HEADER    MEMBRANE PROTEIN                        13-AUG-07   2Z73              
TITLE     CRYSTAL STRUCTURE 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                               
KEYWDS    VISUAL PIGMENT, GQ-TYPE, G-PROTEIN COUPLED RECEPTOR, CHROMOPHORE,     
KEYWDS   2 GLYCOPROTEIN, LIPOPROTEIN, MEMBRANE, PALMITATE, PHOSPHORYLATION,     
KEYWDS   3 PHOTORECEPTOR PROTEIN, RETINAL PROTEIN, SENSORY TRANSDUCTION,        
KEYWDS   4 TRANSDUCER, TRANSMEMBRANE, VISION, MEMBRANE PROTEIN                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MURAKAMI,T.KOUYAMA                                                  
REVDAT   5   29-JUL-20 2Z73    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   11-OCT-17 2Z73    1       REMARK                                   
REVDAT   3   24-FEB-09 2Z73    1       VERSN                                    
REVDAT   2   20-MAY-08 2Z73    1       JRNL                                     
REVDAT   1   13-MAY-08 2Z73    0                                                
JRNL        AUTH   M.MURAKAMI,T.KOUYAMA                                         
JRNL        TITL   CRYSTAL STRUCTURE OF SQUID RHODOPSIN.                        
JRNL        REF    NATURE                        V. 453   363 2008              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   18480818                                                     
JRNL        DOI    10.1038/NATURE06925                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2204034.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 43279                          
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) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2161                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.59                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.08                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3989                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2781                       
REMARK   3   BIN FREE R VALUE                    : 0.2978                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 182                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.035                        
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          : 236                                     
REMARK   3   SOLVENT ATOMS            : 57                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14400                                             
REMARK   3    B22 (A**2) : -0.14400                                             
REMARK   3    B33 (A**2) : 0.28800                                              
REMARK   3    B12 (A**2) : -1.10000                                             
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) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.34                            
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) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.180                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.840                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.660 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.660 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.410 ; 2.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.170 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Z73 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-AUG-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000027603.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL38B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46274                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GZM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3M AMMONIUM SULFATE, 30MM MES, 30MM      
REMARK 280  EDTA, 10MM BETA-MERCAPTOETHANOL, PH6.4, VAPOR DIFFUSION, SITTING    
REMARK 280  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      105.82667            
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       52.91333            
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      105.82667            
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       52.91333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.2 KCAL/MOL                        
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 350   BIOMT1   2 -1.000000  0.000000  0.000000       61.27500            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      106.13141            
REMARK 350   BIOMT3   2  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: 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    LYS A 100      145.85   -171.16                                   
REMARK 500    PHE A 209      -70.88    -98.74                                   
REMARK 500    MET A 225       42.09    -79.55                                   
REMARK 500    SER A 226       -2.42   -159.42                                   
REMARK 500    LEU A 241       22.23     47.34                                   
REMARK 500    ALA A 243     -167.44    -60.25                                   
REMARK 500    PRO A 288       93.11    -66.54                                   
REMARK 500    VAL A 292       74.25    -67.71                                   
REMARK 500    ALA A 308        4.47    -67.45                                   
REMARK 500    THR A 335      -71.06    -51.73                                   
REMARK 500    GLN A 338      131.75    -37.91                                   
REMARK 500    ALA A 356       63.54     63.19                                   
REMARK 500    LYS B 100      135.11   -170.95                                   
REMARK 500    SER B 144      133.86    -38.82                                   
REMARK 500    ILE B 223      -74.36    -62.21                                   
REMARK 500    SER B 226      -14.95   -163.66                                   
REMARK 500    ALA B 236        6.85    -66.98                                   
REMARK 500    ALA B 243      -84.47    -96.65                                   
REMARK 500    VAL B 292       84.87    -69.28                                   
REMARK 500    SER B 318      -27.64   -149.10                                   
REMARK 500    THR B 329      -49.79   -132.51                                   
REMARK 500    THR B 352      101.57    -54.95                                   
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     PLM B 1001                                                       
REMARK 610     PC1 B 1004                                                       
DBREF  2Z73 A    1   448  UNP    P31356   OPSD_TODPA       1    448             
DBREF  2Z73 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    BOG  A1005      20                                                       
HET    RET  A1000      20                                                       
HET    PLM  A1001      17                                                       
HET    PLM  A1002      17                                                       
HET    TWT  A1003      22                                                       
HET    BOG  B1005      20                                                       
HET    SO4  B1006       5                                                       
HET    RET  B1000      20                                                       
HET    PLM  B1001      17                                                       
HET    PLM  B1002      17                                                       
HET    TWT  B1003      22                                                       
HET    PC1  B1004      39                                                       
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE                                     
HETNAM     RET RETINAL                                                          
HETNAM     PLM PALMITIC ACID                                                    
HETNAM     TWT DOCOSANE                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE                           
HETSYN     PC1 3-SN-PHOSPHATIDYLCHOLINE                                         
FORMUL   3  BOG    2(C14 H28 O6)                                                
FORMUL   4  RET    2(C20 H28 O)                                                 
FORMUL   5  PLM    4(C16 H32 O2)                                                
FORMUL   7  TWT    2(C22 H46)                                                   
FORMUL   9  SO4    O4 S 2-                                                      
FORMUL  14  PC1    C44 H88 N O8 P                                               
FORMUL  15  HOH   *57(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  ILE A  168  1                                  21    
HELIX    7   7 GLY A  169  GLY A  173  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 PRO A  288  VAL A  292  5                                   5    
HELIX   13  13 THR A  293  SER A  307  1                                  15    
HELIX   14  14 HIS A  310  HIS A  319  1                                  10    
HELIX   15  15 HIS A  319  PHE A  330  1                                  12    
HELIX   16  16 PRO A  331  THR A  335  5                                   5    
HELIX   17  17 ASP A  340  GLU A  343  5                                   4    
HELIX   18  18 THR A  344  THR A  352  1                                   9    
HELIX   19  19 HIS B   20  GLU B   25  1                                   6    
HELIX   20  20 PRO B   30  THR B   62  1                                  33    
HELIX   21  21 LYS B   63  GLN B   66  5                                   4    
HELIX   22  22 THR B   67  PRO B   68  5                                   2    
HELIX   23  23 ALA B   69  GLY B   88  1                                  20    
HELIX   24  24 PRO B   90  LEU B   98  1                                   9    
HELIX   25  25 PHE B  103  ILE B  137  1                                  35    
HELIX   26  26 SER B  148  GLY B  169  1                                  22    
HELIX   27  27 PRO B  170  GLY B  173  5                                   4    
HELIX   28  28 ASP B  194  PHE B  209  1                                  16    
HELIX   29  29 PHE B  209  MET B  225  1                                  17    
HELIX   30  30 SER B  226  LYS B  239  1                                  14    
HELIX   31  31 LYS B  244  GLY B  287  1                                  44    
HELIX   32  32 PRO B  288  VAL B  292  5                                   5    
HELIX   33  33 THR B  293  SER B  307  1                                  15    
HELIX   34  34 ILE B  309  VAL B  317  1                                   9    
HELIX   35  35 HIS B  319  GLN B  328  1                                  10    
HELIX   36  36 PHE B  330  GLN B  338  5                                   9    
HELIX   37  37 ASP B  340  GLU B  343  5                                   4    
HELIX   38  38 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  2.02  
SSBOND   2 CYS B  108    CYS B  186                          1555   1555  2.03  
LINK         NZ  LYS A 305                 C15 RET A1000     1555   1555  1.32  
LINK         SG  CYS A 337                 C1  PLM A1002     1555   1555  1.80  
LINK         NZ  LYS B 305                 C15 RET B1000     1555   1555  1.31  
LINK         SG  CYS B 337                 C1  PLM B1002     1555   1555  1.80  
CISPEP   1 PHE A   89    PRO A   90          0         0.44                     
CISPEP   2 PHE B   89    PRO B   90          0         1.65                     
CRYST1  122.550  122.550  158.740  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      0.008160  0.004711  0.000000        0.00000                         
SCALE2      0.000000  0.009422  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006300        0.00000                         
ATOM      1  N   GLU A   9       5.011  32.057  32.041  1.00 71.96           N  
ATOM      2  CA  GLU A   9       6.355  32.375  31.472  1.00 72.88           C  
ATOM      3  C   GLU A   9       7.470  32.238  32.511  1.00 72.11           C  
ATOM      4  O   GLU A   9       8.579  31.821  32.181  1.00 72.64           O  
ATOM      5  CB  GLU A   9       6.367  33.796  30.917  1.00 75.96           C  
ATOM      6  CG  GLU A   9       7.376  34.002  29.799  1.00 81.64           C  
ATOM      7  CD  GLU A   9       6.972  33.291  28.518  1.00 82.41           C  
ATOM      8  OE1 GLU A   9       5.913  33.637  27.953  1.00 82.62           O  
ATOM      9  OE2 GLU A   9       7.711  32.386  28.078  1.00 86.69           O  
ATOM     10  N   THR A  10       7.168  32.607  33.758  1.00 70.09           N  
ATOM     11  CA  THR A  10       8.123  32.520  34.863  1.00 63.01           C  
ATOM     12  C   THR A  10       7.415  31.978  36.105  1.00 61.08           C  
ATOM     13  O   THR A  10       6.182  31.921  36.148  1.00 58.92           O  
ATOM     14  CB  THR A  10       8.754  33.904  35.187  1.00 62.93           C  
ATOM     15  OG1 THR A  10       7.767  34.773  35.751  1.00 60.66           O  
ATOM     16  CG2 THR A  10       9.303  34.546  33.919  1.00 61.41           C  
ATOM     17  N   TRP A  11       8.201  31.577  37.104  1.00 58.68           N  
ATOM     18  CA  TRP A  11       7.681  31.025  38.358  1.00 55.01           C  
ATOM     19  C   TRP A  11       7.704  32.045  39.484  1.00 55.47           C  
ATOM     20  O   TRP A  11       7.123  31.820  40.540  1.00 58.96           O  
ATOM     21  CB  TRP A  11       8.520  29.833  38.814  1.00 52.23           C  
ATOM     22  CG  TRP A  11       9.939  30.209  39.163  1.00 51.18           C  
ATOM     23  CD1 TRP A  11      11.020  30.211  38.326  1.00 52.20           C  
ATOM     24  CD2 TRP A  11      10.409  30.733  40.414  1.00 51.63           C  
ATOM     25  NE1 TRP A  11      12.131  30.709  38.972  1.00 48.94           N  
ATOM     26  CE2 TRP A  11      11.782  31.036  40.254  1.00 49.78           C  
ATOM     27  CE3 TRP A  11       9.804  30.981  41.655  1.00 50.50           C  
ATOM     28  CZ2 TRP A  11      12.556  31.574  41.286  1.00 49.20           C  
ATOM     29  CZ3 TRP A  11      10.575  31.516  42.682  1.00 50.55           C  
ATOM     30  CH2 TRP A  11      11.940  31.806  42.487  1.00 51.45           C  
ATOM     31  N   TRP A  12       8.389  33.158  39.264  1.00 54.25           N  
ATOM     32  CA  TRP A  12       8.523  34.178  40.285  1.00 53.19           C  
ATOM     33  C   TRP A  12       7.668  35.421  40.064  1.00 51.38           C  
ATOM     34  O   TRP A  12       7.538  36.247  40.967  1.00 51.29           O  
ATOM     35  CB  TRP A  12       9.994  34.606  40.374  1.00 55.43           C  
ATOM     36  CG  TRP A  12      10.540  35.014  39.030  1.00 56.65           C  
ATOM     37  CD1 TRP A  12      11.173  34.208  38.124  1.00 58.99           C  
ATOM     38  CD2 TRP A  12      10.367  36.282  38.384  1.00 57.75           C  
ATOM     39  NE1 TRP A  12      11.396  34.892  36.948  1.00 58.11           N  
ATOM     40  CE2 TRP A  12      10.910  36.167  37.080  1.00 58.25           C  
ATOM     41  CE3 TRP A  12       9.799  37.502  38.775  1.00 57.01           C  
ATOM     42  CZ2 TRP A  12      10.900  37.226  36.167  1.00 58.46           C  
ATOM     43  CZ3 TRP A  12       9.786  38.558  37.861  1.00 59.49           C  
ATOM     44  CH2 TRP A  12      10.334  38.410  36.572  1.00 59.05           C  
ATOM     45  N   TYR A  13       7.087  35.563  38.878  1.00 49.82           N  
ATOM     46  CA  TYR A  13       6.306  36.758  38.574  1.00 51.13           C  
ATOM     47  C   TYR A  13       5.193  37.127  39.522  1.00 50.79           C  
ATOM     48  O   TYR A  13       4.280  36.343  39.769  1.00 50.90           O  
ATOM     49  CB  TYR A  13       5.704  36.700  37.176  1.00 52.55           C  
ATOM     50  CG  TYR A  13       4.989  37.986  36.814  1.00 55.98           C  
ATOM     51  CD1 TYR A  13       3.604  38.025  36.684  1.00 59.61           C  
ATOM     52  CD2 TYR A  13       5.701  39.165  36.615  1.00 56.94           C  
ATOM     53  CE1 TYR A  13       2.943  39.210  36.362  1.00 61.44           C  
ATOM     54  CE2 TYR A  13       5.060  40.351  36.295  1.00 59.06           C  
ATOM     55  CZ  TYR A  13       3.677  40.365  36.170  1.00 62.75           C  
ATOM     56  OH  TYR A  13       3.019  41.535  35.849  1.00 64.03           O  
ATOM     57  N   ASN A  14       5.266  38.348  40.034  1.00 48.69           N  
ATOM     58  CA  ASN A  14       4.243  38.843  40.923  1.00 47.87           C  
ATOM     59  C   ASN A  14       3.583  40.057  40.277  1.00 48.35           C  
ATOM     60  O   ASN A  14       4.233  41.054  39.980  1.00 46.58           O  
ATOM     61  CB  ASN A  14       4.838  39.229  42.275  1.00 45.43           C  
ATOM     62  CG  ASN A  14       3.777  39.426  43.326  1.00 44.89           C  
ATOM     63  OD1 ASN A  14       2.826  40.189  43.133  1.00 42.42           O  
ATOM     64  ND2 ASN A  14       3.923  38.734  44.443  1.00 43.22           N  
ATOM     65  N   PRO A  15       2.273  39.981  40.046  1.00 50.04           N  
ATOM     66  CA  PRO A  15       1.560  41.096  39.428  1.00 48.75           C  
ATOM     67  C   PRO A  15       1.474  42.349  40.286  1.00 48.31           C  
ATOM     68  O   PRO A  15       1.180  43.427  39.774  1.00 48.29           O  
ATOM     69  CB  PRO A  15       0.186  40.496  39.142  1.00 50.53           C  
ATOM     70  CG  PRO A  15       0.008  39.539  40.280  1.00 50.77           C  
ATOM     71  CD  PRO A  15       1.357  38.860  40.314  1.00 50.75           C  
ATOM     72  N   SER A  16       1.746  42.214  41.583  1.00 49.09           N  
ATOM     73  CA  SER A  16       1.661  43.340  42.521  1.00 47.28           C  
ATOM     74  C   SER A  16       2.999  43.978  42.865  1.00 49.04           C  
ATOM     75  O   SER A  16       3.078  45.185  43.098  1.00 48.66           O  
ATOM     76  CB  SER A  16       1.028  42.887  43.838  1.00 48.21           C  
ATOM     77  OG  SER A  16      -0.205  42.220  43.644  1.00 51.81           O  
ATOM     78  N   ILE A  17       4.045  43.158  42.903  1.00 50.93           N  
ATOM     79  CA  ILE A  17       5.371  43.606  43.294  1.00 49.88           C  
ATOM     80  C   ILE A  17       6.420  43.230  42.250  1.00 52.39           C  
ATOM     81  O   ILE A  17       6.429  42.106  41.753  1.00 54.40           O  
ATOM     82  CB  ILE A  17       5.719  42.955  44.657  1.00 51.05           C  
ATOM     83  CG1 ILE A  17       4.603  43.282  45.662  1.00 46.38           C  
ATOM     84  CG2 ILE A  17       7.106  43.410  45.145  1.00 50.93           C  
ATOM     85  CD1 ILE A  17       4.598  42.438  46.907  1.00 42.68           C  
ATOM     86  N   VAL A  18       7.301  44.170  41.913  1.00 49.62           N  
ATOM     87  CA  VAL A  18       8.338  43.895  40.926  1.00 47.50           C  
ATOM     88  C   VAL A  18       9.512  43.232  41.613  1.00 44.80           C  
ATOM     89  O   VAL A  18      10.237  43.885  42.345  1.00 42.14           O  
ATOM     90  CB  VAL A  18       8.862  45.186  40.241  1.00 50.56           C  
ATOM     91  CG1 VAL A  18      10.002  44.845  39.284  1.00 46.63           C  
ATOM     92  CG2 VAL A  18       7.734  45.881  39.487  1.00 48.77           C  
ATOM     93  N   VAL A  19       9.691  41.938  41.368  1.00 44.08           N  
ATOM     94  CA  VAL A  19      10.789  41.170  41.942  1.00 43.69           C  
ATOM     95  C   VAL A  19      12.142  41.593  41.379  1.00 43.87           C  
ATOM     96  O   VAL A  19      12.318  41.657  40.170  1.00 48.86           O  
ATOM     97  CB  VAL A  19      10.614  39.682  41.643  1.00 44.56           C  
ATOM     98  CG1 VAL A  19      11.884  38.919  42.010  1.00 41.99           C  
ATOM     99  CG2 VAL A  19       9.399  39.145  42.391  1.00 43.85           C  
ATOM    100  N   HIS A  20      13.100  41.877  42.249  1.00 45.30           N  
ATOM    101  CA  HIS A  20      14.424  42.278  41.801  1.00 45.86           C  
ATOM    102  C   HIS A  20      15.000  41.181  40.935  1.00 48.52           C  
ATOM    103  O   HIS A  20      14.874  40.000  41.259  1.00 49.87           O  
ATOM    104  CB  HIS A  20      15.359  42.508  42.980  1.00 45.38           C  
ATOM    105  CG  HIS A  20      16.666  43.121  42.596  1.00 48.15           C  
ATOM    106  ND1 HIS A  20      17.622  42.440  41.877  1.00 47.25           N  
ATOM    107  CD2 HIS A  20      17.164  44.363  42.807  1.00 47.41           C  
ATOM    108  CE1 HIS A  20      18.653  43.237  41.660  1.00 48.50           C  
ATOM    109  NE2 HIS A  20      18.401  44.409  42.214  1.00 47.37           N  
ATOM    110  N   PRO A  21      15.645  41.556  39.817  1.00 49.22           N  
ATOM    111  CA  PRO A  21      16.259  40.626  38.868  1.00 48.14           C  
ATOM    112  C   PRO A  21      17.076  39.538  39.553  1.00 49.44           C  
ATOM    113  O   PRO A  21      17.087  38.386  39.122  1.00 51.32           O  
ATOM    114  CB  PRO A  21      17.120  41.542  38.016  1.00 46.40           C  
ATOM    115  CG  PRO A  21      16.317  42.788  37.977  1.00 45.90           C  
ATOM    116  CD  PRO A  21      15.900  42.950  39.411  1.00 48.05           C  
ATOM    117  N   HIS A  22      17.758  39.911  40.628  1.00 48.63           N  
ATOM    118  CA  HIS A  22      18.583  38.963  41.351  1.00 46.28           C  
ATOM    119  C   HIS A  22      17.862  37.702  41.789  1.00 46.06           C  
ATOM    120  O   HIS A  22      18.412  36.607  41.684  1.00 49.75           O  
ATOM    121  CB  HIS A  22      19.209  39.604  42.578  1.00 44.45           C  
ATOM    122  CG  HIS A  22      19.889  38.614  43.462  1.00 49.31           C  
ATOM    123  ND1 HIS A  22      20.847  37.743  42.992  1.00 49.65           N  
ATOM    124  CD2 HIS A  22      19.715  38.312  44.770  1.00 52.82           C  
ATOM    125  CE1 HIS A  22      21.235  36.947  43.971  1.00 51.11           C  
ATOM    126  NE2 HIS A  22      20.563  37.271  45.061  1.00 55.27           N  
ATOM    127  N   TRP A  23      16.641  37.841  42.288  1.00 45.13           N  
ATOM    128  CA  TRP A  23      15.892  36.669  42.745  1.00 45.22           C  
ATOM    129  C   TRP A  23      15.264  35.919  41.578  1.00 44.52           C  
ATOM    130  O   TRP A  23      14.820  34.785  41.714  1.00 43.05           O  
ATOM    131  CB  TRP A  23      14.790  37.086  43.733  1.00 44.59           C  
ATOM    132  CG  TRP A  23      15.283  37.832  44.947  1.00 45.31           C  
ATOM    133  CD1 TRP A  23      14.999  39.122  45.280  1.00 44.07           C  
ATOM    134  CD2 TRP A  23      16.144  37.336  45.981  1.00 44.37           C  
ATOM    135  NE1 TRP A  23      15.626  39.462  46.451  1.00 44.87           N  
ATOM    136  CE2 TRP A  23      16.336  38.383  46.902  1.00 44.86           C  
ATOM    137  CE3 TRP A  23      16.772  36.109  46.215  1.00 47.80           C  
ATOM    138  CZ2 TRP A  23      17.131  38.244  48.043  1.00 45.45           C  
ATOM    139  CZ3 TRP A  23      17.567  35.966  47.349  1.00 48.72           C  
ATOM    140  CH2 TRP A  23      17.739  37.031  48.251  1.00 49.46           C  
ATOM    141  N   ARG A  24      15.251  36.559  40.419  1.00 46.30           N  
ATOM    142  CA  ARG A  24      14.649  35.989  39.223  1.00 46.17           C  
ATOM    143  C   ARG A  24      15.497  34.984  38.472  1.00 47.68           C  
ATOM    144  O   ARG A  24      14.975  34.197  37.692  1.00 48.87           O  
ATOM    145  CB  ARG A  24      14.251  37.133  38.294  1.00 46.92           C  
ATOM    146  CG  ARG A  24      13.193  38.018  38.914  1.00 49.08           C  
ATOM    147  CD  ARG A  24      13.304  39.466  38.518  1.00 47.53           C  
ATOM    148  NE  ARG A  24      13.091  39.699  37.095  1.00 46.77           N  
ATOM    149  CZ  ARG A  24      12.685  40.863  36.588  1.00 48.36           C  
ATOM    150  NH1 ARG A  24      12.439  41.900  37.387  1.00 37.97           N  
ATOM    151  NH2 ARG A  24      12.545  40.998  35.272  1.00 48.58           N  
ATOM    152  N   GLU A  25      16.801  34.993  38.697  1.00 49.01           N  
ATOM    153  CA  GLU A  25      17.658  34.072  37.976  1.00 50.09           C  
ATOM    154  C   GLU A  25      17.701  32.671  38.577  1.00 49.48           C  
ATOM    155  O   GLU A  25      18.243  31.746  37.976  1.00 53.39           O  
ATOM    156  CB  GLU A  25      19.075  34.641  37.895  1.00 49.66           C  
ATOM    157  CG  GLU A  25      19.888  34.421  39.137  1.00 47.88           C  
ATOM    158  CD  GLU A  25      21.164  35.211  39.121  1.00 49.34           C  
ATOM    159  OE1 GLU A  25      22.157  34.737  39.712  1.00 53.18           O  
ATOM    160  OE2 GLU A  25      21.176  36.308  38.528  1.00 48.27           O  
ATOM    161  N   PHE A  26      17.116  32.497  39.750  1.00 48.05           N  
ATOM    162  CA  PHE A  26      17.150  31.196  40.394  1.00 48.02           C  
ATOM    163  C   PHE A  26      15.994  30.296  40.032  1.00 49.02           C  
ATOM    164  O   PHE A  26      14.954  30.757  39.570  1.00 48.05           O  
ATOM    165  CB  PHE A  26      17.205  31.367  41.911  1.00 44.32           C  
ATOM    166  CG  PHE A  26      18.370  32.187  42.372  1.00 46.38           C  
ATOM    167  CD1 PHE A  26      19.648  31.636  42.450  1.00 45.15           C  
ATOM    168  CD2 PHE A  26      18.201  33.528  42.701  1.00 44.88           C  
ATOM    169  CE1 PHE A  26      20.734  32.408  42.850  1.00 42.37           C  
ATOM    170  CE2 PHE A  26      19.288  34.303  43.101  1.00 46.98           C  
ATOM    171  CZ  PHE A  26      20.557  33.739  43.175  1.00 41.92           C  
ATOM    172  N   ASP A  27      16.201  28.996  40.223  1.00 52.11           N  
ATOM    173  CA  ASP A  27      15.171  28.014  39.954  1.00 52.71           C  
ATOM    174  C   ASP A  27      14.266  28.058  41.161  1.00 53.48           C  
ATOM    175  O   ASP A  27      14.673  28.497  42.237  1.00 54.76           O  
ATOM    176  CB  ASP A  27      15.752  26.605  39.825  1.00 53.37           C  
ATOM    177  CG  ASP A  27      16.522  26.397  38.537  1.00 56.26           C  
ATOM    178  OD1 ASP A  27      16.155  26.993  37.501  1.00 58.38           O  
ATOM    179  OD2 ASP A  27      17.488  25.614  38.556  1.00 60.13           O  
ATOM    180  N   GLN A  28      13.037  27.597  40.996  1.00 53.99           N  
ATOM    181  CA  GLN A  28      12.103  27.611  42.100  1.00 51.84           C  
ATOM    182  C   GLN A  28      12.337  26.444  43.036  1.00 51.98           C  
ATOM    183  O   GLN A  28      12.336  25.288  42.611  1.00 52.63           O  
ATOM    184  CB  GLN A  28      10.678  27.576  41.576  1.00 50.05           C  
ATOM    185  CG  GLN A  28       9.653  27.579  42.670  1.00 53.89           C  
ATOM    186  CD  GLN A  28       8.262  27.719  42.125  1.00 55.91           C  
ATOM    187  OE1 GLN A  28       7.907  27.075  41.141  1.00 50.90           O  
ATOM    188  NE2 GLN A  28       7.458  28.560  42.764  1.00 55.99           N  
ATOM    189  N   VAL A  29      12.536  26.754  44.315  1.00 51.08           N  
ATOM    190  CA  VAL A  29      12.757  25.740  45.333  1.00 50.64           C  
ATOM    191  C   VAL A  29      11.587  24.767  45.316  1.00 53.84           C  
ATOM    192  O   VAL A  29      10.497  25.105  44.877  1.00 57.85           O  
ATOM    193  CB  VAL A  29      12.884  26.379  46.732  1.00 50.94           C  
ATOM    194  CG1 VAL A  29      14.021  27.396  46.727  1.00 48.20           C  
ATOM    195  CG2 VAL A  29      11.559  27.039  47.142  1.00 49.25           C  
ATOM    196  N   PRO A  30      11.802  23.538  45.797  1.00 56.05           N  
ATOM    197  CA  PRO A  30      10.776  22.493  45.838  1.00 56.28           C  
ATOM    198  C   PRO A  30       9.554  22.834  46.696  1.00 56.91           C  
ATOM    199  O   PRO A  30       9.640  23.628  47.632  1.00 57.81           O  
ATOM    200  CB  PRO A  30      11.536  21.289  46.392  1.00 57.53           C  
ATOM    201  CG  PRO A  30      12.961  21.567  46.007  1.00 56.25           C  
ATOM    202  CD  PRO A  30      13.085  23.025  46.303  1.00 55.64           C  
ATOM    203  N   ASP A  31       8.423  22.208  46.383  1.00 55.40           N  
ATOM    204  CA  ASP A  31       7.187  22.430  47.128  1.00 55.74           C  
ATOM    205  C   ASP A  31       7.395  22.216  48.626  1.00 57.41           C  
ATOM    206  O   ASP A  31       6.996  23.042  49.449  1.00 59.64           O  
ATOM    207  CB  ASP A  31       6.099  21.474  46.651  1.00 55.07           C  
ATOM    208  CG  ASP A  31       5.675  21.731  45.223  1.00 56.41           C  
ATOM    209  OD1 ASP A  31       6.237  22.638  44.579  1.00 60.04           O  
ATOM    210  OD2 ASP A  31       4.772  21.016  44.741  1.00 57.44           O  
ATOM    211  N   ALA A  32       8.016  21.095  48.972  1.00 56.51           N  
ATOM    212  CA  ALA A  32       8.256  20.755  50.360  1.00 53.79           C  
ATOM    213  C   ALA A  32       8.937  21.879  51.114  1.00 53.80           C  
ATOM    214  O   ALA A  32       8.735  22.031  52.320  1.00 54.45           O  
ATOM    215  CB  ALA A  32       9.093  19.492  50.443  1.00 53.96           C  
ATOM    216  N   VAL A  33       9.742  22.670  50.413  1.00 52.02           N  
ATOM    217  CA  VAL A  33      10.450  23.763  51.066  1.00 51.95           C  
ATOM    218  C   VAL A  33       9.511  24.917  51.388  1.00 52.09           C  
ATOM    219  O   VAL A  33       9.633  25.562  52.434  1.00 52.83           O  
ATOM    220  CB  VAL A  33      11.596  24.300  50.190  1.00 51.59           C  
ATOM    221  CG1 VAL A  33      12.283  25.464  50.895  1.00 51.49           C  
ATOM    222  CG2 VAL A  33      12.592  23.191  49.899  1.00 49.27           C  
ATOM    223  N   TYR A  34       8.587  25.188  50.478  1.00 51.02           N  
ATOM    224  CA  TYR A  34       7.629  26.257  50.679  1.00 51.57           C  
ATOM    225  C   TYR A  34       6.720  25.882  51.830  1.00 53.02           C  
ATOM    226  O   TYR A  34       6.445  26.702  52.706  1.00 50.45           O  
ATOM    227  CB  TYR A  34       6.774  26.464  49.432  1.00 50.91           C  
ATOM    228  CG  TYR A  34       7.439  27.235  48.325  1.00 52.70           C  
ATOM    229  CD1 TYR A  34       7.845  26.596  47.151  1.00 53.29           C  
ATOM    230  CD2 TYR A  34       7.602  28.622  48.422  1.00 51.52           C  
ATOM    231  CE1 TYR A  34       8.390  27.325  46.089  1.00 55.95           C  
ATOM    232  CE2 TYR A  34       8.142  29.358  47.374  1.00 54.23           C  
ATOM    233  CZ  TYR A  34       8.531  28.709  46.206  1.00 56.13           C  
ATOM    234  OH  TYR A  34       9.027  29.442  45.156  1.00 57.46           O  
ATOM    235  N   TYR A  35       6.261  24.632  51.810  1.00 53.54           N  
ATOM    236  CA  TYR A  35       5.367  24.096  52.833  1.00 55.20           C  
ATOM    237  C   TYR A  35       6.004  24.091  54.220  1.00 52.95           C  
ATOM    238  O   TYR A  35       5.360  24.430  55.214  1.00 54.96           O  
ATOM    239  CB  TYR A  35       4.934  22.685  52.432  1.00 59.07           C  
ATOM    240  CG  TYR A  35       4.196  22.676  51.111  1.00 68.16           C  
ATOM    241  CD1 TYR A  35       4.109  21.519  50.333  1.00 70.34           C  
ATOM    242  CD2 TYR A  35       3.606  23.843  50.625  1.00 70.83           C  
ATOM    243  CE1 TYR A  35       3.455  21.535  49.098  1.00 73.44           C  
ATOM    244  CE2 TYR A  35       2.953  23.868  49.402  1.00 73.90           C  
ATOM    245  CZ  TYR A  35       2.881  22.717  48.640  1.00 74.88           C  
ATOM    246  OH  TYR A  35       2.249  22.772  47.417  1.00 76.74           O  
ATOM    247  N   SER A  36       7.271  23.714  54.285  1.00 49.42           N  
ATOM    248  CA  SER A  36       7.956  23.692  55.548  1.00 49.35           C  
ATOM    249  C   SER A  36       8.110  25.123  56.037  1.00 48.48           C  
ATOM    250  O   SER A  36       7.931  25.410  57.223  1.00 46.50           O  
ATOM    251  CB  SER A  36       9.325  23.034  55.392  1.00 48.62           C  
ATOM    252  OG  SER A  36       9.161  21.701  54.954  1.00 51.68           O  
ATOM    253  N   LEU A  37       8.432  26.024  55.119  1.00 47.52           N  
ATOM    254  CA  LEU A  37       8.608  27.424  55.485  1.00 49.22           C  
ATOM    255  C   LEU A  37       7.328  27.995  56.102  1.00 49.56           C  
ATOM    256  O   LEU A  37       7.370  28.644  57.144  1.00 48.35           O  
ATOM    257  CB  LEU A  37       9.022  28.249  54.256  1.00 48.10           C  
ATOM    258  CG  LEU A  37      10.493  28.122  53.834  1.00 45.59           C  
ATOM    259  CD1 LEU A  37      10.769  28.988  52.612  1.00 46.27           C  
ATOM    260  CD2 LEU A  37      11.386  28.557  54.991  1.00 43.56           C  
ATOM    261  N   GLY A  38       6.195  27.732  55.455  1.00 50.84           N  
ATOM    262  CA  GLY A  38       4.921  28.214  55.952  1.00 50.76           C  
ATOM    263  C   GLY A  38       4.584  27.609  57.302  1.00 51.37           C  
ATOM    264  O   GLY A  38       4.160  28.308  58.218  1.00 53.43           O  
ATOM    265  N   ILE A  39       4.770  26.301  57.430  1.00 49.85           N  
ATOM    266  CA  ILE A  39       4.489  25.632  58.686  1.00 46.84           C  
ATOM    267  C   ILE A  39       5.393  26.213  59.752  1.00 45.31           C  
ATOM    268  O   ILE A  39       4.968  26.487  60.868  1.00 46.64           O  
ATOM    269  CB  ILE A  39       4.741  24.122  58.574  1.00 46.71           C  
ATOM    270  CG1 ILE A  39       3.677  23.501  57.663  1.00 47.48           C  
ATOM    271  CG2 ILE A  39       4.771  23.487  59.965  1.00 41.12           C  
ATOM    272  CD1 ILE A  39       3.918  22.049  57.316  1.00 50.81           C  
ATOM    273  N   PHE A  40       6.650  26.411  59.393  1.00 46.32           N  
ATOM    274  CA  PHE A  40       7.621  26.944  60.333  1.00 46.03           C  
ATOM    275  C   PHE A  40       7.200  28.290  60.917  1.00 45.64           C  
ATOM    276  O   PHE A  40       6.999  28.418  62.135  1.00 45.23           O  
ATOM    277  CB  PHE A  40       8.986  27.104  59.663  1.00 43.58           C  
ATOM    278  CG  PHE A  40      10.041  27.609  60.589  1.00 38.87           C  
ATOM    279  CD1 PHE A  40      10.693  26.736  61.443  1.00 35.31           C  
ATOM    280  CD2 PHE A  40      10.336  28.965  60.649  1.00 38.33           C  
ATOM    281  CE1 PHE A  40      11.626  27.207  62.351  1.00 38.79           C  
ATOM    282  CE2 PHE A  40      11.266  29.450  61.551  1.00 38.45           C  
ATOM    283  CZ  PHE A  40      11.913  28.570  62.406  1.00 40.52           C  
ATOM    284  N   ILE A  41       7.075  29.291  60.045  1.00 43.47           N  
ATOM    285  CA  ILE A  41       6.707  30.631  60.484  1.00 42.58           C  
ATOM    286  C   ILE A  41       5.333  30.671  61.162  1.00 41.19           C  
ATOM    287  O   ILE A  41       5.095  31.505  62.033  1.00 38.11           O  
ATOM    288  CB  ILE A  41       6.761  31.629  59.306  1.00 42.16           C  
ATOM    289  CG1 ILE A  41       6.935  33.047  59.845  1.00 44.56           C  
ATOM    290  CG2 ILE A  41       5.512  31.524  58.465  1.00 44.99           C  
ATOM    291  CD1 ILE A  41       8.176  33.219  60.754  1.00 40.09           C  
ATOM    292  N   GLY A  42       4.447  29.757  60.761  1.00 40.24           N  
ATOM    293  CA  GLY A  42       3.128  29.679  61.355  1.00 39.35           C  
ATOM    294  C   GLY A  42       3.244  29.280  62.814  1.00 40.47           C  
ATOM    295  O   GLY A  42       2.510  29.774  63.677  1.00 43.05           O  
ATOM    296  N   ILE A  43       4.183  28.389  63.104  1.00 41.53           N  
ATOM    297  CA  ILE A  43       4.398  27.938  64.467  1.00 42.94           C  
ATOM    298  C   ILE A  43       5.105  29.029  65.283  1.00 42.64           C  
ATOM    299  O   ILE A  43       5.051  29.024  66.511  1.00 45.32           O  
ATOM    300  CB  ILE A  43       5.197  26.604  64.481  1.00 44.48           C  
ATOM    301  CG1 ILE A  43       4.327  25.502  63.872  1.00 46.36           C  
ATOM    302  CG2 ILE A  43       5.621  26.236  65.906  1.00 44.21           C  
ATOM    303  CD1 ILE A  43       4.876  24.079  64.028  1.00 46.74           C  
ATOM    304  N   CYS A  44       5.765  29.970  64.616  1.00 42.72           N  
ATOM    305  CA  CYS A  44       6.394  31.061  65.349  1.00 43.12           C  
ATOM    306  C   CYS A  44       5.260  32.012  65.700  1.00 40.31           C  
ATOM    307  O   CYS A  44       5.290  32.696  66.722  1.00 38.72           O  
ATOM    308  CB  CYS A  44       7.447  31.785  64.497  1.00 46.94           C  
ATOM    309  SG  CYS A  44       8.987  30.855  64.242  1.00 45.95           S  
ATOM    310  N   GLY A  45       4.246  32.042  64.844  1.00 39.02           N  
ATOM    311  CA  GLY A  45       3.087  32.877  65.099  1.00 40.03           C  
ATOM    312  C   GLY A  45       2.370  32.403  66.350  1.00 39.71           C  
ATOM    313  O   GLY A  45       2.069  33.185  67.250  1.00 39.18           O  
ATOM    314  N   ILE A  46       2.102  31.106  66.412  1.00 38.64           N  
ATOM    315  CA  ILE A  46       1.420  30.536  67.568  1.00 40.76           C  
ATOM    316  C   ILE A  46       2.228  30.728  68.859  1.00 42.46           C  
ATOM    317  O   ILE A  46       1.738  31.324  69.829  1.00 44.26           O  
ATOM    318  CB  ILE A  46       1.154  29.021  67.366  1.00 41.57           C  
ATOM    319  CG1 ILE A  46       0.153  28.812  66.232  1.00 40.50           C  
ATOM    320  CG2 ILE A  46       0.629  28.397  68.649  1.00 38.59           C  
ATOM    321  CD1 ILE A  46       0.057  27.364  65.785  1.00 41.85           C  
ATOM    322  N   ILE A  47       3.459  30.223  68.875  1.00 42.70           N  
ATOM    323  CA  ILE A  47       4.292  30.331  70.059  1.00 42.10           C  
ATOM    324  C   ILE A  47       4.544  31.781  70.408  1.00 42.72           C  
ATOM    325  O   ILE A  47       4.400  32.182  71.568  1.00 45.39           O  
ATOM    326  CB  ILE A  47       5.636  29.606  69.869  1.00 46.23           C  
ATOM    327  CG1 ILE A  47       5.388  28.098  69.715  1.00 49.00           C  
ATOM    328  CG2 ILE A  47       6.559  29.875  71.052  1.00 46.78           C  
ATOM    329  CD1 ILE A  47       6.648  27.263  69.559  1.00 49.16           C  
ATOM    330  N   GLY A  48       4.908  32.578  69.411  1.00 40.21           N  
ATOM    331  CA  GLY A  48       5.162  33.991  69.653  1.00 40.13           C  
ATOM    332  C   GLY A  48       3.979  34.739  70.251  1.00 41.49           C  
ATOM    333  O   GLY A  48       4.112  35.391  71.291  1.00 39.97           O  
ATOM    334  N   CYS A  49       2.819  34.661  69.600  1.00 42.35           N  
ATOM    335  CA  CYS A  49       1.630  35.350  70.111  1.00 39.96           C  
ATOM    336  C   CYS A  49       1.195  34.710  71.424  1.00 37.87           C  
ATOM    337  O   CYS A  49       0.812  35.399  72.364  1.00 37.74           O  
ATOM    338  CB  CYS A  49       0.483  35.286  69.093  1.00 38.71           C  
ATOM    339  SG  CYS A  49       0.822  36.102  67.518  1.00 38.84           S  
ATOM    340  N   GLY A  50       1.265  33.386  71.486  1.00 36.98           N  
ATOM    341  CA  GLY A  50       0.879  32.706  72.702  1.00 38.99           C  
ATOM    342  C   GLY A  50       1.748  33.139  73.866  1.00 40.60           C  
ATOM    343  O   GLY A  50       1.256  33.688  74.865  1.00 42.23           O  
ATOM    344  N   GLY A  51       3.052  32.910  73.734  1.00 38.73           N  
ATOM    345  CA  GLY A  51       3.972  33.276  74.792  1.00 37.82           C  
ATOM    346  C   GLY A  51       4.018  34.751  75.145  1.00 35.55           C  
ATOM    347  O   GLY A  51       4.057  35.116  76.315  1.00 35.77           O  
ATOM    348  N   ASN A  52       4.017  35.618  74.148  1.00 37.23           N  
ATOM    349  CA  ASN A  52       4.081  37.037  74.445  1.00 42.37           C  
ATOM    350  C   ASN A  52       2.792  37.543  75.056  1.00 43.25           C  
ATOM    351  O   ASN A  52       2.804  38.489  75.848  1.00 41.90           O  
ATOM    352  CB  ASN A  52       4.445  37.836  73.189  1.00 44.34           C  
ATOM    353  CG  ASN A  52       5.926  37.711  72.828  1.00 44.29           C  
ATOM    354  OD1 ASN A  52       6.812  38.042  73.623  1.00 44.07           O  
ATOM    355  ND2 ASN A  52       6.193  37.233  71.624  1.00 44.33           N  
ATOM    356  N   GLY A  53       1.676  36.914  74.694  1.00 43.31           N  
ATOM    357  CA  GLY A  53       0.402  37.328  75.259  1.00 41.53           C  
ATOM    358  C   GLY A  53       0.422  37.047  76.755  1.00 41.07           C  
ATOM    359  O   GLY A  53       0.017  37.872  77.566  1.00 40.44           O  
ATOM    360  N   ILE A  54       0.916  35.867  77.111  1.00 38.87           N  
ATOM    361  CA  ILE A  54       0.991  35.472  78.500  1.00 38.68           C  
ATOM    362  C   ILE A  54       1.815  36.440  79.338  1.00 41.13           C  
ATOM    363  O   ILE A  54       1.413  36.802  80.440  1.00 43.99           O  
ATOM    364  CB  ILE A  54       1.594  34.075  78.645  1.00 38.03           C  
ATOM    365  CG1 ILE A  54       0.732  33.066  77.890  1.00 37.78           C  
ATOM    366  CG2 ILE A  54       1.702  33.712  80.110  1.00 32.88           C  
ATOM    367  CD1 ILE A  54       1.173  31.633  78.066  1.00 39.57           C  
ATOM    368  N   VAL A  55       2.971  36.855  78.831  1.00 42.91           N  
ATOM    369  CA  VAL A  55       3.793  37.776  79.591  1.00 42.64           C  
ATOM    370  C   VAL A  55       3.043  39.088  79.750  1.00 40.88           C  
ATOM    371  O   VAL A  55       2.945  39.618  80.859  1.00 43.07           O  
ATOM    372  CB  VAL A  55       5.216  37.991  78.940  1.00 41.50           C  
ATOM    373  CG1 VAL A  55       5.133  37.880  77.442  1.00 47.06           C  
ATOM    374  CG2 VAL A  55       5.791  39.346  79.346  1.00 41.03           C  
ATOM    375  N   ILE A  56       2.476  39.598  78.667  1.00 41.22           N  
ATOM    376  CA  ILE A  56       1.715  40.837  78.762  1.00 46.67           C  
ATOM    377  C   ILE A  56       0.545  40.697  79.744  1.00 47.49           C  
ATOM    378  O   ILE A  56       0.309  41.582  80.568  1.00 46.94           O  
ATOM    379  CB  ILE A  56       1.138  41.265  77.407  1.00 47.49           C  
ATOM    380  CG1 ILE A  56       2.270  41.577  76.422  1.00 45.32           C  
ATOM    381  CG2 ILE A  56       0.226  42.480  77.603  1.00 46.96           C  
ATOM    382  CD1 ILE A  56       1.774  42.020  75.056  1.00 44.43           C  
ATOM    383  N   TYR A  57      -0.185  39.588  79.648  1.00 48.96           N  
ATOM    384  CA  TYR A  57      -1.325  39.345  80.528  1.00 48.79           C  
ATOM    385  C   TYR A  57      -0.860  39.275  81.971  1.00 49.73           C  
ATOM    386  O   TYR A  57      -1.288  40.075  82.799  1.00 50.07           O  
ATOM    387  CB  TYR A  57      -2.036  38.040  80.137  1.00 51.98           C  
ATOM    388  CG  TYR A  57      -3.207  37.658  81.028  1.00 54.48           C  
ATOM    389  CD1 TYR A  57      -3.120  36.569  81.894  1.00 54.18           C  
ATOM    390  CD2 TYR A  57      -4.397  38.387  81.006  1.00 53.11           C  
ATOM    391  CE1 TYR A  57      -4.179  36.216  82.709  1.00 53.82           C  
ATOM    392  CE2 TYR A  57      -5.460  38.044  81.823  1.00 52.96           C  
ATOM    393  CZ  TYR A  57      -5.345  36.957  82.671  1.00 54.62           C  
ATOM    394  OH  TYR A  57      -6.396  36.603  83.491  1.00 56.82           O  
ATOM    395  N   LEU A  58       0.030  38.328  82.262  1.00 49.26           N  
ATOM    396  CA  LEU A  58       0.557  38.152  83.613  1.00 48.99           C  
ATOM    397  C   LEU A  58       1.252  39.392  84.196  1.00 49.64           C  
ATOM    398  O   LEU A  58       1.001  39.759  85.344  1.00 47.80           O  
ATOM    399  CB  LEU A  58       1.515  36.956  83.648  1.00 47.34           C  
ATOM    400  CG  LEU A  58       0.980  35.652  84.252  1.00 48.75           C  
ATOM    401  CD1 LEU A  58      -0.501  35.487  83.963  1.00 49.48           C  
ATOM    402  CD2 LEU A  58       1.770  34.474  83.705  1.00 44.53           C  
ATOM    403  N   PHE A  59       2.112  40.045  83.417  1.00 50.96           N  
ATOM    404  CA  PHE A  59       2.807  41.218  83.940  1.00 52.35           C  
ATOM    405  C   PHE A  59       1.914  42.427  84.221  1.00 50.84           C  
ATOM    406  O   PHE A  59       2.143  43.143  85.192  1.00 47.74           O  
ATOM    407  CB  PHE A  59       3.979  41.618  83.028  1.00 52.70           C  
ATOM    408  CG  PHE A  59       5.290  40.954  83.393  1.00 52.02           C  
ATOM    409  CD1 PHE A  59       5.552  39.634  83.032  1.00 52.01           C  
ATOM    410  CD2 PHE A  59       6.255  41.649  84.116  1.00 52.69           C  
ATOM    411  CE1 PHE A  59       6.760  39.018  83.388  1.00 50.62           C  
ATOM    412  CE2 PHE A  59       7.461  41.043  84.476  1.00 50.37           C  
ATOM    413  CZ  PHE A  59       7.715  39.727  84.112  1.00 48.89           C  
ATOM    414  N   THR A  60       0.901  42.663  83.394  1.00 52.35           N  
ATOM    415  CA  THR A  60       0.017  43.797  83.651  1.00 54.81           C  
ATOM    416  C   THR A  60      -1.000  43.506  84.757  1.00 56.83           C  
ATOM    417  O   THR A  60      -1.550  44.432  85.344  1.00 59.00           O  
ATOM    418  CB  THR A  60      -0.793  44.221  82.401  1.00 51.68           C  
ATOM    419  OG1 THR A  60      -1.368  43.067  81.788  1.00 50.82           O  
ATOM    420  CG2 THR A  60       0.079  44.950  81.407  1.00 51.33           C  
ATOM    421  N   LYS A  61      -1.228  42.232  85.061  1.00 57.56           N  
ATOM    422  CA  LYS A  61      -2.220  41.890  86.062  1.00 59.00           C  
ATOM    423  C   LYS A  61      -1.750  41.328  87.402  1.00 59.77           C  
ATOM    424  O   LYS A  61      -2.554  41.188  88.326  1.00 61.10           O  
ATOM    425  CB  LYS A  61      -3.248  40.945  85.441  1.00 60.53           C  
ATOM    426  CG  LYS A  61      -4.023  41.597  84.300  1.00 64.56           C  
ATOM    427  CD  LYS A  61      -4.714  42.872  84.780  1.00 65.73           C  
ATOM    428  CE  LYS A  61      -5.302  43.660  83.623  1.00 68.26           C  
ATOM    429  NZ  LYS A  61      -5.953  44.925  84.079  1.00 68.79           N  
ATOM    430  N   THR A  62      -0.467  41.007  87.522  1.00 57.53           N  
ATOM    431  CA  THR A  62       0.033  40.479  88.779  1.00 55.70           C  
ATOM    432  C   THR A  62       0.581  41.619  89.624  1.00 57.84           C  
ATOM    433  O   THR A  62       1.242  42.517  89.099  1.00 59.75           O  
ATOM    434  CB  THR A  62       1.133  39.442  88.556  1.00 53.42           C  
ATOM    435  OG1 THR A  62       0.603  38.339  87.808  1.00 51.02           O  
ATOM    436  CG2 THR A  62       1.657  38.942  89.877  1.00 48.61           C  
ATOM    437  N   LYS A  63       0.303  41.585  90.928  1.00 58.07           N  
ATOM    438  CA  LYS A  63       0.745  42.632  91.846  1.00 57.49           C  
ATOM    439  C   LYS A  63       2.244  42.611  92.111  1.00 58.05           C  
ATOM    440  O   LYS A  63       2.877  43.663  92.229  1.00 58.11           O  
ATOM    441  CB  LYS A  63      -0.006  42.522  93.178  1.00 58.01           C  
ATOM    442  CG  LYS A  63       0.329  43.645  94.165  1.00 61.50           C  
ATOM    443  CD  LYS A  63      -0.444  43.539  95.478  1.00 62.29           C  
ATOM    444  CE  LYS A  63      -0.028  42.322  96.286  1.00 65.95           C  
ATOM    445  NZ  LYS A  63      -0.735  42.258  97.601  1.00 65.92           N  
ATOM    446  N   SER A  64       2.816  41.418  92.212  1.00 56.47           N  
ATOM    447  CA  SER A  64       4.240  41.291  92.474  1.00 56.26           C  
ATOM    448  C   SER A  64       5.087  41.752  91.297  1.00 58.64           C  
ATOM    449  O   SER A  64       6.285  41.996  91.449  1.00 61.33           O  
ATOM    450  CB  SER A  64       4.580  39.843  92.826  1.00 55.66           C  
ATOM    451  OG  SER A  64       4.135  38.950  91.825  1.00 59.02           O  
ATOM    452  N   LEU A  65       4.466  41.881  90.127  1.00 58.03           N  
ATOM    453  CA  LEU A  65       5.180  42.315  88.930  1.00 57.41           C  
ATOM    454  C   LEU A  65       4.792  43.740  88.510  1.00 59.78           C  
ATOM    455  O   LEU A  65       4.916  44.096  87.342  1.00 59.53           O  
ATOM    456  CB  LEU A  65       4.873  41.358  87.778  1.00 57.37           C  
ATOM    457  CG  LEU A  65       4.880  39.845  88.027  1.00 58.12           C  
ATOM    458  CD1 LEU A  65       4.607  39.107  86.715  1.00 53.63           C  
ATOM    459  CD2 LEU A  65       6.220  39.421  88.603  1.00 59.36           C  
ATOM    460  N   GLN A  66       4.354  44.561  89.460  1.00 63.77           N  
ATOM    461  CA  GLN A  66       3.914  45.926  89.161  1.00 69.21           C  
ATOM    462  C   GLN A  66       4.944  47.068  89.172  1.00 71.52           C  
ATOM    463  O   GLN A  66       4.559  48.246  89.151  1.00 73.67           O  
ATOM    464  CB  GLN A  66       2.768  46.302  90.102  1.00 72.50           C  
ATOM    465  CG  GLN A  66       1.489  46.689  89.395  1.00 74.92           C  
ATOM    466  CD  GLN A  66       0.900  45.538  88.616  1.00 76.01           C  
ATOM    467  OE1 GLN A  66       1.543  44.987  87.730  1.00 76.16           O  
ATOM    468  NE2 GLN A  66      -0.334  45.162  88.948  1.00 78.43           N  
ATOM    469  N   THR A  67       6.233  46.747  89.205  1.00 70.31           N  
ATOM    470  CA  THR A  67       7.256  47.792  89.212  1.00 68.74           C  
ATOM    471  C   THR A  67       7.408  48.452  87.840  1.00 65.36           C  
ATOM    472  O   THR A  67       7.148  47.827  86.816  1.00 65.11           O  
ATOM    473  CB  THR A  67       8.621  47.228  89.660  1.00 71.06           C  
ATOM    474  OG1 THR A  67       8.772  45.893  89.159  1.00 74.15           O  
ATOM    475  CG2 THR A  67       8.726  47.216  91.177  1.00 73.35           C  
ATOM    476  N   PRO A  68       7.833  49.729  87.803  1.00 63.43           N  
ATOM    477  CA  PRO A  68       8.019  50.474  86.552  1.00 61.65           C  
ATOM    478  C   PRO A  68       8.883  49.811  85.480  1.00 60.13           C  
ATOM    479  O   PRO A  68       8.497  49.768  84.315  1.00 59.08           O  
ATOM    480  CB  PRO A  68       8.598  51.802  87.031  1.00 60.93           C  
ATOM    481  CG  PRO A  68       7.905  52.002  88.330  1.00 60.26           C  
ATOM    482  CD  PRO A  68       8.025  50.623  88.960  1.00 62.79           C  
ATOM    483  N   ALA A  69      10.048  49.301  85.867  1.00 61.35           N  
ATOM    484  CA  ALA A  69      10.950  48.652  84.912  1.00 61.16           C  
ATOM    485  C   ALA A  69      10.263  47.547  84.110  1.00 59.63           C  
ATOM    486  O   ALA A  69      10.537  47.371  82.926  1.00 59.57           O  
ATOM    487  CB  ALA A  69      12.160  48.081  85.643  1.00 61.34           C  
ATOM    488  N   ASN A  70       9.375  46.804  84.764  1.00 59.26           N  
ATOM    489  CA  ASN A  70       8.645  45.717  84.119  1.00 55.93           C  
ATOM    490  C   ASN A  70       7.840  46.195  82.923  1.00 54.65           C  
ATOM    491  O   ASN A  70       7.403  45.393  82.100  1.00 51.97           O  
ATOM    492  CB  ASN A  70       7.725  45.038  85.126  1.00 55.14           C  
ATOM    493  CG  ASN A  70       8.449  44.041  85.979  1.00 54.89           C  
ATOM    494  OD1 ASN A  70       7.902  43.531  86.949  1.00 58.16           O  
ATOM    495  ND2 ASN A  70       9.684  43.740  85.615  1.00 56.50           N  
ATOM    496  N   MET A  71       7.630  47.505  82.844  1.00 53.71           N  
ATOM    497  CA  MET A  71       6.913  48.084  81.720  1.00 53.51           C  
ATOM    498  C   MET A  71       7.732  47.757  80.464  1.00 53.36           C  
ATOM    499  O   MET A  71       7.172  47.424  79.416  1.00 51.12           O  
ATOM    500  CB  MET A  71       6.778  49.602  81.901  1.00 55.16           C  
ATOM    501  CG  MET A  71       5.727  50.029  82.935  1.00 57.77           C  
ATOM    502  SD  MET A  71       5.734  51.815  83.328  1.00 59.41           S  
ATOM    503  CE  MET A  71       5.468  52.510  81.640  1.00 51.50           C  
ATOM    504  N   PHE A  72       9.061  47.839  80.588  1.00 52.43           N  
ATOM    505  CA  PHE A  72       9.952  47.537  79.473  1.00 49.82           C  
ATOM    506  C   PHE A  72       9.675  46.115  79.007  1.00 47.58           C  
ATOM    507  O   PHE A  72       9.597  45.857  77.809  1.00 44.68           O  
ATOM    508  CB  PHE A  72      11.430  47.646  79.871  1.00 52.28           C  
ATOM    509  CG  PHE A  72      11.860  49.022  80.309  1.00 51.88           C  
ATOM    510  CD1 PHE A  72      11.412  50.159  79.649  1.00 52.10           C  
ATOM    511  CD2 PHE A  72      12.726  49.179  81.389  1.00 52.26           C  
ATOM    512  CE1 PHE A  72      11.819  51.436  80.064  1.00 52.47           C  
ATOM    513  CE2 PHE A  72      13.135  50.445  81.808  1.00 50.70           C  
ATOM    514  CZ  PHE A  72      12.682  51.572  81.148  1.00 49.50           C  
ATOM    515  N   ILE A  73       9.537  45.195  79.962  1.00 48.00           N  
ATOM    516  CA  ILE A  73       9.263  43.794  79.646  1.00 51.34           C  
ATOM    517  C   ILE A  73       7.963  43.681  78.855  1.00 51.60           C  
ATOM    518  O   ILE A  73       7.875  42.944  77.872  1.00 50.28           O  
ATOM    519  CB  ILE A  73       9.135  42.923  80.929  1.00 54.82           C  
ATOM    520  CG1 ILE A  73      10.521  42.609  81.497  1.00 56.97           C  
ATOM    521  CG2 ILE A  73       8.413  41.614  80.615  1.00 55.71           C  
ATOM    522  CD1 ILE A  73      10.488  41.792  82.789  1.00 57.24           C  
ATOM    523  N   ILE A  74       6.955  44.423  79.293  1.00 49.33           N  
ATOM    524  CA  ILE A  74       5.678  44.400  78.618  1.00 47.96           C  
ATOM    525  C   ILE A  74       5.851  44.951  77.210  1.00 46.40           C  
ATOM    526  O   ILE A  74       5.405  44.345  76.233  1.00 46.65           O  
ATOM    527  CB  ILE A  74       4.620  45.214  79.418  1.00 49.04           C  
ATOM    528  CG1 ILE A  74       4.283  44.461  80.715  1.00 49.58           C  
ATOM    529  CG2 ILE A  74       3.347  45.417  78.592  1.00 46.66           C  
ATOM    530  CD1 ILE A  74       3.429  45.231  81.689  1.00 46.80           C  
ATOM    531  N   ASN A  75       6.515  46.098  77.111  1.00 45.66           N  
ATOM    532  CA  ASN A  75       6.752  46.738  75.823  1.00 44.23           C  
ATOM    533  C   ASN A  75       7.449  45.763  74.867  1.00 44.03           C  
ATOM    534  O   ASN A  75       7.110  45.693  73.680  1.00 40.89           O  
ATOM    535  CB  ASN A  75       7.604  48.000  76.005  1.00 43.83           C  
ATOM    536  CG  ASN A  75       7.819  48.742  74.700  1.00 47.79           C  
ATOM    537  OD1 ASN A  75       6.884  49.312  74.136  1.00 48.34           O  
ATOM    538  ND2 ASN A  75       9.048  48.730  74.207  1.00 52.84           N  
ATOM    539  N   LEU A  76       8.419  45.019  75.399  1.00 42.58           N  
ATOM    540  CA  LEU A  76       9.167  44.037  74.618  1.00 40.80           C  
ATOM    541  C   LEU A  76       8.215  42.939  74.123  1.00 41.84           C  
ATOM    542  O   LEU A  76       8.272  42.522  72.965  1.00 41.88           O  
ATOM    543  CB  LEU A  76      10.248  43.399  75.489  1.00 41.84           C  
ATOM    544  CG  LEU A  76      11.597  43.024  74.882  1.00 42.41           C  
ATOM    545  CD1 LEU A  76      12.294  42.043  75.812  1.00 40.93           C  
ATOM    546  CD2 LEU A  76      11.427  42.401  73.503  1.00 44.78           C  
ATOM    547  N   ALA A  77       7.342  42.470  75.011  1.00 41.96           N  
ATOM    548  CA  ALA A  77       6.395  41.425  74.661  1.00 41.12           C  
ATOM    549  C   ALA A  77       5.395  41.899  73.611  1.00 42.02           C  
ATOM    550  O   ALA A  77       4.990  41.119  72.751  1.00 43.48           O  
ATOM    551  CB  ALA A  77       5.666  40.944  75.898  1.00 39.81           C  
ATOM    552  N   PHE A  78       4.985  43.163  73.682  1.00 41.79           N  
ATOM    553  CA  PHE A  78       4.032  43.693  72.705  1.00 43.93           C  
ATOM    554  C   PHE A  78       4.748  43.695  71.358  1.00 45.62           C  
ATOM    555  O   PHE A  78       4.178  43.334  70.324  1.00 46.20           O  
ATOM    556  CB  PHE A  78       3.624  45.129  73.054  1.00 45.88           C  
ATOM    557  CG  PHE A  78       2.647  45.733  72.084  1.00 48.45           C  
ATOM    558  CD1 PHE A  78       1.294  45.785  72.379  1.00 48.71           C  
ATOM    559  CD2 PHE A  78       3.076  46.205  70.847  1.00 49.59           C  
ATOM    560  CE1 PHE A  78       0.382  46.291  71.461  1.00 49.30           C  
ATOM    561  CE2 PHE A  78       2.165  46.714  69.920  1.00 49.24           C  
ATOM    562  CZ  PHE A  78       0.821  46.755  70.227  1.00 48.09           C  
ATOM    563  N   SER A  79       6.006  44.112  71.399  1.00 44.01           N  
ATOM    564  CA  SER A  79       6.848  44.166  70.233  1.00 42.04           C  
ATOM    565  C   SER A  79       6.948  42.789  69.597  1.00 41.18           C  
ATOM    566  O   SER A  79       6.664  42.609  68.412  1.00 40.72           O  
ATOM    567  CB  SER A  79       8.245  44.645  70.635  1.00 43.76           C  
ATOM    568  OG  SER A  79       9.110  44.750  69.524  1.00 47.91           O  
ATOM    569  N   ASP A  80       7.349  41.807  70.389  1.00 43.10           N  
ATOM    570  CA  ASP A  80       7.499  40.445  69.895  1.00 45.32           C  
ATOM    571  C   ASP A  80       6.164  39.836  69.501  1.00 46.54           C  
ATOM    572  O   ASP A  80       6.082  39.016  68.570  1.00 46.31           O  
ATOM    573  CB  ASP A  80       8.204  39.599  70.945  1.00 48.92           C  
ATOM    574  CG  ASP A  80       9.616  40.070  71.199  1.00 52.23           C  
ATOM    575  OD1 ASP A  80      10.225  39.653  72.212  1.00 54.88           O  
ATOM    576  OD2 ASP A  80      10.118  40.857  70.378  1.00 50.93           O  
ATOM    577  N   PHE A  81       5.107  40.236  70.194  1.00 45.63           N  
ATOM    578  CA  PHE A  81       3.790  39.728  69.864  1.00 44.66           C  
ATOM    579  C   PHE A  81       3.433  40.124  68.426  1.00 43.62           C  
ATOM    580  O   PHE A  81       3.134  39.269  67.598  1.00 44.03           O  
ATOM    581  CB  PHE A  81       2.724  40.306  70.799  1.00 44.63           C  
ATOM    582  CG  PHE A  81       1.331  39.860  70.449  1.00 44.94           C  
ATOM    583  CD1 PHE A  81       0.855  38.632  70.880  1.00 40.57           C  
ATOM    584  CD2 PHE A  81       0.524  40.637  69.623  1.00 42.89           C  
ATOM    585  CE1 PHE A  81      -0.395  38.186  70.491  1.00 41.81           C  
ATOM    586  CE2 PHE A  81      -0.733  40.199  69.228  1.00 40.53           C  
ATOM    587  CZ  PHE A  81      -1.194  38.972  69.661  1.00 39.98           C  
ATOM    588  N   THR A  82       3.475  41.430  68.161  1.00 42.03           N  
ATOM    589  CA  THR A  82       3.143  41.989  66.857  1.00 42.13           C  
ATOM    590  C   THR A  82       4.036  41.447  65.746  1.00 41.65           C  
ATOM    591  O   THR A  82       3.586  41.253  64.622  1.00 43.07           O  
ATOM    592  CB  THR A  82       3.258  43.544  66.849  1.00 44.03           C  
ATOM    593  OG1 THR A  82       2.717  44.079  68.059  1.00 40.98           O  
ATOM    594  CG2 THR A  82       2.490  44.135  65.668  1.00 40.92           C  
ATOM    595  N   PHE A  83       5.308  41.226  66.053  1.00 41.44           N  
ATOM    596  CA  PHE A  83       6.228  40.697  65.047  1.00 41.19           C  
ATOM    597  C   PHE A  83       5.731  39.319  64.614  1.00 38.54           C  
ATOM    598  O   PHE A  83       5.538  39.043  63.433  1.00 39.02           O  
ATOM    599  CB  PHE A  83       7.628  40.546  65.636  1.00 43.61           C  
ATOM    600  CG  PHE A  83       8.683  40.265  64.613  1.00 40.78           C  
ATOM    601  CD1 PHE A  83       9.474  41.298  64.121  1.00 40.97           C  
ATOM    602  CD2 PHE A  83       8.874  38.976  64.126  1.00 39.35           C  
ATOM    603  CE1 PHE A  83      10.442  41.057  63.158  1.00 40.32           C  
ATOM    604  CE2 PHE A  83       9.838  38.718  63.162  1.00 39.23           C  
ATOM    605  CZ  PHE A  83      10.627  39.758  62.675  1.00 41.65           C  
ATOM    606  N   SER A  84       5.530  38.456  65.600  1.00 39.85           N  
ATOM    607  CA  SER A  84       5.076  37.103  65.353  1.00 39.47           C  
ATOM    608  C   SER A  84       3.730  37.056  64.630  1.00 39.56           C  
ATOM    609  O   SER A  84       3.529  36.211  63.750  1.00 39.61           O  
ATOM    610  CB  SER A  84       4.987  36.341  66.681  1.00 38.86           C  
ATOM    611  OG  SER A  84       6.206  36.470  67.417  1.00 35.20           O  
ATOM    612  N   LEU A  85       2.819  37.960  64.995  1.00 35.85           N  
ATOM    613  CA  LEU A  85       1.497  38.005  64.376  1.00 35.98           C  
ATOM    614  C   LEU A  85       1.600  38.343  62.887  1.00 36.85           C  
ATOM    615  O   LEU A  85       1.231  37.549  62.010  1.00 38.58           O  
ATOM    616  CB  LEU A  85       0.623  39.078  65.035  1.00 34.62           C  
ATOM    617  CG  LEU A  85      -0.910  38.892  65.083  1.00 35.95           C  
ATOM    618  CD1 LEU A  85      -1.566  40.264  65.026  1.00 30.62           C  
ATOM    619  CD2 LEU A  85      -1.416  38.020  63.939  1.00 33.71           C  
ATOM    620  N   VAL A  86       2.100  39.547  62.631  1.00 37.93           N  
ATOM    621  CA  VAL A  86       2.235  40.073  61.297  1.00 36.67           C  
ATOM    622  C   VAL A  86       3.200  39.324  60.381  1.00 39.46           C  
ATOM    623  O   VAL A  86       2.946  39.191  59.191  1.00 39.35           O  
ATOM    624  CB  VAL A  86       2.650  41.556  61.347  1.00 35.37           C  
ATOM    625  CG1 VAL A  86       2.795  42.113  59.934  1.00 30.56           C  
ATOM    626  CG2 VAL A  86       1.626  42.349  62.117  1.00 29.89           C  
ATOM    627  N   ASN A  87       4.303  38.839  60.935  1.00 40.50           N  
