1.00 61.45           C  
ATOM   2811  CH2 TRP B  11      16.614  28.839  30.116  1.00 61.56           C  
ATOM   2812  N   TRP B  12      20.093  27.812  33.274  1.00 55.96           N  
ATOM   2813  CA  TRP B  12      20.633  28.599  32.139  1.00 54.85           C  
ATOM   2814  C   TRP B  12      22.163  28.788  32.227  1.00 53.41           C  
ATOM   2815  O   TRP B  12      22.834  29.087  31.215  1.00 51.42           O  
ATOM   2816  CB  TRP B  12      19.965  30.003  32.067  1.00 52.10           C  
ATOM   2817  CG  TRP B  12      20.039  30.706  33.347  1.00 50.10           C  
ATOM   2818  CD1 TRP B  12      19.093  30.709  34.298  1.00 52.04           C  
ATOM   2819  CD2 TRP B  12      21.196  31.332  33.934  1.00 51.25           C  
ATOM   2820  NE1 TRP B  12      19.570  31.282  35.472  1.00 50.83           N  
ATOM   2821  CE2 TRP B  12      20.860  31.669  35.271  1.00 51.30           C  
ATOM   2822  CE3 TRP B  12      22.489  31.635  33.463  1.00 53.76           C  
ATOM   2823  CZ2 TRP B  12      21.756  32.288  36.145  1.00 51.70           C  
ATOM   2824  CZ3 TRP B  12      23.398  32.258  34.331  1.00 52.66           C  
ATOM   2825  CH2 TRP B  12      23.018  32.576  35.665  1.00 53.10           C  
ATOM   2826  N   TYR B  13      22.688  28.633  33.449  1.00 52.90           N  
ATOM   2827  CA  TYR B  13      24.119  28.804  33.746  1.00 51.68           C  
ATOM   2828  C   TYR B  13      25.082  28.211  32.753  1.00 49.00           C  
ATOM   2829  O   TYR B  13      24.972  27.056  32.386  1.00 48.91           O  
ATOM   2830  CB  TYR B  13      24.484  28.207  35.094  1.00 53.23           C  
ATOM   2831  CG  TYR B  13      25.930  28.448  35.387  1.00 57.95           C  
ATOM   2832  CD1 TYR B  13      26.839  27.394  35.584  1.00 58.35           C  
ATOM   2833  CD2 TYR B  13      26.400  29.765  35.485  1.00 63.19           C  
ATOM   2834  CE1 TYR B  13      28.209  27.660  35.886  1.00 61.30           C  
ATOM   2835  CE2 TYR B  13      27.748  30.067  35.781  1.00 65.10           C  
ATOM   2836  CZ  TYR B  13      28.665  29.017  35.988  1.00 64.90           C  
ATOM   2837  OH  TYR B  13      29.989  29.387  36.311  1.00 63.14           O  
ATOM   2838  N   ASN B  14      26.059  28.993  32.341  1.00 47.75           N  
ATOM   2839  CA  ASN B  14      27.030  28.463  31.402  1.00 45.95           C  
ATOM   2840  C   ASN B  14      28.418  28.785  31.903  1.00 44.50           C  
ATOM   2841  O   ASN B  14      28.766  29.956  32.052  1.00 46.67           O  
ATOM   2842  CB  ASN B  14      26.845  29.068  30.013  1.00 44.45           C  
ATOM   2843  CG  ASN B  14      27.675  28.353  28.962  1.00 43.32           C  
ATOM   2844  OD1 ASN B  14      28.907  28.313  29.041  1.00 42.47           O  
ATOM   2845  ND2 ASN B  14      27.003  27.780  27.976  1.00 42.40           N  
ATOM   2846  N   PRO B  15      29.239  27.756  32.152  1.00 41.89           N  
ATOM   2847  CA  PRO B  15      30.590  28.017  32.642  1.00 40.00           C  
ATOM   2848  C   PRO B  15      31.384  28.912  31.715  1.00 39.28           C  
ATOM   2849  O   PRO B  15      32.216  29.660  32.183  1.00 39.78           O  
ATOM   2850  CB  PRO B  15      31.189  26.630  32.719  1.00 39.77           C  
ATOM   2851  CG  PRO B  15      30.528  25.933  31.532  1.00 38.51           C  
ATOM   2852  CD  PRO B  15      29.098  26.351  31.730  1.00 39.69           C  
ATOM   2853  N   SER B  16      31.100  28.864  30.414  1.00 39.06           N  
ATOM   2854  CA  SER B  16      31.869  29.638  29.445  1.00 39.83           C  
ATOM   2855  C   SER B  16      31.465  31.073  29.181  1.00 40.68           C  
ATOM   2856  O   SER B  16      32.296  31.990  29.167  1.00 43.71           O  
ATOM   2857  CB  SER B  16      31.895  28.940  28.074  1.00 39.01           C  
ATOM   2858  OG  SER B  16      32.283  27.590  28.113  1.00 36.29           O  
ATOM   2859  N   ILE B  17      30.184  31.254  28.915  1.00 40.59           N  
ATOM   2860  CA  ILE B  17      29.636  32.555  28.567  1.00 37.82           C  
ATOM   2861  C   ILE B  17      28.769  33.148  29.668  1.00 37.83           C  
ATOM   2862  O   ILE B  17      28.058  32.410  30.377  1.00 39.98           O  
ATOM   2863  CB  ILE B  17      28.822  32.399  27.289  1.00 36.41           C  
ATOM   2864  CG1 ILE B  17      29.710  31.805  26.213  1.00 34.66           C  
ATOM   2865  CG2 ILE B  17      28.321  33.718  26.804  1.00 38.65           C  
ATOM   2866  CD1 ILE B  17      28.969  31.578  24.973  1.00 37.89           C  
ATOM   2867  N   VAL B  18      28.844  34.470  29.857  1.00 37.03           N  
ATOM   2868  CA  VAL B  18      27.982  35.078  30.873  1.00 35.35           C  
ATOM   2869  C   VAL B  18      26.619  35.314  30.172  1.00 34.87           C  
ATOM   2870  O   VAL B  18      26.525  36.027  29.186  1.00 34.83           O  
ATOM   2871  CB  VAL B  18      28.571  36.409  31.468  1.00 34.14           C  
ATOM   2872  CG1 VAL B  18      27.487  37.163  32.154  1.00 33.84           C  
ATOM   2873  CG2 VAL B  18      29.672  36.126  32.501  1.00 30.26           C  
ATOM   2874  N   VAL B  19      25.592  34.612  30.633  1.00 34.17           N  
ATOM   2875  CA  VAL B  19      24.270  34.758  30.080  1.00 34.53           C  
ATOM   2876  C   VAL B  19      23.716  36.082  30.649  1.00 39.75           C  
ATOM   2877  O   VAL B  19      23.835  36.368  31.867  1.00 38.48           O  
ATOM   2878  CB  VAL B  19      23.366  33.588  30.503  1.00 31.86           C  
ATOM   2879  CG1 VAL B  19      21.931  33.893  30.205  1.00 28.36           C  
ATOM   2880  CG2 VAL B  19      23.771  32.339  29.788  1.00 31.44           C  
ATOM   2881  N   HIS B  20      23.145  36.896  29.751  1.00 41.22           N  
ATOM   2882  CA  HIS B  20      22.579  38.178  30.113  1.00 41.12           C  
ATOM   2883  C   HIS B  20      21.421  37.897  31.009  1.00 41.15           C  
ATOM   2884  O   HIS B  20      20.587  37.067  30.659  1.00 41.82           O  
ATOM   2885  CB  HIS B  20      22.053  38.913  28.900  1.00 45.01           C  
ATOM   2886  CG  HIS B  20      21.650  40.319  29.211  1.00 49.04           C  
ATOM   2887  ND1 HIS B  20      20.533  40.626  29.952  1.00 51.27           N  
ATOM   2888  CD2 HIS B  20      22.294  41.497  29.006  1.00 50.98           C  
ATOM   2889  CE1 HIS B  20      20.509  41.927  30.197  1.00 51.59           C  
ATOM   2890  NE2 HIS B  20      21.568  42.477  29.634  1.00 49.35           N  
ATOM   2891  N   PRO B  21      21.316  38.618  32.143  1.00 41.07           N  
ATOM   2892  CA  PRO B  21      20.246  38.458  33.138  1.00 41.90           C  
ATOM   2893  C   PRO B  21      18.841  38.327  32.565  1.00 44.42           C  
ATOM   2894  O   PRO B  21      17.985  37.605  33.130  1.00 46.69           O  
ATOM   2895  CB  PRO B  21      20.396  39.704  34.006  1.00 39.70           C  
ATOM   2896  CG  PRO B  21      21.819  39.947  33.973  1.00 37.96           C  
ATOM   2897  CD  PRO B  21      22.127  39.794  32.483  1.00 40.65           C  
ATOM   2898  N   HIS B  22      18.618  39.038  31.451  1.00 45.07           N  
ATOM   2899  CA  HIS B  22      17.328  39.051  30.738  1.00 46.25           C  
ATOM   2900  C   HIS B  22      16.913  37.655  30.289  1.00 46.14           C  
ATOM   2901  O   HIS B  22      15.731  37.381  30.034  1.00 46.72           O  
ATOM   2902  CB  HIS B  22      17.378  39.951  29.477  1.00 44.20           C  
ATOM   2903  CG  HIS B  22      16.112  39.924  28.672  1.00 41.19           C  
ATOM   2904  ND1 HIS B  22      14.879  40.222  29.219  1.00 39.32           N  
ATOM   2905  CD2 HIS B  22      15.878  39.574  27.382  1.00 42.22           C  
ATOM   2906  CE1 HIS B  22      13.943  40.050  28.304  1.00 40.36           C  
ATOM   2907  NE2 HIS B  22      14.519  39.659  27.178  1.00 40.82           N  
ATOM   2908  N   TRP B  23      17.891  36.772  30.179  1.00 46.03           N  
ATOM   2909  CA  TRP B  23      17.594  35.445  29.704  1.00 45.45           C  
ATOM   2910  C   TRP B  23      17.463  34.484  30.839  1.00 45.28           C  
ATOM   2911  O   TRP B  23      16.827  33.434  30.647  1.00 48.09           O  
ATOM   2912  CB  TRP B  23      18.679  34.947  28.741  1.00 46.08           C  
ATOM   2913  CG  TRP B  23      18.801  35.699  27.470  1.00 42.20           C  
ATOM   2914  CD1 TRP B  23      19.915  36.281  26.986  1.00 41.59           C  
ATOM   2915  CD2 TRP B  23      17.775  35.927  26.514  1.00 40.54           C  
ATOM   2916  NE1 TRP B  23      19.656  36.865  25.774  1.00 42.23           N  
ATOM   2917  CE2 TRP B  23      18.344  36.662  25.460  1.00 40.78           C  
ATOM   2918  CE3 TRP B  23      16.434  35.579  26.441  1.00 40.64           C  
ATOM   2919  CZ2 TRP B  23      17.615  37.065  24.334  1.00 42.64           C  
ATOM   2920  CZ3 TRP B  23      15.698  35.981  25.310  1.00 43.21           C  
ATOM   2921  CH2 TRP B  23      16.296  36.714  24.274  1.00 41.26           C  
ATOM   2922  N   ARG B  24      18.063  34.829  31.997  1.00 43.97           N  
ATOM   2923  CA  ARG B  24      18.044  33.982  33.228  1.00 41.79           C  
ATOM   2924  C   ARG B  24      16.753  34.106  33.985  1.00 42.39           C  
ATOM   2925  O   ARG B  24      16.469  33.316  34.872  1.00 40.71           O  
ATOM   2926  CB  ARG B  24      19.119  34.375  34.240  1.00 38.38           C  
ATOM   2927  CG  ARG B  24      20.247  35.186  33.715  1.00 36.29           C  
ATOM   2928  CD  ARG B  24      21.318  35.341  34.767  1.00 38.12           C  
ATOM   2929  NE  ARG B  24      22.468  36.056  34.227  1.00 41.24           N  
ATOM   2930  CZ  ARG B  24      23.434  36.572  34.978  1.00 44.15           C  
ATOM   2931  NH1 ARG B  24      23.366  36.437  36.308  1.00 44.74           N  
ATOM   2932  NH2 ARG B  24      24.455  37.224  34.406  1.00 44.92           N  
ATOM   2933  N   GLU B  25      15.997  35.141  33.653  1.00 44.63           N  
ATOM   2934  CA  GLU B  25      14.773  35.358  34.331  1.00 45.24           C  
ATOM   2935  C   GLU B  25      13.666  34.493  33.796  1.00 47.67           C  
ATOM   2936  O   GLU B  25      12.599  34.394  34.395  1.00 49.56           O  
ATOM   2937  CB  GLU B  25      14.432  36.817  34.276  1.00 43.36           C  
ATOM   2938  CG  GLU B  25      14.153  37.325  32.956  1.00 42.84           C  
ATOM   2939  CD  GLU B  25      13.454  38.647  33.097  1.00 43.90           C  
ATOM   2940  OE1 GLU B  25      14.008  39.457  33.863  1.00 40.90           O  
ATOM   2941  OE2 GLU B  25      12.370  38.866  32.479  1.00 46.46           O  
ATOM   2942  N   PHE B  26      13.892  33.817  32.687  1.00 51.13           N  
ATOM   2943  CA  PHE B  26      12.809  32.953  32.221  1.00 56.90           C  
ATOM   2944  C   PHE B  26      12.746  31.534  32.853  1.00 60.48           C  
ATOM   2945  O   PHE B  26      13.011  31.324  34.073  1.00 61.34           O  
ATOM   2946  CB  PHE B  26      12.834  32.886  30.704  1.00 55.22           C  
ATOM   2947  CG  PHE B  26      12.465  34.183  30.081  1.00 56.12           C  
ATOM   2948  CD1 PHE B  26      11.142  34.499  29.852  1.00 55.50           C  
ATOM   2949  CD2 PHE B  26      13.442  35.139  29.813  1.00 56.74           C  
ATOM   2950  CE1 PHE B  26      10.798  35.743  29.372  1.00 55.56           C  
ATOM   2951  CE2 PHE B  26      13.108  36.396  29.327  1.00 53.20           C  
ATOM   2952  CZ  PHE B  26      11.790  36.696  29.110  1.00 55.93           C  
ATOM   2953  N   ASP B  27      12.334  30.578  32.029  1.00 61.62           N  
ATOM   2954  CA  ASP B  27      12.205  29.186  32.448  1.00 61.45           C  
ATOM   2955  C   ASP B  27      12.814  28.398  31.323  1.00 62.76           C  
ATOM   2956  O   ASP B  27      13.083  28.961  30.254  1.00 66.77           O  
ATOM   2957  CB  ASP B  27      10.741  28.776  32.565  1.00 57.67           C  
ATOM   2958  CG  ASP B  27      10.153  29.112  33.881  1.00 54.30           C  
ATOM   2959  OD1 ASP B  27      10.874  29.561  34.802  1.00 55.75           O  
ATOM   2960  OD2 ASP B  27       8.948  28.910  33.971  1.00 52.49           O  
ATOM   2961  N   GLN B  28      13.032  27.108  31.540  1.00 60.94           N  
ATOM   2962  CA  GLN B  28      13.603  26.280  30.494  1.00 61.11           C  
ATOM   2963  C   GLN B  28      12.478  25.743  29.597  1.00 60.97           C  
ATOM   2964  O   GLN B  28      11.538  25.118  30.095  1.00 62.09           O  
ATOM   2965  CB  GLN B  28      14.375  25.121  31.135  1.00 63.06           C  
ATOM   2966  CG  GLN B  28      14.980  24.097  30.174  1.00 62.61           C  
ATOM   2967  CD  GLN B  28      16.509  24.145  30.182  1.00 63.75           C  
ATOM   2968  OE1 GLN B  28      17.151  24.193  31.255  1.00 62.89           O  
ATOM   2969  NE2 GLN B  28      17.103  24.118  28.986  1.00 61.75           N  
ATOM   2970  N   VAL B  29      12.558  25.985  28.282  1.00 60.03           N  
ATOM   2971  CA  VAL B  29      11.526  25.457  27.386  1.00 58.34           C  
ATOM   2972  C   VAL B  29      11.666  23.921  27.370  1.00 60.14           C  
ATOM   2973  O   VAL B  29      12.668  23.339  27.840  1.00 60.15           O  
ATOM   2974  CB  VAL B  29      11.649  26.002  25.943  1.00 55.09           C  
ATOM   2975  CG1 VAL B  29      12.197  27.388  25.974  1.00 55.53           C  
ATOM   2976  CG2 VAL B  29      12.535  25.108  25.104  1.00 55.27           C  
ATOM   2977  N   PRO B  30      10.657  23.243  26.829  1.00 60.75           N  
ATOM   2978  CA  PRO B  30      10.571  21.776  26.711  1.00 60.81           C  
ATOM   2979  C   PRO B  30      11.580  21.125  25.768  1.00 59.19           C  
ATOM   2980  O   PRO B  30      11.781  21.599  24.648  1.00 58.69           O  
ATOM   2981  CB  PRO B  30       9.133  21.547  26.229  1.00 61.96           C  
ATOM   2982  CG  PRO B  30       8.396  22.800  26.732  1.00 63.13           C  
ATOM   2983  CD  PRO B  30       9.402  23.884  26.410  1.00 61.30           C  
ATOM   2984  N   ASP B  31      12.173  20.017  26.217  1.00 57.27           N  
ATOM   2985  CA  ASP B  31      13.140  19.312  25.399  1.00 56.44           C  
ATOM   2986  C   ASP B  31      12.738  19.293  23.931  1.00 54.56           C  
ATOM   2987  O   ASP B  31      13.590  19.412  23.044  1.00 54.77           O  
ATOM   2988  CB  ASP B  31      13.268  17.864  25.826  1.00 61.16           C  
ATOM   2989  CG  ASP B  31      13.525  17.699  27.321  1.00 66.83           C  
ATOM   2990  OD1 ASP B  31      14.245  18.541  27.944  1.00 68.12           O  
ATOM   2991  OD2 ASP B  31      13.017  16.678  27.863  1.00 69.88           O  
ATOM   2992  N   ALA B  32      11.441  19.131  23.675  1.00 50.97           N  
ATOM   2993  CA  ALA B  32      10.944  19.053  22.318  1.00 45.51           C  
ATOM   2994  C   ALA B  32      11.285  20.293  21.540  1.00 44.91           C  
ATOM   2995  O   ALA B  32      11.688  20.198  20.385  1.00 43.84           O  
ATOM   2996  CB  ALA B  32       9.461  18.827  22.332  1.00 46.42           C  
ATOM   2997  N   VAL B  33      11.136  21.463  22.168  1.00 44.08           N  
ATOM   2998  CA  VAL B  33      11.454  22.733  21.492  1.00 41.30           C  
ATOM   2999  C   VAL B  33      12.929  22.702  21.094  1.00 42.62           C  
ATOM   3000  O   VAL B  33      13.257  22.909  19.920  1.00 41.31           O  
ATOM   3001  CB  VAL B  33      11.171  23.938  22.395  1.00 38.37           C  
ATOM   3002  CG1 VAL B  33      11.661  25.187  21.758  1.00 34.65           C  
ATOM   3003  CG2 VAL B  33       9.687  24.034  22.633  1.00 37.64           C  
ATOM   3004  N   TYR B  34      13.804  22.417  22.068  1.00 42.67           N  
ATOM   3005  CA  TYR B  34      15.247  22.310  21.841  1.00 41.70           C  
ATOM   3006  C   TYR B  34      15.575  21.333  20.721  1.00 44.22           C  
ATOM   3007  O   TYR B  34      16.334  21.653  19.799  1.00 43.94           O  
ATOM   3008  CB  TYR B  34      15.938  21.821  23.095  1.00 40.11           C  
ATOM   3009  CG  TYR B  34      16.236  22.897  24.114  1.00 40.15           C  
ATOM   3010  CD1 TYR B  34      17.184  23.873  23.871  1.00 37.58           C  
ATOM   3011  CD2 TYR B  34      15.620  22.886  25.358  1.00 46.27           C  
ATOM   3012  CE1 TYR B  34      17.524  24.801  24.835  1.00 39.08           C  
ATOM   3013  CE2 TYR B  34      15.946  23.813  26.337  1.00 46.07           C  
ATOM   3014  CZ  TYR B  34      16.903  24.761  26.055  1.00 44.65           C  
ATOM   3015  OH  TYR B  34      17.236  25.675  27.006  1.00 51.60           O  
ATOM   3016  N   TYR B  35      15.008  20.131  20.821  1.00 46.70           N  
ATOM   3017  CA  TYR B  35      15.225  19.076  19.834  1.00 47.15           C  
ATOM   3018  C   TYR B  35      14.701  19.503  18.477  1.00 45.28           C  
ATOM   3019  O   TYR B  35      15.326  19.252  17.454  1.00 43.53           O  
ATOM   3020  CB  TYR B  35      14.554  17.775  20.297  1.00 51.18           C  
ATOM   3021  CG  TYR B  35      15.080  17.265  21.640  1.00 57.10           C  
ATOM   3022  CD1 TYR B  35      14.404  16.257  22.355  1.00 59.40           C  
ATOM   3023  CD2 TYR B  35      16.238  17.811  22.208  1.00 60.33           C  
ATOM   3024  CE1 TYR B  35      14.866  15.811  23.601  1.00 62.06           C  
ATOM   3025  CE2 TYR B  35      16.715  17.378  23.453  1.00 63.25           C  
ATOM   3026  CZ  TYR B  35      16.031  16.379  24.147  1.00 64.35           C  
ATOM   3027  OH  TYR B  35      16.526  15.957  25.379  1.00 67.33           O  
ATOM   3028  N   SER B  36      13.552  20.161  18.465  1.00 45.41           N  
ATOM   3029  CA  SER B  36      12.989  20.626  17.209  1.00 44.01           C  
ATOM   3030  C   SER B  36      13.965  21.642  16.641  1.00 43.15           C  
ATOM   3031  O   SER B  36      14.296  21.612  15.453  1.00 40.52           O  
ATOM   3032  CB  SER B  36      11.626  21.277  17.445  1.00 44.46           C  
ATOM   3033  OG  SER B  36      10.683  20.327  17.913  1.00 44.88           O  
ATOM   3034  N   LEU B  37      14.453  22.527  17.504  1.00 44.03           N  
ATOM   3035  CA  LEU B  37      15.382  23.574  17.062  1.00 46.11           C  
ATOM   3036  C   LEU B  37      16.638  23.000  16.424  1.00 48.03           C  
ATOM   3037  O   LEU B  37      17.043  23.415  15.329  1.00 46.45           O  
ATOM   3038  CB  LEU B  37      15.755  24.501  18.235  1.00 42.24           C  
ATOM   3039  CG  LEU B  37      14.655  25.444  18.734  1.00 39.14           C  
ATOM   3040  CD1 LEU B  37      15.091  26.010  20.052  1.00 36.87           C  
ATOM   3041  CD2 LEU B  37      14.360  26.548  17.704  1.00 31.10           C  
ATOM   3042  N   GLY B  38      17.247  22.044  17.131  1.00 51.45           N  
ATOM   3043  CA  GLY B  38      18.460  21.381  16.651  1.00 51.28           C  
ATOM   3044  C   GLY B  38      18.341  20.741  15.268  1.00 49.87           C  
ATOM   3045  O   GLY B  38      19.235  20.920  14.435  1.00 45.75           O  
ATOM   3046  N   ILE B  39      17.243  20.010  15.028  1.00 49.93           N  
ATOM   3047  CA  ILE B  39      17.033  19.362  13.744  1.00 50.60           C  
ATOM   3048  C   ILE B  39      16.592  20.358  12.710  1.00 51.04           C  
ATOM   3049  O   ILE B  39      16.924  20.210  11.534  1.00 54.42           O  
ATOM   3050  CB  ILE B  39      16.025  18.196  13.808  1.00 49.50           C  
ATOM   3051  CG1 ILE B  39      14.752  18.628  14.491  1.00 54.11           C  
ATOM   3052  CG2 ILE B  39      16.618  17.043  14.578  1.00 47.41           C  
ATOM   3053  CD1 ILE B  39      13.761  17.483  14.656  1.00 58.83           C  
ATOM   3054  N   PHE B  40      15.866  21.390  13.130  1.00 50.22           N  
ATOM   3055  CA  PHE B  40      15.439  22.417  12.165  1.00 49.40           C  
ATOM   3056  C   PHE B  40      16.694  23.079  11.542  1.00 49.14           C  
ATOM   3057  O   PHE B  40      16.851  23.166  10.307  1.00 47.16           O  
ATOM   3058  CB  PHE B  40      14.587  23.517  12.837  1.00 45.31           C  
ATOM   3059  CG  PHE B  40      14.290  24.678  11.929  1.00 42.36           C  
ATOM   3060  CD1 PHE B  40      13.348  24.561  10.907  1.00 42.98           C  
ATOM   3061  CD2 PHE B  40      15.020  25.861  12.023  1.00 38.75           C  
ATOM   3062  CE1 PHE B  40      13.139  25.620   9.984  1.00 42.96           C  
ATOM   3063  CE2 PHE B  40      14.818  26.916  11.107  1.00 37.44           C  
ATOM   3064  CZ  PHE B  40      13.877  26.800  10.084  1.00 36.94           C  
ATOM   3065  N   ILE B  41      17.587  23.529  12.418  1.00 49.23           N  
ATOM   3066  CA  ILE B  41      18.791  24.198  11.980  1.00 50.06           C  
ATOM   3067  C   ILE B  41      19.724  23.181  11.351  1.00 50.04           C  
ATOM   3068  O   ILE B  41      20.519  23.511  10.461  1.00 49.94           O  
ATOM   3069  CB  ILE B  41      19.485  24.909  13.161  1.00 50.97           C  
ATOM   3070  CG1 ILE B  41      20.479  25.953  12.617  1.00 51.85           C  
ATOM   3071  CG2 ILE B  41      20.126  23.878  14.098  1.00 51.22           C  
ATOM   3072  CD1 ILE B  41      19.832  27.047  11.743  1.00 47.59           C  
ATOM   3073  N   GLY B  42      19.638  21.944  11.823  1.00 49.46           N  
ATOM   3074  CA  GLY B  42      20.460  20.895  11.232  1.00 53.08           C  
ATOM   3075  C   GLY B  42      20.106  20.722   9.746  1.00 53.24           C  
ATOM   3076  O   GLY B  42      20.987  20.642   8.877  1.00 54.96           O  
ATOM   3077  N   ILE B  43      18.805  20.663   9.451  1.00 52.29           N  
ATOM   3078  CA  ILE B  43      18.321  20.532   8.084  1.00 47.85           C  
ATOM   3079  C   ILE B  43      18.682  21.750   7.229  1.00 48.34           C  
ATOM   3080  O   ILE B  43      18.838  21.641   5.999  1.00 47.18           O  
ATOM   3081  CB  ILE B  43      16.826  20.346   8.069  1.00 44.21           C  
ATOM   3082  CG1 ILE B  43      16.493  19.036   8.733  1.00 42.98           C  
ATOM   3083  CG2 ILE B  43      16.318  20.329   6.637  1.00 44.68           C  
ATOM   3084  CD1 ILE B  43      15.041  18.673   8.569  1.00 46.91           C  
ATOM   3085  N   CYS B  44      18.813  22.910   7.873  1.00 48.82           N  
ATOM   3086  CA  CYS B  44      19.198  24.128   7.149  1.00 48.88           C  
ATOM   3087  C   CYS B  44      20.658  23.971   6.708  1.00 45.99           C  
ATOM   3088  O   CYS B  44      21.030  24.370   5.609  1.00 45.45           O  
ATOM   3089  CB  CYS B  44      19.059  25.385   8.033  1.00 52.90           C  
ATOM   3090  SG  CYS B  44      17.346  25.995   8.384  1.00 51.27           S  
ATOM   3091  N   GLY B  45      21.476  23.389   7.579  1.00 42.31           N  
ATOM   3092  CA  GLY B  45      22.859  23.174   7.231  1.00 39.71           C  
ATOM   3093  C   GLY B  45      22.900  22.232   6.037  1.00 39.14           C  
ATOM   3094  O   GLY B  45      23.632  22.459   5.072  1.00 42.48           O  
ATOM   3095  N   ILE B  46      22.119  21.164   6.093  1.00 36.70           N  
ATOM   3096  CA  ILE B  46      22.096  20.214   5.005  1.00 35.69           C  
ATOM   3097  C   ILE B  46      21.665  20.878   3.697  1.00 38.91           C  
ATOM   3098  O   ILE B  46      22.438  20.898   2.706  1.00 40.48           O  
ATOM   3099  CB  ILE B  46      21.149  19.067   5.313  1.00 32.24           C  
ATOM   3100  CG1 ILE B  46      21.742  18.229   6.421  1.00 28.04           C  
ATOM   3101  CG2 ILE B  46      20.871  18.256   4.060  1.00 26.00           C  
ATOM   3102  CD1 ILE B  46      20.809  17.165   6.882  1.00 32.29           C  
ATOM   3103  N   ILE B  47      20.439  21.414   3.688  1.00 39.23           N  
ATOM   3104  CA  ILE B  47      19.895  22.079   2.495  1.00 41.16           C  
ATOM   3105  C   ILE B  47      20.710  23.304   2.029  1.00 43.71           C  
ATOM   3106  O   ILE B  47      20.864  23.531   0.820  1.00 46.53           O  
ATOM   3107  CB  ILE B  47      18.433  22.496   2.723  1.00 39.28           C  
ATOM   3108  CG1 ILE B  47      17.596  21.250   3.019  1.00 39.20           C  
ATOM   3109  CG2 ILE B  47      17.911  23.271   1.516  1.00 33.46           C  
ATOM   3110  CD1 ILE B  47      16.167  21.532   3.389  1.00 39.01           C  
ATOM   3111  N   GLY B  48      21.226  24.078   2.985  1.00 43.47           N  
ATOM   3112  CA  GLY B  48      22.039  25.238   2.657  1.00 42.87           C  
ATOM   3113  C   GLY B  48      23.405  24.864   2.068  1.00 43.34           C  
ATOM   3114  O   GLY B  48      23.772  25.342   0.992  1.00 40.68           O  
ATOM   3115  N   CYS B  49      24.175  24.017   2.755  1.00 45.76           N  
ATOM   3116  CA  CYS B  49      25.492  23.631   2.247  1.00 47.70           C  
ATOM   3117  C   CYS B  49      25.350  22.901   0.930  1.00 50.35           C  
ATOM   3118  O   CYS B  49      26.093  23.157  -0.038  1.00 51.75           O  
ATOM   3119  CB  CYS B  49      26.208  22.761   3.257  1.00 46.70           C  
ATOM   3120  SG  CYS B  49      26.521  23.709   4.751  1.00 44.77           S  
ATOM   3121  N   GLY B  50      24.378  22.002   0.884  1.00 51.49           N  
ATOM   3122  CA  GLY B  50      24.167  21.284  -0.346  1.00 54.93           C  
ATOM   3123  C   GLY B  50      23.811  22.229  -1.495  1.00 56.51           C  
ATOM   3124  O   GLY B  50      24.564  22.347  -2.481  1.00 59.58           O  
ATOM   3125  N   GLY B  51      22.649  22.891  -1.377  1.00 54.88           N  
ATOM   3126  CA  GLY B  51      22.184  23.781  -2.427  1.00 48.83           C  
ATOM   3127  C   GLY B  51      23.222  24.790  -2.881  1.00 45.94           C  
ATOM   3128  O   GLY B  51      23.502  24.931  -4.073  1.00 43.22           O  
ATOM   3129  N   ASN B  52      23.804  25.490  -1.920  1.00 44.95           N  
ATOM   3130  CA  ASN B  52      24.768  26.509  -2.242  1.00 43.82           C  
ATOM   3131  C   ASN B  52      26.010  25.894  -2.782  1.00 44.58           C  
ATOM   3132  O   ASN B  52      26.773  26.566  -3.492  1.00 42.91           O  
ATOM   3133  CB  ASN B  52      25.074  27.364  -1.024  1.00 43.06           C  
ATOM   3134  CG  ASN B  52      24.034  28.438  -0.827  1.00 39.94           C  
ATOM   3135  OD1 ASN B  52      23.797  29.221  -1.743  1.00 34.68           O  
ATOM   3136  ND2 ASN B  52      23.398  28.479   0.359  1.00 39.92           N  
ATOM   3137  N   GLY B  53      26.213  24.622  -2.425  1.00 45.42           N  
ATOM   3138  CA  GLY B  53      27.367  23.875  -2.914  1.00 48.74           C  
ATOM   3139  C   GLY B  53      27.200  23.643  -4.420  1.00 49.56           C  
ATOM   3140  O   GLY B  53      28.119  23.875  -5.237  1.00 50.58           O  
ATOM   3141  N   ILE B  54      25.999  23.188  -4.784  1.00 48.72           N  
ATOM   3142  CA  ILE B  54      25.641  22.934  -6.176  1.00 45.02           C  
ATOM   3143  C   ILE B  54      25.836  24.222  -6.981  1.00 44.55           C  
ATOM   3144  O   ILE B  54      26.575  24.227  -7.967  1.00 45.33           O  
ATOM   3145  CB  ILE B  54      24.156  22.448  -6.303  1.00 42.20           C  
ATOM   3146  CG1 ILE B  54      24.007  21.054  -5.717  1.00 36.42           C  
ATOM   3147  CG2 ILE B  54      23.723  22.445  -7.755  1.00 41.24           C  
ATOM   3148  CD1 ILE B  54      22.607  20.656  -5.580  1.00 32.70           C  
ATOM   3149  N   VAL B  55      25.201  25.310  -6.549  1.00 43.30           N  
ATOM   3150  CA  VAL B  55      25.345  26.579  -7.262  1.00 44.34           C  
ATOM   3151  C   VAL B  55      26.809  27.038  -7.411  1.00 43.22           C  
ATOM   3152  O   VAL B  55      27.191  27.518  -8.480  1.00 42.62           O  
ATOM   3153  CB  VAL B  55      24.473  27.719  -6.608  1.00 43.80           C  
ATOM   3154  CG1 VAL B  55      24.626  27.686  -5.126  1.00 48.23           C  
ATOM   3155  CG2 VAL B  55      24.868  29.097  -7.133  1.00 40.12           C  
ATOM   3156  N   ILE B  56      27.639  26.880  -6.379  1.00 43.45           N  
ATOM   3157  CA  ILE B  56      29.027  27.320  -6.531  1.00 44.87           C  
ATOM   3158  C   ILE B  56      29.657  26.458  -7.599  1.00 49.12           C  
ATOM   3159  O   ILE B  56      30.285  26.963  -8.551  1.00 50.75           O  
ATOM   3160  CB  ILE B  56      29.876  27.168  -5.251  1.00 40.78           C  
ATOM   3161  CG1 ILE B  56      29.398  28.129  -4.168  1.00 39.72           C  
ATOM   3162  CG2 ILE B  56      31.307  27.496  -5.556  1.00 35.70           C  
ATOM   3163  CD1 ILE B  56      30.212  28.018  -2.902  1.00 39.51           C  
ATOM   3164  N   TYR B  57      29.450  25.151  -7.452  1.00 53.35           N  
ATOM   3165  CA  TYR B  57      30.015  24.150  -8.372  1.00 56.34           C  
ATOM   3166  C   TYR B  57      29.635  24.370  -9.857  1.00 56.49           C  
ATOM   3167  O   TYR B  57      30.504  24.567 -10.747  1.00 55.88           O  
ATOM   3168  CB  TYR B  57      29.604  22.732  -7.900  1.00 57.54           C  
ATOM   3169  CG  TYR B  57      30.087  21.620  -8.804  1.00 59.31           C  
ATOM   3170  CD1 TYR B  57      29.227  21.062  -9.768  1.00 59.51           C  
ATOM   3171  CD2 TYR B  57      31.423  21.160  -8.739  1.00 60.70           C  
ATOM   3172  CE1 TYR B  57      29.681  20.084 -10.636  1.00 61.00           C  
ATOM   3173  CE2 TYR B  57      31.888  20.185  -9.602  1.00 60.84           C  
ATOM   3174  CZ  TYR B  57      31.022  19.652 -10.542  1.00 61.98           C  
ATOM   3175  OH  TYR B  57      31.512  18.682 -11.397  1.00 67.42           O  
ATOM   3176  N   LEU B  58      28.330  24.343 -10.113  1.00 55.42           N  
ATOM   3177  CA  LEU B  58      27.812  24.519 -11.470  1.00 53.05           C  
ATOM   3178  C   LEU B  58      28.149  25.869 -12.128  1.00 51.87           C  
ATOM   3179  O   LEU B  58      28.451  25.918 -13.330  1.00 51.21           O  
ATOM   3180  CB  LEU B  58      26.288  24.306 -11.477  1.00 49.48           C  
ATOM   3181  CG  LEU B  58      25.770  23.007 -12.042  1.00 44.09           C  
ATOM   3182  CD1 LEU B  58      26.566  21.861 -11.465  1.00 43.76           C  
ATOM   3183  CD2 LEU B  58      24.321  22.899 -11.709  1.00 44.89           C  
ATOM   3184  N   PHE B  59      28.087  26.955 -11.361  1.00 50.35           N  
ATOM   3185  CA  PHE B  59      28.371  28.270 -11.930  1.00 49.50           C  
ATOM   3186  C   PHE B  59      29.838  28.480 -12.250  1.00 50.40           C  
ATOM   3187  O   PHE B  59      30.155  29.187 -13.198  1.00 50.17           O  
ATOM   3188  CB  PHE B  59      27.889  29.399 -11.021  1.00 47.46           C  
ATOM   3189  CG  PHE B  59      26.475  29.813 -11.290  1.00 45.84           C  
ATOM   3190  CD1 PHE B  59      25.399  29.075 -10.805  1.00 45.50           C  
ATOM   3191  CD2 PHE B  59      26.214  30.921 -12.073  1.00 48.32           C  
ATOM   3192  CE1 PHE B  59      24.086  29.438 -11.102  1.00 43.40           C  
ATOM   3193  CE2 PHE B  59      24.903  31.293 -12.376  1.00 48.05           C  
ATOM   3194  CZ  PHE B  59      23.844  30.549 -11.888  1.00 45.24           C  
ATOM   3195  N   THR B  60      30.741  27.880 -11.477  1.00 49.49           N  