ATOM    628  CA  ASN A  87       5.298  38.148  60.135  1.00 43.51           C  
ATOM    629  C   ASN A  87       5.063  36.662  59.903  1.00 43.07           C  
ATOM    630  O   ASN A  87       5.781  36.039  59.130  1.00 43.38           O  
ATOM    631  CB  ASN A  87       6.686  38.353  60.751  1.00 47.34           C  
ATOM    632  CG  ASN A  87       7.193  39.772  60.579  1.00 50.70           C  
ATOM    633  OD1 ASN A  87       7.587  40.172  59.486  1.00 52.00           O  
ATOM    634  ND2 ASN A  87       7.173  40.544  61.657  1.00 51.94           N  
ATOM    635  N   GLY A  88       4.069  36.087  60.566  1.00 41.28           N  
ATOM    636  CA  GLY A  88       3.815  34.669  60.392  1.00 41.42           C  
ATOM    637  C   GLY A  88       2.533  34.390  59.645  1.00 41.96           C  
ATOM    638  O   GLY A  88       2.488  34.424  58.402  1.00 38.69           O  
ATOM    639  N   PHE A  89       1.483  34.099  60.410  1.00 42.62           N  
ATOM    640  CA  PHE A  89       0.175  33.827  59.822  1.00 45.02           C  
ATOM    641  C   PHE A  89      -0.659  35.102  59.858  1.00 43.81           C  
ATOM    642  O   PHE A  89      -0.702  35.790  60.883  1.00 41.95           O  
ATOM    643  CB  PHE A  89      -0.537  32.700  60.569  1.00 42.94           C  
ATOM    644  CG  PHE A  89      -1.925  32.434  60.066  1.00 44.91           C  
ATOM    645  CD1 PHE A  89      -3.017  33.114  60.604  1.00 43.85           C  
ATOM    646  CD2 PHE A  89      -2.136  31.560  59.013  1.00 44.31           C  
ATOM    647  CE1 PHE A  89      -4.301  32.929  60.093  1.00 39.58           C  
ATOM    648  CE2 PHE A  89      -3.416  31.367  58.494  1.00 46.29           C  
ATOM    649  CZ  PHE A  89      -4.502  32.059  59.039  1.00 42.12           C  
ATOM    650  N   PRO A  90      -1.358  35.419  58.749  1.00 41.90           N  
ATOM    651  CA  PRO A  90      -1.430  34.678  57.488  1.00 41.59           C  
ATOM    652  C   PRO A  90      -0.592  35.203  56.316  1.00 41.91           C  
ATOM    653  O   PRO A  90      -0.462  34.525  55.299  1.00 38.98           O  
ATOM    654  CB  PRO A  90      -2.906  34.766  57.154  1.00 42.20           C  
ATOM    655  CG  PRO A  90      -3.166  36.208  57.453  1.00 41.75           C  
ATOM    656  CD  PRO A  90      -2.452  36.408  58.808  1.00 42.80           C  
ATOM    657  N   LEU A  91      -0.040  36.405  56.436  1.00 41.95           N  
ATOM    658  CA  LEU A  91       0.724  36.980  55.334  1.00 41.05           C  
ATOM    659  C   LEU A  91       1.827  36.086  54.744  1.00 44.50           C  
ATOM    660  O   LEU A  91       1.921  35.940  53.521  1.00 44.48           O  
ATOM    661  CB  LEU A  91       1.292  38.345  55.753  1.00 40.70           C  
ATOM    662  CG  LEU A  91       0.221  39.409  56.068  1.00 39.34           C  
ATOM    663  CD1 LEU A  91       0.850  40.701  56.558  1.00 35.53           C  
ATOM    664  CD2 LEU A  91      -0.611  39.662  54.834  1.00 33.48           C  
ATOM    665  N   MET A  92       2.662  35.476  55.581  1.00 44.04           N  
ATOM    666  CA  MET A  92       3.717  34.634  55.028  1.00 44.71           C  
ATOM    667  C   MET A  92       3.253  33.201  54.845  1.00 45.02           C  
ATOM    668  O   MET A  92       3.345  32.643  53.752  1.00 45.93           O  
ATOM    669  CB  MET A  92       4.973  34.659  55.902  1.00 42.81           C  
ATOM    670  CG  MET A  92       6.177  34.012  55.210  1.00 42.41           C  
ATOM    671  SD  MET A  92       7.731  33.965  56.149  1.00 41.60           S  
ATOM    672  CE  MET A  92       8.730  33.070  55.027  1.00 39.13           C  
ATOM    673  N   THR A  93       2.750  32.607  55.916  1.00 44.59           N  
ATOM    674  CA  THR A  93       2.281  31.236  55.869  1.00 43.78           C  
ATOM    675  C   THR A  93       1.385  30.970  54.667  1.00 45.94           C  
ATOM    676  O   THR A  93       1.595  29.996  53.947  1.00 49.29           O  
ATOM    677  CB  THR A  93       1.537  30.879  57.161  1.00 44.32           C  
ATOM    678  OG1 THR A  93       2.406  31.122  58.271  1.00 44.40           O  
ATOM    679  CG2 THR A  93       1.102  29.406  57.162  1.00 42.15           C  
ATOM    680  N   ILE A  94       0.390  31.827  54.445  1.00 43.49           N  
ATOM    681  CA  ILE A  94      -0.516  31.639  53.317  1.00 41.54           C  
ATOM    682  C   ILE A  94       0.248  31.803  52.006  1.00 42.23           C  
ATOM    683  O   ILE A  94       0.017  31.066  51.054  1.00 41.11           O  
ATOM    684  CB  ILE A  94      -1.705  32.632  53.375  1.00 41.63           C  
ATOM    685  CG1 ILE A  94      -2.639  32.243  54.520  1.00 41.21           C  
ATOM    686  CG2 ILE A  94      -2.484  32.631  52.067  1.00 39.28           C  
ATOM    687  CD1 ILE A  94      -3.218  30.860  54.393  1.00 41.36           C  
ATOM    688  N   SER A  95       1.168  32.764  51.971  1.00 45.45           N  
ATOM    689  CA  SER A  95       1.964  33.006  50.782  1.00 43.86           C  
ATOM    690  C   SER A  95       2.770  31.776  50.417  1.00 41.28           C  
ATOM    691  O   SER A  95       2.855  31.403  49.245  1.00 37.39           O  
ATOM    692  CB  SER A  95       2.905  34.187  50.994  1.00 47.72           C  
ATOM    693  OG  SER A  95       2.213  35.399  50.793  1.00 50.35           O  
ATOM    694  N   CYS A  96       3.359  31.141  51.421  1.00 39.70           N  
ATOM    695  CA  CYS A  96       4.146  29.945  51.167  1.00 42.81           C  
ATOM    696  C   CYS A  96       3.300  28.838  50.556  1.00 43.62           C  
ATOM    697  O   CYS A  96       3.603  28.359  49.465  1.00 44.38           O  
ATOM    698  CB  CYS A  96       4.805  29.453  52.458  1.00 43.84           C  
ATOM    699  SG  CYS A  96       6.184  30.484  53.013  1.00 41.97           S  
ATOM    700  N   PHE A  97       2.228  28.441  51.237  1.00 47.04           N  
ATOM    701  CA  PHE A  97       1.367  27.372  50.726  1.00 47.09           C  
ATOM    702  C   PHE A  97       0.863  27.560  49.311  1.00 47.36           C  
ATOM    703  O   PHE A  97       0.347  26.622  48.721  1.00 47.47           O  
ATOM    704  CB  PHE A  97       0.173  27.147  51.650  1.00 46.10           C  
ATOM    705  CG  PHE A  97       0.555  26.728  53.034  1.00 48.92           C  
ATOM    706  CD1 PHE A  97       1.662  25.911  53.247  1.00 48.59           C  
ATOM    707  CD2 PHE A  97      -0.193  27.146  54.123  1.00 48.67           C  
ATOM    708  CE1 PHE A  97       2.021  25.519  54.533  1.00 50.67           C  
ATOM    709  CE2 PHE A  97       0.156  26.761  55.411  1.00 51.83           C  
ATOM    710  CZ  PHE A  97       1.264  25.948  55.620  1.00 51.06           C  
ATOM    711  N   LEU A  98       1.003  28.765  48.768  1.00 48.69           N  
ATOM    712  CA  LEU A  98       0.560  29.051  47.400  1.00 49.32           C  
ATOM    713  C   LEU A  98       1.782  29.317  46.547  1.00 49.51           C  
ATOM    714  O   LEU A  98       1.683  29.558  45.337  1.00 52.29           O  
ATOM    715  CB  LEU A  98      -0.344  30.287  47.366  1.00 49.86           C  
ATOM    716  CG  LEU A  98      -1.688  30.187  48.079  1.00 49.50           C  
ATOM    717  CD1 LEU A  98      -2.332  31.564  48.110  1.00 48.16           C  
ATOM    718  CD2 LEU A  98      -2.579  29.165  47.361  1.00 51.41           C  
ATOM    719  N   LYS A  99       2.938  29.293  47.195  1.00 49.68           N  
ATOM    720  CA  LYS A  99       4.200  29.542  46.518  1.00 50.18           C  
ATOM    721  C   LYS A  99       4.188  30.917  45.866  1.00 49.31           C  
ATOM    722  O   LYS A  99       4.773  31.104  44.806  1.00 50.19           O  
ATOM    723  CB  LYS A  99       4.445  28.443  45.487  1.00 51.59           C  
ATOM    724  CG  LYS A  99       4.581  27.069  46.146  1.00 54.82           C  
ATOM    725  CD  LYS A  99       3.942  25.949  45.349  1.00 54.70           C  
ATOM    726  CE  LYS A  99       4.711  25.640  44.090  1.00 55.54           C  
ATOM    727  NZ  LYS A  99       4.103  24.482  43.382  1.00 57.55           N  
ATOM    728  N   LYS A 100       3.526  31.880  46.513  1.00 49.59           N  
ATOM    729  CA  LYS A 100       3.437  33.240  45.994  1.00 48.46           C  
ATOM    730  C   LYS A 100       2.822  34.229  46.986  1.00 47.12           C  
ATOM    731  O   LYS A 100       1.943  33.860  47.758  1.00 48.72           O  
ATOM    732  CB  LYS A 100       2.612  33.245  44.706  1.00 46.46           C  
ATOM    733  CG  LYS A 100       2.465  34.612  44.072  1.00 49.54           C  
ATOM    734  CD  LYS A 100       1.968  34.510  42.633  1.00 52.83           C  
ATOM    735  CE  LYS A 100       2.913  33.667  41.782  1.00 51.68           C  
ATOM    736  NZ  LYS A 100       4.318  34.148  41.872  1.00 51.50           N  
ATOM    737  N   TRP A 101       3.294  35.477  46.962  1.00 45.50           N  
ATOM    738  CA  TRP A 101       2.765  36.528  47.826  1.00 45.72           C  
ATOM    739  C   TRP A 101       1.553  37.137  47.144  1.00 46.22           C  
ATOM    740  O   TRP A 101       1.679  37.928  46.205  1.00 49.40           O  
ATOM    741  CB  TRP A 101       3.815  37.620  48.084  1.00 42.64           C  
ATOM    742  CG  TRP A 101       3.285  38.800  48.883  1.00 41.57           C  
ATOM    743  CD1 TRP A 101       2.622  39.889  48.392  1.00 40.03           C  
ATOM    744  CD2 TRP A 101       3.362  38.987  50.303  1.00 38.16           C  
ATOM    745  NE1 TRP A 101       2.284  40.740  49.412  1.00 36.81           N  
ATOM    746  CE2 TRP A 101       2.724  40.213  50.597  1.00 37.18           C  
ATOM    747  CE3 TRP A 101       3.906  38.236  51.359  1.00 41.00           C  
ATOM    748  CZ2 TRP A 101       2.612  40.713  51.910  1.00 37.18           C  
ATOM    749  CZ3 TRP A 101       3.795  38.735  52.672  1.00 38.17           C  
ATOM    750  CH2 TRP A 101       3.153  39.961  52.928  1.00 37.71           C  
ATOM    751  N   ILE A 102       0.374  36.760  47.622  1.00 46.00           N  
ATOM    752  CA  ILE A 102      -0.896  37.216  47.055  1.00 45.76           C  
ATOM    753  C   ILE A 102      -1.551  38.387  47.772  1.00 44.95           C  
ATOM    754  O   ILE A 102      -2.723  38.646  47.538  1.00 46.87           O  
ATOM    755  CB  ILE A 102      -1.933  36.087  47.086  1.00 45.30           C  
ATOM    756  CG1 ILE A 102      -2.167  35.664  48.552  1.00 43.54           C  
ATOM    757  CG2 ILE A 102      -1.462  34.918  46.240  1.00 44.34           C  
ATOM    758  CD1 ILE A 102      -3.390  34.800  48.785  1.00 41.12           C  
ATOM    759  N   PHE A 103      -0.825  39.101  48.623  1.00 43.93           N  
ATOM    760  CA  PHE A 103      -1.456  40.181  49.372  1.00 43.10           C  
ATOM    761  C   PHE A 103      -1.189  41.601  48.920  1.00 42.13           C  
ATOM    762  O   PHE A 103      -1.565  42.550  49.607  1.00 44.61           O  
ATOM    763  CB  PHE A 103      -1.129  40.022  50.859  1.00 43.58           C  
ATOM    764  CG  PHE A 103      -1.542  38.687  51.424  1.00 45.33           C  
ATOM    765  CD1 PHE A 103      -2.888  38.398  51.651  1.00 43.16           C  
ATOM    766  CD2 PHE A 103      -0.594  37.701  51.674  1.00 42.41           C  
ATOM    767  CE1 PHE A 103      -3.279  37.140  52.116  1.00 45.65           C  
ATOM    768  CE2 PHE A 103      -0.974  36.441  52.138  1.00 41.22           C  
ATOM    769  CZ  PHE A 103      -2.312  36.159  52.357  1.00 43.51           C  
ATOM    770  N   GLY A 104      -0.558  41.752  47.761  1.00 40.87           N  
ATOM    771  CA  GLY A 104      -0.291  43.079  47.237  1.00 37.91           C  
ATOM    772  C   GLY A 104       0.893  43.818  47.812  1.00 35.74           C  
ATOM    773  O   GLY A 104       1.405  43.472  48.865  1.00 37.60           O  
ATOM    774  N   PHE A 105       1.307  44.868  47.112  1.00 38.87           N  
ATOM    775  CA  PHE A 105       2.443  45.691  47.512  1.00 42.08           C  
ATOM    776  C   PHE A 105       2.256  46.404  48.843  1.00 41.95           C  
ATOM    777  O   PHE A 105       3.166  46.435  49.660  1.00 45.83           O  
ATOM    778  CB  PHE A 105       2.754  46.711  46.418  1.00 45.01           C  
ATOM    779  CG  PHE A 105       4.200  47.131  46.372  1.00 50.33           C  
ATOM    780  CD1 PHE A 105       4.579  48.296  45.717  1.00 50.42           C  
ATOM    781  CD2 PHE A 105       5.183  46.366  46.990  1.00 50.80           C  
ATOM    782  CE1 PHE A 105       5.907  48.695  45.681  1.00 46.66           C  
ATOM    783  CE2 PHE A 105       6.516  46.759  46.955  1.00 52.74           C  
ATOM    784  CZ  PHE A 105       6.874  47.926  46.300  1.00 50.25           C  
ATOM    785  N   ALA A 106       1.082  46.987  49.059  1.00 42.48           N  
ATOM    786  CA  ALA A 106       0.795  47.702  50.306  1.00 40.88           C  
ATOM    787  C   ALA A 106       1.005  46.797  51.518  1.00 40.66           C  
ATOM    788  O   ALA A 106       1.582  47.214  52.522  1.00 41.03           O  
ATOM    789  CB  ALA A 106      -0.632  48.231  50.292  1.00 41.46           C  
ATOM    790  N   ALA A 107       0.533  45.560  51.425  1.00 40.05           N  
ATOM    791  CA  ALA A 107       0.697  44.622  52.518  1.00 40.88           C  
ATOM    792  C   ALA A 107       2.184  44.340  52.723  1.00 41.56           C  
ATOM    793  O   ALA A 107       2.667  44.294  53.849  1.00 42.62           O  
ATOM    794  CB  ALA A 107      -0.055  43.334  52.220  1.00 41.38           C  
ATOM    795  N   CYS A 108       2.907  44.161  51.626  1.00 42.50           N  
ATOM    796  CA  CYS A 108       4.344  43.901  51.661  1.00 42.46           C  
ATOM    797  C   CYS A 108       5.049  45.004  52.434  1.00 41.94           C  
ATOM    798  O   CYS A 108       5.859  44.734  53.319  1.00 40.90           O  
ATOM    799  CB  CYS A 108       4.877  43.841  50.227  1.00 45.86           C  
ATOM    800  SG  CYS A 108       6.660  43.533  49.951  1.00 50.12           S  
ATOM    801  N   LYS A 109       4.733  46.251  52.103  1.00 41.08           N  
ATOM    802  CA  LYS A 109       5.353  47.379  52.787  1.00 44.55           C  
ATOM    803  C   LYS A 109       5.037  47.310  54.278  1.00 45.84           C  
ATOM    804  O   LYS A 109       5.928  47.377  55.124  1.00 47.32           O  
ATOM    805  CB  LYS A 109       4.845  48.696  52.203  1.00 42.59           C  
ATOM    806  CG  LYS A 109       5.018  48.781  50.702  1.00 41.00           C  
ATOM    807  CD  LYS A 109       4.553  50.112  50.173  1.00 43.84           C  
ATOM    808  CE  LYS A 109       4.774  50.206  48.674  1.00 46.61           C  
ATOM    809  NZ  LYS A 109       4.563  51.593  48.170  1.00 50.40           N  
ATOM    810  N   VAL A 110       3.756  47.169  54.594  1.00 48.47           N  
ATOM    811  CA  VAL A 110       3.332  47.077  55.981  1.00 47.74           C  
ATOM    812  C   VAL A 110       4.075  45.935  56.649  1.00 46.95           C  
ATOM    813  O   VAL A 110       4.554  46.056  57.779  1.00 47.86           O  
ATOM    814  CB  VAL A 110       1.823  46.812  56.083  1.00 48.76           C  
ATOM    815  CG1 VAL A 110       1.476  46.304  57.483  1.00 47.85           C  
ATOM    816  CG2 VAL A 110       1.051  48.096  55.764  1.00 46.88           C  
ATOM    817  N   TYR A 111       4.174  44.819  55.939  1.00 46.18           N  
ATOM    818  CA  TYR A 111       4.850  43.649  56.475  1.00 45.32           C  
ATOM    819  C   TYR A 111       6.294  43.986  56.807  1.00 46.10           C  
ATOM    820  O   TYR A 111       6.713  43.891  57.960  1.00 46.71           O  
ATOM    821  CB  TYR A 111       4.794  42.512  55.467  1.00 44.92           C  
ATOM    822  CG  TYR A 111       5.432  41.225  55.928  1.00 48.73           C  
ATOM    823  CD1 TYR A 111       4.650  40.114  56.256  1.00 49.33           C  
ATOM    824  CD2 TYR A 111       6.824  41.097  56.001  1.00 48.19           C  
ATOM    825  CE1 TYR A 111       5.239  38.907  56.643  1.00 46.79           C  
ATOM    826  CE2 TYR A 111       7.419  39.895  56.386  1.00 46.09           C  
ATOM    827  CZ  TYR A 111       6.621  38.810  56.704  1.00 46.11           C  
ATOM    828  OH  TYR A 111       7.205  37.631  57.095  1.00 42.53           O  
ATOM    829  N   GLY A 112       7.055  44.382  55.797  1.00 45.96           N  
ATOM    830  CA  GLY A 112       8.455  44.707  56.014  1.00 45.32           C  
ATOM    831  C   GLY A 112       8.689  45.798  57.040  1.00 45.06           C  
ATOM    832  O   GLY A 112       9.608  45.700  57.847  1.00 47.19           O  
ATOM    833  N   PHE A 113       7.856  46.835  56.994  1.00 42.98           N  
ATOM    834  CA  PHE A 113       7.943  47.972  57.906  1.00 42.20           C  
ATOM    835  C   PHE A 113       7.673  47.569  59.368  1.00 43.54           C  
ATOM    836  O   PHE A 113       8.319  48.070  60.296  1.00 41.12           O  
ATOM    837  CB  PHE A 113       6.947  49.038  57.457  1.00 45.52           C  
ATOM    838  CG  PHE A 113       6.869  50.232  58.364  1.00 48.26           C  
ATOM    839  CD1 PHE A 113       8.011  50.917  58.745  1.00 46.19           C  
ATOM    840  CD2 PHE A 113       5.631  50.703  58.798  1.00 53.64           C  
ATOM    841  CE1 PHE A 113       7.936  52.052  59.542  1.00 48.58           C  
ATOM    842  CE2 PHE A 113       5.541  51.844  59.601  1.00 55.28           C  
ATOM    843  CZ  PHE A 113       6.703  52.520  59.972  1.00 53.04           C  
ATOM    844  N   ILE A 114       6.707  46.674  59.557  1.00 42.86           N  
ATOM    845  CA  ILE A 114       6.349  46.189  60.869  1.00 41.23           C  
ATOM    846  C   ILE A 114       7.452  45.288  61.398  1.00 40.95           C  
ATOM    847  O   ILE A 114       7.767  45.288  62.596  1.00 40.87           O  
ATOM    848  CB  ILE A 114       5.036  45.393  60.817  1.00 44.30           C  
ATOM    849  CG1 ILE A 114       3.862  46.355  60.634  1.00 46.38           C  
ATOM    850  CG2 ILE A 114       4.867  44.562  62.079  1.00 42.15           C  
ATOM    851  CD1 ILE A 114       3.645  47.287  61.811  1.00 40.47           C  
ATOM    852  N   GLY A 115       8.041  44.514  60.497  1.00 41.20           N  
ATOM    853  CA  GLY A 115       9.110  43.619  60.887  1.00 42.47           C  
ATOM    854  C   GLY A 115      10.291  44.424  61.383  1.00 42.86           C  
ATOM    855  O   GLY A 115      10.889  44.114  62.419  1.00 40.82           O  
ATOM    856  N   GLY A 116      10.617  45.485  60.654  1.00 43.01           N  
ATOM    857  CA  GLY A 116      11.746  46.300  61.044  1.00 45.25           C  
ATOM    858  C   GLY A 116      11.499  47.144  62.269  1.00 48.43           C  
ATOM    859  O   GLY A 116      12.346  47.231  63.163  1.00 50.36           O  
ATOM    860  N   ILE A 117      10.326  47.765  62.305  1.00 51.10           N  
ATOM    861  CA  ILE A 117       9.936  48.640  63.398  1.00 52.69           C  
ATOM    862  C   ILE A 117       9.985  47.943  64.743  1.00 50.44           C  
ATOM    863  O   ILE A 117      10.410  48.537  65.723  1.00 50.05           O  
ATOM    864  CB  ILE A 117       8.516  49.215  63.152  1.00 55.65           C  
ATOM    865  CG1 ILE A 117       8.219  50.345  64.137  1.00 59.46           C  
ATOM    866  CG2 ILE A 117       7.485  48.135  63.311  1.00 57.41           C  
ATOM    867  CD1 ILE A 117       6.901  51.051  63.864  1.00 62.81           C  
ATOM    868  N   PHE A 118       9.564  46.682  64.798  1.00 52.26           N  
ATOM    869  CA  PHE A 118       9.585  45.956  66.070  1.00 51.46           C  
ATOM    870  C   PHE A 118      10.872  45.202  66.326  1.00 48.74           C  
ATOM    871  O   PHE A 118      11.129  44.763  67.440  1.00 47.99           O  
ATOM    872  CB  PHE A 118       8.377  45.023  66.180  1.00 50.03           C  
ATOM    873  CG  PHE A 118       7.092  45.760  66.366  1.00 46.20           C  
ATOM    874  CD1 PHE A 118       6.193  45.908  65.312  1.00 43.97           C  
ATOM    875  CD2 PHE A 118       6.827  46.391  67.571  1.00 43.31           C  
ATOM    876  CE1 PHE A 118       5.050  46.681  65.456  1.00 43.82           C  
ATOM    877  CE2 PHE A 118       5.685  47.173  67.732  1.00 47.09           C  
ATOM    878  CZ  PHE A 118       4.791  47.319  66.664  1.00 44.96           C  
ATOM    879  N   GLY A 119      11.676  45.047  65.283  1.00 50.68           N  
ATOM    880  CA  GLY A 119      12.959  44.393  65.441  1.00 48.72           C  
ATOM    881  C   GLY A 119      13.844  45.446  66.084  1.00 49.10           C  
ATOM    882  O   GLY A 119      14.630  45.156  66.986  1.00 46.35           O  
ATOM    883  N   PHE A 120      13.699  46.688  65.626  1.00 47.46           N  
ATOM    884  CA  PHE A 120      14.483  47.784  66.187  1.00 49.62           C  
ATOM    885  C   PHE A 120      13.999  48.065  67.603  1.00 50.30           C  
ATOM    886  O   PHE A 120      14.769  48.479  68.462  1.00 52.49           O  
ATOM    887  CB  PHE A 120      14.332  49.064  65.343  1.00 49.31           C  
ATOM    888  CG  PHE A 120      14.971  48.992  63.981  1.00 44.46           C  
ATOM    889  CD1 PHE A 120      14.380  49.635  62.900  1.00 44.23           C  
ATOM    890  CD2 PHE A 120      16.164  48.300  63.783  1.00 45.35           C  
ATOM    891  CE1 PHE A 120      14.961  49.596  61.622  1.00 45.50           C  
ATOM    892  CE2 PHE A 120      16.761  48.249  62.516  1.00 47.09           C  
ATOM    893  CZ  PHE A 120      16.152  48.904  61.426  1.00 46.88           C  
ATOM    894  N   MET A 121      12.712  47.828  67.836  1.00 53.82           N  
ATOM    895  CA  MET A 121      12.105  48.075  69.140  1.00 50.63           C  
ATOM    896  C   MET A 121      12.509  47.057  70.189  1.00 50.18           C  
ATOM    897  O   MET A 121      12.713  47.415  71.344  1.00 52.74           O  
ATOM    898  CB  MET A 121      10.585  48.113  69.032  1.00 51.00           C  
ATOM    899  CG  MET A 121       9.915  48.763  70.234  1.00 52.48           C  
ATOM    900  SD  MET A 121       8.199  49.292  69.916  1.00 57.64           S  
ATOM    901  CE  MET A 121       7.300  48.053  70.775  1.00 57.71           C  
ATOM    902  N   SER A 122      12.637  45.794  69.806  1.00 48.58           N  
ATOM    903  CA  SER A 122      13.025  44.802  70.786  1.00 50.45           C  
ATOM    904  C   SER A 122      14.422  45.029  71.384  1.00 50.78           C  
ATOM    905  O   SER A 122      14.613  44.854  72.590  1.00 50.60           O  
ATOM    906  CB  SER A 122      12.891  43.399  70.198  1.00 50.13           C  
ATOM    907  OG  SER A 122      11.523  43.039  70.136  1.00 49.16           O  
ATOM    908  N   ILE A 123      15.394  45.431  70.568  1.00 51.64           N  
ATOM    909  CA  ILE A 123      16.740  45.691  71.089  1.00 53.82           C  
ATOM    910  C   ILE A 123      16.798  47.006  71.850  1.00 52.80           C  
ATOM    911  O   ILE A 123      17.446  47.095  72.893  1.00 52.74           O  
ATOM    912  CB  ILE A 123      17.808  45.774  69.988  1.00 56.37           C  
ATOM    913  CG1 ILE A 123      17.141  45.805  68.614  1.00 58.22           C  
ATOM    914  CG2 ILE A 123      18.804  44.637  70.148  1.00 55.13           C  
ATOM    915  CD1 ILE A 123      18.083  46.136  67.487  1.00 60.13           C  
ATOM    916  N   MET A 124      16.133  48.034  71.336  1.00 53.55           N  
ATOM    917  CA  MET A 124      16.158  49.322  72.023  1.00 54.40           C  
ATOM    918  C   MET A 124      15.441  49.206  73.371  1.00 54.77           C  
ATOM    919  O   MET A 124      15.813  49.873  74.346  1.00 54.74           O  
ATOM    920  CB  MET A 124      15.510  50.411  71.171  1.00 52.57           C  
ATOM    921  CG  MET A 124      15.774  51.803  71.694  1.00 53.91           C  
ATOM    922  SD  MET A 124      17.522  52.074  72.097  1.00 54.29           S  
ATOM    923  CE  MET A 124      18.190  52.540  70.526  1.00 52.31           C  
ATOM    924  N   THR A 125      14.415  48.358  73.429  1.00 52.42           N  
ATOM    925  CA  THR A 125      13.703  48.170  74.679  1.00 50.91           C  
ATOM    926  C   THR A 125      14.697  47.490  75.599  1.00 49.72           C  
ATOM    927  O   THR A 125      14.822  47.857  76.763  1.00 46.60           O  
ATOM    928  CB  THR A 125      12.460  47.263  74.532  1.00 50.86           C  
ATOM    929  OG1 THR A 125      11.516  47.879  73.658  1.00 50.78           O  
ATOM    930  CG2 THR A 125      11.800  47.043  75.884  1.00 47.59           C  
ATOM    931  N   MET A 126      15.405  46.495  75.070  1.00 50.05           N  
ATOM    932  CA  MET A 126      16.401  45.795  75.868  1.00 52.27           C  
ATOM    933  C   MET A 126      17.430  46.819  76.349  1.00 53.64           C  
ATOM    934  O   MET A 126      17.904  46.748  77.482  1.00 52.59           O  
ATOM    935  CB  MET A 126      17.069  44.678  75.057  1.00 51.31           C  
ATOM    936  CG  MET A 126      16.208  43.426  74.925  1.00 52.04           C  
ATOM    937  SD  MET A 126      16.982  42.072  73.994  1.00 56.93           S  
ATOM    938  CE  MET A 126      15.630  41.528  72.938  1.00 54.16           C  
ATOM    939  N   ALA A 127      17.749  47.790  75.496  1.00 54.04           N  
ATOM    940  CA  ALA A 127      18.700  48.827  75.873  1.00 53.60           C  
ATOM    941  C   ALA A 127      18.180  49.540  77.130  1.00 55.66           C  
ATOM    942  O   ALA A 127      18.919  49.709  78.103  1.00 57.40           O  
ATOM    943  CB  ALA A 127      18.872  49.823  74.732  1.00 55.96           C  
ATOM    944  N   MET A 128      16.911  49.953  77.108  1.00 55.64           N  
ATOM    945  CA  MET A 128      16.311  50.628  78.253  1.00 55.03           C  
ATOM    946  C   MET A 128      16.360  49.719  79.475  1.00 55.92           C  
ATOM    947  O   MET A 128      16.467  50.186  80.617  1.00 54.67           O  
ATOM    948  CB  MET A 128      14.851  50.987  77.978  1.00 56.16           C  
ATOM    949  CG  MET A 128      14.641  51.900  76.800  1.00 58.22           C  
ATOM    950  SD  MET A 128      15.704  53.344  76.898  1.00 63.61           S  
ATOM    951  CE  MET A 128      16.341  53.366  75.235  1.00 61.34           C  
ATOM    952  N   ILE A 129      16.266  48.414  79.240  1.00 56.68           N  
ATOM    953  CA  ILE A 129      16.302  47.470  80.336  1.00 58.09           C  
ATOM    954  C   ILE A 129      17.719  47.371  80.870  1.00 59.58           C  
ATOM    955  O   ILE A 129      17.927  47.224  82.075  1.00 60.85           O  
ATOM    956  CB  ILE A 129      15.844  46.071  79.904  1.00 57.54           C  
ATOM    957  CG1 ILE A 129      14.386  46.118  79.446  1.00 58.96           C  
ATOM    958  CG2 ILE A 129      15.999  45.095  81.073  1.00 57.74           C  
ATOM    959  CD1 ILE A 129      13.861  44.791  78.901  1.00 56.78           C  
ATOM    960  N   SER A 130      18.693  47.459  79.971  1.00 59.39           N  
ATOM    961  CA  SER A 130      20.095  47.377  80.359  1.00 59.21           C  
ATOM    962  C   SER A 130      20.477  48.610  81.170  1.00 58.89           C  
ATOM    963  O   SER A 130      21.398  48.567  81.990  1.00 61.70           O  
ATOM    964  CB  SER A 130      20.989  47.286  79.122  1.00 59.60           C  
ATOM    965  OG  SER A 130      20.995  48.513  78.415  1.00 61.77           O  
ATOM    966  N   ILE A 131      19.763  49.707  80.937  1.00 54.87           N  
ATOM    967  CA  ILE A 131      20.022  50.948  81.647  1.00 51.75           C  
ATOM    968  C   ILE A 131      19.503  50.841  83.071  1.00 54.24           C  
ATOM    969  O   ILE A 131      20.167  51.251  84.029  1.00 54.61           O  
ATOM    970  CB  ILE A 131      19.345  52.122  80.947  1.00 49.74           C  
ATOM    971  CG1 ILE A 131      19.953  52.302  79.556  1.00 48.66           C  
ATOM    972  CG2 ILE A 131      19.500  53.373  81.764  1.00 49.85           C  
ATOM    973  CD1 ILE A 131      19.351  53.436  78.768  1.00 51.33           C  
ATOM    974  N   ASP A 132      18.301  50.290  83.207  1.00 54.49           N  
ATOM    975  CA  ASP A 132      17.701  50.110  84.522  1.00 51.14           C  
ATOM    976  C   ASP A 132      18.624  49.217  85.333  1.00 49.78           C  
ATOM    977  O   ASP A 132      18.880  49.483  86.502  1.00 50.72           O  
ATOM    978  CB  ASP A 132      16.323  49.467  84.395  1.00 47.79           C  
ATOM    979  CG  ASP A 132      15.784  48.992  85.717  1.00 45.99           C  
ATOM    980  OD1 ASP A 132      15.759  47.771  85.944  1.00 43.34           O  
ATOM    981  OD2 ASP A 132      15.392  49.844  86.529  1.00 47.96           O  
ATOM    982  N   ARG A 133      19.119  48.159  84.698  1.00 50.45           N  
ATOM    983  CA  ARG A 133      20.022  47.231  85.361  1.00 54.03           C  
ATOM    984  C   ARG A 133      21.258  47.967  85.884  1.00 56.61           C  
ATOM    985  O   ARG A 133      21.713  47.721  87.001  1.00 54.15           O  
ATOM    986  CB  ARG A 133      20.435  46.117  84.404  1.00 52.55           C  
ATOM    987  CG  ARG A 133      19.325  45.129  84.059  1.00 52.06           C  
ATOM    988  CD  ARG A 133      18.740  44.452  85.293  1.00 51.29           C  
ATOM    989  NE  ARG A 133      17.856  45.356  86.032  1.00 53.67           N  
ATOM    990  CZ  ARG A 133      17.370  45.124  87.250  1.00 53.11           C  
ATOM    991  NH1 ARG A 133      17.669  44.006  87.904  1.00 52.05           N  
ATOM    992  NH2 ARG A 133      16.587  46.021  87.820  1.00 50.46           N  
ATOM    993  N   TYR A 134      21.791  48.876  85.075  1.00 58.76           N  
ATOM    994  CA  TYR A 134      22.957  49.651  85.471  1.00 60.07           C  
ATOM    995  C   TYR A 134      22.671  50.566  86.658  1.00 61.55           C  
ATOM    996  O   TYR A 134      23.552  50.801  87.479  1.00 63.79           O  
ATOM    997  CB  TYR A 134      23.461  50.497  84.301  1.00 60.61           C  
ATOM    998  CG  TYR A 134      24.392  51.616  84.720  1.00 60.13           C  
ATOM    999  CD1 TYR A 134      23.986  52.950  84.667  1.00 59.29           C  
ATOM   1000  CD2 TYR A 134      25.677  51.338  85.178  1.00 59.82           C  
ATOM   1001  CE1 TYR A 134      24.841  53.976  85.058  1.00 59.25           C  
ATOM   1002  CE2 TYR A 134      26.535  52.350  85.571  1.00 59.10           C  
ATOM   1003  CZ  TYR A 134      26.112  53.667  85.509  1.00 60.37           C  
ATOM   1004  OH  TYR A 134      26.969  54.670  85.908  1.00 64.66           O  
ATOM   1005  N   ASN A 135      21.452  51.094  86.742  1.00 62.32           N  
ATOM   1006  CA  ASN A 135      21.098  51.985  87.846  1.00 64.17           C  
ATOM   1007  C   ASN A 135      20.880  51.243  89.165  1.00 64.55           C  
ATOM   1008  O   ASN A 135      21.105  51.793  90.242  1.00 63.23           O  
ATOM   1009  CB  ASN A 135      19.838  52.787  87.520  1.00 66.54           C  
ATOM   1010  CG  ASN A 135      20.122  53.996  86.658  1.00 69.26           C  
ATOM   1011  OD1 ASN A 135      21.005  54.795  86.968  1.00 71.23           O  
ATOM   1012  ND2 ASN A 135      19.364  54.146  85.574  1.00 71.89           N  
ATOM   1013  N   VAL A 136      20.433  49.998  89.079  1.00 64.85           N  
ATOM   1014  CA  VAL A 136      20.188  49.226  90.282  1.00 66.52           C  
ATOM   1015  C   VAL A 136      21.376  48.347  90.666  1.00 66.06           C  
ATOM   1016  O   VAL A 136      21.628  48.135  91.850  1.00 66.84           O  
ATOM   1017  CB  VAL A 136      18.912  48.338  90.134  1.00 67.55           C  
ATOM   1018  CG1 VAL A 136      19.035  47.430  88.928  1.00 69.38           C  
ATOM   1019  CG2 VAL A 136      18.704  47.506  91.391  1.00 65.37           C  
ATOM   1020  N   ILE A 137      22.110  47.852  89.672  1.00 65.22           N  
ATOM   1021  CA  ILE A 137      23.262  46.990  89.921  1.00 63.77           C  
ATOM   1022  C   ILE A 137      24.591  47.574  89.460  1.00 61.99           C  
ATOM   1023  O   ILE A 137      25.615  47.330  90.077  1.00 62.31           O  
ATOM   1024  CB  ILE A 137      23.106  45.617  89.232  1.00 64.26           C  
ATOM   1025  CG1 ILE A 137      21.919  44.859  89.823  1.00 65.35           C  
ATOM   1026  CG2 ILE A 137      24.376  44.800  89.409  1.00 65.82           C  
ATOM   1027  CD1 ILE A 137      22.098  44.496  91.287  1.00 66.09           C  
ATOM   1028  N   GLY A 138      24.576  48.329  88.370  1.00 61.88           N  
ATOM   1029  CA  GLY A 138      25.801  48.906  87.848  1.00 63.48           C  
ATOM   1030  C   GLY A 138      26.444  49.970  88.714  1.00 65.26           C  
ATOM   1031  O   GLY A 138      27.670  50.050  88.798  1.00 64.14           O  
ATOM   1032  N   ARG A 139      25.618  50.789  89.358  1.00 68.48           N  
ATOM   1033  CA  ARG A 139      26.101  51.865  90.225  1.00 72.28           C  
ATOM   1034  C   ARG A 139      26.348  51.349  91.645  1.00 74.13           C  
ATOM   1035  O   ARG A 139      25.988  50.219  91.971  1.00 75.69           O  
ATOM   1036  CB  ARG A 139      25.077  53.005  90.243  1.00 72.47           C  
ATOM   1037  CG  ARG A 139      24.566  53.357  88.856  1.00 72.66           C  
ATOM   1038  CD  ARG A 139      23.550  54.485  88.849  1.00 72.18           C  
ATOM   1039  NE  ARG A 139      24.172  55.787  89.037  1.00 74.17           N  
ATOM   1040  CZ  ARG A 139      23.649  56.928  88.600  1.00 77.15           C  
ATOM   1041  NH1 ARG A 139      22.495  56.922  87.946  1.00 74.65           N  
ATOM   1042  NH2 ARG A 139      24.274  58.079  88.820  1.00 79.74           N  
ATOM   1043  N   PRO A 140      26.981  52.163  92.508  1.00 75.94           N  
ATOM   1044  CA  PRO A 140      27.230  51.695  93.876  1.00 77.39           C  
ATOM   1045  C   PRO A 140      25.941  51.619  94.706  1.00 78.76           C  
ATOM   1046  O   PRO A 140      25.014  52.404  94.500  1.00 78.52           O  
ATOM   1047  CB  PRO A 140      28.225  52.721  94.412  1.00 76.79           C  
ATOM   1048  CG  PRO A 140      27.832  53.974  93.702  1.00 75.35           C  
ATOM   1049  CD  PRO A 140      27.577  53.494  92.290  1.00 75.46           C  
ATOM   1050  N   MET A 141      25.895  50.670  95.637  1.00 80.00           N  
ATOM   1051  CA  MET A 141      24.721  50.469  96.484  1.00 80.41           C  
ATOM   1052  C   MET A 141      24.234  51.743  97.155  1.00 78.18           C  
ATOM   1053  O   MET A 141      23.049  51.887  97.447  1.00 77.99           O  
ATOM   1054  CB  MET A 141      25.013  49.416  97.554  1.00 83.99           C  
ATOM   1055  CG  MET A 141      25.387  48.049  96.990  1.00 88.98           C  
ATOM   1056  SD  MET A 141      25.687  46.812  98.274  1.00 96.33           S  
ATOM   1057  CE  MET A 141      24.160  45.849  98.194  1.00 92.94           C  
ATOM   1058  N   ALA A 142      25.153  52.669  97.392  1.00 77.12           N  
ATOM   1059  CA  ALA A 142      24.806  53.932  98.029  1.00 74.93           C  
ATOM   1060  C   ALA A 142      24.029  54.831  97.071  1.00 73.33           C  
ATOM   1061  O   ALA A 142      23.155  55.586  97.494  1.00 71.13           O  
ATOM   1062  CB  ALA A 142      26.076  54.638  98.517  1.00 72.49           C  
ATOM   1063  N   ALA A 143      24.344  54.739  95.780  1.00 73.84           N  
ATOM   1064  CA  ALA A 143      23.684  55.562  94.765  1.00 74.27           C  
ATOM   1065  C   ALA A 143      22.669  54.792  93.914  1.00 73.41           C  
ATOM   1066  O   ALA A 143      22.122  55.330  92.947  1.00 69.97           O  
ATOM   1067  CB  ALA A 143      24.734  56.213  93.868  1.00 74.15           C  
ATOM   1068  N   SER A 144      22.419  53.539  94.287  1.00 74.33           N  
ATOM   1069  CA  SER A 144      21.467  52.682  93.586  1.00 75.80           C  
ATOM   1070  C   SER A 144      20.167  53.428  93.303  1.00 76.93           C  
ATOM   1071  O   SER A 144      19.615  54.077  94.189  1.00 77.64           O  
ATOM   1072  CB  SER A 144      21.171  51.438  94.427  1.00 74.40           C  
ATOM   1073  OG  SER A 144      20.168  50.639  93.827  1.00 73.23           O  
ATOM   1074  N   LYS A 145      19.675  53.332  92.072  1.00 78.44           N  
ATOM   1075  CA  LYS A 145      18.449  54.026  91.695  1.00 79.55           C  
ATOM   1076  C   LYS A 145      17.460  53.088  91.007  1.00 79.61           C  
ATOM   1077  O   LYS A 145      17.809  52.395  90.049  1.00 79.84           O  
ATOM   1078  CB  LYS A 145      18.788  55.194  90.762  1.00 81.58           C  
ATOM   1079  CG  LYS A 145      18.042  56.496  91.035  1.00 82.46           C  
ATOM   1080  CD  LYS A 145      16.559  56.386  90.737  1.00 84.71           C  
ATOM   1081  CE  LYS A 145      15.885  57.757  90.758  1.00 87.18           C  
ATOM   1082  NZ  LYS A 145      16.015  58.462  92.067  1.00 88.19           N  
ATOM   1083  N   LYS A 146      16.227  53.071  91.505  1.00 78.66           N  
ATOM   1084  CA  LYS A 146      15.179  52.236  90.938  1.00 77.13           C  
ATOM   1085  C   LYS A 146      14.426  53.002  89.854  1.00 75.71           C  
ATOM   1086  O   LYS A 146      14.388  54.232  89.860  1.00 73.08           O  
ATOM   1087  CB  LYS A 146      14.192  51.801  92.023  1.00 77.82           C  
ATOM   1088  CG  LYS A 146      14.071  50.295  92.185  1.00 78.56           C  
ATOM   1089  CD  LYS A 146      15.353  49.694  92.735  1.00 77.86           C  
ATOM   1090  CE  LYS A 146      15.227  48.195  92.895  1.00 77.75           C  
ATOM   1091  NZ  LYS A 146      16.424  47.613  93.559  1.00 77.64           N  
ATOM   1092  N   MET A 147      13.820  52.262  88.931  1.00 74.43           N  
ATOM   1093  CA  MET A 147      13.076  52.862  87.834  1.00 72.81           C  
ATOM   1094  C   MET A 147      11.758  53.480  88.301  1.00 72.58           C  
ATOM   1095  O   MET A 147      11.060  52.919  89.148  1.00 70.56           O  
ATOM   1096  CB  MET A 147      12.803  51.810  86.758  1.00 70.58           C  
ATOM   1097  CG  MET A 147      12.189  52.356  85.486  1.00 68.13           C  
ATOM   1098  SD  MET A 147      13.177  53.681  84.770  1.00 67.38           S  
ATOM   1099  CE  MET A 147      14.471  52.732  83.952  1.00 67.30           C  
ATOM   1100  N   SER A 148      11.427  54.641  87.744  1.00 72.51           N  
ATOM   1101  CA  SER A 148      10.192  55.326  88.090  1.00 73.33           C  
ATOM   1102  C   SER A 148       9.263  55.343  86.878  1.00 75.38           C  
ATOM   1103  O   SER A 148       9.723  55.338  85.736  1.00 73.55           O  
ATOM   1104  CB  SER A 148      10.483  56.763  88.530  1.00 71.39           C  
ATOM   1105  OG  SER A 148      10.965  57.545  87.449  1.00 70.27           O  
ATOM   1106  N   HIS A 149       7.957  55.355  87.135  1.00 77.85           N  
ATOM   1107  CA  HIS A 149       6.969  55.382  86.066  1.00 79.24           C  
ATOM   1108  C   HIS A 149       7.260  56.532  85.113  1.00 78.52           C  
ATOM   1109  O   HIS A 149       7.219  56.360  83.893  1.00 79.85           O  
ATOM   1110  CB  HIS A 149       5.561  55.522  86.648  1.00 81.97           C  
ATOM   1111  CG  HIS A 149       5.078  54.296  87.359  1.00 86.02           C  
ATOM   1112  ND1 HIS A 149       4.756  53.131  86.698  1.00 87.78           N  
ATOM   1113  CD2 HIS A 149       4.878  54.049  88.676  1.00 88.28           C  
ATOM   1114  CE1 HIS A 149       4.379  52.218  87.577  1.00 89.33           C  
ATOM   1115  NE2 HIS A 149       4.444  52.750  88.785  1.00 88.50           N  
ATOM   1116  N   ARG A 150       7.553  57.705  85.666  1.00 77.10           N  
ATOM   1117  CA  ARG A 150       7.862  58.863  84.841  1.00 76.11           C  
ATOM   1118  C   ARG A 150       8.955  58.477  83.864  1.00 74.39           C  
ATOM   1119  O   ARG A 150       8.724  58.407  82.659  1.00 74.35           O  
ATOM   1120  CB  ARG A 150       8.335  60.035  85.708  1.00 79.27           C  
ATOM   1121  CG  ARG A 150       7.210  60.915  86.243  1.00 83.97           C  
ATOM   1122  CD  ARG A 150       6.174  60.105  87.007  1.00 86.84           C  
ATOM   1123  NE  ARG A 150       6.779  59.360  88.105  1.00 89.83           N  
ATOM   1124  CZ  ARG A 150       6.127  58.477  88.853  1.00 92.08           C  
ATOM   1125  NH1 ARG A 150       6.757  57.844  89.835  1.00 92.48           N  
ATOM   1126  NH2 ARG A 150       4.848  58.224  88.616  1.00 93.53           N  
ATOM   1127  N   ARG A 151      10.144  58.211  84.395  1.00 72.48           N  
ATOM   1128  CA  ARG A 151      11.273  57.822  83.563  1.00 71.44           C  
ATOM   1129  C   ARG A 151      10.885  56.734  82.564  1.00 68.86           C  
ATOM   1130  O   ARG A 151      10.952  56.941  81.348  1.00 67.99           O  
ATOM   1131  CB  ARG A 151      12.440  57.342  84.433  1.00 73.61           C  
ATOM   1132  CG  ARG A 151      13.564  58.361  84.591  1.00 76.57           C  
ATOM   1133  CD  ARG A 151      13.094  59.635  85.292  1.00 81.84           C  
ATOM   1134  NE  ARG A 151      13.100  59.507  86.749  1.00 84.26           N  
ATOM   1135  CZ  ARG A 151      12.679  60.454  87.583  1.00 83.20           C  
ATOM   1136  NH1 ARG A 151      12.211  61.600  87.106  1.00 81.02           N  
ATOM   1137  NH2 ARG A 151      12.740  60.259  88.894  1.00 82.01           N  
ATOM   1138  N   ALA A 152      10.476  55.581  83.080  1.00 65.90           N  
ATOM   1139  CA  ALA A 152      10.092  54.457  82.236  1.00 64.72           C  
ATOM   1140  C   ALA A 152       9.206  54.892  81.072  1.00 65.54           C  
ATOM   1141  O   ALA A 152       9.517  54.624  79.908  1.00 65.29           O  
ATOM   1142  CB  ALA A 152       9.374  53.409  83.068  1.00 63.61           C  
ATOM   1143  N   PHE A 153       8.103  55.566  81.388  1.00 65.36           N  
ATOM   1144  CA  PHE A 153       7.182  56.030  80.362  1.00 64.96           C  
ATOM   1145  C   PHE A 153       7.888  56.856  79.283  1.00 63.20           C  
ATOM   1146  O   PHE A 153       7.652  56.656  78.093  1.00 64.57           O  
ATOM   1147  CB  PHE A 153       6.051  56.843  80.999  1.00 68.25           C  
ATOM   1148  CG  PHE A 153       5.070  57.405  80.008  1.00 70.42           C  
ATOM   1149  CD1 PHE A 153       4.410  56.571  79.114  1.00 72.70           C  
ATOM   1150  CD2 PHE A 153       4.820  58.772  79.958  1.00 72.54           C  
ATOM   1151  CE1 PHE A 153       3.512  57.094  78.175  1.00 73.44           C  
ATOM   1152  CE2 PHE A 153       3.926  59.303  79.027  1.00 73.68           C  
ATOM   1153  CZ  PHE A 153       3.272  58.460  78.132  1.00 72.25           C  
ATOM   1154  N   ILE A 154       8.754  57.779  79.689  1.00 61.44           N  
ATOM   1155  CA  ILE A 154       9.472  58.607  78.721  1.00 58.77           C  
ATOM   1156  C   ILE A 154      10.404  57.723  77.897  1.00 57.95           C  
ATOM   1157  O   ILE A 154      10.517  57.877  76.687  1.00 58.68           O  
ATOM   1158  CB  ILE A 154      10.313  59.698  79.426  1.00 57.93           C  
ATOM   1159  CG1 ILE A 154       9.427  60.505  80.374  1.00 55.27           C  
ATOM   1160  CG2 ILE A 154      10.929  60.629  78.397  1.00 53.58           C  
ATOM   1161  CD1 ILE A 154      10.209  61.341  81.368  1.00 56.37           C  
ATOM   1162  N   MET A 155      11.069  56.784  78.556  1.00 58.41           N  
ATOM   1163  CA  MET A 155      11.978  55.887  77.854  1.00 58.51           C  
ATOM   1164  C   MET A 155      11.288  55.094  76.732  1.00 59.22           C  
ATOM   1165  O   MET A 155      11.792  55.057  75.608  1.00 57.52           O  
ATOM   1166  CB  MET A 155      12.679  54.953  78.863  1.00 57.65           C  
ATOM   1167  CG  MET A 155      13.837  55.656  79.602  1.00 55.40           C  
ATOM   1168  SD  MET A 155      14.365  55.010  81.218  1.00 58.56           S  
ATOM   1169  CE  MET A 155      15.651  53.846  80.734  1.00 56.23           C  
ATOM   1170  N   ILE A 156      10.132  54.485  77.001  1.00 61.43           N  
ATOM   1171  CA  ILE A 156       9.471  53.734  75.932  1.00 62.06           C  
ATOM   1172  C   ILE A 156       9.046  54.665  74.794  1.00 61.04           C  
ATOM   1173  O   ILE A 156       9.086  54.274  73.626  1.00 59.87           O  
ATOM   1174  CB  ILE A 156       8.237  52.931  76.427  1.00 62.01           C  
ATOM   1175  CG1 ILE A 156       7.052  53.860  76.665  1.00 64.07           C  
ATOM   1176  CG2 ILE A 156       8.590  52.168  77.696  1.00 58.21           C  
ATOM   1177  CD1 ILE A 156       5.786  53.124  77.045  1.00 65.33           C  
ATOM   1178  N   ILE A 157       8.646  55.892  75.130  1.00 60.31           N  
ATOM   1179  CA  ILE A 157       8.262  56.859  74.107  1.00 60.84           C  
ATOM   1180  C   ILE A 157       9.466  57.075  73.194  1.00 60.38           C  
ATOM   1181  O   ILE A 157       9.318  57.194  71.971  1.00 59.52           O  
ATOM   1182  CB  ILE A 157       7.861  58.226  74.706  1.00 63.04           C  
ATOM   1183  CG1 ILE A 157       6.530  58.106  75.448  1.00 63.80           C  
ATOM   1184  CG2 ILE A 157       7.750  59.263  73.596  1.00 62.37           C  
ATOM   1185  CD1 ILE A 157       6.038  59.418  76.032  1.00 61.84           C  
ATOM   1186  N   PHE A 158      10.657  57.139  73.788  1.00 58.03           N  
ATOM   1187  CA  PHE A 158      11.863  57.305  72.988  1.00 57.94           C  
ATOM   1188  C   PHE A 158      11.988  56.062  72.111  1.00 57.32           C  
ATOM   1189  O   PHE A 158      12.254  56.150  70.909  1.00 56.05           O  
ATOM   1190  CB  PHE A 158      13.109  57.421  73.865  1.00 57.69           C  
ATOM   1191  CG  PHE A 158      14.389  57.135  73.127  1.00 59.01           C  
ATOM   1192  CD1 PHE A 158      14.803  57.954  72.079  1.00 59.72           C  
ATOM   1193  CD2 PHE A 158      15.160  56.021  73.448  1.00 59.76           C  
ATOM   1194  CE1 PHE A 158      15.970  57.664  71.354  1.00 58.69           C  
ATOM   1195  CE2 PHE A 158      16.326  55.723  72.729  1.00 60.31           C  
ATOM   1196  CZ  PHE A 158      16.728  56.548  71.681  1.00 59.75           C  
ATOM   1197  N   VAL A 159      11.797  54.903  72.735  1.00 55.16           N  
ATOM   1198  CA  VAL A 159      11.878  53.637  72.032  1.00 54.26           C  
ATOM   1199  C   VAL A 159      10.965  53.631  70.811  1.00 55.84           C  
ATOM   1200  O   VAL A 159      11.396  53.308  69.707  1.00 56.42           O  
ATOM   1201  CB  VAL A 159      11.452  52.461  72.925  1.00 54.75           C  
ATOM   1202  CG1 VAL A 159      11.583  51.162  72.145  1.00 53.06           C  
ATOM   1203  CG2 VAL A 159      12.286  52.432  74.210  1.00 52.44           C  
ATOM   1204  N   TRP A 160       9.697  53.979  71.010  1.00 54.46           N  
ATOM   1205  CA  TRP A 160       8.760  53.985  69.902  1.00 53.24           C  
ATOM   1206  C   TRP A 160       9.178  54.958  68.814  1.00 52.70           C  
ATOM   1207  O   TRP A 160       9.242  54.591  67.647  1.00 54.92           O  
ATOM   1208  CB  TRP A 160       7.337  54.285  70.391  1.00 54.69           C  
ATOM   1209  CG  TRP A 160       6.615  53.067  70.928  1.00 52.14           C  
ATOM   1210  CD1 TRP A 160       6.742  52.516  72.170  1.00 53.32           C  
ATOM   1211  CD2 TRP A 160       5.679  52.239  70.218  1.00 51.81           C  
ATOM   1212  NE1 TRP A 160       5.943  51.398  72.282  1.00 53.86           N  
ATOM   1213  CE2 TRP A 160       5.281  51.207  71.098  1.00 52.70           C  
ATOM   1214  CE3 TRP A 160       5.137  52.271  68.923  1.00 51.06           C  
ATOM   1215  CZ2 TRP A 160       4.366  50.217  70.726  1.00 51.95           C  
ATOM   1216  CZ3 TRP A 160       4.226  51.285  68.554  1.00 51.24           C  
ATOM   1217  CH2 TRP A 160       3.851  50.272  69.455  1.00 51.28           C  
ATOM   1218  N   LEU A 161       9.475  56.196  69.182  1.00 55.76           N  
ATOM   1219  CA  LEU A 161       9.895  57.176  68.188  1.00 54.94           C  
ATOM   1220  C   LEU A 161      11.112  56.665  67.435  1.00 55.74           C  
ATOM   1221  O   LEU A 161      11.138  56.646  66.200  1.00 56.49           O  
ATOM   1222  CB  LEU A 161      10.215  58.515  68.850  1.00 56.10           C  
ATOM   1223  CG  LEU A 161       9.038  59.483  68.883  1.00 57.71           C  
ATOM   1224  CD1 LEU A 161       8.509  59.653  67.462  1.00 59.29           C  
ATOM   1225  CD2 LEU A 161       7.939  58.950  69.786  1.00 61.98           C  
ATOM   1226  N   TRP A 162      12.123  56.248  68.184  1.00 54.85           N  
ATOM   1227  CA  TRP A 162      13.344  55.722  67.598  1.00 56.70           C  
ATOM   1228  C   TRP A 162      13.021  54.618  66.586  1.00 55.78           C  
ATOM   1229  O   TRP A 162      13.350  54.731  65.406  1.00 54.64           O  
ATOM   1230  CB  TRP A 162      14.237  55.181  68.715  1.00 62.44           C  
ATOM   1231  CG  TRP A 162      15.575  54.706  68.273  1.00 67.49           C  
ATOM   1232  CD1 TRP A 162      15.926  53.428  67.958  1.00 68.74           C  
ATOM   1233  CD2 TRP A 162      16.754  55.500  68.111  1.00 70.90           C  
ATOM   1234  NE1 TRP A 162      17.257  53.374  67.613  1.00 71.01           N  
ATOM   1235  CE2 TRP A 162      17.788  54.634  67.698  1.00 70.99           C  
ATOM   1236  CE3 TRP A 162      17.038  56.862  68.277  1.00 72.19           C  
ATOM   1237  CZ2 TRP A 162      19.089  55.086  67.446  1.00 72.04           C  
ATOM   1238  CZ3 TRP A 162      18.332  57.311  68.027  1.00 72.35           C  
ATOM   1239  CH2 TRP A 162      19.341  56.422  67.616  1.00 71.69           C  
ATOM   1240  N   SER A 163      12.354  53.564  67.054  1.00 55.56           N  
ATOM   1241  CA  SER A 163      11.985  52.426  66.210  1.00 54.28           C  
ATOM   1242  C   SER A 163      11.261  52.807  64.921  1.00 53.71           C  
ATOM   1243  O   SER A 163      11.595  52.319  63.846  1.00 53.35           O  
ATOM   1244  CB  SER A 163      11.115  51.457  66.993  1.00 53.85           C  
ATOM   1245  OG  SER A 163      11.796  50.992  68.136  1.00 53.25           O  
ATOM   1246  N   VAL A 164      10.258  53.665  65.029  1.00 52.72           N  
ATOM   1247  CA  VAL A 164       9.536  54.064  63.842  1.00 52.72           C  
ATOM   1248  C   VAL A 164      10.468  54.831  62.916  1.00 53.69           C  
ATOM   1249  O   VAL A 164      10.503  54.576  61.709  1.00 53.58           O  
ATOM   1250  CB  VAL A 164       8.332  54.950  64.192  1.00 52.55           C  
ATOM   1251  CG1 VAL A 164       7.531  55.269  62.932  1.00 49.25           C  
ATOM   1252  CG2 VAL A 164       7.472  54.246  65.219  1.00 47.81           C  
ATOM   1253  N   LEU A 165      11.234  55.754  63.494  1.00 52.74           N  
ATOM   1254  CA  LEU A 165      12.165  56.581  62.737  1.00 53.35           C  
ATOM   1255  C   LEU A 165      13.122  55.843  61.808  1.00 53.48           C  
ATOM   1256  O   LEU A 165      13.273  56.205  60.638  1.00 52.26           O  
ATOM   1257  CB  LEU A 165      12.989  57.445  63.691  1.00 54.26           C  
ATOM   1258  CG  LEU A 165      14.144  58.216  63.047  1.00 52.93           C  
ATOM   1259  CD1 LEU A 165      13.617  59.142  61.952  1.00 52.49           C  
ATOM   1260  CD2 LEU A 165      14.866  58.999  64.116  1.00 53.44           C  
ATOM   1261  N   TRP A 166      13.778  54.811  62.319  1.00 54.66           N  
ATOM   1262  CA  TRP A 166      14.736  54.081  61.507  1.00 57.04           C  
ATOM   1263  C   TRP A 166      14.149  52.988  60.635  1.00 55.82           C  
ATOM   1264  O   TRP A 166      14.873  52.338  59.884  1.00 58.77           O  
ATOM   1265  CB  TRP A 166      15.841  53.515  62.403  1.00 58.83           C  
ATOM   1266  CG  TRP A 166      16.552  54.601  63.133  1.00 61.80           C  
ATOM   1267  CD1 TRP A 166      16.724  54.704  64.480  1.00 63.30           C  
ATOM   1268  CD2 TRP A 166      17.111  55.789  62.562  1.00 63.37           C  
ATOM   1269  NE1 TRP A 166      17.350  55.888  64.789  1.00 66.03           N  
ATOM   1270  CE2 TRP A 166      17.599  56.574  63.629  1.00 65.27           C  
ATOM   1271  CE3 TRP A 166      17.245  56.270  61.251  1.00 64.36           C  
ATOM   1272  CZ2 TRP A 166      18.214  57.819  63.428  1.00 65.89           C  
ATOM   1273  CZ3 TRP A 166      17.858  57.510  61.048  1.00 64.90           C  
ATOM   1274  CH2 TRP A 166      18.334  58.269  62.135  1.00 65.44           C  
ATOM   1275  N   ALA A 167      12.839  52.791  60.718  1.00 54.76           N  
ATOM   1276  CA  ALA A 167      12.195  51.767  59.911  1.00 52.70           C  
ATOM   1277  C   ALA A 167      11.269  52.373  58.872  1.00 51.51           C  
ATOM   1278  O   ALA A 167      10.901  51.710  57.900  1.00 50.62           O  
ATOM   1279  CB  ALA A 167      11.415  50.814  60.800  1.00 50.22           C  
ATOM   1280  N   ILE A 168      10.913  53.639  59.055  1.00 49.16           N  
ATOM   1281  CA  ILE A 168       9.993  54.278  58.128  1.00 51.34           C  
ATOM   1282  C   ILE A 168      10.618  54.817  56.844  1.00 53.02           C  
ATOM   1283  O   ILE A 168       9.901  55.188  55.911  1.00 54.88           O  
ATOM   1284  CB  ILE A 168       9.205  55.405  58.828  1.00 52.43           C  
ATOM   1285  CG1 ILE A 168       7.900  55.654  58.073  1.00 52.33           C  
ATOM   1286  CG2 ILE A 168      10.050  56.672  58.922  1.00 48.74           C  
ATOM   1287  CD1 ILE A 168       6.837  56.350  58.909  1.00 52.79           C  
ATOM   1288  N   GLY A 169      11.946  54.848  56.787  1.00 52.37           N  
ATOM   1289  CA  GLY A 169      12.617  55.352  55.605  1.00 46.48           C  
ATOM   1290  C   GLY A 169      12.029  54.811  54.317  1.00 45.93           C  
ATOM   1291  O   GLY A 169      11.470  55.566  53.525  1.00 46.12           O  
ATOM   1292  N   PRO A 170      12.126  53.497  54.082  1.00 45.76           N  
ATOM   1293  CA  PRO A 170      11.595  52.881  52.869  1.00 45.73           C  
ATOM   1294  C   PRO A 170      10.137  53.231  52.572  1.00 47.45           C  
ATOM   1295  O   PRO A 170       9.682  53.126  51.425  1.00 46.45           O  
ATOM   1296  CB  PRO A 170      11.794  51.395  53.131  1.00 44.75           C  
ATOM   1297  CG  PRO A 170      13.050  51.386  53.925  1.00 44.25           C  
ATOM   1298  CD  PRO A 170      12.775  52.484  54.924  1.00 45.48           C  
ATOM   1299  N   ILE A 171       9.400  53.644  53.596  1.00 48.83           N  
ATOM   1300  CA  ILE A 171       8.003  54.002  53.401  1.00 52.03           C  
ATOM   1301  C   ILE A 171       7.930  55.282  52.580  1.00 54.50           C  
ATOM   1302  O   ILE A 171       6.960  55.514  51.859  1.00 52.75           O  
ATOM   1303  CB  ILE A 171       7.279  54.212  54.747  1.00 51.20           C  
ATOM   1304  CG1 ILE A 171       7.195  52.882  55.494  1.00 50.96           C  
ATOM   1305  CG2 ILE A 171       5.889  54.812  54.521  1.00 47.34           C  
ATOM   1306  CD1 ILE A 171       6.434  51.799  54.753  1.00 49.35           C  
ATOM   1307  N   PHE A 172       8.970  56.103  52.675  1.00 57.43           N  
ATOM   1308  CA  PHE A 172       8.992  57.361  51.946  1.00 59.14           C  
ATOM   1309  C   PHE A 172       9.993  57.445  50.804  1.00 59.51           C  
ATOM   1310  O   PHE A 172      10.292  58.531  50.316  1.00 60.56           O  
ATOM   1311  CB  PHE A 172       9.211  58.514  52.924  1.00 59.62           C  
ATOM   1312  CG  PHE A 172       8.036  58.767  53.819  1.00 63.69           C  
ATOM   1313  CD1 PHE A 172       6.768  58.976  53.272  1.00 63.99           C  
ATOM   1314  CD2 PHE A 172       8.184  58.798  55.201  1.00 63.62           C  
ATOM   1315  CE1 PHE A 172       5.666  59.209  54.089  1.00 63.73           C  
ATOM   1316  CE2 PHE A 172       7.089  59.032  56.029  1.00 63.81           C  
ATOM   1317  CZ  PHE A 172       5.829  59.237  55.471  1.00 63.56           C  
ATOM   1318  N   GLY A 173      10.504  56.299  50.369  1.00 60.81           N  
ATOM   1319  CA  GLY A 173      11.447  56.291  49.263  1.00 58.55           C  
ATOM   1320  C   GLY A 173      12.896  56.096  49.658  1.00 55.19           C  
ATOM   1321  O   GLY A 173      13.698  55.594  48.876  1.00 57.03           O  
ATOM   1322  N   TRP A 174      13.238  56.503  50.870  1.00 53.11           N  
ATOM   1323  CA  TRP A 174      14.600  56.356  51.357  1.00 52.91           C  
ATOM   1324  C   TRP A 174      14.824  54.878  51.676  1.00 52.78           C  
ATOM   1325  O   TRP A 174      14.998  54.485  52.833  1.00 53.00           O  
ATOM   1326  CB  TRP A 174      14.786  57.223  52.596  1.00 51.45           C  
ATOM   1327  CG  TRP A 174      16.167  57.241  53.137  1.00 51.10           C  
ATOM   1328  CD1 TRP A 174      17.325  57.030  52.449  1.00 48.55           C  
ATOM   1329  CD2 TRP A 174      16.544  57.559  54.479  1.00 50.19           C  
ATOM   1330  NE1 TRP A 174      18.405  57.202  53.282  1.00 50.71           N  
ATOM   1331  CE2 TRP A 174      17.953  57.527  54.535  1.00 51.63           C  
ATOM   1332  CE3 TRP A 174      15.826  57.875  55.638  1.00 50.29           C  
ATOM   1333  CZ2 TRP A 174      18.662  57.798  55.710  1.00 54.13           C  
ATOM   1334  CZ3 TRP A 174      16.529  58.148  56.808  1.00 52.51           C  
ATOM   1335  CH2 TRP A 174      17.935  58.107  56.833  1.00 53.83           C  
ATOM   1336  N   GLY A 175      14.810  54.071  50.624  1.00 51.46           N  
ATOM   1337  CA  GLY A 175      14.981  52.643  50.766  1.00 53.08           C  
ATOM   1338  C   GLY A 175      13.714  51.981  50.260  1.00 53.41           C  
ATOM   1339  O   GLY A 175      12.862  52.642  49.655  1.00 55.16           O  
ATOM   1340  N   ALA A 176      13.563  50.685  50.495  1.00 49.49           N  
ATOM   1341  CA  ALA A 176      12.370  50.023  50.030  1.00 45.35           C  
ATOM   1342  C   ALA A 176      12.112  48.700  50.724  1.00 45.51           C  
ATOM   1343  O   ALA A 176      13.021  48.059  51.259  1.00 43.07           O  
ATOM   1344  CB  ALA A 176      12.443  49.821  48.528  1.00 37.64           C  
ATOM   1345  N   TYR A 177      10.845  48.307  50.708  1.00 45.11           N  
ATOM   1346  CA  TYR A 177      10.405  47.060  51.293  1.00 44.44           C  
ATOM   1347  C   TYR A 177       9.838  46.233  50.154  1.00 44.93           C  
ATOM   1348  O   TYR A 177       8.845  46.601  49.536  1.00 48.24           O  
ATOM   1349  CB  TYR A 177       9.340  47.323  52.353  1.00 40.57           C  
ATOM   1350  CG  TYR A 177       9.913  47.781  53.669  1.00 39.65           C  
ATOM   1351  CD1 TYR A 177      10.778  46.954  54.383  1.00 38.83           C  
ATOM   1352  CD2 TYR A 177       9.575  49.021  54.218  1.00 36.64           C  
ATOM   1353  CE1 TYR A 177      11.291  47.338  55.618  1.00 36.87           C  
ATOM   1354  CE2 TYR A 177      10.090  49.420  55.466  1.00 37.51           C  
ATOM   1355  CZ  TYR A 177      10.945  48.563  56.159  1.00 35.58           C  
ATOM   1356  OH  TYR A 177      11.436  48.889  57.400  1.00 37.29           O  
ATOM   1357  N   THR A 178      10.480  45.115  49.866  1.00 43.34           N  
ATOM   1358  CA  THR A 178      10.024  44.279  48.779  1.00 43.64           C  
ATOM   1359  C   THR A 178      10.239  42.813  49.118  1.00 42.86           C  
ATOM   1360  O   THR A 178      10.621  42.487  50.244  1.00 44.20           O  
ATOM   1361  CB  THR A 178      10.784  44.659  47.479  1.00 41.85           C  
ATOM   1362  OG1 THR A 178      10.443  43.744  46.435  1.00 46.85           O  
ATOM   1363  CG2 THR A 178      12.281  44.643  47.712  1.00 37.86           C  
ATOM   1364  N   LEU A 179       9.980  41.933  48.157  1.00 41.76           N  
ATOM   1365  CA  LEU A 179      10.154  40.501  48.373  1.00 44.54           C  
ATOM   1366  C   LEU A 179      11.638  40.094  48.414  1.00 47.56           C  
ATOM   1367  O   LEU A 179      12.504  40.790  47.888  1.00 47.59           O  
ATOM   1368  CB  LEU A 179       9.443  39.735  47.262  1.00 40.60           C  
ATOM   1369  CG  LEU A 179       7.978  40.126  47.028  1.00 41.74           C  
ATOM   1370  CD1 LEU A 179       7.606  39.833  45.573  1.00 39.33           C  
ATOM   1371  CD2 LEU A 179       7.052  39.387  48.002  1.00 38.27           C  
ATOM   1372  N   GLU A 180      11.921  38.968  49.058  1.00 49.07           N  
ATOM   1373  CA  GLU A 180      13.280  38.455  49.146  1.00 47.48           C  
ATOM   1374  C   GLU A 180      13.229  36.933  49.037  1.00 47.75           C  
ATOM   1375  O   GLU A 180      12.147  36.347  48.979  1.00 46.54           O  
ATOM   1376  CB  GLU A 180      13.944  38.869  50.472  1.00 48.36           C  
ATOM   1377  CG  GLU A 180      13.494  38.088  51.702  1.00 45.37           C  
ATOM   1378  CD  GLU A 180      14.211  38.542  52.954  1.00 48.00           C  
ATOM   1379  OE1 GLU A 180      15.403  38.887  52.846  1.00 50.22           O  
ATOM   1380  OE2 GLU A 180      13.592  38.545  54.049  1.00 44.86           O  
ATOM   1381  N   GLY A 181      14.402  36.307  48.991  1.00 47.43           N  
ATOM   1382  CA  GLY A 181      14.480  34.861  48.906  1.00 42.59           C  
ATOM   1383  C   GLY A 181      13.474  34.173  48.006  1.00 39.13           C  
ATOM   1384  O   GLY A 181      13.439  34.423  46.803  1.00 39.08           O  
ATOM   1385  N   VAL A 182      12.658  33.295  48.578  1.00 40.12           N  
ATOM   1386  CA  VAL A 182      11.671  32.566  47.793  1.00 44.03           C  
ATOM   1387  C   VAL A 182      10.456  33.420  47.442  1.00 46.83           C  
ATOM   1388  O   VAL A 182       9.480  32.926  46.873  1.00 45.07           O  
ATOM   1389  CB  VAL A 182      11.211  31.304  48.516  1.00 43.72           C  
ATOM   1390  CG1 VAL A 182      12.373  30.336  48.653  1.00 45.28           C  
ATOM   1391  CG2 VAL A 182      10.659  31.665  49.878  1.00 48.31           C  
ATOM   1392  N   LEU A 183      10.516  34.701  47.806  1.00 47.70           N  
ATOM   1393  CA  LEU A 183       9.453  35.636  47.481  1.00 46.01           C  
ATOM   1394  C   LEU A 183       8.105  35.411  48.166  1.00 46.63           C  
ATOM   1395  O   LEU A 183       7.068  35.583  47.543  1.00 44.78           O  
ATOM   1396  CB  LEU A 183       9.257  35.621  45.970  1.00 46.09           C  
ATOM   1397  CG  LEU A 183      10.579  35.684  45.209  1.00 44.82           C  
ATOM   1398  CD1 LEU A 183      10.323  35.648  43.708  1.00 47.07           C  
ATOM   1399  CD2 LEU A 183      11.325  36.957  45.597  1.00 46.31           C  
ATOM   1400  N   CYS A 184       8.114  35.025  49.439  1.00 47.26           N  
ATOM   1401  CA  CYS A 184       6.867  34.793  50.163  1.00 45.77           C  
ATOM   1402  C   CYS A 184       6.818  35.559  51.468  1.00 44.44           C  
ATOM   1403  O   CYS A 184       6.036  35.254  52.360  1.00 45.76           O  
ATOM   1404  CB  CYS A 184       6.639  33.304  50.406  1.00 41.70           C  
ATOM   1405  SG  CYS A 184       6.087  32.470  48.915  1.00 50.05           S  
ATOM   1406  N   ASN A 185       7.693  36.542  51.581  1.00 42.38           N  
ATOM   1407  CA  ASN A 185       7.700  37.407  52.741  1.00 44.20           C  
ATOM   1408  C   ASN A 185       8.434  38.644  52.263  1.00 46.33           C  
ATOM   1409  O   ASN A 185       9.065  38.629  51.204  1.00 48.21           O  
ATOM   1410  CB  ASN A 185       8.370  36.755  53.962  1.00 43.48           C  
ATOM   1411  CG  ASN A 185       9.875  36.745  53.883  1.00 43.46           C  
ATOM   1412  OD1 ASN A 185      10.470  35.793  53.381  1.00 42.73           O  
ATOM   1413  ND2 ASN A 185      10.507  37.811  54.384  1.00 40.19           N  
ATOM   1414  N   CYS A 186       8.327  39.728  53.010  1.00 46.42           N  
ATOM   1415  CA  CYS A 186       8.962  40.955  52.588  1.00 45.26           C  
ATOM   1416  C   CYS A 186       9.999  41.432  53.582  1.00 44.51           C  
ATOM   1417  O   CYS A 186      10.081  40.927  54.692  1.00 43.23           O  
ATOM   1418  CB  CYS A 186       7.872  42.014  52.335  1.00 44.57           C  
ATOM   1419  SG  CYS A 186       7.020  41.704  50.740  1.00 48.76           S  
ATOM   1420  N   SER A 187      10.820  42.380  53.154  1.00 48.25           N  
ATOM   1421  CA  SER A 187      11.873  42.945  53.991  1.00 50.01           C  
ATOM   1422  C   SER A 187      12.362  44.188  53.264  1.00 50.82           C  
ATOM   1423  O   SER A 187      11.763  44.591  52.269  1.00 50.56           O  
ATOM   1424  CB  SER A 187      13.019  41.942  54.143  1.00 48.96           C  
ATOM   1425  OG  SER A 187      13.988  42.417  55.062  1.00 50.61           O  
ATOM   1426  N   PHE A 188      13.435  44.804  53.751  1.00 51.61           N  
ATOM   1427  CA  PHE A 188      13.963  45.987  53.078  1.00 52.76           C  
ATOM   1428  C   PHE A 188      14.831  45.557  51.905  1.00 52.83           C  
ATOM   1429  O   PHE A 188      15.167  44.382  51.766  1.00 53.60           O  
ATOM   1430  CB  PHE A 188      14.757  46.856  54.052  1.00 54.15           C  
ATOM   1431  CG  PHE A 188      15.938  46.166  54.678  1.00 58.01           C  
ATOM   1432  CD1 PHE A 188      17.238  46.496  54.295  1.00 59.14           C  
ATOM   1433  CD2 PHE A 188      15.758  45.210  55.664  1.00 57.05           C  
ATOM   1434  CE1 PHE A 188      18.345  45.882  54.887  1.00 57.20           C  
ATOM   1435  CE2 PHE A 188      16.855  44.589  56.264  1.00 57.95           C  
ATOM   1436  CZ  PHE A 188      18.153  44.929  55.871  1.00 57.35           C  
ATOM   1437  N   ASP A 189      15.187  46.504  51.049  1.00 55.69           N  
ATOM   1438  CA  ASP A 189      16.015  46.207  49.881  1.00 55.95           C  
ATOM   1439  C   ASP A 189      17.511  46.332  50.203  1.00 56.93           C  
ATOM   1440  O   ASP A 189      18.035  47.438  50.365  1.00 56.77           O  
ATOM   1441  CB  ASP A 189      15.635  47.153  48.742  1.00 53.69           C  
ATOM   1442  CG  ASP A 189      16.254  46.759  47.427  1.00 55.30           C  
ATOM   1443  OD1 ASP A 189      16.971  45.738  47.381  1.00 55.01           O  
ATOM   1444  OD2 ASP A 189      16.016  47.478  46.437  1.00 57.25           O  
ATOM   1445  N   TYR A 190      18.185  45.188  50.305  1.00 56.85           N  
ATOM   1446  CA  TYR A 190      19.618  45.157  50.607  1.00 55.12           C  
ATOM   1447  C   TYR A 190      20.413  44.812  49.355  1.00 53.71           C  
ATOM   1448  O   TYR A 190      21.623  44.609  49.408  1.00 55.32           O  
ATOM   1449  CB  TYR A 190      19.912  44.137  51.715  1.00 53.99           C  
ATOM   1450  CG  TYR A 190      19.239  42.792  51.522  1.00 54.39           C  
ATOM   1451  CD1 TYR A 190      18.253  42.348  52.407  1.00 53.55           C  
ATOM   1452  CD2 TYR A 190      19.573  41.970  50.448  1.00 54.63           C  
ATOM   1453  CE1 TYR A 190      17.617  41.120  52.228  1.00 51.18           C  
ATOM   1454  CE2 TYR A 190      18.942  40.743  50.256  1.00 55.79           C  
ATOM   1455  CZ  TYR A 190      17.962  40.324  51.153  1.00 53.09           C  
ATOM   1456  OH  TYR A 190      17.320  39.121  50.958  1.00 51.65           O  
ATOM   1457  N   ILE A 191      19.719  44.756  48.227  1.00 51.22           N  
ATOM   1458  CA  ILE A 191      20.358  44.445  46.958  1.00 50.46           C  
ATOM   1459  C   ILE A 191      20.724  45.725  46.186  1.00 53.19           C  
ATOM   1460  O   ILE A 191      21.888  45.944  45.853  1.00 52.72           O  
ATOM   1461  CB  ILE A 191      19.440  43.561  46.109  1.00 45.71           C  
ATOM   1462  CG1 ILE A 191      19.221  42.222  46.825  1.00 44.29           C  
ATOM   1463  CG2 ILE A 191      20.038  43.361  44.745  1.00 44.21           C  
ATOM   1464  CD1 ILE A 191      18.212  41.313  46.138  1.00 44.47           C  
ATOM   1465  N   SER A 192      19.732  46.565  45.909  1.00 53.99           N  
ATOM   1466  CA  SER A 192      19.967  47.821  45.204  1.00 55.79           C  
ATOM   1467  C   SER A 192      21.095  48.588  45.883  1.00 57.99           C  
ATOM   1468  O   SER A 192      21.112  48.718  47.105  1.00 58.24           O  
ATOM   1469  CB  SER A 192      18.700  48.674  45.207  1.00 53.55           C  
ATOM   1470  OG  SER A 192      17.701  48.086  44.394  1.00 55.36           O  
ATOM   1471  N   ARG A 193      22.026  49.109  45.087  1.00 60.17           N  
ATOM   1472  CA  ARG A 193      23.172  49.825  45.634  1.00 61.93           C  
ATOM   1473  C   ARG A 193      23.257  51.322  45.369  1.00 63.88           C  
ATOM   1474  O   ARG A 193      24.346  51.899  45.425  1.00 63.47           O  
ATOM   1475  CB  ARG A 193      24.453  49.159  45.164  1.00 58.87           C  
ATOM   1476  CG  ARG A 193      24.503  47.693  45.496  1.00 57.91           C  
ATOM   1477  CD  ARG A 193      25.876  47.133  45.266  1.00 60.71           C  
ATOM   1478  NE  ARG A 193      25.979  45.741  45.688  1.00 62.84           N  
ATOM   1479  CZ  ARG A 193      27.105  45.044  45.647  1.00 60.67           C  
ATOM   1480  NH1 ARG A 193      27.123  43.786  46.048  1.00 62.49           N  
ATOM   1481  NH2 ARG A 193      28.215  45.614  45.209  1.00 61.16           N  
ATOM   1482  N   ASP A 194      22.117  51.954  45.097  1.00 65.75           N  
ATOM   1483  CA  ASP A 194      22.101  53.390  44.843  1.00 65.29           C  
ATOM   1484  C   ASP A 194      22.369  54.145  46.125  1.00 64.83           C  
ATOM   1485  O   ASP A 194      22.231  53.602  47.222  1.00 64.38           O  
ATOM   1486  CB  ASP A 194      20.757  53.834  44.277  1.00 68.16           C  
ATOM   1487  CG  ASP A 194      19.603  53.400  45.135  1.00 69.42           C  
ATOM   1488  OD1 ASP A 194      19.112  52.269  44.934  1.00 70.02           O  
ATOM   1489  OD2 ASP A 194      19.201  54.185  46.018  1.00 71.17           O  
ATOM   1490  N   SER A 195      22.751  55.407  45.979  1.00 66.01           N  
ATOM   1491  CA  SER A 195      23.053  56.251  47.125  1.00 67.85           C  
ATOM   1492  C   SER A 195      21.942  56.184  48.161  1.00 67.84           C  
ATOM   1493  O   SER A 195      22.186  55.893  49.329  1.00 69.78           O  
ATOM   1494  CB  SER A 195      23.251  57.698  46.671  1.00 67.68           C  
ATOM   1495  OG  SER A 195      23.381  58.557  47.790  1.00 73.05           O  
ATOM   1496  N   THR A 196      20.720  56.452  47.719  1.00 67.01           N  
ATOM   1497  CA  THR A 196      19.564  56.439  48.601  1.00 65.95           C  
ATOM   1498  C   THR A 196      19.453  55.152  49.412  1.00 61.89           C  
ATOM   1499  O   THR A 196      19.486  55.181  50.636  1.00 59.03           O  
ATOM   1500  CB  THR A 196      18.255  56.615  47.798  1.00 68.36           C  
ATOM   1501  OG1 THR A 196      18.350  57.790  46.985  1.00 67.87           O  
ATOM   1502  CG2 THR A 196      17.059  56.748  48.749  1.00 70.45           C  
ATOM   1503  N   THR A 197      19.319  54.028  48.716  1.00 59.63           N  
ATOM   1504  CA  THR A 197      19.180  52.735  49.373  1.00 59.43           C  
ATOM   1505  C   THR A 197      20.310  52.424  50.343  1.00 60.97           C  
ATOM   1506  O   THR A 197      20.070  51.957  51.464  1.00 62.35           O  
ATOM   1507  CB  THR A 197      19.113  51.584  48.357  1.00 58.34           C  
ATOM   1508  OG1 THR A 197      18.083  51.844  47.388  1.00 52.20           O  
ATOM   1509  CG2 THR A 197      18.814  50.276  49.080  1.00 56.23           C  
ATOM   1510  N   ARG A 198      21.542  52.687  49.920  1.00 59.84           N  
ATOM   1511  CA  ARG A 198      22.707  52.398  50.752  1.00 57.41           C  
ATOM   1512  C   ARG A 198      22.780  53.220  52.022  1.00 55.12           C  
ATOM   1513  O   ARG A 198      23.220  52.720  53.058  1.00 56.10           O  
ATOM   1514  CB  ARG A 198      23.992  52.580  49.937  1.00 61.97           C  
ATOM   1515  CG  ARG A 198      25.268  52.288  50.708  1.00 63.88           C  
ATOM   1516  CD  ARG A 198      26.458  52.140  49.775  1.00 62.46           C  
ATOM   1517  NE  ARG A 198      26.466  50.842  49.105  1.00 65.36           N  
ATOM   1518  CZ  ARG A 198      27.387  50.461  48.224  1.00 66.45           C  
ATOM   1519  NH1 ARG A 198      28.373  51.285  47.904  1.00 68.24           N  
ATOM   1520  NH2 ARG A 198      27.329  49.254  47.673  1.00 64.37           N  
ATOM   1521  N   SER A 199      22.357  54.478  51.958  1.00 56.04           N  
ATOM   1522  CA  SER A 199      22.381  55.339  53.142  1.00 57.66           C  
ATOM   1523  C   SER A 199      21.360  54.845  54.160  1.00 58.01           C  
ATOM   1524  O   SER A 199      21.626  54.825  55.368  1.00 58.38           O  
ATOM   1525  CB  SER A 199      22.081  56.799  52.766  1.00 59.06           C  
ATOM   1526  OG  SER A 199      20.891  56.919  52.009  1.00 61.14           O  
ATOM   1527  N   ASN A 200      20.193  54.439  53.673  1.00 57.66           N  
ATOM   1528  CA  ASN A 200      19.156  53.934  54.556  1.00 57.45           C  
ATOM   1529  C   ASN A 200      19.625  52.639  55.209  1.00 55.99           C  
ATOM   1530  O   ASN A 200      19.358  52.402  56.384  1.00 57.14           O  
ATOM   1531  CB  ASN A 200      17.859  53.702  53.789  1.00 57.73           C  
ATOM   1532  CG  ASN A 200      16.713  53.319  54.701  1.00 56.35           C  
ATOM   1533  OD1 ASN A 200      16.217  52.194  54.656  1.00 57.07           O  
ATOM   1534  ND2 ASN A 200      16.287  54.260  55.539  1.00 53.83           N  
ATOM   1535  N   ILE A 201      20.323  51.798  54.454  1.00 53.48           N  
ATOM   1536  CA  ILE A 201      20.840  50.556  55.027  1.00 52.54           C  
ATOM   1537  C   ILE A 201      21.851  50.913  56.108  1.00 54.63           C  
ATOM   1538  O   ILE A 201      21.770  50.428  57.235  1.00 55.05           O  
ATOM   1539  CB  ILE A 201      21.557  49.681  53.981  1.00 50.63           C  
ATOM   1540  CG1 ILE A 201      20.542  49.101  53.002  1.00 48.29           C  
ATOM   1541  CG2 ILE A 201      22.331  48.581  54.679  1.00 48.57           C  
ATOM   1542  CD1 ILE A 201      21.140  48.225  51.948  1.00 46.45           C  
ATOM   1543  N   LEU A 202      22.808  51.769  55.765  1.00 57.40           N  
ATOM   1544  CA  LEU A 202      23.827  52.168  56.729  1.00 59.34           C  
ATOM   1545  C   LEU A 202      23.183  52.752  57.983  1.00 59.46           C  
ATOM   1546  O   LEU A 202      23.672  52.555  59.100  1.00 59.18           O  
ATOM   1547  CB  LEU A 202      24.781  53.184  56.096  1.00 60.71           C  
ATOM   1548  CG  LEU A 202      25.586  52.614  54.925  1.00 61.28           C  
ATOM   1549  CD1 LEU A 202      26.383  53.719  54.274  1.00 60.17           C  
ATOM   1550  CD2 LEU A 202      26.499  51.496  55.415  1.00 59.03           C  
ATOM   1551  N   CYS A 203      22.080  53.468  57.793  1.00 58.07           N  
ATOM   1552  CA  CYS A 203      21.364  54.060  58.912  1.00 57.53           C  
ATOM   1553  C   CYS A 203      20.705  52.977  59.766  1.00 54.93           C  
ATOM   1554  O   CYS A 203      20.733  53.042  61.002  1.00 51.70           O  
ATOM   1555  CB  CYS A 203      20.298  55.027  58.405  1.00 60.84           C  
ATOM   1556  SG  CYS A 203      20.906  56.672  58.036  1.00 66.96           S  
ATOM   1557  N   MET A 204      20.105  51.992  59.099  1.00 52.04           N  
ATOM   1558  CA  MET A 204      19.445  50.904  59.797  1.00 50.82           C  
ATOM   1559  C   MET A 204      20.440  50.171  60.673  1.00 52.04           C  
ATOM   1560  O   MET A 204      20.234  50.028  61.883  1.00 54.13           O  
ATOM   1561  CB  MET A 204      18.812  49.922  58.809  1.00 52.47           C  
ATOM   1562  CG  MET A 204      17.414  50.317  58.351  1.00 53.64           C  
ATOM   1563  SD  MET A 204      16.663  49.088  57.299  1.00 52.17           S  
ATOM   1564  CE  MET A 204      15.066  49.824  57.022  1.00 53.85           C  
ATOM   1565  N   PHE A 205      21.525  49.713  60.058  1.00 51.84           N  
ATOM   1566  CA  PHE A 205      22.566  48.988  60.767  1.00 50.50           C  
ATOM   1567  C   PHE A 205      23.227  49.778  61.889  1.00 53.41           C  
ATOM   1568  O   PHE A 205      23.403  49.278  62.994  1.00 54.79           O  
ATOM   1569  CB  PHE A 205      23.630  48.542  59.773  1.00 48.60           C  
ATOM   1570  CG  PHE A 205      23.324  47.235  59.109  1.00 46.45           C  
ATOM   1571  CD1 PHE A 205      23.743  46.042  59.678  1.00 46.98           C  
ATOM   1572  CD2 PHE A 205      22.601  47.191  57.935  1.00 43.37           C  
ATOM   1573  CE1 PHE A 205      23.445  44.825  59.086  1.00 45.63           C  
ATOM   1574  CE2 PHE A 205      22.300  45.981  57.339  1.00 45.29           C  
ATOM   1575  CZ  PHE A 205      22.725  44.792  57.919  1.00 42.50           C  
ATOM   1576  N   ILE A 206      23.598  51.018  61.609  1.00 56.31           N  
ATOM   1577  CA  ILE A 206      24.266  51.836  62.612  1.00 57.31           C  
ATOM   1578  C   ILE A 206      23.315  52.425  63.655  1.00 57.08           C  
ATOM   1579  O   ILE A 206      23.521  52.243  64.854  1.00 56.51           O  
ATOM   1580  CB  ILE A 206      25.086  52.948  61.919  1.00 58.23           C  
ATOM   1581  CG1 ILE A 206      26.104  52.295  60.983  1.00 59.75           C  
ATOM   1582  CG2 ILE A 206      25.821  53.783  62.944  1.00 56.86           C  
ATOM   1583  CD1 ILE A 206      26.697  53.223  59.950  1.00 61.38           C  
ATOM   1584  N   LEU A 207      22.269  53.115  63.211  1.00 57.45           N  
ATOM   1585  CA  LEU A 207      21.327  53.710  64.157  1.00 60.66           C  
ATOM   1586  C   LEU A 207      20.375  52.697  64.788  1.00 60.52           C  
ATOM   1587  O   LEU A 207      20.165  52.693  65.997  1.00 59.47           O  
ATOM   1588  CB  LEU A 207      20.514  54.818  63.487  1.00 62.26           C  
ATOM   1589  CG  LEU A 207      21.251  56.114  63.133  1.00 62.71           C  
ATOM   1590  CD1 LEU A 207      22.019  56.613  64.353  1.00 59.34           C  
ATOM   1591  CD2 LEU A 207      22.194  55.871  61.968  1.00 61.79           C  
ATOM   1592  N   GLY A 208      19.799  51.834  63.966  1.00 62.39           N  
ATOM   1593  CA  GLY A 208      18.870  50.852  64.481  1.00 63.95           C  
ATOM   1594  C   GLY A 208      19.490  49.697  65.238  1.00 65.37           C  
ATOM   1595  O   GLY A 208      18.965  49.278  66.268  1.00 67.15           O  
ATOM   1596  N   PHE A 209      20.610  49.182  64.744  1.00 65.66           N  
ATOM   1597  CA  PHE A 209      21.266  48.041  65.369  1.00 63.95           C  
ATOM   1598  C   PHE A 209      22.448  48.380  66.285  1.00 64.54           C  
ATOM   1599  O   PHE A 209      22.344  48.246  67.508  1.00 65.28           O  
ATOM   1600  CB  PHE A 209      21.695  47.068  64.269  1.00 65.10           C  
ATOM   1601  CG  PHE A 209      22.130  45.720  64.773  1.00 67.31           C  
ATOM   1602  CD1 PHE A 209      21.544  45.156  65.904  1.00 67.50           C  
ATOM   1603  CD2 PHE A 209      23.090  44.987  64.082  1.00 66.21           C  
ATOM   1604  CE1 PHE A 209      21.911  43.880  66.333  1.00 66.88           C  
ATOM   1605  CE2 PHE A 209      23.461  43.713  64.505  1.00 64.11           C  
ATOM   1606  CZ  PHE A 209      22.869  43.160  65.632  1.00 65.44           C  
ATOM   1607  N   PHE A 210      23.567  48.816  65.711  1.00 62.53           N  
ATOM   1608  CA  PHE A 210      24.745  49.146  66.513  1.00 59.17           C  
ATOM   1609  C   PHE A 210      24.439  50.101  67.661  1.00 56.57           C  
ATOM   1610  O   PHE A 210      25.000  49.983  68.747  1.00 56.90           O  
ATOM   1611  CB  PHE A 210      25.842  49.757  65.633  1.00 59.41           C  
ATOM   1612  CG  PHE A 210      26.278  48.867  64.501  1.00 61.92           C  
ATOM   1613  CD1 PHE A 210      26.454  47.500  64.703  1.00 61.01           C  
ATOM   1614  CD2 PHE A 210      26.540  49.396  63.241  1.00 62.26           C  
ATOM   1615  CE1 PHE A 210      26.884  46.675  63.669  1.00 61.53           C  
ATOM   1616  CE2 PHE A 210      26.973  48.578  62.201  1.00 61.87           C  
ATOM   1617  CZ  PHE A 210      27.145  47.214  62.418  1.00 62.21           C  
ATOM   1618  N   GLY A 211      23.545  51.048  67.415  1.00 55.17           N  
ATOM   1619  CA  GLY A 211      23.193  52.010  68.438  1.00 52.76           C  
ATOM   1620  C   GLY A 211      22.889  51.393  69.786  1.00 52.29           C  
ATOM   1621  O   GLY A 211      23.713  51.475  70.697  1.00 51.84           O  
ATOM   1622  N   PRO A 212      21.711  50.768  69.947  1.00 53.44           N  
ATOM   1623  CA  PRO A 212      21.301  50.133  71.203  1.00 53.77           C  
ATOM   1624  C   PRO A 212      22.330  49.131  71.714  1.00 53.76           C  
ATOM   1625  O   PRO A 212      22.423  48.866  72.911  1.00 52.21           O  
ATOM   1626  CB  PRO A 212      19.965  49.482  70.843  1.00 56.06           C  
ATOM   1627  CG  PRO A 212      20.097  49.222  69.360  1.00 56.09           C  
ATOM   1628  CD  PRO A 212      20.733  50.497  68.881  1.00 53.76           C  
ATOM   1629  N   ILE A 213      23.111  48.576  70.801  1.00 55.03           N  
ATOM   1630  CA  ILE A 213      24.143  47.636  71.198  1.00 56.73           C  
ATOM   1631  C   ILE A 213      25.147  48.349  72.100  1.00 58.05           C  
ATOM   1632  O   ILE A 213      25.524  47.837  73.153  1.00 56.26           O  
ATOM   1633  CB  ILE A 213      24.873  47.062  69.979  1.00 55.79           C  
ATOM   1634  CG1 ILE A 213      23.930  46.121  69.218  1.00 56.31           C  
ATOM   1635  CG2 ILE A 213      26.141  46.368  70.423  1.00 55.32           C  
ATOM   1636  CD1 ILE A 213      24.584  45.313  68.114  1.00 57.79           C  
ATOM   1637  N   LEU A 214      25.571  49.539  71.687  1.00 59.91           N  
ATOM   1638  CA  LEU A 214      26.523  50.315  72.471  1.00 61.71           C  
ATOM   1639  C   LEU A 214      25.967  50.568  73.866  1.00 62.36           C  
ATOM   1640  O   LEU A 214      26.670  50.413  74.868  1.00 62.13           O  
ATOM   1641  CB  LEU A 214      26.827  51.639  71.772  1.00 63.98           C  
ATOM   1642  CG  LEU A 214      27.601  51.517  70.455  1.00 67.73           C  
ATOM   1643  CD1 LEU A 214      27.667  52.874  69.763  1.00 69.53           C  
ATOM   1644  CD2 LEU A 214      29.001  50.988  70.732  1.00 68.18           C  
ATOM   1645  N   ILE A 215      24.701  50.961  73.929  1.00 62.60           N  
ATOM   1646  CA  ILE A 215      24.055  51.206  75.212  1.00 60.71           C  
ATOM   1647  C   ILE A 215      24.131  49.917  76.025  1.00 60.09           C  
ATOM   1648  O   ILE A 215      24.502  49.930  77.195  1.00 60.94           O  
ATOM   1649  CB  ILE A 215      22.583  51.606  75.021  1.00 61.70           C  
ATOM   1650  CG1 ILE A 215      22.502  52.931  74.269  1.00 63.31           C  
ATOM   1651  CG2 ILE A 215      21.903  51.741  76.360  1.00 61.28           C  
ATOM   1652  CD1 ILE A 215      21.085  53.389  73.990  1.00 65.32           C  
ATOM   1653  N   ILE A 216      23.782  48.802  75.395  1.00 59.22           N  
ATOM   1654  CA  ILE A 216      23.831  47.512  76.069  1.00 60.42           C  
ATOM   1655  C   ILE A 216      25.219  47.272  76.670  1.00 61.54           C  
ATOM   1656  O   ILE A 216      25.368  47.253  77.889  1.00 58.27           O  
ATOM   1657  CB  ILE A 216      23.478  46.363  75.089  1.00 59.25           C  
ATOM   1658  CG1 ILE A 216      21.986  46.415  74.753  1.00 58.17           C  
ATOM   1659  CG2 ILE A 216      23.836  45.024  75.698  1.00 55.69           C  
ATOM   1660  CD1 ILE A 216      21.604  45.627  73.526  1.00 59.17           C  
ATOM   1661  N   PHE A 217      26.229  47.108  75.816  1.00 65.78           N  
ATOM   1662  CA  PHE A 217      27.603  46.869  76.268  1.00 69.89           C  
ATOM   1663  C   PHE A 217      28.081  47.876  77.311  1.00 69.08           C  
ATOM   1664  O   PHE A 217      28.713  47.496  78.305  1.00 66.65           O  
ATOM   1665  CB  PHE A 217      28.576  46.861  75.071  1.00 72.25           C  
ATOM   1666  CG  PHE A 217      30.039  46.910  75.468  1.00 75.66           C  
ATOM   1667  CD1 PHE A 217      30.680  48.128  75.685  1.00 75.30           C  
ATOM   1668  CD2 PHE A 217      30.770  45.737  75.635  1.00 75.62           C  
ATOM   1669  CE1 PHE A 217      32.024  48.181  76.059  1.00 72.60           C  
ATOM   1670  CE2 PHE A 217      32.118  45.784  76.010  1.00 76.45           C  
ATOM   1671  CZ  PHE A 217      32.742  47.011  76.221  1.00 73.24           C  
ATOM   1672  N   PHE A 218      27.788  49.153  77.081  1.00 68.83           N  
ATOM   1673  CA  PHE A 218      28.186  50.211  78.005  1.00 69.89           C  
ATOM   1674  C   PHE A 218      27.553  50.019  79.373  1.00 69.74           C  
ATOM   1675  O   PHE A 218      28.118  50.423  80.379  1.00 69.93           O  
ATOM   1676  CB  PHE A 218      27.793  51.582  77.443  1.00 72.27           C  
ATOM   1677  CG  PHE A 218      27.990  52.722  78.411  1.00 72.73           C  
ATOM   1678  CD1 PHE A 218      27.043  52.991  79.394  1.00 72.39           C  
ATOM   1679  CD2 PHE A 218      29.124  53.525  78.338  1.00 72.52           C  
ATOM   1680  CE1 PHE A 218      27.223  54.042  80.286  1.00 72.63           C  
ATOM   1681  CE2 PHE A 218      29.313  54.577  79.225  1.00 71.71           C  
ATOM   1682  CZ  PHE A 218      28.362  54.837  80.200  1.00 73.39           C  
ATOM   1683  N   CYS A 219      26.373  49.407  79.399  1.00 71.65           N  
ATOM   1684  CA  CYS A 219      25.661  49.162  80.650  1.00 72.05           C  
ATOM   1685  C   CYS A 219      26.103  47.866  81.315  1.00 72.40           C  
ATOM   1686  O   CYS A 219      26.322  47.826  82.523  1.00 71.90           O  
ATOM   1687  CB  CYS A 219      24.149  49.119  80.409  1.00 72.32           C  
ATOM   1688  SG  CYS A 219      23.373  50.737  80.191  1.00 70.07           S  
ATOM   1689  N   TYR A 220      26.226  46.804  80.533  1.00 73.80           N  
ATOM   1690  CA  TYR A 220      26.634  45.541  81.109  1.00 78.15           C  
ATOM   1691  C   TYR A 220      28.111  45.530  81.423  1.00 78.51           C  
ATOM   1692  O   TYR A 220      28.515  45.056  82.483  1.00 78.19           O  
ATOM   1693  CB  TYR A 220      26.254  44.382  80.186  1.00 81.98           C  
ATOM   1694  CG  TYR A 220      24.755  44.196  80.140  1.00 87.40           C  
ATOM   1695  CD1 TYR A 220      24.035  43.934  81.305  1.00 87.81           C  
ATOM   1696  CD2 TYR A 220      24.047  44.362  78.954  1.00 90.10           C  
ATOM   1697  CE1 TYR A 220      22.653  43.849  81.293  1.00 90.18           C  
ATOM   1698  CE2 TYR A 220      22.661  44.280  78.930  1.00 92.83           C  
ATOM   1699  CZ  TYR A 220      21.969  44.026  80.104  1.00 93.35           C  
ATOM   1700  OH  TYR A 220      20.591  43.974  80.092  1.00 96.41           O  
ATOM   1701  N   PHE A 221      28.926  46.064  80.521  1.00 80.13           N  
ATOM   1702  CA  PHE A 221      30.355  46.095  80.793  1.00 83.50           C  
ATOM   1703  C   PHE A 221      30.572  46.973  82.019  1.00 83.18           C  
ATOM   1704  O   PHE A 221      31.573  46.838  82.725  1.00 83.47           O  
ATOM   1705  CB  PHE A 221      31.132  46.671  79.612  1.00 86.55           C  
ATOM   1706  CG  PHE A 221      32.620  46.662  79.816  1.00 89.08           C  
ATOM   1707  CD1 PHE A 221      33.311  45.457  79.908  1.00 89.68           C  
ATOM   1708  CD2 PHE A 221      33.331  47.852  79.936  1.00 89.72           C  
ATOM   1709  CE1 PHE A 221      34.686  45.437  80.115  1.00 91.30           C  
ATOM   1710  CE2 PHE A 221      34.706  47.843  80.143  1.00 90.52           C  
ATOM   1711  CZ  PHE A 221      35.386  46.632  80.232  1.00 91.23           C  
ATOM   1712  N   ASN A 222      29.612  47.863  82.262  1.00 81.30           N  
ATOM   1713  CA  ASN A 222      29.663  48.793  83.387  1.00 78.29           C  
ATOM   1714  C   ASN A 222      29.182  48.110  84.661  1.00 77.12           C  
ATOM   1715  O   ASN A 222      29.464  48.561  85.767  1.00 76.75           O  
ATOM   1716  CB  ASN A 222      28.787  50.010  83.093  1.00 75.94           C  
ATOM   1717  CG  ASN A 222      29.231  51.246  83.843  1.00 75.00           C  
ATOM   1718  OD1 ASN A 222      29.382  51.229  85.064  1.00 73.20           O  
ATOM   1719  ND2 ASN A 222      29.437  52.334  83.110  1.00 72.13           N  
ATOM   1720  N   ILE A 223      28.441  47.024  84.496  1.00 79.05           N  
ATOM   1721  CA  ILE A 223      27.928  46.269  85.630  1.00 79.51           C  
ATOM   1722  C   ILE A 223      28.996  45.265  86.037  1.00 81.00           C  
ATOM   1723  O   ILE A 223      29.085  44.863  87.197  1.00 80.96           O  
ATOM   1724  CB  ILE A 223      26.605  45.544  85.250  1.00 77.90           C  
ATOM   1725  CG1 ILE A 223      25.476  46.577  85.153  1.00 77.14           C  
ATOM   1726  CG2 ILE A 223      26.269  44.457  86.262  1.00 73.42           C  
ATOM   1727  CD1 ILE A 223      24.148  46.010  84.690  1.00 77.70           C  
ATOM   1728  N   VAL A 224      29.817  44.874  85.069  1.00 83.74           N  
ATOM   1729  CA  VAL A 224      30.896  43.929  85.309  1.00 87.02           C  
ATOM   1730  C   VAL A 224      32.034  44.669  85.991  1.00 89.61           C  
ATOM   1731  O   VAL A 224      32.598  44.189  86.974  1.00 89.69           O  
ATOM   1732  CB  VAL A 224      31.415  43.333  83.990  1.00 86.64           C  
ATOM   1733  CG1 VAL A 224      32.595  42.413  84.265  1.00 86.42           C  
ATOM   1734  CG2 VAL A 224      30.296  42.582  83.285  1.00 85.17           C  
ATOM   1735  N   MET A 225      32.367  45.841  85.455  1.00 92.88           N  
ATOM   1736  CA  MET A 225      33.432  46.670  86.010  1.00 95.45           C  
ATOM   1737  C   MET A 225      32.875  47.412  87.216  1.00 96.00           C  
ATOM   1738  O   MET A 225      33.132  48.599  87.398  1.00 96.73           O  
ATOM   1739  CB  MET A 225      33.921  47.688  84.975  1.00 97.56           C  
ATOM   1740  CG  MET A 225      34.538  47.097  83.709  1.00100.41           C  
ATOM   1741  SD  MET A 225      36.167  46.353  83.938  1.00102.65           S  
ATOM   1742  CE  MET A 225      35.776  44.603  83.764  1.00101.87           C  
ATOM   1743  N   SER A 226      32.099  46.700  88.025  1.00 97.60           N  
ATOM   1744  CA  SER A 226      31.491  47.273  89.217  1.00 99.87           C  
ATOM   1745  C   SER A 226      31.113  46.153  90.170  1.00100.65           C  
ATOM   1746  O   SER A 226      30.614  46.398  91.267  1.00101.06           O  
ATOM   1747  CB  SER A 226      30.244  48.080  88.847  1.00100.93           C  
ATOM   1748  OG  SER A 226      29.294  47.273  88.174  1.00103.39           O  
ATOM   1749  N   VAL A 227      31.348  44.920  89.737  1.00102.38           N  
ATOM   1750  CA  VAL A 227      31.041  43.763  90.565  1.00105.56           C  
ATOM   1751  C   VAL A 227      31.974  43.809  91.766  1.00107.97           C  
ATOM   1752  O   VAL A 227      31.604  43.415  92.870  1.00107.91           O  
ATOM   1753  CB  VAL A 227      31.272  42.437  89.806  1.00104.82           C  
ATOM   1754  CG1 VAL A 227      30.755  41.277  90.637  1.00103.88           C  
ATOM   1755  CG2 VAL A 227      30.579  42.474  88.449  1.00104.16           C  
ATOM   1756  N   SER A 228      33.188  44.299  91.534  1.00111.33           N  
ATOM   1757  CA  SER A 228      34.185  44.416  92.587  1.00114.56           C  
ATOM   1758  C   SER A 228      33.987  45.722  93.345  1.00115.90           C  
ATOM   1759  O   SER A 228      34.213  45.785  94.552  1.00116.15           O  
ATOM   1760  CB  SER A 228      35.594  44.360  91.995  1.00115.93           C  
ATOM   1761  OG  SER A 228      35.864  43.073  91.463  1.00119.09           O  
ATOM   1762  N   ASN A 229      33.570  46.765  92.631  1.00117.63           N  
ATOM   1763  CA  ASN A 229      33.313  48.053  93.263  1.00119.50           C  
ATOM   1764  C   ASN A 229      32.284  47.753  94.346  1.00121.88           C  
ATOM   1765  O   ASN A 229      32.300  48.334  95.431  1.00122.81           O  
ATOM   1766  CB  ASN A 229      32.718  49.047  92.257  1.00118.01           C  
ATOM   1767  CG  ASN A 229      33.637  49.323  91.078  1.00117.34           C  
ATOM   1768  OD1 ASN A 229      33.306  50.113  90.191  1.00113.92           O  
ATOM   1769  ND2 ASN A 229      34.796  48.674  91.062  1.00117.76           N  
ATOM   1770  N   HIS A 230      31.395  46.820  94.020  1.00123.73           N  
ATOM   1771  CA  HIS A 230      30.328  46.378  94.908  1.00125.11           C  
ATOM   1772  C   HIS A 230      30.849  45.332  95.890  1.00125.59           C  
ATOM   1773  O   HIS A 230      30.427  45.288  97.044  1.00125.51           O  
ATOM   1774  CB  HIS A 230      29.180  45.805  94.063  1.00125.91           C  
ATOM   1775  CG  HIS A 230      28.261  44.888  94.809  1.00126.08           C  
ATOM   1776  ND1 HIS A 230      27.593  45.266  95.953  1.00126.00           N  
ATOM   1777  CD2 HIS A 230      27.887  43.611  94.559  1.00125.96           C  
ATOM   1778  CE1 HIS A 230      26.847  44.261  96.376  1.00125.93           C  
ATOM   1779  NE2 HIS A 230      27.008  43.244  95.548  1.00125.86           N  
ATOM   1780  N   GLU A 231      31.773  44.498  95.427  1.00126.76           N  
ATOM   1781  CA  GLU A 231      32.348  43.454  96.264  1.00128.71           C  
ATOM   1782  C   GLU A 231      32.911  44.059  97.546  1.00128.74           C  
ATOM   1783  O   GLU A 231      32.626  43.589  98.649  1.00128.63           O  
ATOM   1784  CB  GLU A 231      33.462  42.722  95.508  1.00130.40           C  
ATOM   1785  CG  GLU A 231      33.970  41.462  96.203  1.00132.05           C  
ATOM   1786  CD  GLU A 231      35.192  40.864  95.523  1.00133.11           C  
ATOM   1787  OE1 GLU A 231      35.144  40.643  94.293  1.00133.71           O  
ATOM   1788  OE2 GLU A 231      36.199  40.611  96.219  1.00132.98           O  
ATOM   1789  N   LYS A 232      33.718  45.103  97.394  1.00128.60           N  
ATOM   1790  CA  LYS A 232      34.312  45.778  98.538  1.00128.68           C  
ATOM   1791  C   LYS A 232      33.216  46.457  99.348  1.00128.82           C  
ATOM   1792  O   LYS A 232      33.041  46.181 100.534  1.00129.42           O  
ATOM   1793  CB  LYS A 232      35.326  46.830  98.070  1.00128.55           C  
ATOM   1794  CG  LYS A 232      36.636  46.273  97.523  1.00127.29           C  
ATOM   1795  CD  LYS A 232      37.537  45.762  98.640  1.00126.19           C  
ATOM   1796  CE  LYS A 232      38.907  45.363  98.108  1.00125.23           C  
ATOM   1797  NZ  LYS A 232      39.827  44.921  99.192  1.00124.22           N  
ATOM   1798  N   GLU A 233      32.476  47.341  98.687  1.00128.60           N  
ATOM   1799  CA  GLU A 233      31.391  48.090  99.311  1.00127.46           C  
ATOM   1800  C   GLU A 233      30.479  47.240 100.187  1.00127.68           C  
ATOM   1801  O   GLU A 233      30.060  47.674 101.260  1.00126.59           O  
ATOM   1802  CB  GLU A 233      30.557  48.782  98.233  1.00126.39           C  
ATOM   1803  CG  GLU A 233      29.343  49.514  98.768  1.00125.03           C  
ATOM   1804  CD  GLU A 233      28.523  50.149  97.668  1.00124.23           C  
ATOM   1805  OE1 GLU A 233      28.123  49.423  96.734  1.00123.99           O  
ATOM   1806  OE2 GLU A 233      28.276  51.369  97.741  1.00123.87           O  
ATOM   1807  N   MET A 234      30.166  46.034  99.726  1.00129.16           N  
ATOM   1808  CA  MET A 234      29.299  45.131 100.473  1.00130.46           C  
ATOM   1809  C   MET A 234      29.891  44.883 101.856  1.00130.70           C  
ATOM   1810  O   MET A 234      29.176  44.877 102.859  1.00129.97           O  
ATOM   1811  CB  MET A 234      29.159  43.799  99.727  1.00131.72           C  
ATOM   1812  CG  MET A 234      27.724  43.294  99.577  1.00133.98           C  
ATOM   1813  SD  MET A 234      26.859  42.990 101.137  1.00136.30           S  
ATOM   1814  CE  MET A 234      25.715  44.370 101.169  1.00135.54           C  
ATOM   1815  N   ALA A 235      31.206  44.693 101.898  1.00131.45           N  
ATOM   1816  CA  ALA A 235      31.912  44.438 103.147  1.00132.07           C  
ATOM   1817  C   ALA A 235      31.958  45.657 104.064  1.00132.49           C  
ATOM   1818  O   ALA A 235      31.620  45.566 105.242  1.00132.23           O  
ATOM   1819  CB  ALA A 235      33.329  43.961 102.847  1.00132.16           C  
ATOM   1820  N   ALA A 236      32.376  46.795 103.518  1.00133.38           N  
ATOM   1821  CA  ALA A 236      32.482  48.030 104.292  1.00133.77           C  
ATOM   1822  C   ALA A 236      31.221  48.331 105.093  1.00134.18           C  
ATOM   1823  O   ALA A 236      31.299  48.773 106.240  1.00133.78           O  
ATOM   1824  CB  ALA A 236      32.801  49.198 103.365  1.00134.27           C  
ATOM   1825  N   MET A 237      30.063  48.097 104.485  1.00135.18           N  
ATOM   1826  CA  MET A 237      28.792  48.341 105.155  1.00136.00           C  
ATOM   1827  C   MET A 237      28.420  47.128 105.997  1.00136.19           C  
ATOM   1828  O   MET A 237      27.704  47.242 106.992  1.00136.45           O  
ATOM   1829  CB  MET A 237      27.689  48.615 104.123  1.00136.83           C  
ATOM   1830  CG  MET A 237      27.512  47.514 103.082  1.00138.55           C  
ATOM   1831  SD  MET A 237      26.065  47.749 102.007  1.00139.13           S  
ATOM   1832  CE  MET A 237      26.724  48.909 100.793  1.00139.32           C  
ATOM   1833  N   ALA A 238      28.922  45.968 105.589  1.00136.20           N  
ATOM   1834  CA  ALA A 238      28.651  44.719 106.290  1.00136.85           C  
ATOM   1835  C   ALA A 238      29.137  44.768 107.735  1.00137.64           C  
ATOM   1836  O   ALA A 238      28.366  44.527 108.665  1.00137.42           O  
ATOM   1837  CB  ALA A 238      29.316  43.561 105.555  1.00136.48           C  
ATOM   1838  N   LYS A 239      30.417  45.077 107.919  1.00138.63           N  
ATOM   1839  CA  LYS A 239      30.990  45.151 109.257  1.00139.02           C  
ATOM   1840  C   LYS A 239      30.658  46.500 109.883  1.00138.98           C  
ATOM   1841  O   LYS A 239      31.079  46.798 111.000  1.00139.26           O  
ATOM   1842  CB  LYS A 239      32.510  44.965 109.204  1.00139.54           C  
ATOM   1843  CG  LYS A 239      33.282  46.170 108.686  1.00139.99           C  
ATOM   1844  CD  LYS A 239      34.784  45.932 108.754  1.00139.48           C  
ATOM   1845  CE  LYS A 239      35.563  47.211 108.484  1.00139.04           C  
ATOM   1846  NZ  LYS A 239      35.235  47.803 107.157  1.00138.88           N  
ATOM   1847  N   ARG A 240      29.904  47.313 109.152  1.00138.53           N  
ATOM   1848  CA  ARG A 240      29.503  48.626 109.637  1.00138.43           C  
ATOM   1849  C   ARG A 240      28.388  48.410 110.655  1.00137.86           C  
ATOM   1850  O   ARG A 240      27.292  48.958 110.525  1.00137.85           O  
ATOM   1851  CB  ARG A 240      29.001  49.481 108.467  1.00138.93           C  
ATOM   1852  CG  ARG A 240      28.927  50.978 108.743  1.00139.71           C  
ATOM   1853  CD  ARG A 240      30.302  51.569 109.019  1.00140.12           C  
ATOM   1854  NE  ARG A 240      30.785  51.234 110.354  1.00140.70           N  
ATOM   1855  CZ  ARG A 240      32.009  51.504 110.796  1.00141.17           C  
ATOM   1856  NH1 ARG A 240      32.359  51.165 112.029  1.00141.30           N  
ATOM   1857  NH2 ARG A 240      32.885  52.105 110.002  1.00141.28           N  
ATOM   1858  N   LEU A 241      28.684  47.598 111.668  1.00136.86           N  
ATOM   1859  CA  LEU A 241      27.730  47.259 112.722  1.00134.87           C  
ATOM   1860  C   LEU A 241      26.372  46.865 112.152  1.00133.63           C  
ATOM   1861  O   LEU A 241      25.354  46.934 112.842  1.00134.25           O  
ATOM   1862  CB  LEU A 241      27.560  48.424 113.706  1.00133.62           C  
ATOM   1863  CG  LEU A 241      28.687  48.664 114.719  1.00132.05           C  
ATOM   1864  CD1 LEU A 241      29.913  49.219 114.012  1.00131.52           C  
ATOM   1865  CD2 LEU A 241      28.208  49.635 115.787  1.00131.55           C  
ATOM   1866  N   ASN A 242      26.366  46.444 110.890  1.00131.04           N  
ATOM   1867  CA  ASN A 242      25.134  46.036 110.223  1.00127.74           C  
ATOM   1868  C   ASN A 242      24.774  44.619 110.659  1.00125.49           C  
ATOM   1869  O   ASN A 242      25.449  43.656 110.297  1.00125.18           O  
ATOM   1870  CB  ASN A 242      25.316  46.091 108.705  1.00128.18           C  
ATOM   1871  CG  ASN A 242      23.996  46.103 107.959  1.00128.33           C  
ATOM   1872  OD1 ASN A 242      23.965  46.159 106.731  1.00128.26           O  
ATOM   1873  ND2 ASN A 242      22.897  46.053 108.702  1.00128.95           N  
ATOM   1874  N   ALA A 243      23.702  44.507 111.436  1.00122.95           N  
ATOM   1875  CA  ALA A 243      23.235  43.228 111.960  1.00120.88           C  
ATOM   1876  C   ALA A 243      22.857  42.198 110.897  1.00119.10           C  
ATOM   1877  O   ALA A 243      23.161  42.359 109.718  1.00118.72           O  
ATOM   1878  CB  ALA A 243      22.053  43.461 112.892  1.00121.07           C  
ATOM   1879  N   LYS A 244      22.191  41.136 111.342  1.00117.11           N  
ATOM   1880  CA  LYS A 244      21.746  40.065 110.459  1.00115.07           C  
ATOM   1881  C   LYS A 244      20.857  40.653 109.363  1.00114.73           C  
ATOM   1882  O   LYS A 244      20.552  39.995 108.367  1.00113.72           O  
ATOM   1883  CB  LYS A 244      20.968  39.015 111.268  1.00114.44           C  
ATOM   1884  CG  LYS A 244      21.769  38.348 112.399  1.00111.52           C  
ATOM   1885  CD  LYS A 244      20.921  37.314 113.155  1.00108.86           C  
ATOM   1886  CE  LYS A 244      21.735  36.506 114.173  1.00107.41           C  
ATOM   1887  NZ  LYS A 244      22.250  37.309 115.324  1.00105.47           N  
ATOM   1888  N   GLU A 245      20.452  41.904 109.566  1.00114.89           N  
ATOM   1889  CA  GLU A 245      19.612  42.641 108.625  1.00114.00           C  
ATOM   1890  C   GLU A 245      20.393  42.936 107.350  1.00112.13           C  
ATOM   1891  O   GLU A 245      19.881  43.553 106.415  1.00112.11           O  
ATOM   1892  CB  GLU A 245      19.144  43.946 109.273  1.00115.60           C  
ATOM   1893  CG  GLU A 245      20.238  44.649 110.069  1.00119.43           C  
ATOM   1894  CD  GLU A 245      19.706  45.732 110.995  1.00121.31           C  
ATOM   1895  OE1 GLU A 245      19.246  46.780 110.490  1.00122.04           O  
ATOM   1896  OE2 GLU A 245      19.747  45.530 112.231  1.00120.76           O  
ATOM   1897  N   LEU A 246      21.644  42.492 107.331  1.00109.76           N  
ATOM   1898  CA  LEU A 246      22.515  42.674 106.180  1.00107.12           C  
ATOM   1899  C   LEU A 246      22.120  41.660 105.117  1.00104.78           C  
ATOM   1900  O   LEU A 246      22.271  41.904 103.922  1.00105.06           O  
ATOM   1901  CB  LEU A 246      23.968  42.456 106.595  1.00108.16           C  
ATOM   1902  CG  LEU A 246      25.022  42.399 105.494  1.00108.23           C  
ATOM   1903  CD1 LEU A 246      25.095  43.729 104.770  1.00107.61           C  
ATOM   1904  CD2 LEU A 246      26.362  42.050 106.118  1.00110.16           C  
ATOM   1905  N   ARG A 247      21.614  40.518 105.569  1.00102.13           N  
ATOM   1906  CA  ARG A 247      21.180  39.453 104.674  1.00100.29           C  
ATOM   1907  C   ARG A 247      20.140  39.999 103.708  1.00 99.11           C  
ATOM   1908  O   ARG A 247      20.173  39.713 102.511  1.00 99.03           O  
ATOM   1909  CB  ARG A 247      20.574  38.311 105.483  1.00101.83           C  
ATOM   1910  CG  ARG A 247      21.547  37.611 106.420  1.00104.38           C  
ATOM   1911  CD  ARG A 247      20.783  36.722 107.381  1.00106.20           C  
ATOM   1912  NE  ARG A 247      19.814  35.888 106.673  1.00108.05           N  
ATOM   1913  CZ  ARG A 247      18.768  35.307 107.250  1.00108.31           C  
ATOM   1914  NH1 ARG A 247      17.938  34.566 106.528  1.00107.96           N  
ATOM   1915  NH2 ARG A 247      18.547  35.475 108.547  1.00108.52           N  
ATOM   1916  N   LYS A 248      19.208  40.782 104.242  1.00 96.70           N  
ATOM   1917  CA  LYS A 248      18.165  41.391 103.426  1.00 94.70           C  
ATOM   1918  C   LYS A 248      18.817  42.012 102.196  1.00 93.12           C  
ATOM   1919  O   LYS A 248      18.608  41.563 101.067  1.00 92.15           O  
ATOM   1920  CB  LYS A 248      17.433  42.468 104.231  1.00 95.23           C  
ATOM   1921  CG  LYS A 248      16.447  43.322 103.432  1.00 95.69           C  
ATOM   1922  CD  LYS A 248      15.917  44.474 104.285  1.00 95.55           C  
ATOM   1923  CE  LYS A 248      15.060  45.449 103.483  1.00 95.45           C  
ATOM   1924  NZ  LYS A 248      13.743  44.884 103.090  1.00 94.94           N  
ATOM   1925  N   ALA A 249      19.624  43.040 102.429  1.00 91.56           N  
ATOM   1926  CA  ALA A 249      20.316  43.743 101.358  1.00 90.41           C  
ATOM   1927  C   ALA A 249      20.978  42.784 100.381  1.00 89.91           C  
ATOM   1928  O   ALA A 249      20.914  42.986  99.169  1.00 90.22           O  
ATOM   1929  CB  ALA A 249      21.353  44.687 101.941  1.00 89.81           C  
ATOM   1930  N   GLN A 250      21.610  41.738 100.901  1.00 89.99           N  
ATOM   1931  CA  GLN A 250      22.289  40.776 100.044  1.00 90.24           C  
ATOM   1932  C   GLN A 250      21.304  40.073  99.119  1.00 89.35           C  
ATOM   1933  O   GLN A 250      21.561  39.934  97.921  1.00 91.37           O  
ATOM   1934  CB  GLN A 250      23.042  39.741 100.882  1.00 90.95           C  
ATOM   1935  CG  GLN A 250      24.119  38.986 100.112  1.00 92.66           C  
ATOM   1936  CD  GLN A 250      25.328  39.852  99.779  1.00 93.80           C  
ATOM   1937  OE1 GLN A 250      25.199  40.914  99.161  1.00 93.59           O  
ATOM   1938  NE2 GLN A 250      26.510  39.400 100.187  1.00 93.81           N  
ATOM   1939  N   ALA A 251      20.175  39.631  99.665  1.00 86.93           N  
ATOM   1940  CA  ALA A 251      19.163  38.946  98.863  1.00 84.41           C  
ATOM   1941  C   ALA A 251      18.720  39.841  97.707  1.00 83.62           C  
ATOM   1942  O   ALA A 251      18.584  39.393  96.570  1.00 82.83           O  
ATOM   1943  CB  ALA A 251      17.963  38.588  99.727  1.00 82.61           C  
ATOM   1944  N   GLY A 252      18.500  41.112  98.013  1.00 83.04           N  
ATOM   1945  CA  GLY A 252      18.074  42.045  96.996  1.00 82.04           C  
ATOM   1946  C   GLY A 252      19.032  42.071  95.828  1.00 82.06           C  
ATOM   1947  O   GLY A 252      18.608  42.021  94.675  1.00 84.28           O  
ATOM   1948  N   ALA A 253      20.325  42.150  96.122  1.00 80.53           N  
ATOM   1949  CA  ALA A 253      21.340  42.185  95.079  1.00 78.69           C  
ATOM   1950  C   ALA A 253      21.309  40.906  94.244  1.00 78.20           C  
ATOM   1951  O   ALA A 253      21.489  40.950  93.029  1.00 78.27           O  
ATOM   1952  CB  ALA A 253      22.714  42.378  95.703  1.00 78.35           C  
ATOM   1953  N   ASN A 254      21.084  39.768  94.897  1.00 77.06           N  
ATOM   1954  CA  ASN A 254      21.011  38.490  94.196  1.00 76.24           C  
ATOM   1955  C   ASN A 254      19.832  38.530  93.235  1.00 75.41           C  
ATOM   1956  O   ASN A 254      19.957  38.209  92.051  1.00 74.94           O  
ATOM   1957  CB  ASN A 254      20.798  37.337  95.180  1.00 78.28           C  
ATOM   1958  CG  ASN A 254      22.062  36.947  95.918  1.00 78.70           C  
ATOM   1959  OD1 ASN A 254      22.579  37.701  96.732  1.00 79.59           O  
ATOM   1960  ND2 ASN A 254      22.569  35.750  95.627  1.00 79.88           N  
ATOM   1961  N   ALA A 255      18.682  38.924  93.773  1.00 73.55           N  
ATOM   1962  CA  ALA A 255      17.450  39.022  93.008  1.00 71.61           C  
ATOM   1963  C   ALA A 255      17.645  39.906  91.779  1.00 70.87           C  
ATOM   1964  O   ALA A 255      17.287  39.522  90.670  1.00 71.68           O  
ATOM   1965  CB  ALA A 255      16.342  39.576  93.888  1.00 71.23           C  
ATOM   1966  N   GLU A 256      18.216  41.086  91.979  1.00 70.08           N  
ATOM   1967  CA  GLU A 256      18.455  42.004  90.875  1.00 71.32           C  
ATOM   1968  C   GLU A 256      19.461  41.410  89.890  1.00 70.62           C  
ATOM   1969  O   GLU A 256      19.271  41.471  88.671  1.00 67.77           O  
ATOM   1970  CB  GLU A 256      18.984  43.337  91.408  1.00 72.64           C  
ATOM   1971  CG  GLU A 256      18.040  44.028  92.377  1.00 77.05           C  
ATOM   1972  CD  GLU A 256      16.739  44.461  91.724  1.00 79.23           C  
ATOM   1973  OE1 GLU A 256      15.808  44.838  92.463  1.00 80.03           O  
ATOM   1974  OE2 GLU A 256      16.650  44.433  90.477  1.00 80.11           O  
ATOM   1975  N   MET A 257      20.530  40.832  90.431  1.00 70.45           N  
ATOM   1976  CA  MET A 257      21.572  40.231  89.616  1.00 69.96           C  
ATOM   1977  C   MET A 257      20.970  39.190  88.690  1.00 70.19           C  
ATOM   1978  O   MET A 257      21.293  39.139  87.504  1.00 70.85           O  
ATOM   1979  CB  MET A 257      22.632  39.576  90.504  1.00 69.59           C  
ATOM   1980  CG  MET A 257      23.835  39.003  89.749  1.00 69.50           C  
ATOM   1981  SD  MET A 257      24.793  40.245  88.834  1.00 70.56           S  
ATOM   1982  CE  MET A 257      24.760  39.569  87.201  1.00 66.57           C  
ATOM   1983  N   ARG A 258      20.085  38.361  89.232  1.00 69.47           N  
ATOM   1984  CA  ARG A 258      19.451  37.321  88.428  1.00 68.42           C  
ATOM   1985  C   ARG A 258      18.712  37.911  87.228  1.00 66.09           C  
ATOM   1986  O   ARG A 258      18.804  37.384  86.117  1.00 64.68           O  
ATOM   1987  CB  ARG A 258      18.473  36.496  89.266  1.00 68.56           C  
ATOM   1988  CG  ARG A 258      18.016  35.251  88.530  1.00 71.28           C  
ATOM   1989  CD  ARG A 258      17.013  34.434  89.316  1.00 76.47           C  
ATOM   1990  NE  ARG A 258      16.684  33.194  88.620  1.00 77.64           N  
ATOM   1991  CZ  ARG A 258      17.327  32.043  88.790  1.00 77.43           C  
ATOM   1992  NH1 ARG A 258      16.957  30.970  88.101  1.00 76.69           N  
ATOM   1993  NH2 ARG A 258      18.322  31.955  89.661  1.00 75.76           N  
ATOM   1994  N   LEU A 259      17.977  38.996  87.460  1.00 63.17           N  
ATOM   1995  CA  LEU A 259      17.232  39.647  86.398  1.00 62.87           C  
ATOM   1996  C   LEU A 259      18.196  40.232  85.367  1.00 62.42           C  
ATOM   1997  O   LEU A 259      17.937  40.179  84.158  1.00 61.69           O  
ATOM   1998  CB  LEU A 259      16.340  40.764  86.962  1.00 66.39           C  
ATOM   1999  CG  LEU A 259      14.930  40.473  87.510  1.00 65.03           C  
ATOM   2000  CD1 LEU A 259      14.119  39.747  86.450  1.00 65.95           C  
ATOM   2001  CD2 LEU A 259      14.999  39.644  88.777  1.00 67.41           C  
ATOM   2002  N   ALA A 260      19.306  40.790  85.844  1.00 60.22           N  
ATOM   2003  CA  ALA A 260      20.304  41.368  84.958  1.00 57.09           C  
ATOM   2004  C   ALA A 260      20.821  40.256  84.070  1.00 55.44           C  
ATOM   2005  O   ALA A 260      20.989  40.431  82.857  1.00 56.61           O  
ATOM   2006  CB  ALA A 260      21.435  41.963  85.764  1.00 57.81           C  
ATOM   2007  N   LYS A 261      21.080  39.107  84.680  1.00 53.93           N  
ATOM   2008  CA  LYS A 261      21.548  37.952  83.936  1.00 53.54           C  
ATOM   2009  C   LYS A 261      20.523  37.655  82.842  1.00 53.36           C  
ATOM   2010  O   LYS A 261      20.864  37.604  81.664  1.00 54.99           O  
ATOM   2011  CB  LYS A 261      21.697  36.752  84.866  1.00 54.31           C  
ATOM   2012  CG  LYS A 261      22.994  36.731  85.652  1.00 55.00           C  
ATOM   2013  CD  LYS A 261      22.975  35.618  86.693  1.00 58.16           C  
ATOM   2014  CE  LYS A 261      24.358  35.360  87.275  1.00 59.01           C  
ATOM   2015  NZ  LYS A 261      24.968  36.594  87.844  1.00 58.78           N  
ATOM   2016  N   ILE A 262      19.264  37.482  83.235  1.00 53.15           N  
ATOM   2017  CA  ILE A 262      18.195  37.218  82.273  1.00 51.58           C  
ATOM   2018  C   ILE A 262      18.289  38.169  81.082  1.00 51.32           C  
ATOM   2019  O   ILE A 262      18.308  37.731  79.924  1.00 51.40           O  
ATOM   2020  CB  ILE A 262      16.800  37.400  82.910  1.00 52.69           C  
ATOM   2021  CG1 ILE A 262      16.646  36.466  84.109  1.00 53.89           C  
ATOM   2022  CG2 ILE A 262      15.714  37.094  81.889  1.00 49.55           C  
ATOM   2023  CD1 ILE A 262      15.362  36.670  84.873  1.00 54.23           C  
ATOM   2024  N   SER A 263      18.339  39.468  81.374  1.00 48.95           N  
ATOM   2025  CA  SER A 263      18.423  40.503  80.349  1.00 49.24           C  
ATOM   2026  C   SER A 263      19.477  40.187  79.309  1.00 52.27           C  
ATOM   2027  O   SER A 263      19.258  40.373  78.109  1.00 54.04           O  
ATOM   2028  CB  SER A 263      18.780  41.842  80.981  1.00 51.25           C  
ATOM   2029  OG  SER A 263      17.853  42.195  81.980  1.00 57.13           O  
ATOM   2030  N   ILE A 264      20.632  39.728  79.782  1.00 53.47           N  
ATOM   2031  CA  ILE A 264      21.740  39.392  78.910  1.00 51.29           C  
ATOM   2032  C   ILE A 264      21.422  38.200  78.038  1.00 49.42           C  
ATOM   2033  O   ILE A 264      21.774  38.183  76.855  1.00 49.66           O  
ATOM   2034  CB  ILE A 264      23.026  39.130  79.737  1.00 56.95           C  
ATOM   2035  CG1 ILE A 264      23.786  40.445  79.911  1.00 57.11           C  
ATOM   2036  CG2 ILE A 264      23.906  38.072  79.061  1.00 56.32           C  
ATOM   2037  CD1 ILE A 264      25.016  40.338  80.802  1.00 62.64           C  
ATOM   2038  N   VAL A 265      20.752  37.198  78.590  1.00 47.07           N  
ATOM   2039  CA  VAL A 265      20.434  36.035  77.767  1.00 47.26           C  
ATOM   2040  C   VAL A 265      19.484  36.390  76.619  1.00 48.74           C  
ATOM   2041  O   VAL A 265      19.660  35.915  75.501  1.00 46.52           O  
ATOM   2042  CB  VAL A 265      19.801  34.893  78.595  1.00 45.56           C  
ATOM   2043  CG1 VAL A 265      19.506  33.701  77.694  1.00 39.83           C  
ATOM   2044  CG2 VAL A 265      20.736  34.485  79.704  1.00 41.42           C  
ATOM   2045  N   ILE A 266      18.482  37.226  76.891  1.00 51.79           N  
ATOM   2046  CA  ILE A 266      17.536  37.596  75.853  1.00 51.74           C  
ATOM   2047  C   ILE A 266      18.212  38.484  74.818  1.00 52.91           C  
ATOM   2048  O   ILE A 266      17.851  38.463  73.632  1.00 52.74           O  
ATOM   2049  CB  ILE A 266      16.278  38.294  76.441  1.00 54.18           C  
ATOM   2050  CG1 ILE A 266      16.653  39.603  77.129  1.00 57.95           C  
ATOM   2051  CG2 ILE A 266      15.587  37.355  77.440  1.00 50.14           C  
ATOM   2052  CD1 ILE A 266      15.448  40.339  77.731  1.00 60.02           C  
ATOM   2053  N   VAL A 267      19.206  39.255  75.263  1.00 52.56           N  
ATOM   2054  CA  VAL A 267      19.964  40.104  74.347  1.00 50.63           C  
ATOM   2055  C   VAL A 267      20.813  39.174  73.471  1.00 50.28           C  
ATOM   2056  O   VAL A 267      20.874  39.327  72.253  1.00 51.66           O  
ATOM   2057  CB  VAL A 267      20.878  41.085  75.107  1.00 50.16           C  
ATOM   2058  CG1 VAL A 267      21.939  41.657  74.180  1.00 52.67           C  
ATOM   2059  CG2 VAL A 267      20.059  42.221  75.657  1.00 50.35           C  
ATOM   2060  N   SER A 268      21.454  38.201  74.102  1.00 48.56           N  
ATOM   2061  CA  SER A 268      22.293  37.258  73.372  1.00 48.30           C  
ATOM   2062  C   SER A 268      21.446  36.535  72.354  1.00 47.91           C  
ATOM   2063  O   SER A 268      21.894  36.248  71.247  1.00 49.74           O  
ATOM   2064  CB  SER A 268      22.901  36.234  74.328  1.00 48.41           C  
ATOM   2065  OG  SER A 268      23.332  36.862  75.527  1.00 49.03           O  
ATOM   2066  N   GLN A 269      20.214  36.238  72.746  1.00 49.88           N  
ATOM   2067  CA  GLN A 269      19.276  35.536  71.881  1.00 50.91           C  
ATOM   2068  C   GLN A 269      19.008  36.374  70.629  1.00 51.36           C  
ATOM   2069  O   GLN A 269      19.089  35.884  69.493  1.00 49.33           O  
ATOM   2070  CB  GLN A 269      17.980  35.266  72.655  1.00 49.23           C  
ATOM   2071  CG  GLN A 269      16.855  34.707  71.823  1.00 51.36           C  
ATOM   2072  CD  GLN A 269      16.018  35.791  71.184  1.00 51.39           C  
ATOM   2073  OE1 GLN A 269      15.249  36.476  71.854  1.00 49.79           O  
ATOM   2074  NE2 GLN A 269      16.166  35.955  69.883  1.00 55.34           N  
ATOM   2075  N   PHE A 270      18.719  37.652  70.849  1.00 50.67           N  
ATOM   2076  CA  PHE A 270      18.441  38.577  69.764  1.00 49.16           C  
ATOM   2077  C   PHE A 270      19.601  38.631  68.784  1.00 48.39           C  
ATOM   2078  O   PHE A 270      19.421  38.419  67.583  1.00 47.17           O  
ATOM   2079  CB  PHE A 270      18.167  39.969  70.336  1.00 51.91           C  
ATOM   2080  CG  PHE A 270      17.749  40.969  69.307  1.00 52.80           C  
ATOM   2081  CD1 PHE A 270      18.697  41.615  68.511  1.00 56.21           C  
ATOM   2082  CD2 PHE A 270      16.401  41.224  69.082  1.00 52.98           C  
ATOM   2083  CE1 PHE A 270      18.305  42.497  67.502  1.00 55.47           C  
ATOM   2084  CE2 PHE A 270      16.000  42.100  68.080  1.00 55.42           C  
ATOM   2085  CZ  PHE A 270      16.953  42.738  67.286  1.00 54.83           C  
ATOM   2086  N   LEU A 271      20.789  38.930  69.302  1.00 49.00           N  
ATOM   2087  CA  LEU A 271      21.993  39.016  68.476  1.00 49.75           C  
ATOM   2088  C   LEU A 271      22.252  37.731  67.689  1.00 49.53           C  
ATOM   2089  O   LEU A 271      22.416  37.765  66.464  1.00 49.72           O  
ATOM   2090  CB  LEU A 271      23.205  39.338  69.352  1.00 48.19           C  
ATOM   2091  CG  LEU A 271      23.047  40.658  70.106  1.00 50.04           C  
ATOM   2092  CD1 LEU A 271      24.222  40.873  71.033  1.00 49.36           C  
ATOM   2093  CD2 LEU A 271      22.915  41.801  69.107  1.00 49.27           C  
ATOM   2094  N   LEU A 272      22.290  36.600  68.386  1.00 49.02           N  
ATOM   2095  CA  LEU A 272      22.518  35.316  67.732  1.00 50.07           C  
ATOM   2096  C   LEU A 272      21.471  35.055  66.667  1.00 48.91           C  
ATOM   2097  O   LEU A 272      21.744  34.388  65.675  1.00 49.07           O  
ATOM   2098  CB  LEU A 272      22.471  34.171  68.750  1.00 53.45           C  
ATOM   2099  CG  LEU A 272      23.655  34.035  69.697  1.00 56.87           C  
ATOM   2100  CD1 LEU A 272      23.329  32.997  70.752  1.00 59.66           C  
ATOM   2101  CD2 LEU A 272      24.898  33.645  68.912  1.00 56.81           C  
ATOM   2102  N   SER A 273      20.267  35.576  66.876  1.00 48.63           N  
ATOM   2103  CA  SER A 273      19.182  35.384  65.918  1.00 45.83           C  
ATOM   2104  C   SER A 273      19.252  36.310  64.696  1.00 46.14           C  
ATOM   2105  O   SER A 273      19.017  35.871  63.573  1.00 45.82           O  
ATOM   2106  CB  SER A 273      17.827  35.575  66.608  1.00 44.12           C  
ATOM   2107  OG  SER A 273      17.682  34.702  67.703  1.00 42.28           O  
ATOM   2108  N   TRP A 274      19.576  37.583  64.909  1.00 46.57           N  
ATOM   2109  CA  TRP A 274      19.631  38.528  63.798  1.00 50.36           C  
ATOM   2110  C   TRP A 274      20.964  38.697  63.074  1.00 49.45           C  
ATOM   2111  O   TRP A 274      20.982  38.897  61.858  1.00 51.07           O  
ATOM   2112  CB  TRP A 274      19.148  39.919  64.240  1.00 53.73           C  
ATOM   2113  CG  TRP A 274      17.679  40.006  64.509  1.00 55.80           C  
ATOM   2114  CD1 TRP A 274      17.045  39.752  65.690  1.00 56.99           C  
ATOM   2115  CD2 TRP A 274      16.651  40.355  63.571  1.00 56.54           C  
ATOM   2116  NE1 TRP A 274      15.691  39.921  65.548  1.00 56.13           N  
ATOM   2117  CE2 TRP A 274      15.420  40.292  64.260  1.00 56.31           C  
ATOM   2118  CE3 TRP A 274      16.651  40.715  62.215  1.00 56.13           C  
ATOM   2119  CZ2 TRP A 274      14.194  40.577  63.640  1.00 57.23           C  
ATOM   2120  CZ3 TRP A 274      15.430  40.999  61.591  1.00 54.36           C  
ATOM   2121  CH2 TRP A 274      14.222  40.928  62.305  1.00 55.88           C  
ATOM   2122  N   SER A 275      22.074  38.625  63.801  1.00 46.48           N  
ATOM   2123  CA  SER A 275      23.378  38.822  63.179  1.00 43.67           C  
ATOM   2124  C   SER A 275      23.626  38.025  61.908  1.00 43.55           C  
ATOM   2125  O   SER A 275      24.221  38.540  60.969  1.00 44.12           O  
ATOM   2126  CB  SER A 275      24.482  38.566  64.192  1.00 44.46           C  
ATOM   2127  OG  SER A 275      24.370  39.492  65.263  1.00 43.22           O  
ATOM   2128  N   PRO A 276      23.178  36.763  61.853  1.00 43.30           N  
ATOM   2129  CA  PRO A 276      23.422  36.018  60.614  1.00 41.37           C  
ATOM   2130  C   PRO A 276      22.796  36.728  59.401  1.00 42.82           C  
ATOM   2131  O   PRO A 276      23.498  37.117  58.467  1.00 44.57           O  
ATOM   2132  CB  PRO A 276      22.770  34.667  60.896  1.00 40.70           C  
ATOM   2133  CG  PRO A 276      22.946  34.518  62.376  1.00 37.90           C  
ATOM   2134  CD  PRO A 276      22.615  35.888  62.895  1.00 39.92           C  
ATOM   2135  N   TYR A 277      21.472  36.900  59.441  1.00 43.69           N  
ATOM   2136  CA  TYR A 277      20.715  37.551  58.374  1.00 40.59           C  
ATOM   2137  C   TYR A 277      21.326  38.901  58.066  1.00 39.48           C  
ATOM   2138  O   TYR A 277      21.497  39.268  56.901  1.00 40.60           O  
ATOM   2139  CB  TYR A 277      19.244  37.719  58.785  1.00 39.95           C  
ATOM   2140  CG  TYR A 277      18.350  38.368  57.743  1.00 37.17           C  
ATOM   2141  CD1 TYR A 277      17.918  39.691  57.880  1.00 32.71           C  
ATOM   2142  CD2 TYR A 277      17.961  37.661  56.604  1.00 37.72           C  
ATOM   2143  CE1 TYR A 277      17.123  40.295  56.907  1.00 32.86           C  
ATOM   2144  CE2 TYR A 277      17.165  38.249  55.618  1.00 36.49           C  
ATOM   2145  CZ  TYR A 277      16.748  39.563  55.774  1.00 38.60           C  
ATOM   2146  OH  TYR A 277      15.944  40.124  54.796  1.00 34.90           O  
ATOM   2147  N   ALA A 278      21.661  39.643  59.110  1.00 37.69           N  
ATOM   2148  CA  ALA A 278      22.259  40.957  58.926  1.00 41.15           C  
ATOM   2149  C   ALA A 278      23.473  40.829  58.015  1.00 43.71           C  
ATOM   2150  O   ALA A 278      23.622  41.581  57.051  1.00 47.06           O  
ATOM   2151  CB  ALA A 278      22.671  41.536  60.266  1.00 37.53           C  
ATOM   2152  N   VAL A 279      24.326  39.856  58.324  1.00 46.04           N  
ATOM   2153  CA  VAL A 279      25.536  39.620  57.560  1.00 46.11           C  
ATOM   2154  C   VAL A 279      25.212  39.323  56.099  1.00 49.86           C  
ATOM   2155  O   VAL A 279      25.747  39.974  55.200  1.00 50.48           O  
ATOM   2156  CB  VAL A 279      26.366  38.462  58.187  1.00 46.56           C  
ATOM   2157  CG1 VAL A 279      27.438  37.975  57.226  1.00 47.51           C  
ATOM   2158  CG2 VAL A 279      27.038  38.954  59.468  1.00 43.07           C  
ATOM   2159  N   VAL A 280      24.334  38.354  55.857  1.00 50.87           N  
ATOM   2160  CA  VAL A 280      23.969  38.012  54.493  1.00 51.97           C  
ATOM   2161  C   VAL A 280      23.467  39.233  53.746  1.00 54.80           C  
ATOM   2162  O   VAL A 280      23.647  39.347  52.535  1.00 54.77           O  
ATOM   2163  CB  VAL A 280      22.862  36.963  54.439  1.00 52.48           C  
ATOM   2164  CG1 VAL A 280      22.481  36.681  52.978  1.00 49.72           C  
ATOM   2165  CG2 VAL A 280      23.323  35.694  55.139  1.00 54.39           C  
ATOM   2166  N   ALA A 281      22.823  40.143  54.465  1.00 57.34           N  
ATOM   2167  CA  ALA A 281      22.305  41.349  53.836  1.00 58.88           C  
ATOM   2168  C   ALA A 281      23.479  42.197  53.378  1.00 59.05           C  
ATOM   2169  O   ALA A 281      23.536  42.640  52.229  1.00 58.95           O  
ATOM   2170  CB  ALA A 281      21.447  42.129  54.822  1.00 60.67           C  
ATOM   2171  N   LEU A 282      24.422  42.412  54.288  1.00 59.58           N  
ATOM   2172  CA  LEU A 282      25.601  43.213  53.990  1.00 58.32           C  
ATOM   2173  C   LEU A 282      26.388  42.692  52.804  1.00 58.18           C  
ATOM   2174  O   LEU A 282      26.905  43.476  52.015  1.00 59.24           O  
ATOM   2175  CB  LEU A 282      26.498  43.301  55.225  1.00 54.59           C  
ATOM   2176  CG  LEU A 282      25.957  44.293  56.251  1.00 52.81           C  