ATOM   3196  CA  THR B  60      32.146  28.054 -11.784  1.00 48.57           C  
ATOM   3197  C   THR B  60      32.627  27.069 -12.836  1.00 52.02           C  
ATOM   3198  O   THR B  60      33.694  27.268 -13.412  1.00 53.52           O  
ATOM   3199  CB  THR B  60      33.012  27.862 -10.574  1.00 46.10           C  
ATOM   3200  OG1 THR B  60      32.952  26.504 -10.150  1.00 47.81           O  
ATOM   3201  CG2 THR B  60      32.556  28.739  -9.474  1.00 46.36           C  
ATOM   3202  N   LYS B  61      31.850  26.013 -13.104  1.00 54.60           N  
ATOM   3203  CA  LYS B  61      32.259  24.994 -14.086  1.00 54.75           C  
ATOM   3204  C   LYS B  61      31.534  25.041 -15.419  1.00 52.91           C  
ATOM   3205  O   LYS B  61      32.159  25.033 -16.480  1.00 51.57           O  
ATOM   3206  CB  LYS B  61      32.097  23.599 -13.468  1.00 58.48           C  
ATOM   3207  CG  LYS B  61      32.876  23.394 -12.164  1.00 59.26           C  
ATOM   3208  CD  LYS B  61      34.362  23.589 -12.377  1.00 64.30           C  
ATOM   3209  CE  LYS B  61      35.087  23.504 -11.053  1.00 70.24           C  
ATOM   3210  NZ  LYS B  61      36.572  23.736 -11.165  1.00 75.07           N  
ATOM   3211  N   THR B  62      30.209  25.041 -15.337  1.00 53.67           N  
ATOM   3212  CA  THR B  62      29.355  25.093 -16.509  1.00 55.14           C  
ATOM   3213  C   THR B  62      29.796  26.320 -17.293  1.00 57.65           C  
ATOM   3214  O   THR B  62      29.512  27.450 -16.878  1.00 58.33           O  
ATOM   3215  CB  THR B  62      27.886  25.232 -16.098  1.00 52.35           C  
ATOM   3216  OG1 THR B  62      27.546  24.189 -15.181  1.00 46.42           O  
ATOM   3217  CG2 THR B  62      26.988  25.143 -17.317  1.00 51.16           C  
ATOM   3218  N   LYS B  63      30.483  26.095 -18.415  1.00 59.59           N  
ATOM   3219  CA  LYS B  63      31.014  27.193 -19.214  1.00 63.82           C  
ATOM   3220  C   LYS B  63      30.010  28.268 -19.592  1.00 64.93           C  
ATOM   3221  O   LYS B  63      30.381  29.462 -19.714  1.00 64.06           O  
ATOM   3222  CB  LYS B  63      31.659  26.675 -20.488  1.00 65.99           C  
ATOM   3223  CG  LYS B  63      32.971  27.387 -20.836  1.00 69.54           C  
ATOM   3224  CD  LYS B  63      34.182  26.572 -20.288  1.00 73.05           C  
ATOM   3225  CE  LYS B  63      35.564  26.943 -20.944  1.00 73.54           C  
ATOM   3226  NZ  LYS B  63      35.674  26.983 -22.467  1.00 67.74           N  
ATOM   3227  N   SER B  64      28.753  27.830 -19.773  1.00 65.39           N  
ATOM   3228  CA  SER B  64      27.613  28.695 -20.163  1.00 65.96           C  
ATOM   3229  C   SER B  64      27.362  29.797 -19.154  1.00 66.87           C  
ATOM   3230  O   SER B  64      26.940  30.904 -19.512  1.00 69.02           O  
ATOM   3231  CB  SER B  64      26.309  27.874 -20.302  1.00 65.17           C  
ATOM   3232  OG  SER B  64      25.702  27.564 -19.042  1.00 63.26           O  
ATOM   3233  N   LEU B  65      27.615  29.461 -17.891  1.00 66.30           N  
ATOM   3234  CA  LEU B  65      27.424  30.363 -16.774  1.00 63.87           C  
ATOM   3235  C   LEU B  65      28.681  31.140 -16.429  1.00 64.55           C  
ATOM   3236  O   LEU B  65      28.807  31.579 -15.295  1.00 64.63           O  
ATOM   3237  CB  LEU B  65      26.985  29.566 -15.541  1.00 59.94           C  
ATOM   3238  CG  LEU B  65      25.700  28.758 -15.616  1.00 54.14           C  
ATOM   3239  CD1 LEU B  65      25.593  27.968 -14.341  1.00 49.85           C  
ATOM   3240  CD2 LEU B  65      24.496  29.681 -15.810  1.00 52.74           C  
ATOM   3241  N   GLN B  66      29.606  31.324 -17.370  1.00 65.88           N  
ATOM   3242  CA  GLN B  66      30.825  32.064 -17.037  1.00 68.83           C  
ATOM   3243  C   GLN B  66      30.867  33.598 -17.290  1.00 69.09           C  
ATOM   3244  O   GLN B  66      31.960  34.177 -17.385  1.00 71.08           O  
ATOM   3245  CB  GLN B  66      32.044  31.412 -17.691  1.00 71.94           C  
ATOM   3246  CG  GLN B  66      32.889  30.536 -16.771  1.00 78.63           C  
ATOM   3247  CD  GLN B  66      32.452  29.047 -16.796  1.00 84.73           C  
ATOM   3248  OE1 GLN B  66      31.292  28.723 -16.442  1.00 86.27           O  
ATOM   3249  NE2 GLN B  66      33.383  28.135 -17.205  1.00 84.25           N  
ATOM   3250  N   THR B  67      29.707  34.257 -17.382  1.00 66.58           N  
ATOM   3251  CA  THR B  67      29.670  35.717 -17.551  1.00 64.33           C  
ATOM   3252  C   THR B  67      29.995  36.393 -16.176  1.00 62.47           C  
ATOM   3253  O   THR B  67      29.689  35.832 -15.107  1.00 61.36           O  
ATOM   3254  CB  THR B  67      28.273  36.183 -18.045  1.00 65.43           C  
ATOM   3255  OG1 THR B  67      27.462  36.638 -16.941  1.00 65.61           O  
ATOM   3256  CG2 THR B  67      27.571  35.033 -18.763  1.00 65.20           C  
ATOM   3257  N   PRO B  68      30.599  37.610 -16.194  1.00 59.13           N  
ATOM   3258  CA  PRO B  68      30.982  38.373 -14.993  1.00 57.82           C  
ATOM   3259  C   PRO B  68      29.956  38.525 -13.851  1.00 57.29           C  
ATOM   3260  O   PRO B  68      30.202  38.103 -12.695  1.00 57.00           O  
ATOM   3261  CB  PRO B  68      31.402  39.728 -15.570  1.00 56.19           C  
ATOM   3262  CG  PRO B  68      31.948  39.369 -16.873  1.00 56.97           C  
ATOM   3263  CD  PRO B  68      30.925  38.385 -17.402  1.00 57.39           C  
ATOM   3264  N   ALA B  69      28.815  39.132 -14.170  1.00 55.75           N  
ATOM   3265  CA  ALA B  69      27.794  39.367 -13.164  1.00 54.33           C  
ATOM   3266  C   ALA B  69      27.607  38.107 -12.361  1.00 54.13           C  
ATOM   3267  O   ALA B  69      27.396  38.176 -11.145  1.00 57.37           O  
ATOM   3268  CB  ALA B  69      26.484  39.789 -13.804  1.00 51.58           C  
ATOM   3269  N   ASN B  70      27.715  36.949 -13.014  1.00 51.33           N  
ATOM   3270  CA  ASN B  70      27.540  35.688 -12.282  1.00 48.90           C  
ATOM   3271  C   ASN B  70      28.488  35.522 -11.063  1.00 46.58           C  
ATOM   3272  O   ASN B  70      28.177  34.803 -10.094  1.00 48.01           O  
ATOM   3273  CB  ASN B  70      27.657  34.500 -13.239  1.00 47.32           C  
ATOM   3274  CG  ASN B  70      26.351  34.213 -13.966  1.00 48.05           C  
ATOM   3275  OD1 ASN B  70      26.291  33.338 -14.822  1.00 51.60           O  
ATOM   3276  ND2 ASN B  70      25.294  34.945 -13.622  1.00 49.57           N  
ATOM   3277  N   MET B  71      29.623  36.205 -11.098  1.00 40.95           N  
ATOM   3278  CA  MET B  71      30.533  36.122  -9.998  1.00 41.11           C  
ATOM   3279  C   MET B  71      29.768  36.511  -8.715  1.00 45.76           C  
ATOM   3280  O   MET B  71      30.035  35.994  -7.615  1.00 50.08           O  
ATOM   3281  CB  MET B  71      31.690  37.077 -10.223  1.00 37.00           C  
ATOM   3282  CG  MET B  71      32.603  36.679 -11.327  1.00 38.31           C  
ATOM   3283  SD  MET B  71      33.882  37.900 -11.698  1.00 41.35           S  
ATOM   3284  CE  MET B  71      34.922  37.780 -10.280  1.00 39.38           C  
ATOM   3285  N   PHE B  72      28.797  37.418  -8.850  1.00 46.43           N  
ATOM   3286  CA  PHE B  72      28.018  37.893  -7.699  1.00 43.46           C  
ATOM   3287  C   PHE B  72      27.214  36.757  -7.129  1.00 44.37           C  
ATOM   3288  O   PHE B  72      27.104  36.637  -5.897  1.00 46.08           O  
ATOM   3289  CB  PHE B  72      27.093  39.064  -8.097  1.00 40.78           C  
ATOM   3290  CG  PHE B  72      27.850  40.306  -8.518  1.00 40.42           C  
ATOM   3291  CD1 PHE B  72      28.985  40.728  -7.812  1.00 40.78           C  
ATOM   3292  CD2 PHE B  72      27.472  41.039  -9.622  1.00 39.14           C  
ATOM   3293  CE1 PHE B  72      29.722  41.864  -8.216  1.00 38.39           C  
ATOM   3294  CE2 PHE B  72      28.216  42.166 -10.013  1.00 38.27           C  
ATOM   3295  CZ  PHE B  72      29.336  42.571  -9.305  1.00 35.07           C  
ATOM   3296  N   ILE B  73      26.662  35.914  -8.011  1.00 43.04           N  
ATOM   3297  CA  ILE B  73      25.873  34.775  -7.549  1.00 43.43           C  
ATOM   3298  C   ILE B  73      26.778  33.842  -6.774  1.00 43.99           C  
ATOM   3299  O   ILE B  73      26.453  33.428  -5.638  1.00 42.35           O  
ATOM   3300  CB  ILE B  73      25.253  34.037  -8.707  1.00 44.22           C  
ATOM   3301  CG1 ILE B  73      24.183  34.944  -9.325  1.00 47.81           C  
ATOM   3302  CG2 ILE B  73      24.646  32.701  -8.234  1.00 45.45           C  
ATOM   3303  CD1 ILE B  73      23.479  34.347 -10.559  1.00 52.80           C  
ATOM   3304  N   ILE B  74      27.926  33.534  -7.386  1.00 42.06           N  
ATOM   3305  CA  ILE B  74      28.908  32.678  -6.744  1.00 39.86           C  
ATOM   3306  C   ILE B  74      29.245  33.224  -5.343  1.00 37.31           C  
ATOM   3307  O   ILE B  74      29.105  32.503  -4.357  1.00 36.17           O  
ATOM   3308  CB  ILE B  74      30.169  32.547  -7.615  1.00 40.12           C  
ATOM   3309  CG1 ILE B  74      29.774  31.884  -8.944  1.00 41.76           C  
ATOM   3310  CG2 ILE B  74      31.231  31.708  -6.892  1.00 35.35           C  
ATOM   3311  CD1 ILE B  74      30.894  31.795 -10.005  1.00 43.50           C  
ATOM   3312  N   ASN B  75      29.655  34.486  -5.235  1.00 35.46           N  
ATOM   3313  CA  ASN B  75      29.954  35.021  -3.908  1.00 34.87           C  
ATOM   3314  C   ASN B  75      28.724  34.944  -2.962  1.00 36.33           C  
ATOM   3315  O   ASN B  75      28.870  34.761  -1.742  1.00 34.33           O  
ATOM   3316  CB  ASN B  75      30.427  36.459  -3.986  1.00 30.42           C  
ATOM   3317  CG  ASN B  75      30.946  36.951  -2.652  1.00 31.16           C  
ATOM   3318  OD1 ASN B  75      32.003  36.536  -2.225  1.00 27.19           O  
ATOM   3319  ND2 ASN B  75      30.190  37.829  -1.973  1.00 34.84           N  
ATOM   3320  N   LEU B  76      27.516  35.093  -3.512  1.00 37.51           N  
ATOM   3321  CA  LEU B  76      26.299  35.010  -2.696  1.00 37.80           C  
ATOM   3322  C   LEU B  76      26.144  33.569  -2.152  1.00 36.86           C  
ATOM   3323  O   LEU B  76      25.765  33.345  -0.993  1.00 31.25           O  
ATOM   3324  CB  LEU B  76      25.057  35.364  -3.541  1.00 40.30           C  
ATOM   3325  CG  LEU B  76      23.957  36.217  -2.861  1.00 42.63           C  
ATOM   3326  CD1 LEU B  76      22.692  36.049  -3.647  1.00 43.13           C  
ATOM   3327  CD2 LEU B  76      23.668  35.818  -1.409  1.00 43.64           C  
ATOM   3328  N   ALA B  77      26.420  32.599  -3.022  1.00 37.89           N  
ATOM   3329  CA  ALA B  77      26.339  31.182  -2.652  1.00 38.44           C  
ATOM   3330  C   ALA B  77      27.394  30.855  -1.581  1.00 38.47           C  
ATOM   3331  O   ALA B  77      27.106  30.261  -0.532  1.00 38.06           O  
ATOM   3332  CB  ALA B  77      26.552  30.269  -3.910  1.00 35.45           C  
ATOM   3333  N   PHE B  78      28.623  31.254  -1.846  1.00 38.80           N  
ATOM   3334  CA  PHE B  78      29.690  30.973  -0.926  1.00 40.01           C  
ATOM   3335  C   PHE B  78      29.309  31.476   0.454  1.00 40.03           C  
ATOM   3336  O   PHE B  78      29.430  30.757   1.444  1.00 41.10           O  
ATOM   3337  CB  PHE B  78      30.970  31.636  -1.419  1.00 43.74           C  
ATOM   3338  CG  PHE B  78      32.090  31.522  -0.465  1.00 49.52           C  
ATOM   3339  CD1 PHE B  78      32.804  30.333  -0.371  1.00 53.32           C  
ATOM   3340  CD2 PHE B  78      32.392  32.579   0.401  1.00 49.48           C  
ATOM   3341  CE1 PHE B  78      33.810  30.194   0.588  1.00 56.50           C  
ATOM   3342  CE2 PHE B  78      33.387  32.463   1.357  1.00 53.08           C  
ATOM   3343  CZ  PHE B  78      34.103  31.268   1.459  1.00 56.49           C  
ATOM   3344  N   SER B  79      28.843  32.719   0.506  1.00 40.37           N  
ATOM   3345  CA  SER B  79      28.430  33.373   1.756  1.00 39.61           C  
ATOM   3346  C   SER B  79      27.317  32.578   2.453  1.00 37.08           C  
ATOM   3347  O   SER B  79      27.416  32.207   3.629  1.00 30.91           O  
ATOM   3348  CB  SER B  79      27.957  34.814   1.436  1.00 43.42           C  
ATOM   3349  OG  SER B  79      27.566  35.557   2.586  1.00 44.73           O  
ATOM   3350  N   ASP B  80      26.247  32.330   1.706  1.00 40.06           N  
ATOM   3351  CA  ASP B  80      25.103  31.577   2.237  1.00 42.91           C  
ATOM   3352  C   ASP B  80      25.570  30.166   2.615  1.00 43.21           C  
ATOM   3353  O   ASP B  80      25.033  29.557   3.571  1.00 44.29           O  
ATOM   3354  CB  ASP B  80      23.970  31.506   1.205  1.00 41.54           C  
ATOM   3355  CG  ASP B  80      23.301  32.854   0.979  1.00 39.20           C  
ATOM   3356  OD1 ASP B  80      22.718  33.041  -0.107  1.00 40.70           O  
ATOM   3357  OD2 ASP B  80      23.346  33.710   1.884  1.00 36.25           O  
ATOM   3358  N   PHE B  81      26.569  29.652   1.874  1.00 41.00           N  
ATOM   3359  CA  PHE B  81      27.107  28.334   2.180  1.00 38.05           C  
ATOM   3360  C   PHE B  81      27.691  28.367   3.584  1.00 37.35           C  
ATOM   3361  O   PHE B  81      27.295  27.582   4.445  1.00 38.48           O  
ATOM   3362  CB  PHE B  81      28.214  27.934   1.221  1.00 36.41           C  
ATOM   3363  CG  PHE B  81      28.803  26.591   1.540  1.00 35.49           C  
ATOM   3364  CD1 PHE B  81      28.183  25.426   1.115  1.00 36.59           C  
ATOM   3365  CD2 PHE B  81      29.951  26.490   2.302  1.00 35.12           C  
ATOM   3366  CE1 PHE B  81      28.693  24.183   1.442  1.00 32.53           C  
ATOM   3367  CE2 PHE B  81      30.481  25.257   2.640  1.00 33.17           C  
ATOM   3368  CZ  PHE B  81      29.846  24.105   2.206  1.00 36.67           C  
ATOM   3369  N   THR B  82      28.610  29.304   3.807  1.00 37.69           N  
ATOM   3370  CA  THR B  82      29.287  29.441   5.094  1.00 41.06           C  
ATOM   3371  C   THR B  82      28.338  29.685   6.274  1.00 44.55           C  
ATOM   3372  O   THR B  82      28.499  29.099   7.372  1.00 45.68           O  
ATOM   3373  CB  THR B  82      30.328  30.549   5.033  1.00 39.42           C  
ATOM   3374  OG1 THR B  82      31.172  30.344   3.875  1.00 37.67           O  
ATOM   3375  CG2 THR B  82      31.159  30.537   6.295  1.00 36.21           C  
ATOM   3376  N   PHE B  83      27.338  30.533   6.043  1.00 45.41           N  
ATOM   3377  CA  PHE B  83      26.351  30.837   7.077  1.00 43.45           C  
ATOM   3378  C   PHE B  83      25.628  29.549   7.499  1.00 43.34           C  
ATOM   3379  O   PHE B  83      25.464  29.276   8.696  1.00 45.05           O  
ATOM   3380  CB  PHE B  83      25.342  31.860   6.549  1.00 41.80           C  
ATOM   3381  CG  PHE B  83      24.396  32.342   7.585  1.00 40.81           C  
ATOM   3382  CD1 PHE B  83      23.344  31.538   8.029  1.00 42.77           C  
ATOM   3383  CD2 PHE B  83      24.574  33.590   8.157  1.00 43.47           C  
ATOM   3384  CE1 PHE B  83      22.475  31.978   9.045  1.00 42.68           C  
ATOM   3385  CE2 PHE B  83      23.723  34.060   9.177  1.00 44.09           C  
ATOM   3386  CZ  PHE B  83      22.673  33.251   9.623  1.00 44.07           C  
ATOM   3387  N   SER B  84      25.204  28.760   6.515  1.00 40.04           N  
ATOM   3388  CA  SER B  84      24.501  27.511   6.785  1.00 40.77           C  
ATOM   3389  C   SER B  84      25.411  26.497   7.477  1.00 41.94           C  
ATOM   3390  O   SER B  84      24.950  25.683   8.308  1.00 42.81           O  
ATOM   3391  CB  SER B  84      24.010  26.879   5.476  1.00 41.20           C  
ATOM   3392  OG  SER B  84      23.247  27.795   4.681  1.00 45.27           O  
ATOM   3393  N   LEU B  85      26.700  26.530   7.120  1.00 40.70           N  
ATOM   3394  CA  LEU B  85      27.662  25.607   7.679  1.00 36.97           C  
ATOM   3395  C   LEU B  85      27.866  25.944   9.107  1.00 38.02           C  
ATOM   3396  O   LEU B  85      27.637  25.117   9.958  1.00 42.14           O  
ATOM   3397  CB  LEU B  85      28.992  25.726   6.985  1.00 33.21           C  
ATOM   3398  CG  LEU B  85      29.812  24.443   7.003  1.00 35.25           C  
ATOM   3399  CD1 LEU B  85      31.249  24.860   6.944  1.00 40.51           C  
ATOM   3400  CD2 LEU B  85      29.562  23.605   8.245  1.00 33.54           C  
ATOM   3401  N   VAL B  86      28.278  27.179   9.366  1.00 39.17           N  
ATOM   3402  CA  VAL B  86      28.575  27.636  10.731  1.00 40.96           C  
ATOM   3403  C   VAL B  86      27.370  27.778  11.680  1.00 42.19           C  
ATOM   3404  O   VAL B  86      27.437  27.438  12.862  1.00 43.18           O  
ATOM   3405  CB  VAL B  86      29.382  29.014  10.704  1.00 39.63           C  
ATOM   3406  CG1 VAL B  86      29.784  29.461  12.093  1.00 34.15           C  
ATOM   3407  CG2 VAL B  86      30.653  28.866   9.912  1.00 42.14           C  
ATOM   3408  N   ASN B  87      26.255  28.260  11.173  1.00 43.75           N  
ATOM   3409  CA  ASN B  87      25.132  28.461  12.059  1.00 44.44           C  
ATOM   3410  C   ASN B  87      24.271  27.258  12.374  1.00 42.48           C  
ATOM   3411  O   ASN B  87      23.402  27.330  13.244  1.00 43.24           O  
ATOM   3412  CB  ASN B  87      24.269  29.591  11.515  1.00 46.13           C  
ATOM   3413  CG  ASN B  87      24.925  30.928  11.664  1.00 49.44           C  
ATOM   3414  OD1 ASN B  87      24.727  31.622  12.685  1.00 50.58           O  
ATOM   3415  ND2 ASN B  87      25.740  31.312  10.653  1.00 51.53           N  
ATOM   3416  N   GLY B  88      24.498  26.163  11.670  1.00 41.04           N  
ATOM   3417  CA  GLY B  88      23.703  24.974  11.917  1.00 42.93           C  
ATOM   3418  C   GLY B  88      24.446  23.890  12.700  1.00 44.19           C  
ATOM   3419  O   GLY B  88      24.674  23.997  13.932  1.00 43.74           O  
ATOM   3420  N   PHE B  89      24.826  22.828  11.980  1.00 42.90           N  
ATOM   3421  CA  PHE B  89      25.544  21.718  12.580  1.00 40.81           C  
ATOM   3422  C   PHE B  89      27.044  21.916  12.402  1.00 38.09           C  
ATOM   3423  O   PHE B  89      27.496  22.249  11.321  1.00 36.28           O  
ATOM   3424  CB  PHE B  89      25.120  20.418  11.913  1.00 45.10           C  
ATOM   3425  CG  PHE B  89      25.977  19.254  12.308  1.00 50.78           C  
ATOM   3426  CD1 PHE B  89      27.146  18.952  11.601  1.00 52.71           C  
ATOM   3427  CD2 PHE B  89      25.679  18.518  13.446  1.00 49.89           C  
ATOM   3428  CE1 PHE B  89      27.998  17.942  12.030  1.00 52.01           C  
ATOM   3429  CE2 PHE B  89      26.523  17.510  13.882  1.00 49.60           C  
ATOM   3430  CZ  PHE B  89      27.688  17.216  13.179  1.00 50.90           C  
ATOM   3431  N   PRO B  90      27.835  21.638  13.439  1.00 38.52           N  
ATOM   3432  CA  PRO B  90      27.450  21.131  14.755  1.00 41.70           C  
ATOM   3433  C   PRO B  90      27.202  22.162  15.889  1.00 42.21           C  
ATOM   3434  O   PRO B  90      26.537  21.874  16.903  1.00 42.36           O  
ATOM   3435  CB  PRO B  90      28.631  20.209  15.100  1.00 42.08           C  
ATOM   3436  CG  PRO B  90      29.784  21.009  14.642  1.00 38.37           C  
ATOM   3437  CD  PRO B  90      29.295  21.465  13.260  1.00 39.96           C  
ATOM   3438  N   LEU B  91      27.756  23.355  15.735  1.00 42.58           N  
ATOM   3439  CA  LEU B  91      27.626  24.376  16.774  1.00 40.21           C  
ATOM   3440  C   LEU B  91      26.242  24.507  17.388  1.00 40.77           C  
ATOM   3441  O   LEU B  91      26.088  24.265  18.587  1.00 41.11           O  
ATOM   3442  CB  LEU B  91      28.111  25.736  16.257  1.00 33.39           C  
ATOM   3443  CG  LEU B  91      29.597  25.687  15.955  1.00 27.67           C  
ATOM   3444  CD1 LEU B  91      30.067  27.103  15.747  1.00 23.05           C  
ATOM   3445  CD2 LEU B  91      30.366  24.999  17.113  1.00 25.71           C  
ATOM   3446  N   MET B  92      25.230  24.854  16.598  1.00 40.78           N  
ATOM   3447  CA  MET B  92      23.930  25.013  17.207  1.00 41.82           C  
ATOM   3448  C   MET B  92      23.208  23.687  17.437  1.00 42.25           C  
ATOM   3449  O   MET B  92      22.674  23.419  18.536  1.00 42.35           O  
ATOM   3450  CB  MET B  92      23.033  25.968  16.398  1.00 40.84           C  
ATOM   3451  CG  MET B  92      21.759  26.329  17.199  1.00 40.23           C  
ATOM   3452  SD  MET B  92      20.485  27.246  16.375  1.00 42.26           S  
ATOM   3453  CE  MET B  92      19.394  27.681  17.661  1.00 33.73           C  
ATOM   3454  N   THR B  93      23.204  22.831  16.428  1.00 42.66           N  
ATOM   3455  CA  THR B  93      22.488  21.567  16.578  1.00 45.34           C  
ATOM   3456  C   THR B  93      22.857  20.811  17.868  1.00 45.09           C  
ATOM   3457  O   THR B  93      22.013  20.581  18.721  1.00 43.55           O  
ATOM   3458  CB  THR B  93      22.689  20.643  15.352  1.00 45.17           C  
ATOM   3459  OG1 THR B  93      22.203  21.272  14.151  1.00 45.22           O  
ATOM   3460  CG2 THR B  93      21.876  19.393  15.557  1.00 48.59           C  
ATOM   3461  N   ILE B  94      24.122  20.441  18.006  1.00 46.58           N  
ATOM   3462  CA  ILE B  94      24.594  19.726  19.196  1.00 47.61           C  
ATOM   3463  C   ILE B  94      24.281  20.471  20.528  1.00 50.15           C  
ATOM   3464  O   ILE B  94      24.064  19.843  21.599  1.00 51.07           O  
ATOM   3465  CB  ILE B  94      26.144  19.440  19.089  1.00 45.85           C  
ATOM   3466  CG1 ILE B  94      26.429  18.627  17.814  1.00 44.06           C  
ATOM   3467  CG2 ILE B  94      26.648  18.680  20.309  1.00 41.69           C  
ATOM   3468  CD1 ILE B  94      25.585  17.385  17.671  1.00 47.43           C  
ATOM   3469  N   SER B  95      24.266  21.805  20.477  1.00 51.06           N  
ATOM   3470  CA  SER B  95      23.982  22.599  21.674  1.00 48.43           C  
ATOM   3471  C   SER B  95      22.520  22.404  22.012  1.00 48.05           C  
ATOM   3472  O   SER B  95      22.180  22.304  23.178  1.00 48.33           O  
ATOM   3473  CB  SER B  95      24.258  24.090  21.436  1.00 48.51           C  
ATOM   3474  OG  SER B  95      25.644  24.362  21.317  1.00 47.00           O  
ATOM   3475  N   CYS B  96      21.655  22.351  20.994  1.00 45.94           N  
ATOM   3476  CA  CYS B  96      20.233  22.158  21.239  1.00 43.96           C  
ATOM   3477  C   CYS B  96      19.984  20.797  21.884  1.00 44.64           C  
ATOM   3478  O   CYS B  96      19.352  20.685  22.926  1.00 47.35           O  
ATOM   3479  CB  CYS B  96      19.449  22.245  19.937  1.00 41.90           C  
ATOM   3480  SG  CYS B  96      19.366  23.847  19.249  1.00 42.36           S  
ATOM   3481  N   PHE B  97      20.501  19.754  21.263  1.00 44.65           N  
ATOM   3482  CA  PHE B  97      20.323  18.397  21.760  1.00 44.11           C  
ATOM   3483  C   PHE B  97      20.820  18.240  23.186  1.00 45.32           C  
ATOM   3484  O   PHE B  97      20.400  17.331  23.905  1.00 46.64           O  
ATOM   3485  CB  PHE B  97      21.049  17.406  20.839  1.00 44.54           C  
ATOM   3486  CG  PHE B  97      20.459  17.317  19.459  1.00 46.29           C  
ATOM   3487  CD1 PHE B  97      21.192  16.801  18.399  1.00 44.84           C  
ATOM   3488  CD2 PHE B  97      19.149  17.759  19.220  1.00 48.48           C  
ATOM   3489  CE1 PHE B  97      20.619  16.725  17.108  1.00 50.05           C  
ATOM   3490  CE2 PHE B  97      18.570  17.690  17.930  1.00 49.75           C  
ATOM   3491  CZ  PHE B  97      19.299  17.175  16.873  1.00 49.27           C  
ATOM   3492  N   LEU B  98      21.731  19.120  23.596  1.00 46.80           N  
ATOM   3493  CA  LEU B  98      22.285  19.085  24.960  1.00 45.97           C  
ATOM   3494  C   LEU B  98      21.751  20.228  25.815  1.00 46.54           C  
ATOM   3495  O   LEU B  98      22.186  20.402  26.949  1.00 46.69           O  
ATOM   3496  CB  LEU B  98      23.813  19.170  24.916  1.00 43.38           C  
ATOM   3497  CG  LEU B  98      24.583  17.855  24.966  1.00 41.56           C  
ATOM   3498  CD1 LEU B  98      24.025  16.927  23.914  1.00 41.12           C  
ATOM   3499  CD2 LEU B  98      26.082  18.123  24.761  1.00 40.37           C  
ATOM   3500  N   LYS B  99      20.817  21.004  25.255  1.00 48.06           N  
ATOM   3501  CA  LYS B  99      20.227  22.158  25.948  1.00 49.95           C  
ATOM   3502  C   LYS B  99      21.361  22.965  26.615  1.00 50.26           C  
ATOM   3503  O   LYS B  99      21.291  23.341  27.801  1.00 52.50           O  
ATOM   3504  CB  LYS B  99      19.213  21.659  27.000  1.00 50.94           C  
ATOM   3505  CG  LYS B  99      18.286  20.578  26.441  1.00 52.79           C  
ATOM   3506  CD  LYS B  99      17.120  20.233  27.357  1.00 53.81           C  
ATOM   3507  CE  LYS B  99      17.543  19.785  28.744  1.00 52.37           C  
ATOM   3508  NZ  LYS B  99      16.266  19.548  29.477  1.00 54.47           N  
ATOM   3509  N   LYS B 100      22.416  23.232  25.852  1.00 48.87           N  
ATOM   3510  CA  LYS B 100      23.556  23.929  26.409  1.00 46.46           C  
ATOM   3511  C   LYS B 100      24.583  24.208  25.312  1.00 46.26           C  
ATOM   3512  O   LYS B 100      24.853  23.353  24.463  1.00 46.25           O  
ATOM   3513  CB  LYS B 100      24.169  23.037  27.470  1.00 46.54           C  
ATOM   3514  CG  LYS B 100      25.196  23.701  28.293  1.00 50.79           C  
ATOM   3515  CD  LYS B 100      24.546  24.666  29.208  1.00 52.29           C  
ATOM   3516  CE  LYS B 100      24.050  23.923  30.386  1.00 54.71           C  
ATOM   3517  NZ  LYS B 100      23.500  24.896  31.387  1.00 58.57           N  
ATOM   3518  N   TRP B 101      25.132  25.416  25.303  1.00 44.61           N  
ATOM   3519  CA  TRP B 101      26.152  25.742  24.318  1.00 41.75           C  
ATOM   3520  C   TRP B 101      27.443  25.274  24.980  1.00 42.71           C  
ATOM   3521  O   TRP B 101      27.994  25.964  25.838  1.00 40.04           O  
ATOM   3522  CB  TRP B 101      26.205  27.247  24.066  1.00 35.66           C  
ATOM   3523  CG  TRP B 101      27.444  27.665  23.284  1.00 30.72           C  
ATOM   3524  CD1 TRP B 101      28.690  27.962  23.783  1.00 27.89           C  
ATOM   3525  CD2 TRP B 101      27.526  27.868  21.870  1.00 26.05           C  
ATOM   3526  NE1 TRP B 101      29.529  28.352  22.758  1.00 25.36           N  
ATOM   3527  CE2 TRP B 101      28.838  28.294  21.580  1.00 23.72           C  
ATOM   3528  CE3 TRP B 101      26.612  27.740  20.829  1.00 24.01           C  
ATOM   3529  CZ2 TRP B 101      29.247  28.582  20.310  1.00 24.71           C  
ATOM   3530  CZ3 TRP B 101      27.016  28.034  19.565  1.00 24.75           C  
ATOM   3531  CH2 TRP B 101      28.325  28.450  19.309  1.00 28.18           C  
ATOM   3532  N   ILE B 102      27.932  24.107  24.587  1.00 44.78           N  
ATOM   3533  CA  ILE B 102      29.143  23.619  25.229  1.00 48.90           C  
ATOM   3534  C   ILE B 102      30.478  23.908  24.508  1.00 49.48           C  
ATOM   3535  O   ILE B 102      31.549  23.415  24.948  1.00 51.40           O  
ATOM   3536  CB  ILE B 102      29.029  22.059  25.568  1.00 49.85           C  
ATOM   3537  CG1 ILE B 102      29.550  21.156  24.411  1.00 50.11           C  
ATOM   3538  CG2 ILE B 102      27.581  21.731  25.969  1.00 49.52           C  
ATOM   3539  CD1 ILE B 102      28.789  21.172  23.115  1.00 51.49           C  
ATOM   3540  N   PHE B 103      30.433  24.720  23.444  1.00 46.32           N  
ATOM   3541  CA  PHE B 103      31.635  25.028  22.652  1.00 44.47           C  
ATOM   3542  C   PHE B 103      32.522  26.235  23.113  1.00 45.70           C  
ATOM   3543  O   PHE B 103      33.560  26.559  22.506  1.00 45.06           O  
ATOM   3544  CB  PHE B 103      31.192  25.140  21.180  1.00 41.28           C  
ATOM   3545  CG  PHE B 103      30.418  23.936  20.711  1.00 41.33           C  
ATOM   3546  CD1 PHE B 103      31.049  22.698  20.567  1.00 41.41           C  
ATOM   3547  CD2 PHE B 103      29.042  24.015  20.482  1.00 42.68           C  
ATOM   3548  CE1 PHE B 103      30.319  21.545  20.206  1.00 40.37           C  
ATOM   3549  CE2 PHE B 103      28.283  22.869  20.115  1.00 42.22           C  
ATOM   3550  CZ  PHE B 103      28.923  21.634  19.978  1.00 42.86           C  
ATOM   3551  N   GLY B 104      32.134  26.876  24.217  1.00 45.81           N  
ATOM   3552  CA  GLY B 104      32.905  28.004  24.707  1.00 45.27           C  
ATOM   3553  C   GLY B 104      32.579  29.388  24.131  1.00 45.94           C  
ATOM   3554  O   GLY B 104      31.786  29.610  23.169  1.00 39.90           O  
ATOM   3555  N   PHE B 105      33.244  30.344  24.774  1.00 48.44           N  
ATOM   3556  CA  PHE B 105      33.110  31.755  24.438  1.00 48.92           C  
ATOM   3557  C   PHE B 105      33.686  32.088  23.056  1.00 46.11           C  
ATOM   3558  O   PHE B 105      33.052  32.772  22.255  1.00 45.34           O  
ATOM   3559  CB  PHE B 105      33.801  32.619  25.517  1.00 53.89           C  
ATOM   3560  CG  PHE B 105      33.285  34.047  25.585  1.00 57.91           C  
ATOM   3561  CD1 PHE B 105      33.996  35.037  26.290  1.00 57.37           C  
ATOM   3562  CD2 PHE B 105      32.078  34.406  24.936  1.00 60.02           C  
ATOM   3563  CE1 PHE B 105      33.521  36.356  26.344  1.00 55.05           C  
ATOM   3564  CE2 PHE B 105      31.594  35.724  24.983  1.00 57.58           C  
ATOM   3565  CZ  PHE B 105      32.321  36.702  25.691  1.00 54.85           C  
ATOM   3566  N   ALA B 106      34.883  31.609  22.778  1.00 43.59           N  
ATOM   3567  CA  ALA B 106      35.480  31.900  21.509  1.00 42.32           C  
ATOM   3568  C   ALA B 106      34.621  31.389  20.384  1.00 41.91           C  
ATOM   3569  O   ALA B 106      34.436  32.086  19.377  1.00 43.41           O  
ATOM   3570  CB  ALA B 106      36.834  31.277  21.433  1.00 48.03           C  
ATOM   3571  N   ALA B 107      34.110  30.168  20.532  1.00 40.74           N  
ATOM   3572  CA  ALA B 107      33.275  29.584  19.473  1.00 41.62           C  
ATOM   3573  C   ALA B 107      32.093  30.492  19.239  1.00 42.56           C  
ATOM   3574  O   ALA B 107      31.764  30.812  18.093  1.00 41.11           O  
ATOM   3575  CB  ALA B 107      32.794  28.187  19.864  1.00 42.14           C  
ATOM   3576  N   CYS B 108      31.470  30.903  20.354  1.00 44.44           N  
ATOM   3577  CA  CYS B 108      30.317  31.813  20.364  1.00 42.95           C  
ATOM   3578  C   CYS B 108      30.626  33.123  19.622  1.00 41.51           C  
ATOM   3579  O   CYS B 108      29.834  33.558  18.807  1.00 42.07           O  
ATOM   3580  CB  CYS B 108      29.921  32.085  21.805  1.00 42.95           C  