ATOM   2177  CD1 LEU A 282      26.834  44.295  57.489  1.00 49.90           C  
ATOM   2178  CD2 LEU A 282      25.887  45.682  55.627  1.00 47.48           C  
ATOM   2179  N   LEU A 283      26.484  41.373  52.677  1.00 58.38           N  
ATOM   2180  CA  LEU A 283      27.202  40.783  51.554  1.00 58.25           C  
ATOM   2181  C   LEU A 283      26.499  41.185  50.267  1.00 59.63           C  
ATOM   2182  O   LEU A 283      27.135  41.540  49.281  1.00 60.87           O  
ATOM   2183  CB  LEU A 283      27.221  39.251  51.662  1.00 57.42           C  
ATOM   2184  CG  LEU A 283      28.308  38.582  52.505  1.00 57.97           C  
ATOM   2185  CD1 LEU A 283      28.409  39.224  53.889  1.00 57.70           C  
ATOM   2186  CD2 LEU A 283      27.985  37.106  52.620  1.00 57.55           C  
ATOM   2187  N   ALA A 284      25.173  41.138  50.292  1.00 61.03           N  
ATOM   2188  CA  ALA A 284      24.379  41.482  49.124  1.00 60.44           C  
ATOM   2189  C   ALA A 284      24.522  42.952  48.754  1.00 60.65           C  
ATOM   2190  O   ALA A 284      24.387  43.321  47.588  1.00 60.68           O  
ATOM   2191  CB  ALA A 284      22.915  41.144  49.377  1.00 58.67           C  
ATOM   2192  N   GLN A 285      24.804  43.793  49.739  1.00 60.25           N  
ATOM   2193  CA  GLN A 285      24.928  45.221  49.484  1.00 60.27           C  
ATOM   2194  C   GLN A 285      26.369  45.683  49.294  1.00 61.44           C  
ATOM   2195  O   GLN A 285      26.614  46.759  48.727  1.00 60.87           O  
ATOM   2196  CB  GLN A 285      24.288  46.000  50.639  1.00 58.85           C  
ATOM   2197  CG  GLN A 285      24.463  47.514  50.583  1.00 57.59           C  
ATOM   2198  CD  GLN A 285      23.681  48.158  49.457  1.00 56.24           C  
ATOM   2199  OE1 GLN A 285      23.738  49.371  49.265  1.00 54.63           O  
ATOM   2200  NE2 GLN A 285      22.943  47.351  48.711  1.00 55.28           N  
ATOM   2201  N   PHE A 286      27.324  44.878  49.755  1.00 60.65           N  
ATOM   2202  CA  PHE A 286      28.732  45.248  49.650  1.00 59.02           C  
ATOM   2203  C   PHE A 286      29.660  44.165  49.124  1.00 57.80           C  
ATOM   2204  O   PHE A 286      30.774  44.468  48.704  1.00 58.07           O  
ATOM   2205  CB  PHE A 286      29.250  45.700  51.010  1.00 59.34           C  
ATOM   2206  CG  PHE A 286      28.627  46.967  51.511  1.00 59.01           C  
ATOM   2207  CD1 PHE A 286      28.020  47.003  52.759  1.00 57.97           C  
ATOM   2208  CD2 PHE A 286      28.692  48.137  50.761  1.00 58.96           C  
ATOM   2209  CE1 PHE A 286      27.492  48.182  53.255  1.00 57.38           C  
ATOM   2210  CE2 PHE A 286      28.166  49.324  51.251  1.00 56.93           C  
ATOM   2211  CZ  PHE A 286      27.565  49.347  52.503  1.00 58.60           C  
ATOM   2212  N   GLY A 287      29.215  42.914  49.147  1.00 56.72           N  
ATOM   2213  CA  GLY A 287      30.066  41.835  48.681  1.00 55.97           C  
ATOM   2214  C   GLY A 287      29.548  41.037  47.500  1.00 56.88           C  
ATOM   2215  O   GLY A 287      28.832  41.565  46.649  1.00 57.32           O  
ATOM   2216  N   PRO A 288      29.915  39.749  47.414  1.00 56.69           N  
ATOM   2217  CA  PRO A 288      29.503  38.842  46.339  1.00 56.83           C  
ATOM   2218  C   PRO A 288      28.005  38.536  46.338  1.00 58.51           C  
ATOM   2219  O   PRO A 288      27.550  37.606  47.012  1.00 59.93           O  
ATOM   2220  CB  PRO A 288      30.327  37.585  46.610  1.00 55.34           C  
ATOM   2221  CG  PRO A 288      31.523  38.103  47.327  1.00 57.88           C  
ATOM   2222  CD  PRO A 288      30.933  39.112  48.263  1.00 56.45           C  
ATOM   2223  N   LEU A 289      27.233  39.304  45.577  1.00 57.92           N  
ATOM   2224  CA  LEU A 289      25.802  39.060  45.513  1.00 58.17           C  
ATOM   2225  C   LEU A 289      25.537  37.624  45.090  1.00 58.81           C  
ATOM   2226  O   LEU A 289      24.470  37.088  45.365  1.00 59.24           O  
ATOM   2227  CB  LEU A 289      25.132  40.002  44.512  1.00 59.77           C  
ATOM   2228  CG  LEU A 289      23.623  39.793  44.271  1.00 59.15           C  
ATOM   2229  CD1 LEU A 289      22.832  40.199  45.524  1.00 57.85           C  
ATOM   2230  CD2 LEU A 289      23.176  40.619  43.069  1.00 55.10           C  
ATOM   2231  N   GLU A 290      26.504  37.001  44.419  1.00 60.78           N  
ATOM   2232  CA  GLU A 290      26.313  35.629  43.962  1.00 63.04           C  
ATOM   2233  C   GLU A 290      26.232  34.668  45.128  1.00 62.91           C  
ATOM   2234  O   GLU A 290      25.863  33.507  44.962  1.00 61.90           O  
ATOM   2235  CB  GLU A 290      27.416  35.189  42.985  1.00 63.45           C  
ATOM   2236  CG  GLU A 290      28.832  35.561  43.383  1.00 67.51           C  
ATOM   2237  CD  GLU A 290      29.194  36.983  42.991  1.00 69.73           C  
ATOM   2238  OE1 GLU A 290      30.335  37.410  43.271  1.00 70.06           O  
ATOM   2239  OE2 GLU A 290      28.341  37.670  42.397  1.00 70.69           O  
ATOM   2240  N   TRP A 291      26.573  35.159  46.314  1.00 63.21           N  
ATOM   2241  CA  TRP A 291      26.502  34.332  47.513  1.00 65.65           C  
ATOM   2242  C   TRP A 291      25.065  34.308  48.021  1.00 65.44           C  
ATOM   2243  O   TRP A 291      24.569  33.283  48.489  1.00 65.39           O  
ATOM   2244  CB  TRP A 291      27.415  34.889  48.608  1.00 67.24           C  
ATOM   2245  CG  TRP A 291      28.874  34.687  48.347  1.00 70.33           C  
ATOM   2246  CD1 TRP A 291      29.433  33.870  47.406  1.00 70.82           C  
ATOM   2247  CD2 TRP A 291      29.963  35.268  49.071  1.00 70.87           C  
ATOM   2248  NE1 TRP A 291      30.803  33.903  47.503  1.00 72.20           N  
ATOM   2249  CE2 TRP A 291      31.156  34.753  48.517  1.00 71.59           C  
ATOM   2250  CE3 TRP A 291      30.048  36.172  50.137  1.00 72.80           C  
ATOM   2251  CZ2 TRP A 291      32.423  35.111  48.993  1.00 70.23           C  
ATOM   2252  CZ3 TRP A 291      31.310  36.530  50.614  1.00 72.23           C  
ATOM   2253  CH2 TRP A 291      32.480  35.997  50.039  1.00 71.42           C  
ATOM   2254  N   VAL A 292      24.401  35.453  47.913  1.00 64.45           N  
ATOM   2255  CA  VAL A 292      23.034  35.592  48.379  1.00 60.60           C  
ATOM   2256  C   VAL A 292      22.044  34.782  47.563  1.00 58.50           C  
ATOM   2257  O   VAL A 292      21.292  35.327  46.768  1.00 59.25           O  
ATOM   2258  CB  VAL A 292      22.594  37.064  48.372  1.00 60.08           C  
ATOM   2259  CG1 VAL A 292      21.275  37.208  49.094  1.00 58.10           C  
ATOM   2260  CG2 VAL A 292      23.654  37.928  49.028  1.00 57.34           C  
ATOM   2261  N   THR A 293      22.053  33.470  47.766  1.00 57.09           N  
ATOM   2262  CA  THR A 293      21.135  32.572  47.077  1.00 55.57           C  
ATOM   2263  C   THR A 293      19.814  32.494  47.844  1.00 54.82           C  
ATOM   2264  O   THR A 293      19.723  32.928  49.004  1.00 55.34           O  
ATOM   2265  CB  THR A 293      21.695  31.150  47.013  1.00 54.47           C  
ATOM   2266  OG1 THR A 293      21.993  30.706  48.344  1.00 54.52           O  
ATOM   2267  CG2 THR A 293      22.948  31.102  46.164  1.00 53.31           C  
ATOM   2268  N   PRO A 294      18.775  31.920  47.211  1.00 52.71           N  
ATOM   2269  CA  PRO A 294      17.452  31.773  47.827  1.00 52.23           C  
ATOM   2270  C   PRO A 294      17.519  31.271  49.273  1.00 51.40           C  
ATOM   2271  O   PRO A 294      16.863  31.834  50.136  1.00 52.87           O  
ATOM   2272  CB  PRO A 294      16.757  30.792  46.897  1.00 52.09           C  
ATOM   2273  CG  PRO A 294      17.298  31.185  45.572  1.00 51.13           C  
ATOM   2274  CD  PRO A 294      18.773  31.362  45.847  1.00 51.61           C  
ATOM   2275  N   TYR A 295      18.310  30.225  49.525  1.00 51.69           N  
ATOM   2276  CA  TYR A 295      18.466  29.672  50.874  1.00 52.17           C  
ATOM   2277  C   TYR A 295      19.410  30.542  51.701  1.00 51.51           C  
ATOM   2278  O   TYR A 295      19.254  30.661  52.916  1.00 52.55           O  
ATOM   2279  CB  TYR A 295      19.035  28.252  50.839  1.00 52.36           C  
ATOM   2280  CG  TYR A 295      18.156  27.220  50.174  1.00 57.52           C  
ATOM   2281  CD1 TYR A 295      18.690  26.329  49.238  1.00 57.01           C  
ATOM   2282  CD2 TYR A 295      16.794  27.131  50.463  1.00 58.66           C  
ATOM   2283  CE1 TYR A 295      17.897  25.385  48.604  1.00 57.02           C  
ATOM   2284  CE2 TYR A 295      15.982  26.177  49.828  1.00 58.97           C  
ATOM   2285  CZ  TYR A 295      16.547  25.313  48.902  1.00 58.08           C  
ATOM   2286  OH  TYR A 295      15.768  24.374  48.262  1.00 58.63           O  
ATOM   2287  N   ALA A 296      20.397  31.137  51.039  1.00 51.13           N  
ATOM   2288  CA  ALA A 296      21.367  31.982  51.726  1.00 50.66           C  
ATOM   2289  C   ALA A 296      20.649  33.075  52.497  1.00 49.69           C  
ATOM   2290  O   ALA A 296      21.059  33.458  53.600  1.00 47.33           O  
ATOM   2291  CB  ALA A 296      22.334  32.604  50.721  1.00 52.71           C  
ATOM   2292  N   ALA A 297      19.572  33.581  51.903  1.00 48.73           N  
ATOM   2293  CA  ALA A 297      18.790  34.632  52.531  1.00 45.18           C  
ATOM   2294  C   ALA A 297      17.641  34.028  53.337  1.00 45.88           C  
ATOM   2295  O   ALA A 297      17.502  34.301  54.532  1.00 45.87           O  
ATOM   2296  CB  ALA A 297      18.263  35.592  51.468  1.00 42.31           C  
ATOM   2297  N   GLN A 298      16.840  33.179  52.703  1.00 45.86           N  
ATOM   2298  CA  GLN A 298      15.701  32.580  53.389  1.00 46.91           C  
ATOM   2299  C   GLN A 298      15.972  31.935  54.759  1.00 46.78           C  
ATOM   2300  O   GLN A 298      15.473  32.410  55.768  1.00 45.96           O  
ATOM   2301  CB  GLN A 298      15.012  31.559  52.481  1.00 46.56           C  
ATOM   2302  CG  GLN A 298      13.517  31.433  52.768  1.00 50.65           C  
ATOM   2303  CD  GLN A 298      12.792  32.760  52.599  1.00 52.40           C  
ATOM   2304  OE1 GLN A 298      12.714  33.292  51.489  1.00 50.50           O  
ATOM   2305  NE2 GLN A 298      12.267  33.306  53.703  1.00 49.68           N  
ATOM   2306  N   LEU A 299      16.754  30.857  54.790  1.00 49.56           N  
ATOM   2307  CA  LEU A 299      17.048  30.158  56.040  1.00 49.42           C  
ATOM   2308  C   LEU A 299      17.506  31.056  57.187  1.00 48.40           C  
ATOM   2309  O   LEU A 299      17.111  30.849  58.332  1.00 48.00           O  
ATOM   2310  CB  LEU A 299      18.073  29.048  55.800  1.00 52.47           C  
ATOM   2311  CG  LEU A 299      17.490  27.669  55.483  1.00 55.64           C  
ATOM   2312  CD1 LEU A 299      16.556  27.738  54.283  1.00 54.35           C  
ATOM   2313  CD2 LEU A 299      18.627  26.697  55.219  1.00 55.65           C  
ATOM   2314  N   PRO A 300      18.362  32.049  56.901  1.00 46.18           N  
ATOM   2315  CA  PRO A 300      18.809  32.930  57.979  1.00 43.88           C  
ATOM   2316  C   PRO A 300      17.738  33.937  58.404  1.00 42.12           C  
ATOM   2317  O   PRO A 300      17.773  34.439  59.533  1.00 43.48           O  
ATOM   2318  CB  PRO A 300      20.034  33.609  57.383  1.00 44.13           C  
ATOM   2319  CG  PRO A 300      20.561  32.570  56.471  1.00 44.81           C  
ATOM   2320  CD  PRO A 300      19.310  32.105  55.779  1.00 46.15           C  
ATOM   2321  N   VAL A 301      16.791  34.242  57.518  1.00 40.28           N  
ATOM   2322  CA  VAL A 301      15.725  35.182  57.883  1.00 42.67           C  
ATOM   2323  C   VAL A 301      14.711  34.481  58.786  1.00 40.69           C  
ATOM   2324  O   VAL A 301      14.157  35.093  59.689  1.00 39.23           O  
ATOM   2325  CB  VAL A 301      14.982  35.775  56.642  1.00 41.16           C  
ATOM   2326  CG1 VAL A 301      13.979  34.778  56.105  1.00 44.15           C  
ATOM   2327  CG2 VAL A 301      14.274  37.075  57.023  1.00 38.92           C  
ATOM   2328  N   MET A 302      14.474  33.199  58.545  1.00 42.05           N  
ATOM   2329  CA  MET A 302      13.549  32.437  59.382  1.00 47.71           C  
ATOM   2330  C   MET A 302      14.093  32.413  60.815  1.00 50.47           C  
ATOM   2331  O   MET A 302      13.367  32.643  61.783  1.00 51.33           O  
ATOM   2332  CB  MET A 302      13.415  30.998  58.864  1.00 47.05           C  
ATOM   2333  CG  MET A 302      12.939  30.911  57.434  1.00 50.09           C  
ATOM   2334  SD  MET A 302      11.556  32.041  57.145  1.00 53.62           S  
ATOM   2335  CE  MET A 302      10.197  30.871  57.101  1.00 55.21           C  
ATOM   2336  N   PHE A 303      15.384  32.133  60.934  1.00 54.06           N  
ATOM   2337  CA  PHE A 303      16.042  32.098  62.230  1.00 55.31           C  
ATOM   2338  C   PHE A 303      15.825  33.450  62.895  1.00 52.58           C  
ATOM   2339  O   PHE A 303      15.502  33.524  64.080  1.00 51.95           O  
ATOM   2340  CB  PHE A 303      17.541  31.835  62.045  1.00 61.00           C  
ATOM   2341  CG  PHE A 303      18.257  31.481  63.313  1.00 64.29           C  
ATOM   2342  CD1 PHE A 303      17.974  30.292  63.973  1.00 65.39           C  
ATOM   2343  CD2 PHE A 303      19.211  32.344  63.857  1.00 66.76           C  
ATOM   2344  CE1 PHE A 303      18.627  29.959  65.166  1.00 69.29           C  
ATOM   2345  CE2 PHE A 303      19.875  32.026  65.049  1.00 68.88           C  
ATOM   2346  CZ  PHE A 303      19.580  30.829  65.706  1.00 68.06           C  
ATOM   2347  N   ALA A 304      15.993  34.524  62.126  1.00 51.48           N  
ATOM   2348  CA  ALA A 304      15.800  35.877  62.659  1.00 52.25           C  
ATOM   2349  C   ALA A 304      14.350  36.098  63.089  1.00 49.16           C  
ATOM   2350  O   ALA A 304      14.091  36.575  64.194  1.00 47.07           O  
ATOM   2351  CB  ALA A 304      16.219  36.937  61.619  1.00 49.96           C  
ATOM   2352  N   LYS A 305      13.405  35.736  62.228  1.00 45.57           N  
ATOM   2353  CA  LYS A 305      11.992  35.917  62.551  1.00 44.82           C  
ATOM   2354  C   LYS A 305      11.543  35.200  63.834  1.00 45.89           C  
ATOM   2355  O   LYS A 305      10.689  35.703  64.565  1.00 47.94           O  
ATOM   2356  CB  LYS A 305      11.120  35.456  61.381  1.00 40.04           C  
ATOM   2357  CG  LYS A 305      11.243  36.308  60.135  1.00 36.20           C  
ATOM   2358  CD  LYS A 305      10.092  36.039  59.184  1.00 33.05           C  
ATOM   2359  CE  LYS A 305      10.330  36.630  57.807  1.00 33.45           C  
ATOM   2360  NZ  LYS A 305      10.100  38.067  57.709  1.00 40.92           N  
ATOM   2361  N   ALA A 306      12.115  34.029  64.103  1.00 45.04           N  
ATOM   2362  CA  ALA A 306      11.749  33.274  65.292  1.00 42.98           C  
ATOM   2363  C   ALA A 306      12.247  33.961  66.560  1.00 42.38           C  
ATOM   2364  O   ALA A 306      11.745  33.708  67.648  1.00 43.83           O  
ATOM   2365  CB  ALA A 306      12.301  31.851  65.205  1.00 40.02           C  
ATOM   2366  N   SER A 307      13.228  34.847  66.419  1.00 44.58           N  
ATOM   2367  CA  SER A 307      13.758  35.549  67.589  1.00 43.22           C  
ATOM   2368  C   SER A 307      12.652  36.077  68.479  1.00 41.13           C  
ATOM   2369  O   SER A 307      12.740  35.993  69.685  1.00 41.80           O  
ATOM   2370  CB  SER A 307      14.660  36.726  67.180  1.00 42.09           C  
ATOM   2371  OG  SER A 307      15.151  37.436  68.322  1.00 39.88           O  
ATOM   2372  N   ALA A 308      11.602  36.616  67.879  1.00 45.53           N  
ATOM   2373  CA  ALA A 308      10.509  37.187  68.656  1.00 47.89           C  
ATOM   2374  C   ALA A 308       9.674  36.191  69.468  1.00 49.44           C  
ATOM   2375  O   ALA A 308       8.688  36.582  70.091  1.00 53.34           O  
ATOM   2376  CB  ALA A 308       9.596  38.010  67.743  1.00 44.17           C  
ATOM   2377  N   ILE A 309      10.058  34.919  69.476  1.00 46.36           N  
ATOM   2378  CA  ILE A 309       9.296  33.929  70.229  1.00 45.55           C  
ATOM   2379  C   ILE A 309      10.126  33.304  71.341  1.00 47.93           C  
ATOM   2380  O   ILE A 309       9.734  32.275  71.898  1.00 51.06           O  
ATOM   2381  CB  ILE A 309       8.858  32.752  69.355  1.00 43.51           C  
ATOM   2382  CG1 ILE A 309      10.075  31.856  69.095  1.00 43.35           C  
ATOM   2383  CG2 ILE A 309       8.219  33.266  68.064  1.00 45.55           C  
ATOM   2384  CD1 ILE A 309       9.757  30.473  68.620  1.00 43.32           C  
ATOM   2385  N   HIS A 310      11.258  33.908  71.679  1.00 46.31           N  
ATOM   2386  CA  HIS A 310      12.109  33.302  72.683  1.00 42.25           C  
ATOM   2387  C   HIS A 310      12.056  33.826  74.104  1.00 41.01           C  
ATOM   2388  O   HIS A 310      12.068  33.040  75.037  1.00 44.63           O  
ATOM   2389  CB  HIS A 310      13.551  33.298  72.183  1.00 41.21           C  
ATOM   2390  CG  HIS A 310      13.783  32.359  71.041  1.00 39.06           C  
ATOM   2391  ND1 HIS A 310      14.534  32.699  69.935  1.00 41.53           N  
ATOM   2392  CD2 HIS A 310      13.358  31.091  70.831  1.00 36.45           C  
ATOM   2393  CE1 HIS A 310      14.558  31.682  69.093  1.00 38.70           C  
ATOM   2394  NE2 HIS A 310      13.853  30.694  69.613  1.00 38.21           N  
ATOM   2395  N   ASN A 311      11.990  35.134  74.282  1.00 41.83           N  
ATOM   2396  CA  ASN A 311      11.970  35.694  75.621  1.00 44.33           C  
ATOM   2397  C   ASN A 311      10.971  35.027  76.559  1.00 46.86           C  
ATOM   2398  O   ASN A 311      11.326  34.647  77.666  1.00 49.40           O  
ATOM   2399  CB  ASN A 311      11.705  37.203  75.563  1.00 49.04           C  
ATOM   2400  CG  ASN A 311      12.714  37.936  74.705  1.00 48.17           C  
ATOM   2401  OD1 ASN A 311      13.723  37.361  74.298  1.00 47.99           O  
ATOM   2402  ND2 ASN A 311      12.448  39.207  74.423  1.00 49.35           N  
ATOM   2403  N   PRO A 312       9.705  34.885  76.136  1.00 48.65           N  
ATOM   2404  CA  PRO A 312       8.735  34.244  77.024  1.00 47.60           C  
ATOM   2405  C   PRO A 312       9.216  32.884  77.549  1.00 47.62           C  
ATOM   2406  O   PRO A 312       9.114  32.597  78.751  1.00 45.76           O  
ATOM   2407  CB  PRO A 312       7.491  34.138  76.151  1.00 47.54           C  
ATOM   2408  CG  PRO A 312       7.587  35.387  75.326  1.00 47.96           C  
ATOM   2409  CD  PRO A 312       9.045  35.365  74.910  1.00 48.04           C  
ATOM   2410  N   MET A 313       9.746  32.047  76.666  1.00 46.70           N  
ATOM   2411  CA  MET A 313      10.231  30.752  77.106  1.00 50.29           C  
ATOM   2412  C   MET A 313      11.449  30.926  78.025  1.00 51.18           C  
ATOM   2413  O   MET A 313      11.614  30.193  79.001  1.00 52.16           O  
ATOM   2414  CB  MET A 313      10.578  29.877  75.901  1.00 52.20           C  
ATOM   2415  CG  MET A 313       9.424  29.745  74.914  1.00 55.62           C  
ATOM   2416  SD  MET A 313       9.630  28.485  73.634  1.00 61.04           S  
ATOM   2417  CE  MET A 313      10.517  29.401  72.359  1.00 52.43           C  
ATOM   2418  N   ILE A 314      12.296  31.905  77.729  1.00 53.20           N  
ATOM   2419  CA  ILE A 314      13.466  32.154  78.562  1.00 55.18           C  
ATOM   2420  C   ILE A 314      12.985  32.530  79.967  1.00 57.62           C  
ATOM   2421  O   ILE A 314      13.471  31.988  80.971  1.00 59.58           O  
ATOM   2422  CB  ILE A 314      14.338  33.306  77.984  1.00 54.93           C  
ATOM   2423  CG1 ILE A 314      14.874  32.913  76.603  1.00 56.01           C  
ATOM   2424  CG2 ILE A 314      15.514  33.595  78.894  1.00 53.03           C  
ATOM   2425  CD1 ILE A 314      15.627  34.033  75.892  1.00 55.94           C  
ATOM   2426  N   TYR A 315      12.021  33.448  80.027  1.00 56.68           N  
ATOM   2427  CA  TYR A 315      11.443  33.905  81.289  1.00 56.68           C  
ATOM   2428  C   TYR A 315      10.877  32.744  82.095  1.00 57.23           C  
ATOM   2429  O   TYR A 315      11.104  32.640  83.298  1.00 56.59           O  
ATOM   2430  CB  TYR A 315      10.293  34.877  81.033  1.00 58.17           C  
ATOM   2431  CG  TYR A 315      10.643  36.170  80.332  1.00 59.90           C  
ATOM   2432  CD1 TYR A 315       9.767  36.731  79.401  1.00 59.92           C  
ATOM   2433  CD2 TYR A 315      11.801  36.876  80.647  1.00 59.98           C  
ATOM   2434  CE1 TYR A 315      10.027  37.959  78.803  1.00 57.44           C  
ATOM   2435  CE2 TYR A 315      12.070  38.115  80.053  1.00 59.05           C  
ATOM   2436  CZ  TYR A 315      11.176  38.645  79.135  1.00 55.40           C  
ATOM   2437  OH  TYR A 315      11.429  39.862  78.562  1.00 51.90           O  
ATOM   2438  N   SER A 316      10.128  31.876  81.420  1.00 58.32           N  
ATOM   2439  CA  SER A 316       9.476  30.748  82.085  1.00 59.64           C  
ATOM   2440  C   SER A 316      10.401  29.752  82.771  1.00 62.23           C  
ATOM   2441  O   SER A 316       9.956  28.989  83.633  1.00 63.39           O  
ATOM   2442  CB  SER A 316       8.571  30.005  81.101  1.00 56.83           C  
ATOM   2443  OG  SER A 316       9.322  29.252  80.176  1.00 56.22           O  
ATOM   2444  N   VAL A 317      11.681  29.751  82.407  1.00 64.27           N  
ATOM   2445  CA  VAL A 317      12.632  28.818  83.023  1.00 63.79           C  
ATOM   2446  C   VAL A 317      13.627  29.486  83.958  1.00 63.06           C  
ATOM   2447  O   VAL A 317      14.406  28.796  84.606  1.00 63.47           O  
ATOM   2448  CB  VAL A 317      13.457  28.053  81.962  1.00 61.56           C  
ATOM   2449  CG1 VAL A 317      12.546  27.260  81.066  1.00 63.28           C  
ATOM   2450  CG2 VAL A 317      14.288  29.024  81.146  1.00 61.29           C  
ATOM   2451  N   SER A 318      13.608  30.816  84.030  1.00 62.30           N  
ATOM   2452  CA  SER A 318      14.567  31.524  84.881  1.00 60.22           C  
ATOM   2453  C   SER A 318      14.012  32.699  85.660  1.00 58.37           C  
ATOM   2454  O   SER A 318      14.712  33.276  86.485  1.00 61.40           O  
ATOM   2455  CB  SER A 318      15.723  32.039  84.036  1.00 59.88           C  
ATOM   2456  OG  SER A 318      15.257  33.041  83.153  1.00 64.71           O  
ATOM   2457  N   HIS A 319      12.769  33.074  85.403  1.00 55.62           N  
ATOM   2458  CA  HIS A 319      12.196  34.206  86.118  1.00 52.97           C  
ATOM   2459  C   HIS A 319      11.272  33.729  87.240  1.00 53.04           C  
ATOM   2460  O   HIS A 319      10.148  33.303  86.983  1.00 54.42           O  
ATOM   2461  CB  HIS A 319      11.433  35.095  85.142  1.00 47.71           C  
ATOM   2462  CG  HIS A 319      11.183  36.468  85.662  1.00 42.68           C  
ATOM   2463  ND1 HIS A 319      10.443  36.706  86.800  1.00 43.98           N  
ATOM   2464  CD2 HIS A 319      11.597  37.677  85.220  1.00 42.44           C  
ATOM   2465  CE1 HIS A 319      10.412  38.005  87.040  1.00 41.27           C  
ATOM   2466  NE2 HIS A 319      11.105  38.616  86.096  1.00 43.05           N  
ATOM   2467  N   PRO A 320      11.736  33.814  88.502  1.00 53.09           N  
ATOM   2468  CA  PRO A 320      10.980  33.391  89.688  1.00 53.92           C  
ATOM   2469  C   PRO A 320       9.570  33.964  89.847  1.00 55.00           C  
ATOM   2470  O   PRO A 320       8.595  33.214  89.805  1.00 55.89           O  
ATOM   2471  CB  PRO A 320      11.904  33.774  90.843  1.00 53.46           C  
ATOM   2472  CG  PRO A 320      12.630  34.959  90.314  1.00 52.40           C  
ATOM   2473  CD  PRO A 320      12.960  34.529  88.901  1.00 53.56           C  
ATOM   2474  N   LYS A 321       9.446  35.275  90.031  1.00 54.54           N  
ATOM   2475  CA  LYS A 321       8.117  35.854  90.188  1.00 55.63           C  
ATOM   2476  C   LYS A 321       7.213  35.469  89.032  1.00 54.82           C  
ATOM   2477  O   LYS A 321       6.062  35.095  89.237  1.00 56.16           O  
ATOM   2478  CB  LYS A 321       8.186  37.382  90.299  1.00 57.76           C  
ATOM   2479  CG  LYS A 321       8.505  37.882  91.702  1.00 60.52           C  
ATOM   2480  CD  LYS A 321       8.562  39.400  91.756  1.00 63.23           C  
ATOM   2481  CE  LYS A 321       8.883  39.884  93.160  1.00 67.27           C  
ATOM   2482  NZ  LYS A 321       8.974  41.368  93.240  1.00 71.14           N  
ATOM   2483  N   PHE A 322       7.744  35.541  87.816  1.00 54.31           N  
ATOM   2484  CA  PHE A 322       6.970  35.199  86.629  1.00 52.40           C  
ATOM   2485  C   PHE A 322       6.574  33.733  86.655  1.00 53.42           C  
ATOM   2486  O   PHE A 322       5.438  33.379  86.334  1.00 53.68           O  
ATOM   2487  CB  PHE A 322       7.779  35.486  85.369  1.00 49.72           C  
ATOM   2488  CG  PHE A 322       7.052  35.168  84.096  1.00 48.85           C  
ATOM   2489  CD1 PHE A 322       5.852  35.796  83.789  1.00 47.69           C  
ATOM   2490  CD2 PHE A 322       7.574  34.250  83.197  1.00 46.26           C  
ATOM   2491  CE1 PHE A 322       5.187  35.515  82.604  1.00 46.53           C  
ATOM   2492  CE2 PHE A 322       6.918  33.963  82.008  1.00 49.13           C  
ATOM   2493  CZ  PHE A 322       5.721  34.597  81.710  1.00 47.50           C  
ATOM   2494  N   ARG A 323       7.511  32.876  87.035  1.00 53.48           N  
ATOM   2495  CA  ARG A 323       7.231  31.450  87.105  1.00 54.78           C  
ATOM   2496  C   ARG A 323       6.182  31.183  88.171  1.00 54.79           C  
ATOM   2497  O   ARG A 323       5.388  30.244  88.064  1.00 55.92           O  
ATOM   2498  CB  ARG A 323       8.513  30.672  87.433  1.00 55.98           C  
ATOM   2499  CG  ARG A 323       9.418  30.436  86.235  1.00 51.77           C  
ATOM   2500  CD  ARG A 323      10.773  29.915  86.666  1.00 53.18           C  
ATOM   2501  NE  ARG A 323      10.696  28.710  87.493  1.00 53.62           N  
ATOM   2502  CZ  ARG A 323      10.417  27.490  87.041  1.00 53.81           C  
ATOM   2503  NH1 ARG A 323      10.183  27.284  85.749  1.00 49.72           N  
ATOM   2504  NH2 ARG A 323      10.382  26.469  87.884  1.00 55.46           N  
ATOM   2505  N   GLU A 324       6.182  32.016  89.201  1.00 54.37           N  
ATOM   2506  CA  GLU A 324       5.225  31.876  90.292  1.00 55.34           C  
ATOM   2507  C   GLU A 324       3.846  32.071  89.668  1.00 54.85           C  
ATOM   2508  O   GLU A 324       3.007  31.171  89.658  1.00 54.55           O  
ATOM   2509  CB  GLU A 324       5.499  32.960  91.340  1.00 56.24           C  
ATOM   2510  CG  GLU A 324       5.105  32.627  92.764  1.00 59.84           C  
ATOM   2511  CD  GLU A 324       5.130  33.856  93.658  1.00 62.68           C  
ATOM   2512  OE1 GLU A 324       5.072  33.704  94.896  1.00 63.39           O  
ATOM   2513  OE2 GLU A 324       5.199  34.983  93.110  1.00 65.30           O  
ATOM   2514  N   ALA A 325       3.638  33.260  89.120  1.00 53.64           N  
ATOM   2515  CA  ALA A 325       2.383  33.619  88.476  1.00 52.52           C  
ATOM   2516  C   ALA A 325       1.874  32.542  87.521  1.00 50.78           C  
ATOM   2517  O   ALA A 325       0.693  32.209  87.525  1.00 52.25           O  
ATOM   2518  CB  ALA A 325       2.555  34.952  87.729  1.00 51.31           C  
ATOM   2519  N   ILE A 326       2.751  31.998  86.693  1.00 51.84           N  
ATOM   2520  CA  ILE A 326       2.312  30.971  85.758  1.00 53.46           C  
ATOM   2521  C   ILE A 326       1.714  29.797  86.519  1.00 56.13           C  
ATOM   2522  O   ILE A 326       0.610  29.350  86.220  1.00 55.24           O  
ATOM   2523  CB  ILE A 326       3.483  30.473  84.854  1.00 51.70           C  
ATOM   2524  CG1 ILE A 326       3.985  31.618  83.975  1.00 49.95           C  
ATOM   2525  CG2 ILE A 326       3.009  29.337  83.947  1.00 48.07           C  
ATOM   2526  CD1 ILE A 326       5.024  31.196  82.968  1.00 49.16           C  
ATOM   2527  N   SER A 327       2.443  29.312  87.517  1.00 59.99           N  
ATOM   2528  CA  SER A 327       1.983  28.175  88.315  1.00 61.96           C  
ATOM   2529  C   SER A 327       0.604  28.433  88.910  1.00 62.11           C  
ATOM   2530  O   SER A 327      -0.176  27.503  89.126  1.00 60.76           O  
ATOM   2531  CB  SER A 327       2.980  27.886  89.440  1.00 62.16           C  
ATOM   2532  OG  SER A 327       2.979  28.922  90.405  1.00 61.77           O  
ATOM   2533  N   GLN A 328       0.317  29.707  89.161  1.00 63.64           N  
ATOM   2534  CA  GLN A 328      -0.954  30.137  89.740  1.00 62.55           C  
ATOM   2535  C   GLN A 328      -2.056  30.422  88.720  1.00 62.28           C  
ATOM   2536  O   GLN A 328      -3.212  30.557  89.099  1.00 65.56           O  
ATOM   2537  CB  GLN A 328      -0.742  31.397  90.589  1.00 62.30           C  
ATOM   2538  CG  GLN A 328      -0.030  31.173  91.914  1.00 64.68           C  
ATOM   2539  CD  GLN A 328       0.632  32.435  92.443  1.00 66.12           C  
ATOM   2540  OE1 GLN A 328       0.728  32.631  93.649  1.00 68.03           O  
ATOM   2541  NE2 GLN A 328       1.112  33.288  91.539  1.00 68.37           N  
ATOM   2542  N   THR A 329      -1.722  30.523  87.436  1.00 60.28           N  
ATOM   2543  CA  THR A 329      -2.755  30.815  86.445  1.00 58.24           C  
ATOM   2544  C   THR A 329      -2.805  29.857  85.242  1.00 58.53           C  
ATOM   2545  O   THR A 329      -3.883  29.454  84.812  1.00 59.21           O  
ATOM   2546  CB  THR A 329      -2.625  32.275  85.952  1.00 57.90           C  
ATOM   2547  OG1 THR A 329      -1.559  32.381  85.006  1.00 61.23           O  
ATOM   2548  CG2 THR A 329      -2.312  33.190  87.118  1.00 54.55           C  
ATOM   2549  N   PHE A 330      -1.649  29.497  84.697  1.00 58.83           N  
ATOM   2550  CA  PHE A 330      -1.584  28.582  83.560  1.00 60.66           C  
ATOM   2551  C   PHE A 330      -0.564  27.486  83.874  1.00 62.65           C  
ATOM   2552  O   PHE A 330       0.274  27.128  83.042  1.00 62.19           O  
ATOM   2553  CB  PHE A 330      -1.173  29.344  82.291  1.00 58.85           C  
ATOM   2554  CG  PHE A 330      -2.128  30.436  81.909  1.00 59.60           C  
ATOM   2555  CD1 PHE A 330      -3.403  30.131  81.441  1.00 60.73           C  
ATOM   2556  CD2 PHE A 330      -1.768  31.770  82.053  1.00 60.69           C  
ATOM   2557  CE1 PHE A 330      -4.309  31.143  81.123  1.00 61.14           C  
ATOM   2558  CE2 PHE A 330      -2.665  32.791  81.740  1.00 61.96           C  
ATOM   2559  CZ  PHE A 330      -3.941  32.475  81.274  1.00 61.90           C  
ATOM   2560  N   PRO A 331      -0.653  26.908  85.081  1.00 65.95           N  
ATOM   2561  CA  PRO A 331       0.247  25.855  85.547  1.00 66.78           C  
ATOM   2562  C   PRO A 331       0.667  24.771  84.560  1.00 67.79           C  
ATOM   2563  O   PRO A 331       1.755  24.221  84.694  1.00 68.93           O  
ATOM   2564  CB  PRO A 331      -0.493  25.286  86.762  1.00 67.10           C  
ATOM   2565  CG  PRO A 331      -1.925  25.540  86.444  1.00 66.22           C  
ATOM   2566  CD  PRO A 331      -1.857  26.948  85.931  1.00 67.63           C  
ATOM   2567  N   TRP A 332      -0.164  24.448  83.576  1.00 70.11           N  
ATOM   2568  CA  TRP A 332       0.233  23.390  82.651  1.00 74.54           C  
ATOM   2569  C   TRP A 332       1.515  23.756  81.926  1.00 76.13           C  
ATOM   2570  O   TRP A 332       2.308  22.884  81.581  1.00 77.68           O  
ATOM   2571  CB  TRP A 332      -0.865  23.087  81.621  1.00 77.52           C  
ATOM   2572  CG  TRP A 332      -1.140  24.193  80.655  1.00 82.36           C  
ATOM   2573  CD1 TRP A 332      -2.098  25.162  80.764  1.00 82.02           C  
ATOM   2574  CD2 TRP A 332      -0.438  24.458  79.435  1.00 84.93           C  
ATOM   2575  NE1 TRP A 332      -2.037  26.013  79.688  1.00 83.86           N  
ATOM   2576  CE2 TRP A 332      -1.027  25.605  78.856  1.00 85.64           C  
ATOM   2577  CE3 TRP A 332       0.632  23.839  78.773  1.00 85.27           C  
ATOM   2578  CZ2 TRP A 332      -0.580  26.148  77.643  1.00 85.78           C  
ATOM   2579  CZ3 TRP A 332       1.077  24.379  77.568  1.00 86.25           C  
ATOM   2580  CH2 TRP A 332       0.468  25.524  77.016  1.00 85.58           C  
ATOM   2581  N   VAL A 333       1.721  25.051  81.712  1.00 76.57           N  
ATOM   2582  CA  VAL A 333       2.905  25.527  81.012  1.00 76.15           C  
ATOM   2583  C   VAL A 333       4.208  25.176  81.728  1.00 77.24           C  
ATOM   2584  O   VAL A 333       5.221  24.906  81.081  1.00 77.21           O  
ATOM   2585  CB  VAL A 333       2.859  27.054  80.810  1.00 75.04           C  
ATOM   2586  CG1 VAL A 333       4.036  27.494  79.965  1.00 74.48           C  
ATOM   2587  CG2 VAL A 333       1.552  27.457  80.144  1.00 74.50           C  
ATOM   2588  N   LEU A 334       4.184  25.177  83.059  1.00 77.96           N  
ATOM   2589  CA  LEU A 334       5.375  24.861  83.843  1.00 78.58           C  
ATOM   2590  C   LEU A 334       5.567  23.379  84.156  1.00 79.86           C  
ATOM   2591  O   LEU A 334       6.285  23.035  85.099  1.00 79.52           O  
ATOM   2592  CB  LEU A 334       5.375  25.641  85.159  1.00 77.63           C  
ATOM   2593  CG  LEU A 334       5.658  27.143  85.094  1.00 79.66           C  
ATOM   2594  CD1 LEU A 334       5.870  27.690  86.505  1.00 77.56           C  
ATOM   2595  CD2 LEU A 334       6.901  27.393  84.247  1.00 81.29           C  
ATOM   2596  N   THR A 335       4.937  22.504  83.379  1.00 79.75           N  
ATOM   2597  CA  THR A 335       5.071  21.076  83.618  1.00 81.12           C  
ATOM   2598  C   THR A 335       6.533  20.671  83.709  1.00 82.68           C  
ATOM   2599  O   THR A 335       7.037  20.353  84.785  1.00 84.35           O  
ATOM   2600  CB  THR A 335       4.422  20.254  82.498  1.00 81.63           C  
ATOM   2601  OG1 THR A 335       4.741  20.849  81.234  1.00 85.47           O  
ATOM   2602  CG2 THR A 335       2.916  20.192  82.678  1.00 80.43           C  
ATOM   2603  N   CYS A 336       7.218  20.698  82.575  1.00 83.89           N  
ATOM   2604  CA  CYS A 336       8.622  20.319  82.515  1.00 85.09           C  
ATOM   2605  C   CYS A 336       9.514  21.289  83.279  1.00 85.69           C  
ATOM   2606  O   CYS A 336      10.712  21.055  83.420  1.00 86.65           O  
ATOM   2607  CB  CYS A 336       9.067  20.262  81.054  1.00 85.84           C  
ATOM   2608  SG  CYS A 336       7.873  19.453  79.965  1.00 87.57           S  
ATOM   2609  N   CYS A 337       8.924  22.368  83.781  1.00 86.94           N  
ATOM   2610  CA  CYS A 337       9.678  23.389  84.502  1.00 88.82           C  
ATOM   2611  C   CYS A 337       9.010  23.700  85.840  1.00 88.94           C  
ATOM   2612  O   CYS A 337       8.895  24.862  86.232  1.00 89.50           O  
ATOM   2613  CB  CYS A 337       9.729  24.651  83.644  1.00 89.32           C  
ATOM   2614  SG  CYS A 337       9.435  24.274  81.900  1.00 94.48           S  
ATOM   2615  N   GLN A 338       8.583  22.650  86.534  1.00 88.26           N  
ATOM   2616  CA  GLN A 338       7.897  22.775  87.814  1.00 87.01           C  
ATOM   2617  C   GLN A 338       8.397  23.870  88.755  1.00 84.30           C  
ATOM   2618  O   GLN A 338       9.593  24.004  89.009  1.00 83.07           O  
ATOM   2619  CB  GLN A 338       7.913  21.430  88.542  1.00 89.86           C  
ATOM   2620  CG  GLN A 338       6.538  21.020  89.029  1.00 94.82           C  
ATOM   2621  CD  GLN A 338       5.537  20.938  87.892  1.00 97.50           C  
ATOM   2622  OE1 GLN A 338       5.610  20.041  87.054  1.00 99.58           O  
ATOM   2623  NE2 GLN A 338       4.604  21.885  87.849  1.00 99.11           N  
ATOM   2624  N   PHE A 339       7.453  24.646  89.278  1.00 82.04           N  
ATOM   2625  CA  PHE A 339       7.760  25.736  90.194  1.00 80.04           C  
ATOM   2626  C   PHE A 339       7.820  25.278  91.650  1.00 80.03           C  
ATOM   2627  O   PHE A 339       7.207  24.279  92.033  1.00 79.04           O  
ATOM   2628  CB  PHE A 339       6.707  26.842  90.064  1.00 76.75           C  
ATOM   2629  CG  PHE A 339       6.890  27.964  91.045  1.00 73.15           C  
ATOM   2630  CD1 PHE A 339       7.976  28.824  90.939  1.00 71.43           C  
ATOM   2631  CD2 PHE A 339       5.995  28.142  92.095  1.00 71.58           C  
ATOM   2632  CE1 PHE A 339       8.170  29.844  91.863  1.00 69.51           C  
ATOM   2633  CE2 PHE A 339       6.182  29.160  93.025  1.00 70.34           C  
ATOM   2634  CZ  PHE A 339       7.271  30.012  92.907  1.00 69.66           C  
ATOM   2635  N   ASP A 340       8.567  26.024  92.454  1.00 80.65           N  
ATOM   2636  CA  ASP A 340       8.715  25.738  93.872  1.00 81.14           C  
ATOM   2637  C   ASP A 340       8.828  27.032  94.662  1.00 81.41           C  
ATOM   2638  O   ASP A 340       9.327  28.034  94.158  1.00 81.33           O  
ATOM   2639  CB  ASP A 340       9.961  24.907  94.133  1.00 81.50           C  
ATOM   2640  CG  ASP A 340      10.250  24.772  95.605  1.00 81.66           C  
ATOM   2641  OD1 ASP A 340       9.462  24.094  96.296  1.00 83.94           O  
ATOM   2642  OD2 ASP A 340      11.247  25.357  96.073  1.00 79.47           O  
ATOM   2643  N   ASP A 341       8.381  26.997  95.912  1.00 81.89           N  
ATOM   2644  CA  ASP A 341       8.417  28.173  96.773  1.00 82.79           C  
ATOM   2645  C   ASP A 341       9.821  28.745  96.920  1.00 82.95           C  
ATOM   2646  O   ASP A 341      10.010  29.962  96.889  1.00 83.34           O  
ATOM   2647  CB  ASP A 341       7.871  27.820  98.152  1.00 83.58           C  
ATOM   2648  CG  ASP A 341       6.577  27.044  98.079  1.00 85.78           C  
ATOM   2649  OD1 ASP A 341       6.070  26.614  99.142  1.00 85.89           O  
ATOM   2650  OD2 ASP A 341       6.068  26.860  96.954  1.00 86.68           O  
ATOM   2651  N   LYS A 342      10.803  27.863  97.080  1.00 82.68           N  
ATOM   2652  CA  LYS A 342      12.186  28.288  97.258  1.00 82.84           C  
ATOM   2653  C   LYS A 342      12.709  29.241  96.188  1.00 81.96           C  
ATOM   2654  O   LYS A 342      13.690  29.946  96.413  1.00 81.65           O  
ATOM   2655  CB  LYS A 342      13.110  27.068  97.350  1.00 83.20           C  
ATOM   2656  CG  LYS A 342      13.146  26.410  98.728  1.00 82.46           C  
ATOM   2657  CD  LYS A 342      14.243  25.351  98.810  1.00 82.32           C  
ATOM   2658  CE  LYS A 342      14.588  24.990 100.256  1.00 82.05           C  
ATOM   2659  NZ  LYS A 342      13.456  24.367 101.004  1.00 81.11           N  
ATOM   2660  N   GLU A 343      12.053  29.273  95.033  1.00 81.34           N  
ATOM   2661  CA  GLU A 343      12.484  30.143  93.942  1.00 81.23           C  
ATOM   2662  C   GLU A 343      12.237  31.626  94.238  1.00 81.76           C  
ATOM   2663  O   GLU A 343      12.895  32.500  93.667  1.00 81.30           O  
ATOM   2664  CB  GLU A 343      11.758  29.762  92.646  1.00 81.65           C  
ATOM   2665  CG  GLU A 343      11.767  28.270  92.317  1.00 82.12           C  
ATOM   2666  CD  GLU A 343      11.152  27.964  90.953  1.00 82.45           C  
ATOM   2667  OE1 GLU A 343      10.980  26.769  90.617  1.00 80.73           O  
ATOM   2668  OE2 GLU A 343      10.847  28.920  90.214  1.00 82.66           O  
ATOM   2669  N   THR A 344      11.299  31.908  95.135  1.00 82.68           N  
ATOM   2670  CA  THR A 344      10.945  33.282  95.477  1.00 83.87           C  
ATOM   2671  C   THR A 344      11.514  33.794  96.802  1.00 84.61           C  
ATOM   2672  O   THR A 344      11.292  34.945  97.179  1.00 82.57           O  
ATOM   2673  CB  THR A 344       9.411  33.439  95.506  1.00 83.71           C  
ATOM   2674  OG1 THR A 344       8.842  32.402  96.311  1.00 82.59           O  
ATOM   2675  CG2 THR A 344       8.843  33.344  94.095  1.00 82.58           C  
ATOM   2676  N   GLU A 345      12.255  32.941  97.497  1.00 86.50           N  
ATOM   2677  CA  GLU A 345      12.841  33.301  98.779  1.00 87.81           C  
ATOM   2678  C   GLU A 345      13.619  34.610  98.755  1.00 88.81           C  
ATOM   2679  O   GLU A 345      13.321  35.522  99.525  1.00 88.69           O  
ATOM   2680  CB  GLU A 345      13.748  32.174  99.267  1.00 88.86           C  
ATOM   2681  CG  GLU A 345      13.027  30.852  99.433  1.00 91.37           C  
ATOM   2682  CD  GLU A 345      13.957  29.734  99.842  1.00 92.25           C  
ATOM   2683  OE1 GLU A 345      14.952  29.497  99.124  1.00 93.43           O  
ATOM   2684  OE2 GLU A 345      13.693  29.091 100.878  1.00 93.17           O  
ATOM   2685  N   ASP A 346      14.613  34.704  97.874  1.00 90.33           N  
ATOM   2686  CA  ASP A 346      15.427  35.912  97.778  1.00 92.43           C  
ATOM   2687  C   ASP A 346      14.604  37.186  97.618  1.00 93.29           C  
ATOM   2688  O   ASP A 346      15.045  38.265  98.014  1.00 92.81           O  
ATOM   2689  CB  ASP A 346      16.432  35.803  96.627  1.00 93.41           C  
ATOM   2690  CG  ASP A 346      17.669  34.991  96.998  1.00 93.22           C  
ATOM   2691  OD1 ASP A 346      17.539  33.770  97.232  1.00 93.15           O  
ATOM   2692  OD2 ASP A 346      18.771  35.577  97.055  1.00 91.33           O  
ATOM   2693  N   ASP A 347      13.414  37.071  97.036  1.00 94.95           N  
ATOM   2694  CA  ASP A 347      12.553  38.240  96.869  1.00 96.82           C  
ATOM   2695  C   ASP A 347      11.842  38.547  98.181  1.00 97.84           C  
ATOM   2696  O   ASP A 347      11.542  39.702  98.485  1.00 98.24           O  
ATOM   2697  CB  ASP A 347      11.515  38.009  95.767  1.00 96.45           C  
ATOM   2698  CG  ASP A 347      12.111  38.093  94.376  1.00 95.82           C  
ATOM   2699  OD1 ASP A 347      12.734  37.110  93.926  1.00 95.23           O  
ATOM   2700  OD2 ASP A 347      11.958  39.155  93.739  1.00 96.02           O  
ATOM   2701  N   LYS A 348      11.580  37.501  98.957  1.00 98.62           N  
ATOM   2702  CA  LYS A 348      10.910  37.639 100.243  1.00 99.91           C  
ATOM   2703  C   LYS A 348      11.749  38.486 101.196  1.00101.05           C  
ATOM   2704  O   LYS A 348      11.293  39.517 101.697  1.00100.43           O  
ATOM   2705  CB  LYS A 348      10.678  36.255 100.849  1.00100.57           C  
ATOM   2706  CG  LYS A 348       9.894  35.315  99.943  1.00102.41           C  
ATOM   2707  CD  LYS A 348       9.788  33.916 100.532  1.00103.86           C  
ATOM   2708  CE  LYS A 348       8.996  32.990  99.616  1.00104.75           C  
ATOM   2709  NZ  LYS A 348       8.981  31.583 100.115  1.00104.86           N  
ATOM   2710  N   ASP A 349      12.980  38.045 101.437  1.00101.99           N  
ATOM   2711  CA  ASP A 349      13.899  38.745 102.329  1.00102.58           C  
ATOM   2712  C   ASP A 349      14.216  40.148 101.836  1.00101.91           C  
ATOM   2713  O   ASP A 349      14.253  41.098 102.619  1.00102.12           O  
ATOM   2714  CB  ASP A 349      15.202  37.956 102.471  1.00104.07           C  
ATOM   2715  CG  ASP A 349      14.997  36.599 103.118  1.00105.36           C  
ATOM   2716  OD1 ASP A 349      14.227  35.782 102.573  1.00106.35           O  
ATOM   2717  OD2 ASP A 349      15.610  36.351 104.178  1.00106.50           O  
ATOM   2718  N   ALA A 350      14.449  40.274 100.536  1.00101.29           N  
ATOM   2719  CA  ALA A 350      14.775  41.563  99.943  1.00101.45           C  
ATOM   2720  C   ALA A 350      13.706  42.615 100.211  1.00101.00           C  
ATOM   2721  O   ALA A 350      14.000  43.809 100.257  1.00100.62           O  
ATOM   2722  CB  ALA A 350      14.977  41.403  98.439  1.00101.85           C  
ATOM   2723  N   GLU A 351      12.468  42.175 100.401  1.00101.04           N  
ATOM   2724  CA  GLU A 351      11.375  43.107 100.636  1.00101.86           C  
ATOM   2725  C   GLU A 351      10.861  43.133 102.071  1.00102.47           C  
ATOM   2726  O   GLU A 351      10.284  44.132 102.505  1.00101.67           O  
ATOM   2727  CB  GLU A 351      10.235  42.809  99.658  1.00101.74           C  
ATOM   2728  CG  GLU A 351      10.649  43.008  98.203  1.00101.63           C  
ATOM   2729  CD  GLU A 351       9.634  42.478  97.214  1.00101.97           C  
ATOM   2730  OE1 GLU A 351       8.469  42.919  97.267  1.00103.23           O  
ATOM   2731  OE2 GLU A 351      10.006  41.624  96.378  1.00101.22           O  
ATOM   2732  N   THR A 352      11.065  42.046 102.809  1.00103.81           N  
ATOM   2733  CA  THR A 352      10.627  42.002 104.200  1.00106.00           C  
ATOM   2734  C   THR A 352      11.391  43.077 104.966  1.00107.93           C  
ATOM   2735  O   THR A 352      12.589  42.943 105.210  1.00107.82           O  
ATOM   2736  CB  THR A 352      10.904  40.626 104.844  1.00105.48           C  
ATOM   2737  OG1 THR A 352      12.242  40.213 104.548  1.00104.97           O  
ATOM   2738  CG2 THR A 352       9.922  39.589 104.323  1.00105.27           C  
ATOM   2739  N   GLU A 353      10.691  44.145 105.335  1.00110.61           N  
ATOM   2740  CA  GLU A 353      11.309  45.258 106.047  1.00113.38           C  
ATOM   2741  C   GLU A 353      11.615  44.952 107.513  1.00113.45           C  
ATOM   2742  O   GLU A 353      11.002  44.073 108.121  1.00113.50           O  
ATOM   2743  CB  GLU A 353      10.415  46.497 105.950  1.00116.00           C  
ATOM   2744  CG  GLU A 353      11.120  47.793 106.308  1.00120.71           C  
ATOM   2745  CD  GLU A 353      12.341  48.043 105.441  1.00123.39           C  
ATOM   2746  OE1 GLU A 353      12.178  48.174 104.208  1.00125.42           O  
ATOM   2747  OE2 GLU A 353      13.462  48.106 105.992  1.00124.14           O  
ATOM   2748  N   ILE A 354      12.573  45.691 108.068  1.00114.02           N  
ATOM   2749  CA  ILE A 354      12.994  45.529 109.457  1.00114.42           C  
ATOM   2750  C   ILE A 354      12.327  46.568 110.362  1.00115.80           C  
ATOM   2751  O   ILE A 354      12.466  47.773 110.151  1.00115.70           O  
ATOM   2752  CB  ILE A 354      14.521  45.668 109.582  1.00113.54           C  
ATOM   2753  CG1 ILE A 354      14.972  46.981 108.933  1.00113.16           C  
ATOM   2754  CG2 ILE A 354      15.206  44.481 108.923  1.00112.00           C  
ATOM   2755  CD1 ILE A 354      16.444  47.287 109.105  1.00112.25           C  
ATOM   2756  N   PRO A 355      11.600  46.105 111.393  1.00116.91           N  
ATOM   2757  CA  PRO A 355      10.886  46.952 112.357  1.00117.92           C  
ATOM   2758  C   PRO A 355      11.740  47.682 113.391  1.00118.54           C  
ATOM   2759  O   PRO A 355      11.796  47.275 114.552  1.00119.15           O  
ATOM   2760  CB  PRO A 355       9.920  45.972 113.009  1.00118.18           C  
ATOM   2761  CG  PRO A 355      10.725  44.714 113.047  1.00117.32           C  
ATOM   2762  CD  PRO A 355      11.336  44.679 111.661  1.00116.98           C  
ATOM   2763  N   ALA A 356      12.381  48.772 112.979  1.00118.86           N  
ATOM   2764  CA  ALA A 356      13.223  49.555 113.885  1.00119.73           C  
ATOM   2765  C   ALA A 356      14.401  48.723 114.377  1.00120.15           C  
ATOM   2766  O   ALA A 356      14.530  48.456 115.575  1.00120.43           O  
ATOM   2767  CB  ALA A 356      12.396  50.045 115.072  1.00120.25           C  
ATOM   2768  N   GLY A 357      15.264  48.325 113.446  1.00120.15           N  
ATOM   2769  CA  GLY A 357      16.412  47.510 113.801  1.00118.99           C  
ATOM   2770  C   GLY A 357      15.927  46.144 114.243  1.00118.85           C  
ATOM   2771  O   GLY A 357      16.648  45.399 114.899  1.00119.19           O  
ATOM   2772  N   GLU A 358      14.690  45.827 113.872  1.00119.14           N  
ATOM   2773  CA  GLU A 358      14.051  44.563 114.218  1.00119.91           C  
ATOM   2774  C   GLU A 358      13.729  44.531 115.707  1.00119.62           C  
ATOM   2775  O   GLU A 358      12.599  44.129 116.055  1.00119.27           O  
ATOM   2776  CB  GLU A 358      14.948  43.375 113.853  1.00121.57           C  
ATOM   2777  CG  GLU A 358      14.177  42.157 113.344  1.00124.08           C  
ATOM   2778  CD  GLU A 358      13.169  41.621 114.349  1.00125.68           C  
ATOM   2779  OE1 GLU A 358      13.584  40.959 115.321  1.00126.70           O  
ATOM   2780  OE2 GLU A 358      11.956  41.869 114.165  1.00125.65           O  
TER    2781      GLU A 358                                                      
ATOM   2782  N   GLU B   9      22.304  24.402  40.140  1.00 83.24           N  
ATOM   2783  CA  GLU B   9      21.342  25.328  40.809  1.00 83.81           C  
ATOM   2784  C   GLU B   9      20.449  26.089  39.833  1.00 82.40           C  
ATOM   2785  O   GLU B   9      19.340  26.495  40.193  1.00 82.15           O  
ATOM   2786  CB  GLU B   9      22.096  26.311  41.699  1.00 87.06           C  
ATOM   2787  CG  GLU B   9      22.539  25.708  43.023  1.00 93.97           C  
ATOM   2788  CD  GLU B   9      21.370  25.168  43.837  1.00 96.59           C  
ATOM   2789  OE1 GLU B   9      20.376  25.907  44.009  1.00 97.85           O  
ATOM   2790  OE2 GLU B   9      21.446  24.013  44.310  1.00 97.87           O  
ATOM   2791  N   THR B  10      20.933  26.304  38.611  1.00 79.27           N  
ATOM   2792  CA  THR B  10      20.140  26.984  37.587  1.00 74.38           C  
ATOM   2793  C   THR B  10      20.224  26.155  36.315  1.00 71.88           C  
ATOM   2794  O   THR B  10      20.894  25.117  36.282  1.00 71.75           O  
ATOM   2795  CB  THR B  10      20.645  28.413  37.273  1.00 73.69           C  
ATOM   2796  OG1 THR B  10      21.552  28.377  36.163  1.00 74.25           O  
ATOM   2797  CG2 THR B  10      21.349  29.003  38.472  1.00 75.38           C  
ATOM   2798  N   TRP B  11      19.552  26.622  35.268  1.00 67.69           N  
ATOM   2799  CA  TRP B  11      19.526  25.911  33.993  1.00 63.56           C  
ATOM   2800  C   TRP B  11      20.172  26.703  32.865  1.00 61.31           C  
ATOM   2801  O   TRP B  11      20.612  26.135  31.873  1.00 62.13           O  
ATOM   2802  CB  TRP B  11      18.083  25.616  33.593  1.00 62.44           C  
ATOM   2803  CG  TRP B  11      17.333  26.846  33.181  1.00 60.33           C  
ATOM   2804  CD1 TRP B  11      16.608  27.680  33.982  1.00 60.73           C  
ATOM   2805  CD2 TRP B  11      17.260  27.395  31.864  1.00 60.54           C  
ATOM   2806  NE1 TRP B  11      16.085  28.715  33.244  1.00 57.85           N  
ATOM   2807  CE2 TRP B  11      16.468  28.565  31.939  1.00 60.32           C  
ATOM   2808  CE3 TRP B  11      17.788  27.013  30.624  1.00 59.97           C  
ATOM   2809  CZ2 TRP B  11      16.190  29.356  30.820  1.00 62.96           C  
ATOM   2810  CZ3 TRP B  11      17.513  27.800  29.509  1.00 60.85           C  
ATOM   2811  CH2 TRP B  11      16.722  28.956  29.616  1.00 62.98           C  
ATOM   2812  N   TRP B  12      20.198  28.020  33.007  1.00 58.11           N  
ATOM   2813  CA  TRP B  12      20.756  28.882  31.977  1.00 51.93           C  
ATOM   2814  C   TRP B  12      22.261  29.037  32.157  1.00 49.75           C  
ATOM   2815  O   TRP B  12      22.968  29.429  31.232  1.00 51.39           O  
ATOM   2816  CB  TRP B  12      20.074  30.262  32.033  1.00 45.46           C  
ATOM   2817  CG  TRP B  12      20.140  30.845  33.398  1.00 40.73           C  
ATOM   2818  CD1 TRP B  12      19.221  30.692  34.407  1.00 38.15           C  
ATOM   2819  CD2 TRP B  12      21.274  31.489  33.988  1.00 41.17           C  
ATOM   2820  NE1 TRP B  12      19.726  31.189  35.593  1.00 36.71           N  
ATOM   2821  CE2 TRP B  12      20.983  31.682  35.365  1.00 39.79           C  
ATOM   2822  CE3 TRP B  12      22.512  31.909  33.491  1.00 35.52           C  
ATOM   2823  CZ2 TRP B  12      21.886  32.274  36.243  1.00 39.19           C  
ATOM   2824  CZ3 TRP B  12      23.413  32.495  34.364  1.00 38.83           C  
ATOM   2825  CH2 TRP B  12      23.097  32.673  35.729  1.00 39.09           C  
ATOM   2826  N   TYR B  13      22.752  28.709  33.345  1.00 49.55           N  
ATOM   2827  CA  TYR B  13      24.173  28.862  33.653  1.00 49.59           C  
ATOM   2828  C   TYR B  13      25.157  28.281  32.652  1.00 48.12           C  
ATOM   2829  O   TYR B  13      25.017  27.148  32.207  1.00 50.13           O  
ATOM   2830  CB  TYR B  13      24.495  28.289  35.047  1.00 47.04           C  
ATOM   2831  CG  TYR B  13      25.945  28.487  35.426  1.00 48.25           C  
ATOM   2832  CD1 TYR B  13      26.828  27.408  35.468  1.00 47.75           C  
ATOM   2833  CD2 TYR B  13      26.456  29.768  35.656  1.00 45.76           C  
ATOM   2834  CE1 TYR B  13      28.184  27.598  35.721  1.00 46.87           C  
ATOM   2835  CE2 TYR B  13      27.804  29.968  35.908  1.00 46.38           C  
ATOM   2836  CZ  TYR B  13      28.662  28.879  35.938  1.00 48.59           C  
ATOM   2837  OH  TYR B  13      30.003  29.073  36.182  1.00 49.16           O  
ATOM   2838  N   ASN B  14      26.160  29.071  32.293  1.00 47.57           N  
ATOM   2839  CA  ASN B  14      27.179  28.608  31.367  1.00 46.26           C  
ATOM   2840  C   ASN B  14      28.541  28.960  31.939  1.00 45.83           C  
ATOM   2841  O   ASN B  14      28.824  30.109  32.246  1.00 44.78           O  
ATOM   2842  CB  ASN B  14      26.998  29.241  29.983  1.00 46.46           C  
ATOM   2843  CG  ASN B  14      27.760  28.493  28.907  1.00 49.15           C  
ATOM   2844  OD1 ASN B  14      28.992  28.440  28.933  1.00 52.24           O  
ATOM   2845  ND2 ASN B  14      27.037  27.899  27.964  1.00 45.65           N  
ATOM   2846  N   PRO B  15      29.400  27.956  32.111  1.00 46.63           N  
ATOM   2847  CA  PRO B  15      30.739  28.178  32.661  1.00 45.45           C  
ATOM   2848  C   PRO B  15      31.645  29.001  31.760  1.00 42.59           C  
ATOM   2849  O   PRO B  15      32.621  29.582  32.211  1.00 42.09           O  
ATOM   2850  CB  PRO B  15      31.255  26.752  32.884  1.00 46.63           C  
ATOM   2851  CG  PRO B  15      30.561  25.966  31.818  1.00 46.49           C  
ATOM   2852  CD  PRO B  15      29.162  26.524  31.849  1.00 45.31           C  
ATOM   2853  N   SER B  16      31.295  29.069  30.483  1.00 44.54           N  
ATOM   2854  CA  SER B  16      32.089  29.796  29.493  1.00 43.96           C  
ATOM   2855  C   SER B  16      31.643  31.234  29.194  1.00 43.92           C  
ATOM   2856  O   SER B  16      32.473  32.131  29.055  1.00 43.50           O  
ATOM   2857  CB  SER B  16      32.103  29.006  28.178  1.00 46.29           C  
ATOM   2858  OG  SER B  16      32.529  27.673  28.363  1.00 47.82           O  
ATOM   2859  N   ILE B  17      30.336  31.443  29.096  1.00 42.14           N  
ATOM   2860  CA  ILE B  17      29.794  32.750  28.753  1.00 40.21           C  
ATOM   2861  C   ILE B  17      28.828  33.299  29.800  1.00 39.71           C  
ATOM   2862  O   ILE B  17      27.976  32.566  30.280  1.00 42.90           O  
ATOM   2863  CB  ILE B  17      29.057  32.642  27.403  1.00 40.72           C  
ATOM   2864  CG1 ILE B  17      29.980  31.997  26.370  1.00 39.43           C  
ATOM   2865  CG2 ILE B  17      28.621  33.999  26.922  1.00 41.08           C  
ATOM   2866  CD1 ILE B  17      29.244  31.407  25.181  1.00 38.62           C  
ATOM   2867  N   VAL B  18      28.963  34.576  30.161  1.00 39.38           N  
ATOM   2868  CA  VAL B  18      28.056  35.175  31.148  1.00 38.41           C  
ATOM   2869  C   VAL B  18      26.732  35.439  30.443  1.00 36.59           C  
ATOM   2870  O   VAL B  18      26.665  36.241  29.526  1.00 39.47           O  
ATOM   2871  CB  VAL B  18      28.562  36.539  31.711  1.00 40.14           C  
ATOM   2872  CG1 VAL B  18      27.533  37.104  32.663  1.00 35.70           C  
ATOM   2873  CG2 VAL B  18      29.909  36.388  32.431  1.00 32.70           C  
ATOM   2874  N   VAL B  19      25.682  34.749  30.855  1.00 38.41           N  
ATOM   2875  CA  VAL B  19      24.390  34.938  30.231  1.00 38.92           C  
ATOM   2876  C   VAL B  19      23.771  36.226  30.745  1.00 40.71           C  
ATOM   2877  O   VAL B  19      23.820  36.520  31.941  1.00 41.39           O  
ATOM   2878  CB  VAL B  19      23.448  33.769  30.519  1.00 37.69           C  
ATOM   2879  CG1 VAL B  19      22.075  34.061  29.938  1.00 43.58           C  
ATOM   2880  CG2 VAL B  19      24.000  32.495  29.907  1.00 37.88           C  
ATOM   2881  N   HIS B  20      23.202  37.009  29.840  1.00 41.43           N  
ATOM   2882  CA  HIS B  20      22.596  38.260  30.242  1.00 41.22           C  
ATOM   2883  C   HIS B  20      21.437  37.947  31.159  1.00 41.07           C  
ATOM   2884  O   HIS B  20      20.688  36.993  30.917  1.00 41.23           O  
ATOM   2885  CB  HIS B  20      22.102  39.037  29.026  1.00 41.62           C  
ATOM   2886  CG  HIS B  20      21.798  40.469  29.323  1.00 44.70           C  
ATOM   2887  ND1 HIS B  20      20.633  40.870  29.938  1.00 42.36           N  
ATOM   2888  CD2 HIS B  20      22.534  41.591  29.143  1.00 43.31           C  
ATOM   2889  CE1 HIS B  20      20.668  42.176  30.126  1.00 43.40           C  
ATOM   2890  NE2 HIS B  20      21.811  42.637  29.655  1.00 42.29           N  
ATOM   2891  N   PRO B  21      21.279  38.731  32.234  1.00 38.57           N  
ATOM   2892  CA  PRO B  21      20.206  38.561  33.212  1.00 39.98           C  
ATOM   2893  C   PRO B  21      18.836  38.403  32.546  1.00 42.86           C  
ATOM   2894  O   PRO B  21      18.029  37.568  32.957  1.00 44.27           O  
ATOM   2895  CB  PRO B  21      20.299  39.839  34.035  1.00 39.49           C  
ATOM   2896  CG  PRO B  21      21.755  40.126  34.050  1.00 33.20           C  
ATOM   2897  CD  PRO B  21      22.112  39.890  32.586  1.00 41.57           C  
ATOM   2898  N   HIS B  22      18.582  39.202  31.512  1.00 42.75           N  
ATOM   2899  CA  HIS B  22      17.308  39.148  30.807  1.00 43.56           C  
ATOM   2900  C   HIS B  22      16.905  37.742  30.435  1.00 47.36           C  
ATOM   2901  O   HIS B  22      15.724  37.389  30.460  1.00 49.10           O  
ATOM   2902  CB  HIS B  22      17.349  39.966  29.519  1.00 40.54           C  
ATOM   2903  CG  HIS B  22      16.110  39.830  28.693  1.00 40.94           C  
ATOM   2904  ND1 HIS B  22      14.857  40.096  29.191  1.00 41.46           N  
ATOM   2905  CD2 HIS B  22      15.926  39.430  27.414  1.00 45.73           C  
ATOM   2906  CE1 HIS B  22      13.952  39.867  28.257  1.00 41.19           C  
ATOM   2907  NE2 HIS B  22      14.575  39.461  27.168  1.00 41.99           N  
ATOM   2908  N   TRP B  23      17.893  36.943  30.066  1.00 48.97           N  
ATOM   2909  CA  TRP B  23      17.624  35.588  29.643  1.00 46.79           C  
ATOM   2910  C   TRP B  23      17.479  34.651  30.821  1.00 47.35           C  
ATOM   2911  O   TRP B  23      16.802  33.631  30.725  1.00 50.24           O  
ATOM   2912  CB  TRP B  23      18.744  35.104  28.725  1.00 46.97           C  
ATOM   2913  CG  TRP B  23      18.869  35.883  27.432  1.00 44.63           C  
ATOM   2914  CD1 TRP B  23      19.988  36.491  26.952  1.00 42.62           C  
ATOM   2915  CD2 TRP B  23      17.851  36.087  26.445  1.00 43.07           C  
ATOM   2916  NE1 TRP B  23      19.738  37.057  25.730  1.00 41.04           N  
ATOM   2917  CE2 TRP B  23      18.430  36.826  25.397  1.00 42.05           C  
ATOM   2918  CE3 TRP B  23      16.504  35.715  26.345  1.00 42.67           C  
ATOM   2919  CZ2 TRP B  23      17.707  37.205  24.257  1.00 44.83           C  
ATOM   2920  CZ3 TRP B  23      15.790  36.090  25.213  1.00 43.68           C  
ATOM   2921  CH2 TRP B  23      16.397  36.830  24.184  1.00 44.34           C  
ATOM   2922  N   ARG B  24      18.097  35.000  31.941  1.00 46.45           N  
ATOM   2923  CA  ARG B  24      18.028  34.148  33.121  1.00 44.39           C  
ATOM   2924  C   ARG B  24      16.666  34.159  33.785  1.00 46.35           C  
ATOM   2925  O   ARG B  24      16.297  33.195  34.441  1.00 45.60           O  
ATOM   2926  CB  ARG B  24      19.055  34.574  34.159  1.00 41.15           C  
ATOM   2927  CG  ARG B  24      20.361  35.068  33.603  1.00 39.90           C  
ATOM   2928  CD  ARG B  24      21.260  35.547  34.729  1.00 38.98           C  
ATOM   2929  NE  ARG B  24      22.440  36.218  34.205  1.00 42.69           N  
ATOM   2930  CZ  ARG B  24      23.435  36.690  34.945  1.00 42.36           C  
ATOM   2931  NH1 ARG B  24      23.407  36.567  36.267  1.00 42.96           N  
ATOM   2932  NH2 ARG B  24      24.457  37.297  34.355  1.00 41.88           N  
ATOM   2933  N   GLU B  25      15.911  35.236  33.619  1.00 47.45           N  
ATOM   2934  CA  GLU B  25      14.619  35.308  34.276  1.00 49.56           C  
ATOM   2935  C   GLU B  25      13.551  34.377  33.733  1.00 49.86           C  
ATOM   2936  O   GLU B  25      12.496  34.221  34.336  1.00 50.49           O  
ATOM   2937  CB  GLU B  25      14.093  36.741  34.260  1.00 51.14           C  
ATOM   2938  CG  GLU B  25      13.610  37.239  32.932  1.00 50.38           C  
ATOM   2939  CD  GLU B  25      13.069  38.636  33.044  1.00 50.88           C  
ATOM   2940  OE1 GLU B  25      13.821  39.518  33.514  1.00 49.34           O  
ATOM   2941  OE2 GLU B  25      11.900  38.854  32.672  1.00 54.16           O  
ATOM   2942  N   PHE B  26      13.825  33.733  32.613  1.00 51.23           N  
ATOM   2943  CA  PHE B  26      12.834  32.842  32.024  1.00 53.68           C  
ATOM   2944  C   PHE B  26      12.958  31.392  32.431  1.00 54.61           C  
ATOM   2945  O   PHE B  26      14.002  30.951  32.926  1.00 53.79           O  
ATOM   2946  CB  PHE B  26      12.890  32.947  30.505  1.00 51.70           C  
ATOM   2947  CG  PHE B  26      12.548  34.301  30.005  1.00 55.26           C  
ATOM   2948  CD1 PHE B  26      11.222  34.710  29.928  1.00 51.09           C  
ATOM   2949  CD2 PHE B  26      13.554  35.204  29.681  1.00 55.97           C  
ATOM   2950  CE1 PHE B  26      10.900  35.996  29.540  1.00 52.13           C  
ATOM   2951  CE2 PHE B  26      13.241  36.500  29.290  1.00 57.40           C  
ATOM   2952  CZ  PHE B  26      11.912  36.896  29.221  1.00 55.46           C  
ATOM   2953  N   ASP B  27      11.868  30.660  32.222  1.00 55.35           N  
ATOM   2954  CA  ASP B  27      11.828  29.244  32.530  1.00 55.46           C  
ATOM   2955  C   ASP B  27      12.419  28.502  31.349  1.00 55.72           C  
ATOM   2956  O   ASP B  27      12.363  28.983  30.219  1.00 57.21           O  
ATOM   2957  CB  ASP B  27      10.390  28.785  32.743  1.00 54.62           C  
ATOM   2958  CG  ASP B  27       9.852  29.175  34.091  1.00 54.71           C  
ATOM   2959  OD1 ASP B  27      10.607  29.765  34.895  1.00 57.07           O  
ATOM   2960  OD2 ASP B  27       8.671  28.883  34.347  1.00 53.78           O  
ATOM   2961  N   GLN B  28      12.987  27.336  31.609  1.00 54.29           N  
ATOM   2962  CA  GLN B  28      13.572  26.545  30.550  1.00 54.65           C  
ATOM   2963  C   GLN B  28      12.456  25.925  29.710  1.00 54.63           C  
ATOM   2964  O   GLN B  28      11.485  25.398  30.258  1.00 56.93           O  
ATOM   2965  CB  GLN B  28      14.469  25.463  31.151  1.00 55.75           C  
ATOM   2966  CG  GLN B  28      15.117  24.529  30.148  1.00 58.96           C  
ATOM   2967  CD  GLN B  28      16.343  23.854  30.731  1.00 60.74           C  
ATOM   2968  OE1 GLN B  28      16.395  23.577  31.924  1.00 63.03           O  
ATOM   2969  NE2 GLN B  28      17.334  23.577  29.887  1.00 63.41           N  
ATOM   2970  N   VAL B  29      12.586  26.013  28.384  1.00 52.19           N  
ATOM   2971  CA  VAL B  29      11.596  25.459  27.474  1.00 50.65           C  
ATOM   2972  C   VAL B  29      11.717  23.942  27.469  1.00 53.21           C  
ATOM   2973  O   VAL B  29      12.714  23.394  27.931  1.00 56.29           O  
ATOM   2974  CB  VAL B  29      11.797  25.985  26.037  1.00 50.43           C  
ATOM   2975  CG1 VAL B  29      11.709  27.483  26.026  1.00 51.66           C  
ATOM   2976  CG2 VAL B  29      13.139  25.541  25.491  1.00 50.85           C  
ATOM   2977  N   PRO B  30      10.698  23.245  26.943  1.00 53.97           N  
ATOM   2978  CA  PRO B  30      10.646  21.778  26.858  1.00 53.78           C  
ATOM   2979  C   PRO B  30      11.681  21.188  25.893  1.00 52.53           C  
ATOM   2980  O   PRO B  30      11.980  21.784  24.861  1.00 54.13           O  
ATOM   2981  CB  PRO B  30       9.218  21.508  26.382  1.00 55.15           C  
ATOM   2982  CG  PRO B  30       8.468  22.724  26.815  1.00 54.57           C  
ATOM   2983  CD  PRO B  30       9.426  23.826  26.493  1.00 52.56           C  
ATOM   2984  N   ASP B  31      12.194  20.002  26.215  1.00 49.39           N  
ATOM   2985  CA  ASP B  31      13.197  19.349  25.379  1.00 48.42           C  
ATOM   2986  C   ASP B  31      12.801  19.342  23.910  1.00 48.71           C  
ATOM   2987  O   ASP B  31      13.644  19.511  23.028  1.00 47.03           O  
ATOM   2988  CB  ASP B  31      13.419  17.898  25.803  1.00 48.10           C  
ATOM   2989  CG  ASP B  31      13.603  17.739  27.289  1.00 49.05           C  
ATOM   2990  OD1 ASP B  31      14.224  18.618  27.923  1.00 52.69           O  
ATOM   2991  OD2 ASP B  31      13.130  16.716  27.823  1.00 50.36           O  
ATOM   2992  N   ALA B  32      11.513  19.121  23.663  1.00 48.79           N  
ATOM   2993  CA  ALA B  32      10.999  19.053  22.310  1.00 48.68           C  
ATOM   2994  C   ALA B  32      11.315  20.316  21.521  1.00 49.63           C  
ATOM   2995  O   ALA B  32      11.644  20.237  20.331  1.00 50.04           O  
ATOM   2996  CB  ALA B  32       9.499  18.798  22.338  1.00 48.70           C  
ATOM   2997  N   VAL B  33      11.224  21.476  22.171  1.00 48.04           N  
ATOM   2998  CA  VAL B  33      11.522  22.731  21.493  1.00 47.60           C  
ATOM   2999  C   VAL B  33      12.993  22.708  21.090  1.00 47.40           C  
ATOM   3000  O   VAL B  33      13.338  22.928  19.926  1.00 47.69           O  
ATOM   3001  CB  VAL B  33      11.263  23.947  22.406  1.00 47.18           C  
ATOM   3002  CG1 VAL B  33      11.679  25.224  21.700  1.00 44.44           C  
ATOM   3003  CG2 VAL B  33       9.780  24.014  22.770  1.00 47.70           C  
ATOM   3004  N   TYR B  34      13.853  22.426  22.060  1.00 45.52           N  
ATOM   3005  CA  TYR B  34      15.289  22.346  21.813  1.00 47.35           C  
ATOM   3006  C   TYR B  34      15.597  21.373  20.677  1.00 49.31           C  
ATOM   3007  O   TYR B  34      16.275  21.726  19.711  1.00 50.52           O  
ATOM   3008  CB  TYR B  34      16.010  21.864  23.062  1.00 43.67           C  
ATOM   3009  CG  TYR B  34      16.304  22.928  24.083  1.00 43.84           C  
ATOM   3010  CD1 TYR B  34      17.304  23.864  23.865  1.00 39.47           C  
ATOM   3011  CD2 TYR B  34      15.638  22.948  25.306  1.00 46.62           C  
ATOM   3012  CE1 TYR B  34      17.645  24.786  24.838  1.00 46.16           C  
ATOM   3013  CE2 TYR B  34      15.974  23.865  26.293  1.00 49.11           C  
ATOM   3014  CZ  TYR B  34      16.981  24.779  26.051  1.00 49.27           C  
ATOM   3015  OH  TYR B  34      17.345  25.678  27.034  1.00 52.87           O  
ATOM   3016  N   TYR B  35      15.096  20.147  20.814  1.00 50.51           N  
ATOM   3017  CA  TYR B  35      15.307  19.101  19.828  1.00 51.36           C  
ATOM   3018  C   TYR B  35      14.786  19.532  18.457  1.00 50.25           C  
ATOM   3019  O   TYR B  35      15.415  19.266  17.432  1.00 49.72           O  
ATOM   3020  CB  TYR B  35      14.627  17.811  20.300  1.00 56.06           C  
ATOM   3021  CG  TYR B  35      15.165  17.293  21.625  1.00 61.55           C  
ATOM   3022  CD1 TYR B  35      14.532  16.251  22.303  1.00 66.29           C  
ATOM   3023  CD2 TYR B  35      16.306  17.854  22.206  1.00 66.24           C  
ATOM   3024  CE1 TYR B  35      15.020  15.783  23.531  1.00 69.99           C  
ATOM   3025  CE2 TYR B  35      16.805  17.399  23.428  1.00 68.92           C  
ATOM   3026  CZ  TYR B  35      16.155  16.363  24.085  1.00 72.11           C  
ATOM   3027  OH  TYR B  35      16.637  15.914  25.299  1.00 74.11           O  
ATOM   3028  N   SER B  36      13.646  20.217  18.448  1.00 50.10           N  
ATOM   3029  CA  SER B  36      13.062  20.691  17.209  1.00 48.16           C  
ATOM   3030  C   SER B  36      13.978  21.731  16.600  1.00 46.23           C  
ATOM   3031  O   SER B  36      14.178  21.762  15.382  1.00 41.77           O  
ATOM   3032  CB  SER B  36      11.687  21.310  17.462  1.00 48.53           C  
ATOM   3033  OG  SER B  36      10.783  20.334  17.943  1.00 51.47           O  
ATOM   3034  N   LEU B  37      14.528  22.584  17.459  1.00 45.05           N  
ATOM   3035  CA  LEU B  37      15.441  23.634  17.016  1.00 48.30           C  
ATOM   3036  C   LEU B  37      16.683  23.006  16.411  1.00 49.38           C  
ATOM   3037  O   LEU B  37      17.111  23.388  15.327  1.00 49.60           O  
ATOM   3038  CB  LEU B  37      15.842  24.530  18.195  1.00 47.92           C  
ATOM   3039  CG  LEU B  37      14.722  25.429  18.736  1.00 47.71           C  
ATOM   3040  CD1 LEU B  37      15.119  26.046  20.072  1.00 44.52           C  
ATOM   3041  CD2 LEU B  37      14.408  26.498  17.686  1.00 43.99           C  
ATOM   3042  N   GLY B  38      17.243  22.027  17.116  1.00 50.93           N  
ATOM   3043  CA  GLY B  38      18.447  21.362  16.649  1.00 52.00           C  
ATOM   3044  C   GLY B  38      18.367  20.771  15.253  1.00 53.27           C  
ATOM   3045  O   GLY B  38      19.258  20.981  14.430  1.00 52.43           O  
ATOM   3046  N   ILE B  39      17.306  20.019  14.984  1.00 55.87           N  
ATOM   3047  CA  ILE B  39      17.151  19.397  13.684  1.00 57.35           C  
ATOM   3048  C   ILE B  39      16.725  20.403  12.637  1.00 55.08           C  
ATOM   3049  O   ILE B  39      17.093  20.279  11.471  1.00 59.99           O  
ATOM   3050  CB  ILE B  39      16.147  18.212  13.725  1.00 61.19           C  
ATOM   3051  CG1 ILE B  39      14.868  18.621  14.445  1.00 67.43           C  
ATOM   3052  CG2 ILE B  39      16.780  17.028  14.442  1.00 61.78           C  
ATOM   3053  CD1 ILE B  39      13.859  17.483  14.579  1.00 72.53           C  
ATOM   3054  N   PHE B  40      15.964  21.410  13.039  1.00 51.86           N  
ATOM   3055  CA  PHE B  40      15.537  22.425  12.084  1.00 48.44           C  
ATOM   3056  C   PHE B  40      16.773  23.088  11.495  1.00 46.23           C  
ATOM   3057  O   PHE B  40      16.943  23.162  10.280  1.00 44.35           O  
ATOM   3058  CB  PHE B  40      14.694  23.512  12.752  1.00 48.43           C  
ATOM   3059  CG  PHE B  40      14.396  24.664  11.844  1.00 45.42           C  
ATOM   3060  CD1 PHE B  40      13.421  24.556  10.861  1.00 46.42           C  
ATOM   3061  CD2 PHE B  40      15.150  25.836  11.911  1.00 43.67           C  
ATOM   3062  CE1 PHE B  40      13.204  25.603   9.951  1.00 47.00           C  
ATOM   3063  CE2 PHE B  40      14.943  26.886  11.008  1.00 40.81           C  
ATOM   3064  CZ  PHE B  40      13.973  26.769  10.030  1.00 41.94           C  
ATOM   3065  N   ILE B  41      17.635  23.577  12.376  1.00 44.14           N  
ATOM   3066  CA  ILE B  41      18.846  24.236  11.947  1.00 44.74           C  
ATOM   3067  C   ILE B  41      19.790  23.217  11.315  1.00 45.94           C  
ATOM   3068  O   ILE B  41      20.568  23.562  10.428  1.00 47.15           O  
ATOM   3069  CB  ILE B  41      19.538  24.944  13.127  1.00 43.08           C  
ATOM   3070  CG1 ILE B  41      20.562  25.955  12.610  1.00 43.91           C  
ATOM   3071  CG2 ILE B  41      20.191  23.924  14.027  1.00 46.35           C  
ATOM   3072  CD1 ILE B  41      19.953  27.071  11.732  1.00 38.97           C  
ATOM   3073  N   GLY B  42      19.715  21.964  11.760  1.00 44.76           N  
ATOM   3074  CA  GLY B  42      20.565  20.934  11.185  1.00 45.53           C  
ATOM   3075  C   GLY B  42      20.218  20.753   9.711  1.00 48.52           C  
ATOM   3076  O   GLY B  42      21.097  20.671   8.841  1.00 49.35           O  
ATOM   3077  N   ILE B  43      18.919  20.699   9.431  1.00 47.93           N  
ATOM   3078  CA  ILE B  43      18.440  20.549   8.071  1.00 45.84           C  
ATOM   3079  C   ILE B  43      18.810  21.768   7.229  1.00 46.77           C  
ATOM   3080  O   ILE B  43      19.012  21.650   6.019  1.00 47.30           O  
ATOM   3081  CB  ILE B  43      16.912  20.329   8.046  1.00 44.79           C  
ATOM   3082  CG1 ILE B  43      16.592  18.984   8.694  1.00 44.07           C  
ATOM   3083  CG2 ILE B  43      16.386  20.364   6.619  1.00 37.49           C  
ATOM   3084  CD1 ILE B  43      15.152  18.593   8.610  1.00 48.30           C  
ATOM   3085  N   CYS B  44      18.900  22.935   7.865  1.00 49.85           N  
ATOM   3086  CA  CYS B  44      19.286  24.152   7.158  1.00 49.73           C  
ATOM   3087  C   CYS B  44      20.734  24.017   6.703  1.00 47.56           C  
ATOM   3088  O   CYS B  44      21.095  24.437   5.600  1.00 47.44           O  
ATOM   3089  CB  CYS B  44      19.148  25.380   8.056  1.00 52.09           C  
ATOM   3090  SG  CYS B  44      17.445  25.938   8.275  1.00 51.05           S  
ATOM   3091  N   GLY B  45      21.558  23.421   7.557  1.00 44.79           N  
ATOM   3092  CA  GLY B  45      22.942  23.210   7.198  1.00 42.68           C  
ATOM   3093  C   GLY B  45      22.979  22.283   5.993  1.00 45.04           C  
ATOM   3094  O   GLY B  45      23.670  22.545   5.011  1.00 46.05           O  
ATOM   3095  N   ILE B  46      22.215  21.199   6.049  1.00 43.95           N  
ATOM   3096  CA  ILE B  46      22.199  20.248   4.953  1.00 43.20           C  
ATOM   3097  C   ILE B  46      21.766  20.904   3.652  1.00 44.11           C  
ATOM   3098  O   ILE B  46      22.515  20.926   2.676  1.00 46.07           O  
ATOM   3099  CB  ILE B  46      21.257  19.066   5.245  1.00 43.76           C  
ATOM   3100  CG1 ILE B  46      21.813  18.230   6.393  1.00 44.50           C  
ATOM   3101  CG2 ILE B  46      21.084  18.221   3.999  1.00 42.95           C  
ATOM   3102  CD1 ILE B  46      20.865  17.173   6.888  1.00 46.27           C  
ATOM   3103  N   ILE B  47      20.553  21.443   3.646  1.00 44.46           N  
ATOM   3104  CA  ILE B  47      20.016  22.086   2.460  1.00 43.26           C  
ATOM   3105  C   ILE B  47      20.853  23.290   2.032  1.00 43.96           C  
ATOM   3106  O   ILE B  47      21.045  23.526   0.827  1.00 45.33           O  
ATOM   3107  CB  ILE B  47      18.567  22.505   2.690  1.00 40.31           C  
ATOM   3108  CG1 ILE B  47      17.720  21.260   2.935  1.00 41.90           C  
ATOM   3109  CG2 ILE B  47      18.050  23.276   1.509  1.00 37.12           C  
ATOM   3110  CD1 ILE B  47      16.277  21.535   3.274  1.00 48.58           C  
ATOM   3111  N   GLY B  48      21.356  24.036   3.014  1.00 40.97           N  
ATOM   3112  CA  GLY B  48      22.173  25.199   2.725  1.00 39.09           C  
ATOM   3113  C   GLY B  48      23.503  24.855   2.086  1.00 37.35           C  
ATOM   3114  O   GLY B  48      23.825  25.327   1.001  1.00 35.92           O  
ATOM   3115  N   CYS B  49      24.288  24.022   2.752  1.00 40.48           N  
ATOM   3116  CA  CYS B  49      25.589  23.637   2.214  1.00 40.55           C  
ATOM   3117  C   CYS B  49      25.458  22.891   0.899  1.00 40.32           C  
ATOM   3118  O   CYS B  49      26.242  23.109  -0.017  1.00 41.06           O  
ATOM   3119  CB  CYS B  49      26.349  22.777   3.219  1.00 38.78           C  
ATOM   3120  SG  CYS B  49      26.877  23.686   4.676  1.00 40.40           S  
ATOM   3121  N   GLY B  50      24.463  22.015   0.809  1.00 40.97           N  
ATOM   3122  CA  GLY B  50      24.255  21.260  -0.409  1.00 40.65           C  
ATOM   3123  C   GLY B  50      23.836  22.144  -1.561  1.00 42.56           C  
ATOM   3124  O   GLY B  50      24.473  22.156  -2.616  1.00 45.40           O  
ATOM   3125  N   GLY B  51      22.761  22.899  -1.357  1.00 43.54           N  
ATOM   3126  CA  GLY B  51      22.262  23.780  -2.400  1.00 41.20           C  
ATOM   3127  C   GLY B  51      23.270  24.820  -2.841  1.00 41.11           C  
ATOM   3128  O   GLY B  51      23.505  24.993  -4.033  1.00 42.44           O  
ATOM   3129  N   ASN B  52      23.871  25.519  -1.884  1.00 40.14           N  
ATOM   3130  CA  ASN B  52      24.844  26.538  -2.228  1.00 41.33           C  
ATOM   3131  C   ASN B  52      26.105  25.923  -2.799  1.00 41.28           C  
ATOM   3132  O   ASN B  52      26.842  26.580  -3.539  1.00 39.71           O  
ATOM   3133  CB  ASN B  52      25.167  27.407  -1.020  1.00 41.72           C  
ATOM   3134  CG  ASN B  52      24.145  28.497  -0.816  1.00 38.43           C  
ATOM   3135  OD1 ASN B  52      23.934  29.330  -1.689  1.00 40.16           O  
ATOM   3136  ND2 ASN B  52      23.501  28.496   0.341  1.00 40.32           N  
ATOM   3137  N   GLY B  53      26.346  24.661  -2.460  1.00 41.81           N  
ATOM   3138  CA  GLY B  53      27.507  23.973  -2.979  1.00 42.47           C  
ATOM   3139  C   GLY B  53      27.282  23.706  -4.454  1.00 44.64           C  
ATOM   3140  O   GLY B  53      28.176  23.898  -5.279  1.00 45.70           O  
ATOM   3141  N   ILE B  54      26.075  23.270  -4.792  1.00 43.83           N  
ATOM   3142  CA  ILE B  54      25.742  22.985  -6.181  1.00 44.08           C  
ATOM   3143  C   ILE B  54      25.947  24.237  -7.018  1.00 46.42           C  
ATOM   3144  O   ILE B  54      26.631  24.206  -8.047  1.00 48.38           O  
ATOM   3145  CB  ILE B  54      24.269  22.518  -6.325  1.00 43.78           C  
ATOM   3146  CG1 ILE B  54      24.102  21.117  -5.716  1.00 43.57           C  
ATOM   3147  CG2 ILE B  54      23.858  22.523  -7.781  1.00 37.46           C  
ATOM   3148  CD1 ILE B  54      22.663  20.643  -5.660  1.00 42.10           C  
ATOM   3149  N   VAL B  55      25.368  25.346  -6.564  1.00 46.21           N  
ATOM   3150  CA  VAL B  55      25.484  26.598  -7.298  1.00 45.53           C  
ATOM   3151  C   VAL B  55      26.928  27.081  -7.455  1.00 40.74           C  
ATOM   3152  O   VAL B  55      27.297  27.559  -8.517  1.00 40.90           O  
ATOM   3153  CB  VAL B  55      24.576  27.704  -6.675  1.00 45.57           C  
ATOM   3154  CG1 VAL B  55      24.680  27.680  -5.181  1.00 54.52           C  
ATOM   3155  CG2 VAL B  55      24.960  29.072  -7.206  1.00 46.21           C  
ATOM   3156  N   ILE B  56      27.757  26.953  -6.428  1.00 40.21           N  
ATOM   3157  CA  ILE B  56      29.147  27.379  -6.585  1.00 42.20           C  
ATOM   3158  C   ILE B  56      29.807  26.487  -7.632  1.00 44.76           C  
ATOM   3159  O   ILE B  56      30.479  26.962  -8.550  1.00 45.14           O  
ATOM   3160  CB  ILE B  56      29.964  27.242  -5.295  1.00 40.10           C  
ATOM   3161  CG1 ILE B  56      29.479  28.235  -4.242  1.00 38.78           C  
ATOM   3162  CG2 ILE B  56      31.422  27.510  -5.589  1.00 40.16           C  
ATOM   3163  CD1 ILE B  56      30.233  28.130  -2.940  1.00 41.80           C  
ATOM   3164  N   TYR B  57      29.602  25.183  -7.478  1.00 47.60           N  
ATOM   3165  CA  TYR B  57      30.166  24.186  -8.377  1.00 48.42           C  
ATOM   3166  C   TYR B  57      29.749  24.396  -9.831  1.00 48.63           C  
ATOM   3167  O   TYR B  57      30.592  24.577 -10.712  1.00 46.34           O  
ATOM   3168  CB  TYR B  57      29.752  22.778  -7.909  1.00 49.66           C  
ATOM   3169  CG  TYR B  57      30.201  21.661  -8.823  1.00 50.26           C  
ATOM   3170  CD1 TYR B  57      29.321  21.084  -9.738  1.00 47.70           C  
ATOM   3171  CD2 TYR B  57      31.522  21.205  -8.798  1.00 52.30           C  
ATOM   3172  CE1 TYR B  57      29.741  20.082 -10.604  1.00 47.61           C  
ATOM   3173  CE2 TYR B  57      31.955  20.202  -9.666  1.00 51.69           C  
ATOM   3174  CZ  TYR B  57      31.060  19.644 -10.563  1.00 49.79           C  
ATOM   3175  OH  TYR B  57      31.490  18.644 -11.394  1.00 50.14           O  
ATOM   3176  N   LEU B  58      28.443  24.376 -10.076  1.00 50.07           N  
ATOM   3177  CA  LEU B  58      27.914  24.530 -11.426  1.00 51.39           C  
ATOM   3178  C   LEU B  58      28.239  25.867 -12.096  1.00 52.18           C  
ATOM   3179  O   LEU B  58      28.548  25.910 -13.292  1.00 52.54           O  
ATOM   3180  CB  LEU B  58      26.399  24.310 -11.413  1.00 51.94           C  
ATOM   3181  CG  LEU B  58      25.863  23.002 -11.999  1.00 52.33           C  
ATOM   3182  CD1 LEU B  58      26.633  21.818 -11.462  1.00 53.38           C  
ATOM   3183  CD2 LEU B  58      24.389  22.873 -11.670  1.00 51.07           C  
ATOM   3184  N   PHE B  59      28.167  26.959 -11.340  1.00 51.72           N  
ATOM   3185  CA  PHE B  59      28.453  28.258 -11.922  1.00 51.17           C  
ATOM   3186  C   PHE B  59      29.922  28.450 -12.250  1.00 50.87           C  
ATOM   3187  O   PHE B  59      30.253  29.154 -13.194  1.00 53.61           O  
ATOM   3188  CB  PHE B  59      27.967  29.393 -11.017  1.00 49.46           C  
ATOM   3189  CG  PHE B  59      26.563  29.835 -11.305  1.00 48.05           C  
ATOM   3190  CD1 PHE B  59      25.478  29.130 -10.798  1.00 49.98           C  
ATOM   3191  CD2 PHE B  59      26.321  30.941 -12.112  1.00 48.81           C  
ATOM   3192  CE1 PHE B  59      24.163  29.524 -11.094  1.00 49.49           C  
ATOM   3193  CE2 PHE B  59      25.013  31.341 -12.413  1.00 48.88           C  
ATOM   3194  CZ  PHE B  59      23.932  30.626 -11.900  1.00 46.91           C  
ATOM   3195  N   THR B  60      30.817  27.831 -11.495  1.00 51.49           N  
ATOM   3196  CA  THR B  60      32.230  28.006 -11.805  1.00 55.00           C  
ATOM   3197  C   THR B  60      32.719  27.034 -12.869  1.00 57.47           C  
ATOM   3198  O   THR B  60      33.798  27.227 -13.434  1.00 58.83           O  
ATOM   3199  CB  THR B  60      33.124  27.818 -10.577  1.00 54.84           C  
ATOM   3200  OG1 THR B  60      33.007  26.474 -10.111  1.00 55.73           O  
ATOM   3201  CG2 THR B  60      32.732  28.780  -9.478  1.00 55.61           C  
ATOM   3202  N   LYS B  61      31.938  25.994 -13.149  1.00 58.96           N  
ATOM   3203  CA  LYS B  61      32.356  25.004 -14.133  1.00 61.00           C  
ATOM   3204  C   LYS B  61      31.615  25.089 -15.463  1.00 61.44           C  
ATOM   3205  O   LYS B  61      32.222  24.966 -16.522  1.00 64.23           O  
ATOM   3206  CB  LYS B  61      32.224  23.597 -13.545  1.00 61.45           C  
ATOM   3207  CG  LYS B  61      33.011  23.389 -12.247  1.00 62.51           C  
ATOM   3208  CD  LYS B  61      34.505  23.635 -12.426  1.00 62.14           C  
ATOM   3209  CE  LYS B  61      35.226  23.538 -11.089  1.00 65.66           C  
ATOM   3210  NZ  LYS B  61      36.713  23.660 -11.203  1.00 67.61           N  
ATOM   3211  N   THR B  62      30.307  25.302 -15.414  1.00 61.04           N  
ATOM   3212  CA  THR B  62      29.513  25.410 -16.632  1.00 59.52           C  
ATOM   3213  C   THR B  62      29.963  26.609 -17.465  1.00 59.61           C  
ATOM   3214  O   THR B  62      29.806  27.756 -17.056  1.00 59.60           O  
ATOM   3215  CB  THR B  62      28.021  25.580 -16.305  1.00 57.93           C  
ATOM   3216  OG1 THR B  62      27.549  24.424 -15.606  1.00 58.42           O  
ATOM   3217  CG2 THR B  62      27.224  25.759 -17.565  1.00 56.25           C  
ATOM   3218  N   LYS B  63      30.511  26.333 -18.642  1.00 60.81           N  
ATOM   3219  CA  LYS B  63      30.997  27.376 -19.534  1.00 62.01           C  
ATOM   3220  C   LYS B  63      29.973  28.438 -19.922  1.00 60.93           C  
ATOM   3221  O   LYS B  63      30.321  29.609 -20.077  1.00 61.30           O  
ATOM   3222  CB  LYS B  63      31.575  26.748 -20.802  1.00 65.77           C  
ATOM   3223  CG  LYS B  63      33.090  26.846 -20.904  1.00 69.76           C  
ATOM   3224  CD  LYS B  63      33.784  26.087 -19.788  1.00 74.36           C  
ATOM   3225  CE  LYS B  63      35.283  26.392 -19.767  1.00 78.22           C  
ATOM   3226  NZ  LYS B  63      35.957  26.135 -21.076  1.00 79.83           N  
ATOM   3227  N   SER B  64      28.718  28.041 -20.084  1.00 59.51           N  
ATOM   3228  CA  SER B  64      27.691  29.000 -20.475  1.00 59.94           C  
ATOM   3229  C   SER B  64      27.435  30.033 -19.400  1.00 60.40           C  
ATOM   3230  O   SER B  64      27.009  31.147 -19.687  1.00 62.06           O  
ATOM   3231  CB  SER B  64      26.377  28.287 -20.802  1.00 57.93           C  
ATOM   3232  OG  SER B  64      25.821  27.681 -19.652  1.00 58.59           O  
ATOM   3233  N   LEU B  65      27.707  29.653 -18.157  1.00 61.18           N  
ATOM   3234  CA  LEU B  65      27.485  30.519 -17.006  1.00 59.41           C  
ATOM   3235  C   LEU B  65      28.704  31.326 -16.586  1.00 60.90           C  
ATOM   3236  O   LEU B  65      28.700  31.911 -15.511  1.00 64.40           O  
ATOM   3237  CB  LEU B  65      27.029  29.677 -15.815  1.00 56.62           C  
ATOM   3238  CG  LEU B  65      25.742  28.857 -15.932  1.00 53.74           C  
ATOM   3239  CD1 LEU B  65      25.590  28.003 -14.680  1.00 51.38           C  
ATOM   3240  CD2 LEU B  65      24.540  29.785 -16.109  1.00 51.46           C  
ATOM   3241  N   GLN B  66      29.738  31.371 -17.420  1.00 62.81           N  
ATOM   3242  CA  GLN B  66      30.951  32.101 -17.066  1.00 64.08           C  
ATOM   3243  C   GLN B  66      30.974  33.619 -17.278  1.00 63.95           C  
ATOM   3244  O   GLN B  66      32.046  34.204 -17.428  1.00 65.21           O  
ATOM   3245  CB  GLN B  66      32.149  31.485 -17.783  1.00 66.79           C  
ATOM   3246  CG  GLN B  66      32.956  30.517 -16.939  1.00 70.64           C  
ATOM   3247  CD  GLN B  66      32.149  29.322 -16.481  1.00 73.82           C  
ATOM   3248  OE1 GLN B  66      31.181  29.460 -15.742  1.00 72.39           O  
ATOM   3249  NE2 GLN B  66      32.550  28.133 -16.926  1.00 77.38           N  
ATOM   3250  N   THR B  67      29.814  34.267 -17.271  1.00 63.06           N  
ATOM   3251  CA  THR B  67      29.771  35.717 -17.463  1.00 62.05           C  
ATOM   3252  C   THR B  67      30.109  36.433 -16.146  1.00 59.70           C  
ATOM   3253  O   THR B  67      29.843  35.917 -15.070  1.00 61.60           O  
ATOM   3254  CB  THR B  67      28.388  36.161 -17.969  1.00 62.35           C  
ATOM   3255  OG1 THR B  67      27.461  36.205 -16.879  1.00 63.47           O  
ATOM   3256  CG2 THR B  67      27.879  35.165 -19.004  1.00 62.83           C  
ATOM   3257  N   PRO B  68      30.693  37.636 -16.222  1.00 56.72           N  
ATOM   3258  CA  PRO B  68      31.066  38.394 -15.023  1.00 55.02           C  
ATOM   3259  C   PRO B  68      30.037  38.522 -13.887  1.00 54.99           C  
ATOM   3260  O   PRO B  68      30.273  38.044 -12.769  1.00 55.02           O  
ATOM   3261  CB  PRO B  68      31.482  39.751 -15.589  1.00 54.38           C  
ATOM   3262  CG  PRO B  68      32.067  39.383 -16.927  1.00 54.34           C  
ATOM   3263  CD  PRO B  68      31.056  38.377 -17.445  1.00 53.89           C  
ATOM   3264  N   ALA B  69      28.911  39.174 -14.163  1.00 51.51           N  
ATOM   3265  CA  ALA B  69      27.890  39.376 -13.147  1.00 47.79           C  
ATOM   3266  C   ALA B  69      27.673  38.119 -12.317  1.00 48.48           C  
ATOM   3267  O   ALA B  69      27.427  38.185 -11.114  1.00 45.17           O  
ATOM   3268  CB  ALA B  69      26.584  39.810 -13.789  1.00 46.50           C  
ATOM   3269  N   ASN B  70      27.768  36.968 -12.969  1.00 49.88           N  
ATOM   3270  CA  ASN B  70      27.568  35.710 -12.273  1.00 50.62           C  
ATOM   3271  C   ASN B  70      28.507  35.523 -11.083  1.00 50.57           C  
ATOM   3272  O   ASN B  70      28.204  34.757 -10.173  1.00 53.81           O  
ATOM   3273  CB  ASN B  70      27.688  34.541 -13.254  1.00 48.73           C  
ATOM   3274  CG  ASN B  70      26.417  34.320 -14.049  1.00 50.05           C  
ATOM   3275  OD1 ASN B  70      26.378  33.483 -14.948  1.00 55.65           O  
ATOM   3276  ND2 ASN B  70      25.371  35.061 -13.721  1.00 45.53           N  
ATOM   3277  N   MET B  71      29.640  36.221 -11.087  1.00 48.56           N  
ATOM   3278  CA  MET B  71      30.586  36.124  -9.979  1.00 45.78           C  
ATOM   3279  C   MET B  71      29.865  36.542  -8.703  1.00 46.06           C  
ATOM   3280  O   MET B  71      30.196  36.082  -7.614  1.00 49.25           O  
ATOM   3281  CB  MET B  71      31.791  37.049 -10.199  1.00 45.68           C  
ATOM   3282  CG  MET B  71      32.687  36.650 -11.358  1.00 51.57           C  
ATOM   3283  SD  MET B  71      34.034  37.827 -11.721  1.00 57.69           S  
ATOM   3284  CE  MET B  71      34.984  37.716 -10.254  1.00 53.23           C  
ATOM   3285  N   PHE B  72      28.878  37.426  -8.856  1.00 45.14           N  
ATOM   3286  CA  PHE B  72      28.101  37.914  -7.729  1.00 42.95           C  
ATOM   3287  C   PHE B  72      27.284  36.773  -7.145  1.00 41.04           C  
ATOM   3288  O   PHE B  72      27.147  36.655  -5.932  1.00 44.17           O  
ATOM   3289  CB  PHE B  72      27.185  39.071  -8.152  1.00 40.63           C  
ATOM   3290  CG  PHE B  72      27.928  40.326  -8.535  1.00 41.57           C  
ATOM   3291  CD1 PHE B  72      29.062  40.728  -7.828  1.00 41.35           C  
ATOM   3292  CD2 PHE B  72      27.485  41.128  -9.592  1.00 43.86           C  
ATOM   3293  CE1 PHE B  72      29.747  41.912  -8.166  1.00 41.21           C  
ATOM   3294  CE2 PHE B  72      28.162  42.317  -9.942  1.00 39.85           C  
ATOM   3295  CZ  PHE B  72      29.290  42.706  -9.230  1.00 41.70           C  
ATOM   3296  N   ILE B  73      26.756  35.926  -8.013  1.00 40.08           N  
ATOM   3297  CA  ILE B  73      25.967  34.800  -7.563  1.00 41.19           C  
ATOM   3298  C   ILE B  73      26.873  33.853  -6.803  1.00 39.47           C  
ATOM   3299  O   ILE B  73      26.537  33.372  -5.722  1.00 37.75           O  
ATOM   3300  CB  ILE B  73      25.332  34.061  -8.751  1.00 42.89           C  
ATOM   3301  CG1 ILE B  73      24.226  34.931  -9.352  1.00 45.38           C  
ATOM   3302  CG2 ILE B  73      24.769  32.725  -8.307  1.00 43.59           C  
ATOM   3303  CD1 ILE B  73      23.568  34.336 -10.595  1.00 48.47           C  
ATOM   3304  N   ILE B  74      28.036  33.594  -7.375  1.00 38.57           N  
ATOM   3305  CA  ILE B  74      28.987  32.705  -6.748  1.00 37.88           C  
ATOM   3306  C   ILE B  74      29.320  33.221  -5.354  1.00 39.82           C  
ATOM   3307  O   ILE B  74      29.238  32.474  -4.382  1.00 41.17           O  
ATOM   3308  CB  ILE B  74      30.259  32.574  -7.622  1.00 38.09           C  
ATOM   3309  CG1 ILE B  74      29.891  31.858  -8.931  1.00 37.48           C  
ATOM   3310  CG2 ILE B  74      31.339  31.787  -6.899  1.00 33.25           C  
ATOM   3311  CD1 ILE B  74      31.013  31.789  -9.929  1.00 35.25           C  
ATOM   3312  N   ASN B  75      29.662  34.503  -5.246  1.00 40.41           N  
ATOM   3313  CA  ASN B  75      29.994  35.067  -3.939  1.00 39.26           C  
ATOM   3314  C   ASN B  75      28.807  34.976  -2.993  1.00 39.37           C  
ATOM   3315  O   ASN B  75      28.983  34.785  -1.791  1.00 40.83           O  
ATOM   3316  CB  ASN B  75      30.439  36.521  -4.055  1.00 38.22           C  
ATOM   3317  CG  ASN B  75      30.972  37.071  -2.737  1.00 40.12           C  
ATOM   3318  OD1 ASN B  75      32.044  36.689  -2.292  1.00 43.09           O  
ATOM   3319  ND2 ASN B  75      30.217  37.964  -2.107  1.00 38.84           N  
ATOM   3320  N   LEU B  76      27.602  35.122  -3.534  1.00 37.97           N  
ATOM   3321  CA  LEU B  76      26.398  35.032  -2.713  1.00 38.90           C  
ATOM   3322  C   LEU B  76      26.273  33.602  -2.187  1.00 38.18           C  
ATOM   3323  O   LEU B  76      25.963  33.367  -1.016  1.00 36.97           O  
ATOM   3324  CB  LEU B  76      25.151  35.373  -3.536  1.00 41.89           C  
ATOM   3325  CG  LEU B  76      24.089  36.257  -2.880  1.00 45.77           C  
ATOM   3326  CD1 LEU B  76      22.787  36.183  -3.679  1.00 43.06           C  
ATOM   3327  CD2 LEU B  76      23.840  35.823  -1.439  1.00 44.83           C  
ATOM   3328  N   ALA B  77      26.519  32.646  -3.072  1.00 40.71           N  
ATOM   3329  CA  ALA B  77      26.424  31.239  -2.719  1.00 40.87           C  
ATOM   3330  C   ALA B  77      27.461  30.876  -1.676  1.00 39.63           C  
ATOM   3331  O   ALA B  77      27.149  30.206  -0.702  1.00 40.72           O  
ATOM   3332  CB  ALA B  77      26.586  30.365  -3.966  1.00 38.78           C  
ATOM   3333  N   PHE B  78      28.697  31.313  -1.887  1.00 38.63           N  
ATOM   3334  CA  PHE B  78      29.770  31.025  -0.942  1.00 41.08           C  
ATOM   3335  C   PHE B  78      29.410  31.554   0.444  1.00 41.46           C  
ATOM   3336  O   PHE B  78      29.615  30.884   1.448  1.00 41.49           O  
ATOM   3337  CB  PHE B  78      31.066  31.679  -1.396  1.00 43.88           C  
ATOM   3338  CG  PHE B  78      32.180  31.537  -0.407  1.00 49.20           C  
ATOM   3339  CD1 PHE B  78      32.867  30.333  -0.280  1.00 48.18           C  
ATOM   3340  CD2 PHE B  78      32.520  32.602   0.429  1.00 50.42           C  
ATOM   3341  CE1 PHE B  78      33.875  30.192   0.663  1.00 50.84           C  
ATOM   3342  CE2 PHE B  78      33.525  32.470   1.376  1.00 51.35           C  
ATOM   3343  CZ  PHE B  78      34.205  31.264   1.494  1.00 52.96           C  
ATOM   3344  N   SER B  79      28.889  32.777   0.471  1.00 43.67           N  
ATOM   3345  CA  SER B  79      28.480  33.427   1.700  1.00 41.56           C  
ATOM   3346  C   SER B  79      27.347  32.624   2.357  1.00 39.80           C  
ATOM   3347  O   SER B  79      27.417  32.257   3.532  1.00 38.34           O  
ATOM   3348  CB  SER B  79      28.018  34.854   1.400  1.00 45.19           C  
ATOM   3349  OG  SER B  79      27.579  35.524   2.568  1.00 48.12           O  
ATOM   3350  N   ASP B  80      26.299  32.338   1.598  1.00 39.44           N  
ATOM   3351  CA  ASP B  80      25.189  31.579   2.144  1.00 40.04           C  
ATOM   3352  C   ASP B  80      25.649  30.199   2.575  1.00 39.48           C  
ATOM   3353  O   ASP B  80      25.131  29.626   3.544  1.00 38.16           O  
ATOM   3354  CB  ASP B  80      24.071  31.490   1.118  1.00 41.02           C  
ATOM   3355  CG  ASP B  80      23.413  32.839   0.871  1.00 44.12           C  
ATOM   3356  OD1 ASP B  80      22.832  33.036  -0.218  1.00 42.01           O  
ATOM   3357  OD2 ASP B  80      23.471  33.707   1.772  1.00 40.22           O  
ATOM   3358  N   PHE B  81      26.650  29.683   1.875  1.00 38.53           N  
ATOM   3359  CA  PHE B  81      27.196  28.375   2.188  1.00 38.54           C  
ATOM   3360  C   PHE B  81      27.780  28.384   3.596  1.00 38.62           C  
ATOM   3361  O   PHE B  81      27.401  27.579   4.444  1.00 40.15           O  
ATOM   3362  CB  PHE B  81      28.302  28.005   1.204  1.00 40.34           C  
ATOM   3363  CG  PHE B  81      28.934  26.669   1.489  1.00 41.82           C  
ATOM   3364  CD1 PHE B  81      28.336  25.499   1.047  1.00 39.87           C  
ATOM   3365  CD2 PHE B  81      30.095  26.582   2.252  1.00 40.14           C  
ATOM   3366  CE1 PHE B  81      28.871  24.269   1.358  1.00 35.57           C  
ATOM   3367  CE2 PHE B  81      30.633  25.347   2.566  1.00 40.12           C  
ATOM   3368  CZ  PHE B  81      30.019  24.193   2.118  1.00 39.36           C  
ATOM   3369  N   THR B  82      28.710  29.307   3.819  1.00 38.67           N  
ATOM   3370  CA  THR B  82      29.386  29.453   5.094  1.00 40.10           C  
ATOM   3371  C   THR B  82      28.413  29.694   6.247  1.00 38.64           C  
ATOM   3372  O   THR B  82      28.540  29.106   7.316  1.00 41.95           O  
ATOM   3373  CB  THR B  82      30.400  30.623   5.040  1.00 40.73           C  
ATOM   3374  OG1 THR B  82      31.180  30.515   3.843  1.00 38.27           O  
ATOM   3375  CG2 THR B  82      31.334  30.582   6.242  1.00 37.13           C  
ATOM   3376  N   PHE B  83      27.440  30.563   6.024  1.00 40.51           N  
ATOM   3377  CA  PHE B  83      26.453  30.863   7.052  1.00 39.76           C  
ATOM   3378  C   PHE B  83      25.737  29.596   7.500  1.00 38.21           C  
ATOM   3379  O   PHE B  83      25.574  29.358   8.700  1.00 39.33           O  
ATOM   3380  CB  PHE B  83      25.433  31.879   6.526  1.00 40.25           C  
ATOM   3381  CG  PHE B  83      24.492  32.386   7.577  1.00 38.82           C  
ATOM   3382  CD1 PHE B  83      23.457  31.585   8.057  1.00 41.83           C  
ATOM   3383  CD2 PHE B  83      24.672  33.643   8.126  1.00 38.34           C  
ATOM   3384  CE1 PHE B  83      22.621  32.035   9.073  1.00 39.24           C  
ATOM   3385  CE2 PHE B  83      23.851  34.100   9.132  1.00 36.16           C  
ATOM   3386  CZ  PHE B  83      22.824  33.298   9.609  1.00 39.11           C  
ATOM   3387  N   SER B  84      25.313  28.794   6.527  1.00 38.86           N  
ATOM   3388  CA  SER B  84      24.598  27.543   6.789  1.00 39.22           C  
ATOM   3389  C   SER B  84      25.506  26.513   7.455  1.00 38.46           C  
ATOM   3390  O   SER B  84      25.058  25.704   8.265  1.00 36.40           O  
ATOM   3391  CB  SER B  84      24.049  26.956   5.481  1.00 38.23           C  
ATOM   3392  OG  SER B  84      23.290  27.912   4.762  1.00 36.16           O  
ATOM   3393  N   LEU B  85      26.786  26.546   7.109  1.00 38.32           N  
ATOM   3394  CA  LEU B  85      27.729  25.606   7.689  1.00 39.48           C  
ATOM   3395  C   LEU B  85      27.923  25.925   9.173  1.00 41.79           C  
ATOM   3396  O   LEU B  85      27.636  25.112  10.056  1.00 41.72           O  
ATOM   3397  CB  LEU B  85      29.080  25.721   6.999  1.00 35.85           C  
ATOM   3398  CG  LEU B  85      29.956  24.479   6.995  1.00 35.96           C  
ATOM   3399  CD1 LEU B  85      31.407  24.915   6.962  1.00 31.85           C  
ATOM   3400  CD2 LEU B  85      29.683  23.621   8.196  1.00 34.90           C  
ATOM   3401  N   VAL B  86      28.408  27.138   9.415  1.00 42.46           N  
ATOM   3402  CA  VAL B  86      28.714  27.611  10.741  1.00 41.68           C  
ATOM   3403  C   VAL B  86      27.544  27.805  11.705  1.00 43.83           C  
ATOM   3404  O   VAL B  86      27.683  27.554  12.896  1.00 44.97           O  
ATOM   3405  CB  VAL B  86      29.489  28.928  10.666  1.00 42.11           C  
ATOM   3406  CG1 VAL B  86      29.842  29.407  12.068  1.00 38.77           C  
ATOM   3407  CG2 VAL B  86      30.747  28.739   9.814  1.00 39.72           C  
ATOM   3408  N   ASN B  87      26.397  28.248  11.204  1.00 44.29           N  
ATOM   3409  CA  ASN B  87      25.265  28.504  12.075  1.00 44.56           C  
ATOM   3410  C   ASN B  87      24.355  27.321  12.357  1.00 44.18           C  
ATOM   3411  O   ASN B  87      23.426  27.428  13.168  1.00 47.10           O  
ATOM   3412  CB  ASN B  87      24.439  29.664  11.522  1.00 44.77           C  
ATOM   3413  CG  ASN B  87      25.147  30.996  11.654  1.00 44.86           C  
ATOM   3414  OD1 ASN B  87      25.002  31.680  12.653  1.00 47.66           O  
ATOM   3415  ND2 ASN B  87      25.934  31.361  10.644  1.00 42.77           N  
ATOM   3416  N   GLY B  88      24.613  26.193  11.711  1.00 41.66           N  
ATOM   3417  CA  GLY B  88      23.776  25.026  11.926  1.00 40.28           C  
ATOM   3418  C   GLY B  88      24.492  23.916  12.662  1.00 37.56           C  
ATOM   3419  O   GLY B  88      24.634  23.959  13.893  1.00 34.36           O  
ATOM   3420  N   PHE B  89      24.932  22.909  11.911  1.00 37.10           N  
ATOM   3421  CA  PHE B  89      25.656  21.791  12.504  1.00 40.09           C  
ATOM   3422  C   PHE B  89      27.168  21.998  12.374  1.00 36.73           C  
ATOM   3423  O   PHE B  89      27.657  22.433  11.338  1.00 32.88           O  
ATOM   3424  CB  PHE B  89      25.244  20.473  11.840  1.00 41.79           C  
ATOM   3425  CG  PHE B  89      26.092  19.302  12.245  1.00 45.65           C  
ATOM   3426  CD1 PHE B  89      27.252  18.996  11.545  1.00 44.54           C  
ATOM   3427  CD2 PHE B  89      25.780  18.563  13.383  1.00 47.06           C  
ATOM   3428  CE1 PHE B  89      28.096  17.981  11.970  1.00 45.98           C  
ATOM   3429  CE2 PHE B  89      26.623  17.542  13.821  1.00 47.83           C  
ATOM   3430  CZ  PHE B  89      27.784  17.255  13.112  1.00 47.50           C  
ATOM   3431  N   PRO B  90      27.929  21.692  13.437  1.00 36.31           N  
ATOM   3432  CA  PRO B  90      27.521  21.142  14.735  1.00 37.98           C  
ATOM   3433  C   PRO B  90      27.240  22.158  15.845  1.00 39.43           C  
ATOM   3434  O   PRO B  90      26.514  21.860  16.789  1.00 38.84           O  
ATOM   3435  CB  PRO B  90      28.706  20.271  15.108  1.00 38.72           C  
ATOM   3436  CG  PRO B  90      29.855  21.138  14.660  1.00 38.16           C  
ATOM   3437  CD  PRO B  90      29.396  21.583  13.277  1.00 37.34           C  
ATOM   3438  N   LEU B  91      27.835  23.340  15.734  1.00 42.17           N  
ATOM   3439  CA  LEU B  91      27.699  24.373  16.754  1.00 41.50           C  
ATOM   3440  C   LEU B  91      26.324  24.552  17.391  1.00 43.26           C  
ATOM   3441  O   LEU B  91      26.184  24.384  18.600  1.00 42.11           O  
ATOM   3442  CB  LEU B  91      28.219  25.704  16.209  1.00 41.15           C  
ATOM   3443  CG  LEU B  91      29.720  25.656  15.930  1.00 38.96           C  
ATOM   3444  CD1 LEU B  91      30.266  27.047  15.670  1.00 34.39           C  
ATOM   3445  CD2 LEU B  91      30.429  25.032  17.124  1.00 35.04           C  
ATOM   3446  N   MET B  92      25.305  24.888  16.609  1.00 44.65           N  
ATOM   3447  CA  MET B  92      23.986  25.064  17.214  1.00 46.84           C  
ATOM   3448  C   MET B  92      23.223  23.752  17.426  1.00 44.41           C  
ATOM   3449  O   MET B  92      22.624  23.536  18.471  1.00 43.69           O  
ATOM   3450  CB  MET B  92      23.124  26.031  16.389  1.00 46.53           C  
ATOM   3451  CG  MET B  92      21.834  26.401  17.092  1.00 46.76           C  
ATOM   3452  SD  MET B  92      20.704  27.461  16.165  1.00 48.54           S  
ATOM   3453  CE  MET B  92      19.442  27.731  17.427  1.00 45.42           C  
ATOM   3454  N   THR B  93      23.246  22.871  16.438  1.00 44.12           N  
ATOM   3455  CA  THR B  93      22.543  21.599  16.562  1.00 44.75           C  
ATOM   3456  C   THR B  93      22.933  20.830  17.814  1.00 45.35           C  
ATOM   3457  O   THR B  93      22.082  20.506  18.621  1.00 48.48           O  
ATOM   3458  CB  THR B  93      22.792  20.700  15.340  1.00 45.88           C  
ATOM   3459  OG1 THR B  93      22.290  21.340  14.170  1.00 44.31           O  
ATOM   3460  CG2 THR B  93      22.098  19.350  15.521  1.00 45.45           C  
ATOM   3461  N   ILE B  94      24.216  20.531  17.976  1.00 46.03           N  
ATOM   3462  CA  ILE B  94      24.659  19.781  19.144  1.00 44.72           C  
ATOM   3463  C   ILE B  94      24.367  20.500  20.463  1.00 46.66           C  
ATOM   3464  O   ILE B  94      24.167  19.861  21.490  1.00 48.88           O  
ATOM   3465  CB  ILE B  94      26.178  19.470  19.064  1.00 44.40           C  
ATOM   3466  CG1 ILE B  94      26.458  18.647  17.805  1.00 41.90           C  
ATOM   3467  CG2 ILE B  94      26.642  18.718  20.308  1.00 37.35           C  
ATOM   3468  CD1 ILE B  94      25.604  17.383  17.702  1.00 46.45           C  
ATOM   3469  N   SER B  95      24.355  21.828  20.435  1.00 48.94           N  
ATOM   3470  CA  SER B  95      24.076  22.606  21.634  1.00 47.15           C  
ATOM   3471  C   SER B  95      22.619  22.423  22.015  1.00 47.80           C  
ATOM   3472  O   SER B  95      22.281  22.295  23.192  1.00 46.24           O  
ATOM   3473  CB  SER B  95      24.358  24.087  21.392  1.00 47.39           C  
ATOM   3474  OG  SER B  95      25.746  24.322  21.257  1.00 48.04           O  
ATOM   3475  N   CYS B  96      21.753  22.416  21.007  1.00 48.27           N  
ATOM   3476  CA  CYS B  96      20.333  22.236  21.254  1.00 50.70           C  
ATOM   3477  C   CYS B  96      20.101  20.866  21.869  1.00 51.69           C  
ATOM   3478  O   CYS B  96      19.482  20.757  22.926  1.00 53.76           O  
ATOM   3479  CB  CYS B  96      19.536  22.379  19.962  1.00 50.31           C  
ATOM   3480  SG  CYS B  96      19.343  24.088  19.413  1.00 51.55           S  
ATOM   3481  N   PHE B  97      20.613  19.828  21.218  1.00 51.24           N  
ATOM   3482  CA  PHE B  97      20.454  18.470  21.711  1.00 50.20           C  
ATOM   3483  C   PHE B  97      20.958  18.304  23.146  1.00 48.89           C  
ATOM   3484  O   PHE B  97      20.586  17.355  23.826  1.00 51.69           O  
ATOM   3485  CB  PHE B  97      21.176  17.488  20.776  1.00 51.89           C  
ATOM   3486  CG  PHE B  97      20.538  17.365  19.417  1.00 54.13           C  
ATOM   3487  CD1 PHE B  97      21.237  16.819  18.350  1.00 54.18           C  
ATOM   3488  CD2 PHE B  97      19.228  17.792  19.207  1.00 55.06           C  
ATOM   3489  CE1 PHE B  97      20.646  16.700  17.098  1.00 53.81           C  
ATOM   3490  CE2 PHE B  97      18.632  17.677  17.956  1.00 53.10           C  
ATOM   3491  CZ  PHE B  97      19.341  17.132  16.904  1.00 52.69           C  
ATOM   3492  N   LEU B  98      21.796  19.228  23.604  1.00 46.39           N  
ATOM   3493  CA  LEU B  98      22.332  19.177  24.958  1.00 45.18           C  
ATOM   3494  C   LEU B  98      21.814  20.339  25.790  1.00 44.48           C  
ATOM   3495  O   LEU B  98      22.247  20.556  26.928  1.00 43.93           O  
ATOM   3496  CB  LEU B  98      23.863  19.229  24.935  1.00 47.59           C  
ATOM   3497  CG  LEU B  98      24.655  17.922  24.892  1.00 46.83           C  
ATOM   3498  CD1 LEU B  98      24.084  16.970  23.852  1.00 41.51           C  
ATOM   3499  CD2 LEU B  98      26.110  18.257  24.611  1.00 44.83           C  
ATOM   3500  N   LYS B  99      20.885  21.087  25.212  1.00 45.94           N  
ATOM   3501  CA  LYS B  99      20.291  22.241  25.876  1.00 45.91           C  
ATOM   3502  C   LYS B  99      21.370  23.090  26.517  1.00 43.68           C  
ATOM   3503  O   LYS B  99      21.190  23.602  27.619  1.00 45.52           O  
ATOM   3504  CB  LYS B  99      19.308  21.773  26.941  1.00 44.06           C  
ATOM   3505  CG  LYS B  99      18.209  20.903  26.391  1.00 47.22           C  
ATOM   3506  CD  LYS B  99      17.145  20.649  27.439  1.00 46.81           C  
ATOM   3507  CE  LYS B  99      17.669  19.770  28.542  1.00 46.75           C  
ATOM   3508  NZ  LYS B  99      16.604  19.458  29.534  1.00 53.42           N  
ATOM   3509  N   LYS B 100      22.485  23.250  25.818  1.00 41.82           N  
ATOM   3510  CA  LYS B 100      23.595  24.012  26.361  1.00 42.61           C  
ATOM   3511  C   LYS B 100      24.697  24.270  25.327  1.00 43.10           C  
ATOM   3512  O   LYS B 100      25.085  23.367  24.594  1.00 43.68           O  
ATOM   3513  CB  LYS B 100      24.189  23.246  27.542  1.00 41.16           C  
ATOM   3514  CG  LYS B 100      25.382  23.888  28.193  1.00 40.96           C  
ATOM   3515  CD  LYS B 100      24.935  24.834  29.258  1.00 45.79           C  
ATOM   3516  CE  LYS B 100      24.055  24.141  30.275  1.00 45.61           C  
ATOM   3517  NZ  LYS B 100      23.427  25.121  31.192  1.00 45.67           N  
ATOM   3518  N   TRP B 101      25.191  25.504  25.278  1.00 40.82           N  
ATOM   3519  CA  TRP B 101      26.272  25.831  24.375  1.00 39.97           C  
ATOM   3520  C   TRP B 101      27.532  25.312  25.037  1.00 40.72           C  
ATOM   3521  O   TRP B 101      27.974  25.857  26.039  1.00 42.28           O  
ATOM   3522  CB  TRP B 101      26.395  27.338  24.179  1.00 37.14           C  
ATOM   3523  CG  TRP B 101      27.512  27.733  23.241  1.00 33.63           C  
ATOM   3524  CD1 TRP B 101      28.811  28.006  23.581  1.00 32.20           C  
ATOM   3525  CD2 TRP B 101      27.427  27.901  21.818  1.00 27.19           C  
ATOM   3526  NE1 TRP B 101      29.534  28.343  22.456  1.00 29.63           N  
ATOM   3527  CE2 TRP B 101      28.708  28.287  21.364  1.00 27.05           C  
ATOM   3528  CE3 TRP B 101      26.394  27.764  20.885  1.00 30.52           C  
ATOM   3529  CZ2 TRP B 101      28.983  28.543  20.016  1.00 28.47           C  
ATOM   3530  CZ3 TRP B 101      26.668  28.022  19.537  1.00 27.02           C  
ATOM   3531  CH2 TRP B 101      27.956  28.409  19.120  1.00 28.91           C  
ATOM   3532  N   ILE B 102      28.124  24.262  24.489  1.00 43.11           N  
ATOM   3533  CA  ILE B 102      29.315  23.724  25.117  1.00 43.09           C  
ATOM   3534  C   ILE B 102      30.623  23.963  24.360  1.00 42.38           C  
ATOM   3535  O   ILE B 102      31.641  23.363  24.695  1.00 44.86           O  
ATOM   3536  CB  ILE B 102      29.148  22.216  25.364  1.00 43.07           C  
ATOM   3537  CG1 ILE B 102      29.243  21.446  24.037  1.00 42.35           C  
ATOM   3538  CG2 ILE B 102      27.792  21.964  26.022  1.00 35.89           C  
ATOM   3539  CD1 ILE B 102      28.062  21.655  23.131  1.00 46.09           C  
ATOM   3540  N   PHE B 103      30.617  24.848  23.369  1.00 39.38           N  
ATOM   3541  CA  PHE B 103      31.833  25.087  22.601  1.00 39.87           C  
ATOM   3542  C   PHE B 103      32.688  26.289  23.015  1.00 39.23           C  
ATOM   3543  O   PHE B 103      33.591  26.687  22.278  1.00 42.17           O  
ATOM   3544  CB  PHE B 103      31.485  25.159  21.107  1.00 38.77           C  
ATOM   3545  CG  PHE B 103      30.657  23.993  20.637  1.00 42.10           C  
ATOM   3546  CD1 PHE B 103      31.241  22.749  20.421  1.00 40.57           C  
ATOM   3547  CD2 PHE B 103      29.275  24.116  20.498  1.00 42.96           C  
ATOM   3548  CE1 PHE B 103      30.457  21.644  20.079  1.00 40.76           C  
ATOM   3549  CE2 PHE B 103      28.482  23.012  20.155  1.00 42.35           C  
ATOM   3550  CZ  PHE B 103      29.072  21.777  19.946  1.00 41.62           C  
ATOM   3551  N   GLY B 104      32.427  26.837  24.198  1.00 37.84           N  
ATOM   3552  CA  GLY B 104      33.198  27.964  24.696  1.00 38.23           C  
ATOM   3553  C   GLY B 104      32.902  29.354  24.137  1.00 38.58           C  
ATOM   3554  O   GLY B 104      32.255  29.486  23.089  1.00 35.10           O  
ATOM   3555  N   PHE B 105      33.405  30.380  24.837  1.00 39.23           N  
ATOM   3556  CA  PHE B 105      33.245  31.796  24.475  1.00 41.02           C  
ATOM   3557  C   PHE B 105      33.796  32.148  23.082  1.00 42.83           C  
ATOM   3558  O   PHE B 105      33.135  32.841  22.308  1.00 44.47           O  
ATOM   3559  CB  PHE B 105      33.932  32.686  25.524  1.00 40.49           C  
ATOM   3560  CG  PHE B 105      33.380  34.091  25.602  1.00 44.30           C  
ATOM   3561  CD1 PHE B 105      34.039  35.067  26.340  1.00 39.44           C  
ATOM   3562  CD2 PHE B 105      32.194  34.443  24.944  1.00 48.56           C  
ATOM   3563  CE1 PHE B 105      33.536  36.363  26.426  1.00 39.47           C  
ATOM   3564  CE2 PHE B 105      31.682  35.747  25.025  1.00 43.98           C  
ATOM   3565  CZ  PHE B 105      32.356  36.702  25.767  1.00 39.30           C  
ATOM   3566  N   ALA B 106      35.003  31.687  22.769  1.00 42.48           N  
ATOM   3567  CA  ALA B 106      35.591  31.968  21.460  1.00 43.60           C  
ATOM   3568  C   ALA B 106      34.705  31.435  20.336  1.00 43.37           C  
ATOM   3569  O   ALA B 106      34.471  32.120  19.345  1.00 46.61           O  
ATOM   3570  CB  ALA B 106      37.001  31.355  21.348  1.00 41.26           C  
ATOM   3571  N   ALA B 107      34.212  30.210  20.485  1.00 44.27           N  
ATOM   3572  CA  ALA B 107      33.366  29.632  19.455  1.00 45.93           C  
ATOM   3573  C   ALA B 107      32.174  30.551  19.238  1.00 46.01           C  
ATOM   3574  O   ALA B 107      31.821  30.884  18.101  1.00 47.18           O  
ATOM   3575  CB  ALA B 107      32.896  28.243  19.861  1.00 45.29           C  
ATOM   3576  N   CYS B 108      31.570  30.969  20.342  1.00 45.81           N  
ATOM   3577  CA  CYS B 108      30.405  31.843  20.331  1.00 43.26           C  
ATOM   3578  C   CYS B 108      30.675  33.123  19.566  1.00 40.02           C  
ATOM   3579  O   CYS B 108      29.855  33.551  18.767  1.00 37.78           O  
ATOM   3580  CB  CYS B 108      30.004  32.160  21.772  1.00 43.19           C  
ATOM   3581  SG  CYS B 108      28.614  33.317  22.049  1.00 46.88           S  
ATOM   3582  N   LYS B 109      31.832  33.727  19.812  1.00 37.31           N  
ATOM   3583  CA  LYS B 109      32.190  34.953  19.121  1.00 38.35           C  
ATOM   3584  C   LYS B 109      32.317  34.692  17.626  1.00 39.61           C  
ATOM   3585  O   LYS B 109      31.744  35.417  16.826  1.00 41.86           O  
ATOM   3586  CB  LYS B 109      33.504  35.506  19.662  1.00 37.19           C  
ATOM   3587  CG  LYS B 109      33.460  35.761  21.157  1.00 40.56           C  
ATOM   3588  CD  LYS B 109      34.701  36.473  21.626  1.00 41.56           C  
ATOM   3589  CE  LYS B 109      34.667  36.655  23.108  1.00 42.89           C  
ATOM   3590  NZ  LYS B 109      35.783  37.536  23.515  1.00 49.70           N  
ATOM   3591  N   VAL B 110      33.060  33.647  17.267  1.00 37.92           N  
ATOM   3592  CA  VAL B 110      33.256  33.297  15.869  1.00 35.97           C  
ATOM   3593  C   VAL B 110      31.908  33.088  15.201  1.00 36.06           C  
ATOM   3594  O   VAL B 110      31.629  33.667  14.154  1.00 38.54           O  
ATOM   3595  CB  VAL B 110      34.108  32.019  15.716  1.00 36.94           C  
ATOM   3596  CG1 VAL B 110      34.147  31.578  14.259  1.00 30.53           C  
ATOM   3597  CG2 VAL B 110      35.524  32.278  16.215  1.00 34.42           C  
ATOM   3598  N   TYR B 111      31.082  32.247  15.819  1.00 37.10           N  
ATOM   3599  CA  TYR B 111      29.737  31.945  15.324  1.00 37.88           C  
ATOM   3600  C   TYR B 111      28.975  33.253  15.050  1.00 37.40           C  
ATOM   3601  O   TYR B 111      28.498  33.499  13.937  1.00 35.10           O  
ATOM   3602  CB  TYR B 111      28.994  31.136  16.373  1.00 38.43           C  
ATOM   3603  CG  TYR B 111      27.598  30.688  16.000  1.00 41.29           C  
ATOM   3604  CD1 TYR B 111      27.365  29.396  15.536  1.00 40.04           C  
ATOM   3605  CD2 TYR B 111      26.493  31.538  16.176  1.00 41.35           C  
ATOM   3606  CE1 TYR B 111      26.066  28.952  15.263  1.00 42.01           C  
ATOM   3607  CE2 TYR B 111      25.193  31.104  15.905  1.00 37.35           C  
ATOM   3608  CZ  TYR B 111      24.985  29.808  15.451  1.00 41.76           C  
ATOM   3609  OH  TYR B 111      23.705  29.353  15.201  1.00 41.62           O  
ATOM   3610  N   GLY B 112      28.871  34.087  16.076  1.00 32.45           N  
ATOM   3611  CA  GLY B 112      28.168  35.343  15.922  1.00 34.23           C  
ATOM   3612  C   GLY B 112      28.807  36.240  14.879  1.00 35.48           C  
ATOM   3613  O   GLY B 112      28.119  36.927  14.124  1.00 39.20           O  
ATOM   3614  N   PHE B 113      30.131  36.228  14.843  1.00 34.44           N  
ATOM   3615  CA  PHE B 113      30.881  37.056  13.927  1.00 34.88           C  
ATOM   3616  C   PHE B 113      30.669  36.593  12.495  1.00 36.82           C  
ATOM   3617  O   PHE B 113      30.409  37.392  11.598  1.00 34.89           O  
ATOM   3618  CB  PHE B 113      32.359  37.000  14.294  1.00 38.13           C  
ATOM   3619  CG  PHE B 113      33.254  37.737  13.348  1.00 39.91           C  
ATOM   3620  CD1 PHE B 113      32.872  38.963  12.812  1.00 36.76           C  
ATOM   3621  CD2 PHE B 113      34.516  37.229  13.043  1.00 39.63           C  
ATOM   3622  CE1 PHE B 113      33.727  39.682  11.992  1.00 37.24           C  
ATOM   3623  CE2 PHE B 113      35.386  37.938  12.219  1.00 40.33           C  
ATOM   3624  CZ  PHE B 113      34.990  39.169  11.693  1.00 42.70           C  
ATOM   3625  N   ILE B 114      30.776  35.291  12.283  1.00 36.74           N  
ATOM   3626  CA  ILE B 114      30.576  34.748  10.971  1.00 36.42           C  
ATOM   3627  C   ILE B 114      29.151  35.000  10.505  1.00 35.52           C  
ATOM   3628  O   ILE B 114      28.943  35.507   9.404  1.00 35.80           O  
ATOM   3629  CB  ILE B 114      30.912  33.239  10.938  1.00 38.30           C  
ATOM   3630  CG1 ILE B 114      32.434  33.077  10.907  1.00 38.05           C  
ATOM   3631  CG2 ILE B 114      30.239  32.554   9.747  1.00 33.45           C  
ATOM   3632  CD1 ILE B 114      32.897  31.694  10.515  1.00 39.42           C  
ATOM   3633  N   GLY B 115      28.166  34.659  11.326  1.00 35.80           N  
ATOM   3634  CA  GLY B 115      26.786  34.893  10.932  1.00 39.02           C  
ATOM   3635  C   GLY B 115      26.571  36.342  10.531  1.00 40.46           C  
ATOM   3636  O   GLY B 115      25.849  36.652   9.580  1.00 40.27           O  
ATOM   3637  N   GLY B 116      27.223  37.243  11.252  1.00 40.78           N  
ATOM   3638  CA  GLY B 116      27.084  38.650  10.957  1.00 42.20           C  
ATOM   3639  C   GLY B 116      27.729  39.120   9.669  1.00 44.33           C  
ATOM   3640  O   GLY B 116      27.108  39.860   8.908  1.00 46.57           O  
ATOM   3641  N   ILE B 117      28.965  38.707   9.406  1.00 43.65           N  
ATOM   3642  CA  ILE B 117      29.637  39.172   8.199  1.00 43.63           C  
ATOM   3643  C   ILE B 117      28.957  38.618   6.945  1.00 44.41           C  
ATOM   3644  O   ILE B 117      28.872  39.304   5.918  1.00 44.64           O  
ATOM   3645  CB  ILE B 117      31.172  38.807   8.191  1.00 42.68           C  
ATOM   3646  CG1 ILE B 117      31.429  37.520   7.423  1.00 40.09           C  
ATOM   3647  CG2 ILE B 117      31.689  38.631   9.593  1.00 46.47           C  
ATOM   3648  CD1 ILE B 117      31.717  37.761   5.991  1.00 42.73           C  
ATOM   3649  N   PHE B 118      28.450  37.392   7.023  1.00 42.56           N  
ATOM   3650  CA  PHE B 118      27.808  36.810   5.865  1.00 41.87           C  
ATOM   3651  C   PHE B 118      26.355  37.189   5.689  1.00 40.19           C  
ATOM   3652  O   PHE B 118      25.791  37.055   4.597  1.00 35.20           O  
ATOM   3653  CB  PHE B 118      28.041  35.303   5.847  1.00 41.75           C  
ATOM   3654  CG  PHE B 118      29.463  34.957   5.515  1.00 41.72           C  
ATOM   3655  CD1 PHE B 118      29.985  35.298   4.273  1.00 39.53           C  
ATOM   3656  CD2 PHE B 118      30.314  34.413   6.474  1.00 42.94           C  
ATOM   3657  CE1 PHE B 118      31.337  35.113   3.993  1.00 41.18           C  
ATOM   3658  CE2 PHE B 118      31.664  34.223   6.204  1.00 37.26           C  
ATOM   3659  CZ  PHE B 118      32.181  34.576   4.958  1.00 38.50           C  
ATOM   3660  N   GLY B 119      25.747  37.689   6.756  1.00 40.73           N  
ATOM   3661  CA  GLY B 119      24.381  38.162   6.638  1.00 44.74           C  
ATOM   3662  C   GLY B 119      24.530  39.456   5.840  1.00 46.22           C  
ATOM   3663  O   GLY B 119      23.816  39.709   4.871  1.00 44.81           O  
ATOM   3664  N   PHE B 120      25.499  40.273   6.249  1.00 46.22           N  
ATOM   3665  CA  PHE B 120      25.770  41.546   5.583  1.00 43.23           C  
ATOM   3666  C   PHE B 120      26.264  41.321   4.161  1.00 44.08           C  
ATOM   3667  O   PHE B 120      25.989  42.120   3.269  1.00 44.76           O  
ATOM   3668  CB  PHE B 120      26.854  42.320   6.326  1.00 40.81           C  
ATOM   3669  CG  PHE B 120      26.460  42.762   7.689  1.00 39.40           C  
ATOM   3670  CD1 PHE B 120      27.424  42.932   8.673  1.00 38.60           C  
ATOM   3671  CD2 PHE B 120      25.133  43.022   7.996  1.00 38.74           C  
ATOM   3672  CE1 PHE B 120      27.079  43.353   9.943  1.00 38.68           C  
ATOM   3673  CE2 PHE B 120      24.774  43.443   9.260  1.00 39.28           C  
ATOM   3674  CZ  PHE B 120      25.748  43.611  10.244  1.00 40.99           C  
ATOM   3675  N   MET B 121      27.019  40.239   3.977  1.00 45.22           N  
ATOM   3676  CA  MET B 121      27.584  39.918   2.682  1.00 42.33           C  
ATOM   3677  C   MET B 121      26.533  39.576   1.636  1.00 42.18           C  
ATOM   3678  O   MET B 121      26.715  39.875   0.466  1.00 41.86           O  
ATOM   3679  CB  MET B 121      28.588  38.772   2.798  1.00 43.29           C  
ATOM   3680  CG  MET B 121      29.320  38.498   1.489  1.00 44.35           C  
ATOM   3681  SD  MET B 121      31.003  37.898   1.704  1.00 46.47           S  
ATOM   3682  CE  MET B 121      30.920  36.414   0.787  1.00 54.23           C  
ATOM   3683  N   SER B 122      25.429  38.973   2.058  1.00 43.11           N  
ATOM   3684  CA  SER B 122      24.384  38.612   1.127  1.00 45.40           C  
ATOM   3685  C   SER B 122      23.588  39.805   0.588  1.00 46.59           C  
ATOM   3686  O   SER B 122      23.329  39.889  -0.622  1.00 47.91           O  
ATOM   3687  CB  SER B 122      23.452  37.570   1.754  1.00 46.86           C  
ATOM   3688  OG  SER B 122      24.098  36.303   1.822  1.00 44.08           O  
ATOM   3689  N   ILE B 123      23.196  40.736   1.449  1.00 44.46           N  
ATOM   3690  CA  ILE B 123      22.462  41.900   0.953  1.00 45.29           C  
ATOM   3691  C   ILE B 123      23.371  42.797   0.123  1.00 45.24           C  
ATOM   3692  O   ILE B 123      22.983  43.262  -0.942  1.00 48.63           O  
ATOM   3693  CB  ILE B 123      21.869  42.755   2.090  1.00 45.91           C  
ATOM   3694  CG1 ILE B 123      22.316  42.196   3.441  1.00 47.50           C  
ATOM   3695  CG2 ILE B 123      20.342  42.820   1.939  1.00 43.80           C  
ATOM   3696  CD1 ILE B 123      21.878  43.009   4.631  1.00 50.96           C  
ATOM   3697  N   MET B 124      24.585  43.034   0.602  1.00 45.44           N  
ATOM   3698  CA  MET B 124      25.504  43.890  -0.121  1.00 44.83           C  
ATOM   3699  C   MET B 124      25.848  43.290  -1.487  1.00 45.57           C  
ATOM   3700  O   MET B 124      26.105  44.016  -2.449  1.00 46.25           O  
ATOM   3701  CB  MET B 124      26.774  44.121   0.701  1.00 44.84           C  
ATOM   3702  CG  MET B 124      27.625  45.271   0.188  1.00 48.53           C  
ATOM   3703  SD  MET B 124      26.633  46.737  -0.263  1.00 48.33           S  
ATOM   3704  CE  MET B 124      26.262  47.396   1.317  1.00 48.04           C  
ATOM   3705  N   THR B 125      25.851  41.964  -1.576  1.00 42.93           N  
ATOM   3706  CA  THR B 125      26.141  41.329  -2.838  1.00 40.17           C  
ATOM   3707  C   THR B 125      24.909  41.508  -3.692  1.00 40.82           C  
ATOM   3708  O   THR B 125      25.003  41.659  -4.903  1.00 41.27           O  
ATOM   3709  CB  THR B 125      26.441  39.843  -2.673  1.00 39.60           C  
ATOM   3710  OG1 THR B 125      27.646  39.696  -1.920  1.00 41.95           O  
ATOM   3711  CG2 THR B 125      26.617  39.173  -4.044  1.00 37.97           C  
ATOM   3712  N   MET B 126      23.746  41.498  -3.051  1.00 42.24           N  
ATOM   3713  CA  MET B 126      22.500  41.705  -3.773  1.00 44.07           C  
ATOM   3714  C   MET B 126      22.472  43.156  -4.270  1.00 43.67           C  
ATOM   3715  O   MET B 126      22.016  43.440  -5.374  1.00 41.27           O  
ATOM   3716  CB  MET B 126      21.301  41.403  -2.868  1.00 46.49           C  
ATOM   3717  CG  MET B 126      21.017  39.911  -2.732  1.00 45.30           C  
ATOM   3718  SD  MET B 126      19.673  39.487  -1.608  1.00 49.55           S  
ATOM   3719  CE  MET B 126      20.442  38.191  -0.646  1.00 48.88           C  
ATOM   3720  N   ALA B 127      22.975  44.082  -3.465  1.00 44.23           N  
ATOM   3721  CA  ALA B 127      22.998  45.465  -3.908  1.00 45.64           C  
ATOM   3722  C   ALA B 127      23.925  45.560  -5.128  1.00 45.88           C  
ATOM   3723  O   ALA B 127      23.672  46.330  -6.048  1.00 48.85           O  
ATOM   3724  CB  ALA B 127      23.483  46.377  -2.793  1.00 44.74           C  
ATOM   3725  N   MET B 128      24.997  44.775  -5.135  1.00 45.00           N  