ATOM   3581  SG  CYS B 108      28.587  33.299  22.050  1.00 45.62           S  
ATOM   3582  N   LYS B 109      31.770  33.748  19.899  1.00 38.76           N  
ATOM   3583  CA  LYS B 109      32.136  34.949  19.181  1.00 38.72           C  
ATOM   3584  C   LYS B 109      32.259  34.649  17.699  1.00 41.35           C  
ATOM   3585  O   LYS B 109      31.649  35.344  16.888  1.00 44.49           O  
ATOM   3586  CB  LYS B 109      33.455  35.481  19.667  1.00 39.27           C  
ATOM   3587  CG  LYS B 109      33.445  35.662  21.153  1.00 43.37           C  
ATOM   3588  CD  LYS B 109      34.649  36.449  21.619  1.00 44.58           C  
ATOM   3589  CE  LYS B 109      34.566  36.604  23.127  1.00 45.63           C  
ATOM   3590  NZ  LYS B 109      35.630  37.527  23.587  1.00 50.87           N  
ATOM   3591  N   VAL B 110      33.052  33.628  17.337  1.00 40.29           N  
ATOM   3592  CA  VAL B 110      33.219  33.250  15.935  1.00 37.91           C  
ATOM   3593  C   VAL B 110      31.865  33.027  15.267  1.00 39.24           C  
ATOM   3594  O   VAL B 110      31.602  33.600  14.211  1.00 42.65           O  
ATOM   3595  CB  VAL B 110      34.006  31.963  15.788  1.00 37.22           C  
ATOM   3596  CG1 VAL B 110      34.066  31.552  14.294  1.00 33.21           C  
ATOM   3597  CG2 VAL B 110      35.372  32.159  16.360  1.00 38.66           C  
ATOM   3598  N   TYR B 111      31.014  32.205  15.875  1.00 36.19           N  
ATOM   3599  CA  TYR B 111      29.697  31.925  15.319  1.00 35.90           C  
ATOM   3600  C   TYR B 111      28.957  33.256  15.035  1.00 36.94           C  
ATOM   3601  O   TYR B 111      28.514  33.581  13.907  1.00 36.68           O  
ATOM   3602  CB  TYR B 111      28.937  31.086  16.341  1.00 37.02           C  
ATOM   3603  CG  TYR B 111      27.555  30.633  15.956  1.00 38.43           C  
ATOM   3604  CD1 TYR B 111      27.328  29.326  15.541  1.00 39.79           C  
ATOM   3605  CD2 TYR B 111      26.456  31.489  16.095  1.00 39.95           C  
ATOM   3606  CE1 TYR B 111      26.037  28.869  15.281  1.00 42.43           C  
ATOM   3607  CE2 TYR B 111      25.153  31.049  15.835  1.00 41.90           C  
ATOM   3608  CZ  TYR B 111      24.950  29.728  15.431  1.00 42.80           C  
ATOM   3609  OH  TYR B 111      23.678  29.235  15.195  1.00 40.73           O  
ATOM   3610  N   GLY B 112      28.866  34.068  16.067  1.00 36.49           N  
ATOM   3611  CA  GLY B 112      28.147  35.311  15.900  1.00 35.90           C  
ATOM   3612  C   GLY B 112      28.780  36.142  14.833  1.00 34.92           C  
ATOM   3613  O   GLY B 112      28.121  36.716  13.981  1.00 37.47           O  
ATOM   3614  N   PHE B 113      30.087  36.195  14.882  1.00 34.72           N  
ATOM   3615  CA  PHE B 113      30.819  37.001  13.952  1.00 36.60           C  
ATOM   3616  C   PHE B 113      30.546  36.552  12.544  1.00 37.64           C  
ATOM   3617  O   PHE B 113      30.271  37.371  11.662  1.00 37.63           O  
ATOM   3618  CB  PHE B 113      32.314  36.901  14.274  1.00 39.40           C  
ATOM   3619  CG  PHE B 113      33.216  37.633  13.303  1.00 39.98           C  
ATOM   3620  CD1 PHE B 113      32.874  38.895  12.818  1.00 40.34           C  
ATOM   3621  CD2 PHE B 113      34.465  37.116  12.985  1.00 38.26           C  
ATOM   3622  CE1 PHE B 113      33.754  39.633  12.055  1.00 37.43           C  
ATOM   3623  CE2 PHE B 113      35.343  37.849  12.225  1.00 38.65           C  
ATOM   3624  CZ  PHE B 113      34.985  39.115  11.762  1.00 39.41           C  
ATOM   3625  N   ILE B 114      30.623  35.245  12.336  1.00 37.73           N  
ATOM   3626  CA  ILE B 114      30.434  34.700  11.008  1.00 38.41           C  
ATOM   3627  C   ILE B 114      28.991  34.919  10.576  1.00 40.10           C  
ATOM   3628  O   ILE B 114      28.741  35.397   9.463  1.00 43.71           O  
ATOM   3629  CB  ILE B 114      30.842  33.201  10.943  1.00 36.96           C  
ATOM   3630  CG1 ILE B 114      32.358  33.072  10.852  1.00 33.96           C  
ATOM   3631  CG2 ILE B 114      30.225  32.537   9.752  1.00 37.05           C  
ATOM   3632  CD1 ILE B 114      32.773  31.683  10.523  1.00 36.56           C  
ATOM   3633  N   GLY B 115      28.026  34.599  11.428  1.00 39.20           N  
ATOM   3634  CA  GLY B 115      26.653  34.845  11.012  1.00 39.75           C  
ATOM   3635  C   GLY B 115      26.507  36.301  10.563  1.00 41.05           C  
ATOM   3636  O   GLY B 115      25.915  36.622   9.520  1.00 40.39           O  
ATOM   3637  N   GLY B 116      27.079  37.199  11.360  1.00 41.41           N  
ATOM   3638  CA  GLY B 116      27.024  38.609  11.044  1.00 41.10           C  
ATOM   3639  C   GLY B 116      27.679  39.042   9.749  1.00 39.70           C  
ATOM   3640  O   GLY B 116      27.042  39.709   8.959  1.00 42.32           O  
ATOM   3641  N   ILE B 117      28.929  38.661   9.510  1.00 38.61           N  
ATOM   3642  CA  ILE B 117      29.594  39.112   8.291  1.00 38.56           C  
ATOM   3643  C   ILE B 117      28.899  38.606   7.029  1.00 39.85           C  
ATOM   3644  O   ILE B 117      28.782  39.353   6.041  1.00 40.46           O  
ATOM   3645  CB  ILE B 117      31.133  38.740   8.272  1.00 36.35           C  
ATOM   3646  CG1 ILE B 117      31.378  37.449   7.564  1.00 33.55           C  
ATOM   3647  CG2 ILE B 117      31.648  38.511   9.639  1.00 36.57           C  
ATOM   3648  CD1 ILE B 117      31.612  37.687   6.118  1.00 42.72           C  
ATOM   3649  N   PHE B 118      28.409  37.360   7.062  1.00 39.64           N  
ATOM   3650  CA  PHE B 118      27.760  36.775   5.886  1.00 37.55           C  
ATOM   3651  C   PHE B 118      26.297  37.173   5.720  1.00 41.13           C  
ATOM   3652  O   PHE B 118      25.739  37.085   4.611  1.00 42.66           O  
ATOM   3653  CB  PHE B 118      27.993  35.267   5.868  1.00 31.16           C  
ATOM   3654  CG  PHE B 118      29.409  34.913   5.527  1.00 25.24           C  
ATOM   3655  CD1 PHE B 118      29.947  35.297   4.301  1.00 23.01           C  
ATOM   3656  CD2 PHE B 118      30.235  34.313   6.450  1.00 20.67           C  
ATOM   3657  CE1 PHE B 118      31.290  35.091   4.017  1.00 22.50           C  
ATOM   3658  CE2 PHE B 118      31.572  34.106   6.173  1.00 20.00           C  
ATOM   3659  CZ  PHE B 118      32.100  34.494   4.963  1.00 20.00           C  
ATOM   3660  N   GLY B 119      25.675  37.638   6.810  1.00 43.27           N  
ATOM   3661  CA  GLY B 119      24.316  38.151   6.691  1.00 44.48           C  
ATOM   3662  C   GLY B 119      24.458  39.451   5.868  1.00 44.62           C  
ATOM   3663  O   GLY B 119      23.778  39.679   4.870  1.00 43.81           O  
ATOM   3664  N   PHE B 120      25.386  40.296   6.298  1.00 44.03           N  
ATOM   3665  CA  PHE B 120      25.651  41.542   5.632  1.00 43.80           C  
ATOM   3666  C   PHE B 120      26.141  41.272   4.247  1.00 47.08           C  
ATOM   3667  O   PHE B 120      25.876  42.087   3.348  1.00 51.78           O  
ATOM   3668  CB  PHE B 120      26.745  42.320   6.343  1.00 41.29           C  
ATOM   3669  CG  PHE B 120      26.369  42.770   7.708  1.00 41.70           C  
ATOM   3670  CD1 PHE B 120      27.344  42.899   8.716  1.00 41.42           C  
ATOM   3671  CD2 PHE B 120      25.042  43.039   8.017  1.00 40.41           C  
ATOM   3672  CE1 PHE B 120      27.000  43.286  10.040  1.00 40.35           C  
ATOM   3673  CE2 PHE B 120      24.684  43.427   9.325  1.00 43.30           C  
ATOM   3674  CZ  PHE B 120      25.674  43.553  10.349  1.00 41.40           C  
ATOM   3675  N   MET B 121      26.868  40.156   4.059  1.00 48.18           N  
ATOM   3676  CA  MET B 121      27.476  39.842   2.751  1.00 47.58           C  
ATOM   3677  C   MET B 121      26.461  39.540   1.688  1.00 47.04           C  
ATOM   3678  O   MET B 121      26.638  39.929   0.516  1.00 47.00           O  
ATOM   3679  CB  MET B 121      28.473  38.684   2.848  1.00 48.29           C  
ATOM   3680  CG  MET B 121      29.214  38.436   1.520  1.00 52.08           C  
ATOM   3681  SD  MET B 121      30.941  37.807   1.786  1.00 54.86           S  
ATOM   3682  CE  MET B 121      30.879  36.424   0.834  1.00 59.31           C  
ATOM   3683  N   SER B 122      25.378  38.884   2.102  1.00 46.11           N  
ATOM   3684  CA  SER B 122      24.326  38.542   1.151  1.00 44.91           C  
ATOM   3685  C   SER B 122      23.520  39.739   0.619  1.00 43.40           C  
ATOM   3686  O   SER B 122      23.286  39.798  -0.580  1.00 44.65           O  
ATOM   3687  CB  SER B 122      23.411  37.469   1.744  1.00 45.18           C  
ATOM   3688  OG  SER B 122      24.092  36.218   1.781  1.00 41.10           O  
ATOM   3689  N   ILE B 123      23.102  40.678   1.473  1.00 41.21           N  
ATOM   3690  CA  ILE B 123      22.371  41.838   0.975  1.00 40.17           C  
ATOM   3691  C   ILE B 123      23.303  42.732   0.151  1.00 40.97           C  
ATOM   3692  O   ILE B 123      22.926  43.190  -0.937  1.00 41.60           O  
ATOM   3693  CB  ILE B 123      21.788  42.720   2.090  1.00 39.56           C  
ATOM   3694  CG1 ILE B 123      22.244  42.220   3.441  1.00 39.37           C  
ATOM   3695  CG2 ILE B 123      20.279  42.769   1.967  1.00 38.23           C  
ATOM   3696  CD1 ILE B 123      21.760  43.057   4.568  1.00 42.08           C  
ATOM   3697  N   MET B 124      24.513  42.986   0.648  1.00 39.95           N  
ATOM   3698  CA  MET B 124      25.416  43.848  -0.094  1.00 41.65           C  
ATOM   3699  C   MET B 124      25.743  43.228  -1.453  1.00 43.80           C  
ATOM   3700  O   MET B 124      25.953  43.947  -2.437  1.00 46.73           O  
ATOM   3701  CB  MET B 124      26.698  44.109   0.690  1.00 42.88           C  
ATOM   3702  CG  MET B 124      27.534  45.263   0.094  1.00 42.77           C  
ATOM   3703  SD  MET B 124      26.513  46.743  -0.320  1.00 46.22           S  
ATOM   3704  CE  MET B 124      26.175  47.454   1.312  1.00 38.84           C  
ATOM   3705  N   THR B 125      25.797  41.897  -1.521  1.00 41.91           N  
ATOM   3706  CA  THR B 125      26.061  41.251  -2.789  1.00 39.38           C  
ATOM   3707  C   THR B 125      24.830  41.458  -3.623  1.00 40.48           C  
ATOM   3708  O   THR B 125      24.917  41.627  -4.812  1.00 44.30           O  
ATOM   3709  CB  THR B 125      26.319  39.760  -2.608  1.00 38.36           C  
ATOM   3710  OG1 THR B 125      27.564  39.610  -1.922  1.00 42.18           O  
ATOM   3711  CG2 THR B 125      26.412  39.031  -3.951  1.00 34.06           C  
ATOM   3712  N   MET B 126      23.670  41.457  -2.997  1.00 41.07           N  
ATOM   3713  CA  MET B 126      22.440  41.679  -3.734  1.00 43.12           C  
ATOM   3714  C   MET B 126      22.398  43.132  -4.242  1.00 44.93           C  
ATOM   3715  O   MET B 126      21.927  43.411  -5.363  1.00 46.16           O  
ATOM   3716  CB  MET B 126      21.240  41.371  -2.838  1.00 44.16           C  
ATOM   3717  CG  MET B 126      20.943  39.859  -2.734  1.00 46.10           C  
ATOM   3718  SD  MET B 126      19.633  39.383  -1.548  1.00 49.38           S  
ATOM   3719  CE  MET B 126      20.396  38.079  -0.672  1.00 50.53           C  
ATOM   3720  N   ALA B 127      22.890  44.068  -3.438  1.00 45.42           N  
ATOM   3721  CA  ALA B 127      22.916  45.455  -3.892  1.00 46.03           C  
ATOM   3722  C   ALA B 127      23.837  45.515  -5.111  1.00 45.66           C  
ATOM   3723  O   ALA B 127      23.550  46.230  -6.073  1.00 46.63           O  
ATOM   3724  CB  ALA B 127      23.430  46.393  -2.786  1.00 47.20           C  
ATOM   3725  N   MET B 128      24.941  44.769  -5.068  1.00 45.06           N  
ATOM   3726  CA  MET B 128      25.863  44.726  -6.201  1.00 45.94           C  
ATOM   3727  C   MET B 128      25.152  44.182  -7.462  1.00 46.55           C  
ATOM   3728  O   MET B 128      25.351  44.669  -8.584  1.00 48.50           O  
ATOM   3729  CB  MET B 128      27.069  43.860  -5.873  1.00 43.17           C  
ATOM   3730  CG  MET B 128      27.892  44.413  -4.773  1.00 47.67           C  
ATOM   3731  SD  MET B 128      28.314  46.134  -5.041  1.00 56.10           S  
ATOM   3732  CE  MET B 128      26.996  46.977  -4.122  1.00 53.47           C  
ATOM   3733  N   ILE B 129      24.317  43.174  -7.272  1.00 45.93           N  
ATOM   3734  CA  ILE B 129      23.571  42.598  -8.371  1.00 47.33           C  
ATOM   3735  C   ILE B 129      22.607  43.645  -8.928  1.00 51.34           C  
ATOM   3736  O   ILE B 129      22.526  43.867 -10.155  1.00 51.18           O  
ATOM   3737  CB  ILE B 129      22.784  41.385  -7.884  1.00 44.84           C  
ATOM   3738  CG1 ILE B 129      23.764  40.209  -7.732  1.00 47.20           C  
ATOM   3739  CG2 ILE B 129      21.626  41.080  -8.814  1.00 36.32           C  
ATOM   3740  CD1 ILE B 129      23.222  39.034  -6.862  1.00 43.57           C  
ATOM   3741  N   SER B 130      21.889  44.317  -8.020  1.00 54.84           N  
ATOM   3742  CA  SER B 130      20.900  45.338  -8.429  1.00 54.53           C  
ATOM   3743  C   SER B 130      21.578  46.399  -9.264  1.00 52.95           C  
ATOM   3744  O   SER B 130      21.046  46.821 -10.293  1.00 51.54           O  
ATOM   3745  CB  SER B 130      20.232  45.955  -7.201  1.00 54.58           C  
ATOM   3746  OG  SER B 130      21.200  46.343  -6.258  1.00 53.13           O  
ATOM   3747  N   ILE B 131      22.762  46.802  -8.817  1.00 51.46           N  
ATOM   3748  CA  ILE B 131      23.556  47.780  -9.542  1.00 52.60           C  
ATOM   3749  C   ILE B 131      23.724  47.319 -11.024  1.00 57.84           C  
ATOM   3750  O   ILE B 131      23.578  48.115 -11.987  1.00 60.29           O  
ATOM   3751  CB  ILE B 131      24.956  47.954  -8.870  1.00 46.66           C  
ATOM   3752  CG1 ILE B 131      24.799  48.665  -7.528  1.00 38.45           C  
ATOM   3753  CG2 ILE B 131      25.913  48.702  -9.803  1.00 44.03           C  
ATOM   3754  CD1 ILE B 131      26.085  48.903  -6.868  1.00 30.98           C  
ATOM   3755  N   ASP B 132      24.032  46.031 -11.207  1.00 60.42           N  
ATOM   3756  CA  ASP B 132      24.202  45.473 -12.556  1.00 61.57           C  
ATOM   3757  C   ASP B 132      22.836  45.441 -13.267  1.00 64.64           C  
ATOM   3758  O   ASP B 132      22.686  45.947 -14.395  1.00 66.80           O  
ATOM   3759  CB  ASP B 132      24.764  44.056 -12.482  1.00 56.66           C  
ATOM   3760  CG  ASP B 132      24.993  43.460 -13.847  1.00 54.88           C  
ATOM   3761  OD1 ASP B 132      24.577  42.307 -14.094  1.00 51.55           O  
ATOM   3762  OD2 ASP B 132      25.593  44.160 -14.680  1.00 55.22           O  
ATOM   3763  N   ARG B 133      21.852  44.838 -12.596  1.00 64.93           N  
ATOM   3764  CA  ARG B 133      20.508  44.747 -13.115  1.00 64.49           C  
ATOM   3765  C   ARG B 133      20.042  46.123 -13.585  1.00 66.80           C  
ATOM   3766  O   ARG B 133      19.364  46.244 -14.604  1.00 68.58           O  
ATOM   3767  CB  ARG B 133      19.584  44.229 -12.025  1.00 61.98           C  
ATOM   3768  CG  ARG B 133      18.945  42.899 -12.355  1.00 61.86           C  
ATOM   3769  CD  ARG B 133      19.986  41.871 -12.761  1.00 62.12           C  
ATOM   3770  NE  ARG B 133      19.954  41.527 -14.187  1.00 61.74           N  
ATOM   3771  CZ  ARG B 133      20.997  41.652 -15.014  1.00 59.74           C  
ATOM   3772  NH1 ARG B 133      22.163  42.128 -14.550  1.00 54.59           N  
ATOM   3773  NH2 ARG B 133      20.874  41.288 -16.295  1.00 53.00           N  
ATOM   3774  N   TYR B 134      20.411  47.165 -12.846  1.00 68.23           N  
ATOM   3775  CA  TYR B 134      20.018  48.519 -13.221  1.00 69.37           C  
ATOM   3776  C   TYR B 134      20.807  49.047 -14.438  1.00 70.91           C  
ATOM   3777  O   TYR B 134      20.306  49.900 -15.188  1.00 72.74           O  
ATOM   3778  CB  TYR B 134      20.159  49.452 -12.007  1.00 67.60           C  
ATOM   3779  CG  TYR B 134      20.430  50.890 -12.349  1.00 68.01           C  
ATOM   3780  CD1 TYR B 134      21.728  51.353 -12.482  1.00 67.97           C  
ATOM   3781  CD2 TYR B 134      19.388  51.785 -12.569  1.00 71.44           C  
ATOM   3782  CE1 TYR B 134      21.993  52.684 -12.824  1.00 72.19           C  
ATOM   3783  CE2 TYR B 134      19.642  53.125 -12.921  1.00 74.97           C  
ATOM   3784  CZ  TYR B 134      20.948  53.567 -13.042  1.00 73.93           C  
ATOM   3785  OH  TYR B 134      21.197  54.887 -13.361  1.00 75.67           O  
ATOM   3786  N   ASN B 135      22.016  48.526 -14.660  1.00 70.79           N  
ATOM   3787  CA  ASN B 135      22.822  48.961 -15.804  1.00 70.18           C  
ATOM   3788  C   ASN B 135      22.460  48.300 -17.150  1.00 70.63           C  
ATOM   3789  O   ASN B 135      22.853  48.789 -18.224  1.00 70.33           O  
ATOM   3790  CB  ASN B 135      24.297  48.737 -15.508  1.00 68.45           C  
ATOM   3791  CG  ASN B 135      24.828  49.723 -14.526  1.00 67.41           C  
ATOM   3792  OD1 ASN B 135      24.590  50.919 -14.653  1.00 69.47           O  
ATOM   3793  ND2 ASN B 135      25.564  49.240 -13.542  1.00 67.20           N  
ATOM   3794  N   VAL B 136      21.709  47.201 -17.092  1.00 70.16           N  
ATOM   3795  CA  VAL B 136      21.317  46.486 -18.297  1.00 70.69           C  
ATOM   3796  C   VAL B 136      19.847  46.688 -18.605  1.00 71.30           C  
ATOM   3797  O   VAL B 136      19.429  46.569 -19.752  1.00 73.34           O  
ATOM   3798  CB  VAL B 136      21.577  44.999 -18.152  1.00 70.07           C  
ATOM   3799  CG1 VAL B 136      23.056  44.753 -17.963  1.00 71.09           C  
ATOM   3800  CG2 VAL B 136      20.812  44.472 -16.972  1.00 72.40           C  
ATOM   3801  N   ILE B 137      19.060  46.992 -17.581  1.00 72.23           N  
ATOM   3802  CA  ILE B 137      17.624  47.226 -17.760  1.00 73.26           C  
ATOM   3803  C   ILE B 137      17.274  48.679 -17.392  1.00 73.96           C  
ATOM   3804  O   ILE B 137      16.844  49.467 -18.245  1.00 73.57           O  
ATOM   3805  CB  ILE B 137      16.779  46.271 -16.871  1.00 72.98           C  
ATOM   3806  CG1 ILE B 137      17.268  44.831 -17.035  1.00 71.63           C  
ATOM   3807  CG2 ILE B 137      15.310  46.375 -17.242  1.00 72.93           C  
ATOM   3808  CD1 ILE B 137      17.310  44.354 -18.458  1.00 69.98           C  
ATOM   3809  N   GLY B 138      17.480  49.019 -16.120  1.00 73.85           N  
ATOM   3810  CA  GLY B 138      17.182  50.355 -15.633  1.00 74.49           C  
ATOM   3811  C   GLY B 138      17.738  51.546 -16.413  1.00 74.06           C  
ATOM   3812  O   GLY B 138      17.827  52.676 -15.920  1.00 73.27           O  
ATOM   3813  N   ARG B 139      18.126  51.320 -17.645  1.00 74.45           N  
ATOM   3814  CA  ARG B 139      18.632  52.420 -18.401  1.00 76.49           C  
ATOM   3815  C   ARG B 139      18.238  52.256 -19.841  1.00 78.61           C  
ATOM   3816  O   ARG B 139      17.666  51.244 -20.246  1.00 79.29           O  
ATOM   3817  CB  ARG B 139      20.138  52.515 -18.216  1.00 75.93           C  
ATOM   3818  CG  ARG B 139      20.493  52.721 -16.763  1.00 74.80           C  
ATOM   3819  CD  ARG B 139      21.933  53.070 -16.633  1.00 77.70           C  
ATOM   3820  NE  ARG B 139      22.180  54.484 -16.882  1.00 79.09           N  
ATOM   3821  CZ  ARG B 139      23.283  54.935 -17.468  1.00 81.35           C  
ATOM   3822  NH1 ARG B 139      24.213  54.067 -17.867  1.00 82.66           N  
ATOM   3823  NH2 ARG B 139      23.466  56.242 -17.633  1.00 83.04           N  
ATOM   3824  N   PRO B 140      18.507  53.272 -20.633  1.00 80.71           N  
ATOM   3825  CA  PRO B 140      18.153  53.208 -22.042  1.00 84.83           C  
ATOM   3826  C   PRO B 140      18.879  52.107 -22.831  1.00 87.61           C  
ATOM   3827  O   PRO B 140      19.934  51.611 -22.420  1.00 88.82           O  
ATOM   3828  CB  PRO B 140      18.471  54.625 -22.520  1.00 85.18           C  
ATOM   3829  CG  PRO B 140      18.160  55.448 -21.273  1.00 83.52           C  
ATOM   3830  CD  PRO B 140      18.854  54.641 -20.230  1.00 81.26           C  
ATOM   3831  N   MET B 141      18.273  51.719 -23.952  1.00 89.18           N  
ATOM   3832  CA  MET B 141      18.816  50.702 -24.834  1.00 90.09           C  
ATOM   3833  C   MET B 141      20.265  51.037 -25.156  1.00 89.11           C  
ATOM   3834  O   MET B 141      21.145  50.180 -25.074  1.00 88.95           O  
ATOM   3835  CB  MET B 141      17.995  50.656 -26.133  1.00 94.13           C  
ATOM   3836  CG  MET B 141      16.516  50.279 -25.943  1.00 98.68           C  
ATOM   3837  SD  MET B 141      16.228  48.472 -25.730  1.00103.61           S  
ATOM   3838  CE  MET B 141      17.182  48.124 -24.108  1.00103.94           C  
ATOM   3839  N   ALA B 142      20.505  52.298 -25.504  1.00 88.06           N  
ATOM   3840  CA  ALA B 142      21.836  52.757 -25.871  1.00 87.28           C  
ATOM   3841  C   ALA B 142      22.750  52.914 -24.686  1.00 86.41           C  
ATOM   3842  O   ALA B 142      23.965  52.939 -24.852  1.00 88.75           O  
ATOM   3843  CB  ALA B 142      21.753  54.074 -26.621  1.00 86.79           C  
ATOM   3844  N   ALA B 143      22.167  53.019 -23.499  1.00 84.58           N  
ATOM   3845  CA  ALA B 143      22.938  53.184 -22.266  1.00 84.74           C  
ATOM   3846  C   ALA B 143      23.327  51.864 -21.586  1.00 84.28           C  
ATOM   3847  O   ALA B 143      24.310  51.813 -20.835  1.00 83.34           O  
ATOM   3848  CB  ALA B 143      22.155  54.041 -21.286  1.00 86.92           C  
ATOM   3849  N   SER B 144      22.545  50.813 -21.842  1.00 83.02           N  
ATOM   3850  CA  SER B 144      22.779  49.496 -21.262  1.00 81.12           C  
ATOM   3851  C   SER B 144      24.264  49.107 -21.271  1.00 80.73           C  
ATOM   3852  O   SER B 144      24.972  49.288 -22.273  1.00 80.15           O  
ATOM   3853  CB  SER B 144      21.953  48.444 -22.010  1.00 81.61           C  
ATOM   3854  OG  SER B 144      21.965  47.213 -21.304  1.00 80.91           O  
ATOM   3855  N   LYS B 145      24.719  48.572 -20.139  1.00 78.98           N  
ATOM   3856  CA  LYS B 145      26.104  48.160 -19.962  1.00 76.80           C  
ATOM   3857  C   LYS B 145      26.167  46.799 -19.268  1.00 76.70           C  
ATOM   3858  O   LYS B 145      25.602  46.617 -18.180  1.00 76.69           O  
ATOM   3859  CB  LYS B 145      26.838  49.204 -19.113  1.00 76.58           C  
ATOM   3860  CG  LYS B 145      28.297  48.888 -18.806  1.00 76.18           C  
ATOM   3861  CD  LYS B 145      28.842  49.742 -17.662  1.00 75.57           C  
ATOM   3862  CE  LYS B 145      29.145  51.176 -18.078  1.00 77.19           C  
ATOM   3863  NZ  LYS B 145      30.350  51.306 -18.971  1.00 77.60           N  
ATOM   3864  N   LYS B 146      26.853  45.844 -19.899  1.00 75.79           N  
ATOM   3865  CA  LYS B 146      27.023  44.488 -19.345  1.00 74.44           C  
ATOM   3866  C   LYS B 146      28.123  44.526 -18.273  1.00 72.46           C  
ATOM   3867  O   LYS B 146      29.093  45.264 -18.400  1.00 74.09           O  
ATOM   3868  CB  LYS B 146      27.448  43.522 -20.456  1.00 76.38           C  
ATOM   3869  CG  LYS B 146      26.547  42.308 -20.654  1.00 79.77           C  
ATOM   3870  CD  LYS B 146      25.239  42.673 -21.310  1.00 83.93           C  
ATOM   3871  CE  LYS B 146      24.374  41.435 -21.549  1.00 86.81           C  
ATOM   3872  NZ  LYS B 146      23.071  41.767 -22.262  1.00 87.95           N  
ATOM   3873  N   MET B 147      27.995  43.736 -17.219  1.00 68.40           N  
ATOM   3874  CA  MET B 147      29.028  43.760 -16.190  1.00 65.57           C  
ATOM   3875  C   MET B 147      30.337  43.207 -16.732  1.00 64.18           C  
ATOM   3876  O   MET B 147      30.319  42.347 -17.606  1.00 64.57           O  
ATOM   3877  CB  MET B 147      28.606  42.920 -14.988  1.00 65.02           C  
ATOM   3878  CG  MET B 147      29.685  42.840 -13.890  1.00 61.45           C  
ATOM   3879  SD  MET B 147      30.117  44.467 -13.210  1.00 56.40           S  
ATOM   3880  CE  MET B 147      28.606  44.809 -12.286  1.00 57.43           C  
ATOM   3881  N   SER B 148      31.462  43.683 -16.214  1.00 62.05           N  
ATOM   3882  CA  SER B 148      32.745  43.186 -16.670  1.00 64.24           C  
ATOM   3883  C   SER B 148      33.452  42.539 -15.500  1.00 68.54           C  
ATOM   3884  O   SER B 148      33.062  42.767 -14.345  1.00 71.23           O  
ATOM   3885  CB  SER B 148      33.599  44.325 -17.197  1.00 62.48           C  
ATOM   3886  OG  SER B 148      34.077  45.132 -16.139  1.00 57.61           O  
ATOM   3887  N   HIS B 149      34.482  41.738 -15.781  1.00 70.67           N  
ATOM   3888  CA  HIS B 149      35.220  41.082 -14.711  1.00 72.88           C  
ATOM   3889  C   HIS B 149      35.907  42.141 -13.846  1.00 70.83           C  
ATOM   3890  O   HIS B 149      35.971  42.009 -12.619  1.00 70.83           O  
ATOM   3891  CB  HIS B 149      36.253  40.116 -15.294  1.00 80.24           C  
ATOM   3892  CG  HIS B 149      37.137  39.484 -14.265  1.00 90.56           C  
ATOM   3893  ND1 HIS B 149      38.388  38.983 -14.566  1.00 95.66           N  
ATOM   3894  CD2 HIS B 149      36.961  39.281 -12.932  1.00 95.15           C  
ATOM   3895  CE1 HIS B 149      38.948  38.503 -13.464  1.00 99.65           C  
ATOM   3896  NE2 HIS B 149      38.103  38.672 -12.458  1.00 99.81           N  
ATOM   3897  N   ARG B 150      36.383  43.203 -14.492  1.00 68.54           N  
ATOM   3898  CA  ARG B 150      37.077  44.298 -13.814  1.00 66.50           C  
ATOM   3899  C   ARG B 150      36.222  44.912 -12.719  1.00 63.26           C  
ATOM   3900  O   ARG B 150      36.617  44.915 -11.563  1.00 60.76           O  
ATOM   3901  CB  ARG B 150      37.485  45.367 -14.837  1.00 71.65           C  
ATOM   3902  CG  ARG B 150      38.153  44.789 -16.132  1.00 76.64           C  
ATOM   3903  CD  ARG B 150      37.130  44.137 -17.097  1.00 74.56           C  
ATOM   3904  NE  ARG B 150      37.705  43.088 -17.942  1.00 72.67           N  
ATOM   3905  CZ  ARG B 150      36.989  42.255 -18.700  1.00 72.10           C  
ATOM   3906  NH1 ARG B 150      37.602  41.333 -19.429  1.00 72.54           N  
ATOM   3907  NH2 ARG B 150      35.663  42.333 -18.738  1.00 69.97           N  
ATOM   3908  N   ARG B 151      35.052  45.428 -13.076  1.00 61.61           N  
ATOM   3909  CA  ARG B 151      34.158  46.017 -12.078  1.00 61.60           C  
ATOM   3910  C   ARG B 151      33.615  45.000 -11.062  1.00 60.75           C  
ATOM   3911  O   ARG B 151      33.539  45.283  -9.859  1.00 62.16           O  
ATOM   3912  CB  ARG B 151      32.976  46.717 -12.750  1.00 63.05           C  
ATOM   3913  CG  ARG B 151      33.239  48.167 -13.093  1.00 68.73           C  
ATOM   3914  CD  ARG B 151      32.031  48.821 -13.749  1.00 73.20           C  
ATOM   3915  NE  ARG B 151      31.856  48.395 -15.132  1.00 77.57           N  
ATOM   3916  CZ  ARG B 151      30.726  47.861 -15.609  1.00 81.27           C  
ATOM   3917  NH1 ARG B 151      29.667  47.690 -14.802  1.00 78.78           N  
ATOM   3918  NH2 ARG B 151      30.661  47.490 -16.898  1.00 82.92           N  
ATOM   3919  N   ALA B 152      33.222  43.823 -11.542  1.00 58.22           N  
ATOM   3920  CA  ALA B 152      32.684  42.802 -10.662  1.00 56.43           C  
ATOM   3921  C   ALA B 152      33.657  42.511  -9.536  1.00 56.83           C  
ATOM   3922  O   ALA B 152      33.270  42.368  -8.376  1.00 55.63           O  
ATOM   3923  CB  ALA B 152      32.426  41.564 -11.445  1.00 57.04           C  
ATOM   3924  N   PHE B 153      34.932  42.433  -9.901  1.00 58.79           N  
ATOM   3925  CA  PHE B 153      36.009  42.150  -8.966  1.00 59.02           C  
ATOM   3926  C   PHE B 153      36.169  43.252  -7.940  1.00 56.11           C  
ATOM   3927  O   PHE B 153      36.324  42.966  -6.768  1.00 57.84           O  
ATOM   3928  CB  PHE B 153      37.307  41.970  -9.726  1.00 65.92           C  
ATOM   3929  CG  PHE B 153      38.393  41.356  -8.915  1.00 74.90           C  
ATOM   3930  CD1 PHE B 153      38.229  40.080  -8.373  1.00 78.94           C  
ATOM   3931  CD2 PHE B 153      39.595  42.048  -8.689  1.00 78.57           C  
ATOM   3932  CE1 PHE B 153      39.252  39.497  -7.612  1.00 82.72           C  
ATOM   3933  CE2 PHE B 153      40.636  41.481  -7.929  1.00 81.05           C  
ATOM   3934  CZ  PHE B 153      40.470  40.205  -7.387  1.00 82.54           C  
ATOM   3935  N   ILE B 154      36.160  44.509  -8.371  1.00 52.70           N  
ATOM   3936  CA  ILE B 154      36.269  45.626  -7.429  1.00 49.52           C  
ATOM   3937  C   ILE B 154      35.075  45.516  -6.456  1.00 51.85           C  
ATOM   3938  O   ILE B 154      35.210  45.633  -5.214  1.00 53.21           O  
ATOM   3939  CB  ILE B 154      36.164  46.990  -8.145  1.00 45.92           C  
ATOM   3940  CG1 ILE B 154      37.345  47.171  -9.077  1.00 43.22           C  
ATOM   3941  CG2 ILE B 154      36.088  48.102  -7.141  1.00 41.00           C  
ATOM   3942  CD1 ILE B 154      37.211  48.365  -9.966  1.00 45.73           C  
ATOM   3943  N   MET B 155      33.897  45.273  -7.027  1.00 49.53           N  
ATOM   3944  CA  MET B 155      32.703  45.188  -6.223  1.00 45.90           C  
ATOM   3945  C   MET B 155      32.765  44.109  -5.148  1.00 44.43           C  
ATOM   3946  O   MET B 155      32.450  44.395  -3.995  1.00 44.62           O  
ATOM   3947  CB  MET B 155      31.480  45.004  -7.135  1.00 47.61           C  
ATOM   3948  CG  MET B 155      30.935  46.316  -7.682  1.00 47.42           C  
ATOM   3949  SD  MET B 155      30.210  46.233  -9.353  1.00 49.59           S  
ATOM   3950  CE  MET B 155      28.389  46.116  -9.011  1.00 43.69           C  
ATOM   3951  N   ILE B 156      33.184  42.885  -5.489  1.00 42.19           N  
ATOM   3952  CA  ILE B 156      33.204  41.833  -4.480  1.00 39.53           C  
ATOM   3953  C   ILE B 156      34.216  42.153  -3.379  1.00 40.18           C  
ATOM   3954  O   ILE B 156      33.977  41.855  -2.212  1.00 39.51           O  
ATOM   3955  CB  ILE B 156      33.513  40.471  -5.083  1.00 39.60           C  
ATOM   3956  CG1 ILE B 156      34.944  40.471  -5.587  1.00 46.92           C  
ATOM   3957  CG2 ILE B 156      32.526  40.140  -6.195  1.00 29.64           C  
ATOM   3958  CD1 ILE B 156      35.505  39.087  -5.953  1.00 54.24           C  
ATOM   3959  N   ILE B 157      35.343  42.778  -3.731  1.00 41.75           N  
ATOM   3960  CA  ILE B 157      36.340  43.148  -2.722  1.00 40.75           C  
ATOM   3961  C   ILE B 157      35.675  44.159  -1.789  1.00 43.19           C  
ATOM   3962  O   ILE B 157      35.831  44.097  -0.544  1.00 42.37           O  
ATOM   3963  CB  ILE B 157      37.578  43.720  -3.380  1.00 36.96           C  
ATOM   3964  CG1 ILE B 157      38.296  42.583  -4.126  1.00 38.18           C  
ATOM   3965  CG2 ILE B 157      38.472  44.319  -2.349  1.00 34.80           C  
ATOM   3966  CD1 ILE B 157      39.508  42.991  -4.902  1.00 43.37           C  
ATOM   3967  N   PHE B 158      34.899  45.073  -2.392  1.00 44.15           N  
ATOM   3968  CA  PHE B 158      34.161  46.046  -1.591  1.00 44.24           C  
ATOM   3969  C   PHE B 158      33.254  45.288  -0.609  1.00 44.64           C  
ATOM   3970  O   PHE B 158      33.329  45.522   0.609  1.00 47.28           O  
ATOM   3971  CB  PHE B 158      33.282  46.956  -2.430  1.00 41.73           C  
ATOM   3972  CG  PHE B 158      32.349  47.772  -1.602  1.00 38.28           C  
ATOM   3973  CD1 PHE B 158      32.842  48.750  -0.747  1.00 35.33           C  
ATOM   3974  CD2 PHE B 158      30.992  47.519  -1.625  1.00 37.96           C  
ATOM   3975  CE1 PHE B 158      31.995  49.454   0.069  1.00 36.85           C  
ATOM   3976  CE2 PHE B 158      30.138  48.224  -0.808  1.00 39.54           C  
ATOM   3977  CZ  PHE B 158      30.635  49.189   0.040  1.00 38.16           C  
ATOM   3978  N   VAL B 159      32.411  44.384  -1.127  1.00 44.95           N  
ATOM   3979  CA  VAL B 159      31.528  43.587  -0.264  1.00 44.71           C  
ATOM   3980  C   VAL B 159      32.267  42.912   0.916  1.00 46.36           C  
ATOM   3981  O   VAL B 159      31.784  42.923   2.060  1.00 44.98           O  
ATOM   3982  CB  VAL B 159      30.822  42.492  -1.044  1.00 42.12           C  
ATOM   3983  CG1 VAL B 159      29.876  41.731  -0.104  1.00 42.29           C  
ATOM   3984  CG2 VAL B 159      30.082  43.099  -2.190  1.00 40.76           C  
ATOM   3985  N   TRP B 160      33.440  42.337   0.634  1.00 47.65           N  
ATOM   3986  CA  TRP B 160      34.198  41.663   1.670  1.00 46.62           C  
ATOM   3987  C   TRP B 160      34.661  42.637   2.728  1.00 46.55           C  
ATOM   3988  O   TRP B 160      34.435  42.404   3.926  1.00 48.32           O  
ATOM   3989  CB  TRP B 160      35.388  40.909   1.072  1.00 45.51           C  
ATOM   3990  CG  TRP B 160      34.962  39.552   0.566  1.00 43.89           C  
ATOM   3991  CD1 TRP B 160      34.362  39.260  -0.636  1.00 42.70           C  
ATOM   3992  CD2 TRP B 160      34.976  38.331   1.309  1.00 43.50           C  
ATOM   3993  NE1 TRP B 160      33.991  37.935  -0.680  1.00 40.86           N  
ATOM   3994  CE2 TRP B 160      34.352  37.339   0.501  1.00 43.17           C  
ATOM   3995  CE3 TRP B 160      35.450  37.975   2.591  1.00 43.56           C  
ATOM   3996  CZ2 TRP B 160      34.183  36.017   0.933  1.00 41.99           C  
ATOM   3997  CZ3 TRP B 160      35.282  36.669   3.023  1.00 44.24           C  
ATOM   3998  CH2 TRP B 160      34.645  35.699   2.185  1.00 44.26           C  
ATOM   3999  N   LEU B 161      35.289  43.735   2.309  1.00 44.48           N  
ATOM   4000  CA  LEU B 161      35.774  44.710   3.283  1.00 44.04           C  
ATOM   4001  C   LEU B 161      34.600  45.255   4.123  1.00 43.34           C  
ATOM   4002  O   LEU B 161      34.660  45.314   5.380  1.00 42.60           O  
ATOM   4003  CB  LEU B 161      36.489  45.841   2.552  1.00 44.00           C  
ATOM   4004  CG  LEU B 161      37.841  45.460   1.959  1.00 42.00           C  
ATOM   4005  CD1 LEU B 161      38.265  46.542   1.008  1.00 40.85           C  
ATOM   4006  CD2 LEU B 161      38.866  45.264   3.072  1.00 41.36           C  
ATOM   4007  N   TRP B 162      33.529  45.621   3.427  1.00 40.12           N  
ATOM   4008  CA  TRP B 162      32.365  46.149   4.089  1.00 38.09           C  
ATOM   4009  C   TRP B 162      31.886  45.158   5.122  1.00 40.31           C  
ATOM   4010  O   TRP B 162      31.968  45.409   6.337  1.00 39.85           O  
ATOM   4011  CB  TRP B 162      31.257  46.372   3.092  1.00 38.11           C  
ATOM   4012  CG  TRP B 162      30.154  47.186   3.617  1.00 38.15           C  
ATOM   4013  CD1 TRP B 162      28.893  46.771   3.892  1.00 37.37           C  
ATOM   4014  CD2 TRP B 162      30.183  48.594   3.868  1.00 40.08           C  
ATOM   4015  NE1 TRP B 162      28.124  47.827   4.290  1.00 38.81           N  
ATOM   4016  CE2 TRP B 162      28.893  48.964   4.282  1.00 40.56           C  
ATOM   4017  CE3 TRP B 162      31.179  49.584   3.779  1.00 39.50           C  
ATOM   4018  CZ2 TRP B 162      28.566  50.291   4.603  1.00 40.34           C  
ATOM   4019  CZ3 TRP B 162      30.852  50.889   4.098  1.00 37.61           C  
ATOM   4020  CH2 TRP B 162      29.557  51.232   4.505  1.00 36.94           C  
ATOM   4021  N   SER B 163      31.400  44.013   4.637  1.00 42.77           N  
ATOM   4022  CA  SER B 163      30.855  42.949   5.511  1.00 44.21           C  
ATOM   4023  C   SER B 163      31.695  42.610   6.755  1.00 45.71           C  
ATOM   4024  O   SER B 163      31.160  42.460   7.869  1.00 47.93           O  
ATOM   4025  CB  SER B 163      30.601  41.661   4.711  1.00 43.50           C  
ATOM   4026  OG  SER B 163      29.703  41.876   3.625  1.00 39.26           O  
ATOM   4027  N   VAL B 164      33.003  42.466   6.596  1.00 46.69           N  
ATOM   4028  CA  VAL B 164      33.797  42.159   7.775  1.00 45.47           C  
ATOM   4029  C   VAL B 164      33.877  43.399   8.669  1.00 43.43           C  
ATOM   4030  O   VAL B 164      33.763  43.288   9.904  1.00 41.76           O  
ATOM   4031  CB  VAL B 164      35.207  41.679   7.400  1.00 47.45           C  
ATOM   4032  CG1 VAL B 164      36.070  41.565   8.666  1.00 48.58           C  
ATOM   4033  CG2 VAL B 164      35.106  40.304   6.720  1.00 47.97           C  
ATOM   4034  N   LEU B 165      34.038  44.581   8.063  1.00 40.94           N  
ATOM   4035  CA  LEU B 165      34.113  45.807   8.871  1.00 38.82           C  
ATOM   4036  C   LEU B 165      32.916  46.025   9.815  1.00 38.18           C  
ATOM   4037  O   LEU B 165      33.106  46.324  11.011  1.00 37.48           O  
ATOM   4038  CB  LEU B 165      34.271  47.026   7.972  1.00 36.70           C  
ATOM   4039  CG  LEU B 165      34.158  48.376   8.685  1.00 34.11           C  
ATOM   4040  CD1 LEU B 165      35.165  48.505   9.843  1.00 30.22           C  
ATOM   4041  CD2 LEU B 165      34.349  49.451   7.645  1.00 32.03           C  
ATOM   4042  N   TRP B 166      31.693  45.879   9.297  1.00 35.38           N  
ATOM   4043  CA  TRP B 166      30.527  46.069  10.149  1.00 34.24           C  
ATOM   4044  C   TRP B 166      30.150  44.873  11.036  1.00 36.62           C  
ATOM   4045  O   TRP B 166      29.113  44.888  11.706  1.00 37.72           O  
ATOM   4046  CB  TRP B 166      29.342  46.534   9.311  1.00 29.68           C  
ATOM   4047  CG  TRP B 166      29.658  47.840   8.688  1.00 29.85           C  
ATOM   4048  CD1 TRP B 166      29.900  48.084   7.361  1.00 31.92           C  
ATOM   4049  CD2 TRP B 166      30.018  49.038   9.380  1.00 27.86           C  
ATOM   4050  NE1 TRP B 166      30.415  49.343   7.192  1.00 29.10           N  
ATOM   4051  CE2 TRP B 166      30.504  49.947   8.418  1.00 28.94           C  
ATOM   4052  CE3 TRP B 166      29.994  49.428  10.731  1.00 28.85           C  
ATOM   4053  CZ2 TRP B 166      30.971  51.213   8.764  1.00 29.28           C  
ATOM   4054  CZ3 TRP B 166      30.463  50.699  11.076  1.00 26.80           C  
ATOM   4055  CH2 TRP B 166      30.946  51.566  10.098  1.00 29.26           C  
ATOM   4056  N   ALA B 167      30.987  43.835  11.061  1.00 38.22           N  
ATOM   4057  CA  ALA B 167      30.716  42.672  11.912  1.00 38.26           C  
ATOM   4058  C   ALA B 167      31.865  42.492  12.933  1.00 38.07           C  
ATOM   4059  O   ALA B 167      31.704  41.911  13.996  1.00 37.04           O  
ATOM   4060  CB  ALA B 167      30.557  41.431  11.045  1.00 36.61           C  
ATOM   4061  N   ILE B 168      33.017  43.047  12.606  1.00 38.93           N  
ATOM   4062  CA  ILE B 168      34.183  42.948  13.445  1.00 38.84           C  
ATOM   4063  C   ILE B 168      34.045  43.642  14.788  1.00 38.07           C  
ATOM   4064  O   ILE B 168      34.609  43.206  15.780  1.00 40.78           O  
ATOM   4065  CB  ILE B 168      35.414  43.539  12.692  1.00 41.89           C  
ATOM   4066  CG1 ILE B 168      36.708  42.889  13.193  1.00 43.72           C  
ATOM   4067  CG2 ILE B 168      35.498  45.045  12.858  1.00 39.28           C  
ATOM   4068  CD1 ILE B 168      36.858  41.407  12.723  1.00 43.74           C  
ATOM   4069  N   GLY B 169      33.309  44.737  14.817  1.00 37.30           N  
ATOM   4070  CA  GLY B 169      33.156  45.503  16.049  1.00 34.42           C  
ATOM   4071  C   GLY B 169      33.041  44.770  17.374  1.00 31.78           C  
ATOM   4072  O   GLY B 169      33.772  45.036  18.317  1.00 32.14           O  
ATOM   4073  N   PRO B 170      32.096  43.842  17.493  1.00 32.85           N  
ATOM   4074  CA  PRO B 170      32.038  43.176  18.799  1.00 31.50           C  
ATOM   4075  C   PRO B 170      33.290  42.392  19.166  1.00 29.66           C  
ATOM   4076  O   PRO B 170      33.603  42.210  20.341  1.00 28.96           O  
ATOM   4077  CB  PRO B 170      30.799  42.293  18.666  1.00 32.27           C  
ATOM   4078  CG  PRO B 170      29.913  43.122  17.754  1.00 30.58           C  
ATOM   4079  CD  PRO B 170      30.875  43.575  16.698  1.00 31.94           C  
ATOM   4080  N   ILE B 171      34.022  41.939  18.166  1.00 31.23           N  
ATOM   4081  CA  ILE B 171      35.211  41.172  18.463  1.00 35.83           C  
ATOM   4082  C   ILE B 171      36.175  41.959  19.271  1.00 38.67           C  
ATOM   4083  O   ILE B 171      36.904  41.365  20.071  1.00 39.86           O  
ATOM   4084  CB  ILE B 171      35.934  40.684  17.221  1.00 34.18           C  
ATOM   4085  CG1 ILE B 171      35.023  39.656  16.480  1.00 35.33           C  
ATOM   4086  CG2 ILE B 171      37.278  40.095  17.622  1.00 33.25           C  
ATOM   4087  CD1 ILE B 171      34.497  38.414  17.323  1.00 28.48           C  
ATOM   4088  N   PHE B 172      36.172  43.288  19.062  1.00 41.17           N  
ATOM   4089  CA  PHE B 172      37.062  44.224  19.777  1.00 40.00           C  
ATOM   4090  C   PHE B 172      36.423  44.882  20.961  1.00 39.51           C  
ATOM   4091  O   PHE B 172      37.105  45.624  21.656  1.00 42.27           O  
ATOM   4092  CB  PHE B 172      37.613  45.275  18.837  1.00 39.01           C  
ATOM   4093  CG  PHE B 172      38.537  44.697  17.826  1.00 42.20           C  
ATOM   4094  CD1 PHE B 172      39.853  44.377  18.178  1.00 40.79           C  
ATOM   4095  CD2 PHE B 172      38.069  44.380  16.542  1.00 44.46           C  
ATOM   4096  CE1 PHE B 172      40.684  43.754  17.283  1.00 41.53           C  
ATOM   4097  CE2 PHE B 172      38.889  43.751  15.624  1.00 44.81           C  
ATOM   4098  CZ  PHE B 172      40.209  43.433  15.993  1.00 45.56           C  
ATOM   4099  N   GLY B 173      35.134  44.579  21.197  1.00 39.58           N  
ATOM   4100  CA  GLY B 173      34.412  45.123  22.352  1.00 40.96           C  
ATOM   4101  C   GLY B 173      33.378  46.213  22.094  1.00 40.99           C  
ATOM   4102  O   GLY B 173      32.668  46.699  23.000  1.00 40.50           O  
ATOM   4103  N   TRP B 174      33.304  46.619  20.841  1.00 40.03           N  
ATOM   4104  CA  TRP B 174      32.356  47.626  20.485  1.00 40.72           C  
ATOM   4105  C   TRP B 174      31.147  46.799  20.064  1.00 38.41           C  
ATOM   4106  O   TRP B 174      30.985  46.439  18.904  1.00 37.96           O  
ATOM   4107  CB  TRP B 174      32.921  48.481  19.344  1.00 45.29           C  
ATOM   4108  CG  TRP B 174      31.943  49.493  18.821  1.00 52.40           C  
ATOM   4109  CD1 TRP B 174      30.983  50.183  19.546  1.00 51.22           C  
ATOM   4110  CD2 TRP B 174      31.825  49.944  17.460  1.00 54.03           C  
ATOM   4111  NE1 TRP B 174      30.288  51.020  18.713  1.00 52.04           N  
ATOM   4112  CE2 TRP B 174      30.778  50.902  17.434  1.00 51.97           C  
ATOM   4113  CE3 TRP B 174      32.508  49.633  16.262  1.00 54.07           C  
ATOM   4114  CZ2 TRP B 174      30.393  51.552  16.265  1.00 50.97           C  
ATOM   4115  CZ3 TRP B 174      32.124  50.284  15.092  1.00 53.26           C  
ATOM   4116  CH2 TRP B 174      31.067  51.237  15.108  1.00 52.84           C  
ATOM   4117  N   GLY B 175      30.301  46.494  21.034  1.00 36.10           N  
ATOM   4118  CA  GLY B 175      29.144  45.679  20.759  1.00 35.36           C  
ATOM   4119  C   GLY B 175      29.554  44.381  21.393  1.00 37.26           C  
ATOM   4120  O   GLY B 175      30.588  44.317  22.078  1.00 41.22           O  
ATOM   4121  N   ALA B 176      28.797  43.319  21.188  1.00 35.44           N  
ATOM   4122  CA  ALA B 176      29.199  42.074  21.812  1.00 31.99           C  
ATOM   4123  C   ALA B 176      28.560  40.898  21.153  1.00 31.28           C  
ATOM   4124  O   ALA B 176      27.450  40.990  20.657  1.00 31.24           O  
ATOM   4125  CB  ALA B 176      28.833  42.104  23.269  1.00 30.94           C  
ATOM   4126  N   TYR B 177      29.280  39.792  21.113  1.00 31.15           N  
ATOM   4127  CA  TYR B 177      28.687  38.606  20.551  1.00 33.08           C  
ATOM   4128  C   TYR B 177      28.529  37.673  21.733  1.00 35.05           C  
ATOM   4129  O   TYR B 177      29.521  37.381  22.414  1.00 37.89           O  
ATOM   4130  CB  TYR B 177      29.564  37.998  19.501  1.00 29.47           C  
ATOM   4131  CG  TYR B 177      29.476  38.689  18.171  1.00 29.42           C  
ATOM   4132  CD1 TYR B 177      28.271  38.795  17.502  1.00 27.02           C  
ATOM   4133  CD2 TYR B 177      30.653  39.119  17.514  1.00 27.55           C  
ATOM   4134  CE1 TYR B 177      28.252  39.304  16.183  1.00 29.96           C  
ATOM   4135  CE2 TYR B 177      30.646  39.619  16.231  1.00 24.17           C  
ATOM   4136  CZ  TYR B 177      29.453  39.712  15.553  1.00 25.98           C  
ATOM   4137  OH  TYR B 177      29.438  40.178  14.256  1.00 20.00           O  
ATOM   4138  N   THR B 178      27.277  37.245  21.993  1.00 35.89           N  
ATOM   4139  CA  THR B 178      26.951  36.388  23.132  1.00 33.48           C  
ATOM   4140  C   THR B 178      25.749  35.496  22.912  1.00 34.41           C  
ATOM   4141  O   THR B 178      25.215  35.412  21.809  1.00 35.10           O  
ATOM   4142  CB  THR B 178      26.666  37.229  24.372  1.00 31.89           C  
ATOM   4143  OG1 THR B 178      26.694  36.379  25.519  1.00 33.42           O  
ATOM   4144  CG2 THR B 178      25.284  37.939  24.255  1.00 30.73           C  
ATOM   4145  N   LEU B 179      25.331  34.833  23.978  1.00 34.55           N  
ATOM   4146  CA  LEU B 179      24.189  33.955  23.922  1.00 37.20           C  
ATOM   4147  C   LEU B 179      22.834  34.712  23.931  1.00 39.13           C  
ATOM   4148  O   LEU B 179      22.688  35.769  24.567  1.00 40.06           O  
ATOM   4149  CB  LEU B 179      24.284  32.961  25.088  1.00 37.71           C  
ATOM   4150  CG  LEU B 179      25.443  31.948  24.986  1.00 39.96           C  
ATOM   4151  CD1 LEU B 179      25.701  31.334  26.349  1.00 37.27           C  
ATOM   4152  CD2 LEU B 179      25.128  30.844  23.950  1.00 38.55           C  
ATOM   4153  N   GLU B 180      21.856  34.146  23.215  1.00 38.33           N  
ATOM   4154  CA  GLU B 180      20.493  34.693  23.088  1.00 38.44           C  
ATOM   4155  C   GLU B 180      19.359  33.633  23.177  1.00 38.64           C  
ATOM   4156  O   GLU B 180      19.567  32.469  22.847  1.00 39.14           O  
ATOM   4157  CB  GLU B 180      20.337  35.421  21.733  1.00 35.94           C  
ATOM   4158  CG  GLU B 180      20.519  34.534  20.460  1.00 31.60           C  
ATOM   4159  CD  GLU B 180      19.854  35.109  19.200  1.00 30.31           C  
ATOM   4160  OE1 GLU B 180      19.177  36.153  19.301  1.00 30.90           O  
ATOM   4161  OE2 GLU B 180      19.992  34.514  18.112  1.00 24.27           O  
ATOM   4162  N   GLY B 181      18.160  34.042  23.593  1.00 39.54           N  
ATOM   4163  CA  GLY B 181      17.033  33.119  23.643  1.00 40.29           C  
ATOM   4164  C   GLY B 181      17.203  31.906  24.537  1.00 42.45           C  
ATOM   4165  O   GLY B 181      17.434  32.062  25.748  1.00 43.63           O  
ATOM   4166  N   VAL B 182      17.077  30.705  23.958  1.00 43.04           N  
ATOM   4167  CA  VAL B 182      17.222  29.437  24.703  1.00 44.17           C  
ATOM   4168  C   VAL B 182      18.672  28.985  24.978  1.00 46.08           C  
ATOM   4169  O   VAL B 182      18.895  27.804  25.323  1.00 46.05           O  
ATOM   4170  CB  VAL B 182      16.488  28.274  23.989  1.00 43.31           C  
ATOM   4171  CG1 VAL B 182      14.982  28.566  23.919  1.00 44.45           C  
ATOM   4172  CG2 VAL B 182      17.052  28.077  22.585  1.00 43.02           C  
ATOM   4173  N   LEU B 183      19.614  29.935  24.777  1.00 45.75           N  
ATOM   4174  CA  LEU B 183      21.082  29.864  24.984  1.00 43.98           C  
ATOM   4175  C   LEU B 183      21.968  28.833  24.224  1.00 45.50           C  
ATOM   4176  O   LEU B 183      23.102  28.516  24.651  1.00 45.16           O  
ATOM   4177  CB  LEU B 183      21.346  29.814  26.497  1.00 41.55           C  
ATOM   4178  CG  LEU B 183      20.367  30.744  27.241  1.00 38.75           C  
ATOM   4179  CD1 LEU B 183      20.492  30.638  28.719  1.00 38.02           C  
ATOM   4180  CD2 LEU B 183      20.652  32.162  26.830  1.00 43.54           C  
ATOM   4181  N   CYS B 184      21.464  28.382  23.070  1.00 45.82           N  
ATOM   4182  CA  CYS B 184      22.141  27.410  22.198  1.00 46.23           C  
ATOM   4183  C   CYS B 184      22.757  27.967  20.907  1.00 45.43           C  
ATOM   4184  O   CYS B 184      23.243  27.197  20.067  1.00 45.18           O  
ATOM   4185  CB  CYS B 184      21.160  26.302  21.819  1.00 46.89           C  
ATOM   4186  SG  CYS B 184      20.805  25.325  23.248  1.00 52.48           S  
ATOM   4187  N   ASN B 185      22.679  29.281  20.703  1.00 42.70           N  
ATOM   4188  CA  ASN B 185      23.285  29.863  19.523  1.00 41.16           C  
ATOM   4189  C   ASN B 185      23.738  31.211  19.935  1.00 39.85           C  
ATOM   4190  O   ASN B 185      23.396  31.669  21.028  1.00 37.46           O  
ATOM   4191  CB  ASN B 185      22.338  29.913  18.293  1.00 43.23           C  
ATOM   4192  CG  ASN B 185      21.215  30.951  18.396  1.00 42.89           C  
ATOM   4193  OD1 ASN B 185      20.237  30.773  19.135  1.00 40.93           O  
ATOM   4194  ND2 ASN B 185      21.344  32.029  17.620  1.00 42.26           N  
ATOM   4195  N   CYS B 186      24.550  31.836  19.099  1.00 39.28           N  
ATOM   4196  CA  CYS B 186      25.043  33.137  19.454  1.00 41.32           C  
ATOM   4197  C   CYS B 186      24.587  34.207  18.481  1.00 41.43           C  
ATOM   4198  O   CYS B 186      24.111  33.904  17.370  1.00 41.79           O  
ATOM   4199  CB  CYS B 186      26.571  33.063  19.657  1.00 42.96           C  
ATOM   4200  SG  CYS B 186      26.925  32.388  21.342  1.00 48.78           S  
ATOM   4201  N   SER B 187      24.679  35.459  18.934  1.00 41.10           N  
ATOM   4202  CA  SER B 187      24.238  36.621  18.152  1.00 39.80           C  
ATOM   4203  C   SER B 187      24.787  37.869  18.807  1.00 39.52           C  
ATOM   4204  O   SER B 187      25.369  37.774  19.879  1.00 41.59           O  
ATOM   4205  CB  SER B 187      22.721  36.706  18.174  1.00 38.38           C  
ATOM   4206  OG  SER B 187      22.298  37.882  17.542  1.00 39.81           O  
ATOM   4207  N   PHE B 188      24.592  39.026  18.184  1.00 38.88           N  
ATOM   4208  CA  PHE B 188      25.079  40.275  18.756  1.00 39.33           C  
ATOM   4209  C   PHE B 188      24.231  40.630  19.976  1.00 38.79           C  
ATOM   4210  O   PHE B 188      23.179  40.008  20.203  1.00 38.73           O  
ATOM   4211  CB  PHE B 188      25.090  41.439  17.707  1.00 40.02           C  
ATOM   4212  CG  PHE B 188      23.715  41.939  17.275  1.00 39.45           C  
ATOM   4213  CD1 PHE B 188      23.302  43.239  17.579  1.00 40.61           C  
ATOM   4214  CD2 PHE B 188      22.845  41.116  16.554  1.00 36.47           C  
ATOM   4215  CE1 PHE B 188      22.048  43.694  17.170  1.00 39.60           C  
ATOM   4216  CE2 PHE B 188      21.608  41.556  16.147  1.00 34.23           C  
ATOM   4217  CZ  PHE B 188      21.200  42.839  16.449  1.00 38.29           C  
ATOM   4218  N   ASP B 189      24.698  41.614  20.748  1.00 36.80           N  
ATOM   4219  CA  ASP B 189      24.018  42.048  21.956  1.00 36.54           C  
ATOM   4220  C   ASP B 189      23.085  43.182  21.722  1.00 37.22           C  
ATOM   4221  O   ASP B 189      23.515  44.345  21.631  1.00 39.01           O  
ATOM   4222  CB  ASP B 189      25.013  42.502  23.021  1.00 37.94           C  
ATOM   4223  CG  ASP B 189      24.335  42.802  24.380  1.00 37.60           C  
ATOM   4224  OD1 ASP B 189      23.159  42.373  24.563  1.00 39.68           O  
ATOM   4225  OD2 ASP B 189      24.987  43.446  25.250  1.00 33.07           O  
ATOM   4226  N   TYR B 190      21.801  42.862  21.660  1.00 38.19           N  
ATOM   4227  CA  TYR B 190      20.770  43.886  21.463  1.00 41.19           C  
ATOM   4228  C   TYR B 190      20.011  44.249  22.760  1.00 42.02           C  
ATOM   4229  O   TYR B 190      19.054  45.019  22.714  1.00 43.41           O  
ATOM   4230  CB  TYR B 190      19.761  43.445  20.376  1.00 39.58           C  
ATOM   4231  CG  TYR B 190      19.207  42.030  20.521  1.00 40.49           C  
ATOM   4232  CD1 TYR B 190      19.530  41.031  19.592  1.00 41.89           C  
ATOM   4233  CD2 TYR B 190      18.381  41.680  21.593  1.00 42.12           C  
ATOM   4234  CE1 TYR B 190      19.048  39.721  19.730  1.00 41.33           C  
ATOM   4235  CE2 TYR B 190      17.892  40.376  21.742  1.00 42.20           C  
ATOM   4236  CZ  TYR B 190      18.233  39.405  20.807  1.00 42.98           C  
ATOM   4237  OH  TYR B 190      17.781  38.112  20.961  1.00 46.37           O  
ATOM   4238  N   ILE B 191      20.444  43.717  23.906  1.00 42.77           N  
ATOM   4239  CA  ILE B 191      19.760  43.975  25.180  1.00 42.97           C  
ATOM   4240  C   ILE B 191      20.350  45.125  25.965  1.00 45.50           C  
ATOM   4241  O   ILE B 191      19.621  45.938  26.548  1.00 46.46           O  
ATOM   4242  CB  ILE B 191      19.753  42.708  26.020  1.00 42.11           C  
ATOM   4243  CG1 ILE B 191      19.002  41.632  25.187  1.00 42.97           C  
ATOM   4244  CG2 ILE B 191      19.246  43.011  27.433  1.00 34.53           C  
ATOM   4245  CD1 ILE B 191      18.941  40.168  25.756  1.00 46.38           C  
ATOM   4246  N   SER B 192      21.675  45.202  25.963  1.00 47.49           N  
ATOM   4247  CA  SER B 192      22.376  46.272  26.654  1.00 50.13           C  
ATOM   4248  C   SER B 192      22.134  47.594  25.922  1.00 50.67           C  
ATOM   4249  O   SER B 192      22.298  47.679  24.703  1.00 51.95           O  
ATOM   4250  CB  SER B 192      23.864  45.948  26.725  1.00 51.82           C  
ATOM   4251  OG  SER B 192      24.017  44.737  27.455  1.00 53.89           O  
ATOM   4252  N   ARG B 193      21.732  48.613  26.684  1.00 50.10           N  
ATOM   4253  CA  ARG B 193      21.406  49.919  26.157  1.00 45.40           C  
ATOM   4254  C   ARG B 193      22.444  50.931  26.431  1.00 44.74           C  
ATOM   4255  O   ARG B 193      22.117  52.098  26.490  1.00 45.36           O  
ATOM   4256  CB  ARG B 193      20.101  50.402  26.756  1.00 42.79           C  
ATOM   4257  CG  ARG B 193      19.058  49.301  26.801  1.00 43.97           C  
ATOM   4258  CD  ARG B 193      17.692  49.900  26.750  1.00 42.54           C  
ATOM   4259  NE  ARG B 193      16.698  48.868  26.709  1.00 41.30           N  
ATOM   4260  CZ  ARG B 193      15.455  49.097  26.338  1.00 44.33           C  
ATOM   4261  NH1 ARG B 193      14.563  48.100  26.321  1.00 48.58           N  
ATOM   4262  NH2 ARG B 193      15.101  50.326  25.987  1.00 43.40           N  
ATOM   4263  N   ASP B 194      23.686  50.512  26.628  1.00 47.71           N  
ATOM   4264  CA  ASP B 194      24.744  51.501  26.860  1.00 51.31           C  
ATOM   4265  C   ASP B 194      25.168  52.157  25.528  1.00 50.51           C  
ATOM   4266  O   ASP B 194      24.672  51.822  24.433  1.00 48.97           O  
ATOM   4267  CB  ASP B 194      26.007  50.889  27.565  1.00 56.78           C  
ATOM   4268  CG  ASP B 194      26.901  50.008  26.615  1.00 61.13           C  
ATOM   4269  OD1 ASP B 194      26.639  48.773  26.539  1.00 65.51           O  
ATOM   4270  OD2 ASP B 194      27.849  50.542  25.958  1.00 59.59           O  
ATOM   4271  N   SER B 195      26.105  53.084  25.650  1.00 50.57           N  
ATOM   4272  CA  SER B 195      26.626  53.799  24.505  1.00 52.97           C  
ATOM   4273  C   SER B 195      27.284  52.882  23.494  1.00 53.47           C  
ATOM   4274  O   SER B 195      26.901  52.843  22.303  1.00 54.13           O  
ATOM   4275  CB  SER B 195      27.658  54.825  24.945  1.00 53.83           C  
ATOM   4276  OG  SER B 195      27.031  55.953  25.533  1.00 62.34           O  
ATOM   4277  N   THR B 196      28.289  52.147  23.979  1.00 52.84           N  
ATOM   4278  CA  THR B 196      29.065  51.223  23.145  1.00 49.10           C  
ATOM   4279  C   THR B 196      28.198  50.199  22.418  1.00 47.48           C  
ATOM   4280  O   THR B 196      28.293  50.095  21.172  1.00 46.69           O  
ATOM   4281  CB  THR B 196      30.103  50.484  23.968  1.00 48.78           C  
ATOM   4282  OG1 THR B 196      30.826  51.429  24.770  1.00 50.38           O  
ATOM   4283  CG2 THR B 196      31.074  49.768  23.037  1.00 48.95           C  
ATOM   4284  N   THR B 197      27.359  49.466  23.172  1.00 41.94           N  
ATOM   4285  CA  THR B 197      26.506  48.473  22.551  1.00 39.26           C  
ATOM   4286  C   THR B 197      25.569  49.100  21.549  1.00 40.57           C  
ATOM   4287  O   THR B 197      25.453  48.627  20.401  1.00 39.83           O  
ATOM   4288  CB  THR B 197      25.637  47.740  23.551  1.00 38.74           C  
ATOM   4289  OG1 THR B 197      26.461  47.142  24.550  1.00 37.01           O  
ATOM   4290  CG2 THR B 197      24.829  46.625  22.821  1.00 39.30           C  
ATOM   4291  N   ARG B 198      24.908  50.175  21.982  1.00 40.91           N  
ATOM   4292  CA  ARG B 198      23.944  50.871  21.131  1.00 41.12           C  
ATOM   4293  C   ARG B 198      24.566  51.457  19.862  1.00 38.78           C  
ATOM   4294  O   ARG B 198      24.060  51.229  18.740  1.00 35.72           O  
ATOM   4295  CB  ARG B 198      23.261  51.979  21.932  1.00 45.49           C  
ATOM   4296  CG  ARG B 198      22.275  52.826  21.108  1.00 50.13           C  
ATOM   4297  CD  ARG B 198      21.249  53.504  21.998  1.00 50.07           C  
ATOM   4298  NE  ARG B 198      20.325  52.523  22.562  1.00 52.23           N  
ATOM   4299  CZ  ARG B 198      19.401  52.835  23.465  1.00 54.02           C  
ATOM   4300  NH1 ARG B 198      19.314  54.097  23.881  1.00 54.85           N  
ATOM   4301  NH2 ARG B 198      18.561  51.910  23.938  1.00 53.56           N  
ATOM   4302  N   SER B 199      25.660  52.203  20.038  1.00 35.73           N  
ATOM   4303  CA  SER B 199      26.317  52.806  18.897  1.00 36.08           C  
ATOM   4304  C   SER B 199      26.659  51.740  17.886  1.00 38.55           C  
ATOM   4305  O   SER B 199      26.498  51.962  16.682  1.00 42.26           O  
ATOM   4306  CB  SER B 199      27.585  53.528  19.304  1.00 34.00           C  
ATOM   4307  OG  SER B 199      28.419  52.633  19.977  1.00 30.89           O  
ATOM   4308  N   ASN B 200      27.126  50.573  18.342  1.00 39.16           N  
ATOM   4309  CA  ASN B 200      27.480  49.522  17.377  1.00 37.75           C  
ATOM   4310  C   ASN B 200      26.219  48.911  16.713  1.00 38.42           C  
ATOM   4311  O   ASN B 200      26.191  48.615  15.485  1.00 39.24           O  
ATOM   4312  CB  ASN B 200      28.354  48.436  18.045  1.00 36.18           C  
ATOM   4313  CG  ASN B 200      28.820  47.347  17.040  1.00 37.19           C  
ATOM   4314  OD1 ASN B 200      28.329  46.194  17.039  1.00 35.40           O  
ATOM   4315  ND2 ASN B 200      29.751  47.722  16.168  1.00 33.67           N  
ATOM   4316  N   ILE B 201      25.169  48.739  17.512  1.00 38.39           N  
ATOM   4317  CA  ILE B 201      23.928  48.188  16.991  1.00 36.69           C  
ATOM   4318  C   ILE B 201      23.474  49.114  15.854  1.00 39.21           C  
ATOM   4319  O   ILE B 201      23.254  48.667  14.722  1.00 38.90           O  
ATOM   4320  CB  ILE B 201      22.832  48.147  18.079  1.00 35.40           C  
ATOM   4321  CG1 ILE B 201      23.243  47.210  19.222  1.00 35.51           C  
ATOM   4322  CG2 ILE B 201      21.530  47.706  17.456  1.00 33.24           C  
ATOM   4323  CD1 ILE B 201      22.395  47.325  20.470  1.00 33.18           C  
ATOM   4324  N   LEU B 202      23.388  50.414  16.143  1.00 40.59           N  
ATOM   4325  CA  LEU B 202      22.908  51.350  15.139  1.00 44.15           C  
ATOM   4326  C   LEU B 202      23.710  51.302  13.854  1.00 46.39           C  
ATOM   4327  O   LEU B 202      23.141  51.333  12.742  1.00 49.51           O  
ATOM   4328  CB  LEU B 202      22.874  52.769  15.693  1.00 43.62           C  
ATOM   4329  CG  LEU B 202      21.786  52.942  16.759  1.00 44.25           C  
ATOM   4330  CD1 LEU B 202      21.858  54.353  17.365  1.00 41.39           C  
ATOM   4331  CD2 LEU B 202      20.415  52.647  16.121  1.00 41.65           C  
ATOM   4332  N   CYS B 203      25.027  51.224  13.991  1.00 48.06           N  
ATOM   4333  CA  CYS B 203      25.901  51.137  12.815  1.00 48.87           C  
ATOM   4334  C   CYS B 203      25.604  49.832  12.041  1.00 48.72           C  
ATOM   4335  O   CYS B 203      25.554  49.820  10.789  1.00 46.10           O  
ATOM   4336  CB  CYS B 203      27.372  51.155  13.246  1.00 49.62           C  
ATOM   4337  SG  CYS B 203      27.979  52.774  13.625  1.00 45.47           S  
ATOM   4338  N   MET B 204      25.408  48.741  12.784  1.00 47.46           N  
ATOM   4339  CA  MET B 204      25.094  47.484  12.123  1.00 49.95           C  
ATOM   4340  C   MET B 204      23.889  47.673  11.212  1.00 49.68           C  
ATOM   4341  O   MET B 204      23.954  47.353  10.001  1.00 51.84           O  
ATOM   4342  CB  MET B 204      24.787  46.368  13.129  1.00 52.00           C  
ATOM   4343  CG  MET B 204      25.971  45.390  13.373  1.00 54.76           C  
ATOM   4344  SD  MET B 204      25.738  43.951  14.553  1.00 54.96           S  
ATOM   4345  CE  MET B 204      27.438  43.574  14.980  1.00 52.59           C  
ATOM   4346  N   PHE B 205      22.800  48.190  11.798  1.00 46.74           N  
ATOM   4347  CA  PHE B 205      21.561  48.441  11.062  1.00 45.22           C  
ATOM   4348  C   PHE B 205      21.754  49.394   9.876  1.00 47.54           C  
ATOM   4349  O   PHE B 205      21.392  49.068   8.735  1.00 48.53           O  
ATOM   4350  CB  PHE B 205      20.490  49.017  11.995  1.00 39.90           C  
ATOM   4351  CG  PHE B 205      19.700  47.976  12.707  1.00 36.06           C  