ATOM   3726  CA  MET B 128      25.924  44.805  -6.259  1.00 47.35           C  
ATOM   3727  C   MET B 128      25.235  44.275  -7.524  1.00 48.24           C  
ATOM   3728  O   MET B 128      25.460  44.776  -8.631  1.00 44.88           O  
ATOM   3729  CB  MET B 128      27.165  43.971  -5.961  1.00 46.35           C  
ATOM   3730  CG  MET B 128      27.992  44.519  -4.827  1.00 53.69           C  
ATOM   3731  SD  MET B 128      28.438  46.260  -5.045  1.00 59.73           S  
ATOM   3732  CE  MET B 128      27.092  47.055  -4.153  1.00 57.95           C  
ATOM   3733  N   ILE B 129      24.401  43.256  -7.334  1.00 46.83           N  
ATOM   3734  CA  ILE B 129      23.658  42.654  -8.416  1.00 44.39           C  
ATOM   3735  C   ILE B 129      22.682  43.675  -8.956  1.00 45.89           C  
ATOM   3736  O   ILE B 129      22.599  43.883 -10.167  1.00 48.17           O  
ATOM   3737  CB  ILE B 129      22.896  41.408  -7.934  1.00 42.01           C  
ATOM   3738  CG1 ILE B 129      23.877  40.251  -7.759  1.00 42.38           C  
ATOM   3739  CG2 ILE B 129      21.771  41.050  -8.902  1.00 37.08           C  
ATOM   3740  CD1 ILE B 129      23.304  39.060  -7.042  1.00 42.74           C  
ATOM   3741  N   SER B 130      21.954  44.326  -8.062  1.00 46.98           N  
ATOM   3742  CA  SER B 130      20.978  45.319  -8.473  1.00 48.20           C  
ATOM   3743  C   SER B 130      21.658  46.400  -9.299  1.00 48.49           C  
ATOM   3744  O   SER B 130      21.110  46.857 -10.304  1.00 47.38           O  
ATOM   3745  CB  SER B 130      20.273  45.924  -7.245  1.00 49.68           C  
ATOM   3746  OG  SER B 130      21.187  46.410  -6.279  1.00 48.23           O  
ATOM   3747  N   ILE B 131      22.861  46.785  -8.881  1.00 49.52           N  
ATOM   3748  CA  ILE B 131      23.625  47.801  -9.594  1.00 50.81           C  
ATOM   3749  C   ILE B 131      23.800  47.369 -11.050  1.00 54.73           C  
ATOM   3750  O   ILE B 131      23.682  48.180 -11.974  1.00 57.21           O  
ATOM   3751  CB  ILE B 131      25.021  47.996  -8.961  1.00 48.77           C  
ATOM   3752  CG1 ILE B 131      24.887  48.697  -7.605  1.00 46.23           C  
ATOM   3753  CG2 ILE B 131      25.920  48.792  -9.893  1.00 43.87           C  
ATOM   3754  CD1 ILE B 131      26.215  48.942  -6.925  1.00 42.20           C  
ATOM   3755  N   ASP B 132      24.077  46.084 -11.245  1.00 55.64           N  
ATOM   3756  CA  ASP B 132      24.257  45.534 -12.577  1.00 55.75           C  
ATOM   3757  C   ASP B 132      22.913  45.498 -13.287  1.00 57.79           C  
ATOM   3758  O   ASP B 132      22.778  45.987 -14.402  1.00 57.57           O  
ATOM   3759  CB  ASP B 132      24.822  44.119 -12.492  1.00 54.59           C  
ATOM   3760  CG  ASP B 132      25.031  43.494 -13.858  1.00 54.73           C  
ATOM   3761  OD1 ASP B 132      24.645  42.324 -14.041  1.00 54.38           O  
ATOM   3762  OD2 ASP B 132      25.586  44.173 -14.746  1.00 55.11           O  
ATOM   3763  N   ARG B 133      21.922  44.909 -12.626  1.00 59.45           N  
ATOM   3764  CA  ARG B 133      20.581  44.799 -13.181  1.00 61.43           C  
ATOM   3765  C   ARG B 133      20.099  46.158 -13.667  1.00 63.91           C  
ATOM   3766  O   ARG B 133      19.400  46.257 -14.670  1.00 65.19           O  
ATOM   3767  CB  ARG B 133      19.620  44.255 -12.122  1.00 62.19           C  
ATOM   3768  CG  ARG B 133      19.000  42.888 -12.440  1.00 62.33           C  
ATOM   3769  CD  ARG B 133      20.040  41.816 -12.775  1.00 57.99           C  
ATOM   3770  NE  ARG B 133      20.024  41.482 -14.193  1.00 54.86           N  
ATOM   3771  CZ  ARG B 133      21.069  41.618 -15.003  1.00 56.48           C  
ATOM   3772  NH1 ARG B 133      22.216  42.083 -14.526  1.00 54.08           N  
ATOM   3773  NH2 ARG B 133      20.969  41.297 -16.291  1.00 52.91           N  
ATOM   3774  N   TYR B 134      20.476  47.210 -12.951  1.00 66.09           N  
ATOM   3775  CA  TYR B 134      20.070  48.558 -13.330  1.00 66.83           C  
ATOM   3776  C   TYR B 134      20.859  49.103 -14.525  1.00 65.86           C  
ATOM   3777  O   TYR B 134      20.389  49.986 -15.226  1.00 63.67           O  
ATOM   3778  CB  TYR B 134      20.194  49.495 -12.119  1.00 67.25           C  
ATOM   3779  CG  TYR B 134      20.472  50.946 -12.454  1.00 68.24           C  
ATOM   3780  CD1 TYR B 134      21.780  51.425 -12.500  1.00 68.51           C  
ATOM   3781  CD2 TYR B 134      19.434  51.836 -12.725  1.00 67.97           C  
ATOM   3782  CE1 TYR B 134      22.049  52.752 -12.803  1.00 68.53           C  
ATOM   3783  CE2 TYR B 134      19.692  53.166 -13.033  1.00 68.61           C  
ATOM   3784  CZ  TYR B 134      21.002  53.617 -13.069  1.00 70.09           C  
ATOM   3785  OH  TYR B 134      21.264  54.937 -13.363  1.00 72.64           O  
ATOM   3786  N   ASN B 135      22.053  48.565 -14.758  1.00 67.34           N  
ATOM   3787  CA  ASN B 135      22.879  49.016 -15.873  1.00 68.39           C  
ATOM   3788  C   ASN B 135      22.539  48.322 -17.197  1.00 68.49           C  
ATOM   3789  O   ASN B 135      22.964  48.753 -18.265  1.00 67.93           O  
ATOM   3790  CB  ASN B 135      24.362  48.816 -15.555  1.00 68.96           C  
ATOM   3791  CG  ASN B 135      24.879  49.818 -14.537  1.00 71.27           C  
ATOM   3792  OD1 ASN B 135      24.609  51.016 -14.639  1.00 73.26           O  
ATOM   3793  ND2 ASN B 135      25.638  49.337 -13.561  1.00 71.54           N  
ATOM   3794  N   VAL B 136      21.764  47.251 -17.121  1.00 69.03           N  
ATOM   3795  CA  VAL B 136      21.390  46.521 -18.312  1.00 70.04           C  
ATOM   3796  C   VAL B 136      19.917  46.732 -18.633  1.00 72.33           C  
ATOM   3797  O   VAL B 136      19.505  46.614 -19.789  1.00 75.16           O  
ATOM   3798  CB  VAL B 136      21.656  45.014 -18.144  1.00 68.92           C  
ATOM   3799  CG1 VAL B 136      23.146  44.768 -17.966  1.00 68.28           C  
ATOM   3800  CG2 VAL B 136      20.891  44.491 -16.947  1.00 68.46           C  
ATOM   3801  N   ILE B 137      19.128  47.043 -17.610  1.00 72.26           N  
ATOM   3802  CA  ILE B 137      17.699  47.270 -17.789  1.00 73.12           C  
ATOM   3803  C   ILE B 137      17.359  48.710 -17.426  1.00 75.27           C  
ATOM   3804  O   ILE B 137      17.013  49.514 -18.290  1.00 78.01           O  
ATOM   3805  CB  ILE B 137      16.856  46.338 -16.895  1.00 73.38           C  
ATOM   3806  CG1 ILE B 137      17.325  44.887 -17.043  1.00 73.43           C  
ATOM   3807  CG2 ILE B 137      15.385  46.470 -17.250  1.00 73.73           C  
ATOM   3808  CD1 ILE B 137      17.315  44.365 -18.465  1.00 71.93           C  
ATOM   3809  N   GLY B 138      17.470  49.025 -16.139  1.00 76.59           N  
ATOM   3810  CA  GLY B 138      17.165  50.358 -15.653  1.00 75.59           C  
ATOM   3811  C   GLY B 138      17.559  51.509 -16.553  1.00 75.60           C  
ATOM   3812  O   GLY B 138      16.911  52.553 -16.541  1.00 77.62           O  
ATOM   3813  N   ARG B 139      18.610  51.335 -17.341  1.00 75.90           N  
ATOM   3814  CA  ARG B 139      19.061  52.402 -18.224  1.00 77.14           C  
ATOM   3815  C   ARG B 139      18.597  52.202 -19.666  1.00 79.73           C  
ATOM   3816  O   ARG B 139      18.136  51.122 -20.034  1.00 80.39           O  
ATOM   3817  CB  ARG B 139      20.585  52.512 -18.166  1.00 74.63           C  
ATOM   3818  CG  ARG B 139      21.128  52.639 -16.759  1.00 71.46           C  
ATOM   3819  CD  ARG B 139      22.529  53.180 -16.783  1.00 72.20           C  
ATOM   3820  NE  ARG B 139      22.542  54.544 -17.300  1.00 71.84           N  
ATOM   3821  CZ  ARG B 139      23.641  55.198 -17.662  1.00 73.60           C  
ATOM   3822  NH1 ARG B 139      24.831  54.619 -17.565  1.00 73.21           N  
ATOM   3823  NH2 ARG B 139      23.548  56.432 -18.132  1.00 74.19           N  
ATOM   3824  N   PRO B 140      18.699  53.254 -20.497  1.00 81.93           N  
ATOM   3825  CA  PRO B 140      18.291  53.205 -21.904  1.00 84.30           C  
ATOM   3826  C   PRO B 140      19.048  52.184 -22.749  1.00 86.87           C  
ATOM   3827  O   PRO B 140      20.197  51.853 -22.466  1.00 87.60           O  
ATOM   3828  CB  PRO B 140      18.539  54.632 -22.383  1.00 83.56           C  
ATOM   3829  CG  PRO B 140      18.304  55.440 -21.157  1.00 82.46           C  
ATOM   3830  CD  PRO B 140      19.024  54.635 -20.104  1.00 82.35           C  
ATOM   3831  N   MET B 141      18.382  51.701 -23.794  1.00 90.01           N  
ATOM   3832  CA  MET B 141      18.948  50.729 -24.722  1.00 90.46           C  
ATOM   3833  C   MET B 141      20.395  51.053 -25.072  1.00 89.40           C  
ATOM   3834  O   MET B 141      21.286  50.212 -24.936  1.00 89.25           O  
ATOM   3835  CB  MET B 141      18.123  50.706 -26.007  1.00 94.86           C  
ATOM   3836  CG  MET B 141      16.702  50.222 -25.832  1.00100.58           C  
ATOM   3837  SD  MET B 141      16.640  48.441 -25.648  1.00106.76           S  
ATOM   3838  CE  MET B 141      16.981  48.268 -23.898  1.00106.95           C  
ATOM   3839  N   ALA B 142      20.616  52.280 -25.531  1.00 87.46           N  
ATOM   3840  CA  ALA B 142      21.947  52.730 -25.918  1.00 86.16           C  
ATOM   3841  C   ALA B 142      22.858  52.894 -24.712  1.00 84.78           C  
ATOM   3842  O   ALA B 142      24.079  52.912 -24.846  1.00 84.87           O  
ATOM   3843  CB  ALA B 142      21.850  54.047 -26.677  1.00 85.97           C  
ATOM   3844  N   ALA B 143      22.257  53.010 -23.534  1.00 83.41           N  
ATOM   3845  CA  ALA B 143      23.021  53.186 -22.308  1.00 82.50           C  
ATOM   3846  C   ALA B 143      23.416  51.861 -21.668  1.00 82.07           C  
ATOM   3847  O   ALA B 143      24.431  51.781 -20.976  1.00 82.10           O  
ATOM   3848  CB  ALA B 143      22.223  54.021 -21.319  1.00 82.53           C  
ATOM   3849  N   SER B 144      22.612  50.829 -21.905  1.00 80.64           N  
ATOM   3850  CA  SER B 144      22.854  49.506 -21.340  1.00 79.91           C  
ATOM   3851  C   SER B 144      24.338  49.122 -21.313  1.00 80.17           C  
ATOM   3852  O   SER B 144      25.060  49.298 -22.294  1.00 79.64           O  
ATOM   3853  CB  SER B 144      22.054  48.457 -22.114  1.00 78.76           C  
ATOM   3854  OG  SER B 144      21.997  47.239 -21.400  1.00 77.48           O  
ATOM   3855  N   LYS B 145      24.778  48.597 -20.173  1.00 79.93           N  
ATOM   3856  CA  LYS B 145      26.165  48.191 -19.984  1.00 79.36           C  
ATOM   3857  C   LYS B 145      26.231  46.820 -19.310  1.00 78.54           C  
ATOM   3858  O   LYS B 145      25.629  46.610 -18.259  1.00 77.98           O  
ATOM   3859  CB  LYS B 145      26.896  49.221 -19.116  1.00 80.18           C  
ATOM   3860  CG  LYS B 145      28.368  48.913 -18.858  1.00 81.24           C  
ATOM   3861  CD  LYS B 145      28.933  49.767 -17.722  1.00 81.61           C  
ATOM   3862  CE  LYS B 145      29.205  51.207 -18.134  1.00 82.07           C  
ATOM   3863  NZ  LYS B 145      30.412  51.343 -19.002  1.00 81.51           N  
ATOM   3864  N   LYS B 146      26.961  45.894 -19.926  1.00 76.99           N  
ATOM   3865  CA  LYS B 146      27.122  44.549 -19.392  1.00 74.45           C  
ATOM   3866  C   LYS B 146      28.231  44.600 -18.341  1.00 71.37           C  
ATOM   3867  O   LYS B 146      29.184  45.361 -18.486  1.00 71.20           O  
ATOM   3868  CB  LYS B 146      27.525  43.584 -20.514  1.00 76.33           C  
ATOM   3869  CG  LYS B 146      26.616  42.365 -20.692  1.00 77.37           C  
ATOM   3870  CD  LYS B 146      25.299  42.724 -21.351  1.00 77.68           C  
ATOM   3871  CE  LYS B 146      24.451  41.489 -21.588  1.00 77.74           C  
ATOM   3872  NZ  LYS B 146      23.178  41.812 -22.291  1.00 77.11           N  
ATOM   3873  N   MET B 147      28.112  43.800 -17.288  1.00 67.23           N  
ATOM   3874  CA  MET B 147      29.129  43.797 -16.247  1.00 64.02           C  
ATOM   3875  C   MET B 147      30.440  43.224 -16.781  1.00 63.60           C  
ATOM   3876  O   MET B 147      30.437  42.353 -17.655  1.00 63.15           O  
ATOM   3877  CB  MET B 147      28.663  42.969 -15.044  1.00 61.82           C  
ATOM   3878  CG  MET B 147      29.694  42.872 -13.931  1.00 58.88           C  
ATOM   3879  SD  MET B 147      30.101  44.492 -13.231  1.00 56.38           S  
ATOM   3880  CE  MET B 147      28.613  44.791 -12.316  1.00 53.61           C  
ATOM   3881  N   SER B 148      31.560  43.720 -16.265  1.00 61.44           N  
ATOM   3882  CA  SER B 148      32.864  43.227 -16.687  1.00 60.56           C  
ATOM   3883  C   SER B 148      33.579  42.607 -15.484  1.00 62.21           C  
ATOM   3884  O   SER B 148      33.220  42.870 -14.340  1.00 61.31           O  
ATOM   3885  CB  SER B 148      33.706  44.366 -17.269  1.00 54.57           C  
ATOM   3886  OG  SER B 148      34.145  45.254 -16.259  1.00 51.39           O  
ATOM   3887  N   HIS B 149      34.579  41.772 -15.745  1.00 66.01           N  
ATOM   3888  CA  HIS B 149      35.326  41.124 -14.677  1.00 70.43           C  
ATOM   3889  C   HIS B 149      36.011  42.193 -13.833  1.00 71.05           C  
ATOM   3890  O   HIS B 149      36.105  42.079 -12.608  1.00 71.06           O  
ATOM   3891  CB  HIS B 149      36.370  40.173 -15.269  1.00 76.05           C  
ATOM   3892  CG  HIS B 149      37.249  39.520 -14.247  1.00 85.71           C  
ATOM   3893  ND1 HIS B 149      38.507  39.041 -14.546  1.00 89.73           N  
ATOM   3894  CD2 HIS B 149      37.056  39.269 -12.930  1.00 90.31           C  
ATOM   3895  CE1 HIS B 149      39.051  38.526 -13.457  1.00 91.93           C  
ATOM   3896  NE2 HIS B 149      38.191  38.651 -12.462  1.00 92.78           N  
ATOM   3897  N   ARG B 150      36.483  43.239 -14.501  1.00 70.17           N  
ATOM   3898  CA  ARG B 150      37.170  44.343 -13.838  1.00 69.47           C  
ATOM   3899  C   ARG B 150      36.308  44.970 -12.736  1.00 67.58           C  
ATOM   3900  O   ARG B 150      36.711  45.007 -11.574  1.00 67.96           O  
ATOM   3901  CB  ARG B 150      37.569  45.403 -14.875  1.00 73.08           C  
ATOM   3902  CG  ARG B 150      38.254  44.821 -16.127  1.00 77.80           C  
ATOM   3903  CD  ARG B 150      37.239  44.163 -17.068  1.00 80.34           C  
ATOM   3904  NE  ARG B 150      37.815  43.113 -17.905  1.00 80.69           N  
ATOM   3905  CZ  ARG B 150      37.104  42.330 -18.714  1.00 80.45           C  
ATOM   3906  NH1 ARG B 150      37.704  41.395 -19.440  1.00 81.73           N  
ATOM   3907  NH2 ARG B 150      35.792  42.475 -18.801  1.00 78.14           N  
ATOM   3908  N   ARG B 151      35.125  45.459 -13.091  1.00 65.51           N  
ATOM   3909  CA  ARG B 151      34.237  46.063 -12.104  1.00 63.23           C  
ATOM   3910  C   ARG B 151      33.712  45.050 -11.090  1.00 61.99           C  
ATOM   3911  O   ARG B 151      33.670  45.326  -9.885  1.00 60.53           O  
ATOM   3912  CB  ARG B 151      33.054  46.756 -12.789  1.00 63.09           C  
ATOM   3913  CG  ARG B 151      33.297  48.231 -13.097  1.00 64.55           C  
ATOM   3914  CD  ARG B 151      32.109  48.863 -13.823  1.00 65.39           C  
ATOM   3915  NE  ARG B 151      31.959  48.352 -15.182  1.00 64.95           N  
ATOM   3916  CZ  ARG B 151      30.842  47.813 -15.658  1.00 65.56           C  
ATOM   3917  NH1 ARG B 151      29.769  47.712 -14.883  1.00 64.55           N  
ATOM   3918  NH2 ARG B 151      30.797  47.371 -16.908  1.00 64.71           N  
ATOM   3919  N   ALA B 152      33.312  43.877 -11.575  1.00 58.91           N  
ATOM   3920  CA  ALA B 152      32.781  42.837 -10.698  1.00 56.66           C  
ATOM   3921  C   ALA B 152      33.758  42.563  -9.567  1.00 54.72           C  
ATOM   3922  O   ALA B 152      33.368  42.441  -8.406  1.00 55.59           O  
ATOM   3923  CB  ALA B 152      32.526  41.561 -11.490  1.00 54.81           C  
ATOM   3924  N   PHE B 153      35.031  42.479  -9.929  1.00 55.59           N  
ATOM   3925  CA  PHE B 153      36.104  42.208  -8.990  1.00 56.83           C  
ATOM   3926  C   PHE B 153      36.236  43.314  -7.947  1.00 55.69           C  
ATOM   3927  O   PHE B 153      36.358  43.033  -6.756  1.00 56.21           O  
ATOM   3928  CB  PHE B 153      37.415  42.044  -9.754  1.00 62.57           C  
ATOM   3929  CG  PHE B 153      38.515  41.424  -8.946  1.00 68.33           C  
ATOM   3930  CD1 PHE B 153      38.351  40.162  -8.386  1.00 72.42           C  
ATOM   3931  CD2 PHE B 153      39.718  42.091  -8.755  1.00 69.51           C  
ATOM   3932  CE1 PHE B 153      39.370  39.571  -7.649  1.00 74.01           C  
ATOM   3933  CE2 PHE B 153      40.744  41.512  -8.020  1.00 72.48           C  
ATOM   3934  CZ  PHE B 153      40.571  40.249  -7.465  1.00 74.62           C  
ATOM   3935  N   ILE B 154      36.220  44.569  -8.389  1.00 53.85           N  
ATOM   3936  CA  ILE B 154      36.319  45.690  -7.463  1.00 51.47           C  
ATOM   3937  C   ILE B 154      35.141  45.603  -6.510  1.00 49.27           C  
ATOM   3938  O   ILE B 154      35.285  45.768  -5.298  1.00 49.58           O  
ATOM   3939  CB  ILE B 154      36.226  47.048  -8.184  1.00 52.86           C  
ATOM   3940  CG1 ILE B 154      37.409  47.224  -9.138  1.00 52.95           C  
ATOM   3941  CG2 ILE B 154      36.159  48.177  -7.152  1.00 52.61           C  
ATOM   3942  CD1 ILE B 154      37.301  48.459 -10.037  1.00 50.02           C  
ATOM   3943  N   MET B 155      33.969  45.340  -7.069  1.00 47.01           N  
ATOM   3944  CA  MET B 155      32.764  45.233  -6.262  1.00 45.69           C  
ATOM   3945  C   MET B 155      32.804  44.139  -5.189  1.00 45.91           C  
ATOM   3946  O   MET B 155      32.423  44.400  -4.049  1.00 47.19           O  
ATOM   3947  CB  MET B 155      31.543  45.057  -7.173  1.00 46.59           C  
ATOM   3948  CG  MET B 155      30.950  46.383  -7.641  1.00 43.15           C  
ATOM   3949  SD  MET B 155      30.230  46.377  -9.307  1.00 46.53           S  
ATOM   3950  CE  MET B 155      28.458  46.211  -8.957  1.00 40.42           C  
ATOM   3951  N   ILE B 156      33.270  42.932  -5.513  1.00 44.65           N  
ATOM   3952  CA  ILE B 156      33.291  41.895  -4.481  1.00 45.96           C  
ATOM   3953  C   ILE B 156      34.276  42.234  -3.353  1.00 43.80           C  
ATOM   3954  O   ILE B 156      34.011  41.963  -2.184  1.00 37.74           O  
ATOM   3955  CB  ILE B 156      33.637  40.495  -5.041  1.00 48.59           C  
ATOM   3956  CG1 ILE B 156      35.052  40.487  -5.605  1.00 54.47           C  
ATOM   3957  CG2 ILE B 156      32.611  40.087  -6.093  1.00 48.04           C  
ATOM   3958  CD1 ILE B 156      35.538  39.110  -6.001  1.00 60.32           C  
ATOM   3959  N   ILE B 157      35.411  42.829  -3.707  1.00 42.54           N  
ATOM   3960  CA  ILE B 157      36.392  43.206  -2.709  1.00 41.67           C  
ATOM   3961  C   ILE B 157      35.732  44.232  -1.797  1.00 42.47           C  
ATOM   3962  O   ILE B 157      35.937  44.232  -0.576  1.00 44.10           O  
ATOM   3963  CB  ILE B 157      37.661  43.789  -3.367  1.00 42.05           C  
ATOM   3964  CG1 ILE B 157      38.378  42.681  -4.135  1.00 44.49           C  
ATOM   3965  CG2 ILE B 157      38.597  44.349  -2.324  1.00 37.04           C  
ATOM   3966  CD1 ILE B 157      39.621  43.140  -4.863  1.00 51.28           C  
ATOM   3967  N   PHE B 158      34.918  45.100  -2.385  1.00 41.90           N  
ATOM   3968  CA  PHE B 158      34.213  46.090  -1.583  1.00 40.23           C  
ATOM   3969  C   PHE B 158      33.299  45.350  -0.607  1.00 37.56           C  
ATOM   3970  O   PHE B 158      33.296  45.636   0.581  1.00 36.54           O  
ATOM   3971  CB  PHE B 158      33.365  47.024  -2.452  1.00 41.09           C  
ATOM   3972  CG  PHE B 158      32.412  47.861  -1.656  1.00 40.76           C  
ATOM   3973  CD1 PHE B 158      32.896  48.842  -0.791  1.00 41.35           C  
ATOM   3974  CD2 PHE B 158      31.050  47.595  -1.676  1.00 38.73           C  
ATOM   3975  CE1 PHE B 158      32.044  49.537   0.053  1.00 41.42           C  
ATOM   3976  CE2 PHE B 158      30.180  48.279  -0.840  1.00 40.06           C  
ATOM   3977  CZ  PHE B 158      30.681  49.252   0.030  1.00 44.09           C  
ATOM   3978  N   VAL B 159      32.526  44.397  -1.117  1.00 38.37           N  
ATOM   3979  CA  VAL B 159      31.628  43.625  -0.267  1.00 39.53           C  
ATOM   3980  C   VAL B 159      32.368  42.947   0.890  1.00 40.96           C  
ATOM   3981  O   VAL B 159      31.883  42.934   2.019  1.00 42.88           O  
ATOM   3982  CB  VAL B 159      30.892  42.517  -1.061  1.00 41.76           C  
ATOM   3983  CG1 VAL B 159      29.968  41.745  -0.123  1.00 41.40           C  
ATOM   3984  CG2 VAL B 159      30.096  43.132  -2.224  1.00 39.55           C  
ATOM   3985  N   TRP B 160      33.534  42.378   0.609  1.00 39.68           N  
ATOM   3986  CA  TRP B 160      34.298  41.710   1.642  1.00 41.77           C  
ATOM   3987  C   TRP B 160      34.777  42.660   2.740  1.00 43.83           C  
ATOM   3988  O   TRP B 160      34.610  42.382   3.928  1.00 42.98           O  
ATOM   3989  CB  TRP B 160      35.474  40.949   1.023  1.00 41.71           C  
ATOM   3990  CG  TRP B 160      35.060  39.600   0.525  1.00 40.00           C  
ATOM   3991  CD1 TRP B 160      34.438  39.316  -0.658  1.00 39.54           C  
ATOM   3992  CD2 TRP B 160      35.095  38.376   1.262  1.00 38.80           C  
ATOM   3993  NE1 TRP B 160      34.070  37.994  -0.700  1.00 37.14           N  
ATOM   3994  CE2 TRP B 160      34.460  37.392   0.470  1.00 40.13           C  
ATOM   3995  CE3 TRP B 160      35.596  38.015   2.522  1.00 39.32           C  
ATOM   3996  CZ2 TRP B 160      34.306  36.069   0.897  1.00 37.40           C  
ATOM   3997  CZ3 TRP B 160      35.446  36.692   2.951  1.00 39.88           C  
ATOM   3998  CH2 TRP B 160      34.802  35.737   2.136  1.00 41.48           C  
ATOM   3999  N   LEU B 161      35.371  43.781   2.346  1.00 46.00           N  
ATOM   4000  CA  LEU B 161      35.851  44.770   3.308  1.00 44.30           C  
ATOM   4001  C   LEU B 161      34.679  45.334   4.097  1.00 42.66           C  
ATOM   4002  O   LEU B 161      34.754  45.506   5.315  1.00 42.71           O  
ATOM   4003  CB  LEU B 161      36.565  45.915   2.588  1.00 44.17           C  
ATOM   4004  CG  LEU B 161      37.909  45.552   1.968  1.00 45.95           C  
ATOM   4005  CD1 LEU B 161      38.329  46.628   0.985  1.00 46.02           C  
ATOM   4006  CD2 LEU B 161      38.949  45.367   3.069  1.00 43.29           C  
ATOM   4007  N   TRP B 162      33.593  45.628   3.397  1.00 40.79           N  
ATOM   4008  CA  TRP B 162      32.422  46.178   4.047  1.00 38.88           C  
ATOM   4009  C   TRP B 162      31.895  45.210   5.090  1.00 39.68           C  
ATOM   4010  O   TRP B 162      31.869  45.508   6.287  1.00 42.31           O  
ATOM   4011  CB  TRP B 162      31.338  46.449   3.015  1.00 39.70           C  
ATOM   4012  CG  TRP B 162      30.208  47.266   3.522  1.00 41.41           C  
ATOM   4013  CD1 TRP B 162      28.933  46.844   3.773  1.00 39.73           C  
ATOM   4014  CD2 TRP B 162      30.227  48.670   3.789  1.00 42.43           C  
ATOM   4015  NE1 TRP B 162      28.156  47.903   4.170  1.00 38.39           N  
ATOM   4016  CE2 TRP B 162      28.926  49.036   4.187  1.00 42.96           C  
ATOM   4017  CE3 TRP B 162      31.217  49.654   3.725  1.00 40.13           C  
ATOM   4018  CZ2 TRP B 162      28.588  50.351   4.516  1.00 43.60           C  
ATOM   4019  CZ3 TRP B 162      30.887  50.957   4.051  1.00 40.28           C  
ATOM   4020  CH2 TRP B 162      29.579  51.297   4.441  1.00 42.15           C  
ATOM   4021  N   SER B 163      31.489  44.036   4.626  1.00 40.65           N  
ATOM   4022  CA  SER B 163      30.930  43.020   5.507  1.00 41.20           C  
ATOM   4023  C   SER B 163      31.733  42.723   6.759  1.00 38.23           C  
ATOM   4024  O   SER B 163      31.174  42.675   7.847  1.00 40.35           O  
ATOM   4025  CB  SER B 163      30.684  41.728   4.728  1.00 42.71           C  
ATOM   4026  OG  SER B 163      29.698  41.940   3.731  1.00 47.12           O  
ATOM   4027  N   VAL B 164      33.036  42.519   6.620  1.00 37.26           N  
ATOM   4028  CA  VAL B 164      33.843  42.209   7.795  1.00 34.72           C  
ATOM   4029  C   VAL B 164      33.944  43.420   8.712  1.00 33.77           C  
ATOM   4030  O   VAL B 164      33.897  43.283   9.943  1.00 30.82           O  
ATOM   4031  CB  VAL B 164      35.269  41.708   7.392  1.00 36.15           C  
ATOM   4032  CG1 VAL B 164      36.148  41.560   8.620  1.00 32.41           C  
ATOM   4033  CG2 VAL B 164      35.155  40.346   6.679  1.00 32.11           C  
ATOM   4034  N   LEU B 165      34.052  44.603   8.109  1.00 33.82           N  
ATOM   4035  CA  LEU B 165      34.160  45.840   8.874  1.00 37.71           C  
ATOM   4036  C   LEU B 165      32.971  46.059   9.804  1.00 40.17           C  
ATOM   4037  O   LEU B 165      33.152  46.384  10.984  1.00 40.71           O  
ATOM   4038  CB  LEU B 165      34.301  47.040   7.953  1.00 35.04           C  
ATOM   4039  CG  LEU B 165      34.230  48.414   8.641  1.00 37.96           C  
ATOM   4040  CD1 LEU B 165      35.296  48.533   9.737  1.00 31.00           C  
ATOM   4041  CD2 LEU B 165      34.409  49.509   7.585  1.00 37.38           C  
ATOM   4042  N   TRP B 166      31.756  45.876   9.297  1.00 41.10           N  
ATOM   4043  CA  TRP B 166      30.598  46.088  10.145  1.00 42.91           C  
ATOM   4044  C   TRP B 166      30.205  44.901  11.024  1.00 45.44           C  
ATOM   4045  O   TRP B 166      29.169  44.930  11.690  1.00 49.36           O  
ATOM   4046  CB  TRP B 166      29.409  46.582   9.306  1.00 42.28           C  
ATOM   4047  CG  TRP B 166      29.730  47.886   8.675  1.00 41.84           C  
ATOM   4048  CD1 TRP B 166      29.904  48.139   7.342  1.00 45.14           C  
ATOM   4049  CD2 TRP B 166      30.094  49.087   9.359  1.00 40.89           C  
ATOM   4050  NE1 TRP B 166      30.368  49.419   7.159  1.00 44.94           N  
ATOM   4051  CE2 TRP B 166      30.495  50.022   8.382  1.00 42.14           C  
ATOM   4052  CE3 TRP B 166      30.129  49.461  10.705  1.00 38.77           C  
ATOM   4053  CZ2 TRP B 166      30.929  51.306   8.715  1.00 42.63           C  
ATOM   4054  CZ3 TRP B 166      30.558  50.733  11.036  1.00 37.04           C  
ATOM   4055  CH2 TRP B 166      30.954  51.639  10.050  1.00 40.38           C  
ATOM   4056  N   ALA B 167      31.029  43.861  11.048  1.00 46.27           N  
ATOM   4057  CA  ALA B 167      30.744  42.716  11.911  1.00 44.20           C  
ATOM   4058  C   ALA B 167      31.888  42.555  12.909  1.00 41.95           C  
ATOM   4059  O   ALA B 167      31.729  41.955  13.963  1.00 39.95           O  
ATOM   4060  CB  ALA B 167      30.574  41.429  11.082  1.00 40.41           C  
ATOM   4061  N   ILE B 168      33.035  43.130  12.573  1.00 42.37           N  
ATOM   4062  CA  ILE B 168      34.230  43.037  13.406  1.00 42.38           C  
ATOM   4063  C   ILE B 168      34.098  43.750  14.753  1.00 43.01           C  
ATOM   4064  O   ILE B 168      34.669  43.314  15.752  1.00 44.98           O  
ATOM   4065  CB  ILE B 168      35.473  43.598  12.630  1.00 44.03           C  
ATOM   4066  CG1 ILE B 168      36.757  42.970  13.166  1.00 43.36           C  
ATOM   4067  CG2 ILE B 168      35.529  45.106  12.715  1.00 37.57           C  
ATOM   4068  CD1 ILE B 168      36.908  41.522  12.794  1.00 41.06           C  
ATOM   4069  N   GLY B 169      33.332  44.838  14.772  1.00 41.68           N  
ATOM   4070  CA  GLY B 169      33.147  45.621  15.986  1.00 36.33           C  
ATOM   4071  C   GLY B 169      33.084  44.887  17.317  1.00 35.15           C  
ATOM   4072  O   GLY B 169      33.863  45.180  18.220  1.00 37.78           O  
ATOM   4073  N   PRO B 170      32.161  43.938  17.485  1.00 35.58           N  
ATOM   4074  CA  PRO B 170      32.126  43.256  18.778  1.00 32.93           C  
ATOM   4075  C   PRO B 170      33.376  42.445  19.149  1.00 33.54           C  
ATOM   4076  O   PRO B 170      33.650  42.220  20.333  1.00 30.63           O  
ATOM   4077  CB  PRO B 170      30.882  42.387  18.664  1.00 35.14           C  
ATOM   4078  CG  PRO B 170      29.972  43.225  17.790  1.00 33.63           C  
ATOM   4079  CD  PRO B 170      30.934  43.670  16.708  1.00 34.62           C  
ATOM   4080  N   ILE B 171      34.141  41.993  18.169  1.00 32.69           N  
ATOM   4081  CA  ILE B 171      35.333  41.217  18.497  1.00 36.05           C  
ATOM   4082  C   ILE B 171      36.316  42.072  19.284  1.00 37.80           C  
ATOM   4083  O   ILE B 171      37.097  41.556  20.069  1.00 37.40           O  
ATOM   4084  CB  ILE B 171      36.055  40.672  17.223  1.00 37.30           C  
ATOM   4085  CG1 ILE B 171      35.155  39.692  16.473  1.00 31.94           C  
ATOM   4086  CG2 ILE B 171      37.364  40.010  17.613  1.00 33.64           C  
ATOM   4087  CD1 ILE B 171      34.668  38.571  17.296  1.00 28.07           C  
ATOM   4088  N   PHE B 172      36.265  43.386  19.088  1.00 40.94           N  
ATOM   4089  CA  PHE B 172      37.179  44.297  19.786  1.00 39.31           C  
ATOM   4090  C   PHE B 172      36.594  44.984  21.019  1.00 40.76           C  
ATOM   4091  O   PHE B 172      37.289  45.756  21.675  1.00 43.83           O  
ATOM   4092  CB  PHE B 172      37.700  45.350  18.815  1.00 37.75           C  
ATOM   4093  CG  PHE B 172      38.626  44.794  17.790  1.00 41.04           C  
ATOM   4094  CD1 PHE B 172      39.934  44.474  18.121  1.00 40.00           C  
ATOM   4095  CD2 PHE B 172      38.172  44.511  16.504  1.00 40.70           C  
ATOM   4096  CE1 PHE B 172      40.779  43.878  17.192  1.00 43.95           C  
ATOM   4097  CE2 PHE B 172      39.008  43.914  15.572  1.00 44.35           C  
ATOM   4098  CZ  PHE B 172      40.313  43.595  15.913  1.00 43.58           C  
ATOM   4099  N   GLY B 173      35.336  44.692  21.337  1.00 39.80           N  
ATOM   4100  CA  GLY B 173      34.720  45.312  22.485  1.00 37.20           C  
ATOM   4101  C   GLY B 173      33.674  46.361  22.147  1.00 38.04           C  
ATOM   4102  O   GLY B 173      33.028  46.910  23.037  1.00 37.91           O  
ATOM   4103  N   TRP B 174      33.511  46.663  20.865  1.00 36.15           N  
ATOM   4104  CA  TRP B 174      32.514  47.639  20.444  1.00 36.79           C  
ATOM   4105  C   TRP B 174      31.285  46.836  20.104  1.00 34.94           C  
ATOM   4106  O   TRP B 174      31.060  46.480  18.953  1.00 36.98           O  
ATOM   4107  CB  TRP B 174      33.000  48.434  19.226  1.00 39.44           C  
ATOM   4108  CG  TRP B 174      32.022  49.474  18.755  1.00 43.07           C  
ATOM   4109  CD1 TRP B 174      31.145  50.180  19.522  1.00 41.39           C  
ATOM   4110  CD2 TRP B 174      31.825  49.928  17.405  1.00 43.01           C  
ATOM   4111  NE1 TRP B 174      30.414  51.041  18.742  1.00 38.34           N  
ATOM   4112  CE2 TRP B 174      30.812  50.908  17.439  1.00 42.42           C  
ATOM   4113  CE3 TRP B 174      32.408  49.603  16.174  1.00 41.68           C  
ATOM   4114  CZ2 TRP B 174      30.366  51.569  16.289  1.00 41.39           C  
ATOM   4115  CZ3 TRP B 174      31.968  50.260  15.028  1.00 43.33           C  
ATOM   4116  CH2 TRP B 174      30.955  51.234  15.096  1.00 42.75           C  
ATOM   4117  N   GLY B 175      30.491  46.550  21.125  1.00 33.59           N  
ATOM   4118  CA  GLY B 175      29.303  45.740  20.942  1.00 35.13           C  
ATOM   4119  C   GLY B 175      29.707  44.358  21.418  1.00 37.41           C  
ATOM   4120  O   GLY B 175      30.827  44.186  21.895  1.00 37.59           O  
ATOM   4121  N   ALA B 176      28.833  43.369  21.290  1.00 33.68           N  
ATOM   4122  CA  ALA B 176      29.204  42.040  21.738  1.00 32.73           C  
ATOM   4123  C   ALA B 176      28.450  40.895  21.097  1.00 33.20           C  
ATOM   4124  O   ALA B 176      27.307  41.025  20.707  1.00 32.85           O  
ATOM   4125  CB  ALA B 176      29.046  41.959  23.259  1.00 29.03           C  
ATOM   4126  N   TYR B 177      29.117  39.759  21.007  1.00 34.71           N  
ATOM   4127  CA  TYR B 177      28.509  38.561  20.461  1.00 35.78           C  
ATOM   4128  C   TYR B 177      28.330  37.642  21.644  1.00 35.09           C  
ATOM   4129  O   TYR B 177      29.302  37.238  22.257  1.00 39.55           O  
ATOM   4130  CB  TYR B 177      29.436  37.913  19.444  1.00 34.09           C  
ATOM   4131  CG  TYR B 177      29.443  38.609  18.111  1.00 34.84           C  
ATOM   4132  CD1 TYR B 177      28.267  38.738  17.387  1.00 31.69           C  
ATOM   4133  CD2 TYR B 177      30.624  39.097  17.552  1.00 33.41           C  
ATOM   4134  CE1 TYR B 177      28.261  39.326  16.139  1.00 31.20           C  
ATOM   4135  CE2 TYR B 177      30.628  39.694  16.302  1.00 30.88           C  
ATOM   4136  CZ  TYR B 177      29.435  39.804  15.601  1.00 31.71           C  
ATOM   4137  OH  TYR B 177      29.381  40.391  14.368  1.00 34.25           O  
ATOM   4138  N   THR B 178      27.099  37.306  21.978  1.00 36.79           N  
ATOM   4139  CA  THR B 178      26.872  36.456  23.131  1.00 36.53           C  
ATOM   4140  C   THR B 178      25.659  35.546  22.911  1.00 38.52           C  
ATOM   4141  O   THR B 178      25.111  35.507  21.813  1.00 38.74           O  
ATOM   4142  CB  THR B 178      26.681  37.346  24.385  1.00 31.68           C  
ATOM   4143  OG1 THR B 178      26.615  36.522  25.539  1.00 38.06           O  
ATOM   4144  CG2 THR B 178      25.416  38.182  24.267  1.00 27.67           C  
ATOM   4145  N   LEU B 179      25.260  34.801  23.938  1.00 38.31           N  
ATOM   4146  CA  LEU B 179      24.118  33.902  23.814  1.00 43.18           C  
ATOM   4147  C   LEU B 179      22.778  34.646  23.782  1.00 44.29           C  
ATOM   4148  O   LEU B 179      22.653  35.775  24.279  1.00 45.47           O  
ATOM   4149  CB  LEU B 179      24.115  32.898  24.967  1.00 43.29           C  
ATOM   4150  CG  LEU B 179      25.320  31.956  25.063  1.00 45.38           C  
ATOM   4151  CD1 LEU B 179      25.369  31.300  26.449  1.00 40.22           C  
ATOM   4152  CD2 LEU B 179      25.231  30.911  23.961  1.00 42.51           C  
ATOM   4153  N   GLU B 180      21.774  34.005  23.196  1.00 43.90           N  
ATOM   4154  CA  GLU B 180      20.444  34.584  23.091  1.00 44.61           C  
ATOM   4155  C   GLU B 180      19.369  33.501  23.175  1.00 46.84           C  
ATOM   4156  O   GLU B 180      19.664  32.308  23.053  1.00 46.52           O  
ATOM   4157  CB  GLU B 180      20.309  35.337  21.770  1.00 43.89           C  
ATOM   4158  CG  GLU B 180      20.237  34.434  20.557  1.00 44.49           C  
ATOM   4159  CD  GLU B 180      19.923  35.193  19.297  1.00 44.44           C  
ATOM   4160  OE1 GLU B 180      19.515  36.369  19.403  1.00 44.45           O  
ATOM   4161  OE2 GLU B 180      20.077  34.615  18.203  1.00 44.42           O  
ATOM   4162  N   GLY B 181      18.125  33.930  23.388  1.00 47.90           N  
ATOM   4163  CA  GLY B 181      17.007  33.005  23.477  1.00 47.60           C  
ATOM   4164  C   GLY B 181      17.185  31.826  24.416  1.00 49.70           C  
ATOM   4165  O   GLY B 181      17.439  32.003  25.613  1.00 49.93           O  
ATOM   4166  N   VAL B 182      17.038  30.615  23.879  1.00 50.94           N  
ATOM   4167  CA  VAL B 182      17.187  29.403  24.678  1.00 49.27           C  
ATOM   4168  C   VAL B 182      18.652  29.073  24.937  1.00 49.65           C  
ATOM   4169  O   VAL B 182      18.981  27.977  25.402  1.00 48.55           O  
ATOM   4170  CB  VAL B 182      16.500  28.201  24.013  1.00 48.75           C  
ATOM   4171  CG1 VAL B 182      15.009  28.455  23.933  1.00 49.62           C  
ATOM   4172  CG2 VAL B 182      17.072  27.973  22.620  1.00 49.49           C  
ATOM   4173  N   LEU B 183      19.514  30.037  24.611  1.00 46.93           N  
ATOM   4174  CA  LEU B 183      20.960  29.961  24.821  1.00 46.46           C  
ATOM   4175  C   LEU B 183      21.737  28.852  24.110  1.00 46.76           C  
ATOM   4176  O   LEU B 183      22.695  28.312  24.661  1.00 47.04           O  
ATOM   4177  CB  LEU B 183      21.242  29.902  26.321  1.00 44.88           C  
ATOM   4178  CG  LEU B 183      20.425  30.919  27.117  1.00 45.03           C  
ATOM   4179  CD1 LEU B 183      20.684  30.751  28.611  1.00 40.30           C  
ATOM   4180  CD2 LEU B 183      20.777  32.335  26.633  1.00 45.90           C  
ATOM   4181  N   CYS B 184      21.336  28.534  22.883  1.00 45.40           N  
ATOM   4182  CA  CYS B 184      22.009  27.511  22.109  1.00 44.42           C  
ATOM   4183  C   CYS B 184      22.614  28.043  20.811  1.00 43.17           C  
ATOM   4184  O   CYS B 184      22.985  27.287  19.903  1.00 42.51           O  
ATOM   4185  CB  CYS B 184      21.062  26.350  21.832  1.00 43.51           C  
ATOM   4186  SG  CYS B 184      20.896  25.315  23.268  1.00 45.55           S  
ATOM   4187  N   ASN B 185      22.683  29.361  20.711  1.00 39.99           N  
ATOM   4188  CA  ASN B 185      23.322  29.978  19.567  1.00 39.35           C  
ATOM   4189  C   ASN B 185      23.746  31.350  20.026  1.00 39.83           C  
ATOM   4190  O   ASN B 185      23.349  31.808  21.097  1.00 35.65           O  
ATOM   4191  CB  ASN B 185      22.414  30.039  18.335  1.00 39.46           C  
ATOM   4192  CG  ASN B 185      21.368  31.111  18.421  1.00 43.17           C  
ATOM   4193  OD1 ASN B 185      20.256  30.869  18.899  1.00 42.87           O  
ATOM   4194  ND2 ASN B 185      21.711  32.311  17.955  1.00 41.63           N  
ATOM   4195  N   CYS B 186      24.582  31.991  19.225  1.00 41.61           N  
ATOM   4196  CA  CYS B 186      25.101  33.299  19.561  1.00 39.59           C  
ATOM   4197  C   CYS B 186      24.708  34.336  18.538  1.00 39.04           C  
ATOM   4198  O   CYS B 186      24.289  34.009  17.437  1.00 40.98           O  
ATOM   4199  CB  CYS B 186      26.612  33.193  19.716  1.00 39.01           C  
ATOM   4200  SG  CYS B 186      26.975  32.383  21.314  1.00 46.49           S  
ATOM   4201  N   SER B 187      24.823  35.596  18.918  1.00 40.47           N  
ATOM   4202  CA  SER B 187      24.476  36.696  18.034  1.00 41.87           C  
ATOM   4203  C   SER B 187      25.034  37.951  18.678  1.00 41.41           C  
ATOM   4204  O   SER B 187      25.708  37.873  19.703  1.00 40.54           O  
ATOM   4205  CB  SER B 187      22.959  36.805  17.911  1.00 41.99           C  
ATOM   4206  OG  SER B 187      22.592  37.754  16.924  1.00 45.00           O  
ATOM   4207  N   PHE B 188      24.763  39.111  18.097  1.00 43.35           N  
ATOM   4208  CA  PHE B 188      25.246  40.328  18.732  1.00 43.95           C  
ATOM   4209  C   PHE B 188      24.327  40.646  19.905  1.00 44.28           C  
ATOM   4210  O   PHE B 188      23.216  40.117  19.998  1.00 43.33           O  
ATOM   4211  CB  PHE B 188      25.280  41.501  17.753  1.00 44.40           C  
ATOM   4212  CG  PHE B 188      23.925  41.937  17.267  1.00 48.25           C  
ATOM   4213  CD1 PHE B 188      23.339  43.100  17.752  1.00 46.94           C  
ATOM   4214  CD2 PHE B 188      23.266  41.225  16.270  1.00 49.98           C  
ATOM   4215  CE1 PHE B 188      22.131  43.550  17.246  1.00 45.54           C  
ATOM   4216  CE2 PHE B 188      22.054  41.671  15.761  1.00 48.97           C  
ATOM   4217  CZ  PHE B 188      21.487  42.836  16.248  1.00 47.15           C  
ATOM   4218  N   ASP B 189      24.806  41.506  20.797  1.00 43.40           N  
ATOM   4219  CA  ASP B 189      24.050  41.915  21.972  1.00 39.65           C  
ATOM   4220  C   ASP B 189      23.142  43.102  21.669  1.00 39.86           C  
ATOM   4221  O   ASP B 189      23.613  44.221  21.456  1.00 40.21           O  
ATOM   4222  CB  ASP B 189      25.020  42.264  23.103  1.00 37.12           C  
ATOM   4223  CG  ASP B 189      24.316  42.772  24.331  1.00 37.01           C  
ATOM   4224  OD1 ASP B 189      23.107  42.511  24.460  1.00 42.15           O  
ATOM   4225  OD2 ASP B 189      24.972  43.421  25.167  1.00 32.07           O  
ATOM   4226  N   TYR B 190      21.840  42.847  21.630  1.00 38.35           N  
ATOM   4227  CA  TYR B 190      20.885  43.912  21.364  1.00 40.32           C  
ATOM   4228  C   TYR B 190      20.122  44.266  22.623  1.00 40.21           C  
ATOM   4229  O   TYR B 190      19.142  44.985  22.570  1.00 44.78           O  
ATOM   4230  CB  TYR B 190      19.905  43.515  20.246  1.00 39.63           C  
ATOM   4231  CG  TYR B 190      19.381  42.104  20.348  1.00 40.02           C  
ATOM   4232  CD1 TYR B 190      19.786  41.123  19.445  1.00 41.98           C  
ATOM   4233  CD2 TYR B 190      18.510  41.739  21.366  1.00 40.72           C  
ATOM   4234  CE1 TYR B 190      19.336  39.814  19.562  1.00 44.99           C  
ATOM   4235  CE2 TYR B 190      18.052  40.435  21.493  1.00 43.65           C  
ATOM   4236  CZ  TYR B 190      18.465  39.479  20.592  1.00 46.50           C  
ATOM   4237  OH  TYR B 190      18.001  38.193  20.719  1.00 48.51           O  
ATOM   4238  N   ILE B 191      20.606  43.783  23.763  1.00 43.37           N  
ATOM   4239  CA  ILE B 191      19.952  44.027  25.043  1.00 40.84           C  
ATOM   4240  C   ILE B 191      20.623  45.099  25.890  1.00 42.38           C  
ATOM   4241  O   ILE B 191      19.950  45.852  26.577  1.00 43.41           O  
ATOM   4242  CB  ILE B 191      19.852  42.721  25.855  1.00 39.43           C  
ATOM   4243  CG1 ILE B 191      19.147  41.646  25.020  1.00 37.66           C  
ATOM   4244  CG2 ILE B 191      19.105  42.979  27.163  1.00 38.48           C  
ATOM   4245  CD1 ILE B 191      18.927  40.328  25.728  1.00 28.51           C  
ATOM   4246  N   SER B 192      21.947  45.161  25.859  1.00 44.32           N  
ATOM   4247  CA  SER B 192      22.664  46.172  26.631  1.00 45.99           C  
ATOM   4248  C   SER B 192      22.426  47.530  25.975  1.00 47.74           C  
ATOM   4249  O   SER B 192      22.672  47.710  24.777  1.00 48.14           O  
ATOM   4250  CB  SER B 192      24.154  45.845  26.677  1.00 49.69           C  
ATOM   4251  OG  SER B 192      24.378  44.634  27.377  1.00 49.78           O  
ATOM   4252  N   ARG B 193      21.948  48.486  26.762  1.00 46.35           N  
ATOM   4253  CA  ARG B 193      21.624  49.793  26.225  1.00 45.68           C  
ATOM   4254  C   ARG B 193      22.668  50.870  26.442  1.00 44.24           C  
ATOM   4255  O   ARG B 193      22.379  52.059  26.317  1.00 44.14           O  
ATOM   4256  CB  ARG B 193      20.275  50.247  26.776  1.00 41.64           C  
ATOM   4257  CG  ARG B 193      19.187  49.208  26.616  1.00 38.09           C  
ATOM   4258  CD  ARG B 193      17.838  49.808  26.883  1.00 37.55           C  
ATOM   4259  NE  ARG B 193      16.765  48.874  26.585  1.00 37.92           N  
ATOM   4260  CZ  ARG B 193      15.514  49.241  26.348  1.00 38.51           C  
ATOM   4261  NH1 ARG B 193      14.589  48.334  26.083  1.00 38.07           N  
ATOM   4262  NH2 ARG B 193      15.197  50.520  26.363  1.00 38.05           N  
ATOM   4263  N   ASP B 194      23.891  50.463  26.748  1.00 44.75           N  
ATOM   4264  CA  ASP B 194      24.957  51.429  26.952  1.00 45.21           C  
ATOM   4265  C   ASP B 194      25.403  52.002  25.611  1.00 46.72           C  
ATOM   4266  O   ASP B 194      25.140  51.420  24.555  1.00 47.43           O  
ATOM   4267  CB  ASP B 194      26.144  50.769  27.641  1.00 46.42           C  
ATOM   4268  CG  ASP B 194      26.719  49.636  26.839  1.00 49.21           C  
ATOM   4269  OD1 ASP B 194      26.095  48.556  26.790  1.00 52.85           O  
ATOM   4270  OD2 ASP B 194      27.796  49.829  26.246  1.00 52.45           O  
ATOM   4271  N   SER B 195      26.076  53.150  25.668  1.00 47.39           N  
ATOM   4272  CA  SER B 195      26.594  53.836  24.492  1.00 46.66           C  
ATOM   4273  C   SER B 195      27.275  52.907  23.496  1.00 46.70           C  
ATOM   4274  O   SER B 195      26.913  52.874  22.315  1.00 48.22           O  
ATOM   4275  CB  SER B 195      27.620  54.890  24.898  1.00 49.39           C  
ATOM   4276  OG  SER B 195      27.020  56.027  25.471  1.00 56.20           O  
ATOM   4277  N   THR B 196      28.279  52.173  23.981  1.00 46.19           N  
ATOM   4278  CA  THR B 196      29.065  51.259  23.155  1.00 43.99           C  
ATOM   4279  C   THR B 196      28.232  50.225  22.407  1.00 42.82           C  
ATOM   4280  O   THR B 196      28.369  50.075  21.188  1.00 41.40           O  
ATOM   4281  CB  THR B 196      30.136  50.522  23.993  1.00 41.44           C  
ATOM   4282  OG1 THR B 196      30.852  51.470  24.783  1.00 42.65           O  
ATOM   4283  CG2 THR B 196      31.136  49.834  23.099  1.00 40.91           C  
ATOM   4284  N   THR B 197      27.371  49.512  23.127  1.00 38.97           N  
ATOM   4285  CA  THR B 197      26.543  48.503  22.479  1.00 39.13           C  
ATOM   4286  C   THR B 197      25.603  49.163  21.475  1.00 40.79           C  
ATOM   4287  O   THR B 197      25.507  48.737  20.321  1.00 41.56           O  
ATOM   4288  CB  THR B 197      25.688  47.718  23.492  1.00 38.36           C  
ATOM   4289  OG1 THR B 197      26.534  47.134  24.483  1.00 40.33           O  
ATOM   4290  CG2 THR B 197      24.933  46.610  22.795  1.00 36.24           C  
ATOM   4291  N   ARG B 198      24.909  50.202  21.926  1.00 41.00           N  
ATOM   4292  CA  ARG B 198      23.968  50.915  21.090  1.00 39.02           C  
ATOM   4293  C   ARG B 198      24.595  51.523  19.835  1.00 37.65           C  
ATOM   4294  O   ARG B 198      24.080  51.325  18.723  1.00 34.55           O  
ATOM   4295  CB  ARG B 198      23.283  52.015  21.909  1.00 43.53           C  
ATOM   4296  CG  ARG B 198      22.339  52.891  21.110  1.00 43.87           C  
ATOM   4297  CD  ARG B 198      21.336  53.540  22.023  1.00 43.69           C  
ATOM   4298  NE  ARG B 198      20.410  52.563  22.600  1.00 45.36           N  
ATOM   4299  CZ  ARG B 198      19.431  52.881  23.441  1.00 46.53           C  
ATOM   4300  NH1 ARG B 198      19.261  54.144  23.800  1.00 48.14           N  
ATOM   4301  NH2 ARG B 198      18.616  51.949  23.910  1.00 42.91           N  
ATOM   4302  N   SER B 199      25.702  52.247  20.000  1.00 32.74           N  
ATOM   4303  CA  SER B 199      26.338  52.854  18.855  1.00 35.73           C  
ATOM   4304  C   SER B 199      26.700  51.814  17.802  1.00 37.15           C  
ATOM   4305  O   SER B 199      26.549  52.054  16.604  1.00 39.76           O  
ATOM   4306  CB  SER B 199      27.589  53.659  19.269  1.00 36.38           C  
ATOM   4307  OG  SER B 199      28.568  52.855  19.896  1.00 39.30           O  
ATOM   4308  N   ASN B 200      27.164  50.651  18.246  1.00 39.63           N  
ATOM   4309  CA  ASN B 200      27.525  49.594  17.304  1.00 38.79           C  
ATOM   4310  C   ASN B 200      26.273  48.962  16.687  1.00 35.47           C  
ATOM   4311  O   ASN B 200      26.250  48.628  15.512  1.00 36.25           O  
ATOM   4312  CB  ASN B 200      28.387  48.528  17.981  1.00 38.46           C  
ATOM   4313  CG  ASN B 200      28.814  47.445  17.013  1.00 42.13           C  
ATOM   4314  OD1 ASN B 200      28.344  46.305  17.083  1.00 36.20           O  
ATOM   4315  ND2 ASN B 200      29.702  47.802  16.084  1.00 38.96           N  
ATOM   4316  N   ILE B 201      25.231  48.804  17.484  1.00 35.82           N  
ATOM   4317  CA  ILE B 201      23.989  48.245  16.971  1.00 37.85           C  
ATOM   4318  C   ILE B 201      23.484  49.111  15.821  1.00 38.58           C  
ATOM   4319  O   ILE B 201      23.205  48.609  14.736  1.00 39.10           O  
ATOM   4320  CB  ILE B 201      22.893  48.230  18.055  1.00 39.65           C  
ATOM   4321  CG1 ILE B 201      23.306  47.269  19.175  1.00 40.16           C  
ATOM   4322  CG2 ILE B 201      21.550  47.871  17.440  1.00 36.66           C  
ATOM   4323  CD1 ILE B 201      22.438  47.358  20.408  1.00 41.92           C  
ATOM   4324  N   LEU B 202      23.375  50.417  16.072  1.00 39.74           N  
ATOM   4325  CA  LEU B 202      22.889  51.358  15.061  1.00 40.66           C  
ATOM   4326  C   LEU B 202      23.706  51.324  13.770  1.00 39.85           C  
ATOM   4327  O   LEU B 202      23.145  51.371  12.668  1.00 37.23           O  
ATOM   4328  CB  LEU B 202      22.862  52.778  15.631  1.00 41.96           C  
ATOM   4329  CG  LEU B 202      21.789  52.986  16.692  1.00 43.10           C  
ATOM   4330  CD1 LEU B 202      21.899  54.378  17.275  1.00 45.32           C  
ATOM   4331  CD2 LEU B 202      20.432  52.766  16.076  1.00 41.49           C  
ATOM   4332  N   CYS B 203      25.027  51.250  13.912  1.00 41.24           N  
ATOM   4333  CA  CYS B 203      25.907  51.179  12.757  1.00 43.23           C  
ATOM   4334  C   CYS B 203      25.636  49.890  11.988  1.00 42.31           C  
ATOM   4335  O   CYS B 203      25.602  49.888  10.752  1.00 42.15           O  
ATOM   4336  CB  CYS B 203      27.370  51.226  13.181  1.00 44.69           C  
ATOM   4337  SG  CYS B 203      27.933  52.873  13.611  1.00 46.70           S  
ATOM   4338  N   MET B 204      25.444  48.796  12.715  1.00 40.36           N  
ATOM   4339  CA  MET B 204      25.161  47.534  12.065  1.00 40.01           C  
ATOM   4340  C   MET B 204      23.954  47.719  11.155  1.00 43.02           C  
ATOM   4341  O   MET B 204      24.016  47.420   9.953  1.00 43.02           O  
ATOM   4342  CB  MET B 204      24.869  46.446  13.096  1.00 39.89           C  
ATOM   4343  CG  MET B 204      26.040  45.529  13.374  1.00 37.40           C  
ATOM   4344  SD  MET B 204      25.661  44.225  14.556  1.00 38.23           S  
ATOM   4345  CE  MET B 204      27.353  43.631  14.890  1.00 35.68           C  
ATOM   4346  N   PHE B 205      22.867  48.231  11.734  1.00 43.26           N  
ATOM   4347  CA  PHE B 205      21.622  48.470  11.003  1.00 41.92           C  
ATOM   4348  C   PHE B 205      21.774  49.431   9.824  1.00 42.79           C  
ATOM   4349  O   PHE B 205      21.340  49.146   8.716  1.00 44.03           O  
ATOM   4350  CB  PHE B 205      20.568  49.028  11.955  1.00 38.88           C  
ATOM   4351  CG  PHE B 205      19.802  47.981  12.680  1.00 35.52           C  
ATOM   4352  CD1 PHE B 205      18.639  47.463  12.141  1.00 37.07           C  
ATOM   4353  CD2 PHE B 205      20.250  47.495  13.897  1.00 36.70           C  
ATOM   4354  CE1 PHE B 205      17.923  46.472  12.800  1.00 39.64           C  
ATOM   4355  CE2 PHE B 205      19.550  46.504  14.570  1.00 35.16           C  
ATOM   4356  CZ  PHE B 205      18.382  45.989  14.024  1.00 36.75           C  
ATOM   4357  N   ILE B 206      22.400  50.572  10.074  1.00 45.71           N  
ATOM   4358  CA  ILE B 206      22.568  51.576   9.042  1.00 45.34           C  
ATOM   4359  C   ILE B 206      23.538  51.220   7.909  1.00 44.55           C  
ATOM   4360  O   ILE B 206      23.180  51.301   6.738  1.00 44.90           O  
ATOM   4361  CB  ILE B 206      22.978  52.923   9.671  1.00 43.97           C  
ATOM   4362  CG1 ILE B 206      21.887  53.374  10.647  1.00 42.49           C  
ATOM   4363  CG2 ILE B 206      23.182  53.972   8.589  1.00 42.53           C  
ATOM   4364  CD1 ILE B 206      22.227  54.621  11.438  1.00 44.46           C  
ATOM   4365  N   LEU B 207      24.764  50.835   8.240  1.00 44.17           N  
ATOM   4366  CA  LEU B 207      25.720  50.497   7.196  1.00 43.60           C  
ATOM   4367  C   LEU B 207      25.529  49.092   6.651  1.00 42.25           C  
ATOM   4368  O   LEU B 207      25.650  48.869   5.452  1.00 42.25           O  
ATOM   4369  CB  LEU B 207      27.167  50.652   7.691  1.00 40.96           C  
ATOM   4370  CG  LEU B 207      27.701  52.043   8.039  1.00 42.41           C  
ATOM   4371  CD1 LEU B 207      27.182  53.038   7.017  1.00 37.36           C  
ATOM   4372  CD2 LEU B 207      27.260  52.451   9.452  1.00 42.18           C  
ATOM   4373  N   GLY B 208      25.224  48.147   7.530  1.00 43.39           N  
ATOM   4374  CA  GLY B 208      25.069  46.765   7.108  1.00 46.97           C  
ATOM   4375  C   GLY B 208      23.727  46.367   6.519  1.00 48.39           C  
ATOM   4376  O   GLY B 208      23.648  45.407   5.761  1.00 48.58           O  
ATOM   4377  N   PHE B 209      22.678  47.107   6.860  1.00 49.19           N  
ATOM   4378  CA  PHE B 209      21.345  46.803   6.374  1.00 47.58           C  
ATOM   4379  C   PHE B 209      20.750  47.902   5.498  1.00 49.50           C  
ATOM   4380  O   PHE B 209      20.478  47.692   4.316  1.00 50.06           O  
ATOM   4381  CB  PHE B 209      20.414  46.565   7.544  1.00 46.42           C  
ATOM   4382  CG  PHE B 209      19.209  45.763   7.195  1.00 48.10           C  
ATOM   4383  CD1 PHE B 209      18.021  45.936   7.892  1.00 47.05           C  
ATOM   4384  CD2 PHE B 209      19.267  44.799   6.201  1.00 48.67           C  
ATOM   4385  CE1 PHE B 209      16.912  45.160   7.601  1.00 48.67           C  
ATOM   4386  CE2 PHE B 209      18.166  44.013   5.903  1.00 50.84           C  
ATOM   4387  CZ  PHE B 209      16.984  44.191   6.602  1.00 48.25           C  
ATOM   4388  N   PHE B 210      20.532  49.073   6.086  1.00 49.42           N  
ATOM   4389  CA  PHE B 210      19.946  50.190   5.355  1.00 47.61           C  
ATOM   4390  C   PHE B 210      20.760  50.589   4.119  1.00 47.80           C  
ATOM   4391  O   PHE B 210      20.197  50.851   3.062  1.00 48.05           O  
ATOM   4392  CB  PHE B 210      19.755  51.390   6.289  1.00 43.31           C  
ATOM   4393  CG  PHE B 210      18.829  51.117   7.448  1.00 43.57           C  
ATOM   4394  CD1 PHE B 210      17.788  50.192   7.330  1.00 43.19           C  
ATOM   4395  CD2 PHE B 210      18.969  51.802   8.650  1.00 41.67           C  
ATOM   4396  CE1 PHE B 210      16.900  49.956   8.401  1.00 42.60           C  
ATOM   4397  CE2 PHE B 210      18.081  51.571   9.718  1.00 40.98           C  
ATOM   4398  CZ  PHE B 210      17.051  50.650   9.590  1.00 35.55           C  
ATOM   4399  N   GLY B 211      22.081  50.620   4.256  1.00 47.62           N  
ATOM   4400  CA  GLY B 211      22.935  50.973   3.140  1.00 47.99           C  
ATOM   4401  C   GLY B 211      22.646  50.132   1.909  1.00 50.32           C  
ATOM   4402  O   GLY B 211      22.266  50.673   0.868  1.00 50.78           O  
ATOM   4403  N   PRO B 212      22.821  48.803   1.981  1.00 50.92           N  
ATOM   4404  CA  PRO B 212      22.535  48.007   0.787  1.00 49.62           C  
ATOM   4405  C   PRO B 212      21.097  48.155   0.308  1.00 49.94           C  
ATOM   4406  O   PRO B 212      20.834  48.152  -0.891  1.00 48.25           O  
ATOM   4407  CB  PRO B 212      22.879  46.578   1.226  1.00 48.92           C  
ATOM   4408  CG  PRO B 212      22.786  46.612   2.712  1.00 46.85           C  
ATOM   4409  CD  PRO B 212      23.363  47.957   3.060  1.00 49.62           C  
ATOM   4410  N   ILE B 213      20.167  48.305   1.239  1.00 50.65           N  
ATOM   4411  CA  ILE B 213      18.767  48.441   0.848  1.00 53.16           C  
ATOM   4412  C   ILE B 213      18.522  49.720   0.052  1.00 54.11           C  
ATOM   4413  O   ILE B 213      17.756  49.722  -0.913  1.00 56.21           O  
ATOM   4414  CB  ILE B 213      17.828  48.430   2.080  1.00 52.08           C  
ATOM   4415  CG1 ILE B 213      17.891  47.065   2.765  1.00 47.79           C  
ATOM   4416  CG2 ILE B 213      16.398  48.752   1.652  1.00 50.21           C  
ATOM   4417  CD1 ILE B 213      17.046  46.981   4.017  1.00 48.93           C  
ATOM   4418  N   LEU B 214      19.171  50.805   0.453  1.00 53.11           N  
ATOM   4419  CA  LEU B 214      19.000  52.067  -0.240  1.00 54.00           C  
ATOM   4420  C   LEU B 214      19.400  51.885  -1.700  1.00 53.24           C  
ATOM   4421  O   LEU B 214      18.697  52.329  -2.604  1.00 52.58           O  
ATOM   4422  CB  LEU B 214      19.877  53.144   0.389  1.00 58.06           C  
ATOM   4423  CG  LEU B 214      19.635  54.544  -0.164  1.00 63.17           C  
ATOM   4424  CD1 LEU B 214      18.417  55.149   0.517  1.00 65.50           C  
ATOM   4425  CD2 LEU B 214      20.850  55.417   0.077  1.00 67.58           C  
ATOM   4426  N   ILE B 215      20.541  51.229  -1.905  1.00 51.56           N  
ATOM   4427  CA  ILE B 215      21.076  50.955  -3.232  1.00 49.24           C  
ATOM   4428  C   ILE B 215      20.112  50.091  -4.028  1.00 50.50           C  
ATOM   4429  O   ILE B 215      19.927  50.277  -5.225  1.00 47.78           O  
ATOM   4430  CB  ILE B 215      22.401  50.184  -3.155  1.00 48.75           C  
ATOM   4431  CG1 ILE B 215      23.468  51.035  -2.471  1.00 49.74           C  
ATOM   4432  CG2 ILE B 215      22.842  49.770  -4.558  1.00 49.08           C  
ATOM   4433  CD1 ILE B 215      24.766  50.307  -2.251  1.00 49.15           C  
ATOM   4434  N   ILE B 216      19.522  49.125  -3.337  1.00 52.65           N  
ATOM   4435  CA  ILE B 216      18.585  48.199  -3.942  1.00 54.10           C  
ATOM   4436  C   ILE B 216      17.312  48.917  -4.348  1.00 54.47           C  
ATOM   4437  O   ILE B 216      16.752  48.646  -5.412  1.00 51.47           O  
ATOM   4438  CB  ILE B 216      18.278  47.051  -2.972  1.00 54.55           C  
ATOM   4439  CG1 ILE B 216      19.523  46.182  -2.837  1.00 53.43           C  
ATOM   4440  CG2 ILE B 216      17.089  46.233  -3.464  1.00 52.70           C  
ATOM   4441  CD1 ILE B 216      19.451  45.168  -1.724  1.00 57.95           C  
ATOM   4442  N   PHE B 217      16.862  49.837  -3.503  1.00 57.23           N  
ATOM   4443  CA  PHE B 217      15.662  50.596  -3.812  1.00 59.83           C  
ATOM   4444  C   PHE B 217      15.892  51.480  -5.032  1.00 58.98           C  
ATOM   4445  O   PHE B 217      15.112  51.457  -5.980  1.00 58.14           O  
ATOM   4446  CB  PHE B 217      15.242  51.461  -2.625  1.00 61.08           C  
ATOM   4447  CG  PHE B 217      14.156  52.440  -2.953  1.00 64.33           C  
ATOM   4448  CD1 PHE B 217      14.467  53.763  -3.263  1.00 67.03           C  
ATOM   4449  CD2 PHE B 217      12.829  52.033  -2.998  1.00 64.06           C  
ATOM   4450  CE1 PHE B 217      13.468  54.673  -3.616  1.00 66.53           C  
ATOM   4451  CE2 PHE B 217      11.819  52.931  -3.351  1.00 65.83           C  
ATOM   4452  CZ  PHE B 217      12.143  54.256  -3.662  1.00 66.56           C  
ATOM   4453  N   PHE B 218      16.972  52.254  -5.007  1.00 58.94           N  
ATOM   4454  CA  PHE B 218      17.286  53.137  -6.115  1.00 60.71           C  
ATOM   4455  C   PHE B 218      17.306  52.353  -7.417  1.00 62.26           C  
ATOM   4456  O   PHE B 218      16.595  52.680  -8.366  1.00 64.78           O  
ATOM   4457  CB  PHE B 218      18.634  53.816  -5.889  1.00 63.08           C  
ATOM   4458  CG  PHE B 218      19.099  54.653  -7.052  1.00 67.92           C  
ATOM   4459  CD1 PHE B 218      19.762  54.065  -8.131  1.00 70.22           C  
ATOM   4460  CD2 PHE B 218      18.871  56.026  -7.076  1.00 68.59           C  
ATOM   4461  CE1 PHE B 218      20.192  54.839  -9.218  1.00 71.35           C  
ATOM   4462  CE2 PHE B 218      19.296  56.806  -8.156  1.00 70.99           C  
ATOM   4463  CZ  PHE B 218      19.958  56.210  -9.229  1.00 71.39           C  
ATOM   4464  N   CYS B 219      18.121  51.310  -7.450  1.00 62.66           N  
ATOM   4465  CA  CYS B 219      18.254  50.471  -8.630  1.00 59.87           C  
ATOM   4466  C   CYS B 219      16.950  49.922  -9.176  1.00 59.92           C  
ATOM   4467  O   CYS B 219      16.619  50.171 -10.327  1.00 58.76           O  
ATOM   4468  CB  CYS B 219      19.215  49.326  -8.342  1.00 57.64           C  
ATOM   4469  SG  CYS B 219      20.898  49.901  -8.229  1.00 49.21           S  
ATOM   4470  N   TYR B 220      16.213  49.168  -8.369  1.00 62.02           N  
ATOM   4471  CA  TYR B 220      14.955  48.608  -8.836  1.00 64.86           C  
ATOM   4472  C   TYR B 220      13.933  49.685  -9.117  1.00 66.06           C  
ATOM   4473  O   TYR B 220      13.028  49.490  -9.923  1.00 68.14           O  
ATOM   4474  CB  TYR B 220      14.400  47.594  -7.836  1.00 67.11           C  
ATOM   4475  CG  TYR B 220      15.242  46.344  -7.791  1.00 69.49           C  
ATOM   4476  CD1 TYR B 220      15.558  45.662  -8.965  1.00 69.52           C  
ATOM   4477  CD2 TYR B 220      15.805  45.898  -6.600  1.00 71.56           C  
ATOM   4478  CE1 TYR B 220      16.422  44.583  -8.959  1.00 70.73           C  
ATOM   4479  CE2 TYR B 220      16.673  44.816  -6.584  1.00 72.86           C  
ATOM   4480  CZ  TYR B 220      16.982  44.170  -7.768  1.00 71.24           C  
ATOM   4481  OH  TYR B 220      17.900  43.148  -7.772  1.00 72.43           O  
ATOM   4482  N   PHE B 221      14.066  50.830  -8.462  1.00 67.49           N  
ATOM   4483  CA  PHE B 221      13.128  51.905  -8.720  1.00 67.38           C  
ATOM   4484  C   PHE B 221      13.404  52.365 -10.145  1.00 67.00           C  
ATOM   4485  O   PHE B 221      12.527  52.307 -11.002  1.00 67.18           O  
ATOM   4486  CB  PHE B 221      13.324  53.070  -7.747  1.00 68.79           C  
ATOM   4487  CG  PHE B 221      12.283  54.149  -7.894  1.00 71.14           C  
ATOM   4488  CD1 PHE B 221      10.945  53.876  -7.632  1.00 70.92           C  
ATOM   4489  CD2 PHE B 221      12.630  55.419  -8.349  1.00 70.75           C  
ATOM   4490  CE1 PHE B 221       9.966  54.850  -7.826  1.00 70.48           C  
ATOM   4491  CE2 PHE B 221      11.661  56.399  -8.545  1.00 68.73           C  
ATOM   4492  CZ  PHE B 221      10.327  56.113  -8.285  1.00 69.86           C  
ATOM   4493  N   ASN B 222      14.637  52.804 -10.390  1.00 66.44           N  
ATOM   4494  CA  ASN B 222      15.047  53.264 -11.708  1.00 66.71           C  
ATOM   4495  C   ASN B 222      14.644  52.249 -12.765  1.00 67.36           C  
ATOM   4496  O   ASN B 222      14.184  52.607 -13.847  1.00 68.45           O  
ATOM   4497  CB  ASN B 222      16.563  53.488 -11.737  1.00 68.06           C  
ATOM   4498  CG  ASN B 222      16.947  54.932 -11.436  1.00 69.94           C  
ATOM   4499  OD1 ASN B 222      16.994  55.774 -12.340  1.00 70.22           O  