ATOM   4352  CD1 PHE B 205      18.550  47.443  12.141  1.00 33.72           C  
ATOM   4353  CD2 PHE B 205      20.129  47.493  13.944  1.00 37.17           C  
ATOM   4354  CE1 PHE B 205      17.829  46.439  12.797  1.00 32.65           C  
ATOM   4355  CE2 PHE B 205      19.419  46.481  14.619  1.00 35.61           C  
ATOM   4356  CZ  PHE B 205      18.268  45.956  14.043  1.00 34.16           C  
ATOM   4357  N   ILE B 206      22.337  50.564  10.138  1.00 48.03           N  
ATOM   4358  CA  ILE B 206      22.520  51.571   9.099  1.00 47.39           C  
ATOM   4359  C   ILE B 206      23.480  51.190   7.964  1.00 47.98           C  
ATOM   4360  O   ILE B 206      23.095  51.227   6.787  1.00 50.04           O  
ATOM   4361  CB  ILE B 206      22.951  52.921   9.739  1.00 47.41           C  
ATOM   4362  CG1 ILE B 206      21.838  53.405  10.679  1.00 44.34           C  
ATOM   4363  CG2 ILE B 206      23.241  53.963   8.665  1.00 45.22           C  
ATOM   4364  CD1 ILE B 206      22.148  54.683  11.429  1.00 42.53           C  
ATOM   4365  N   LEU B 207      24.719  50.835   8.286  1.00 45.27           N  
ATOM   4366  CA  LEU B 207      25.651  50.467   7.226  1.00 43.05           C  
ATOM   4367  C   LEU B 207      25.441  49.043   6.670  1.00 43.47           C  
ATOM   4368  O   LEU B 207      25.524  48.808   5.448  1.00 39.83           O  
ATOM   4369  CB  LEU B 207      27.089  50.621   7.727  1.00 40.76           C  
ATOM   4370  CG  LEU B 207      27.528  52.037   8.102  1.00 39.44           C  
ATOM   4371  CD1 LEU B 207      26.954  52.971   7.098  1.00 41.06           C  
ATOM   4372  CD2 LEU B 207      27.058  52.432   9.482  1.00 39.50           C  
ATOM   4373  N   GLY B 208      25.150  48.109   7.585  1.00 45.36           N  
ATOM   4374  CA  GLY B 208      24.981  46.704   7.234  1.00 45.34           C  
ATOM   4375  C   GLY B 208      23.671  46.294   6.619  1.00 45.50           C  
ATOM   4376  O   GLY B 208      23.641  45.325   5.873  1.00 44.91           O  
ATOM   4377  N   PHE B 209      22.603  47.030   6.927  1.00 45.78           N  
ATOM   4378  CA  PHE B 209      21.277  46.742   6.408  1.00 44.09           C  
ATOM   4379  C   PHE B 209      20.712  47.856   5.549  1.00 47.37           C  
ATOM   4380  O   PHE B 209      20.490  47.670   4.352  1.00 50.96           O  
ATOM   4381  CB  PHE B 209      20.324  46.513   7.543  1.00 41.85           C  
ATOM   4382  CG  PHE B 209      19.130  45.754   7.159  1.00 39.86           C  
ATOM   4383  CD1 PHE B 209      17.966  45.892   7.866  1.00 42.62           C  
ATOM   4384  CD2 PHE B 209      19.182  44.834   6.132  1.00 42.54           C  
ATOM   4385  CE1 PHE B 209      16.844  45.112   7.562  1.00 46.67           C  
ATOM   4386  CE2 PHE B 209      18.072  44.038   5.808  1.00 44.40           C  
ATOM   4387  CZ  PHE B 209      16.902  44.177   6.525  1.00 46.78           C  
ATOM   4388  N   PHE B 210      20.466  49.022   6.145  1.00 48.43           N  
ATOM   4389  CA  PHE B 210      19.899  50.155   5.387  1.00 47.36           C  
ATOM   4390  C   PHE B 210      20.724  50.541   4.153  1.00 47.42           C  
ATOM   4391  O   PHE B 210      20.156  50.740   3.082  1.00 47.29           O  
ATOM   4392  CB  PHE B 210      19.694  51.371   6.310  1.00 44.60           C  
ATOM   4393  CG  PHE B 210      18.780  51.092   7.479  1.00 40.97           C  
ATOM   4394  CD1 PHE B 210      17.718  50.167   7.351  1.00 37.78           C  
ATOM   4395  CD2 PHE B 210      18.976  51.728   8.694  1.00 37.75           C  
ATOM   4396  CE1 PHE B 210      16.864  49.874   8.413  1.00 34.54           C  
ATOM   4397  CE2 PHE B 210      18.120  51.436   9.769  1.00 38.98           C  
ATOM   4398  CZ  PHE B 210      17.057  50.495   9.618  1.00 35.89           C  
ATOM   4399  N   GLY B 211      22.049  50.626   4.299  1.00 47.33           N  
ATOM   4400  CA  GLY B 211      22.905  50.971   3.173  1.00 48.64           C  
ATOM   4401  C   GLY B 211      22.605  50.149   1.931  1.00 50.04           C  
ATOM   4402  O   GLY B 211      22.223  50.701   0.891  1.00 48.41           O  
ATOM   4403  N   PRO B 212      22.766  48.814   1.999  1.00 52.20           N  
ATOM   4404  CA  PRO B 212      22.475  48.007   0.803  1.00 52.41           C  
ATOM   4405  C   PRO B 212      21.045  48.163   0.320  1.00 50.17           C  
ATOM   4406  O   PRO B 212      20.809  48.204  -0.880  1.00 50.43           O  
ATOM   4407  CB  PRO B 212      22.812  46.566   1.233  1.00 52.34           C  
ATOM   4408  CG  PRO B 212      22.674  46.596   2.707  1.00 53.60           C  
ATOM   4409  CD  PRO B 212      23.275  47.961   3.084  1.00 53.37           C  
ATOM   4410  N   ILE B 213      20.096  48.270   1.245  1.00 49.08           N  
ATOM   4411  CA  ILE B 213      18.685  48.433   0.854  1.00 48.45           C  
ATOM   4412  C   ILE B 213      18.436  49.739   0.030  1.00 48.87           C  
ATOM   4413  O   ILE B 213      17.680  49.776  -0.947  1.00 45.74           O  
ATOM   4414  CB  ILE B 213      17.741  48.414   2.119  1.00 44.02           C  
ATOM   4415  CG1 ILE B 213      17.791  47.049   2.804  1.00 42.50           C  
ATOM   4416  CG2 ILE B 213      16.330  48.685   1.700  1.00 41.01           C  
ATOM   4417  CD1 ILE B 213      16.926  46.911   4.031  1.00 40.04           C  
ATOM   4418  N   LEU B 214      19.095  50.807   0.441  1.00 49.57           N  
ATOM   4419  CA  LEU B 214      18.925  52.058  -0.212  1.00 49.07           C  
ATOM   4420  C   LEU B 214      19.299  51.848  -1.627  1.00 49.12           C  
ATOM   4421  O   LEU B 214      18.570  52.270  -2.495  1.00 50.23           O  
ATOM   4422  CB  LEU B 214      19.843  53.085   0.394  1.00 52.65           C  
ATOM   4423  CG  LEU B 214      19.593  54.474  -0.153  1.00 56.79           C  
ATOM   4424  CD1 LEU B 214      18.389  55.089   0.578  1.00 58.03           C  
ATOM   4425  CD2 LEU B 214      20.844  55.318   0.028  1.00 59.42           C  
ATOM   4426  N   ILE B 215      20.446  51.199  -1.849  1.00 50.25           N  
ATOM   4427  CA  ILE B 215      20.979  50.908  -3.201  1.00 50.68           C  
ATOM   4428  C   ILE B 215      20.028  50.038  -4.025  1.00 50.65           C  
ATOM   4429  O   ILE B 215      19.851  50.232  -5.231  1.00 47.60           O  
ATOM   4430  CB  ILE B 215      22.319  50.137  -3.135  1.00 51.65           C  
ATOM   4431  CG1 ILE B 215      23.371  50.980  -2.412  1.00 54.56           C  
ATOM   4432  CG2 ILE B 215      22.781  49.772  -4.556  1.00 49.65           C  
ATOM   4433  CD1 ILE B 215      24.674  50.234  -2.137  1.00 55.32           C  
ATOM   4434  N   ILE B 216      19.450  49.051  -3.352  1.00 52.67           N  
ATOM   4435  CA  ILE B 216      18.517  48.122  -3.961  1.00 54.55           C  
ATOM   4436  C   ILE B 216      17.246  48.851  -4.342  1.00 58.56           C  
ATOM   4437  O   ILE B 216      16.701  48.589  -5.416  1.00 59.24           O  
ATOM   4438  CB  ILE B 216      18.191  46.993  -2.987  1.00 55.30           C  
ATOM   4439  CG1 ILE B 216      19.436  46.134  -2.806  1.00 59.00           C  
ATOM   4440  CG2 ILE B 216      17.022  46.160  -3.474  1.00 53.40           C  
ATOM   4441  CD1 ILE B 216      19.314  45.125  -1.668  1.00 60.81           C  
ATOM   4442  N   PHE B 217      16.760  49.748  -3.467  1.00 61.41           N  
ATOM   4443  CA  PHE B 217      15.559  50.537  -3.766  1.00 62.06           C  
ATOM   4444  C   PHE B 217      15.785  51.453  -4.988  1.00 61.98           C  
ATOM   4445  O   PHE B 217      14.988  51.442  -5.932  1.00 60.64           O  
ATOM   4446  CB  PHE B 217      15.157  51.391  -2.578  1.00 65.34           C  
ATOM   4447  CG  PHE B 217      14.100  52.406  -2.912  1.00 69.46           C  
ATOM   4448  CD1 PHE B 217      14.439  53.737  -3.203  1.00 71.15           C  
ATOM   4449  CD2 PHE B 217      12.768  52.024  -2.984  1.00 70.42           C  
ATOM   4450  CE1 PHE B 217      13.451  54.669  -3.565  1.00 70.10           C  
ATOM   4451  CE2 PHE B 217      11.777  52.939  -3.341  1.00 70.27           C  
ATOM   4452  CZ  PHE B 217      12.118  54.262  -3.633  1.00 69.64           C  
ATOM   4453  N   PHE B 218      16.861  52.246  -4.955  1.00 62.80           N  
ATOM   4454  CA  PHE B 218      17.210  53.126  -6.072  1.00 65.64           C  
ATOM   4455  C   PHE B 218      17.281  52.316  -7.390  1.00 66.63           C  
ATOM   4456  O   PHE B 218      16.589  52.628  -8.370  1.00 69.32           O  
ATOM   4457  CB  PHE B 218      18.555  53.834  -5.824  1.00 67.18           C  
ATOM   4458  CG  PHE B 218      19.022  54.654  -6.988  1.00 71.34           C  
ATOM   4459  CD1 PHE B 218      19.633  54.050  -8.095  1.00 74.93           C  
ATOM   4460  CD2 PHE B 218      18.831  56.031  -7.002  1.00 73.55           C  
ATOM   4461  CE1 PHE B 218      20.062  54.826  -9.223  1.00 75.41           C  
ATOM   4462  CE2 PHE B 218      19.247  56.818  -8.113  1.00 75.32           C  
ATOM   4463  CZ  PHE B 218      19.868  56.210  -9.229  1.00 73.85           C  
ATOM   4464  N   CYS B 219      18.102  51.273  -7.411  1.00 65.17           N  
ATOM   4465  CA  CYS B 219      18.222  50.460  -8.601  1.00 64.35           C  
ATOM   4466  C   CYS B 219      16.900  49.915  -9.131  1.00 64.92           C  
ATOM   4467  O   CYS B 219      16.547  50.183 -10.282  1.00 64.79           O  
ATOM   4468  CB  CYS B 219      19.186  49.318  -8.345  1.00 62.58           C  
ATOM   4469  SG  CYS B 219      20.860  49.893  -8.371  1.00 59.25           S  
ATOM   4470  N   TYR B 220      16.167  49.163  -8.315  1.00 66.32           N  
ATOM   4471  CA  TYR B 220      14.903  48.599  -8.787  1.00 68.79           C  
ATOM   4472  C   TYR B 220      13.879  49.678  -9.056  1.00 70.14           C  
ATOM   4473  O   TYR B 220      12.963  49.478  -9.858  1.00 71.17           O  
ATOM   4474  CB  TYR B 220      14.328  47.561  -7.804  1.00 68.84           C  
ATOM   4475  CG  TYR B 220      15.152  46.292  -7.774  1.00 68.48           C  
ATOM   4476  CD1 TYR B 220      15.462  45.619  -8.957  1.00 67.77           C  
ATOM   4477  CD2 TYR B 220      15.740  45.847  -6.594  1.00 67.23           C  
ATOM   4478  CE1 TYR B 220      16.344  44.559  -8.972  1.00 66.50           C  
ATOM   4479  CE2 TYR B 220      16.624  44.792  -6.605  1.00 66.44           C  
ATOM   4480  CZ  TYR B 220      16.925  44.163  -7.804  1.00 66.60           C  
ATOM   4481  OH  TYR B 220      17.868  43.174  -7.854  1.00 69.04           O  
ATOM   4482  N   PHE B 221      14.016  50.824  -8.393  1.00 70.52           N  
ATOM   4483  CA  PHE B 221      13.073  51.909  -8.650  1.00 70.29           C  
ATOM   4484  C   PHE B 221      13.321  52.375 -10.091  1.00 71.50           C  
ATOM   4485  O   PHE B 221      12.415  52.352 -10.936  1.00 69.19           O  
ATOM   4486  CB  PHE B 221      13.283  53.078  -7.680  1.00 67.64           C  
ATOM   4487  CG  PHE B 221      12.254  54.158  -7.826  1.00 66.15           C  
ATOM   4488  CD1 PHE B 221      10.903  53.884  -7.570  1.00 66.65           C  
ATOM   4489  CD2 PHE B 221      12.612  55.416  -8.274  1.00 62.51           C  
ATOM   4490  CE1 PHE B 221       9.929  54.839  -7.764  1.00 63.74           C  
ATOM   4491  CE2 PHE B 221      11.651  56.373  -8.470  1.00 63.54           C  
ATOM   4492  CZ  PHE B 221      10.298  56.084  -8.214  1.00 65.36           C  
ATOM   4493  N   ASN B 222      14.567  52.779 -10.353  1.00 72.73           N  
ATOM   4494  CA  ASN B 222      14.978  53.235 -11.671  1.00 73.58           C  
ATOM   4495  C   ASN B 222      14.579  52.216 -12.709  1.00 72.10           C  
ATOM   4496  O   ASN B 222      14.109  52.577 -13.775  1.00 74.05           O  
ATOM   4497  CB  ASN B 222      16.492  53.455 -11.718  1.00 77.66           C  
ATOM   4498  CG  ASN B 222      16.888  54.918 -11.442  1.00 82.31           C  
ATOM   4499  OD1 ASN B 222      16.945  55.763 -12.375  1.00 82.17           O  
ATOM   4500  ND2 ASN B 222      17.156  55.226 -10.153  1.00 82.13           N  
ATOM   4501  N   ILE B 223      14.768  50.940 -12.409  1.00 70.85           N  
ATOM   4502  CA  ILE B 223      14.385  49.897 -13.355  1.00 70.29           C  
ATOM   4503  C   ILE B 223      12.876  49.997 -13.620  1.00 71.46           C  
ATOM   4504  O   ILE B 223      12.461  50.448 -14.690  1.00 70.70           O  
ATOM   4505  CB  ILE B 223      14.775  48.474 -12.814  1.00 67.42           C  
ATOM   4506  CG1 ILE B 223      16.296  48.319 -12.865  1.00 65.88           C  
ATOM   4507  CG2 ILE B 223      14.127  47.370 -13.644  1.00 63.83           C  
ATOM   4508  CD1 ILE B 223      16.818  47.207 -12.037  1.00 64.82           C  
ATOM   4509  N   VAL B 224      12.065  49.592 -12.645  1.00 72.94           N  
ATOM   4510  CA  VAL B 224      10.609  49.636 -12.777  1.00 73.96           C  
ATOM   4511  C   VAL B 224      10.165  50.844 -13.595  1.00 76.23           C  
ATOM   4512  O   VAL B 224       9.479  50.693 -14.598  1.00 77.61           O  
ATOM   4513  CB  VAL B 224       9.906  49.706 -11.393  1.00 72.10           C  
ATOM   4514  CG1 VAL B 224       8.420  49.892 -11.581  1.00 67.68           C  
ATOM   4515  CG2 VAL B 224      10.179  48.437 -10.592  1.00 71.70           C  
ATOM   4516  N   MET B 225      10.575  52.038 -13.167  1.00 77.96           N  
ATOM   4517  CA  MET B 225      10.215  53.288 -13.837  1.00 77.69           C  
ATOM   4518  C   MET B 225      11.039  53.496 -15.084  1.00 77.96           C  
ATOM   4519  O   MET B 225      11.756  54.487 -15.202  1.00 78.92           O  
ATOM   4520  CB  MET B 225      10.439  54.474 -12.897  1.00 78.07           C  
ATOM   4521  CG  MET B 225       9.212  55.330 -12.670  1.00 80.93           C  
ATOM   4522  SD  MET B 225       7.906  54.446 -11.796  1.00 79.82           S  
ATOM   4523  CE  MET B 225       6.877  53.796 -13.226  1.00 82.77           C  
ATOM   4524  N   SER B 226      10.939  52.568 -16.019  1.00 78.84           N  
ATOM   4525  CA  SER B 226      11.710  52.678 -17.246  1.00 79.86           C  
ATOM   4526  C   SER B 226      11.169  51.715 -18.300  1.00 81.37           C  
ATOM   4527  O   SER B 226      11.506  51.817 -19.482  1.00 80.78           O  
ATOM   4528  CB  SER B 226      13.172  52.366 -16.953  1.00 79.02           C  
ATOM   4529  OG  SER B 226      13.955  52.560 -18.102  1.00 80.08           O  
ATOM   4530  N   VAL B 227      10.322  50.785 -17.862  1.00 82.50           N  
ATOM   4531  CA  VAL B 227       9.741  49.804 -18.753  1.00 83.04           C  
ATOM   4532  C   VAL B 227       8.978  50.514 -19.836  1.00 84.88           C  
ATOM   4533  O   VAL B 227       8.837  50.008 -20.944  1.00 86.33           O  
ATOM   4534  CB  VAL B 227       8.788  48.866 -18.013  1.00 81.74           C  
ATOM   4535  CG1 VAL B 227       9.554  48.104 -16.958  1.00 83.49           C  
ATOM   4536  CG2 VAL B 227       7.656  49.654 -17.397  1.00 80.37           C  
ATOM   4537  N   SER B 228       8.493  51.701 -19.523  1.00 87.84           N  
ATOM   4538  CA  SER B 228       7.739  52.456 -20.502  1.00 92.44           C  
ATOM   4539  C   SER B 228       8.573  52.765 -21.748  1.00 96.62           C  
ATOM   4540  O   SER B 228       8.200  52.390 -22.867  1.00 97.96           O  
ATOM   4541  CB  SER B 228       7.223  53.751 -19.878  1.00 90.88           C  
ATOM   4542  OG  SER B 228       8.293  54.519 -19.366  1.00 90.48           O  
ATOM   4543  N   ASN B 229       9.706  53.435 -21.562  1.00100.53           N  
ATOM   4544  CA  ASN B 229      10.559  53.801 -22.692  1.00104.05           C  
ATOM   4545  C   ASN B 229      11.202  52.604 -23.356  1.00105.70           C  
ATOM   4546  O   ASN B 229      11.470  52.631 -24.556  1.00105.66           O  
ATOM   4547  CB  ASN B 229      11.651  54.763 -22.247  1.00105.91           C  
ATOM   4548  CG  ASN B 229      11.092  56.006 -21.597  1.00108.23           C  
ATOM   4549  OD1 ASN B 229      10.367  56.782 -22.227  1.00108.80           O  
ATOM   4550  ND2 ASN B 229      11.419  56.202 -20.323  1.00111.09           N  
ATOM   4551  N   HIS B 230      11.462  51.560 -22.575  1.00107.78           N  
ATOM   4552  CA  HIS B 230      12.078  50.371 -23.130  1.00109.88           C  
ATOM   4553  C   HIS B 230      11.286  49.897 -24.337  1.00111.08           C  
ATOM   4554  O   HIS B 230      11.826  49.804 -25.438  1.00111.85           O  
ATOM   4555  CB  HIS B 230      12.143  49.253 -22.094  1.00110.38           C  
ATOM   4556  CG  HIS B 230      12.802  48.009 -22.603  1.00112.86           C  
ATOM   4557  ND1 HIS B 230      12.860  46.842 -21.872  1.00113.04           N  
ATOM   4558  CD2 HIS B 230      13.435  47.750 -23.775  1.00114.52           C  
ATOM   4559  CE1 HIS B 230      13.497  45.918 -22.571  1.00114.91           C  
ATOM   4560  NE2 HIS B 230      13.856  46.443 -23.730  1.00115.98           N  
ATOM   4561  N   GLU B 231      10.006  49.604 -24.133  1.00112.39           N  
ATOM   4562  CA  GLU B 231       9.168  49.135 -25.225  1.00114.99           C  
ATOM   4563  C   GLU B 231       9.074  50.151 -26.358  1.00115.74           C  
ATOM   4564  O   GLU B 231       9.076  49.774 -27.532  1.00116.93           O  
ATOM   4565  CB  GLU B 231       7.777  48.795 -24.710  1.00116.22           C  
ATOM   4566  CG  GLU B 231       7.093  49.931 -24.004  1.00120.26           C  
ATOM   4567  CD  GLU B 231       5.815  49.484 -23.319  1.00123.18           C  
ATOM   4568  OE1 GLU B 231       5.902  48.634 -22.407  1.00123.94           O  
ATOM   4569  OE2 GLU B 231       4.721  49.972 -23.689  1.00125.81           O  
ATOM   4570  N   LYS B 232       9.000  51.436 -26.016  1.00116.01           N  
ATOM   4571  CA  LYS B 232       8.920  52.484 -27.036  1.00115.89           C  
ATOM   4572  C   LYS B 232      10.200  52.533 -27.904  1.00116.17           C  
ATOM   4573  O   LYS B 232      10.136  52.849 -29.099  1.00114.82           O  
ATOM   4574  CB  LYS B 232       8.658  53.845 -26.375  1.00115.42           C  
ATOM   4575  CG  LYS B 232       8.363  54.967 -27.372  1.00115.76           C  
ATOM   4576  CD  LYS B 232       7.695  56.177 -26.718  1.00115.23           C  
ATOM   4577  CE  LYS B 232       8.618  56.895 -25.739  1.00115.42           C  
ATOM   4578  NZ  LYS B 232       7.932  58.030 -25.043  1.00113.89           N  
ATOM   4579  N   GLU B 233      11.350  52.214 -27.295  1.00116.80           N  
ATOM   4580  CA  GLU B 233      12.648  52.183 -27.995  1.00116.28           C  
ATOM   4581  C   GLU B 233      12.694  50.908 -28.843  1.00114.99           C  
ATOM   4582  O   GLU B 233      13.381  50.832 -29.863  1.00114.80           O  
ATOM   4583  CB  GLU B 233      13.813  52.145 -26.993  1.00117.06           C  
ATOM   4584  CG  GLU B 233      13.952  53.362 -26.094  1.00119.61           C  
ATOM   4585  CD  GLU B 233      14.990  53.150 -24.991  1.00121.29           C  
ATOM   4586  OE1 GLU B 233      14.768  52.295 -24.104  1.00121.41           O  
ATOM   4587  OE2 GLU B 233      16.034  53.837 -25.011  1.00123.39           O  
ATOM   4588  N   MET B 234      11.950  49.908 -28.394  1.00113.38           N  
ATOM   4589  CA  MET B 234      11.877  48.632 -29.070  1.00112.66           C  
ATOM   4590  C   MET B 234      11.051  48.842 -30.323  1.00111.05           C  
ATOM   4591  O   MET B 234      11.396  48.364 -31.396  1.00110.23           O  
ATOM   4592  CB  MET B 234      11.192  47.609 -28.151  1.00115.29           C  
ATOM   4593  CG  MET B 234      11.379  46.134 -28.525  1.00117.32           C  
ATOM   4594  SD  MET B 234      13.080  45.539 -28.206  1.00116.44           S  
ATOM   4595  CE  MET B 234      13.842  45.965 -29.854  1.00120.57           C  
ATOM   4596  N   ALA B 235       9.957  49.575 -30.168  1.00110.94           N  
ATOM   4597  CA  ALA B 235       9.050  49.857 -31.269  1.00112.35           C  
ATOM   4598  C   ALA B 235       9.762  50.675 -32.327  1.00113.99           C  
ATOM   4599  O   ALA B 235       9.592  50.431 -33.527  1.00114.34           O  
ATOM   4600  CB  ALA B 235       7.825  50.610 -30.763  1.00110.48           C  
ATOM   4601  N   ALA B 236      10.555  51.652 -31.883  1.00115.91           N  
ATOM   4602  CA  ALA B 236      11.307  52.511 -32.806  1.00117.77           C  
ATOM   4603  C   ALA B 236      12.392  51.711 -33.508  1.00119.09           C  
ATOM   4604  O   ALA B 236      13.212  52.273 -34.235  1.00119.98           O  
ATOM   4605  CB  ALA B 236      11.934  53.687 -32.061  1.00117.00           C  
ATOM   4606  N   MET B 237      12.389  50.398 -33.275  1.00120.37           N  
ATOM   4607  CA  MET B 237      13.358  49.491 -33.884  1.00120.89           C  
ATOM   4608  C   MET B 237      12.672  48.274 -34.501  1.00119.49           C  
ATOM   4609  O   MET B 237      13.198  47.644 -35.417  1.00119.27           O  
ATOM   4610  CB  MET B 237      14.392  49.057 -32.844  1.00123.04           C  
ATOM   4611  CG  MET B 237      15.263  50.207 -32.369  1.00126.59           C  
ATOM   4612  SD  MET B 237      16.734  49.645 -31.513  1.00133.08           S  
ATOM   4613  CE  MET B 237      16.250  49.837 -29.788  1.00131.39           C  
ATOM   4614  N   ALA B 238      11.487  47.954 -33.997  1.00118.05           N  
ATOM   4615  CA  ALA B 238      10.728  46.834 -34.519  1.00116.64           C  
ATOM   4616  C   ALA B 238      10.388  47.156 -35.973  1.00116.30           C  
ATOM   4617  O   ALA B 238      10.053  46.262 -36.754  1.00118.13           O  
ATOM   4618  CB  ALA B 238       9.456  46.645 -33.702  1.00115.31           C  
ATOM   4619  N   LYS B 239      10.493  48.438 -36.327  1.00114.61           N  
ATOM   4620  CA  LYS B 239      10.178  48.908 -37.676  1.00112.38           C  
ATOM   4621  C   LYS B 239      11.424  49.077 -38.516  1.00111.27           C  
ATOM   4622  O   LYS B 239      11.539  48.518 -39.618  1.00112.20           O  
ATOM   4623  CB  LYS B 239       9.487  50.277 -37.636  1.00111.65           C  
ATOM   4624  CG  LYS B 239       8.452  50.471 -36.558  1.00109.09           C  
ATOM   4625  CD  LYS B 239       8.378  51.934 -36.186  1.00106.01           C  
ATOM   4626  CE  LYS B 239       7.548  52.132 -34.952  1.00105.35           C  
ATOM   4627  NZ  LYS B 239       7.719  53.513 -34.434  1.00106.32           N  
ATOM   4628  N   ARG B 240      12.346  49.886 -38.004  1.00108.75           N  
ATOM   4629  CA  ARG B 240      13.553  50.163 -38.752  1.00107.42           C  
ATOM   4630  C   ARG B 240      14.719  49.306 -38.320  1.00104.95           C  
ATOM   4631  O   ARG B 240      14.955  49.116 -37.137  1.00103.78           O  
ATOM   4632  CB  ARG B 240      13.898  51.661 -38.663  1.00109.22           C  
ATOM   4633  CG  ARG B 240      14.174  52.169 -37.268  1.00109.67           C  
ATOM   4634  CD  ARG B 240      15.656  52.483 -37.102  1.00110.11           C  
ATOM   4635  NE  ARG B 240      16.057  52.414 -35.701  1.00109.97           N  
ATOM   4636  CZ  ARG B 240      17.305  52.532 -35.268  1.00109.96           C  
ATOM   4637  NH1 ARG B 240      18.299  52.735 -36.132  1.00109.79           N  
ATOM   4638  NH2 ARG B 240      17.551  52.429 -33.967  1.00109.24           N  
ATOM   4639  N   LEU B 241      15.413  48.766 -39.317  1.00103.52           N  
ATOM   4640  CA  LEU B 241      16.584  47.911 -39.143  1.00101.60           C  
ATOM   4641  C   LEU B 241      16.340  46.697 -38.233  1.00 98.91           C  
ATOM   4642  O   LEU B 241      17.185  46.359 -37.400  1.00 99.42           O  
ATOM   4643  CB  LEU B 241      17.770  48.758 -38.625  1.00103.03           C  
ATOM   4644  CG  LEU B 241      19.218  48.239 -38.700  1.00104.12           C  
ATOM   4645  CD1 LEU B 241      19.596  47.927 -40.149  1.00106.26           C  
ATOM   4646  CD2 LEU B 241      20.168  49.284 -38.128  1.00104.26           C  
ATOM   4647  N   ASN B 242      15.193  46.040 -38.399  1.00 95.09           N  
ATOM   4648  CA  ASN B 242      14.867  44.868 -37.595  1.00 92.04           C  
ATOM   4649  C   ASN B 242      14.166  43.816 -38.429  1.00 88.96           C  
ATOM   4650  O   ASN B 242      13.004  43.957 -38.797  1.00 87.00           O  
ATOM   4651  CB  ASN B 242      13.990  45.244 -36.387  1.00 93.30           C  
ATOM   4652  CG  ASN B 242      14.767  45.228 -35.042  1.00 94.83           C  
ATOM   4653  OD1 ASN B 242      14.176  45.405 -33.959  1.00 94.45           O  
ATOM   4654  ND2 ASN B 242      16.089  45.017 -35.115  1.00 95.37           N  
ATOM   4655  N   ALA B 243      14.900  42.755 -38.716  1.00 86.17           N  
ATOM   4656  CA  ALA B 243      14.391  41.658 -39.507  1.00 85.17           C  
ATOM   4657  C   ALA B 243      14.017  40.546 -38.569  1.00 84.74           C  
ATOM   4658  O   ALA B 243      12.903  40.457 -38.057  1.00 82.92           O  
ATOM   4659  CB  ALA B 243      15.472  41.180 -40.455  1.00 83.36           C  
ATOM   4660  N   LYS B 244      14.986  39.672 -38.375  1.00 86.87           N  
ATOM   4661  CA  LYS B 244      14.824  38.549 -37.483  1.00 88.94           C  
ATOM   4662  C   LYS B 244      15.576  38.970 -36.232  1.00 91.40           C  
ATOM   4663  O   LYS B 244      15.301  38.481 -35.129  1.00 93.47           O  
ATOM   4664  CB  LYS B 244      15.447  37.289 -38.105  1.00 86.20           C  
ATOM   4665  CG  LYS B 244      15.545  36.084 -37.172  1.00 82.83           C  
ATOM   4666  CD  LYS B 244      14.257  35.846 -36.392  1.00 82.06           C  
ATOM   4667  CE  LYS B 244      13.084  35.486 -37.282  1.00 79.97           C  
ATOM   4668  NZ  LYS B 244      11.790  35.546 -36.518  1.00 77.24           N  
ATOM   4669  N   GLU B 245      16.523  39.897 -36.420  1.00 92.40           N  
ATOM   4670  CA  GLU B 245      17.351  40.418 -35.338  1.00 90.96           C  
ATOM   4671  C   GLU B 245      16.459  41.036 -34.270  1.00 90.55           C  
ATOM   4672  O   GLU B 245      16.913  41.359 -33.175  1.00 91.42           O  
ATOM   4673  CB  GLU B 245      18.358  41.436 -35.887  1.00 90.92           C  
ATOM   4674  CG  GLU B 245      17.748  42.558 -36.742  1.00 92.68           C  
ATOM   4675  CD  GLU B 245      18.333  42.633 -38.163  1.00 93.46           C  
ATOM   4676  OE1 GLU B 245      19.563  42.478 -38.297  1.00 94.53           O  
ATOM   4677  OE2 GLU B 245      17.576  42.859 -39.143  1.00 90.17           O  
ATOM   4678  N   LEU B 246      15.178  41.182 -34.597  1.00 90.10           N  
ATOM   4679  CA  LEU B 246      14.208  41.724 -33.650  1.00 89.22           C  
ATOM   4680  C   LEU B 246      13.961  40.635 -32.620  1.00 88.80           C  
ATOM   4681  O   LEU B 246      13.792  40.914 -31.430  1.00 88.51           O  
ATOM   4682  CB  LEU B 246      12.886  42.047 -34.347  1.00 87.51           C  
ATOM   4683  CG  LEU B 246      11.765  42.536 -33.426  1.00 84.97           C  
ATOM   4684  CD1 LEU B 246      12.096  43.946 -32.923  1.00 82.91           C  
ATOM   4685  CD2 LEU B 246      10.430  42.515 -34.182  1.00 83.34           C  
ATOM   4686  N   ARG B 247      13.936  39.393 -33.105  1.00 88.07           N  
ATOM   4687  CA  ARG B 247      13.717  38.227 -32.258  1.00 87.25           C  
ATOM   4688  C   ARG B 247      14.847  38.124 -31.239  1.00 84.50           C  
ATOM   4689  O   ARG B 247      14.625  37.743 -30.087  1.00 83.03           O  
ATOM   4690  CB  ARG B 247      13.682  36.945 -33.103  1.00 90.30           C  
ATOM   4691  CG  ARG B 247      12.544  35.971 -32.770  1.00 93.69           C  
ATOM   4692  CD  ARG B 247      12.498  35.545 -31.278  1.00 96.81           C  
ATOM   4693  NE  ARG B 247      11.804  36.505 -30.406  1.00100.18           N  
ATOM   4694  CZ  ARG B 247      11.440  36.268 -29.139  1.00100.25           C  
ATOM   4695  NH1 ARG B 247      10.808  37.202 -28.424  1.00100.73           N  
ATOM   4696  NH2 ARG B 247      11.700  35.097 -28.577  1.00 97.79           N  
ATOM   4697  N   LYS B 248      16.060  38.459 -31.675  1.00 81.24           N  
ATOM   4698  CA  LYS B 248      17.226  38.397 -30.807  1.00 79.47           C  
ATOM   4699  C   LYS B 248      17.245  39.547 -29.805  1.00 79.79           C  
ATOM   4700  O   LYS B 248      17.395  39.336 -28.604  1.00 79.99           O  
ATOM   4701  CB  LYS B 248      18.498  38.413 -31.643  1.00 77.18           C  
ATOM   4702  CG  LYS B 248      19.750  38.393 -30.811  1.00 78.43           C  
ATOM   4703  CD  LYS B 248      21.002  38.317 -31.667  1.00 79.92           C  
ATOM   4704  CE  LYS B 248      22.270  38.384 -30.814  1.00 77.80           C  
ATOM   4705  NZ  LYS B 248      23.482  38.226 -31.651  1.00 76.97           N  
ATOM   4706  N   ALA B 249      17.093  40.767 -30.299  1.00 81.10           N  
ATOM   4707  CA  ALA B 249      17.080  41.944 -29.431  1.00 82.09           C  
ATOM   4708  C   ALA B 249      15.964  41.862 -28.394  1.00 82.05           C  
ATOM   4709  O   ALA B 249      16.099  42.369 -27.297  1.00 80.62           O  
ATOM   4710  CB  ALA B 249      16.909  43.199 -30.265  1.00 83.60           C  
ATOM   4711  N   GLN B 250      14.858  41.237 -28.759  1.00 83.56           N  
ATOM   4712  CA  GLN B 250      13.750  41.088 -27.844  1.00 86.65           C  
ATOM   4713  C   GLN B 250      13.956  39.816 -27.018  1.00 87.83           C  
ATOM   4714  O   GLN B 250      13.317  39.606 -25.977  1.00 88.04           O  
ATOM   4715  CB  GLN B 250      12.448  40.994 -28.631  1.00 90.72           C  
ATOM   4716  CG  GLN B 250      11.194  41.012 -27.761  1.00 96.99           C  
ATOM   4717  CD  GLN B 250      11.097  42.278 -26.912  1.00 99.42           C  
ATOM   4718  OE1 GLN B 250      11.208  43.395 -27.435  1.00102.02           O  
ATOM   4719  NE2 GLN B 250      10.885  42.111 -25.602  1.00 99.40           N  
ATOM   4720  N   ALA B 251      14.841  38.951 -27.500  1.00 89.21           N  
ATOM   4721  CA  ALA B 251      15.144  37.704 -26.803  1.00 89.75           C  
ATOM   4722  C   ALA B 251      16.065  38.065 -25.641  1.00 89.57           C  
ATOM   4723  O   ALA B 251      15.830  37.658 -24.498  1.00 90.98           O  
ATOM   4724  CB  ALA B 251      15.842  36.731 -27.755  1.00 90.86           C  
ATOM   4725  N   GLY B 252      17.111  38.840 -25.947  1.00 88.35           N  
ATOM   4726  CA  GLY B 252      18.043  39.271 -24.927  1.00 85.40           C  
ATOM   4727  C   GLY B 252      17.363  40.186 -23.923  1.00 84.23           C  
ATOM   4728  O   GLY B 252      17.814  40.301 -22.793  1.00 85.90           O  
ATOM   4729  N   ALA B 253      16.273  40.835 -24.326  1.00 82.53           N  
ATOM   4730  CA  ALA B 253      15.538  41.739 -23.441  1.00 79.65           C  
ATOM   4731  C   ALA B 253      14.702  40.961 -22.424  1.00 78.50           C  
ATOM   4732  O   ALA B 253      14.742  41.224 -21.218  1.00 78.17           O  
ATOM   4733  CB  ALA B 253      14.639  42.643 -24.258  1.00 79.49           C  
ATOM   4734  N   ASN B 254      13.932  40.003 -22.910  1.00 76.60           N  
ATOM   4735  CA  ASN B 254      13.118  39.219 -22.008  1.00 74.96           C  
ATOM   4736  C   ASN B 254      14.012  38.472 -21.027  1.00 72.03           C  
ATOM   4737  O   ASN B 254      13.726  38.417 -19.843  1.00 72.07           O  
ATOM   4738  CB  ASN B 254      12.253  38.233 -22.805  1.00 76.91           C  
ATOM   4739  CG  ASN B 254      11.112  38.921 -23.546  1.00 77.29           C  
ATOM   4740  OD1 ASN B 254      11.327  39.900 -24.253  1.00 77.75           O  
ATOM   4741  ND2 ASN B 254       9.890  38.405 -23.384  1.00 77.44           N  
ATOM   4742  N   ALA B 255      15.101  37.917 -21.533  1.00 68.92           N  
ATOM   4743  CA  ALA B 255      16.012  37.168 -20.712  1.00 68.56           C  
ATOM   4744  C   ALA B 255      16.531  37.994 -19.528  1.00 69.18           C  
ATOM   4745  O   ALA B 255      16.383  37.608 -18.363  1.00 69.65           O  
ATOM   4746  CB  ALA B 255      17.153  36.691 -21.558  1.00 68.78           C  
ATOM   4747  N   GLU B 256      17.130  39.138 -19.821  1.00 68.71           N  
ATOM   4748  CA  GLU B 256      17.676  39.988 -18.775  1.00 69.00           C  
ATOM   4749  C   GLU B 256      16.628  40.345 -17.727  1.00 67.26           C  
ATOM   4750  O   GLU B 256      16.873  40.271 -16.516  1.00 68.46           O  
ATOM   4751  CB  GLU B 256      18.259  41.262 -19.394  1.00 71.05           C  
ATOM   4752  CG  GLU B 256      19.437  41.005 -20.333  1.00 74.66           C  
ATOM   4753  CD  GLU B 256      20.751  40.825 -19.599  1.00 77.10           C  
ATOM   4754  OE1 GLU B 256      20.758  40.153 -18.551  1.00 81.25           O  
ATOM   4755  OE2 GLU B 256      21.783  41.346 -20.063  1.00 78.01           O  
ATOM   4756  N   MET B 257      15.460  40.736 -18.196  1.00 64.72           N  
ATOM   4757  CA  MET B 257      14.382  41.106 -17.301  1.00 64.89           C  
ATOM   4758  C   MET B 257      14.005  39.941 -16.368  1.00 66.22           C  
ATOM   4759  O   MET B 257      13.440  40.160 -15.284  1.00 66.54           O  
ATOM   4760  CB  MET B 257      13.177  41.539 -18.137  1.00 65.85           C  
ATOM   4761  CG  MET B 257      11.898  41.826 -17.365  1.00 65.61           C  
ATOM   4762  SD  MET B 257      12.080  43.092 -16.105  1.00 66.63           S  
ATOM   4763  CE  MET B 257      12.310  44.494 -17.024  1.00 66.36           C  
ATOM   4764  N   ARG B 258      14.319  38.708 -16.778  1.00 66.38           N  
ATOM   4765  CA  ARG B 258      13.996  37.530 -15.966  1.00 66.21           C  
ATOM   4766  C   ARG B 258      14.971  37.411 -14.807  1.00 66.26           C  
ATOM   4767  O   ARG B 258      14.582  37.110 -13.664  1.00 66.40           O  
ATOM   4768  CB  ARG B 258      14.066  36.248 -16.788  1.00 66.82           C  
ATOM   4769  CG  ARG B 258      13.424  35.063 -16.091  1.00 68.14           C  
ATOM   4770  CD  ARG B 258      13.677  33.756 -16.831  1.00 70.20           C  
ATOM   4771  NE  ARG B 258      12.652  32.767 -16.506  1.00 73.02           N  
ATOM   4772  CZ  ARG B 258      11.428  32.737 -17.045  1.00 76.09           C  
ATOM   4773  NH1 ARG B 258      11.059  33.648 -17.955  1.00 76.07           N  
ATOM   4774  NH2 ARG B 258      10.559  31.794 -16.668  1.00 77.53           N  
ATOM   4775  N   LEU B 259      16.246  37.620 -15.103  1.00 65.03           N  
ATOM   4776  CA  LEU B 259      17.243  37.569 -14.054  1.00 66.84           C  
ATOM   4777  C   LEU B 259      16.874  38.629 -13.016  1.00 66.88           C  
ATOM   4778  O   LEU B 259      16.902  38.369 -11.799  1.00 69.25           O  
ATOM   4779  CB  LEU B 259      18.634  37.853 -14.612  1.00 69.99           C  
ATOM   4780  CG  LEU B 259      19.329  36.737 -15.440  1.00 73.71           C  
ATOM   4781  CD1 LEU B 259      19.153  35.396 -14.737  1.00 74.25           C  
ATOM   4782  CD2 LEU B 259      18.764  36.642 -16.850  1.00 75.23           C  
ATOM   4783  N   ALA B 260      16.506  39.813 -13.506  1.00 64.53           N  
ATOM   4784  CA  ALA B 260      16.098  40.921 -12.649  1.00 61.91           C  
ATOM   4785  C   ALA B 260      14.969  40.505 -11.707  1.00 60.74           C  
ATOM   4786  O   ALA B 260      15.034  40.749 -10.491  1.00 61.83           O  
ATOM   4787  CB  ALA B 260      15.660  42.096 -13.497  1.00 59.69           C  
ATOM   4788  N   LYS B 261      13.932  39.876 -12.248  1.00 59.97           N  
ATOM   4789  CA  LYS B 261      12.825  39.453 -11.386  1.00 59.73           C  
ATOM   4790  C   LYS B 261      13.350  38.494 -10.345  1.00 58.79           C  
ATOM   4791  O   LYS B 261      12.994  38.612  -9.171  1.00 57.78           O  
ATOM   4792  CB  LYS B 261      11.705  38.771 -12.179  1.00 58.53           C  
ATOM   4793  CG  LYS B 261      11.106  39.632 -13.249  1.00 60.36           C  
ATOM   4794  CD  LYS B 261       9.738  39.102 -13.630  1.00 63.27           C  
ATOM   4795  CE  LYS B 261       9.111  39.876 -14.802  1.00 65.71           C  
ATOM   4796  NZ  LYS B 261       9.883  39.703 -16.086  1.00 68.58           N  
ATOM   4797  N   ILE B 262      14.210  37.567 -10.776  1.00 58.24           N  
ATOM   4798  CA  ILE B 262      14.772  36.581  -9.862  1.00 60.57           C  
ATOM   4799  C   ILE B 262      15.461  37.297  -8.720  1.00 63.18           C  
ATOM   4800  O   ILE B 262      15.255  36.967  -7.526  1.00 66.04           O  
ATOM   4801  CB  ILE B 262      15.781  35.666 -10.558  1.00 58.51           C  
ATOM   4802  CG1 ILE B 262      15.054  34.759 -11.549  1.00 57.54           C  
ATOM   4803  CG2 ILE B 262      16.514  34.805  -9.521  1.00 58.89           C  
ATOM   4804  CD1 ILE B 262      15.992  33.986 -12.446  1.00 55.57           C  
ATOM   4805  N   SER B 263      16.269  38.293  -9.081  1.00 63.10           N  
ATOM   4806  CA  SER B 263      16.990  39.083  -8.083  1.00 62.59           C  
ATOM   4807  C   SER B 263      15.994  39.653  -7.067  1.00 62.47           C  
ATOM   4808  O   SER B 263      16.227  39.576  -5.853  1.00 65.13           O  
ATOM   4809  CB  SER B 263      17.734  40.224  -8.760  1.00 62.59           C  
ATOM   4810  OG  SER B 263      18.182  39.785 -10.018  1.00 66.89           O  
ATOM   4811  N   ILE B 264      14.887  40.215  -7.565  1.00 59.53           N  
ATOM   4812  CA  ILE B 264      13.870  40.805  -6.701  1.00 56.28           C  
ATOM   4813  C   ILE B 264      13.346  39.761  -5.721  1.00 52.89           C  
ATOM   4814  O   ILE B 264      13.132  40.043  -4.531  1.00 52.13           O  
ATOM   4815  CB  ILE B 264      12.675  41.335  -7.526  1.00 58.69           C  
ATOM   4816  CG1 ILE B 264      13.153  42.354  -8.548  1.00 59.47           C  
ATOM   4817  CG2 ILE B 264      11.661  41.992  -6.616  1.00 58.56           C  
ATOM   4818  CD1 ILE B 264      12.065  42.735  -9.551  1.00 61.30           C  
ATOM   4819  N   VAL B 265      13.152  38.547  -6.210  1.00 48.12           N  
ATOM   4820  CA  VAL B 265      12.618  37.531  -5.346  1.00 45.72           C  
ATOM   4821  C   VAL B 265      13.571  37.172  -4.254  1.00 44.75           C  
ATOM   4822  O   VAL B 265      13.137  37.012  -3.123  1.00 44.17           O  
ATOM   4823  CB  VAL B 265      12.221  36.273  -6.121  1.00 46.40           C  
ATOM   4824  CG1 VAL B 265      11.710  35.207  -5.144  1.00 45.88           C  
ATOM   4825  CG2 VAL B 265      11.142  36.623  -7.136  1.00 41.89           C  
ATOM   4826  N   ILE B 266      14.862  37.049  -4.561  1.00 45.53           N  
ATOM   4827  CA  ILE B 266      15.810  36.692  -3.498  1.00 49.04           C  
ATOM   4828  C   ILE B 266      15.971  37.852  -2.477  1.00 49.61           C  
ATOM   4829  O   ILE B 266      16.197  37.635  -1.271  1.00 52.32           O  
ATOM   4830  CB  ILE B 266      17.191  36.295  -4.046  1.00 49.15           C  
ATOM   4831  CG1 ILE B 266      17.905  37.521  -4.586  1.00 53.81           C  
ATOM   4832  CG2 ILE B 266      17.039  35.275  -5.132  1.00 46.72           C  
ATOM   4833  CD1 ILE B 266      19.377  37.267  -4.914  1.00 57.70           C  
ATOM   4834  N   VAL B 267      15.849  39.081  -2.957  1.00 47.36           N  
ATOM   4835  CA  VAL B 267      15.928  40.224  -2.085  1.00 44.28           C  
ATOM   4836  C   VAL B 267      14.719  40.190  -1.168  1.00 45.80           C  
ATOM   4837  O   VAL B 267      14.834  40.518   0.006  1.00 46.30           O  
ATOM   4838  CB  VAL B 267      15.873  41.509  -2.864  1.00 44.43           C  
ATOM   4839  CG1 VAL B 267      15.456  42.628  -1.945  1.00 43.35           C  
ATOM   4840  CG2 VAL B 267      17.203  41.790  -3.494  1.00 41.92           C  
ATOM   4841  N   SER B 268      13.553  39.796  -1.699  1.00 47.67           N  
ATOM   4842  CA  SER B 268      12.307  39.727  -0.884  1.00 50.58           C  
ATOM   4843  C   SER B 268      12.376  38.638   0.193  1.00 50.31           C  
ATOM   4844  O   SER B 268      11.882  38.806   1.319  1.00 50.46           O  
ATOM   4845  CB  SER B 268      11.100  39.455  -1.772  1.00 50.81           C  
ATOM   4846  OG  SER B 268      11.063  40.403  -2.820  1.00 55.08           O  
ATOM   4847  N   GLN B 269      12.993  37.524  -0.197  1.00 48.86           N  
ATOM   4848  CA  GLN B 269      13.227  36.378   0.653  1.00 46.23           C  
ATOM   4849  C   GLN B 269      14.158  36.794   1.814  1.00 44.73           C  
ATOM   4850  O   GLN B 269      13.913  36.470   2.977  1.00 43.56           O  
ATOM   4851  CB  GLN B 269      13.867  35.303  -0.215  1.00 48.71           C  
ATOM   4852  CG  GLN B 269      14.422  34.101   0.518  1.00 53.76           C  
ATOM   4853  CD  GLN B 269      15.822  34.317   1.076  1.00 51.40           C  
ATOM   4854  OE1 GLN B 269      16.739  34.647   0.348  1.00 47.98           O  
ATOM   4855  NE2 GLN B 269      15.982  34.105   2.377  1.00 54.93           N  
ATOM   4856  N   PHE B 270      15.226  37.515   1.497  1.00 42.87           N  
ATOM   4857  CA  PHE B 270      16.138  37.958   2.522  1.00 43.56           C  
ATOM   4858  C   PHE B 270      15.444  38.932   3.465  1.00 45.72           C  
ATOM   4859  O   PHE B 270      15.441  38.701   4.674  1.00 48.90           O  
ATOM   4860  CB  PHE B 270      17.360  38.624   1.906  1.00 43.74           C  
ATOM   4861  CG  PHE B 270      18.372  39.082   2.925  1.00 45.23           C  
ATOM   4862  CD1 PHE B 270      18.199  40.282   3.608  1.00 44.11           C  
ATOM   4863  CD2 PHE B 270      19.494  38.291   3.221  1.00 43.89           C  
ATOM   4864  CE1 PHE B 270      19.128  40.683   4.568  1.00 45.73           C  
ATOM   4865  CE2 PHE B 270      20.424  38.681   4.174  1.00 40.46           C  
ATOM   4866  CZ  PHE B 270      20.250  39.875   4.851  1.00 43.27           C  
ATOM   4867  N   LEU B 271      14.866  40.013   2.925  1.00 44.27           N  
ATOM   4868  CA  LEU B 271      14.159  41.031   3.727  1.00 43.73           C  
ATOM   4869  C   LEU B 271      13.035  40.445   4.595  1.00 44.87           C  
ATOM   4870  O   LEU B 271      12.828  40.839   5.749  1.00 44.49           O  
ATOM   4871  CB  LEU B 271      13.550  42.096   2.812  1.00 42.52           C  
ATOM   4872  CG  LEU B 271      14.512  43.011   2.042  1.00 43.09           C  
ATOM   4873  CD1 LEU B 271      13.740  43.839   1.044  1.00 32.63           C  
ATOM   4874  CD2 LEU B 271      15.314  43.902   3.026  1.00 42.60           C  
ATOM   4875  N   LEU B 272      12.289  39.520   4.025  1.00 44.34           N  
ATOM   4876  CA  LEU B 272      11.232  38.899   4.763  1.00 46.26           C  
ATOM   4877  C   LEU B 272      11.760  37.989   5.853  1.00 48.51           C  
ATOM   4878  O   LEU B 272      11.125  37.831   6.883  1.00 51.93           O  
ATOM   4879  CB  LEU B 272      10.367  38.096   3.822  1.00 49.03           C  
ATOM   4880  CG  LEU B 272       9.232  38.879   3.199  1.00 52.47           C  
ATOM   4881  CD1 LEU B 272       8.778  38.243   1.878  1.00 51.83           C  
ATOM   4882  CD2 LEU B 272       8.106  38.915   4.238  1.00 55.35           C  
ATOM   4883  N   SER B 273      12.914  37.370   5.633  1.00 49.89           N  
ATOM   4884  CA  SER B 273      13.460  36.453   6.626  1.00 50.22           C  
ATOM   4885  C   SER B 273      14.152  37.171   7.783  1.00 51.53           C  
ATOM   4886  O   SER B 273      14.036  36.747   8.948  1.00 53.46           O  
ATOM   4887  CB  SER B 273      14.428  35.476   5.953  1.00 47.47           C  
ATOM   4888  OG  SER B 273      13.765  34.733   4.950  1.00 45.05           O  
ATOM   4889  N   TRP B 274      14.845  38.266   7.465  1.00 51.41           N  
ATOM   4890  CA  TRP B 274      15.585  39.029   8.478  1.00 52.62           C  
ATOM   4891  C   TRP B 274      14.824  40.130   9.239  1.00 52.33           C  
ATOM   4892  O   TRP B 274      15.114  40.376  10.426  1.00 53.11           O  
ATOM   4893  CB  TRP B 274      16.846  39.646   7.867  1.00 50.99           C  
ATOM   4894  CG  TRP B 274      17.982  38.700   7.746  1.00 49.45           C  
ATOM   4895  CD1 TRP B 274      18.381  38.036   6.617  1.00 49.64           C  
ATOM   4896  CD2 TRP B 274      18.891  38.327   8.779  1.00 47.58           C  
ATOM   4897  NE1 TRP B 274      19.488  37.279   6.886  1.00 51.50           N  
ATOM   4898  CE2 TRP B 274      19.820  37.437   8.211  1.00 50.01           C  
ATOM   4899  CE3 TRP B 274      19.011  38.655  10.127  1.00 48.22           C  
ATOM   4900  CZ2 TRP B 274      20.866  36.867   8.961  1.00 50.08           C  
ATOM   4901  CZ3 TRP B 274      20.053  38.088  10.873  1.00 46.59           C  
ATOM   4902  CH2 TRP B 274      20.959  37.209  10.287  1.00 47.84           C  
ATOM   4903  N   SER B 275      13.862  40.781   8.574  1.00 50.43           N  
ATOM   4904  CA  SER B 275      13.077  41.847   9.202  1.00 47.53           C  
ATOM   4905  C   SER B 275      12.411  41.507  10.532  1.00 46.60           C  
ATOM   4906  O   SER B 275      12.564  42.259  11.507  1.00 49.14           O  
ATOM   4907  CB  SER B 275      12.051  42.380   8.236  1.00 45.60           C  
ATOM   4908  OG  SER B 275      12.721  43.166   7.255  1.00 49.92           O  
ATOM   4909  N   PRO B 276      11.675  40.382  10.616  1.00 43.58           N  
ATOM   4910  CA  PRO B 276      11.048  40.078  11.910  1.00 42.75           C  
ATOM   4911  C   PRO B 276      12.093  40.079  13.042  1.00 42.23           C  
ATOM   4912  O   PRO B 276      11.932  40.727  14.088  1.00 42.24           O  
ATOM   4913  CB  PRO B 276      10.424  38.701  11.674  1.00 42.52           C  
ATOM   4914  CG  PRO B 276      10.072  38.750  10.233  1.00 40.80           C  
ATOM   4915  CD  PRO B 276      11.308  39.377   9.613  1.00 42.84           C  
ATOM   4916  N   TYR B 277      13.185  39.371  12.807  1.00 40.12           N  
ATOM   4917  CA  TYR B 277      14.233  39.309  13.797  1.00 38.30           C  
ATOM   4918  C   TYR B 277      14.879  40.661  14.014  1.00 37.47           C  
ATOM   4919  O   TYR B 277      15.226  41.036  15.139  1.00 38.87           O  
ATOM   4920  CB  TYR B 277      15.301  38.304  13.377  1.00 36.35           C  
ATOM   4921  CG  TYR B 277      16.441  38.162  14.373  1.00 36.83           C  
ATOM   4922  CD1 TYR B 277      17.693  38.671  14.075  1.00 32.67           C  
ATOM   4923  CD2 TYR B 277      16.258  37.511  15.621  1.00 37.66           C  
ATOM   4924  CE1 TYR B 277      18.718  38.552  14.947  1.00 30.94           C  
ATOM   4925  CE2 TYR B 277      17.289  37.389  16.511  1.00 35.36           C  
ATOM   4926  CZ  TYR B 277      18.513  37.914  16.165  1.00 36.84           C  
ATOM   4927  OH  TYR B 277      19.530  37.811  17.083  1.00 43.83           O  
ATOM   4928  N   ALA B 278      15.066  41.400  12.941  1.00 36.79           N  
ATOM   4929  CA  ALA B 278      15.691  42.704  13.084  1.00 38.17           C  
ATOM   4930  C   ALA B 278      14.827  43.575  13.976  1.00 39.77           C  
ATOM   4931  O   ALA B 278      15.339  44.330  14.805  1.00 40.63           O  
ATOM   4932  CB  ALA B 278      15.870  43.368  11.727  1.00 38.28           C  
ATOM   4933  N   VAL B 279      13.513  43.461  13.808  1.00 39.79           N  
ATOM   4934  CA  VAL B 279      12.597  44.248  14.596  1.00 40.46           C  
ATOM   4935  C   VAL B 279      12.592  43.771  16.040  1.00 43.72           C  
ATOM   4936  O   VAL B 279      12.690  44.593  16.970  1.00 47.34           O  
ATOM   4937  CB  VAL B 279      11.219  44.181  14.006  1.00 38.45           C  
ATOM   4938  CG1 VAL B 279      10.228  44.742  14.958  1.00 40.16           C  
ATOM   4939  CG2 VAL B 279      11.198  44.982  12.714  1.00 40.86           C  
ATOM   4940  N   VAL B 280      12.491  42.461  16.252  1.00 42.73           N  
ATOM   4941  CA  VAL B 280      12.528  41.946  17.619  1.00 42.66           C  
ATOM   4942  C   VAL B 280      13.797  42.519  18.323  1.00 42.77           C  
ATOM   4943  O   VAL B 280      13.774  42.845  19.508  1.00 45.96           O  
ATOM   4944  CB  VAL B 280      12.545  40.368  17.626  1.00 41.08           C  
ATOM   4945  CG1 VAL B 280      12.792  39.823  19.037  1.00 40.11           C  
ATOM   4946  CG2 VAL B 280      11.224  39.848  17.114  1.00 36.84           C  
ATOM   4947  N   ALA B 281      14.883  42.682  17.576  1.00 41.78           N  
ATOM   4948  CA  ALA B 281      16.126  43.192  18.138  1.00 39.41           C  
ATOM   4949  C   ALA B 281      15.990  44.631  18.491  1.00 37.81           C  
ATOM   4950  O   ALA B 281      16.462  45.051  19.546  1.00 38.66           O  
ATOM   4951  CB  ALA B 281      17.270  43.023  17.151  1.00 40.53           C  
ATOM   4952  N   LEU B 282      15.366  45.400  17.597  1.00 38.09           N  
ATOM   4953  CA  LEU B 282      15.154  46.844  17.832  1.00 39.29           C  
ATOM   4954  C   LEU B 282      14.234  47.114  19.061  1.00 40.60           C  
ATOM   4955  O   LEU B 282      14.453  48.085  19.823  1.00 38.42           O  
ATOM   4956  CB  LEU B 282      14.591  47.511  16.569  1.00 34.26           C  
ATOM   4957  CG  LEU B 282      15.607  47.794  15.461  1.00 30.65           C  
ATOM   4958  CD1 LEU B 282      14.987  48.673  14.443  1.00 29.78           C  
ATOM   4959  CD2 LEU B 282      16.805  48.491  16.005  1.00 29.84           C  
ATOM   4960  N   LEU B 283      13.236  46.231  19.241  1.00 39.37           N  
ATOM   4961  CA  LEU B 283      12.302  46.286  20.362  1.00 38.04           C  
ATOM   4962  C   LEU B 283      13.058  46.056  21.659  1.00 39.15           C  
ATOM   4963  O   LEU B 283      12.808  46.700  22.674  1.00 40.03           O  
ATOM   4964  CB  LEU B 283      11.241  45.206  20.218  1.00 34.51           C  
ATOM   4965  CG  LEU B 283       9.947  45.671  19.574  1.00 35.96           C  
ATOM   4966  CD1 LEU B 283      10.243  46.348  18.263  1.00 35.76           C  
ATOM   4967  CD2 LEU B 283       9.021  44.480  19.398  1.00 35.96           C  
ATOM   4968  N   ALA B 284      13.990  45.125  21.612  1.00 40.17           N  
ATOM   4969  CA  ALA B 284      14.768  44.798  22.772  1.00 41.20           C  
ATOM   4970  C   ALA B 284      15.669  45.941  23.125  1.00 41.88           C  
ATOM   4971  O   ALA B 284      15.940  46.152  24.297  1.00 45.57           O  
ATOM   4972  CB  ALA B 284      15.591  43.568  22.517  1.00 41.81           C  
ATOM   4973  N   GLN B 285      16.144  46.683  22.133  1.00 41.63           N  
ATOM   4974  CA  GLN B 285      17.061  47.788  22.432  1.00 43.86           C  
ATOM   4975  C   GLN B 285      16.337  49.047  22.857  1.00 46.00           C  
ATOM   4976  O   GLN B 285      16.755  49.740  23.790  1.00 44.51           O  
ATOM   4977  CB  GLN B 285      17.959  48.096  21.209  1.00 44.22           C  
ATOM   4978  CG  GLN B 285      18.978  49.232  21.400  1.00 39.50           C  
ATOM   4979  CD  GLN B 285      20.010  48.957  22.458  1.00 36.58           C  
ATOM   4980  OE1 GLN B 285      20.714  49.865  22.864  1.00 37.36           O  
ATOM   4981  NE2 GLN B 285      20.117  47.710  22.902  1.00 32.23           N  
ATOM   4982  N   PHE B 286      15.232  49.331  22.174  1.00 48.35           N  
ATOM   4983  CA  PHE B 286      14.489  50.546  22.456  1.00 49.18           C  
ATOM   4984  C   PHE B 286      13.097  50.350  23.040  1.00 50.15           C  
ATOM   4985  O   PHE B 286      12.653  51.185  23.824  1.00 54.29           O  
ATOM   4986  CB  PHE B 286      14.408  51.383  21.181  1.00 47.06           C  
ATOM   4987  CG  PHE B 286      15.745  51.597  20.515  1.00 47.04           C  
ATOM   4988  CD1 PHE B 286      16.158  50.793  19.457  1.00 46.54           C  
ATOM   4989  CD2 PHE B 286      16.594  52.611  20.950  1.00 47.07           C  
ATOM   4990  CE1 PHE B 286      17.403  51.015  18.837  1.00 47.14           C  
ATOM   4991  CE2 PHE B 286      17.835  52.838  20.339  1.00 47.12           C  
ATOM   4992  CZ  PHE B 286      18.240  52.051  19.287  1.00 47.03           C  
ATOM   4993  N   GLY B 287      12.438  49.239  22.711  1.00 49.30           N  
ATOM   4994  CA  GLY B 287      11.090  49.007  23.176  1.00 48.78           C  
ATOM   4995  C   GLY B 287      10.946  48.338  24.513  1.00 51.17           C  
ATOM   4996  O   GLY B 287      11.853  48.417  25.346  1.00 51.72           O  
ATOM   4997  N   PRO B 288       9.783  47.673  24.749  1.00 54.02           N  
ATOM   4998  CA  PRO B 288       9.455  46.953  26.001  1.00 52.78           C  
ATOM   4999  C   PRO B 288      10.199  45.613  26.028  1.00 50.52           C  
ATOM   5000  O   PRO B 288       9.788  44.619  25.405  1.00 45.87           O  
ATOM   5001  CB  PRO B 288       7.925  46.766  25.926  1.00 53.42           C  
ATOM   5002  CG  PRO B 288       7.468  47.697  24.837  1.00 54.54           C  
ATOM   5003  CD  PRO B 288       8.611  47.668  23.844  1.00 53.81           C  
ATOM   5004  N   LEU B 289      11.302  45.599  26.756  1.00 49.58           N  
ATOM   5005  CA  LEU B 289      12.111  44.403  26.812  1.00 50.39           C  
ATOM   5006  C   LEU B 289      11.323  43.204  27.239  1.00 50.63           C  
ATOM   5007  O   LEU B 289      11.696  42.082  26.917  1.00 52.90           O  
ATOM   5008  CB  LEU B 289      13.301  44.597  27.752  1.00 48.39           C  
ATOM   5009  CG  LEU B 289      14.313  43.457  27.809  1.00 47.19           C  
ATOM   5010  CD1 LEU B 289      14.857  43.223  26.408  1.00 46.84           C  
ATOM   5011  CD2 LEU B 289      15.425  43.799  28.790  1.00 43.13           C  
ATOM   5012  N   GLU B 290      10.221  43.437  27.938  1.00 51.83           N  
ATOM   5013  CA  GLU B 290       9.427  42.324  28.415  1.00 52.24           C  
ATOM   5014  C   GLU B 290       8.713  41.612  27.292  1.00 52.61           C  
ATOM   5015  O   GLU B 290       8.061  40.604  27.523  1.00 51.99           O  
ATOM   5016  CB  GLU B 290       8.429  42.791  29.454  1.00 51.89           C  
ATOM   5017  CG  GLU B 290       7.410  43.732  28.925  1.00 51.33           C  
ATOM   5018  CD  GLU B 290       7.329  44.944  29.777  1.00 51.57           C  
ATOM   5019  OE1 GLU B 290       6.196  45.333  30.132  1.00 50.69           O  
ATOM   5020  OE2 GLU B 290       8.403  45.505  30.083  1.00 50.67           O  
ATOM   5021  N   TRP B 291       8.840  42.136  26.080  1.00 53.57           N  
ATOM   5022  CA  TRP B 291       8.224  41.501  24.935  1.00 54.73           C  
ATOM   5023  C   TRP B 291       9.186  40.476  24.353  1.00 52.93           C  
ATOM   5024  O   TRP B 291       8.784  39.396  23.925  1.00 53.20           O  
ATOM   5025  CB  TRP B 291       7.899  42.537  23.876  1.00 59.51           C  
ATOM   5026  CG  TRP B 291       6.712  43.420  24.173  1.00 64.78           C  
ATOM   5027  CD1 TRP B 291       6.038  43.586  25.377  1.00 63.20           C  
ATOM   5028  CD2 TRP B 291       6.076  44.288  23.236  1.00 65.74           C  
ATOM   5029  NE1 TRP B 291       5.032  44.505  25.217  1.00 62.85           N  
ATOM   5030  CE2 TRP B 291       5.035  44.950  23.916  1.00 63.83           C  
ATOM   5031  CE3 TRP B 291       6.291  44.572  21.875  1.00 67.75           C  
ATOM   5032  CZ2 TRP B 291       4.213  45.871  23.277  1.00 64.84           C  
ATOM   5033  CZ3 TRP B 291       5.466  45.488  21.246  1.00 66.39           C  
ATOM   5034  CH2 TRP B 291       4.448  46.124  21.941  1.00 64.84           C  
ATOM   5035  N   VAL B 292      10.466  40.815  24.334  1.00 51.68           N  
ATOM   5036  CA  VAL B 292      11.456  39.906  23.779  1.00 50.49           C  
ATOM   5037  C   VAL B 292      11.669  38.709  24.685  1.00 49.50           C  
ATOM   5038  O   VAL B 292      12.597  38.689  25.498  1.00 49.29           O  
ATOM   5039  CB  VAL B 292      12.830  40.595  23.555  1.00 51.15           C  
ATOM   5040  CG1 VAL B 292      13.785  39.617  22.839  1.00 49.34           C  
ATOM   5041  CG2 VAL B 292      12.655  41.893  22.730  1.00 50.46           C  
ATOM   5042  N   THR B 293      10.796  37.718  24.538  1.00 49.61           N  
ATOM   5043  CA  THR B 293      10.872  36.475  25.301  1.00 50.35           C  
ATOM   5044  C   THR B 293      11.683  35.460  24.540  1.00 52.32           C  
ATOM   5045  O   THR B 293      12.034  35.671  23.371  1.00 51.03           O  
ATOM   5046  CB  THR B 293       9.527  35.810  25.475  1.00 48.55           C  
ATOM   5047  OG1 THR B 293       8.749  36.006  24.290  1.00 45.60           O  
ATOM   5048  CG2 THR B 293       8.826  36.347  26.662  1.00 48.74           C  
ATOM   5049  N   PRO B 294      11.963  34.319  25.184  1.00 53.86           N  
ATOM   5050  CA  PRO B 294      12.741  33.273  24.522  1.00 56.71           C  
ATOM   5051  C   PRO B 294      12.236  32.956  23.085  1.00 61.06           C  
ATOM   5052  O   PRO B 294      13.036  32.926  22.132  1.00 65.39           O  
ATOM   5053  CB  PRO B 294      12.606  32.106  25.483  1.00 54.26           C  
ATOM   5054  CG  PRO B 294      12.621  32.809  26.795  1.00 54.97           C  
ATOM   5055  CD  PRO B 294      11.668  33.947  26.577  1.00 53.65           C  
ATOM   5056  N   TYR B 295      10.927  32.742  22.916  1.00 61.34           N  
ATOM   5057  CA  TYR B 295      10.352  32.448  21.603  1.00 59.52           C  
ATOM   5058  C   TYR B 295      10.229  33.699  20.734  1.00 58.53           C  
ATOM   5059  O   TYR B 295      10.333  33.637  19.490  1.00 58.06           O  
ATOM   5060  CB  TYR B 295       8.983  31.822  21.768  1.00 61.95           C  
ATOM   5061  CG  TYR B 295       9.029  30.505  22.484  1.00 67.32           C  
ATOM   5062  CD1 TYR B 295       7.937  30.076  23.251  1.00 70.47           C  
ATOM   5063  CD2 TYR B 295      10.141  29.668  22.385  1.00 66.85           C  
ATOM   5064  CE1 TYR B 295       7.943  28.840  23.904  1.00 72.36           C  
ATOM   5065  CE2 TYR B 295      10.158  28.428  23.037  1.00 71.63           C  
ATOM   5066  CZ  TYR B 295       9.054  28.018  23.797  1.00 71.92           C  
ATOM   5067  OH  TYR B 295       9.068  26.801  24.453  1.00 71.59           O  
ATOM   5068  N   ALA B 296      10.012  34.845  21.374  1.00 56.45           N  
ATOM   5069  CA  ALA B 296       9.882  36.102  20.623  1.00 54.21           C  
ATOM   5070  C   ALA B 296      11.164  36.387  19.851  1.00 53.46           C  
ATOM   5071  O   ALA B 296      11.133  37.044  18.799  1.00 51.52           O  
ATOM   5072  CB  ALA B 296       9.574  37.261  21.578  1.00 54.11           C  
ATOM   5073  N   ALA B 297      12.286  35.883  20.398  1.00 52.51           N  
ATOM   5074  CA  ALA B 297      13.616  36.050  19.809  1.00 48.61           C  
ATOM   5075  C   ALA B 297      14.002  34.833  19.006  1.00 46.73           C  
ATOM   5076  O   ALA B 297      14.314  34.941  17.813  1.00 49.40           O  
ATOM   5077  CB  ALA B 297      14.645  36.303  20.899  1.00 46.65           C  
ATOM   5078  N   GLN B 298      13.945  33.674  19.656  1.00 44.41           N  
ATOM   5079  CA  GLN B 298      14.303  32.399  19.037  1.00 42.93           C  
ATOM   5080  C   GLN B 298      13.631  32.052  17.692  1.00 45.16           C  
ATOM   5081  O   GLN B 298      14.326  31.819  16.702  1.00 45.20           O  
ATOM   5082  CB  GLN B 298      14.059  31.269  20.018  1.00 37.06           C  
ATOM   5083  CG  GLN B 298      14.870  30.067  19.697  1.00 36.53           C  
ATOM   5084  CD  GLN B 298      16.350  30.328  19.811  1.00 35.29           C  
ATOM   5085  OE1 GLN B 298      16.878  30.416  20.888  1.00 33.08           O  
ATOM   5086  NE2 GLN B 298      17.021  30.462  18.686  1.00 39.50           N  
ATOM   5087  N   LEU B 299      12.295  32.017  17.645  1.00 47.98           N  
ATOM   5088  CA  LEU B 299      11.596  31.673  16.405  1.00 47.88           C  
ATOM   5089  C   LEU B 299      12.002  32.549  15.260  1.00 47.49           C  
ATOM   5090  O   LEU B 299      12.375  32.045  14.207  1.00 48.95           O  
ATOM   5091  CB  LEU B 299      10.075  31.730  16.570  1.00 49.86           C  
ATOM   5092  CG  LEU B 299       9.448  30.435  17.139  1.00 55.81           C  
ATOM   5093  CD1 LEU B 299      10.080  30.021  18.502  1.00 55.92           C  
ATOM   5094  CD2 LEU B 299       7.937  30.645  17.302  1.00 59.50           C  
ATOM   5095  N   PRO B 300      11.962  33.875  15.449  1.00 47.69           N  
ATOM   5096  CA  PRO B 300      12.331  34.823  14.382  1.00 47.81           C  
ATOM   5097  C   PRO B 300      13.760  34.673  13.936  1.00 49.67           C  
ATOM   5098  O   PRO B 300      14.075  34.953  12.776  1.00 51.49           O  
ATOM   5099  CB  PRO B 300      12.095  36.194  15.004  1.00 46.68           C  
ATOM   5100  CG  PRO B 300      11.088  35.898  16.105  1.00 49.91           C  
ATOM   5101  CD  PRO B 300      11.549  34.583  16.671  1.00 46.44           C  
ATOM   5102  N   VAL B 301      14.643  34.243  14.842  1.00 50.24           N  
ATOM   5103  CA  VAL B 301      16.059  34.080  14.472  1.00 50.32           C  
ATOM   5104  C   VAL B 301      16.319  32.782  13.723  1.00 52.13           C  
ATOM   5105  O   VAL B 301      17.318  32.686  13.020  1.00 54.51           O  
ATOM   5106  CB  VAL B 301      17.002  34.136  15.690  1.00 48.92           C  
ATOM   5107  CG1 VAL B 301      16.953  32.819  16.452  1.00 48.05           C  
ATOM   5108  CG2 VAL B 301      18.416  34.486  15.234  1.00 43.28           C  
ATOM   5109  N   MET B 302      15.444  31.784  13.887  1.00 53.07           N  
ATOM   5110  CA  MET B 302      15.595  30.514  13.170  1.00 52.99           C  
ATOM   5111  C   MET B 302      15.194  30.769  11.703  1.00 55.41           C  
ATOM   5112  O   MET B 302      15.695  30.132  10.779  1.00 57.18           O  
ATOM   5113  CB  MET B 302      14.699  29.435  13.777  1.00 48.61           C  
ATOM   5114  CG  MET B 302      14.984  29.111  15.240  1.00 47.53           C  
ATOM   5115  SD  MET B 302      16.684  28.738  15.665  1.00 41.38           S  
ATOM   5116  CE  MET B 302      16.938  27.346  14.661  1.00 48.17           C  
ATOM   5117  N   PHE B 303      14.295  31.722  11.497  1.00 57.41           N  
ATOM   5118  CA  PHE B 303      13.860  32.057  10.159  1.00 59.84           C  
ATOM   5119  C   PHE B 303      14.923  32.918   9.458  1.00 59.29           C  
ATOM   5120  O   PHE B 303      15.100  32.831   8.228  1.00 59.80           O  
ATOM   5121  CB  PHE B 303      12.540  32.810  10.229  1.00 64.81           C  