ATOM   4500  ND2 ASN B 222      17.205  55.229 -10.163  1.00 70.23           N  
ATOM   4501  N   ILE B 223      14.814  50.975 -12.450  1.00 68.15           N  
ATOM   4502  CA  ILE B 223      14.445  49.938 -13.385  1.00 68.27           C  
ATOM   4503  C   ILE B 223      12.943  50.035 -13.631  1.00 71.16           C  
ATOM   4504  O   ILE B 223      12.512  50.520 -14.682  1.00 71.46           O  
ATOM   4505  CB  ILE B 223      14.838  48.543 -12.840  1.00 65.58           C  
ATOM   4506  CG1 ILE B 223      16.368  48.409 -12.872  1.00 64.54           C  
ATOM   4507  CG2 ILE B 223      14.172  47.440 -13.654  1.00 61.56           C  
ATOM   4508  CD1 ILE B 223      16.922  47.271 -12.063  1.00 62.57           C  
ATOM   4509  N   VAL B 224      12.146  49.605 -12.658  1.00 73.43           N  
ATOM   4510  CA  VAL B 224      10.692  49.646 -12.788  1.00 76.34           C  
ATOM   4511  C   VAL B 224      10.238  50.845 -13.615  1.00 78.93           C  
ATOM   4512  O   VAL B 224       9.562  50.687 -14.630  1.00 78.92           O  
ATOM   4513  CB  VAL B 224      10.004  49.711 -11.400  1.00 76.78           C  
ATOM   4514  CG1 VAL B 224       8.498  49.892 -11.569  1.00 76.58           C  
ATOM   4515  CG2 VAL B 224      10.286  48.443 -10.619  1.00 76.65           C  
ATOM   4516  N   MET B 225      10.626  52.039 -13.177  1.00 82.43           N  
ATOM   4517  CA  MET B 225      10.259  53.277 -13.854  1.00 84.17           C  
ATOM   4518  C   MET B 225      11.113  53.484 -15.092  1.00 85.93           C  
ATOM   4519  O   MET B 225      11.834  54.476 -15.201  1.00 86.41           O  
ATOM   4520  CB  MET B 225      10.451  54.472 -12.915  1.00 84.38           C  
ATOM   4521  CG  MET B 225       9.225  55.345 -12.754  1.00 85.70           C  
ATOM   4522  SD  MET B 225       7.921  54.473 -11.881  1.00 89.55           S  
ATOM   4523  CE  MET B 225       6.959  53.828 -13.251  1.00 89.20           C  
ATOM   4524  N   SER B 226      11.031  52.547 -16.026  1.00 87.70           N  
ATOM   4525  CA  SER B 226      11.806  52.647 -17.250  1.00 88.92           C  
ATOM   4526  C   SER B 226      11.257  51.702 -18.310  1.00 89.07           C  
ATOM   4527  O   SER B 226      11.579  51.827 -19.489  1.00 87.83           O  
ATOM   4528  CB  SER B 226      13.274  52.322 -16.962  1.00 88.86           C  
ATOM   4529  OG  SER B 226      14.086  52.556 -18.099  1.00 91.37           O  
ATOM   4530  N   VAL B 227      10.420  50.763 -17.879  1.00 90.65           N  
ATOM   4531  CA  VAL B 227       9.821  49.790 -18.784  1.00 94.16           C  
ATOM   4532  C   VAL B 227       9.032  50.473 -19.895  1.00 96.63           C  
ATOM   4533  O   VAL B 227       8.838  49.906 -20.971  1.00 98.26           O  
ATOM   4534  CB  VAL B 227       8.874  48.834 -18.033  1.00 94.07           C  
ATOM   4535  CG1 VAL B 227       9.640  48.076 -16.965  1.00 94.76           C  
ATOM   4536  CG2 VAL B 227       7.735  49.617 -17.408  1.00 94.67           C  
ATOM   4537  N   SER B 228       8.580  51.693 -19.624  1.00 98.46           N  
ATOM   4538  CA  SER B 228       7.806  52.463 -20.588  1.00 98.84           C  
ATOM   4539  C   SER B 228       8.613  52.796 -21.834  1.00100.21           C  
ATOM   4540  O   SER B 228       8.205  52.477 -22.949  1.00100.17           O  
ATOM   4541  CB  SER B 228       7.305  53.757 -19.942  1.00 98.47           C  
ATOM   4542  OG  SER B 228       8.376  54.492 -19.374  1.00 96.93           O  
ATOM   4543  N   ASN B 229       9.761  53.436 -21.641  1.00102.40           N  
ATOM   4544  CA  ASN B 229      10.622  53.817 -22.755  1.00104.90           C  
ATOM   4545  C   ASN B 229      11.263  52.613 -23.427  1.00107.02           C  
ATOM   4546  O   ASN B 229      11.524  52.635 -24.628  1.00106.93           O  
ATOM   4547  CB  ASN B 229      11.722  54.763 -22.278  1.00104.69           C  
ATOM   4548  CG  ASN B 229      11.173  55.997 -21.608  1.00105.11           C  
ATOM   4549  OD1 ASN B 229      10.443  56.778 -22.218  1.00106.37           O  
ATOM   4550  ND2 ASN B 229      11.522  56.185 -20.341  1.00106.25           N  
ATOM   4551  N   HIS B 230      11.524  51.565 -22.654  1.00110.11           N  
ATOM   4552  CA  HIS B 230      12.148  50.373 -23.211  1.00112.93           C  
ATOM   4553  C   HIS B 230      11.363  49.899 -24.420  1.00114.37           C  
ATOM   4554  O   HIS B 230      11.898  49.814 -25.525  1.00114.51           O  
ATOM   4555  CB  HIS B 230      12.208  49.246 -22.176  1.00113.48           C  
ATOM   4556  CG  HIS B 230      12.869  48.001 -22.684  1.00115.22           C  
ATOM   4557  ND1 HIS B 230      12.883  46.821 -21.972  1.00116.72           N  
ATOM   4558  CD2 HIS B 230      13.543  47.755 -23.834  1.00115.24           C  
ATOM   4559  CE1 HIS B 230      13.535  45.901 -22.662  1.00116.29           C  
ATOM   4560  NE2 HIS B 230      13.945  46.442 -23.796  1.00114.98           N  
ATOM   4561  N   GLU B 231      10.089  49.594 -24.207  1.00115.79           N  
ATOM   4562  CA  GLU B 231       9.242  49.123 -25.293  1.00117.13           C  
ATOM   4563  C   GLU B 231       9.169  50.148 -26.419  1.00117.02           C  
ATOM   4564  O   GLU B 231       9.185  49.784 -27.595  1.00116.99           O  
ATOM   4565  CB  GLU B 231       7.841  48.803 -24.767  1.00117.35           C  
ATOM   4566  CG  GLU B 231       7.151  49.955 -24.073  1.00119.13           C  
ATOM   4567  CD  GLU B 231       5.892  49.520 -23.351  1.00121.10           C  
ATOM   4568  OE1 GLU B 231       5.995  48.682 -22.429  1.00120.94           O  
ATOM   4569  OE2 GLU B 231       4.798  50.013 -23.706  1.00122.15           O  
ATOM   4570  N   LYS B 232       9.104  51.427 -26.062  1.00116.83           N  
ATOM   4571  CA  LYS B 232       9.026  52.480 -27.069  1.00116.55           C  
ATOM   4572  C   LYS B 232      10.302  52.533 -27.910  1.00116.43           C  
ATOM   4573  O   LYS B 232      10.259  52.875 -29.092  1.00116.34           O  
ATOM   4574  CB  LYS B 232       8.767  53.839 -26.405  1.00115.78           C  
ATOM   4575  CG  LYS B 232       8.439  54.949 -27.400  1.00115.50           C  
ATOM   4576  CD  LYS B 232       7.768  56.148 -26.733  1.00115.72           C  
ATOM   4577  CE  LYS B 232       8.703  56.881 -25.783  1.00115.17           C  
ATOM   4578  NZ  LYS B 232       8.010  58.021 -25.118  1.00113.75           N  
ATOM   4579  N   GLU B 233      11.433  52.192 -27.299  1.00115.89           N  
ATOM   4580  CA  GLU B 233      12.711  52.183 -28.003  1.00114.74           C  
ATOM   4581  C   GLU B 233      12.764  50.918 -28.842  1.00114.66           C  
ATOM   4582  O   GLU B 233      13.461  50.851 -29.853  1.00114.43           O  
ATOM   4583  CB  GLU B 233      13.878  52.154 -27.011  1.00114.79           C  
ATOM   4584  CG  GLU B 233      14.019  53.380 -26.133  1.00114.22           C  
ATOM   4585  CD  GLU B 233      15.066  53.182 -25.053  1.00113.69           C  
ATOM   4586  OE1 GLU B 233      14.859  52.317 -24.178  1.00112.68           O  
ATOM   4587  OE2 GLU B 233      16.100  53.884 -25.083  1.00113.87           O  
ATOM   4588  N   MET B 234      12.025  49.911 -28.395  1.00114.65           N  
ATOM   4589  CA  MET B 234      11.963  48.631 -29.079  1.00114.97           C  
ATOM   4590  C   MET B 234      11.142  48.823 -30.344  1.00115.31           C  
ATOM   4591  O   MET B 234      11.493  48.324 -31.413  1.00115.93           O  
ATOM   4592  CB  MET B 234      11.290  47.596 -28.178  1.00114.75           C  
ATOM   4593  CG  MET B 234      11.442  46.161 -28.643  1.00114.51           C  
ATOM   4594  SD  MET B 234      13.120  45.549 -28.402  1.00113.99           S  
ATOM   4595  CE  MET B 234      13.864  45.994 -29.951  1.00114.45           C  
ATOM   4596  N   ALA B 235      10.045  49.558 -30.203  1.00114.96           N  
ATOM   4597  CA  ALA B 235       9.147  49.840 -31.312  1.00114.07           C  
ATOM   4598  C   ALA B 235       9.864  50.654 -32.379  1.00113.76           C  
ATOM   4599  O   ALA B 235       9.723  50.391 -33.572  1.00113.70           O  
ATOM   4600  CB  ALA B 235       7.927  50.596 -30.811  1.00114.10           C  
ATOM   4601  N   ALA B 236      10.635  51.644 -31.941  1.00113.50           N  
ATOM   4602  CA  ALA B 236      11.380  52.496 -32.859  1.00114.21           C  
ATOM   4603  C   ALA B 236      12.468  51.690 -33.560  1.00115.53           C  
ATOM   4604  O   ALA B 236      13.301  52.243 -34.281  1.00115.82           O  
ATOM   4605  CB  ALA B 236      11.996  53.665 -32.104  1.00113.13           C  
ATOM   4606  N   MET B 237      12.458  50.380 -33.337  1.00116.72           N  
ATOM   4607  CA  MET B 237      13.437  49.495 -33.951  1.00117.77           C  
ATOM   4608  C   MET B 237      12.758  48.274 -34.548  1.00116.69           C  
ATOM   4609  O   MET B 237      13.312  47.609 -35.424  1.00116.16           O  
ATOM   4610  CB  MET B 237      14.492  49.074 -32.927  1.00120.21           C  
ATOM   4611  CG  MET B 237      15.355  50.231 -32.443  1.00123.48           C  
ATOM   4612  SD  MET B 237      16.847  49.694 -31.584  1.00128.20           S  
ATOM   4613  CE  MET B 237      16.337  49.854 -29.848  1.00127.97           C  
ATOM   4614  N   ALA B 238      11.552  47.984 -34.072  1.00115.83           N  
ATOM   4615  CA  ALA B 238      10.795  46.853 -34.586  1.00115.01           C  
ATOM   4616  C   ALA B 238      10.461  47.165 -36.042  1.00114.75           C  
ATOM   4617  O   ALA B 238      10.153  46.271 -36.828  1.00115.41           O  
ATOM   4618  CB  ALA B 238       9.515  46.668 -33.778  1.00113.90           C  
ATOM   4619  N   LYS B 239      10.543  48.448 -36.390  1.00114.15           N  
ATOM   4620  CA  LYS B 239      10.249  48.914 -37.741  1.00112.84           C  
ATOM   4621  C   LYS B 239      11.518  49.063 -38.566  1.00112.36           C  
ATOM   4622  O   LYS B 239      11.612  48.548 -39.681  1.00113.82           O  
ATOM   4623  CB  LYS B 239       9.561  50.280 -37.708  1.00111.10           C  
ATOM   4624  CG  LYS B 239       8.514  50.458 -36.637  1.00107.89           C  
ATOM   4625  CD  LYS B 239       8.437  51.922 -36.244  1.00105.76           C  
ATOM   4626  CE  LYS B 239       7.613  52.114 -34.986  1.00105.08           C  
ATOM   4627  NZ  LYS B 239       7.793  53.477 -34.412  1.00104.17           N  
ATOM   4628  N   ARG B 240      12.490  49.783 -38.021  1.00110.74           N  
ATOM   4629  CA  ARG B 240      13.727  50.027 -38.745  1.00109.45           C  
ATOM   4630  C   ARG B 240      14.894  49.131 -38.362  1.00107.88           C  
ATOM   4631  O   ARG B 240      15.082  48.783 -37.197  1.00107.65           O  
ATOM   4632  CB  ARG B 240      14.129  51.499 -38.593  1.00110.44           C  
ATOM   4633  CG  ARG B 240      14.617  51.889 -37.210  1.00108.90           C  
ATOM   4634  CD  ARG B 240      16.129  51.861 -37.153  1.00107.27           C  
ATOM   4635  NE  ARG B 240      16.635  52.202 -35.827  1.00107.35           N  
ATOM   4636  CZ  ARG B 240      17.918  52.418 -35.554  1.00107.45           C  
ATOM   4637  NH1 ARG B 240      18.827  52.331 -36.520  1.00106.05           N  
ATOM   4638  NH2 ARG B 240      18.296  52.717 -34.317  1.00106.67           N  
ATOM   4639  N   LEU B 241      15.668  48.762 -39.377  1.00106.20           N  
ATOM   4640  CA  LEU B 241      16.849  47.917 -39.232  1.00104.59           C  
ATOM   4641  C   LEU B 241      16.682  46.745 -38.268  1.00103.05           C  
ATOM   4642  O   LEU B 241      17.520  46.527 -37.395  1.00104.28           O  
ATOM   4643  CB  LEU B 241      18.044  48.775 -38.804  1.00104.39           C  
ATOM   4644  CG  LEU B 241      19.454  48.229 -39.052  1.00103.37           C  
ATOM   4645  CD1 LEU B 241      19.714  48.112 -40.547  1.00102.45           C  
ATOM   4646  CD2 LEU B 241      20.472  49.160 -38.418  1.00102.46           C  
ATOM   4647  N   ASN B 242      15.601  45.991 -38.433  1.00100.43           N  
ATOM   4648  CA  ASN B 242      15.331  44.823 -37.600  1.00 98.17           C  
ATOM   4649  C   ASN B 242      14.555  43.798 -38.419  1.00 96.35           C  
ATOM   4650  O   ASN B 242      13.362  43.962 -38.672  1.00 96.58           O  
ATOM   4651  CB  ASN B 242      14.518  45.210 -36.357  1.00 98.64           C  
ATOM   4652  CG  ASN B 242      15.361  45.266 -35.092  1.00 97.98           C  
ATOM   4653  OD1 ASN B 242      14.860  45.585 -34.014  1.00 97.66           O  
ATOM   4654  ND2 ASN B 242      16.644  44.948 -35.217  1.00 98.92           N  
ATOM   4655  N   ALA B 243      15.240  42.745 -38.842  1.00 93.86           N  
ATOM   4656  CA  ALA B 243      14.607  41.698 -39.629  1.00 92.45           C  
ATOM   4657  C   ALA B 243      14.210  40.572 -38.690  1.00 91.42           C  
ATOM   4658  O   ALA B 243      13.069  40.492 -38.230  1.00 90.22           O  
ATOM   4659  CB  ALA B 243      15.581  41.183 -40.687  1.00 92.10           C  
ATOM   4660  N   LYS B 244      15.168  39.695 -38.419  1.00 90.92           N  
ATOM   4661  CA  LYS B 244      14.968  38.575 -37.515  1.00 91.04           C  
ATOM   4662  C   LYS B 244      15.743  38.949 -36.266  1.00 91.26           C  
ATOM   4663  O   LYS B 244      15.542  38.386 -35.189  1.00 91.59           O  
ATOM   4664  CB  LYS B 244      15.529  37.291 -38.131  1.00 91.58           C  
ATOM   4665  CG  LYS B 244      15.649  36.111 -37.171  1.00 91.51           C  
ATOM   4666  CD  LYS B 244      14.355  35.841 -36.415  1.00 92.53           C  
ATOM   4667  CE  LYS B 244      13.213  35.434 -37.332  1.00 91.61           C  
ATOM   4668  NZ  LYS B 244      11.909  35.483 -36.604  1.00 91.02           N  
ATOM   4669  N   GLU B 245      16.634  39.921 -36.435  1.00 90.03           N  
ATOM   4670  CA  GLU B 245      17.455  40.414 -35.349  1.00 87.90           C  
ATOM   4671  C   GLU B 245      16.559  41.028 -34.286  1.00 87.31           C  
ATOM   4672  O   GLU B 245      17.014  41.371 -33.198  1.00 86.77           O  
ATOM   4673  CB  GLU B 245      18.456  41.443 -35.877  1.00 88.57           C  
ATOM   4674  CG  GLU B 245      17.851  42.544 -36.737  1.00 89.94           C  
ATOM   4675  CD  GLU B 245      18.460  42.600 -38.131  1.00 90.77           C  
ATOM   4676  OE1 GLU B 245      19.683  42.367 -38.254  1.00 90.12           O  
ATOM   4677  OE2 GLU B 245      17.725  42.889 -39.102  1.00 90.27           O  
ATOM   4678  N   LEU B 246      15.279  41.168 -34.613  1.00 87.07           N  
ATOM   4679  CA  LEU B 246      14.310  41.712 -33.673  1.00 86.64           C  
ATOM   4680  C   LEU B 246      14.048  40.624 -32.651  1.00 85.57           C  
ATOM   4681  O   LEU B 246      13.878  40.894 -31.467  1.00 84.49           O  
ATOM   4682  CB  LEU B 246      12.995  42.058 -34.378  1.00 88.40           C  
ATOM   4683  CG  LEU B 246      11.858  42.535 -33.465  1.00 88.30           C  
ATOM   4684  CD1 LEU B 246      12.142  43.953 -32.993  1.00 88.00           C  
ATOM   4685  CD2 LEU B 246      10.532  42.489 -34.207  1.00 87.26           C  
ATOM   4686  N   ARG B 247      14.012  39.386 -33.134  1.00 85.42           N  
ATOM   4687  CA  ARG B 247      13.777  38.232 -32.280  1.00 86.49           C  
ATOM   4688  C   ARG B 247      14.898  38.144 -31.255  1.00 85.83           C  
ATOM   4689  O   ARG B 247      14.665  37.817 -30.094  1.00 85.25           O  
ATOM   4690  CB  ARG B 247      13.750  36.954 -33.116  1.00 89.16           C  
ATOM   4691  CG  ARG B 247      12.582  36.013 -32.824  1.00 93.97           C  
ATOM   4692  CD  ARG B 247      12.505  35.582 -31.360  1.00 99.28           C  
ATOM   4693  NE  ARG B 247      11.838  36.566 -30.509  1.00102.30           N  
ATOM   4694  CZ  ARG B 247      11.503  36.352 -29.239  1.00102.70           C  
ATOM   4695  NH1 ARG B 247      10.895  37.302 -28.539  1.00101.90           N  
ATOM   4696  NH2 ARG B 247      11.773  35.186 -28.666  1.00103.89           N  
ATOM   4697  N   LYS B 248      16.117  38.439 -31.699  1.00 84.77           N  
ATOM   4698  CA  LYS B 248      17.283  38.392 -30.825  1.00 84.53           C  
ATOM   4699  C   LYS B 248      17.283  39.557 -29.837  1.00 84.41           C  
ATOM   4700  O   LYS B 248      17.396  39.354 -28.630  1.00 84.09           O  
ATOM   4701  CB  LYS B 248      18.568  38.405 -31.654  1.00 85.00           C  
ATOM   4702  CG  LYS B 248      19.848  38.362 -30.831  1.00 86.25           C  
ATOM   4703  CD  LYS B 248      21.090  38.316 -31.718  1.00 88.20           C  
ATOM   4704  CE  LYS B 248      22.370  38.367 -30.885  1.00 89.41           C  
ATOM   4705  NZ  LYS B 248      23.620  38.263 -31.696  1.00 88.87           N  
ATOM   4706  N   ALA B 249      17.155  40.778 -30.345  1.00 83.88           N  
ATOM   4707  CA  ALA B 249      17.144  41.951 -29.482  1.00 83.16           C  
ATOM   4708  C   ALA B 249      16.023  41.858 -28.456  1.00 83.19           C  
ATOM   4709  O   ALA B 249      16.136  42.392 -27.356  1.00 83.35           O  
ATOM   4710  CB  ALA B 249      16.985  43.215 -30.311  1.00 81.78           C  
ATOM   4711  N   GLN B 250      14.939  41.181 -28.815  1.00 84.09           N  
ATOM   4712  CA  GLN B 250      13.815  41.032 -27.902  1.00 85.94           C  
ATOM   4713  C   GLN B 250      14.016  39.771 -27.083  1.00 86.00           C  
ATOM   4714  O   GLN B 250      13.359  39.564 -26.062  1.00 85.71           O  
ATOM   4715  CB  GLN B 250      12.503  40.947 -28.682  1.00 89.41           C  
ATOM   4716  CG  GLN B 250      11.252  40.984 -27.810  1.00 95.07           C  
ATOM   4717  CD  GLN B 250      11.146  42.254 -26.976  1.00 97.03           C  
ATOM   4718  OE1 GLN B 250      11.265  43.363 -27.495  1.00 99.00           O  
ATOM   4719  NE2 GLN B 250      10.912  42.093 -25.679  1.00 96.61           N  
ATOM   4720  N   ALA B 251      14.931  38.923 -27.541  1.00 85.99           N  
ATOM   4721  CA  ALA B 251      15.242  37.686 -26.835  1.00 84.00           C  
ATOM   4722  C   ALA B 251      16.156  38.046 -25.672  1.00 82.76           C  
ATOM   4723  O   ALA B 251      15.945  37.612 -24.542  1.00 82.68           O  
ATOM   4724  CB  ALA B 251      15.936  36.707 -27.769  1.00 82.83           C  
ATOM   4725  N   GLY B 252      17.169  38.854 -25.959  1.00 81.16           N  
ATOM   4726  CA  GLY B 252      18.100  39.265 -24.930  1.00 79.51           C  
ATOM   4727  C   GLY B 252      17.443  40.199 -23.936  1.00 78.70           C  
ATOM   4728  O   GLY B 252      17.928  40.363 -22.820  1.00 78.44           O  
ATOM   4729  N   ALA B 253      16.333  40.807 -24.345  1.00 77.55           N  
ATOM   4730  CA  ALA B 253      15.599  41.734 -23.494  1.00 76.18           C  
ATOM   4731  C   ALA B 253      14.778  40.988 -22.452  1.00 76.03           C  
ATOM   4732  O   ALA B 253      14.828  41.300 -21.264  1.00 75.80           O  
ATOM   4733  CB  ALA B 253      14.696  42.608 -24.339  1.00 76.88           C  
ATOM   4734  N   ASN B 254      14.006  40.011 -22.905  1.00 75.34           N  
ATOM   4735  CA  ASN B 254      13.187  39.223 -22.000  1.00 75.13           C  
ATOM   4736  C   ASN B 254      14.078  38.469 -21.019  1.00 72.33           C  
ATOM   4737  O   ASN B 254      13.770  38.375 -19.833  1.00 71.12           O  
ATOM   4738  CB  ASN B 254      12.334  38.225 -22.788  1.00 80.23           C  
ATOM   4739  CG  ASN B 254      11.189  38.890 -23.531  1.00 84.35           C  
ATOM   4740  OD1 ASN B 254      11.387  39.853 -24.273  1.00 85.36           O  
ATOM   4741  ND2 ASN B 254       9.980  38.369 -23.338  1.00 85.14           N  
ATOM   4742  N   ALA B 255      15.187  37.942 -21.528  1.00 68.94           N  
ATOM   4743  CA  ALA B 255      16.123  37.178 -20.718  1.00 66.89           C  
ATOM   4744  C   ALA B 255      16.650  37.978 -19.535  1.00 67.17           C  
ATOM   4745  O   ALA B 255      16.520  37.563 -18.386  1.00 67.33           O  
ATOM   4746  CB  ALA B 255      17.273  36.702 -21.580  1.00 66.75           C  
ATOM   4747  N   GLU B 256      17.245  39.127 -19.823  1.00 66.19           N  
ATOM   4748  CA  GLU B 256      17.791  39.982 -18.783  1.00 66.67           C  
ATOM   4749  C   GLU B 256      16.733  40.339 -17.740  1.00 66.89           C  
ATOM   4750  O   GLU B 256      16.985  40.276 -16.536  1.00 68.38           O  
ATOM   4751  CB  GLU B 256      18.354  41.253 -19.414  1.00 67.26           C  
ATOM   4752  CG  GLU B 256      19.511  40.996 -20.361  1.00 68.95           C  
ATOM   4753  CD  GLU B 256      20.827  40.804 -19.636  1.00 69.66           C  
ATOM   4754  OE1 GLU B 256      20.854  40.055 -18.641  1.00 70.54           O  
ATOM   4755  OE2 GLU B 256      21.837  41.403 -20.064  1.00 70.98           O  
ATOM   4756  N   MET B 257      15.550  40.715 -18.212  1.00 66.02           N  
ATOM   4757  CA  MET B 257      14.446  41.090 -17.341  1.00 65.81           C  
ATOM   4758  C   MET B 257      14.083  39.952 -16.401  1.00 67.07           C  
ATOM   4759  O   MET B 257      13.569  40.184 -15.301  1.00 68.68           O  
ATOM   4760  CB  MET B 257      13.232  41.484 -18.189  1.00 67.13           C  
ATOM   4761  CG  MET B 257      11.952  41.740 -17.410  1.00 71.46           C  
ATOM   4762  SD  MET B 257      12.133  42.951 -16.080  1.00 78.46           S  
ATOM   4763  CE  MET B 257      12.387  44.474 -17.040  1.00 78.79           C  
ATOM   4764  N   ARG B 258      14.352  38.721 -16.828  1.00 65.99           N  
ATOM   4765  CA  ARG B 258      14.044  37.561 -15.999  1.00 65.87           C  
ATOM   4766  C   ARG B 258      15.007  37.464 -14.818  1.00 63.53           C  
ATOM   4767  O   ARG B 258      14.587  37.228 -13.687  1.00 61.35           O  
ATOM   4768  CB  ARG B 258      14.116  36.274 -16.819  1.00 69.12           C  
ATOM   4769  CG  ARG B 258      13.475  35.088 -16.120  1.00 71.78           C  
ATOM   4770  CD  ARG B 258      13.720  33.789 -16.868  1.00 75.74           C  
ATOM   4771  NE  ARG B 258      12.700  32.791 -16.546  1.00 78.24           N  
ATOM   4772  CZ  ARG B 258      11.497  32.733 -17.114  1.00 76.41           C  
ATOM   4773  NH1 ARG B 258      11.146  33.612 -18.048  1.00 71.85           N  
ATOM   4774  NH2 ARG B 258      10.636  31.799 -16.735  1.00 75.39           N  
ATOM   4775  N   LEU B 259      16.299  37.632 -15.093  1.00 61.86           N  
ATOM   4776  CA  LEU B 259      17.314  37.583 -14.048  1.00 60.71           C  
ATOM   4777  C   LEU B 259      16.965  38.640 -13.005  1.00 60.71           C  
ATOM   4778  O   LEU B 259      17.031  38.392 -11.799  1.00 60.86           O  
ATOM   4779  CB  LEU B 259      18.704  37.867 -14.625  1.00 62.82           C  
ATOM   4780  CG  LEU B 259      19.432  36.799 -15.456  1.00 62.41           C  
ATOM   4781  CD1 LEU B 259      19.331  35.466 -14.747  1.00 64.65           C  
ATOM   4782  CD2 LEU B 259      18.838  36.695 -16.843  1.00 66.51           C  
ATOM   4783  N   ALA B 260      16.582  39.819 -13.486  1.00 59.30           N  
ATOM   4784  CA  ALA B 260      16.198  40.917 -12.614  1.00 59.44           C  
ATOM   4785  C   ALA B 260      15.058  40.512 -11.682  1.00 57.64           C  
ATOM   4786  O   ALA B 260      15.106  40.779 -10.483  1.00 57.69           O  
ATOM   4787  CB  ALA B 260      15.782  42.126 -13.443  1.00 60.61           C  
ATOM   4788  N   LYS B 261      14.026  39.878 -12.226  1.00 56.84           N  
ATOM   4789  CA  LYS B 261      12.910  39.464 -11.390  1.00 56.64           C  
ATOM   4790  C   LYS B 261      13.410  38.484 -10.348  1.00 56.82           C  
ATOM   4791  O   LYS B 261      13.025  38.560  -9.175  1.00 55.07           O  
ATOM   4792  CB  LYS B 261      11.808  38.803 -12.224  1.00 57.05           C  
ATOM   4793  CG  LYS B 261      11.221  39.684 -13.307  1.00 59.83           C  
ATOM   4794  CD  LYS B 261       9.864  39.150 -13.719  1.00 65.07           C  
ATOM   4795  CE  LYS B 261       9.240  39.972 -14.832  1.00 66.74           C  
ATOM   4796  NZ  LYS B 261       9.964  39.775 -16.110  1.00 70.71           N  
ATOM   4797  N   ILE B 262      14.275  37.564 -10.770  1.00 57.19           N  
ATOM   4798  CA  ILE B 262      14.818  36.579  -9.843  1.00 58.11           C  
ATOM   4799  C   ILE B 262      15.520  37.325  -8.717  1.00 57.88           C  
ATOM   4800  O   ILE B 262      15.333  37.016  -7.532  1.00 58.09           O  
ATOM   4801  CB  ILE B 262      15.825  35.634 -10.539  1.00 56.95           C  
ATOM   4802  CG1 ILE B 262      15.094  34.730 -11.528  1.00 52.59           C  
ATOM   4803  CG2 ILE B 262      16.546  34.784  -9.502  1.00 56.89           C  
ATOM   4804  CD1 ILE B 262      16.019  33.954 -12.428  1.00 56.14           C  
ATOM   4805  N   SER B 263      16.309  38.324  -9.098  1.00 55.41           N  
ATOM   4806  CA  SER B 263      17.036  39.138  -8.139  1.00 55.91           C  
ATOM   4807  C   SER B 263      16.077  39.703  -7.120  1.00 56.54           C  
ATOM   4808  O   SER B 263      16.337  39.665  -5.923  1.00 60.68           O  
ATOM   4809  CB  SER B 263      17.722  40.288  -8.854  1.00 57.43           C  
ATOM   4810  OG  SER B 263      18.264  39.844 -10.078  1.00 64.03           O  
ATOM   4811  N   ILE B 264      14.963  40.233  -7.607  1.00 56.38           N  
ATOM   4812  CA  ILE B 264      13.950  40.815  -6.743  1.00 55.51           C  
ATOM   4813  C   ILE B 264      13.431  39.788  -5.760  1.00 53.44           C  
ATOM   4814  O   ILE B 264      13.217  40.091  -4.592  1.00 53.78           O  
ATOM   4815  CB  ILE B 264      12.751  41.339  -7.565  1.00 59.38           C  
ATOM   4816  CG1 ILE B 264      13.234  42.347  -8.607  1.00 61.66           C  
ATOM   4817  CG2 ILE B 264      11.734  41.992  -6.638  1.00 61.35           C  
ATOM   4818  CD1 ILE B 264      12.157  42.788  -9.573  1.00 65.23           C  
ATOM   4819  N   VAL B 265      13.236  38.564  -6.229  1.00 51.55           N  
ATOM   4820  CA  VAL B 265      12.709  37.527  -5.357  1.00 52.82           C  
ATOM   4821  C   VAL B 265      13.669  37.106  -4.255  1.00 52.29           C  
ATOM   4822  O   VAL B 265      13.231  36.817  -3.148  1.00 52.00           O  
ATOM   4823  CB  VAL B 265      12.283  36.270  -6.147  1.00 55.16           C  
ATOM   4824  CG1 VAL B 265      11.770  35.211  -5.192  1.00 52.51           C  
ATOM   4825  CG2 VAL B 265      11.204  36.628  -7.153  1.00 51.56           C  
ATOM   4826  N   ILE B 266      14.969  37.060  -4.535  1.00 52.42           N  
ATOM   4827  CA  ILE B 266      15.895  36.669  -3.483  1.00 52.39           C  
ATOM   4828  C   ILE B 266      15.997  37.808  -2.479  1.00 52.00           C  
ATOM   4829  O   ILE B 266      16.139  37.584  -1.275  1.00 53.55           O  
ATOM   4830  CB  ILE B 266      17.295  36.323  -4.020  1.00 53.88           C  
ATOM   4831  CG1 ILE B 266      17.995  37.575  -4.526  1.00 56.75           C  
ATOM   4832  CG2 ILE B 266      17.181  35.282  -5.113  1.00 51.84           C  
ATOM   4833  CD1 ILE B 266      19.450  37.338  -4.877  1.00 59.94           C  
ATOM   4834  N   VAL B 267      15.904  39.036  -2.975  1.00 52.52           N  
ATOM   4835  CA  VAL B 267      15.957  40.209  -2.108  1.00 51.22           C  
ATOM   4836  C   VAL B 267      14.786  40.166  -1.143  1.00 48.59           C  
ATOM   4837  O   VAL B 267      14.947  40.398   0.054  1.00 49.20           O  
ATOM   4838  CB  VAL B 267      15.891  41.523  -2.929  1.00 52.72           C  
ATOM   4839  CG1 VAL B 267      15.422  42.678  -2.042  1.00 55.38           C  
ATOM   4840  CG2 VAL B 267      17.272  41.847  -3.498  1.00 50.51           C  
ATOM   4841  N   SER B 268      13.607  39.866  -1.678  1.00 47.73           N  
ATOM   4842  CA  SER B 268      12.383  39.786  -0.878  1.00 46.55           C  
ATOM   4843  C   SER B 268      12.500  38.687   0.163  1.00 45.14           C  
ATOM   4844  O   SER B 268      12.034  38.823   1.286  1.00 44.51           O  
ATOM   4845  CB  SER B 268      11.193  39.487  -1.782  1.00 46.90           C  
ATOM   4846  OG  SER B 268      11.118  40.425  -2.833  1.00 53.89           O  
ATOM   4847  N   GLN B 269      13.119  37.592  -0.247  1.00 45.59           N  
ATOM   4848  CA  GLN B 269      13.324  36.443   0.605  1.00 45.70           C  
ATOM   4849  C   GLN B 269      14.235  36.836   1.774  1.00 47.18           C  
ATOM   4850  O   GLN B 269      13.988  36.484   2.929  1.00 46.73           O  
ATOM   4851  CB  GLN B 269      13.933  35.314  -0.245  1.00 44.89           C  
ATOM   4852  CG  GLN B 269      14.446  34.113   0.502  1.00 46.40           C  
ATOM   4853  CD  GLN B 269      15.813  34.349   1.105  1.00 47.62           C  
ATOM   4854  OE1 GLN B 269      16.748  34.747   0.411  1.00 43.09           O  
ATOM   4855  NE2 GLN B 269      15.938  34.101   2.403  1.00 47.49           N  
ATOM   4856  N   PHE B 270      15.286  37.587   1.468  1.00 46.63           N  
ATOM   4857  CA  PHE B 270      16.205  38.014   2.503  1.00 47.00           C  
ATOM   4858  C   PHE B 270      15.487  38.962   3.465  1.00 48.53           C  
ATOM   4859  O   PHE B 270      15.399  38.693   4.657  1.00 48.78           O  
ATOM   4860  CB  PHE B 270      17.428  38.681   1.866  1.00 45.30           C  
ATOM   4861  CG  PHE B 270      18.458  39.145   2.861  1.00 49.18           C  
ATOM   4862  CD1 PHE B 270      18.282  40.347   3.565  1.00 49.35           C  
ATOM   4863  CD2 PHE B 270      19.595  38.383   3.113  1.00 46.38           C  
ATOM   4864  CE1 PHE B 270      19.227  40.775   4.501  1.00 46.92           C  
ATOM   4865  CE2 PHE B 270      20.539  38.799   4.042  1.00 47.76           C  
ATOM   4866  CZ  PHE B 270      20.355  39.998   4.738  1.00 48.08           C  
ATOM   4867  N   LEU B 271      14.962  40.060   2.934  1.00 49.81           N  
ATOM   4868  CA  LEU B 271      14.260  41.057   3.740  1.00 49.39           C  
ATOM   4869  C   LEU B 271      13.147  40.463   4.594  1.00 50.62           C  
ATOM   4870  O   LEU B 271      12.947  40.875   5.738  1.00 49.61           O  
ATOM   4871  CB  LEU B 271      13.668  42.143   2.834  1.00 48.78           C  
ATOM   4872  CG  LEU B 271      14.648  43.003   2.031  1.00 47.32           C  
ATOM   4873  CD1 LEU B 271      13.876  43.842   1.029  1.00 46.00           C  
ATOM   4874  CD2 LEU B 271      15.455  43.886   2.967  1.00 44.97           C  
ATOM   4875  N   LEU B 272      12.418  39.501   4.040  1.00 51.76           N  
ATOM   4876  CA  LEU B 272      11.324  38.879   4.775  1.00 54.70           C  
ATOM   4877  C   LEU B 272      11.810  37.968   5.878  1.00 55.36           C  
ATOM   4878  O   LEU B 272      11.151  37.814   6.903  1.00 55.82           O  
ATOM   4879  CB  LEU B 272      10.433  38.084   3.828  1.00 58.08           C  
ATOM   4880  CG  LEU B 272       9.299  38.909   3.223  1.00 63.00           C  
ATOM   4881  CD1 LEU B 272       8.815  38.296   1.917  1.00 65.22           C  
ATOM   4882  CD2 LEU B 272       8.179  38.998   4.244  1.00 64.90           C  
ATOM   4883  N   SER B 273      12.967  37.357   5.666  1.00 56.44           N  
ATOM   4884  CA  SER B 273      13.517  36.444   6.653  1.00 54.02           C  
ATOM   4885  C   SER B 273      14.218  37.180   7.785  1.00 53.68           C  
ATOM   4886  O   SER B 273      14.124  36.766   8.934  1.00 56.41           O  
ATOM   4887  CB  SER B 273      14.494  35.477   5.980  1.00 53.27           C  
ATOM   4888  OG  SER B 273      13.854  34.750   4.952  1.00 52.95           O  
ATOM   4889  N   TRP B 274      14.900  38.276   7.468  1.00 50.24           N  
ATOM   4890  CA  TRP B 274      15.634  39.026   8.476  1.00 49.21           C  
ATOM   4891  C   TRP B 274      14.877  40.134   9.231  1.00 48.46           C  
ATOM   4892  O   TRP B 274      15.170  40.407  10.403  1.00 43.73           O  
ATOM   4893  CB  TRP B 274      16.893  39.623   7.851  1.00 48.50           C  
ATOM   4894  CG  TRP B 274      18.028  38.659   7.736  1.00 48.05           C  
ATOM   4895  CD1 TRP B 274      18.410  37.964   6.627  1.00 47.76           C  
ATOM   4896  CD2 TRP B 274      18.946  38.298   8.771  1.00 46.72           C  
ATOM   4897  NE1 TRP B 274      19.512  37.197   6.904  1.00 45.17           N  
ATOM   4898  CE2 TRP B 274      19.864  37.381   8.214  1.00 44.53           C  
ATOM   4899  CE3 TRP B 274      19.083  38.659  10.118  1.00 45.05           C  
ATOM   4900  CZ2 TRP B 274      20.905  36.820   8.955  1.00 44.13           C  
ATOM   4901  CZ3 TRP B 274      20.121  38.098  10.856  1.00 43.42           C  
ATOM   4902  CH2 TRP B 274      21.015  37.191  10.273  1.00 42.82           C  
ATOM   4903  N   SER B 275      13.913  40.772   8.569  1.00 46.92           N  
ATOM   4904  CA  SER B 275      13.158  41.853   9.196  1.00 43.84           C  
ATOM   4905  C   SER B 275      12.469  41.518  10.513  1.00 41.23           C  
ATOM   4906  O   SER B 275      12.596  42.258  11.485  1.00 44.24           O  
ATOM   4907  CB  SER B 275      12.137  42.417   8.221  1.00 43.25           C  
ATOM   4908  OG  SER B 275      12.787  43.205   7.242  1.00 44.81           O  
ATOM   4909  N   PRO B 276      11.733  40.404  10.576  1.00 38.31           N  
ATOM   4910  CA  PRO B 276      11.087  40.121  11.857  1.00 38.13           C  
ATOM   4911  C   PRO B 276      12.088  40.115  13.019  1.00 38.62           C  
ATOM   4912  O   PRO B 276      11.854  40.732  14.049  1.00 38.72           O  
ATOM   4913  CB  PRO B 276      10.435  38.753  11.626  1.00 35.71           C  
ATOM   4914  CG  PRO B 276      10.155  38.758  10.165  1.00 32.76           C  
ATOM   4915  CD  PRO B 276      11.408  39.372   9.583  1.00 35.65           C  
ATOM   4916  N   TYR B 277      13.207  39.422  12.834  1.00 41.18           N  
ATOM   4917  CA  TYR B 277      14.247  39.333  13.861  1.00 37.60           C  
ATOM   4918  C   TYR B 277      14.926  40.680  14.069  1.00 34.96           C  
ATOM   4919  O   TYR B 277      15.289  41.042  15.180  1.00 33.18           O  
ATOM   4920  CB  TYR B 277      15.288  38.286  13.450  1.00 39.11           C  
ATOM   4921  CG  TYR B 277      16.469  38.177  14.385  1.00 41.09           C  
ATOM   4922  CD1 TYR B 277      17.735  38.628  14.003  1.00 37.28           C  
ATOM   4923  CD2 TYR B 277      16.322  37.618  15.661  1.00 41.03           C  
ATOM   4924  CE1 TYR B 277      18.821  38.523  14.865  1.00 31.66           C  
ATOM   4925  CE2 TYR B 277      17.400  37.511  16.527  1.00 36.60           C  
ATOM   4926  CZ  TYR B 277      18.642  37.960  16.123  1.00 37.01           C  
ATOM   4927  OH  TYR B 277      19.711  37.825  16.968  1.00 42.03           O  
ATOM   4928  N   ALA B 278      15.101  41.419  12.985  1.00 35.16           N  
ATOM   4929  CA  ALA B 278      15.742  42.719  13.074  1.00 38.63           C  
ATOM   4930  C   ALA B 278      14.900  43.613  13.980  1.00 41.79           C  
ATOM   4931  O   ALA B 278      15.433  44.388  14.787  1.00 38.08           O  
ATOM   4932  CB  ALA B 278      15.865  43.338  11.682  1.00 40.26           C  
ATOM   4933  N   VAL B 279      13.579  43.482  13.836  1.00 41.40           N  
ATOM   4934  CA  VAL B 279      12.646  44.273  14.608  1.00 39.39           C  
ATOM   4935  C   VAL B 279      12.610  43.816  16.065  1.00 40.30           C  
ATOM   4936  O   VAL B 279      12.595  44.642  16.980  1.00 42.35           O  
ATOM   4937  CB  VAL B 279      11.245  44.216  13.992  1.00 39.12           C  
ATOM   4938  CG1 VAL B 279      10.234  44.802  14.938  1.00 44.15           C  
ATOM   4939  CG2 VAL B 279      11.227  45.012  12.703  1.00 35.82           C  
ATOM   4940  N   VAL B 280      12.595  42.507  16.280  1.00 38.74           N  
ATOM   4941  CA  VAL B 280      12.595  41.980  17.630  1.00 39.83           C  
ATOM   4942  C   VAL B 280      13.824  42.528  18.351  1.00 40.72           C  
ATOM   4943  O   VAL B 280      13.787  42.815  19.546  1.00 41.02           O  
ATOM   4944  CB  VAL B 280      12.658  40.435  17.637  1.00 38.53           C  
ATOM   4945  CG1 VAL B 280      12.885  39.923  19.039  1.00 36.43           C  
ATOM   4946  CG2 VAL B 280      11.357  39.869  17.078  1.00 39.04           C  
ATOM   4947  N   ALA B 281      14.914  42.686  17.609  1.00 42.55           N  
ATOM   4948  CA  ALA B 281      16.150  43.209  18.168  1.00 42.21           C  
ATOM   4949  C   ALA B 281      16.025  44.690  18.492  1.00 42.28           C  
ATOM   4950  O   ALA B 281      16.486  45.141  19.545  1.00 44.04           O  
ATOM   4951  CB  ALA B 281      17.315  42.976  17.196  1.00 45.48           C  
ATOM   4952  N   LEU B 282      15.420  45.454  17.586  1.00 43.47           N  
ATOM   4953  CA  LEU B 282      15.235  46.885  17.817  1.00 42.29           C  
ATOM   4954  C   LEU B 282      14.299  47.124  19.004  1.00 42.70           C  
ATOM   4955  O   LEU B 282      14.444  48.107  19.727  1.00 43.02           O  
ATOM   4956  CB  LEU B 282      14.677  47.565  16.571  1.00 40.12           C  
ATOM   4957  CG  LEU B 282      15.660  47.784  15.427  1.00 38.12           C  
ATOM   4958  CD1 LEU B 282      14.975  48.592  14.356  1.00 35.74           C  
ATOM   4959  CD2 LEU B 282      16.910  48.517  15.923  1.00 40.16           C  
ATOM   4960  N   LEU B 283      13.344  46.218  19.198  1.00 42.77           N  
ATOM   4961  CA  LEU B 283      12.406  46.326  20.304  1.00 45.31           C  
ATOM   4962  C   LEU B 283      13.154  46.086  21.610  1.00 47.64           C  
ATOM   4963  O   LEU B 283      12.881  46.715  22.634  1.00 48.51           O  
ATOM   4964  CB  LEU B 283      11.290  45.291  20.161  1.00 46.12           C  
ATOM   4965  CG  LEU B 283       9.995  45.737  19.466  1.00 48.39           C  
ATOM   4966  CD1 LEU B 283      10.295  46.310  18.104  1.00 50.53           C  
ATOM   4967  CD2 LEU B 283       9.061  44.549  19.352  1.00 47.99           C  
ATOM   4968  N   ALA B 284      14.111  45.169  21.559  1.00 49.44           N  
ATOM   4969  CA  ALA B 284      14.898  44.843  22.730  1.00 46.54           C  
ATOM   4970  C   ALA B 284      15.787  46.000  23.084  1.00 45.20           C  
ATOM   4971  O   ALA B 284      16.056  46.249  24.249  1.00 48.91           O  
ATOM   4972  CB  ALA B 284      15.732  43.612  22.473  1.00 46.03           C  
ATOM   4973  N   GLN B 285      16.255  46.721  22.085  1.00 45.82           N  
ATOM   4974  CA  GLN B 285      17.146  47.839  22.360  1.00 47.91           C  
ATOM   4975  C   GLN B 285      16.410  49.110  22.746  1.00 49.95           C  
ATOM   4976  O   GLN B 285      16.863  49.845  23.613  1.00 49.18           O  
ATOM   4977  CB  GLN B 285      18.023  48.123  21.141  1.00 47.22           C  
ATOM   4978  CG  GLN B 285      19.017  49.245  21.364  1.00 46.05           C  
ATOM   4979  CD  GLN B 285      20.020  48.936  22.460  1.00 46.06           C  
ATOM   4980  OE1 GLN B 285      20.700  49.841  22.961  1.00 46.42           O  
ATOM   4981  NE2 GLN B 285      20.127  47.651  22.837  1.00 40.37           N  
ATOM   4982  N   PHE B 286      15.264  49.360  22.117  1.00 51.50           N  
ATOM   4983  CA  PHE B 286      14.522  50.582  22.379  1.00 49.43           C  
ATOM   4984  C   PHE B 286      13.118  50.454  22.951  1.00 49.24           C  
ATOM   4985  O   PHE B 286      12.640  51.376  23.608  1.00 49.46           O  
ATOM   4986  CB  PHE B 286      14.466  51.411  21.100  1.00 47.55           C  
ATOM   4987  CG  PHE B 286      15.813  51.637  20.469  1.00 46.15           C  
ATOM   4988  CD1 PHE B 286      16.263  50.816  19.444  1.00 42.22           C  
ATOM   4989  CD2 PHE B 286      16.635  52.667  20.907  1.00 45.16           C  
ATOM   4990  CE1 PHE B 286      17.507  51.017  18.860  1.00 40.57           C  
ATOM   4991  CE2 PHE B 286      17.886  52.876  20.329  1.00 45.92           C  
ATOM   4992  CZ  PHE B 286      18.320  52.046  19.300  1.00 42.47           C  
ATOM   4993  N   GLY B 287      12.462  49.323  22.713  1.00 49.31           N  
ATOM   4994  CA  GLY B 287      11.109  49.129  23.206  1.00 47.80           C  
ATOM   4995  C   GLY B 287      10.955  48.404  24.535  1.00 49.47           C  
ATOM   4996  O   GLY B 287      11.851  48.433  25.373  1.00 48.02           O  
ATOM   4997  N   PRO B 288       9.802  47.752  24.758  1.00 51.94           N  
ATOM   4998  CA  PRO B 288       9.483  47.003  25.979  1.00 51.51           C  
ATOM   4999  C   PRO B 288      10.211  45.660  26.002  1.00 53.81           C  
ATOM   5000  O   PRO B 288       9.772  44.690  25.374  1.00 52.10           O  
ATOM   5001  CB  PRO B 288       7.963  46.821  25.892  1.00 50.14           C  
ATOM   5002  CG  PRO B 288       7.517  47.870  24.923  1.00 51.71           C  
ATOM   5003  CD  PRO B 288       8.611  47.860  23.901  1.00 52.63           C  
ATOM   5004  N   LEU B 289      11.312  45.604  26.746  1.00 53.72           N  
ATOM   5005  CA  LEU B 289      12.116  44.395  26.832  1.00 53.64           C  
ATOM   5006  C   LEU B 289      11.340  43.166  27.264  1.00 54.51           C  
ATOM   5007  O   LEU B 289      11.699  42.053  26.898  1.00 54.52           O  
ATOM   5008  CB  LEU B 289      13.295  44.606  27.779  1.00 52.69           C  
ATOM   5009  CG  LEU B 289      14.315  43.457  27.807  1.00 54.71           C  
ATOM   5010  CD1 LEU B 289      14.893  43.232  26.398  1.00 51.64           C  
ATOM   5011  CD2 LEU B 289      15.425  43.789  28.803  1.00 53.49           C  
ATOM   5012  N   GLU B 290      10.280  43.355  28.042  1.00 58.06           N  
ATOM   5013  CA  GLU B 290       9.503  42.208  28.501  1.00 59.97           C  
ATOM   5014  C   GLU B 290       8.831  41.497  27.339  1.00 58.81           C  
ATOM   5015  O   GLU B 290       8.384  40.361  27.475  1.00 59.41           O  
ATOM   5016  CB  GLU B 290       8.461  42.615  29.550  1.00 60.74           C  
ATOM   5017  CG  GLU B 290       7.513  43.733  29.145  1.00 64.94           C  
ATOM   5018  CD  GLU B 290       7.991  45.094  29.595  1.00 67.70           C  
ATOM   5019  OE1 GLU B 290       7.166  46.030  29.622  1.00 69.96           O  
ATOM   5020  OE2 GLU B 290       9.187  45.235  29.920  1.00 70.89           O  
ATOM   5021  N   TRP B 291       8.766  42.174  26.196  1.00 58.72           N  
ATOM   5022  CA  TRP B 291       8.179  41.592  24.993  1.00 58.80           C  
ATOM   5023  C   TRP B 291       9.153  40.563  24.438  1.00 56.91           C  
ATOM   5024  O   TRP B 291       8.753  39.496  23.982  1.00 59.49           O  
ATOM   5025  CB  TRP B 291       7.938  42.672  23.937  1.00 61.53           C  
ATOM   5026  CG  TRP B 291       6.752  43.555  24.190  1.00 66.52           C  
ATOM   5027  CD1 TRP B 291       6.144  43.802  25.389  1.00 67.37           C  
ATOM   5028  CD2 TRP B 291       6.075  44.363  23.224  1.00 68.50           C  
ATOM   5029  NE1 TRP B 291       5.131  44.717  25.227  1.00 66.86           N  
ATOM   5030  CE2 TRP B 291       5.067  45.078  23.908  1.00 68.78           C  
ATOM   5031  CE3 TRP B 291       6.224  44.554  21.843  1.00 70.67           C  
ATOM   5032  CZ2 TRP B 291       4.211  45.972  23.258  1.00 69.12           C  
ATOM   5033  CZ3 TRP B 291       5.371  45.445  21.194  1.00 70.30           C  
ATOM   5034  CH2 TRP B 291       4.378  46.142  21.905  1.00 70.32           C  
ATOM   5035  N   VAL B 292      10.438  40.893  24.492  1.00 54.61           N  
ATOM   5036  CA  VAL B 292      11.485  40.012  23.995  1.00 52.83           C  
ATOM   5037  C   VAL B 292      11.642  38.769  24.864  1.00 52.40           C  
ATOM   5038  O   VAL B 292      12.483  38.719  25.762  1.00 50.47           O  
ATOM   5039  CB  VAL B 292      12.837  40.745  23.928  1.00 53.54           C  
ATOM   5040  CG1 VAL B 292      13.848  39.908  23.157  1.00 49.18           C  
ATOM   5041  CG2 VAL B 292      12.657  42.103  23.277  1.00 51.87           C  
ATOM   5042  N   THR B 293      10.819  37.767  24.577  1.00 53.52           N  
ATOM   5043  CA  THR B 293      10.843  36.505  25.302  1.00 54.79           C  
ATOM   5044  C   THR B 293      11.692  35.498  24.531  1.00 55.86           C  
ATOM   5045  O   THR B 293      12.091  35.747  23.384  1.00 56.55           O  
ATOM   5046  CB  THR B 293       9.420  35.945  25.467  1.00 53.70           C  
ATOM   5047  OG1 THR B 293       8.833  35.733  24.179  1.00 54.47           O  
ATOM   5048  CG2 THR B 293       8.556  36.926  26.226  1.00 56.31           C  
ATOM   5049  N   PRO B 294      11.985  34.344  25.151  1.00 55.86           N  
ATOM   5050  CA  PRO B 294      12.797  33.320  24.486  1.00 55.32           C  
ATOM   5051  C   PRO B 294      12.323  33.010  23.065  1.00 54.27           C  
ATOM   5052  O   PRO B 294      13.125  32.988  22.139  1.00 53.22           O  
ATOM   5053  CB  PRO B 294      12.676  32.132  25.436  1.00 55.22           C  
ATOM   5054  CG  PRO B 294      12.635  32.805  26.771  1.00 53.30           C  
ATOM   5055  CD  PRO B 294      11.646  33.926  26.524  1.00 55.40           C  
ATOM   5056  N   TYR B 295      11.022  32.783  22.905  1.00 55.16           N  
ATOM   5057  CA  TYR B 295      10.439  32.479  21.598  1.00 57.14           C  
ATOM   5058  C   TYR B 295      10.322  33.727  20.722  1.00 55.25           C  
ATOM   5059  O   TYR B 295      10.441  33.650  19.503  1.00 54.12           O  
ATOM   5060  CB  TYR B 295       9.049  31.850  21.772  1.00 60.83           C  
ATOM   5061  CG  TYR B 295       9.058  30.502  22.462  1.00 66.02           C  
ATOM   5062  CD1 TYR B 295       7.972  30.088  23.230  1.00 68.90           C  
ATOM   5063  CD2 TYR B 295      10.147  29.641  22.345  1.00 69.00           C  
ATOM   5064  CE1 TYR B 295       7.966  28.853  23.869  1.00 71.55           C  
ATOM   5065  CE2 TYR B 295      10.156  28.398  22.979  1.00 72.29           C  
ATOM   5066  CZ  TYR B 295       9.060  28.013  23.739  1.00 73.82           C  
ATOM   5067  OH  TYR B 295       9.055  26.784  24.364  1.00 73.80           O  
ATOM   5068  N   ALA B 296      10.091  34.877  21.349  1.00 54.12           N  
ATOM   5069  CA  ALA B 296       9.964  36.119  20.600  1.00 51.86           C  
ATOM   5070  C   ALA B 296      11.252  36.412  19.837  1.00 50.05           C  
ATOM   5071  O   ALA B 296      11.237  37.092  18.815  1.00 50.70           O  
ATOM   5072  CB  ALA B 296       9.633  37.269  21.540  1.00 50.92           C  
ATOM   5073  N   ALA B 297      12.367  35.899  20.344  1.00 49.07           N  
ATOM   5074  CA  ALA B 297      13.658  36.106  19.699  1.00 46.45           C  
ATOM   5075  C   ALA B 297      14.074  34.873  18.915  1.00 45.64           C  
ATOM   5076  O   ALA B 297      14.454  34.965  17.741  1.00 44.59           O  
ATOM   5077  CB  ALA B 297      14.715  36.425  20.730  1.00 46.08           C  
ATOM   5078  N   GLN B 298      13.971  33.719  19.570  1.00 44.47           N  
ATOM   5079  CA  GLN B 298      14.354  32.444  18.983  1.00 44.42           C  
ATOM   5080  C   GLN B 298      13.681  32.062  17.667  1.00 46.26           C  
ATOM   5081  O   GLN B 298      14.362  31.773  16.686  1.00 48.63           O  
ATOM   5082  CB  GLN B 298      14.128  31.329  19.988  1.00 44.99           C  
ATOM   5083  CG  GLN B 298      14.913  30.098  19.654  1.00 48.33           C  
ATOM   5084  CD  GLN B 298      16.395  30.370  19.689  1.00 48.23           C  
ATOM   5085  OE1 GLN B 298      16.979  30.515  20.765  1.00 47.57           O  
ATOM   5086  NE2 GLN B 298      17.012  30.462  18.520  1.00 46.17           N  
ATOM   5087  N   LEU B 299      12.354  32.039  17.638  1.00 48.30           N  
ATOM   5088  CA  LEU B 299      11.653  31.672  16.417  1.00 49.38           C  
ATOM   5089  C   LEU B 299      12.057  32.543  15.241  1.00 47.81           C  
ATOM   5090  O   LEU B 299      12.425  32.030  14.185  1.00 49.01           O  
ATOM   5091  CB  LEU B 299      10.128  31.738  16.613  1.00 52.62           C  
ATOM   5092  CG  LEU B 299       9.477  30.480  17.200  1.00 55.74           C  
ATOM   5093  CD1 LEU B 299      10.129  30.109  18.531  1.00 55.68           C  
ATOM   5094  CD2 LEU B 299       7.996  30.718  17.383  1.00 54.83           C  
ATOM   5095  N   PRO B 300      12.010  33.874  15.411  1.00 48.04           N  
ATOM   5096  CA  PRO B 300      12.372  34.813  14.342  1.00 47.20           C  
ATOM   5097  C   PRO B 300      13.828  34.689  13.875  1.00 46.44           C  
ATOM   5098  O   PRO B 300      14.149  35.021  12.728  1.00 44.78           O  
ATOM   5099  CB  PRO B 300      12.096  36.181  14.972  1.00 47.56           C  
ATOM   5100  CG  PRO B 300      11.059  35.877  16.029  1.00 45.33           C  
ATOM   5101  CD  PRO B 300      11.587  34.605  16.616  1.00 46.78           C  
ATOM   5102  N   VAL B 301      14.701  34.218  14.763  1.00 44.61           N  
ATOM   5103  CA  VAL B 301      16.109  34.066  14.421  1.00 44.74           C  
ATOM   5104  C   VAL B 301      16.366  32.769  13.664  1.00 45.44           C  
ATOM   5105  O   VAL B 301      17.355  32.663  12.947  1.00 45.73           O  
ATOM   5106  CB  VAL B 301      17.028  34.122  15.684  1.00 44.24           C  
ATOM   5107  CG1 VAL B 301      17.023  32.792  16.424  1.00 40.77           C  
ATOM   5108  CG2 VAL B 301      18.436  34.501  15.269  1.00 44.30           C  
ATOM   5109  N   MET B 302      15.484  31.787  13.821  1.00 45.39           N  
ATOM   5110  CA  MET B 302      15.640  30.524  13.114  1.00 46.42           C  
ATOM   5111  C   MET B 302      15.276  30.750  11.652  1.00 49.91           C  
ATOM   5112  O   MET B 302      15.763  30.057  10.752  1.00 48.84           O  
ATOM   5113  CB  MET B 302      14.724  29.449  13.704  1.00 47.24           C  
ATOM   5114  CG  MET B 302      15.051  29.068  15.143  1.00 49.07           C  
ATOM   5115  SD  MET B 302      16.816  28.773  15.377  1.00 50.29           S  
ATOM   5116  CE  MET B 302      17.040  27.272  14.471  1.00 44.01           C  
ATOM   5117  N   PHE B 303      14.411  31.734  11.427  1.00 53.75           N  
ATOM   5118  CA  PHE B 303      13.976  32.082  10.087  1.00 56.59           C  
ATOM   5119  C   PHE B 303      15.037  32.944   9.422  1.00 53.90           C  
ATOM   5120  O   PHE B 303      15.267  32.833   8.227  1.00 54.14           O  
ATOM   5121  CB  PHE B 303      12.647  32.837  10.136  1.00 62.84           C  
ATOM   5122  CG  PHE B 303      11.705  32.458   9.042  1.00 69.67           C  
ATOM   5123  CD1 PHE B 303      11.410  33.345   8.016  1.00 74.86           C  
ATOM   5124  CD2 PHE B 303      11.136  31.189   9.019  1.00 73.83           C  
ATOM   5125  CE1 PHE B 303      10.560  32.975   6.974  1.00 76.14           C  
ATOM   5126  CE2 PHE B 303      10.285  30.807   7.983  1.00 78.11           C  
ATOM   5127  CZ  PHE B 303       9.997  31.702   6.957  1.00 78.29           C  
ATOM   5128  N   ALA B 304      15.686  33.806  10.195  1.00 52.93           N  
ATOM   5129  CA  ALA B 304      16.735  34.644   9.634  1.00 51.71           C  
ATOM   5130  C   ALA B 304      17.858  33.713   9.193  1.00 50.20           C  
ATOM   5131  O   ALA B 304      18.461  33.913   8.147  1.00 52.73           O  
ATOM   5132  CB  ALA B 304      17.247  35.643  10.667  1.00 49.42           C  
ATOM   5133  N   LYS B 305      18.117  32.684   9.991  1.00 47.42           N  
ATOM   5134  CA  LYS B 305      19.155  31.714   9.683  1.00 44.54           C  
ATOM   5135  C   LYS B 305      18.810  30.856   8.464  1.00 46.26           C  
ATOM   5136  O   LYS B 305      19.686  30.504   7.673  1.00 50.56           O  
ATOM   5137  CB  LYS B 305      19.397  30.794  10.884  1.00 41.11           C  
ATOM   5138  CG  LYS B 305      19.991  31.491  12.093  1.00 40.43           C  
ATOM   5139  CD  LYS B 305      20.479  30.505  13.112  1.00 36.42           C  
ATOM   5140  CE  LYS B 305      20.798  31.175  14.432  1.00 39.81           C  
ATOM   5141  NZ  LYS B 305      22.059  31.918  14.432  1.00 41.75           N  
ATOM   5142  N   ALA B 306      17.536  30.515   8.313  1.00 43.69           N  
ATOM   5143  CA  ALA B 306      17.118  29.689   7.191  1.00 43.35           C  
ATOM   5144  C   ALA B 306      17.198  30.482   5.898  1.00 45.10           C  
ATOM   5145  O   ALA B 306      17.136  29.912   4.813  1.00 48.06           O  
ATOM   5146  CB  ALA B 306      15.701  29.198   7.405  1.00 43.83           C  
ATOM   5147  N   SER B 307      17.336  31.797   6.018  1.00 45.32           N  
ATOM   5148  CA  SER B 307      17.401  32.648   4.852  1.00 44.37           C  
ATOM   5149  C   SER B 307      18.514  32.257   3.897  1.00 46.16           C  
ATOM   5150  O   SER B 307      18.360  32.349   2.688  1.00 47.16           O  
ATOM   5151  CB  SER B 307      17.593  34.104   5.269  1.00 45.44           C  
ATOM   5152  OG  SER B 307      17.741  34.940   4.132  1.00 46.88           O  
ATOM   5153  N   ALA B 308      19.637  31.806   4.446  1.00 49.96           N  
ATOM   5154  CA  ALA B 308      20.800  31.424   3.635  1.00 49.19           C  
ATOM   5155  C   ALA B 308      20.656  30.127   2.841  1.00 48.83           C  
ATOM   5156  O   ALA B 308      21.636  29.637   2.284  1.00 49.51           O  
ATOM   5157  CB  ALA B 308      22.043  31.347   4.521  1.00 45.03           C  
ATOM   5158  N   ILE B 309      19.453  29.571   2.772  1.00 48.77           N  
ATOM   5159  CA  ILE B 309      19.280  28.326   2.038  1.00 48.41           C  
ATOM   5160  C   ILE B 309      18.259  28.423   0.906  1.00 50.01           C  
ATOM   5161  O   ILE B 309      18.093  27.467   0.139  1.00 52.47           O  
ATOM   5162  CB  ILE B 309      18.818  27.189   2.963  1.00 47.92           C  
ATOM   5163  CG1 ILE B 309      17.332  27.368   3.301  1.00 49.91           C  
ATOM   5164  CG2 ILE B 309      19.646  27.189   4.249  1.00 45.44           C  
ATOM   5165  CD1 ILE B 309      16.718  26.208   4.065  1.00 48.87           C  
ATOM   5166  N   HIS B 310      17.582  29.566   0.802  1.00 49.41           N  
ATOM   5167  CA  HIS B 310      16.554  29.771  -0.213  1.00 45.65           C  
ATOM   5168  C   HIS B 310      17.022  30.090  -1.632  1.00 47.22           C  
ATOM   5169  O   HIS B 310      16.413  29.643  -2.603  1.00 49.26           O  
ATOM   5170  CB  HIS B 310      15.589  30.864   0.241  1.00 44.47           C  
ATOM   5171  CG  HIS B 310      14.915  30.573   1.547  1.00 45.10           C  
ATOM   5172  ND1 HIS B 310      14.302  29.367   1.821  1.00 44.54           N  
ATOM   5173  CD2 HIS B 310      14.716  31.350   2.637  1.00 44.01           C  
ATOM   5174  CE1 HIS B 310      13.751  29.415   3.019  1.00 42.30           C  
ATOM   5175  NE2 HIS B 310      13.988  30.608   3.536  1.00 42.34           N  
ATOM   5176  N   ASN B 311      18.096  30.857  -1.768  1.00 49.72           N  
ATOM   5177  CA  ASN B 311      18.572  31.206  -3.103  1.00 52.61           C  
ATOM   5178  C   ASN B 311      18.753  30.024  -4.063  1.00 53.74           C  
ATOM   5179  O   ASN B 311      18.144  29.995  -5.129  1.00 55.17           O  
ATOM   5180  CB  ASN B 311      19.866  32.010  -3.015  1.00 52.34           C  
ATOM   5181  CG  ASN B 311      19.664  33.336  -2.335  1.00 53.29           C  
ATOM   5182  OD1 ASN B 311      18.535  33.794  -2.187  1.00 53.99           O  
ATOM   5183  ND2 ASN B 311      20.753  33.968  -1.927  1.00 55.83           N  
ATOM   5184  N   PRO B 312      19.579  29.032  -3.698  1.00 54.30           N  
ATOM   5185  CA  PRO B 312      19.771  27.891  -4.594  1.00 53.88           C  
ATOM   5186  C   PRO B 312      18.464  27.313  -5.145  1.00 54.20           C  
ATOM   5187  O   PRO B 312      18.353  27.069  -6.348  1.00 53.69           O  
ATOM   5188  CB  PRO B 312      20.537  26.903  -3.724  1.00 54.65           C  
ATOM   5189  CG  PRO B 312      21.371  27.800  -2.889  1.00 56.09           C  
ATOM   5190  CD  PRO B 312      20.379  28.870  -2.473  1.00 54.67           C  
ATOM   5191  N   MET B 313      17.481  27.095  -4.276  1.00 55.06           N  
ATOM   5192  CA  MET B 313      16.190  26.560  -4.715  1.00 56.59           C  
ATOM   5193  C   MET B 313      15.469  27.552  -5.628  1.00 54.71           C  
ATOM   5194  O   MET B 313      14.887  27.165  -6.633  1.00 54.85           O  
ATOM   5195  CB  MET B 313      15.301  26.230  -3.514  1.00 58.78           C  
ATOM   5196  CG  MET B 313      15.878  25.142  -2.630  1.00 62.73           C  
ATOM   5197  SD  MET B 313      14.806  24.683  -1.267  1.00 66.19           S  
ATOM   5198  CE  MET B 313      15.192  26.018  -0.080  1.00 62.35           C  
ATOM   5199  N   ILE B 314      15.515  28.834  -5.273  1.00 54.07           N  
ATOM   5200  CA  ILE B 314      14.892  29.867  -6.088  1.00 51.28           C  
ATOM   5201  C   ILE B 314      15.432  29.783  -7.521  1.00 52.16           C  
ATOM   5202  O   ILE B 314      14.671  29.883  -8.481  1.00 51.96           O  
ATOM   5203  CB  ILE B 314      15.167  31.274  -5.509  1.00 49.59           C  
ATOM   5204  CG1 ILE B 314      14.400  31.445  -4.199  1.00 48.02           C  
ATOM   5205  CG2 ILE B 314      14.765  32.357  -6.503  1.00 48.30           C  
ATOM   5206  CD1 ILE B 314      14.561  32.831  -3.568  1.00 50.00           C  
ATOM   5207  N   TYR B 315      16.744  29.595  -7.662  1.00 53.32           N  
ATOM   5208  CA  TYR B 315      17.349  29.483  -8.989  1.00 54.79           C  
ATOM   5209  C   TYR B 315      16.866  28.210  -9.685  1.00 54.42           C  
ATOM   5210  O   TYR B 315      16.541  28.206 -10.877  1.00 54.32           O  
ATOM   5211  CB  TYR B 315      18.875  29.406  -8.918  1.00 53.63           C  
ATOM   5212  CG  TYR B 315      19.575  30.576  -8.276  1.00 56.26           C  
ATOM   5213  CD1 TYR B 315      19.136  31.887  -8.475  1.00 56.50           C  
ATOM   5214  CD2 TYR B 315      20.704  30.373  -7.484  1.00 56.84           C  
ATOM   5215  CE1 TYR B 315      19.810  32.962  -7.889  1.00 56.05           C  
ATOM   5216  CE2 TYR B 315      21.379  31.432  -6.904  1.00 54.88           C  
ATOM   5217  CZ  TYR B 315      20.931  32.718  -7.102  1.00 53.36           C  
ATOM   5218  OH  TYR B 315      21.587  33.747  -6.482  1.00 51.47           O  
ATOM   5219  N   SER B 316      16.834  27.123  -8.926  1.00 55.92           N  
ATOM   5220  CA  SER B 316      16.432  25.836  -9.460  1.00 57.00           C  
ATOM   5221  C   SER B 316      15.036  25.820 -10.054  1.00 58.84           C  
ATOM   5222  O   SER B 316      14.696  24.906 -10.796  1.00 61.81           O  
ATOM   5223  CB  SER B 316      16.516  24.767  -8.380  1.00 55.82           C  
ATOM   5224  OG  SER B 316      15.459  24.907  -7.450  1.00 58.67           O  
ATOM   5225  N   VAL B 317      14.221  26.815  -9.732  1.00 59.06           N  
ATOM   5226  CA  VAL B 317      12.865  26.850 -10.264  1.00 56.61           C  
ATOM   5227  C   VAL B 317      12.639  28.066 -11.157  1.00 54.85           C  
ATOM   5228  O   VAL B 317      11.511  28.354 -11.535  1.00 54.60           O  
ATOM   5229  CB  VAL B 317      11.816  26.896  -9.133  1.00 58.49           C  
ATOM   5230  CG1 VAL B 317      10.470  26.460  -9.663  1.00 63.24           C  
ATOM   5231  CG2 VAL B 317      12.237  26.009  -7.978  1.00 58.92           C  
ATOM   5232  N   SER B 318      13.707  28.776 -11.502  1.00 52.39           N  
ATOM   5233  CA  SER B 318      13.557  29.967 -12.330  1.00 52.31           C  
ATOM   5234  C   SER B 318      14.729  30.276 -13.246  1.00 53.33           C  
ATOM   5235  O   SER B 318      14.554  30.904 -14.290  1.00 53.80           O  
ATOM   5236  CB  SER B 318      13.306  31.178 -11.441  1.00 52.87           C  
ATOM   5237  OG  SER B 318      14.304  31.262 -10.432  1.00 54.22           O  
ATOM   5238  N   HIS B 319      15.927  29.857 -12.857  1.00 52.52           N  
ATOM   5239  CA  HIS B 319      17.094  30.120 -13.681  1.00 52.54           C  
ATOM   5240  C   HIS B 319      17.227  29.060 -14.771  1.00 54.16           C  
ATOM   5241  O   HIS B 319      17.592  27.916 -14.495  1.00 56.17           O  
ATOM   5242  CB  HIS B 319      18.364  30.153 -12.823  1.00 48.22           C  
ATOM   5243  CG  HIS B 319      19.492  30.899 -13.466  1.00 43.44           C  
ATOM   5244  ND1 HIS B 319      20.079  30.488 -14.642  1.00 41.53           N  
ATOM   5245  CD2 HIS B 319      20.084  32.071 -13.139  1.00 39.86           C  
ATOM   5246  CE1 HIS B 319      20.981  31.377 -15.014  1.00 37.74           C  
ATOM   5247  NE2 HIS B 319      21.003  32.349 -14.120  1.00 38.34           N  
ATOM   5248  N   PRO B 320      16.935  29.431 -16.031  1.00 55.08           N  
ATOM   5249  CA  PRO B 320      17.022  28.502 -17.164  1.00 54.72           C  
ATOM   5250  C   PRO B 320      18.410  27.897 -17.395  1.00 53.77           C  
ATOM   5251  O   PRO B 320      18.585  26.691 -17.288  1.00 53.41           O  
ATOM   5252  CB  PRO B 320      16.533  29.351 -18.338  1.00 54.46           C  
ATOM   5253  CG  PRO B 320      16.926  30.728 -17.942  1.00 55.08           C  
ATOM   5254  CD  PRO B 320      16.525  30.767 -16.493  1.00 55.36           C  
ATOM   5255  N   LYS B 321      19.397  28.730 -17.703  1.00 54.48           N  
ATOM   5256  CA  LYS B 321      20.742  28.226 -17.939  1.00 55.04           C  
ATOM   5257  C   LYS B 321      21.289  27.459 -16.743  1.00 55.29           C  
ATOM   5258  O   LYS B 321      22.180  26.624 -16.902  1.00 56.61           O  
ATOM   5259  CB  LYS B 321      21.682  29.371 -18.328  1.00 56.14           C  
ATOM   5260  CG  LYS B 321      21.318  29.999 -19.674  1.00 62.74           C  
ATOM   5261  CD  LYS B 321      22.219  31.167 -20.069  1.00 67.42           C  
ATOM   5262  CE  LYS B 321      23.604  30.711 -20.505  1.00 71.58           C  
ATOM   5263  NZ  LYS B 321      24.450  31.863 -20.954  1.00 74.66           N  
ATOM   5264  N   PHE B 322      20.765  27.737 -15.549  1.00 53.91           N  
ATOM   5265  CA  PHE B 322      21.199  27.030 -14.347  1.00 50.95           C  
ATOM   5266  C   PHE B 322      20.453  25.704 -14.298  1.00 52.65           C  
ATOM   5267  O   PHE B 322      21.062  24.650 -14.165  1.00 53.89           O  
ATOM   5268  CB  PHE B 322      20.890  27.848 -13.091  1.00 49.84           C  
ATOM   5269  CG  PHE B 322      21.215  27.130 -11.792  1.00 46.46           C  
ATOM   5270  CD1 PHE B 322      22.498  26.658 -11.543  1.00 43.84           C  
ATOM   5271  CD2 PHE B 322      20.239  26.943 -10.831  1.00 40.75           C  
ATOM   5272  CE1 PHE B 322      22.803  26.012 -10.358  1.00 43.71           C  
ATOM   5273  CE2 PHE B 322      20.532  26.297  -9.635  1.00 43.30           C  
ATOM   5274  CZ  PHE B 322      21.821  25.829  -9.398  1.00 43.91           C  