ATOM   5122  CG  PHE B 303      11.599  32.455   9.135  1.00 71.38           C  
ATOM   5123  CD1 PHE B 303      11.317  33.364   8.106  1.00 75.13           C  
ATOM   5124  CD2 PHE B 303      11.000  31.191   9.116  1.00 74.77           C  
ATOM   5125  CE1 PHE B 303      10.441  33.014   7.055  1.00 78.67           C  
ATOM   5126  CE2 PHE B 303      10.129  30.816   8.084  1.00 78.30           C  
ATOM   5127  CZ  PHE B 303       9.844  31.728   7.044  1.00 80.04           C  
ATOM   5128  N   ALA B 304      15.624  33.758  10.222  1.00 55.82           N  
ATOM   5129  CA  ALA B 304      16.652  34.586   9.606  1.00 51.43           C  
ATOM   5130  C   ALA B 304      17.768  33.649   9.207  1.00 48.20           C  
ATOM   5131  O   ALA B 304      18.379  33.817   8.169  1.00 47.32           O  
ATOM   5132  CB  ALA B 304      17.157  35.633  10.577  1.00 54.06           C  
ATOM   5133  N   LYS B 305      18.002  32.636  10.026  1.00 45.15           N  
ATOM   5134  CA  LYS B 305      19.045  31.682   9.727  1.00 43.98           C  
ATOM   5135  C   LYS B 305      18.677  30.866   8.508  1.00 45.34           C  
ATOM   5136  O   LYS B 305      19.536  30.593   7.680  1.00 51.48           O  
ATOM   5137  CB  LYS B 305      19.297  30.734  10.912  1.00 41.42           C  
ATOM   5138  CG  LYS B 305      19.931  31.401  12.130  1.00 39.94           C  
ATOM   5139  CD  LYS B 305      20.283  30.396  13.172  1.00 37.41           C  
ATOM   5140  CE  LYS B 305      20.681  31.052  14.467  1.00 37.70           C  
ATOM   5141  NZ  LYS B 305      21.959  31.740  14.318  1.00 41.02           N  
ATOM   5142  N   ALA B 306      17.419  30.474   8.382  1.00 41.73           N  
ATOM   5143  CA  ALA B 306      17.021  29.662   7.263  1.00 40.66           C  
ATOM   5144  C   ALA B 306      17.113  30.438   5.956  1.00 44.19           C  
ATOM   5145  O   ALA B 306      17.090  29.856   4.852  1.00 46.76           O  
ATOM   5146  CB  ALA B 306      15.641  29.164   7.474  1.00 39.87           C  
ATOM   5147  N   SER B 307      17.236  31.757   6.061  1.00 46.69           N  
ATOM   5148  CA  SER B 307      17.323  32.599   4.864  1.00 48.79           C  
ATOM   5149  C   SER B 307      18.447  32.213   3.922  1.00 51.14           C  
ATOM   5150  O   SER B 307      18.310  32.356   2.709  1.00 53.74           O  
ATOM   5151  CB  SER B 307      17.525  34.064   5.242  1.00 50.66           C  
ATOM   5152  OG  SER B 307      17.750  34.853   4.066  1.00 52.18           O  
ATOM   5153  N   ALA B 308      19.562  31.746   4.479  1.00 52.47           N  
ATOM   5154  CA  ALA B 308      20.723  31.368   3.675  1.00 53.94           C  
ATOM   5155  C   ALA B 308      20.567  30.080   2.884  1.00 54.74           C  
ATOM   5156  O   ALA B 308      21.559  29.546   2.341  1.00 56.01           O  
ATOM   5157  CB  ALA B 308      21.947  31.254   4.557  1.00 54.61           C  
ATOM   5158  N   ILE B 309      19.346  29.559   2.818  1.00 54.04           N  
ATOM   5159  CA  ILE B 309      19.162  28.320   2.081  1.00 54.07           C  
ATOM   5160  C   ILE B 309      18.161  28.423   0.950  1.00 52.70           C  
ATOM   5161  O   ILE B 309      18.021  27.481   0.166  1.00 54.62           O  
ATOM   5162  CB  ILE B 309      18.711  27.169   3.007  1.00 53.57           C  
ATOM   5163  CG1 ILE B 309      17.224  27.344   3.350  1.00 51.62           C  
ATOM   5164  CG2 ILE B 309      19.597  27.139   4.277  1.00 52.49           C  
ATOM   5165  CD1 ILE B 309      16.626  26.127   4.019  1.00 49.75           C  
ATOM   5166  N   HIS B 310      17.485  29.563   0.858  1.00 51.24           N  
ATOM   5167  CA  HIS B 310      16.472  29.775  -0.167  1.00 48.82           C  
ATOM   5168  C   HIS B 310      16.953  30.062  -1.585  1.00 49.33           C  
ATOM   5169  O   HIS B 310      16.360  29.580  -2.557  1.00 49.41           O  
ATOM   5170  CB  HIS B 310      15.533  30.881   0.285  1.00 46.67           C  
ATOM   5171  CG  HIS B 310      14.850  30.588   1.583  1.00 46.77           C  
ATOM   5172  ND1 HIS B 310      14.279  29.363   1.868  1.00 47.63           N  
ATOM   5173  CD2 HIS B 310      14.596  31.376   2.657  1.00 46.90           C  
ATOM   5174  CE1 HIS B 310      13.698  29.408   3.056  1.00 46.87           C  
ATOM   5175  NE2 HIS B 310      13.875  30.621   3.555  1.00 48.29           N  
ATOM   5176  N   ASN B 311      18.022  30.832  -1.721  1.00 50.12           N  
ATOM   5177  CA  ASN B 311      18.525  31.165  -3.051  1.00 52.39           C  
ATOM   5178  C   ASN B 311      18.724  30.007  -4.034  1.00 53.25           C  
ATOM   5179  O   ASN B 311      18.220  30.044  -5.150  1.00 56.35           O  
ATOM   5180  CB  ASN B 311      19.805  31.973  -2.924  1.00 52.59           C  
ATOM   5181  CG  ASN B 311      19.564  33.303  -2.245  1.00 53.95           C  
ATOM   5182  OD1 ASN B 311      18.422  33.770  -2.170  1.00 55.67           O  
ATOM   5183  ND2 ASN B 311      20.630  33.932  -1.758  1.00 55.22           N  
ATOM   5184  N   PRO B 312      19.477  28.979  -3.656  1.00 51.26           N  
ATOM   5185  CA  PRO B 312      19.686  27.854  -4.551  1.00 52.50           C  
ATOM   5186  C   PRO B 312      18.367  27.265  -5.100  1.00 54.33           C  
ATOM   5187  O   PRO B 312      18.262  26.926  -6.300  1.00 56.47           O  
ATOM   5188  CB  PRO B 312      20.427  26.871  -3.668  1.00 52.54           C  
ATOM   5189  CG  PRO B 312      21.255  27.734  -2.861  1.00 53.29           C  
ATOM   5190  CD  PRO B 312      20.288  28.814  -2.449  1.00 54.42           C  
ATOM   5191  N   MET B 313      17.362  27.132  -4.234  1.00 52.74           N  
ATOM   5192  CA  MET B 313      16.074  26.589  -4.664  1.00 51.69           C  
ATOM   5193  C   MET B 313      15.360  27.573  -5.585  1.00 49.55           C  
ATOM   5194  O   MET B 313      14.834  27.183  -6.620  1.00 50.36           O  
ATOM   5195  CB  MET B 313      15.204  26.225  -3.451  1.00 53.48           C  
ATOM   5196  CG  MET B 313      15.794  25.082  -2.601  1.00 55.05           C  
ATOM   5197  SD  MET B 313      14.789  24.521  -1.173  1.00 57.83           S  
ATOM   5198  CE  MET B 313      15.048  25.897   0.001  1.00 58.61           C  
ATOM   5199  N   ILE B 314      15.339  28.842  -5.215  1.00 46.35           N  
ATOM   5200  CA  ILE B 314      14.733  29.850  -6.071  1.00 44.57           C  
ATOM   5201  C   ILE B 314      15.319  29.754  -7.510  1.00 46.18           C  
ATOM   5202  O   ILE B 314      14.594  29.856  -8.486  1.00 47.67           O  
ATOM   5203  CB  ILE B 314      15.009  31.268  -5.506  1.00 43.64           C  
ATOM   5204  CG1 ILE B 314      14.293  31.453  -4.173  1.00 41.20           C  
ATOM   5205  CG2 ILE B 314      14.612  32.328  -6.518  1.00 42.86           C  
ATOM   5206  CD1 ILE B 314      14.481  32.818  -3.543  1.00 37.94           C  
ATOM   5207  N   TYR B 315      16.630  29.567  -7.644  1.00 46.31           N  
ATOM   5208  CA  TYR B 315      17.238  29.460  -8.959  1.00 46.64           C  
ATOM   5209  C   TYR B 315      16.771  28.204  -9.664  1.00 46.83           C  
ATOM   5210  O   TYR B 315      16.440  28.228 -10.840  1.00 48.62           O  
ATOM   5211  CB  TYR B 315      18.765  29.391  -8.862  1.00 48.35           C  
ATOM   5212  CG  TYR B 315      19.469  30.570  -8.191  1.00 48.60           C  
ATOM   5213  CD1 TYR B 315      19.033  31.893  -8.375  1.00 48.44           C  
ATOM   5214  CD2 TYR B 315      20.611  30.365  -7.412  1.00 46.34           C  
ATOM   5215  CE1 TYR B 315      19.728  32.965  -7.787  1.00 44.01           C  
ATOM   5216  CE2 TYR B 315      21.299  31.425  -6.836  1.00 43.09           C  
ATOM   5217  CZ  TYR B 315      20.855  32.701  -7.020  1.00 40.57           C  
ATOM   5218  OH  TYR B 315      21.526  33.699  -6.402  1.00 35.32           O  
ATOM   5219  N   SER B 316      16.777  27.098  -8.941  1.00 47.85           N  
ATOM   5220  CA  SER B 316      16.375  25.810  -9.494  1.00 50.62           C  
ATOM   5221  C   SER B 316      14.970  25.805 -10.075  1.00 53.28           C  
ATOM   5222  O   SER B 316      14.611  24.895 -10.838  1.00 55.21           O  
ATOM   5223  CB  SER B 316      16.443  24.727  -8.424  1.00 49.75           C  
ATOM   5224  OG  SER B 316      15.436  24.937  -7.447  1.00 50.18           O  
ATOM   5225  N   VAL B 317      14.164  26.800  -9.714  1.00 53.74           N  
ATOM   5226  CA  VAL B 317      12.801  26.863 -10.230  1.00 54.33           C  
ATOM   5227  C   VAL B 317      12.558  28.100 -11.112  1.00 53.98           C  
ATOM   5228  O   VAL B 317      11.415  28.393 -11.450  1.00 54.77           O  
ATOM   5229  CB  VAL B 317      11.759  26.891  -9.081  1.00 54.00           C  
ATOM   5230  CG1 VAL B 317      10.418  26.502  -9.602  1.00 57.83           C  
ATOM   5231  CG2 VAL B 317      12.151  25.964  -7.977  1.00 52.72           C  
ATOM   5232  N   SER B 318      13.613  28.822 -11.491  1.00 53.45           N  
ATOM   5233  CA  SER B 318      13.444  30.029 -12.313  1.00 54.49           C  
ATOM   5234  C   SER B 318      14.645  30.365 -13.220  1.00 56.11           C  
ATOM   5235  O   SER B 318      14.490  31.059 -14.241  1.00 55.54           O  
ATOM   5236  CB  SER B 318      13.182  31.237 -11.418  1.00 55.18           C  
ATOM   5237  OG  SER B 318      14.283  31.476 -10.555  1.00 56.87           O  
ATOM   5238  N   HIS B 319      15.844  29.924 -12.830  1.00 55.86           N  
ATOM   5239  CA  HIS B 319      17.015  30.172 -13.645  1.00 54.92           C  
ATOM   5240  C   HIS B 319      17.046  29.060 -14.683  1.00 57.47           C  
ATOM   5241  O   HIS B 319      17.189  27.871 -14.324  1.00 57.28           O  
ATOM   5242  CB  HIS B 319      18.323  30.114 -12.820  1.00 52.36           C  
ATOM   5243  CG  HIS B 319      19.479  30.872 -13.442  1.00 47.71           C  
ATOM   5244  ND1 HIS B 319      20.118  30.469 -14.600  1.00 44.47           N  
ATOM   5245  CD2 HIS B 319      20.101  32.020 -13.060  1.00 42.41           C  
ATOM   5246  CE1 HIS B 319      21.077  31.327 -14.898  1.00 40.29           C  
ATOM   5247  NE2 HIS B 319      21.085  32.276 -13.976  1.00 37.63           N  
ATOM   5248  N   PRO B 320      16.866  29.424 -15.978  1.00 58.22           N  
ATOM   5249  CA  PRO B 320      16.887  28.468 -17.092  1.00 58.00           C  
ATOM   5250  C   PRO B 320      18.303  27.889 -17.316  1.00 58.01           C  
ATOM   5251  O   PRO B 320      18.524  26.685 -17.169  1.00 57.97           O  
ATOM   5252  CB  PRO B 320      16.390  29.306 -18.277  1.00 57.75           C  
ATOM   5253  CG  PRO B 320      16.813  30.710 -17.898  1.00 57.43           C  
ATOM   5254  CD  PRO B 320      16.453  30.764 -16.444  1.00 57.79           C  
ATOM   5255  N   LYS B 321      19.275  28.740 -17.641  1.00 58.11           N  
ATOM   5256  CA  LYS B 321      20.616  28.222 -17.898  1.00 58.03           C  
ATOM   5257  C   LYS B 321      21.132  27.427 -16.700  1.00 57.95           C  
ATOM   5258  O   LYS B 321      21.930  26.498 -16.870  1.00 61.09           O  
ATOM   5259  CB  LYS B 321      21.569  29.362 -18.316  1.00 57.72           C  
ATOM   5260  CG  LYS B 321      21.193  29.962 -19.694  1.00 58.25           C  
ATOM   5261  CD  LYS B 321      22.078  31.123 -20.118  1.00 61.29           C  
ATOM   5262  CE  LYS B 321      23.496  30.697 -20.478  1.00 62.02           C  
ATOM   5263  NZ  LYS B 321      24.363  31.877 -20.838  1.00 61.96           N  
ATOM   5264  N   PHE B 322      20.646  27.752 -15.506  1.00 55.05           N  
ATOM   5265  CA  PHE B 322      21.066  27.034 -14.317  1.00 55.21           C  
ATOM   5266  C   PHE B 322      20.328  25.710 -14.266  1.00 58.63           C  
ATOM   5267  O   PHE B 322      20.943  24.644 -14.111  1.00 61.81           O  
ATOM   5268  CB  PHE B 322      20.768  27.841 -13.042  1.00 51.63           C  
ATOM   5269  CG  PHE B 322      21.116  27.111 -11.738  1.00 46.74           C  
ATOM   5270  CD1 PHE B 322      22.402  26.634 -11.496  1.00 43.12           C  
ATOM   5271  CD2 PHE B 322      20.145  26.908 -10.757  1.00 44.70           C  
ATOM   5272  CE1 PHE B 322      22.699  25.967 -10.309  1.00 41.30           C  
ATOM   5273  CE2 PHE B 322      20.450  26.241  -9.564  1.00 40.56           C  
ATOM   5274  CZ  PHE B 322      21.718  25.771  -9.345  1.00 38.36           C  
ATOM   5275  N   ARG B 323      19.004  25.769 -14.380  1.00 60.95           N  
ATOM   5276  CA  ARG B 323      18.193  24.551 -14.346  1.00 61.95           C  
ATOM   5277  C   ARG B 323      18.703  23.574 -15.406  1.00 64.66           C  
ATOM   5278  O   ARG B 323      18.641  22.352 -15.217  1.00 66.47           O  
ATOM   5279  CB  ARG B 323      16.726  24.882 -14.626  1.00 60.46           C  
ATOM   5280  CG  ARG B 323      16.002  25.521 -13.468  1.00 60.15           C  
ATOM   5281  CD  ARG B 323      14.691  26.100 -13.929  1.00 57.42           C  
ATOM   5282  NE  ARG B 323      13.872  25.085 -14.553  1.00 55.64           N  
ATOM   5283  CZ  ARG B 323      13.172  24.175 -13.892  1.00 54.38           C  
ATOM   5284  NH1 ARG B 323      13.177  24.139 -12.560  1.00 46.42           N  
ATOM   5285  NH2 ARG B 323      12.454  23.296 -14.591  1.00 58.52           N  
ATOM   5286  N   GLU B 324      19.213  24.124 -16.513  1.00 66.27           N  
ATOM   5287  CA  GLU B 324      19.725  23.321 -17.621  1.00 68.20           C  
ATOM   5288  C   GLU B 324      20.982  22.553 -17.189  1.00 68.42           C  
ATOM   5289  O   GLU B 324      21.142  21.345 -17.444  1.00 66.93           O  
ATOM   5290  CB  GLU B 324      20.065  24.231 -18.806  1.00 70.59           C  
ATOM   5291  CG  GLU B 324      20.260  23.481 -20.120  1.00 74.16           C  
ATOM   5292  CD  GLU B 324      20.914  24.346 -21.157  1.00 75.05           C  
ATOM   5293  OE1 GLU B 324      21.019  23.917 -22.332  1.00 77.89           O  
ATOM   5294  OE2 GLU B 324      21.334  25.462 -20.778  1.00 74.01           O  
ATOM   5295  N   ALA B 325      21.879  23.275 -16.528  1.00 68.23           N  
ATOM   5296  CA  ALA B 325      23.118  22.685 -16.046  1.00 67.56           C  
ATOM   5297  C   ALA B 325      22.858  21.567 -15.023  1.00 67.05           C  
ATOM   5298  O   ALA B 325      23.555  20.543 -15.020  1.00 67.24           O  
ATOM   5299  CB  ALA B 325      24.015  23.771 -15.435  1.00 66.30           C  
ATOM   5300  N   ILE B 326      21.864  21.753 -14.156  1.00 66.10           N  
ATOM   5301  CA  ILE B 326      21.578  20.725 -13.167  1.00 65.98           C  
ATOM   5302  C   ILE B 326      21.115  19.426 -13.854  1.00 67.33           C  
ATOM   5303  O   ILE B 326      21.679  18.336 -13.618  1.00 67.83           O  
ATOM   5304  CB  ILE B 326      20.509  21.182 -12.163  1.00 63.02           C  
ATOM   5305  CG1 ILE B 326      20.863  22.558 -11.617  1.00 61.16           C  
ATOM   5306  CG2 ILE B 326      20.466  20.199 -10.998  1.00 62.55           C  
ATOM   5307  CD1 ILE B 326      19.872  23.097 -10.657  1.00 60.92           C  
ATOM   5308  N   SER B 327      20.105  19.545 -14.715  1.00 66.46           N  
ATOM   5309  CA  SER B 327      19.588  18.380 -15.426  1.00 65.57           C  
ATOM   5310  C   SER B 327      20.738  17.610 -16.084  1.00 65.75           C  
ATOM   5311  O   SER B 327      20.718  16.376 -16.121  1.00 66.85           O  
ATOM   5312  CB  SER B 327      18.546  18.799 -16.473  1.00 62.93           C  
ATOM   5313  OG  SER B 327      19.081  19.748 -17.359  1.00 63.67           O  
ATOM   5314  N   GLN B 328      21.749  18.332 -16.574  1.00 64.81           N  
ATOM   5315  CA  GLN B 328      22.905  17.699 -17.214  1.00 64.29           C  
ATOM   5316  C   GLN B 328      23.961  17.169 -16.232  1.00 63.72           C  
ATOM   5317  O   GLN B 328      24.959  16.570 -16.658  1.00 64.90           O  
ATOM   5318  CB  GLN B 328      23.622  18.679 -18.129  1.00 65.08           C  
ATOM   5319  CG  GLN B 328      22.990  18.913 -19.472  1.00 69.38           C  
ATOM   5320  CD  GLN B 328      23.864  19.835 -20.346  1.00 72.64           C  
ATOM   5321  OE1 GLN B 328      23.562  20.087 -21.529  1.00 73.44           O  
ATOM   5322  NE2 GLN B 328      24.960  20.340 -19.757  1.00 73.35           N  
ATOM   5323  N   THR B 329      23.762  17.361 -14.931  1.00 60.20           N  
ATOM   5324  CA  THR B 329      24.771  16.924 -13.991  1.00 58.07           C  
ATOM   5325  C   THR B 329      24.172  16.264 -12.750  1.00 58.86           C  
ATOM   5326  O   THR B 329      24.622  15.211 -12.283  1.00 56.78           O  
ATOM   5327  CB  THR B 329      25.654  18.140 -13.591  1.00 57.28           C  
ATOM   5328  OG1 THR B 329      24.852  19.324 -13.597  1.00 53.00           O  
ATOM   5329  CG2 THR B 329      26.810  18.332 -14.552  1.00 53.58           C  
ATOM   5330  N   PHE B 330      23.155  16.899 -12.199  1.00 60.38           N  
ATOM   5331  CA  PHE B 330      22.504  16.366 -11.012  1.00 61.64           C  
ATOM   5332  C   PHE B 330      21.019  16.366 -11.258  1.00 62.26           C  
ATOM   5333  O   PHE B 330      20.249  16.763 -10.387  1.00 63.24           O  
ATOM   5334  CB  PHE B 330      22.778  17.249  -9.801  1.00 59.88           C  
ATOM   5335  CG  PHE B 330      24.212  17.388  -9.479  1.00 57.51           C  
ATOM   5336  CD1 PHE B 330      24.951  16.284  -9.108  1.00 57.34           C  
ATOM   5337  CD2 PHE B 330      24.836  18.635  -9.563  1.00 55.77           C  
ATOM   5338  CE1 PHE B 330      26.303  16.423  -8.831  1.00 59.40           C  
ATOM   5339  CE2 PHE B 330      26.190  18.781  -9.287  1.00 55.35           C  
ATOM   5340  CZ  PHE B 330      26.928  17.682  -8.926  1.00 55.66           C  
ATOM   5341  N   PRO B 331      20.598  15.903 -12.435  1.00 62.37           N  
ATOM   5342  CA  PRO B 331      19.181  15.858 -12.809  1.00 63.92           C  
ATOM   5343  C   PRO B 331      18.202  15.410 -11.720  1.00 65.63           C  
ATOM   5344  O   PRO B 331      17.094  15.948 -11.609  1.00 63.55           O  
ATOM   5345  CB  PRO B 331      19.171  14.917 -14.004  1.00 61.73           C  
ATOM   5346  CG  PRO B 331      20.299  14.006 -13.662  1.00 62.03           C  
ATOM   5347  CD  PRO B 331      21.367  14.956 -13.247  1.00 62.13           C  
ATOM   5348  N   TRP B 332      18.593  14.456 -10.887  1.00 68.31           N  
ATOM   5349  CA  TRP B 332      17.637  13.989  -9.890  1.00 71.90           C  
ATOM   5350  C   TRP B 332      17.090  15.112  -9.042  1.00 72.13           C  
ATOM   5351  O   TRP B 332      16.007  15.003  -8.475  1.00 71.75           O  
ATOM   5352  CB  TRP B 332      18.265  12.943  -8.998  1.00 75.14           C  
ATOM   5353  CG  TRP B 332      19.246  13.497  -8.132  1.00 78.58           C  
ATOM   5354  CD1 TRP B 332      20.596  13.481  -8.310  1.00 78.87           C  
ATOM   5355  CD2 TRP B 332      18.996  14.108  -6.863  1.00 82.45           C  
ATOM   5356  NE1 TRP B 332      21.216  14.033  -7.216  1.00 82.33           N  
ATOM   5357  CE2 TRP B 332      20.255  14.430  -6.308  1.00 84.31           C  
ATOM   5358  CE3 TRP B 332      17.825  14.416  -6.132  1.00 83.14           C  
ATOM   5359  CZ2 TRP B 332      20.382  15.049  -5.031  1.00 85.04           C  
ATOM   5360  CZ3 TRP B 332      17.952  15.031  -4.870  1.00 83.08           C  
ATOM   5361  CH2 TRP B 332      19.221  15.337  -4.338  1.00 83.67           C  
ATOM   5362  N   VAL B 333      17.865  16.186  -8.953  1.00 73.61           N  
ATOM   5363  CA  VAL B 333      17.495  17.363  -8.174  1.00 74.02           C  
ATOM   5364  C   VAL B 333      16.222  17.995  -8.710  1.00 77.35           C  
ATOM   5365  O   VAL B 333      15.408  18.514  -7.946  1.00 80.36           O  
ATOM   5366  CB  VAL B 333      18.593  18.455  -8.212  1.00 69.40           C  
ATOM   5367  CG1 VAL B 333      18.092  19.698  -7.526  1.00 65.71           C  
ATOM   5368  CG2 VAL B 333      19.862  17.958  -7.568  1.00 66.34           C  
ATOM   5369  N   LEU B 334      16.046  17.958 -10.025  1.00 79.07           N  
ATOM   5370  CA  LEU B 334      14.871  18.569 -10.634  1.00 80.51           C  
ATOM   5371  C   LEU B 334      13.735  17.566 -10.789  1.00 82.91           C  
ATOM   5372  O   LEU B 334      12.841  17.791 -11.603  1.00 84.94           O  
ATOM   5373  CB  LEU B 334      15.247  19.150 -12.008  1.00 76.99           C  
ATOM   5374  CG  LEU B 334      16.252  20.299 -11.985  1.00 74.27           C  
ATOM   5375  CD1 LEU B 334      16.772  20.588 -13.379  1.00 72.51           C  
ATOM   5376  CD2 LEU B 334      15.571  21.515 -11.365  1.00 74.63           C  
ATOM   5377  N   THR B 335      13.752  16.471 -10.021  1.00 84.82           N  
ATOM   5378  CA  THR B 335      12.710  15.442 -10.156  1.00 87.64           C  
ATOM   5379  C   THR B 335      11.315  16.032 -10.228  1.00 88.84           C  
ATOM   5380  O   THR B 335      10.603  15.819 -11.213  1.00 89.52           O  
ATOM   5381  CB  THR B 335      12.764  14.387  -9.009  1.00 88.87           C  
ATOM   5382  OG1 THR B 335      13.452  14.941  -7.882  1.00 93.15           O  
ATOM   5383  CG2 THR B 335      13.469  13.094  -9.474  1.00 88.39           C  
ATOM   5384  N   CYS B 336      10.921  16.789  -9.206  1.00 90.45           N  
ATOM   5385  CA  CYS B 336       9.604  17.428  -9.191  1.00 90.97           C  
ATOM   5386  C   CYS B 336       9.552  18.661 -10.118  1.00 91.58           C  
ATOM   5387  O   CYS B 336       8.484  19.227 -10.333  1.00 91.37           O  
ATOM   5388  CB  CYS B 336       9.241  17.842  -7.757  1.00 91.51           C  
ATOM   5389  SG  CYS B 336       8.526  16.540  -6.742  1.00 91.69           S  
ATOM   5390  N   CYS B 337      10.706  19.055 -10.671  1.00 93.53           N  
ATOM   5391  CA  CYS B 337      10.835  20.234 -11.546  1.00 94.24           C  
ATOM   5392  C   CYS B 337      11.543  19.867 -12.868  1.00 93.80           C  
ATOM   5393  O   CYS B 337      12.570  20.441 -13.213  1.00 95.47           O  
ATOM   5394  CB  CYS B 337      11.617  21.344 -10.780  1.00 94.91           C  
ATOM   5395  SG  CYS B 337      11.717  21.017  -8.970  1.00 96.70           S  
ATOM   5396  N   GLN B 338      10.993  18.906 -13.605  1.00 92.86           N  
ATOM   5397  CA  GLN B 338      11.593  18.444 -14.865  1.00 90.49           C  
ATOM   5398  C   GLN B 338      12.089  19.581 -15.744  1.00 86.87           C  
ATOM   5399  O   GLN B 338      11.395  20.572 -15.940  1.00 85.39           O  
ATOM   5400  CB  GLN B 338      10.566  17.618 -15.651  1.00 94.75           C  
ATOM   5401  CG  GLN B 338      11.089  16.286 -16.177  1.00 98.05           C  
ATOM   5402  CD  GLN B 338      11.351  15.262 -15.063  1.00 99.50           C  
ATOM   5403  OE1 GLN B 338      10.408  14.728 -14.449  1.00 99.14           O  
ATOM   5404  NE2 GLN B 338      12.638  14.988 -14.798  1.00 98.77           N  
ATOM   5405  N   PHE B 339      13.288  19.451 -16.282  1.00 84.11           N  
ATOM   5406  CA  PHE B 339      13.782  20.510 -17.146  1.00 82.70           C  
ATOM   5407  C   PHE B 339      13.255  20.302 -18.565  1.00 85.18           C  
ATOM   5408  O   PHE B 339      12.972  19.160 -18.943  1.00 86.91           O  
ATOM   5409  CB  PHE B 339      15.302  20.516 -17.177  1.00 77.28           C  
ATOM   5410  CG  PHE B 339      15.862  21.533 -18.117  1.00 72.58           C  
ATOM   5411  CD1 PHE B 339      15.565  22.887 -17.954  1.00 69.98           C  
ATOM   5412  CD2 PHE B 339      16.650  21.144 -19.191  1.00 70.14           C  
ATOM   5413  CE1 PHE B 339      16.050  23.835 -18.860  1.00 67.43           C  
ATOM   5414  CE2 PHE B 339      17.140  22.091 -20.106  1.00 67.84           C  
ATOM   5415  CZ  PHE B 339      16.840  23.430 -19.940  1.00 66.01           C  
ATOM   5416  N   ASP B 340      13.119  21.397 -19.334  1.00 87.20           N  
ATOM   5417  CA  ASP B 340      12.633  21.391 -20.748  1.00 89.76           C  
ATOM   5418  C   ASP B 340      13.429  22.360 -21.611  1.00 88.99           C  
ATOM   5419  O   ASP B 340      13.599  23.517 -21.241  1.00 90.77           O  
ATOM   5420  CB  ASP B 340      11.147  21.813 -20.865  1.00 93.53           C  
ATOM   5421  CG  ASP B 340      10.707  22.117 -22.340  1.00 96.71           C  
ATOM   5422  OD1 ASP B 340       9.645  22.770 -22.526  1.00 95.46           O  
ATOM   5423  OD2 ASP B 340      11.404  21.696 -23.307  1.00 98.42           O  
ATOM   5424  N   ASP B 341      13.854  21.910 -22.786  1.00 87.68           N  
ATOM   5425  CA  ASP B 341      14.646  22.743 -23.688  1.00 86.82           C  
ATOM   5426  C   ASP B 341      13.996  24.059 -24.057  1.00 85.79           C  
ATOM   5427  O   ASP B 341      14.667  25.007 -24.478  1.00 84.56           O  
ATOM   5428  CB  ASP B 341      14.968  21.966 -24.957  1.00 88.03           C  
ATOM   5429  CG  ASP B 341      15.927  20.844 -24.706  1.00 89.85           C  
ATOM   5430  OD1 ASP B 341      16.131  20.003 -25.603  1.00 91.39           O  
ATOM   5431  OD2 ASP B 341      16.487  20.808 -23.595  1.00 93.77           O  
ATOM   5432  N   LYS B 342      12.685  24.116 -23.908  1.00 86.05           N  
ATOM   5433  CA  LYS B 342      11.964  25.327 -24.234  1.00 87.89           C  
ATOM   5434  C   LYS B 342      12.407  26.488 -23.345  1.00 87.37           C  
ATOM   5435  O   LYS B 342      12.411  27.635 -23.792  1.00 88.66           O  
ATOM   5436  CB  LYS B 342      10.452  25.099 -24.100  1.00 91.05           C  
ATOM   5437  CG  LYS B 342       9.813  24.289 -25.259  1.00 92.85           C  
ATOM   5438  CD  LYS B 342       8.282  24.200 -25.086  1.00 93.58           C  
ATOM   5439  CE  LYS B 342       7.591  23.660 -26.317  1.00 90.11           C  
ATOM   5440  NZ  LYS B 342       7.800  24.552 -27.473  1.00 90.01           N  
ATOM   5441  N   GLU B 343      12.790  26.186 -22.100  1.00 85.29           N  
ATOM   5442  CA  GLU B 343      13.238  27.203 -21.126  1.00 83.33           C  
ATOM   5443  C   GLU B 343      14.431  28.082 -21.554  1.00 83.02           C  
ATOM   5444  O   GLU B 343      14.485  29.292 -21.269  1.00 81.59           O  
ATOM   5445  CB  GLU B 343      13.633  26.544 -19.810  1.00 82.04           C  
ATOM   5446  CG  GLU B 343      12.572  25.713 -19.161  1.00 81.92           C  
ATOM   5447  CD  GLU B 343      13.017  25.220 -17.798  1.00 82.91           C  
ATOM   5448  OE1 GLU B 343      12.324  24.359 -17.215  1.00 83.09           O  
ATOM   5449  OE2 GLU B 343      14.066  25.700 -17.306  1.00 83.14           O  
ATOM   5450  N   THR B 344      15.397  27.458 -22.217  1.00 81.80           N  
ATOM   5451  CA  THR B 344      16.593  28.145 -22.647  1.00 79.35           C  
ATOM   5452  C   THR B 344      16.515  28.746 -24.043  1.00 80.97           C  
ATOM   5453  O   THR B 344      17.487  29.341 -24.492  1.00 81.36           O  
ATOM   5454  CB  THR B 344      17.786  27.191 -22.565  1.00 76.34           C  
ATOM   5455  OG1 THR B 344      17.463  25.956 -23.219  1.00 75.20           O  
ATOM   5456  CG2 THR B 344      18.110  26.901 -21.131  1.00 73.46           C  
ATOM   5457  N   GLU B 345      15.377  28.600 -24.731  1.00 83.13           N  
ATOM   5458  CA  GLU B 345      15.214  29.163 -26.088  1.00 85.28           C  
ATOM   5459  C   GLU B 345      15.551  30.661 -26.154  1.00 84.71           C  
ATOM   5460  O   GLU B 345      16.230  31.104 -27.077  1.00 84.71           O  
ATOM   5461  CB  GLU B 345      13.782  28.963 -26.599  1.00 86.89           C  
ATOM   5462  CG  GLU B 345      13.371  27.516 -26.737  1.00 93.30           C  
ATOM   5463  CD  GLU B 345      11.896  27.353 -27.096  1.00 98.14           C  
ATOM   5464  OE1 GLU B 345      11.424  26.184 -27.184  1.00100.29           O  
ATOM   5465  OE2 GLU B 345      11.208  28.391 -27.292  1.00101.12           O  
ATOM   5466  N   ASP B 346      15.086  31.429 -25.164  1.00 84.21           N  
ATOM   5467  CA  ASP B 346      15.318  32.872 -25.115  1.00 81.15           C  
ATOM   5468  C   ASP B 346      16.793  33.207 -24.983  1.00 79.49           C  
ATOM   5469  O   ASP B 346      17.266  34.161 -25.589  1.00 77.20           O  
ATOM   5470  CB  ASP B 346      14.534  33.485 -23.955  1.00 81.77           C  
ATOM   5471  CG  ASP B 346      13.803  34.774 -24.343  1.00 82.03           C  
ATOM   5472  OD1 ASP B 346      13.129  35.348 -23.470  1.00 83.02           O  
ATOM   5473  OD2 ASP B 346      13.888  35.221 -25.504  1.00 79.46           O  
ATOM   5474  N   ASP B 347      17.515  32.423 -24.188  1.00 79.98           N  
ATOM   5475  CA  ASP B 347      18.953  32.638 -24.005  1.00 82.13           C  
ATOM   5476  C   ASP B 347      19.727  32.301 -25.298  1.00 82.14           C  
ATOM   5477  O   ASP B 347      20.693  32.981 -25.660  1.00 80.32           O  
ATOM   5478  CB  ASP B 347      19.492  31.767 -22.856  1.00 85.06           C  
ATOM   5479  CG  ASP B 347      19.131  32.300 -21.481  1.00 87.62           C  
ATOM   5480  OD1 ASP B 347      19.618  33.402 -21.097  1.00 89.26           O  
ATOM   5481  OD2 ASP B 347      18.364  31.595 -20.786  1.00 89.44           O  
ATOM   5482  N   LYS B 348      19.303  31.231 -25.973  1.00 83.37           N  
ATOM   5483  CA  LYS B 348      19.919  30.781 -27.223  1.00 81.94           C  
ATOM   5484  C   LYS B 348      19.750  31.851 -28.283  1.00 80.37           C  
ATOM   5485  O   LYS B 348      20.716  32.253 -28.894  1.00 78.48           O  
ATOM   5486  CB  LYS B 348      19.258  29.483 -27.699  1.00 83.19           C  
ATOM   5487  CG  LYS B 348      19.403  28.307 -26.742  1.00 82.77           C  
ATOM   5488  CD  LYS B 348      18.445  27.199 -27.136  1.00 87.05           C  
ATOM   5489  CE  LYS B 348      18.475  26.037 -26.139  1.00 89.60           C  
ATOM   5490  NZ  LYS B 348      17.338  25.057 -26.333  1.00 87.45           N  
ATOM   5491  N   ASP B 349      18.511  32.294 -28.488  1.00 82.24           N  
ATOM   5492  CA  ASP B 349      18.189  33.339 -29.463  1.00 85.54           C  
ATOM   5493  C   ASP B 349      18.947  34.646 -29.168  1.00 88.46           C  
ATOM   5494  O   ASP B 349      19.414  35.336 -30.098  1.00 87.66           O  
ATOM   5495  CB  ASP B 349      16.681  33.627 -29.458  1.00 84.53           C  
ATOM   5496  CG  ASP B 349      15.875  32.515 -30.074  1.00 84.23           C  
ATOM   5497  OD1 ASP B 349      16.085  31.349 -29.696  1.00 88.31           O  
ATOM   5498  OD2 ASP B 349      15.020  32.799 -30.931  1.00 83.50           O  
ATOM   5499  N   ALA B 350      19.052  34.985 -27.875  1.00 91.00           N  
ATOM   5500  CA  ALA B 350      19.751  36.200 -27.420  1.00 92.75           C  
ATOM   5501  C   ALA B 350      21.274  36.131 -27.649  1.00 94.51           C  
ATOM   5502  O   ALA B 350      21.888  37.103 -28.093  1.00 93.90           O  
ATOM   5503  CB  ALA B 350      19.454  36.453 -25.935  1.00 90.13           C  
ATOM   5504  N   GLU B 351      21.875  34.978 -27.359  1.00 96.92           N  
ATOM   5505  CA  GLU B 351      23.311  34.794 -27.523  1.00 98.27           C  
ATOM   5506  C   GLU B 351      23.722  34.430 -28.946  1.00 98.52           C  
ATOM   5507  O   GLU B 351      24.814  34.803 -29.375  1.00 98.42           O  
ATOM   5508  CB  GLU B 351      23.818  33.721 -26.557  1.00 99.88           C  
ATOM   5509  CG  GLU B 351      23.537  34.014 -25.079  1.00103.97           C  
ATOM   5510  CD  GLU B 351      23.973  35.424 -24.637  1.00106.42           C  
ATOM   5511  OE1 GLU B 351      24.968  35.958 -25.190  1.00107.83           O  
ATOM   5512  OE2 GLU B 351      23.329  35.989 -23.721  1.00105.90           O  
ATOM   5513  N   THR B 352      22.860  33.703 -29.668  1.00 99.76           N  
ATOM   5514  CA  THR B 352      23.145  33.281 -31.053  1.00100.34           C  
ATOM   5515  C   THR B 352      23.418  34.514 -31.894  1.00100.95           C  
ATOM   5516  O   THR B 352      22.514  35.294 -32.237  1.00100.67           O  
ATOM   5517  CB  THR B 352      21.965  32.436 -31.699  1.00100.68           C  
ATOM   5518  OG1 THR B 352      21.890  31.149 -31.060  1.00101.16           O  
ATOM   5519  CG2 THR B 352      22.176  32.223 -33.224  1.00 97.64           C  
ATOM   5520  N   GLU B 353      24.694  34.680 -32.210  1.00100.83           N  
ATOM   5521  CA  GLU B 353      25.127  35.807 -32.991  1.00100.82           C  
ATOM   5522  C   GLU B 353      24.639  35.694 -34.427  1.00 99.69           C  
ATOM   5523  O   GLU B 353      24.969  34.735 -35.114  1.00100.75           O  
ATOM   5524  CB  GLU B 353      26.643  35.878 -32.962  1.00102.31           C  
ATOM   5525  CG  GLU B 353      27.144  37.250 -33.304  1.00106.68           C  
ATOM   5526  CD  GLU B 353      26.556  38.318 -32.390  1.00108.28           C  
ATOM   5527  OE1 GLU B 353      26.785  38.228 -31.153  1.00106.55           O  
ATOM   5528  OE2 GLU B 353      25.866  39.241 -32.911  1.00109.87           O  
ATOM   5529  N   ILE B 354      23.841  36.656 -34.878  1.00 97.90           N  
ATOM   5530  CA  ILE B 354      23.353  36.628 -36.257  1.00 95.85           C  
ATOM   5531  C   ILE B 354      24.588  36.467 -37.193  1.00 93.97           C  
ATOM   5532  O   ILE B 354      25.446  37.353 -37.258  1.00 93.95           O  
ATOM   5533  CB  ILE B 354      22.517  37.957 -36.623  1.00 95.54           C  
ATOM   5534  CG1 ILE B 354      23.251  39.219 -36.140  1.00 94.92           C  
ATOM   5535  CG2 ILE B 354      21.085  37.910 -36.026  1.00 92.41           C  
ATOM   5536  CD1 ILE B 354      22.946  39.650 -34.719  1.00 94.31           C  
ATOM   5537  N   PRO B 355      24.702  35.319 -37.901  1.00 91.94           N  
ATOM   5538  CA  PRO B 355      25.825  35.046 -38.816  1.00 89.75           C  
ATOM   5539  C   PRO B 355      25.843  35.943 -40.023  1.00 87.99           C  
ATOM   5540  O   PRO B 355      26.899  36.549 -40.276  1.00 87.25           O  
ATOM   5541  CB  PRO B 355      25.619  33.590 -39.210  1.00 90.43           C  
ATOM   5542  CG  PRO B 355      24.130  33.455 -39.169  1.00 92.64           C  
ATOM   5543  CD  PRO B 355      23.772  34.176 -37.878  1.00 92.26           C  
TER    5544      PRO B 355                                                      
HETATM 5545  C1  PLM A1001      -6.220  45.508  80.422  1.00 48.52           C  
HETATM 5546  O2  PLM A1001      -7.269  44.906  80.438  1.00 45.17           O  
HETATM 5547  C2  PLM A1001      -4.950  44.728  80.143  1.00 51.80           C  
HETATM 5548  C3  PLM A1001      -4.283  45.107  78.816  1.00 58.34           C  
HETATM 5549  C4  PLM A1001      -4.138  43.888  77.912  1.00 62.26           C  
HETATM 5550  C5  PLM A1001      -3.253  44.179  76.724  1.00 65.92           C  
HETATM 5551  C6  PLM A1001      -3.145  42.933  75.854  1.00 67.40           C  
HETATM 5552  C7  PLM A1001      -2.765  43.282  74.416  1.00 66.82           C  
HETATM 5553  C8  PLM A1001      -2.668  42.021  73.531  1.00 65.99           C  
HETATM 5554  C9  PLM A1001      -1.919  42.277  72.222  1.00 70.13           C  
HETATM 5555  CA  PLM A1001      -2.808  42.787  71.098  1.00 69.98           C  
HETATM 5556  CB  PLM A1001      -1.973  43.618  70.131  1.00 72.27           C  
HETATM 5557  CC  PLM A1001      -2.642  43.755  68.770  1.00 73.70           C  
HETATM 5558  CD  PLM A1001      -1.774  44.600  67.830  1.00 74.80           C  
HETATM 5559  CE  PLM A1001      -1.680  43.960  66.443  1.00 71.57           C  
HETATM 5560  CF  PLM A1001      -2.371  44.807  65.360  1.00 69.92           C  
HETATM 5561  CG  PLM A1001      -2.268  44.159  63.971  1.00 68.01           C  
HETATM 5562  C1  BOG A1005      12.307  44.158  90.242  1.00 93.53           C  
HETATM 5563  O1  BOG A1005      13.163  44.112  89.169  1.00 86.85           O  
HETATM 5564  C2  BOG A1005      12.740  42.933  91.081  1.00 97.01           C  
HETATM 5565  O2  BOG A1005      12.604  41.625  90.372  1.00100.87           O  
HETATM 5566  C3  BOG A1005      11.811  43.017  92.221  1.00 97.58           C  
HETATM 5567  O3  BOG A1005      12.195  41.932  93.013  1.00 95.67           O  
HETATM 5568  C4  BOG A1005      11.976  44.405  92.935  1.00 97.06           C  
HETATM 5569  O4  BOG A1005      11.091  44.477  94.001  1.00 95.52           O  
HETATM 5570  C5  BOG A1005      11.574  45.561  92.086  1.00 96.89           C  
HETATM 5571  O5  BOG A1005      12.473  45.470  90.978  1.00 94.93           O  
HETATM 5572  C6  BOG A1005      11.764  46.972  92.816  1.00 96.72           C  
HETATM 5573  O6  BOG A1005      10.559  47.885  92.556  1.00 92.00           O  
HETATM 5574  C1' BOG A1005      12.228  44.283  88.114  1.00 78.94           C  
HETATM 5575  C2' BOG A1005      13.030  44.840  87.027  1.00 73.47           C  
HETATM 5576  C3' BOG A1005      12.769  43.881  85.896  1.00 68.65           C  
HETATM 5577  C4' BOG A1005      14.038  43.874  85.208  1.00 65.31           C  
HETATM 5578  C5' BOG A1005      13.747  43.452  83.793  1.00 59.01           C  
HETATM 5579  C6' BOG A1005      14.830  42.553  83.508  1.00 53.81           C  
HETATM 5580  C7' BOG A1005      14.362  41.893  82.267  1.00 53.71           C  
HETATM 5581  C8' BOG A1005      14.598  40.510  82.566  1.00 50.72           C  
HETATM 5582  C1  RET A1000      19.266  44.725  61.143  1.00 49.63           C  
HETATM 5583  C2  RET A1000      20.391  44.067  62.026  1.00 48.57           C  
HETATM 5584  C3  RET A1000      19.967  43.345  63.177  1.00 47.89           C  
HETATM 5585  C4  RET A1000      18.982  44.109  64.032  1.00 51.88           C  
HETATM 5586  C5  RET A1000      17.769  44.615  63.267  1.00 51.69           C  
HETATM 5587  C6  RET A1000      17.866  44.880  61.941  1.00 50.27           C  
HETATM 5588  C7  RET A1000      16.744  45.284  61.034  1.00 47.65           C  
HETATM 5589  C8  RET A1000      15.681  44.538  60.907  1.00 45.05           C  
HETATM 5590  C9  RET A1000      14.712  44.622  59.854  1.00 43.16           C  
HETATM 5591  C10 RET A1000      13.919  43.526  59.835  1.00 41.88           C  
HETATM 5592  C11 RET A1000      13.053  42.997  58.824  1.00 37.05           C  
HETATM 5593  C12 RET A1000      12.628  41.746  59.060  1.00 35.85           C  
HETATM 5594  C13 RET A1000      12.106  40.794  58.126  1.00 34.80           C  
HETATM 5595  C14 RET A1000      11.504  39.691  58.578  1.00 33.88           C  
HETATM 5596  C15 RET A1000      11.030  38.646  57.685  1.00 34.28           C  
HETATM 5597  C16 RET A1000      19.814  46.135  60.806  1.00 49.34           C  
HETATM 5598  C17 RET A1000      19.129  43.966  59.829  1.00 46.89           C  
HETATM 5599  C18 RET A1000      16.542  44.764  64.129  1.00 53.82           C  
HETATM 5600  C19 RET A1000      14.881  45.638  58.778  1.00 42.57           C  
HETATM 5601  C20 RET A1000      12.404  41.012  56.670  1.00 30.66           C  
HETATM 5602  S   SO4 B 449      34.567  48.350 -17.922  1.00 88.67           S  
HETATM 5603  O1  SO4 B 449      34.657  49.691 -18.533  1.00 87.35           O  
HETATM 5604  O2  SO4 B 449      34.597  48.521 -16.449  1.00 85.56           O  
HETATM 5605  O3  SO4 B 449      33.299  47.706 -18.336  1.00 87.06           O  
HETATM 5606  O4  SO4 B 449      35.693  47.510 -18.407  1.00 86.04           O  
HETATM 5607  O12 PC1 B1004      17.781  56.410  28.242  1.00120.35           O  
HETATM 5608  P   PC1 B1004      17.068  55.943  26.886  1.00119.07           P  
HETATM 5609  O14 PC1 B1004      15.802  56.825  26.548  1.00120.17           O  
HETATM 5610  O13 PC1 B1004      16.746  54.431  27.081  1.00115.89           O  
HETATM 5611  C11 PC1 B1004      15.886  54.130  28.215  1.00112.29           C  
HETATM 5612  C12 PC1 B1004      15.661  52.608  28.291  1.00110.75           C  
HETATM 5613  O11 PC1 B1004      18.028  55.983  25.599  1.00115.57           O  
HETATM 5614  C1  PC1 B1004      19.418  56.408  25.806  1.00106.55           C  
HETATM 5615  C2  PC1 B1004      19.931  57.522  24.839  1.00 99.18           C  
HETATM 5616  O21 PC1 B1004      19.783  57.117  23.402  1.00 96.49           O  
HETATM 5617  C21 PC1 B1004      18.531  57.505  22.527  1.00 90.80           C  
HETATM 5618  O22 PC1 B1004      17.520  58.177  22.926  1.00 88.38           O  
HETATM 5619  C22 PC1 B1004      18.519  57.061  21.106  1.00 84.78           C  
HETATM 5620  C23 PC1 B1004      19.951  57.090  20.452  1.00 76.61           C  
HETATM 5621  C24 PC1 B1004      20.159  58.260  19.482  1.00 69.52           C  
HETATM 5622  C25 PC1 B1004      19.744  57.933  18.011  1.00 64.92           C  
HETATM 5623  C26 PC1 B1004      20.878  58.045  17.057  1.00 57.40           C  
HETATM 5624  C27 PC1 B1004      20.394  57.722  15.631  1.00 54.46           C  
HETATM 5625  C28 PC1 B1004      21.526  57.823  14.727  1.00 57.46           C  
HETATM 5626  C29 PC1 B1004      21.120  58.597  13.535  1.00 59.21           C  
HETATM 5627  C2A PC1 B1004      22.253  58.763  12.503  1.00 55.70           C  
HETATM 5628  C2B PC1 B1004      21.757  59.539  11.335  1.00 55.49           C  
HETATM 5629  C2C PC1 B1004      22.835  59.752  10.229  1.00 61.20           C  
HETATM 5630  C2D PC1 B1004      22.331  60.571   8.992  1.00 61.53           C  
HETATM 5631  C2E PC1 B1004      22.328  59.704   7.675  1.00 62.10           C  
HETATM 5632  C2F PC1 B1004      23.679  59.681   6.954  1.00 59.26           C  
HETATM 5633  C3  PC1 B1004      21.400  57.875  25.154  1.00 94.69           C  
HETATM 5634  O31 PC1 B1004      22.288  56.729  24.804  1.00 85.25           O  
HETATM 5635  C31 PC1 B1004      23.683  57.162  24.565  1.00 78.89           C  
HETATM 5636  O32 PC1 B1004      24.277  57.976  25.308  1.00 79.76           O  
HETATM 5637  C32 PC1 B1004      24.377  56.573  23.364  1.00 71.37           C  
HETATM 5638  C33 PC1 B1004      23.603  56.490  22.050  1.00 65.22           C  
HETATM 5639  C34 PC1 B1004      24.469  55.885  21.025  1.00 59.53           C  
HETATM 5640  C35 PC1 B1004      24.266  56.589  19.689  1.00 54.17           C  
HETATM 5641  C36 PC1 B1004      25.081  56.012  18.701  1.00 48.34           C  
HETATM 5642  C37 PC1 B1004      24.807  56.780  17.411  1.00 44.56           C  
HETATM 5643  C38 PC1 B1004      24.818  55.875  16.284  1.00 46.13           C  
HETATM 5644  C39 PC1 B1004      25.490  56.508  15.067  1.00 47.46           C  
HETATM 5645  C3A PC1 B1004      25.465  55.563  13.905  1.00 48.06           C  
HETATM 5646  C1  BOG B1005      23.481  37.248 -18.421  1.00110.76           C  
HETATM 5647  O1  BOG B1005      22.785  38.075 -17.575  1.00108.96           O  
HETATM 5648  C2  BOG B1005      22.416  36.884 -19.471  1.00111.72           C  
HETATM 5649  O2  BOG B1005      21.221  36.189 -18.913  1.00112.64           O  
HETATM 5650  C3  BOG B1005      23.195  36.005 -20.358  1.00111.24           C  
HETATM 5651  O3  BOG B1005      22.261  35.673 -21.332  1.00109.43           O  
HETATM 5652  C4  BOG B1005      24.438  36.786 -20.917  1.00110.14           C  
HETATM 5653  O4  BOG B1005      25.184  35.955 -21.743  1.00109.62           O  
HETATM 5654  C5  BOG B1005      25.407  37.144 -19.880  1.00109.41           C  
HETATM 5655  O5  BOG B1005      24.666  37.978 -19.015  1.00109.16           O  
HETATM 5656  C6  BOG B1005      26.627  37.947 -20.442  1.00109.58           C  
HETATM 5657  O6  BOG B1005      27.361  38.538 -19.252  1.00109.72           O  
HETATM 5658  C1' BOG B1005      23.266  37.619 -16.320  1.00104.26           C  
HETATM 5659  C2' BOG B1005      22.578  38.521 -15.389  1.00100.41           C  
HETATM 5660  C3' BOG B1005      22.968  37.987 -14.021  1.00 95.80           C  
HETATM 5661  C4' BOG B1005      22.135  38.776 -13.140  1.00 87.71           C  
HETATM 5662  C5' BOG B1005      22.374  38.218 -11.786  1.00 76.78           C  
HETATM 5663  C6' BOG B1005      21.036  38.059 -11.366  1.00 72.35           C  
HETATM 5664  C7' BOG B1005      21.125  36.792 -10.640  1.00 70.98           C  
HETATM 5665  C8' BOG B1005      19.746  36.562 -10.325  1.00 70.18           C  
HETATM 5666  C1  RET B1000      20.443  43.038  11.304  1.00 22.91           C  
HETATM 5667  C2  RET B1000      19.217  43.517  10.454  1.00 21.83           C  
HETATM 5668  C3  RET B1000      18.942  42.846   9.224  1.00 22.45           C  
HETATM 5669  C4  RET B1000      20.141  42.554   8.336  1.00 24.07           C  
HETATM 5670  C5  RET B1000      21.316  41.929   9.076  1.00 25.90           C  
HETATM 5671  C6  RET B1000      21.484  42.163  10.451  1.00 25.11           C  
HETATM 5672  C7  RET B1000      22.515  41.569  11.358  1.00 24.49           C  
HETATM 5673  C8  RET B1000      23.013  40.382  11.196  1.00 23.57           C  
HETATM 5674  C9  RET B1000      23.623  39.700  12.259  1.00 22.16           C  
HETATM 5675  C10 RET B1000      23.603  38.384  12.009  1.00 25.27           C  
HETATM 5676  C11 RET B1000      23.690  37.386  13.004  1.00 27.42           C  
HETATM 5677  C12 RET B1000      23.183  36.157  12.713  1.00 26.03           C  
HETATM 5678  C13 RET B1000      22.775  35.221  13.747  1.00 26.95           C  
HETATM 5679  C14 RET B1000      22.420  33.965  13.405  1.00 31.79           C  
HETATM 5680  C15 RET B1000      21.877  33.021  14.368  1.00 37.45           C  
HETATM 5681  C16 RET B1000      21.130  44.335  11.786  1.00 22.41           C  
HETATM 5682  C17 RET B1000      19.931  42.286  12.509  1.00 20.00           C  
HETATM 5683  C18 RET B1000      22.190  41.096   8.151  1.00 25.14           C  
HETATM 5684  C19 RET B1000      23.820  40.375  13.590  1.00 21.84           C  
HETATM 5685  C20 RET B1000      22.583  35.790  15.144  1.00 20.00           C  
HETATM 5686  O   HOH A 500      10.118  34.511  51.388  1.00 39.93           O  
HETATM 5687  O   HOH A 501      13.116  39.797  66.651  1.00 20.00           O  
HETATM 5688  O   HOH A 502      11.898  37.753  65.141  1.00 26.40           O  
HETATM 5689  O   HOH A 503      13.389  39.442  69.166  1.00 20.00           O  
HETATM 5690  O   HOH A 504      13.127  40.178  71.554  1.00 52.43           O  
HETATM 5691  O   HOH A 505      10.456  41.899  66.786  1.00 20.00           O  
HETATM 5692  O   HOH A 506      12.062  37.935  71.983  1.00 49.64           O  
HETATM 5693  O   HOH A 507       9.606  40.526  77.222  1.00 56.79           O  
HETATM 5694  O   HOH A 508       8.640  39.929  74.294  1.00 48.17           O  
HETATM 5695  O   HOH A 509       7.929  34.949  65.204  1.00 56.72           O  
HETATM 5696  O   HOH A 510      19.888  35.358  61.241  1.00 42.31           O  
HETATM 5697  O   HOH A 511       1.273  34.404  62.583  1.00 36.89           O  
HETATM 5698  O   HOH A 512       0.185  37.377  58.962  1.00 27.83           O  
HETATM 5699  O   HOH A 513       6.810  34.515  43.038  1.00 34.61           O  
HETATM 5700  O   HOH A 514       7.727  32.425  44.803  1.00 44.81           O  
HETATM 5701  O   HOH A 515      14.345  54.980  58.146  1.00 55.29           O  
HETATM 5702  O   HOH A 516      23.729  44.265  45.088  1.00 31.79           O  
HETATM 5703  O   HOH A 517      16.580  43.062  50.007  1.00 42.91           O  
HETATM 5704  O   HOH A 518      16.073  50.372  47.021  1.00 20.00           O  
HETATM 5705  O   HOH A 519       0.067  40.165  45.636  1.00 39.70           O  
HETATM 5706  O   HOH A 520      11.327  48.619  88.747  1.00 30.39           O  
HETATM 5707  O   HOH A 521      11.392  37.630  90.375  1.00 84.38           O  
HETATM 5708  O   HOH A 522      11.227  40.998  86.411  1.00 62.18           O  
HETATM 5709  O   HOH A 523      11.694  29.211  44.986  1.00 39.30           O  
HETATM 5710  O   HOH A 524      -4.611  26.971  81.044  1.00 62.50           O  
HETATM 5711  O   HOH A 525       7.618  39.991  40.303  1.00 40.75           O  
HETATM 5712  O   HOH A 526       8.641  42.967  90.392  1.00 56.74           O  
HETATM 5713  O   HOH A 527      17.857  49.513  94.785  1.00 85.43           O  
HETATM 5714  O   HOH A 529       6.155  34.587  63.439  1.00 56.77           O  
HETATM 5715  O   HOH B 500      19.482  29.666  21.250  1.00 26.08           O  
HETATM 5716  O   HOH B 501      21.367  35.274   5.320  1.00 20.00           O  
HETATM 5717  O   HOH B 502      20.439  33.319   6.865  1.00 38.42           O  
HETATM 5718  O   HOH B 503      20.150  34.946   3.188  1.00 34.87           O  
HETATM 5719  O   HOH B 504      20.208  35.341   0.893  1.00 55.92           O  
HETATM 5720  O   HOH B 505      23.818  34.808   4.594  1.00 48.60           O  
HETATM 5721  O   HOH B 506      20.137  31.964   0.101  1.00 25.53           O  
HETATM 5722  O   HOH B 507      23.734  32.142  -4.849  1.00 69.25           O  
HETATM 5723  O   HOH B 508      23.095  31.602  -2.361  1.00 40.70           O  
HETATM 5724  O   HOH B 509      21.070  27.910   6.916  1.00 53.38           O  
HETATM 5725  O   HOH B 510      13.702  32.058   6.005  1.00 20.00           O  
HETATM 5726  O   HOH B 511      12.653  37.261  11.086  1.00 42.76           O  
HETATM 5727  O   HOH B 512      25.480  23.152   9.175  1.00 20.00           O  
HETATM 5728  O   HOH B 513      28.106  24.385  13.265  1.00 44.58           O  
HETATM 5729  O   HOH B 514      26.042  44.979   3.878  1.00 20.00           O  
HETATM 5730  O   HOH B 515      24.243  28.071  26.670  1.00 23.10           O  
HETATM 5731  O   HOH B 516      19.738  26.297  26.916  1.00 44.55           O  
HETATM 5732  O   HOH B 517      31.130  46.086  13.703  1.00 24.36           O  
HETATM 5733  O   HOH B 518      16.892  45.828  26.579  1.00 37.28           O  
HETATM 5734  O   HOH B 519      22.717  39.568  25.661  1.00 20.00           O  
HETATM 5735  O   HOH B 520      26.454  43.838  20.386  1.00 47.63           O  
HETATM 5736  O   HOH B 521      27.219  44.756  24.972  1.00 20.00           O  
HETATM 5737  O   HOH B 522      30.718  26.314  26.555  1.00 28.53           O  
HETATM 5738  O   HOH B 523      18.727  34.431 -18.989  1.00 50.39           O  
HETATM 5739  O   HOH B 524      20.306  32.466 -17.902  1.00 35.51           O  
HETATM 5740  O   HOH B 525      22.794  34.910 -14.186  1.00 23.91           O  
HETATM 5741  O   HOH B 526      21.067  39.884  21.820  1.00 27.11           O  
HETATM 5742  O   HOH B 527      24.451  32.899 -17.899  1.00 49.58           O  
HETATM 5743  O   HOH B 528      23.997  41.743 -17.682  1.00 82.36           O  
HETATM 5744  O   HOH B 529      21.806  27.143   9.517  1.00 60.03           O  
CONECT  800 1419                                                                
CONECT 1419  800                                                                
CONECT 2360 5596                                                                
CONECT 3581 4200                                                                
CONECT 4200 3581                                                                
CONECT 5141 5680                                                                
CONECT 5545 5546 5547                                                           
CONECT 5546 5545                                                                
CONECT 5547 5545 5548                                                           
CONECT 5548 5547 5549                                                           
CONECT 5549 5548 5550                                                           
CONECT 5550 5549 5551                                                           
CONECT 5551 5550 5552                                                           
CONECT 5552 5551 5553                                                           
CONECT 5553 5552 5554                                                           
CONECT 5554 5553 5555                                                           
CONECT 5555 5554 5556                                                           
CONECT 5556 5555 5557                                                           
CONECT 5557 5556 5558                                                           
CONECT 5558 5557 5559                                                           
CONECT 5559 5558 5560                                                           
CONECT 5560 5559 5561                                                           
CONECT 5561 5560                                                                
CONECT 5562 5563 5564 5571                                                      
CONECT 5563 5562 5574                                                           
CONECT 5564 5562 5565 5566                                                      
CONECT 5565 5564                                                                
CONECT 5566 5564 5567 5568                                                      
CONECT 5567 5566                                                                
CONECT 5568 5566 5569 5570                                                      
CONECT 5569 5568                                                                
CONECT 5570 5568 5571 5572                                                      
CONECT 5571 5562 5570                                                           
CONECT 5572 5570 5573                                                           
CONECT 5573 5572                                                                
CONECT 5574 5563 5575                                                           
CONECT 5575 5574 5576                                                           
CONECT 5576 5575 5577                                                           
CONECT 5577 5576 5578                                                           
CONECT 5578 5577 5579                                                           
CONECT 5579 5578 5580                                                           
CONECT 5580 5579 5581                                                           
CONECT 5581 5580                                                                
CONECT 5582 5583 5587 5597 5598                                                 
CONECT 5583 5582 5584                                                           
CONECT 5584 5583 5585                                                           
CONECT 5585 5584 5586                                                           
CONECT 5586 5585 5587 5599                                                      
CONECT 5587 5582 5586 5588                                                      
CONECT 5588 5587 5589                                                           
CONECT 5589 5588 5590                                                           
CONECT 5590 5589 5591 5600                                                      
CONECT 5591 5590 5592                                                           
CONECT 5592 5591 5593                                                           
CONECT 5593 5592 5594                                                           
CONECT 5594 5593 5595 5601                                                      
CONECT 5595 5594 5596                                                           
CONECT 5596 2360 5595                                                           
CONECT 5597 5582                                                                
CONECT 5598 5582                                                                
CONECT 5599 5586                                                                
CONECT 5600 5590                                                                
CONECT 5601 5594                                                                
CONECT 5602 5603 5604 5605 5606                                                 
CONECT 5603 5602                                                                
CONECT 5604 5602                                                                
CONECT 5605 5602                                                                
CONECT 5606 5602                                                                
CONECT 5607 5608                                                                
CONECT 5608 5607 5609 5610 5613                                                 
CONECT 5609 5608                                                                
CONECT 5610 5608 5611                                                           
CONECT 5611 5610 5612                                                           
CONECT 5612 5611                                                                
CONECT 5613 5608 5614                                                           
CONECT 5614 5613 5615                                                           
CONECT 5615 5614 5616 5633                                                      
CONECT 5616 5615 5617                                                           
CONECT 5617 5616 5618 5619                                                      
CONECT 5618 5617                                                                
CONECT 5619 5617 5620                                                           
CONECT 5620 5619 5621                                                           
CONECT 5621 5620 5622                                                           
CONECT 5622 5621 5623                                                           
CONECT 5623 5622 5624                                                           
CONECT 5624 5623 5625                                                           
CONECT 5625 5624 5626                                                           
CONECT 5626 5625 5627                                                           
CONECT 5627 5626 5628                                                           
CONECT 5628 5627 5629                                                           
CONECT 5629 5628 5630                                                           
CONECT 5630 5629 5631                                                           
CONECT 5631 5630 5632                                                           
CONECT 5632 5631                                                                
CONECT 5633 5615 5634                                                           
CONECT 5634 5633 5635                                                           
CONECT 5635 5634 5636 5637                                                      
CONECT 5636 5635                                                                
CONECT 5637 5635 5638                                                           
CONECT 5638 5637 5639                                                           
CONECT 5639 5638 5640                                                           
CONECT 5640 5639 5641                                                           
CONECT 5641 5640 5642                                                           
CONECT 5642 5641 5643                                                           
CONECT 5643 5642 5644                                                           
CONECT 5644 5643 5645                                                           
CONECT 5645 5644                                                                
CONECT 5646 5647 5648 5655                                                      
CONECT 5647 5646 5658                                                           
CONECT 5648 5646 5649 5650                                                      
CONECT 5649 5648                                                                
CONECT 5650 5648 5651 5652                                                      
CONECT 5651 5650                                                                
CONECT 5652 5650 5653 5654                                                      
CONECT 5653 5652                                                                
CONECT 5654 5652 5655 5656                                                      
CONECT 5655 5646 5654                                                           
CONECT 5656 5654 5657                                                           
CONECT 5657 5656                                                                
CONECT 5658 5647 5659                                                           
CONECT 5659 5658 5660                                                           
CONECT 5660 5659 5661                                                           
CONECT 5661 5660 5662                                                           
CONECT 5662 5661 5663                                                           
CONECT 5663 5662 5664                                                           
CONECT 5664 5663 5665                                                           
CONECT 5665 5664                                                                
CONECT 5666 5667 5671 5681 5682                                                 
CONECT 5667 5666 5668                                                           
CONECT 5668 5667 5669                                                           
CONECT 5669 5668 5670                                                           
CONECT 5670 5669 5671 5683                                                      
CONECT 5671 5666 5670 5672                                                      
CONECT 5672 5671 5673                                                           
CONECT 5673 5672 5674                                                           
CONECT 5674 5673 5675 5684                                                      
CONECT 5675 5674 5676                                                           
CONECT 5676 5675 5677                                                           
CONECT 5677 5676 5678                                                           
CONECT 5678 5677 5679 5685                                                      
CONECT 5679 5678 5680                                                           
CONECT 5680 5141 5679                                                           
CONECT 5681 5666                                                                
CONECT 5682 5666                                                                
CONECT 5683 5670                                                                
CONECT 5684 5674                                                                
CONECT 5685 5678                                                                
MASTER      529    0    7   35    4    0    0    6 5742    2  147   70          
END