ATOM   5275  N   ARG B 323      19.130  25.766 -14.410  1.00 55.37           N  
ATOM   5276  CA  ARG B 323      18.301  24.563 -14.400  1.00 58.51           C  
ATOM   5277  C   ARG B 323      18.780  23.588 -15.470  1.00 60.71           C  
ATOM   5278  O   ARG B 323      18.682  22.371 -15.305  1.00 61.81           O  
ATOM   5279  CB  ARG B 323      16.835  24.918 -14.679  1.00 59.43           C  
ATOM   5280  CG  ARG B 323      16.078  25.515 -13.511  1.00 58.71           C  
ATOM   5281  CD  ARG B 323      14.750  26.086 -13.982  1.00 60.54           C  
ATOM   5282  NE  ARG B 323      13.893  25.090 -14.628  1.00 61.33           N  
ATOM   5283  CZ  ARG B 323      13.183  24.162 -13.987  1.00 58.52           C  
ATOM   5284  NH1 ARG B 323      13.212  24.084 -12.666  1.00 56.23           N  
ATOM   5285  NH2 ARG B 323      12.437  23.309 -14.672  1.00 58.12           N  
ATOM   5286  N   GLU B 324      19.294  24.136 -16.568  1.00 61.81           N  
ATOM   5287  CA  GLU B 324      19.790  23.335 -17.675  1.00 62.87           C  
ATOM   5288  C   GLU B 324      21.043  22.576 -17.252  1.00 62.83           C  
ATOM   5289  O   GLU B 324      21.199  21.392 -17.548  1.00 62.88           O  
ATOM   5290  CB  GLU B 324      20.114  24.236 -18.862  1.00 65.29           C  
ATOM   5291  CG  GLU B 324      20.343  23.487 -20.156  1.00 72.59           C  
ATOM   5292  CD  GLU B 324      21.010  24.338 -21.205  1.00 73.97           C  
ATOM   5293  OE1 GLU B 324      21.081  23.894 -22.369  1.00 77.75           O  
ATOM   5294  OE2 GLU B 324      21.470  25.449 -20.861  1.00 75.42           O  
ATOM   5295  N   ALA B 325      21.930  23.271 -16.550  1.00 61.55           N  
ATOM   5296  CA  ALA B 325      23.174  22.680 -16.076  1.00 61.22           C  
ATOM   5297  C   ALA B 325      22.948  21.584 -15.039  1.00 61.24           C  
ATOM   5298  O   ALA B 325      23.677  20.592 -15.005  1.00 60.67           O  
ATOM   5299  CB  ALA B 325      24.071  23.762 -15.501  1.00 61.62           C  
ATOM   5300  N   ILE B 326      21.951  21.753 -14.182  1.00 61.07           N  
ATOM   5301  CA  ILE B 326      21.698  20.732 -13.176  1.00 62.60           C  
ATOM   5302  C   ILE B 326      21.259  19.444 -13.875  1.00 65.15           C  
ATOM   5303  O   ILE B 326      21.853  18.381 -13.663  1.00 65.62           O  
ATOM   5304  CB  ILE B 326      20.612  21.178 -12.174  1.00 60.96           C  
ATOM   5305  CG1 ILE B 326      20.993  22.522 -11.553  1.00 59.98           C  
ATOM   5306  CG2 ILE B 326      20.472  20.137 -11.075  1.00 58.86           C  
ATOM   5307  CD1 ILE B 326      19.937  23.099 -10.633  1.00 57.76           C  
ATOM   5308  N   SER B 327      20.230  19.551 -14.716  1.00 65.00           N  
ATOM   5309  CA  SER B 327      19.710  18.400 -15.454  1.00 64.08           C  
ATOM   5310  C   SER B 327      20.840  17.608 -16.114  1.00 63.06           C  
ATOM   5311  O   SER B 327      20.792  16.381 -16.185  1.00 62.64           O  
ATOM   5312  CB  SER B 327      18.715  18.861 -16.521  1.00 62.93           C  
ATOM   5313  OG  SER B 327      19.330  19.736 -17.452  1.00 62.36           O  
ATOM   5314  N   GLN B 328      21.854  18.317 -16.592  1.00 60.44           N  
ATOM   5315  CA  GLN B 328      22.997  17.686 -17.233  1.00 60.66           C  
ATOM   5316  C   GLN B 328      24.031  17.140 -16.243  1.00 62.02           C  
ATOM   5317  O   GLN B 328      24.998  16.497 -16.649  1.00 60.92           O  
ATOM   5318  CB  GLN B 328      23.707  18.686 -18.142  1.00 61.91           C  
ATOM   5319  CG  GLN B 328      23.039  18.976 -19.472  1.00 62.65           C  
ATOM   5320  CD  GLN B 328      23.923  19.840 -20.352  1.00 62.88           C  
ATOM   5321  OE1 GLN B 328      23.638  20.060 -21.527  1.00 62.51           O  
ATOM   5322  NE2 GLN B 328      25.012  20.337 -19.776  1.00 64.46           N  
ATOM   5323  N   THR B 329      23.851  17.397 -14.952  1.00 62.75           N  
ATOM   5324  CA  THR B 329      24.816  16.919 -13.970  1.00 63.43           C  
ATOM   5325  C   THR B 329      24.182  16.236 -12.769  1.00 62.76           C  
ATOM   5326  O   THR B 329      24.584  15.138 -12.385  1.00 60.61           O  
ATOM   5327  CB  THR B 329      25.694  18.069 -13.470  1.00 65.02           C  
ATOM   5328  OG1 THR B 329      24.862  19.187 -13.146  1.00 69.75           O  
ATOM   5329  CG2 THR B 329      26.703  18.480 -14.537  1.00 64.48           C  
ATOM   5330  N   PHE B 330      23.196  16.895 -12.172  1.00 63.13           N  
ATOM   5331  CA  PHE B 330      22.499  16.352 -11.009  1.00 63.33           C  
ATOM   5332  C   PHE B 330      20.998  16.376 -11.291  1.00 65.10           C  
ATOM   5333  O   PHE B 330      20.209  16.882 -10.491  1.00 64.67           O  
ATOM   5334  CB  PHE B 330      22.814  17.189  -9.768  1.00 57.12           C  
ATOM   5335  CG  PHE B 330      24.283  17.382  -9.525  1.00 53.24           C  
ATOM   5336  CD1 PHE B 330      25.100  16.305  -9.209  1.00 51.99           C  
ATOM   5337  CD2 PHE B 330      24.847  18.648  -9.609  1.00 49.53           C  
ATOM   5338  CE1 PHE B 330      26.458  16.486  -8.978  1.00 48.06           C  
ATOM   5339  CE2 PHE B 330      26.198  18.838  -9.382  1.00 47.71           C  
ATOM   5340  CZ  PHE B 330      27.007  17.755  -9.066  1.00 48.90           C  
ATOM   5341  N   PRO B 331      20.588  15.797 -12.432  1.00 66.76           N  
ATOM   5342  CA  PRO B 331      19.190  15.738 -12.862  1.00 68.17           C  
ATOM   5343  C   PRO B 331      18.168  15.323 -11.807  1.00 69.89           C  
ATOM   5344  O   PRO B 331      17.061  15.854 -11.781  1.00 70.42           O  
ATOM   5345  CB  PRO B 331      19.235  14.767 -14.039  1.00 67.10           C  
ATOM   5346  CG  PRO B 331      20.360  13.864 -13.672  1.00 66.66           C  
ATOM   5347  CD  PRO B 331      21.395  14.844 -13.212  1.00 65.51           C  
ATOM   5348  N   TRP B 332      18.527  14.385 -10.939  1.00 71.74           N  
ATOM   5349  CA  TRP B 332      17.585  13.935  -9.923  1.00 75.18           C  
ATOM   5350  C   TRP B 332      17.016  15.094  -9.120  1.00 77.30           C  
ATOM   5351  O   TRP B 332      15.853  15.069  -8.723  1.00 78.96           O  
ATOM   5352  CB  TRP B 332      18.236  12.928  -8.972  1.00 76.36           C  
ATOM   5353  CG  TRP B 332      19.311  13.478  -8.102  1.00 80.12           C  
ATOM   5354  CD1 TRP B 332      20.655  13.434  -8.327  1.00 80.69           C  
ATOM   5355  CD2 TRP B 332      19.139  14.115  -6.829  1.00 83.06           C  
ATOM   5356  NE1 TRP B 332      21.333  13.998  -7.271  1.00 81.15           N  
ATOM   5357  CE2 TRP B 332      20.426  14.423  -6.338  1.00 83.12           C  
ATOM   5358  CE3 TRP B 332      18.020  14.452  -6.053  1.00 84.19           C  
ATOM   5359  CZ2 TRP B 332      20.629  15.053  -5.105  1.00 85.04           C  
ATOM   5360  CZ3 TRP B 332      18.219  15.079  -4.826  1.00 84.64           C  
ATOM   5361  CH2 TRP B 332      19.516  15.372  -4.365  1.00 85.53           C  
ATOM   5362  N   VAL B 333      17.841  16.110  -8.890  1.00 78.73           N  
ATOM   5363  CA  VAL B 333      17.423  17.280  -8.131  1.00 78.79           C  
ATOM   5364  C   VAL B 333      16.167  17.915  -8.722  1.00 79.42           C  
ATOM   5365  O   VAL B 333      15.291  18.377  -7.988  1.00 80.43           O  
ATOM   5366  CB  VAL B 333      18.548  18.339  -8.086  1.00 78.37           C  
ATOM   5367  CG1 VAL B 333      18.079  19.579  -7.339  1.00 76.98           C  
ATOM   5368  CG2 VAL B 333      19.775  17.757  -7.417  1.00 77.83           C  
ATOM   5369  N   LEU B 334      16.074  17.927 -10.046  1.00 79.60           N  
ATOM   5370  CA  LEU B 334      14.927  18.526 -10.721  1.00 80.66           C  
ATOM   5371  C   LEU B 334      13.756  17.570 -10.914  1.00 82.81           C  
ATOM   5372  O   LEU B 334      12.886  17.811 -11.750  1.00 83.04           O  
ATOM   5373  CB  LEU B 334      15.351  19.085 -12.079  1.00 77.96           C  
ATOM   5374  CG  LEU B 334      16.351  20.244 -12.044  1.00 76.97           C  
ATOM   5375  CD1 LEU B 334      16.831  20.535 -13.452  1.00 76.73           C  
ATOM   5376  CD2 LEU B 334      15.706  21.475 -11.422  1.00 74.43           C  
ATOM   5377  N   THR B 335      13.730  16.490 -10.143  1.00 85.06           N  
ATOM   5378  CA  THR B 335      12.647  15.525 -10.262  1.00 87.85           C  
ATOM   5379  C   THR B 335      11.284  16.216 -10.307  1.00 90.30           C  
ATOM   5380  O   THR B 335      10.567  16.110 -11.301  1.00 91.42           O  
ATOM   5381  CB  THR B 335      12.684  14.508  -9.105  1.00 88.13           C  
ATOM   5382  OG1 THR B 335      13.181  15.141  -7.920  1.00 88.30           O  
ATOM   5383  CG2 THR B 335      13.577  13.331  -9.463  1.00 87.05           C  
ATOM   5384  N   CYS B 336      10.931  16.933  -9.244  1.00 92.19           N  
ATOM   5385  CA  CYS B 336       9.648  17.628  -9.195  1.00 93.88           C  
ATOM   5386  C   CYS B 336       9.632  18.886 -10.049  1.00 93.78           C  
ATOM   5387  O   CYS B 336       8.611  19.567 -10.134  1.00 93.80           O  
ATOM   5388  CB  CYS B 336       9.294  18.003  -7.751  1.00 95.63           C  
ATOM   5389  SG  CYS B 336       8.424  16.724  -6.804  1.00100.21           S  
ATOM   5390  N   CYS B 337      10.759  19.190 -10.686  1.00 94.74           N  
ATOM   5391  CA  CYS B 337      10.879  20.389 -11.511  1.00 95.97           C  
ATOM   5392  C   CYS B 337      11.567  20.047 -12.835  1.00 94.34           C  
ATOM   5393  O   CYS B 337      12.554  20.671 -13.215  1.00 94.29           O  
ATOM   5394  CB  CYS B 337      11.691  21.442 -10.744  1.00 98.13           C  
ATOM   5395  SG  CYS B 337      11.699  21.132  -8.950  1.00103.95           S  
ATOM   5396  N   GLN B 338      11.030  19.048 -13.527  1.00 93.27           N  
ATOM   5397  CA  GLN B 338      11.572  18.583 -14.802  1.00 91.46           C  
ATOM   5398  C   GLN B 338      11.998  19.727 -15.712  1.00 88.51           C  
ATOM   5399  O   GLN B 338      11.286  20.719 -15.839  1.00 89.38           O  
ATOM   5400  CB  GLN B 338      10.530  17.727 -15.527  1.00 94.92           C  
ATOM   5401  CG  GLN B 338      11.097  16.470 -16.162  1.00 98.50           C  
ATOM   5402  CD  GLN B 338      11.594  15.478 -15.127  1.00 99.95           C  
ATOM   5403  OE1 GLN B 338      10.806  14.879 -14.395  1.00100.88           O  
ATOM   5404  NE2 GLN B 338      12.912  15.306 -15.054  1.00101.38           N  
ATOM   5405  N   PHE B 339      13.157  19.588 -16.349  1.00 85.40           N  
ATOM   5406  CA  PHE B 339      13.648  20.627 -17.250  1.00 83.52           C  
ATOM   5407  C   PHE B 339      13.178  20.418 -18.690  1.00 85.84           C  
ATOM   5408  O   PHE B 339      12.997  19.283 -19.136  1.00 86.19           O  
ATOM   5409  CB  PHE B 339      15.175  20.680 -17.235  1.00 76.45           C  
ATOM   5410  CG  PHE B 339      15.745  21.674 -18.206  1.00 70.26           C  
ATOM   5411  CD1 PHE B 339      15.554  23.039 -18.012  1.00 68.56           C  
ATOM   5412  CD2 PHE B 339      16.443  21.248 -19.326  1.00 67.09           C  
ATOM   5413  CE1 PHE B 339      16.052  23.966 -18.927  1.00 63.98           C  
ATOM   5414  CE2 PHE B 339      16.945  22.168 -20.243  1.00 64.44           C  
ATOM   5415  CZ  PHE B 339      16.747  23.527 -20.041  1.00 63.74           C  
ATOM   5416  N   ASP B 340      12.994  21.522 -19.411  1.00 87.46           N  
ATOM   5417  CA  ASP B 340      12.550  21.484 -20.803  1.00 88.00           C  
ATOM   5418  C   ASP B 340      13.389  22.436 -21.657  1.00 86.59           C  
ATOM   5419  O   ASP B 340      13.554  23.606 -21.314  1.00 85.46           O  
ATOM   5420  CB  ASP B 340      11.081  21.892 -20.901  1.00 91.70           C  
ATOM   5421  CG  ASP B 340      10.556  21.838 -22.324  1.00 96.13           C  
ATOM   5422  OD1 ASP B 340       9.532  22.504 -22.607  1.00 98.75           O  
ATOM   5423  OD2 ASP B 340      11.158  21.127 -23.158  1.00 97.65           O  
ATOM   5424  N   ASP B 341      13.909  21.933 -22.775  1.00 85.68           N  
ATOM   5425  CA  ASP B 341      14.734  22.744 -23.671  1.00 85.49           C  
ATOM   5426  C   ASP B 341      14.067  24.057 -24.064  1.00 84.30           C  
ATOM   5427  O   ASP B 341      14.731  24.991 -24.506  1.00 83.53           O  
ATOM   5428  CB  ASP B 341      15.070  21.950 -24.931  1.00 87.72           C  
ATOM   5429  CG  ASP B 341      16.007  20.795 -24.656  1.00 90.44           C  
ATOM   5430  OD1 ASP B 341      16.200  19.956 -25.562  1.00 91.73           O  
ATOM   5431  OD2 ASP B 341      16.554  20.730 -23.534  1.00 91.87           O  
ATOM   5432  N   LYS B 342      12.752  24.126 -23.911  1.00 83.67           N  
ATOM   5433  CA  LYS B 342      12.036  25.339 -24.255  1.00 84.16           C  
ATOM   5434  C   LYS B 342      12.486  26.502 -23.377  1.00 84.58           C  
ATOM   5435  O   LYS B 342      12.495  27.652 -23.816  1.00 86.44           O  
ATOM   5436  CB  LYS B 342      10.528  25.128 -24.100  1.00 84.42           C  
ATOM   5437  CG  LYS B 342       9.891  24.322 -25.219  1.00 86.77           C  
ATOM   5438  CD  LYS B 342       8.379  24.270 -25.064  1.00 86.37           C  
ATOM   5439  CE  LYS B 342       7.706  23.722 -26.316  1.00 87.35           C  
ATOM   5440  NZ  LYS B 342       7.875  24.622 -27.493  1.00 84.70           N  
ATOM   5441  N   GLU B 343      12.866  26.191 -22.140  1.00 82.84           N  
ATOM   5442  CA  GLU B 343      13.299  27.203 -21.176  1.00 79.89           C  
ATOM   5443  C   GLU B 343      14.468  28.056 -21.637  1.00 79.31           C  
ATOM   5444  O   GLU B 343      14.493  29.265 -21.405  1.00 78.61           O  
ATOM   5445  CB  GLU B 343      13.699  26.554 -19.856  1.00 79.36           C  
ATOM   5446  CG  GLU B 343      12.624  25.754 -19.170  1.00 80.25           C  
ATOM   5447  CD  GLU B 343      13.063  25.269 -17.800  1.00 82.23           C  
ATOM   5448  OE1 GLU B 343      12.362  24.418 -17.214  1.00 84.14           O  
ATOM   5449  OE2 GLU B 343      14.110  25.747 -17.306  1.00 83.39           O  
ATOM   5450  N   THR B 344      15.440  27.422 -22.283  1.00 78.60           N  
ATOM   5451  CA  THR B 344      16.638  28.113 -22.730  1.00 78.44           C  
ATOM   5452  C   THR B 344      16.597  28.732 -24.125  1.00 78.80           C  
ATOM   5453  O   THR B 344      17.588  29.306 -24.584  1.00 76.07           O  
ATOM   5454  CB  THR B 344      17.855  27.171 -22.624  1.00 78.58           C  
ATOM   5455  OG1 THR B 344      17.570  25.941 -23.296  1.00 77.83           O  
ATOM   5456  CG2 THR B 344      18.162  26.872 -21.163  1.00 78.19           C  
ATOM   5457  N   GLU B 345      15.452  28.628 -24.791  1.00 80.37           N  
ATOM   5458  CA  GLU B 345      15.297  29.181 -26.133  1.00 81.88           C  
ATOM   5459  C   GLU B 345      15.641  30.668 -26.175  1.00 82.04           C  
ATOM   5460  O   GLU B 345      16.337  31.131 -27.080  1.00 81.17           O  
ATOM   5461  CB  GLU B 345      13.863  28.985 -26.631  1.00 83.28           C  
ATOM   5462  CG  GLU B 345      13.448  27.535 -26.815  1.00 88.59           C  
ATOM   5463  CD  GLU B 345      11.969  27.383 -27.143  1.00 92.04           C  
ATOM   5464  OE1 GLU B 345      11.496  26.229 -27.253  1.00 93.79           O  
ATOM   5465  OE2 GLU B 345      11.276  28.413 -27.289  1.00 93.48           O  
ATOM   5466  N   ASP B 346      15.153  31.413 -25.191  1.00 82.80           N  
ATOM   5467  CA  ASP B 346      15.397  32.850 -25.137  1.00 84.33           C  
ATOM   5468  C   ASP B 346      16.878  33.196 -25.016  1.00 83.15           C  
ATOM   5469  O   ASP B 346      17.350  34.158 -25.621  1.00 83.00           O  
ATOM   5470  CB  ASP B 346      14.628  33.462 -23.972  1.00 87.56           C  
ATOM   5471  CG  ASP B 346      13.886  34.718 -24.363  1.00 92.41           C  
ATOM   5472  OD1 ASP B 346      13.234  35.317 -23.477  1.00 96.02           O  
ATOM   5473  OD2 ASP B 346      13.949  35.107 -25.553  1.00 94.59           O  
ATOM   5474  N   ASP B 347      17.610  32.417 -24.229  1.00 82.31           N  
ATOM   5475  CA  ASP B 347      19.038  32.648 -24.046  1.00 80.63           C  
ATOM   5476  C   ASP B 347      19.785  32.311 -25.330  1.00 79.42           C  
ATOM   5477  O   ASP B 347      20.715  33.013 -25.717  1.00 78.20           O  
ATOM   5478  CB  ASP B 347      19.574  31.793 -22.885  1.00 81.97           C  
ATOM   5479  CG  ASP B 347      19.210  32.355 -21.514  1.00 80.47           C  
ATOM   5480  OD1 ASP B 347      19.718  33.443 -21.153  1.00 77.99           O  
ATOM   5481  OD2 ASP B 347      18.421  31.707 -20.793  1.00 78.22           O  
ATOM   5482  N   LYS B 348      19.373  31.230 -25.987  1.00 80.83           N  
ATOM   5483  CA  LYS B 348      19.994  30.800 -27.243  1.00 81.47           C  
ATOM   5484  C   LYS B 348      19.829  31.888 -28.297  1.00 79.80           C  
ATOM   5485  O   LYS B 348      20.795  32.328 -28.907  1.00 78.15           O  
ATOM   5486  CB  LYS B 348      19.343  29.502 -27.745  1.00 81.54           C  
ATOM   5487  CG  LYS B 348      19.464  28.328 -26.785  1.00 82.13           C  
ATOM   5488  CD  LYS B 348      18.538  27.187 -27.182  1.00 82.54           C  
ATOM   5489  CE  LYS B 348      18.596  26.051 -26.167  1.00 82.02           C  
ATOM   5490  NZ  LYS B 348      17.550  25.018 -26.401  1.00 79.43           N  
ATOM   5491  N   ASP B 349      18.589  32.313 -28.503  1.00 81.23           N  
ATOM   5492  CA  ASP B 349      18.288  33.355 -29.474  1.00 83.88           C  
ATOM   5493  C   ASP B 349      19.040  34.639 -29.146  1.00 85.00           C  
ATOM   5494  O   ASP B 349      19.518  35.337 -30.037  1.00 85.84           O  
ATOM   5495  CB  ASP B 349      16.785  33.632 -29.493  1.00 84.17           C  
ATOM   5496  CG  ASP B 349      15.989  32.489 -30.092  1.00 84.55           C  
ATOM   5497  OD1 ASP B 349      16.186  31.334 -29.673  1.00 86.06           O  
ATOM   5498  OD2 ASP B 349      15.158  32.750 -30.983  1.00 85.98           O  
ATOM   5499  N   ALA B 350      19.142  34.948 -27.859  1.00 86.01           N  
ATOM   5500  CA  ALA B 350      19.829  36.153 -27.427  1.00 87.50           C  
ATOM   5501  C   ALA B 350      21.329  36.079 -27.700  1.00 90.09           C  
ATOM   5502  O   ALA B 350      21.939  37.067 -28.108  1.00 88.88           O  
ATOM   5503  CB  ALA B 350      19.579  36.384 -25.950  1.00 87.30           C  
ATOM   5504  N   GLU B 351      21.916  34.905 -27.480  1.00 93.21           N  
ATOM   5505  CA  GLU B 351      23.348  34.714 -27.680  1.00 95.50           C  
ATOM   5506  C   GLU B 351      23.732  34.307 -29.099  1.00 95.89           C  
ATOM   5507  O   GLU B 351      24.770  34.727 -29.606  1.00 96.84           O  
ATOM   5508  CB  GLU B 351      23.880  33.667 -26.700  1.00 98.47           C  
ATOM   5509  CG  GLU B 351      23.534  33.938 -25.247  1.00103.38           C  
ATOM   5510  CD  GLU B 351      23.868  35.352 -24.820  1.00106.18           C  
ATOM   5511  OE1 GLU B 351      25.022  35.784 -25.037  1.00108.51           O  
ATOM   5512  OE2 GLU B 351      22.978  36.031 -24.263  1.00107.38           O  
ATOM   5513  N   THR B 352      22.906  33.484 -29.735  1.00 96.92           N  
ATOM   5514  CA  THR B 352      23.191  33.034 -31.093  1.00 98.49           C  
ATOM   5515  C   THR B 352      23.403  34.221 -32.026  1.00 99.34           C  
ATOM   5516  O   THR B 352      22.449  34.861 -32.469  1.00 99.11           O  
ATOM   5517  CB  THR B 352      22.054  32.159 -31.651  1.00 98.47           C  
ATOM   5518  OG1 THR B 352      21.902  30.993 -30.832  1.00 99.65           O  
ATOM   5519  CG2 THR B 352      22.363  31.729 -33.078  1.00 97.44           C  
ATOM   5520  N   GLU B 353      24.668  34.504 -32.315  1.00100.57           N  
ATOM   5521  CA  GLU B 353      25.037  35.608 -33.188  1.00101.84           C  
ATOM   5522  C   GLU B 353      24.414  35.443 -34.569  1.00101.29           C  
ATOM   5523  O   GLU B 353      24.219  34.322 -35.043  1.00100.91           O  
ATOM   5524  CB  GLU B 353      26.560  35.668 -33.326  1.00103.95           C  
ATOM   5525  CG  GLU B 353      27.078  36.935 -33.978  1.00106.73           C  
ATOM   5526  CD  GLU B 353      26.697  38.171 -33.192  1.00109.05           C  
ATOM   5527  OE1 GLU B 353      26.885  38.169 -31.954  1.00110.74           O  
ATOM   5528  OE2 GLU B 353      26.219  39.146 -33.807  1.00109.56           O  
ATOM   5529  N   ILE B 354      24.097  36.560 -35.212  1.00100.43           N  
ATOM   5530  CA  ILE B 354      23.525  36.512 -36.547  1.00100.68           C  
ATOM   5531  C   ILE B 354      24.662  36.301 -37.546  1.00101.33           C  
ATOM   5532  O   ILE B 354      25.595  37.102 -37.617  1.00102.36           O  
ATOM   5533  CB  ILE B 354      22.766  37.819 -36.892  1.00100.27           C  
ATOM   5534  CG1 ILE B 354      23.630  39.045 -36.573  1.00 98.51           C  
ATOM   5535  CG2 ILE B 354      21.446  37.864 -36.133  1.00100.33           C  
ATOM   5536  CD1 ILE B 354      23.740  39.372 -35.100  1.00 97.13           C  
ATOM   5537  N   PRO B 355      24.605  35.207 -38.322  1.00100.91           N  
ATOM   5538  CA  PRO B 355      25.641  34.901 -39.313  1.00100.29           C  
ATOM   5539  C   PRO B 355      25.762  35.946 -40.417  1.00 99.61           C  
ATOM   5540  O   PRO B 355      26.842  36.568 -40.527  1.00 99.04           O  
ATOM   5541  CB  PRO B 355      25.209  33.539 -39.849  1.00100.58           C  
ATOM   5542  CG  PRO B 355      23.713  33.602 -39.742  1.00100.25           C  
ATOM   5543  CD  PRO B 355      23.525  34.206 -38.371  1.00100.53           C  
TER    5544      PRO B 355                                                      
HETATM 5545  C1  BOG A1005      12.233  44.439  90.667  1.00100.97           C  
HETATM 5546  O1  BOG A1005      13.093  44.451  89.610  1.00 93.99           O  
HETATM 5547  C2  BOG A1005      12.595  43.123  91.306  1.00103.78           C  
HETATM 5548  O2  BOG A1005      12.373  41.961  90.418  1.00105.33           O  
HETATM 5549  C3  BOG A1005      11.691  43.113  92.454  1.00105.97           C  
HETATM 5550  O3  BOG A1005      12.026  41.917  93.059  1.00105.83           O  
HETATM 5551  C4  BOG A1005      11.957  44.381  93.364  1.00106.64           C  
HETATM 5552  O4  BOG A1005      11.102  44.378  94.464  1.00107.27           O  
HETATM 5553  C5  BOG A1005      11.603  45.638  92.689  1.00106.27           C  
HETATM 5554  O5  BOG A1005      12.483  45.624  91.571  1.00103.92           O  
HETATM 5555  C6  BOG A1005      11.882  46.913  93.592  1.00107.22           C  
HETATM 5556  O6  BOG A1005      11.477  48.171  92.828  1.00106.49           O  
HETATM 5557  C1' BOG A1005      12.254  44.974  88.619  1.00 83.53           C  
HETATM 5558  C2' BOG A1005      13.219  45.322  87.600  1.00 77.28           C  
HETATM 5559  C3' BOG A1005      12.709  44.563  86.423  1.00 71.90           C  
HETATM 5560  C4' BOG A1005      13.932  44.171  85.814  1.00 67.89           C  
HETATM 5561  C5' BOG A1005      13.524  43.715  84.463  1.00 61.85           C  
HETATM 5562  C6' BOG A1005      14.548  42.761  84.174  1.00 59.91           C  
HETATM 5563  C7' BOG A1005      14.104  42.251  82.864  1.00 60.11           C  
HETATM 5564  C8' BOG A1005      14.667  40.939  82.870  1.00 54.52           C  
HETATM 5565  C1  RET A1000      19.347  44.696  60.681  1.00 54.64           C  
HETATM 5566  C2  RET A1000      20.446  44.147  61.635  1.00 56.03           C  
HETATM 5567  C3  RET A1000      19.955  43.239  62.750  1.00 59.21           C  
HETATM 5568  C4  RET A1000      18.792  43.853  63.548  1.00 58.46           C  
HETATM 5569  C5  RET A1000      17.694  44.428  62.652  1.00 58.59           C  
HETATM 5570  C6  RET A1000      17.919  44.812  61.354  1.00 57.36           C  
HETATM 5571  C7  RET A1000      16.815  45.369  60.466  1.00 56.24           C  
HETATM 5572  C8  RET A1000      15.757  44.613  59.937  1.00 54.05           C  
HETATM 5573  C9  RET A1000      14.583  44.987  59.136  1.00 52.16           C  
HETATM 5574  C10 RET A1000      13.789  43.946  58.854  1.00 49.84           C  
HETATM 5575  C11 RET A1000      12.521  43.872  58.161  1.00 47.63           C  
HETATM 5576  C12 RET A1000      11.764  42.761  57.909  1.00 49.35           C  
HETATM 5577  C13 RET A1000      11.958  41.271  58.097  1.00 46.46           C  
HETATM 5578  C14 RET A1000      10.936  40.408  57.813  1.00 41.26           C  
HETATM 5579  C15 RET A1000      11.049  38.951  57.951  1.00 39.18           C  
HETATM 5580  C16 RET A1000      19.793  46.052  60.134  1.00 52.61           C  
HETATM 5581  C17 RET A1000      19.338  43.728  59.453  1.00 51.45           C  
HETATM 5582  C18 RET A1000      16.393  44.487  63.409  1.00 58.95           C  
HETATM 5583  C19 RET A1000      14.340  46.431  58.745  1.00 49.13           C  
HETATM 5584  C20 RET A1000      13.340  40.807  58.608  1.00 45.59           C  
HETATM 5585  C1  PLM A1001      -6.175  45.632  80.492  1.00 70.61           C  
HETATM 5586  O2  PLM A1001      -7.230  45.024  80.624  1.00 68.14           O  
HETATM 5587  C2  PLM A1001      -4.899  44.846  80.179  1.00 70.91           C  
HETATM 5588  C3  PLM A1001      -4.252  45.226  78.840  1.00 70.14           C  
HETATM 5589  C4  PLM A1001      -4.124  44.003  77.939  1.00 69.46           C  
HETATM 5590  C5  PLM A1001      -3.249  44.282  76.750  1.00 68.77           C  
HETATM 5591  C6  PLM A1001      -3.160  43.047  75.887  1.00 67.87           C  
HETATM 5592  C7  PLM A1001      -2.763  43.418  74.475  1.00 67.50           C  
HETATM 5593  C8  PLM A1001      -2.670  42.189  73.556  1.00 67.42           C  
HETATM 5594  C9  PLM A1001      -1.857  42.477  72.292  1.00 67.60           C  
HETATM 5595  CA  PLM A1001      -2.721  42.916  71.132  1.00 67.48           C  
HETATM 5596  CB  PLM A1001      -1.923  43.778  70.175  1.00 66.79           C  
HETATM 5597  CC  PLM A1001      -2.611  43.895  68.829  1.00 65.53           C  
HETATM 5598  CD  PLM A1001      -1.805  44.764  67.885  1.00 62.41           C  
HETATM 5599  CE  PLM A1001      -1.692  44.108  66.530  1.00 63.97           C  
HETATM 5600  CF  PLM A1001      -2.332  44.933  65.427  1.00 63.33           C  
HETATM 5601  CG  PLM A1001      -2.202  44.248  64.071  1.00 63.51           C  
HETATM 5602  C1  PLM A1002       9.428  25.573  80.656  1.00 96.20           C  
HETATM 5603  O2  PLM A1002       9.472  26.747  80.995  1.00 99.42           O  
HETATM 5604  C2  PLM A1002       9.179  25.222  79.185  1.00 96.65           C  
HETATM 5605  C3  PLM A1002       7.889  25.818  78.609  1.00 97.87           C  
HETATM 5606  C4  PLM A1002       7.517  25.122  77.309  1.00 98.86           C  
HETATM 5607  C5  PLM A1002       7.656  26.042  76.137  1.00100.14           C  
HETATM 5608  C6  PLM A1002       7.283  25.315  74.872  1.00101.83           C  
HETATM 5609  C7  PLM A1002       8.500  25.146  73.987  1.00102.82           C  
HETATM 5610  C8  PLM A1002       8.173  24.412  72.683  1.00103.19           C  
HETATM 5611  C9  PLM A1002       9.103  24.842  71.558  1.00105.45           C  
HETATM 5612  CA  PLM A1002       9.720  23.660  70.856  1.00107.75           C  
HETATM 5613  CB  PLM A1002      10.971  24.081  70.118  1.00109.62           C  
HETATM 5614  CC  PLM A1002      11.317  23.108  69.011  1.00110.20           C  
HETATM 5615  CD  PLM A1002      12.571  23.548  68.285  1.00110.37           C  
HETATM 5616  CE  PLM A1002      13.615  22.460  68.334  1.00110.57           C  
HETATM 5617  CF  PLM A1002      14.833  22.875  69.146  1.00110.73           C  
HETATM 5618  CG  PLM A1002      15.888  21.769  69.197  1.00110.50           C  
HETATM 5619  C1  TWT A1003       5.779  31.534  78.600  1.00 57.07           C  
HETATM 5620  C2  TWT A1003       5.676  30.162  77.975  1.00 61.01           C  
HETATM 5621  C3  TWT A1003       5.194  30.333  76.547  1.00 66.45           C  
HETATM 5622  C4  TWT A1003       5.045  28.994  75.815  1.00 70.46           C  
HETATM 5623  C5  TWT A1003       4.563  29.353  74.409  1.00 72.77           C  
HETATM 5624  C6  TWT A1003       3.424  28.466  73.933  1.00 74.61           C  
HETATM 5625  C7  TWT A1003       2.202  29.378  73.712  1.00 78.20           C  
HETATM 5626  C8  TWT A1003       0.969  28.698  74.290  1.00 83.25           C  
HETATM 5627  C9  TWT A1003      -0.162  28.549  73.256  1.00 86.25           C  
HETATM 5628  C10 TWT A1003       0.016  27.145  72.702  1.00 90.55           C  
HETATM 5629  C11 TWT A1003      -0.962  26.075  73.189  1.00 93.93           C  
HETATM 5630  C12 TWT A1003      -0.813  25.071  72.065  1.00 95.96           C  
HETATM 5631  C13 TWT A1003      -1.618  23.778  72.099  1.00 98.64           C  
HETATM 5632  C14 TWT A1003      -1.651  23.527  70.600  1.00101.28           C  
HETATM 5633  C15 TWT A1003      -2.677  22.576  70.013  1.00102.41           C  
HETATM 5634  C16 TWT A1003      -2.220  22.611  68.556  1.00102.41           C  
HETATM 5635  C17 TWT A1003      -2.443  21.388  67.743  1.00102.22           C  
HETATM 5636  C18 TWT A1003      -2.848  21.996  66.399  1.00101.40           C  
HETATM 5637  C19 TWT A1003      -3.154  20.983  65.310  1.00100.81           C  
HETATM 5638  C20 TWT A1003      -3.527  21.820  64.084  1.00102.40           C  
HETATM 5639  C21 TWT A1003      -3.863  20.934  62.897  1.00102.47           C  
HETATM 5640  C22 TWT A1003      -4.223  21.837  61.721  1.00101.87           C  
HETATM 5641  C1  BOG B1005      23.654  37.044 -18.296  1.00113.61           C  
HETATM 5642  O1  BOG B1005      22.989  37.773 -17.362  1.00109.33           O  
HETATM 5643  C2  BOG B1005      22.499  36.435 -19.055  1.00115.57           C  
HETATM 5644  O2  BOG B1005      21.628  35.580 -18.217  1.00115.84           O  
HETATM 5645  C3  BOG B1005      23.214  35.661 -20.070  1.00116.95           C  
HETATM 5646  O3  BOG B1005      22.168  35.106 -20.788  1.00116.73           O  
HETATM 5647  C4  BOG B1005      24.135  36.620 -20.929  1.00117.42           C  
HETATM 5648  O4  BOG B1005      24.824  35.895 -21.898  1.00118.22           O  
HETATM 5649  C5  BOG B1005      25.227  37.206 -20.143  1.00117.78           C  
HETATM 5650  O5  BOG B1005      24.517  37.940 -19.154  1.00115.18           O  
HETATM 5651  C6  BOG B1005      26.136  38.178 -21.004  1.00119.25           C  
HETATM 5652  O6  BOG B1005      27.365  38.569 -20.188  1.00121.32           O  
HETATM 5653  C1' BOG B1005      23.792  37.507 -16.245  1.00103.55           C  
HETATM 5654  C2' BOG B1005      23.327  38.522 -15.318  1.00 98.79           C  
HETATM 5655  C3' BOG B1005      23.400  37.803 -14.012  1.00 92.24           C  
HETATM 5656  C4' BOG B1005      22.256  38.337 -13.355  1.00 86.13           C  
HETATM 5657  C5' BOG B1005      22.304  37.706 -12.013  1.00 81.43           C  
HETATM 5658  C6' BOG B1005      20.915  37.484 -11.751  1.00 76.37           C  
HETATM 5659  C7' BOG B1005      20.971  36.834 -10.433  1.00 71.92           C  
HETATM 5660  C8' BOG B1005      19.864  35.943 -10.531  1.00 68.73           C  
HETATM 5661  S   SO4 B1006      34.725  48.426 -18.065  1.00 96.71           S  
HETATM 5662  O1  SO4 B1006      35.189  49.306 -19.153  1.00 97.64           O  
HETATM 5663  O2  SO4 B1006      34.794  49.149 -16.781  1.00 96.50           O  
HETATM 5664  O3  SO4 B1006      33.323  48.032 -18.314  1.00 96.45           O  
HETATM 5665  O4  SO4 B1006      35.586  47.226 -18.016  1.00 96.15           O  
HETATM 5666  C1  RET B1000      20.436  43.063  11.424  1.00 37.70           C  
HETATM 5667  C2  RET B1000      19.260  43.459  10.486  1.00 38.59           C  
HETATM 5668  C3  RET B1000      18.915  42.442   9.406  1.00 40.61           C  
HETATM 5669  C4  RET B1000      20.142  42.034   8.574  1.00 38.53           C  
HETATM 5670  C5  RET B1000      21.345  41.658   9.439  1.00 38.80           C  
HETATM 5671  C6  RET B1000      21.489  42.104  10.740  1.00 38.05           C  
HETATM 5672  C7  RET B1000      22.671  41.720  11.597  1.00 35.46           C  
HETATM 5673  C8  RET B1000      22.880  40.449  12.117  1.00 36.51           C  
HETATM 5674  C9  RET B1000      24.008  39.880  12.850  1.00 39.08           C  
HETATM 5675  C10 RET B1000      23.836  38.582  13.142  1.00 40.66           C  
HETATM 5676  C11 RET B1000      24.715  37.602  13.766  1.00 40.91           C  
HETATM 5677  C12 RET B1000      24.443  36.287  14.049  1.00 44.47           C  
HETATM 5678  C13 RET B1000      23.199  35.429  14.000  1.00 37.89           C  
HETATM 5679  C14 RET B1000      23.276  34.087  14.250  1.00 38.00           C  
HETATM 5680  C15 RET B1000      22.094  33.213  14.225  1.00 39.65           C  
HETATM 5681  C16 RET B1000      21.127  44.341  11.920  1.00 37.67           C  
HETATM 5682  C17 RET B1000      19.772  42.405  12.690  1.00 36.94           C  
HETATM 5683  C18 RET B1000      22.289  40.767   8.663  1.00 33.70           C  
HETATM 5684  C19 RET B1000      25.245  40.719  13.148  1.00 36.46           C  
HETATM 5685  C20 RET B1000      21.883  36.146  13.665  1.00 37.42           C  
HETATM 5686  C1  PLM B1001      39.206  24.531  -8.326  1.00 61.28           C  
HETATM 5687  O2  PLM B1001      38.489  23.725  -8.892  1.00 53.04           O  
HETATM 5688  C2  PLM B1001      38.779  25.072  -6.961  1.00 66.49           C  
HETATM 5689  C3  PLM B1001      37.509  25.945  -7.019  1.00 72.18           C  
HETATM 5690  C4  PLM B1001      36.362  25.277  -6.263  1.00 74.61           C  
HETATM 5691  C5  PLM B1001      35.558  26.267  -5.472  1.00 73.68           C  
HETATM 5692  C6  PLM B1001      34.449  25.545  -4.747  1.00 73.71           C  
HETATM 5693  C7  PLM B1001      34.375  26.012  -3.306  1.00 74.65           C  
HETATM 5694  C8  PLM B1001      33.264  25.313  -2.510  1.00 74.52           C  
HETATM 5695  C9  PLM B1001      33.745  24.885  -1.119  1.00 74.58           C  
HETATM 5696  CA  PLM B1001      33.214  25.783  -0.025  1.00 73.09           C  
HETATM 5697  CB  PLM B1001      34.299  26.069   0.998  1.00 73.09           C  
HETATM 5698  CC  PLM B1001      33.800  27.001   2.091  1.00 70.57           C  
HETATM 5699  CD  PLM B1001      34.892  27.281   3.102  1.00 68.55           C  
HETATM 5700  CE  PLM B1001      34.310  27.910   4.345  1.00 65.57           C  
HETATM 5701  CF  PLM B1001      35.155  27.630   5.578  1.00 64.57           C  
HETATM 5702  CG  PLM B1001      34.562  28.266   6.836  1.00 62.40           C  
HETATM 5703  C1  PLM B1002      12.583  22.197  -7.802  1.00105.53           C  
HETATM 5704  O2  PLM B1002      13.224  23.150  -8.211  1.00108.44           O  
HETATM 5705  C2  PLM B1002      12.568  21.888  -6.296  1.00105.72           C  
HETATM 5706  C3  PLM B1002      13.768  21.052  -5.824  1.00104.44           C  
HETATM 5707  C4  PLM B1002      13.495  20.437  -4.457  1.00105.62           C  
HETATM 5708  C5  PLM B1002      14.507  20.876  -3.435  1.00106.07           C  
HETATM 5709  C6  PLM B1002      14.190  20.245  -2.099  1.00106.66           C  
HETATM 5710  C7  PLM B1002      13.701  21.295  -1.119  1.00107.99           C  
HETATM 5711  C8  PLM B1002      13.364  20.697   0.254  1.00108.97           C  
HETATM 5712  C9  PLM B1002      12.630  21.702   1.141  1.00109.92           C  
HETATM 5713  CA  PLM B1002      11.383  21.109   1.751  1.00110.98           C  
HETATM 5714  CB  PLM B1002      10.608  22.164   2.509  1.00111.25           C  
HETATM 5715  CC  PLM B1002       9.117  22.014   2.288  1.00111.70           C  
HETATM 5716  CD  PLM B1002       8.357  23.074   3.056  1.00111.14           C  
HETATM 5717  CE  PLM B1002       7.186  23.576   2.247  1.00109.82           C  
HETATM 5718  CF  PLM B1002       6.958  25.067   2.447  1.00109.27           C  
HETATM 5719  CG  PLM B1002       5.771  25.580   1.630  1.00108.76           C  
HETATM 5720  C1  TWT B1003      19.294  23.363  -5.768  1.00 63.79           C  
HETATM 5721  C2  TWT B1003      18.813  23.210  -4.343  1.00 68.65           C  
HETATM 5722  C3  TWT B1003      19.111  21.790  -3.895  1.00 69.99           C  
HETATM 5723  C4  TWT B1003      18.664  21.522  -2.455  1.00 69.50           C  
HETATM 5724  C5  TWT B1003      19.038  20.069  -2.176  1.00 69.46           C  
HETATM 5725  C6  TWT B1003      20.191  19.942  -1.198  1.00 71.33           C  
HETATM 5726  C7  TWT B1003      21.165  18.897  -1.772  1.00 75.60           C  
HETATM 5727  C8  TWT B1003      21.621  17.975  -0.652  1.00 76.82           C  
HETATM 5728  C9  TWT B1003      21.072  16.552  -0.820  1.00 78.83           C  
HETATM 5729  C10 TWT B1003      20.189  16.354   0.393  1.00 80.26           C  
HETATM 5730  C11 TWT B1003      19.297  15.110   0.391  1.00 83.74           C  
HETATM 5731  C12 TWT B1003      19.769  14.470   1.678  1.00 86.54           C  
HETATM 5732  C13 TWT B1003      19.164  13.155   2.142  1.00 87.55           C  
HETATM 5733  C14 TWT B1003      19.393  13.366   3.627  1.00 88.29           C  
HETATM 5734  C15 TWT B1003      19.787  12.203   4.512  1.00 87.47           C  
HETATM 5735  C16 TWT B1003      20.464  13.004   5.617  1.00 88.04           C  
HETATM 5736  C17 TWT B1003      21.673  12.425   6.259  1.00 86.79           C  
HETATM 5737  C18 TWT B1003      22.147  13.635   7.059  1.00 85.68           C  
HETATM 5738  C19 TWT B1003      23.407  13.440   7.882  1.00 83.20           C  
HETATM 5739  C20 TWT B1003      23.612  14.803   8.548  1.00 82.51           C  
HETATM 5740  C21 TWT B1003      24.837  14.828   9.432  1.00 81.48           C  
HETATM 5741  C22 TWT B1003      24.933  16.223  10.040  1.00 79.64           C  
HETATM 5742  O12 PC1 B1004      18.219  56.853  27.941  1.00120.93           O  
HETATM 5743  P   PC1 B1004      17.463  56.401  26.616  1.00120.29           P  
HETATM 5744  O14 PC1 B1004      16.171  57.255  26.335  1.00120.40           O  
HETATM 5745  O13 PC1 B1004      17.171  54.907  26.788  1.00119.29           O  
HETATM 5746  C11 PC1 B1004      16.331  54.594  27.931  1.00118.16           C  
HETATM 5747  C12 PC1 B1004      16.107  53.068  28.011  1.00116.08           C  
HETATM 5748  O11 PC1 B1004      18.365  56.450  25.340  1.00115.46           O  
HETATM 5749  C1  PC1 B1004      19.717  56.885  25.569  1.00105.29           C  
HETATM 5750  C2  PC1 B1004      20.222  57.896  24.517  1.00 97.36           C  
HETATM 5751  O21 PC1 B1004      20.126  57.266  23.161  1.00 94.84           O  
HETATM 5752  C21 PC1 B1004      18.929  57.525  22.216  1.00 90.36           C  
HETATM 5753  O22 PC1 B1004      17.944  58.266  22.483  1.00 87.69           O  
HETATM 5754  C22 PC1 B1004      18.923  56.860  20.898  1.00 85.69           C  
HETATM 5755  C23 PC1 B1004      20.104  57.309  19.979  1.00 79.39           C  
HETATM 5756  C24 PC1 B1004      19.725  58.452  19.037  1.00 74.29           C  
HETATM 5757  C25 PC1 B1004      19.496  57.994  17.564  1.00 70.03           C  
HETATM 5758  C26 PC1 B1004      20.674  58.273  16.664  1.00 65.69           C  
HETATM 5759  C27 PC1 B1004      20.352  57.795  15.203  1.00 62.33           C  
HETATM 5760  C28 PC1 B1004      21.478  58.050  14.306  1.00 61.51           C  
HETATM 5761  C29 PC1 B1004      20.964  58.736  13.115  1.00 61.18           C  
HETATM 5762  C2A PC1 B1004      22.084  59.041  12.130  1.00 59.54           C  
HETATM 5763  C2B PC1 B1004      21.556  59.726  10.928  1.00 58.86           C  
HETATM 5764  C2C PC1 B1004      22.664  60.054   9.897  1.00 60.62           C  
HETATM 5765  C2D PC1 B1004      22.113  60.762   8.660  1.00 58.80           C  
HETATM 5766  C2E PC1 B1004      22.774  60.178   7.383  1.00 60.77           C  
HETATM 5767  C2F PC1 B1004      23.669  61.196   6.679  1.00 59.34           C  
HETATM 5768  C3  PC1 B1004      21.658  58.309  24.840  1.00 91.41           C  
HETATM 5769  O31 PC1 B1004      22.505  57.112  24.717  1.00 82.45           O  
HETATM 5770  C31 PC1 B1004      23.904  57.416  24.445  1.00 74.20           C  
HETATM 5771  O32 PC1 B1004      24.574  58.113  25.204  1.00 73.09           O  
HETATM 5772  C32 PC1 B1004      24.492  56.811  23.187  1.00 67.47           C  
HETATM 5773  C33 PC1 B1004      23.554  56.584  21.993  1.00 61.87           C  
HETATM 5774  C34 PC1 B1004      24.305  55.989  20.891  1.00 55.21           C  
HETATM 5775  C35 PC1 B1004      24.128  56.822  19.637  1.00 48.89           C  
HETATM 5776  C36 PC1 B1004      24.858  56.231  18.580  1.00 47.78           C  
HETATM 5777  C37 PC1 B1004      24.654  57.108  17.320  1.00 45.15           C  
HETATM 5778  C38 PC1 B1004      24.942  56.353  16.105  1.00 46.13           C  
HETATM 5779  C39 PC1 B1004      25.246  57.283  14.933  1.00 42.46           C  
HETATM 5780  C3A PC1 B1004      25.540  56.486  13.700  1.00 48.81           C  
HETATM 5781  O   HOH A 500       9.925  34.520  51.325  1.00 49.90           O  
HETATM 5782  O   HOH A 501      12.766  39.934  66.632  1.00 35.71           O  
HETATM 5783  O   HOH A 502      11.812  38.093  65.161  1.00 37.47           O  
HETATM 5784  O   HOH A 503      13.672  39.242  69.171  1.00 35.37           O  
HETATM 5785  O   HOH A 504      13.395  40.195  71.546  1.00 47.39           O  
HETATM 5786  O   HOH A 505      10.419  41.843  67.407  1.00 51.52           O  
HETATM 5787  O   HOH A 506      11.707  37.433  72.210  1.00 66.15           O  
HETATM 5788  O   HOH A 507       9.131  40.556  77.059  1.00 52.23           O  
HETATM 5789  O   HOH A 508       8.928  39.892  74.517  1.00 50.13           O  
HETATM 5790  O   HOH A 509       8.133  34.939  65.340  1.00 41.91           O  
HETATM 5791  O   HOH A 510      19.892  35.397  61.207  1.00 41.46           O  
HETATM 5792  O   HOH A 511       1.464  34.605  62.978  1.00 38.32           O  
HETATM 5793  O   HOH A 512       0.668  37.599  59.063  1.00 31.17           O  
HETATM 5794  O   HOH A 513       7.098  34.643  43.076  1.00 40.79           O  
HETATM 5795  O   HOH A 514       7.648  32.461  45.021  1.00 51.13           O  
HETATM 5796  O   HOH A 515      14.378  54.807  58.115  1.00 61.18           O  
HETATM 5797  O   HOH A 516      23.896  43.987  45.396  1.00 51.82           O  
HETATM 5798  O   HOH A 517      16.410  42.829  49.829  1.00 42.02           O  
HETATM 5799  O   HOH A 518      15.684  50.605  47.198  1.00 42.73           O  
HETATM 5800  O   HOH A 519       0.119  40.230  45.734  1.00 37.45           O  
HETATM 5801  O   HOH A 520      11.084  48.606  88.957  1.00 57.71           O  
HETATM 5802  O   HOH A 521      11.316  37.580  90.212  1.00 64.09           O  
HETATM 5803  O   HOH A 522      11.218  41.044  86.264  1.00 43.12           O  
HETATM 5804  O   HOH A 523      11.768  29.653  44.968  1.00 52.71           O  
HETATM 5805  O   HOH A 524      -4.717  27.140  81.230  1.00 50.74           O  
HETATM 5806  O   HOH A 525       7.620  40.352  40.128  1.00 41.26           O  
HETATM 5807  O   HOH A 526       8.826  43.149  90.343  1.00 91.12           O  
HETATM 5808  O   HOH A 527      17.780  49.629  94.931  1.00 78.66           O  
HETATM 5809  O   HOH B 500      19.682  29.433  21.206  1.00 42.96           O  
HETATM 5810  O   HOH B 501      21.639  35.317   5.325  1.00 35.95           O  
HETATM 5811  O   HOH B 502      20.726  33.205   6.779  1.00 30.57           O  
HETATM 5812  O   HOH B 503      20.150  35.198   3.223  1.00 37.58           O  
HETATM 5813  O   HOH B 504      20.872  34.938   0.607  1.00 53.06           O  
HETATM 5814  O   HOH B 505      24.016  34.728   4.366  1.00 45.86           O  
HETATM 5815  O   HOH B 506      20.016  31.681  -0.068  1.00 44.06           O  
HETATM 5816  O   HOH B 507      23.919  32.649  -5.036  1.00 41.46           O  
HETATM 5817  O   HOH B 508      23.060  31.893  -2.321  1.00 43.75           O  
HETATM 5818  O   HOH B 509      20.971  28.257   6.766  1.00 41.99           O  
HETATM 5819  O   HOH B 510      13.789  31.970   6.046  1.00 36.38           O  
HETATM 5820  O   HOH B 511      12.967  37.006  11.064  1.00 39.57           O  
HETATM 5821  O   HOH B 512      25.720  23.125   9.314  1.00 36.67           O  
HETATM 5822  O   HOH B 513      28.099  24.678  13.008  1.00 39.39           O  
HETATM 5823  O   HOH B 514      26.359  45.011   3.953  1.00 38.60           O  
HETATM 5824  O   HOH B 515      24.290  28.006  26.681  1.00 46.79           O  
HETATM 5825  O   HOH B 516      19.733  26.366  27.013  1.00 42.38           O  
HETATM 5826  O   HOH B 517      31.039  46.229  13.806  1.00 32.83           O  
HETATM 5827  O   HOH B 518      17.035  46.057  26.435  1.00 33.13           O  
HETATM 5828  O   HOH B 519      22.564  40.054  25.729  1.00 38.95           O  
HETATM 5829  O   HOH B 520      26.428  44.126  20.480  1.00 34.25           O  
HETATM 5830  O   HOH B 521      27.387  44.479  24.909  1.00 30.25           O  
HETATM 5831  O   HOH B 522      30.821  26.383  26.550  1.00 38.62           O  
HETATM 5832  O   HOH B 523      18.510  34.447 -18.922  1.00 61.90           O  
HETATM 5833  O   HOH B 524      20.890  32.519 -17.638  1.00 64.29           O  
HETATM 5834  O   HOH B 525      22.723  34.699 -14.429  1.00 48.08           O  
HETATM 5835  O   HOH B 526      21.329  39.908  21.856  1.00 43.11           O  
HETATM 5836  O   HOH B 527      24.569  32.946 -17.618  1.00 76.26           O  
HETATM 5837  O   HOH B 528      24.060  41.888 -17.468  1.00 83.93           O  
CONECT  800 1419                                                                
CONECT 1419  800                                                                
CONECT 2360 5579                                                                
CONECT 2614 5602                                                                
CONECT 3581 4200                                                                
CONECT 4200 3581                                                                
CONECT 5141 5680                                                                
CONECT 5395 5703                                                                
CONECT 5545 5546 5547 5554                                                      
CONECT 5546 5545 5557                                                           
CONECT 5547 5545 5548 5549                                                      
CONECT 5548 5547                                                                
CONECT 5549 5547 5550 5551                                                      
CONECT 5550 5549                                                                
CONECT 5551 5549 5552 5553                                                      
CONECT 5552 5551                                                                
CONECT 5553 5551 5554 5555                                                      
CONECT 5554 5545 5553                                                           
CONECT 5555 5553 5556                                                           
CONECT 5556 5555                                                                
CONECT 5557 5546 5558                                                           
CONECT 5558 5557 5559                                                           
CONECT 5559 5558 5560                                                           
CONECT 5560 5559 5561                                                           
CONECT 5561 5560 5562                                                           
CONECT 5562 5561 5563                                                           
CONECT 5563 5562 5564                                                           
CONECT 5564 5563                                                                
CONECT 5565 5566 5570 5580 5581                                                 
CONECT 5566 5565 5567                                                           
CONECT 5567 5566 5568                                                           
CONECT 5568 5567 5569                                                           
CONECT 5569 5568 5570 5582                                                      
CONECT 5570 5565 5569 5571                                                      
CONECT 5571 5570 5572                                                           
CONECT 5572 5571 5573                                                           
CONECT 5573 5572 5574 5583                                                      
CONECT 5574 5573 5575                                                           
CONECT 5575 5574 5576                                                           
CONECT 5576 5575 5577                                                           
CONECT 5577 5576 5578 5584                                                      
CONECT 5578 5577 5579                                                           
CONECT 5579 2360 5578                                                           
CONECT 5580 5565                                                                
CONECT 5581 5565                                                                
CONECT 5582 5569                                                                
CONECT 5583 5573                                                                
CONECT 5584 5577                                                                
CONECT 5585 5586 5587                                                           
CONECT 5586 5585                                                                
CONECT 5587 5585 5588                                                           
CONECT 5588 5587 5589                                                           
CONECT 5589 5588 5590                                                           
CONECT 5590 5589 5591                                                           
CONECT 5591 5590 5592                                                           
CONECT 5592 5591 5593                                                           
CONECT 5593 5592 5594                                                           
CONECT 5594 5593 5595                                                           
CONECT 5595 5594 5596                                                           
CONECT 5596 5595 5597                                                           
CONECT 5597 5596 5598                                                           
CONECT 5598 5597 5599                                                           
CONECT 5599 5598 5600                                                           
CONECT 5600 5599 5601                                                           
CONECT 5601 5600                                                                
CONECT 5602 2614 5603 5604                                                      
CONECT 5603 5602                                                                
CONECT 5604 5602 5605                                                           
CONECT 5605 5604 5606                                                           
CONECT 5606 5605 5607                                                           
CONECT 5607 5606 5608                                                           
CONECT 5608 5607 5609                                                           
CONECT 5609 5608 5610                                                           
CONECT 5610 5609 5611                                                           
CONECT 5611 5610 5612                                                           
CONECT 5612 5611 5613                                                           
CONECT 5613 5612 5614                                                           
CONECT 5614 5613 5615                                                           
CONECT 5615 5614 5616                                                           
CONECT 5616 5615 5617                                                           
CONECT 5617 5616 5618                                                           
CONECT 5618 5617                                                                
CONECT 5619 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 5633                                                           
CONECT 5633 5632 5634                                                           
CONECT 5634 5633 5635                                                           
CONECT 5635 5634 5636                                                           
CONECT 5636 5635 5637                                                           
CONECT 5637 5636 5638                                                           
CONECT 5638 5637 5639                                                           
CONECT 5639 5638 5640                                                           
CONECT 5640 5639                                                                
CONECT 5641 5642 5643 5650                                                      
CONECT 5642 5641 5653                                                           
CONECT 5643 5641 5644 5645                                                      
CONECT 5644 5643                                                                
CONECT 5645 5643 5646 5647                                                      
CONECT 5646 5645                                                                
CONECT 5647 5645 5648 5649                                                      
CONECT 5648 5647                                                                
CONECT 5649 5647 5650 5651                                                      
CONECT 5650 5641 5649                                                           
CONECT 5651 5649 5652                                                           
CONECT 5652 5651                                                                
CONECT 5653 5642 5654                                                           
CONECT 5654 5653 5655                                                           
CONECT 5655 5654 5656                                                           
CONECT 5656 5655 5657                                                           
CONECT 5657 5656 5658                                                           
CONECT 5658 5657 5659                                                           
CONECT 5659 5658 5660                                                           
CONECT 5660 5659                                                                
CONECT 5661 5662 5663 5664 5665                                                 
CONECT 5662 5661                                                                
CONECT 5663 5661                                                                
CONECT 5664 5661                                                                
CONECT 5665 5661                                                                
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                                                                
CONECT 5686 5687 5688                                                           
CONECT 5687 5686                                                                
CONECT 5688 5686 5689                                                           
CONECT 5689 5688 5690                                                           
CONECT 5690 5689 5691                                                           
CONECT 5691 5690 5692                                                           
CONECT 5692 5691 5693                                                           
CONECT 5693 5692 5694                                                           
CONECT 5694 5693 5695                                                           
CONECT 5695 5694 5696                                                           
CONECT 5696 5695 5697                                                           
CONECT 5697 5696 5698                                                           
CONECT 5698 5697 5699                                                           
CONECT 5699 5698 5700                                                           
CONECT 5700 5699 5701                                                           
CONECT 5701 5700 5702                                                           
CONECT 5702 5701                                                                
CONECT 5703 5395 5704 5705                                                      
CONECT 5704 5703                                                                
CONECT 5705 5703 5706                                                           
CONECT 5706 5705 5707                                                           
CONECT 5707 5706 5708                                                           
CONECT 5708 5707 5709                                                           
CONECT 5709 5708 5710                                                           
CONECT 5710 5709 5711                                                           
CONECT 5711 5710 5712                                                           
CONECT 5712 5711 5713                                                           
CONECT 5713 5712 5714                                                           
CONECT 5714 5713 5715                                                           
CONECT 5715 5714 5716                                                           
CONECT 5716 5715 5717                                                           
CONECT 5717 5716 5718                                                           
CONECT 5718 5717 5719                                                           
CONECT 5719 5718                                                                
CONECT 5720 5721                                                                
CONECT 5721 5720 5722                                                           
CONECT 5722 5721 5723                                                           
CONECT 5723 5722 5724                                                           
CONECT 5724 5723 5725                                                           
CONECT 5725 5724 5726                                                           
CONECT 5726 5725 5727                                                           
CONECT 5727 5726 5728                                                           
CONECT 5728 5727 5729                                                           
CONECT 5729 5728 5730                                                           
CONECT 5730 5729 5731                                                           
CONECT 5731 5730 5732                                                           
CONECT 5732 5731 5733                                                           
CONECT 5733 5732 5734                                                           
CONECT 5734 5733 5735                                                           
CONECT 5735 5734 5736                                                           
CONECT 5736 5735 5737                                                           
CONECT 5737 5736 5738                                                           
CONECT 5738 5737 5739                                                           
CONECT 5739 5738 5740                                                           
CONECT 5740 5739 5741                                                           
CONECT 5741 5740                                                                
CONECT 5742 5743                                                                
CONECT 5743 5742 5744 5745 5748                                                 
CONECT 5744 5743                                                                
CONECT 5745 5743 5746                                                           
CONECT 5746 5745 5747                                                           
CONECT 5747 5746                                                                
CONECT 5748 5743 5749                                                           
CONECT 5749 5748 5750                                                           
CONECT 5750 5749 5751 5768                                                      
CONECT 5751 5750 5752                                                           
CONECT 5752 5751 5753 5754                                                      
CONECT 5753 5752                                                                
CONECT 5754 5752 5755                                                           
CONECT 5755 5754 5756                                                           
CONECT 5756 5755 5757                                                           
CONECT 5757 5756 5758                                                           
CONECT 5758 5757 5759                                                           
CONECT 5759 5758 5760                                                           
CONECT 5760 5759 5761                                                           
CONECT 5761 5760 5762                                                           
CONECT 5762 5761 5763                                                           
CONECT 5763 5762 5764                                                           
CONECT 5764 5763 5765                                                           
CONECT 5765 5764 5766                                                           
CONECT 5766 5765 5767                                                           
CONECT 5767 5766                                                                
CONECT 5768 5750 5769                                                           
CONECT 5769 5768 5770                                                           
CONECT 5770 5769 5771 5772                                                      
CONECT 5771 5770                                                                
CONECT 5772 5770 5773                                                           
CONECT 5773 5772 5774                                                           
CONECT 5774 5773 5775                                                           
CONECT 5775 5774 5776                                                           
CONECT 5776 5775 5777                                                           
CONECT 5777 5776 5778                                                           
CONECT 5778 5777 5779                                                           
CONECT 5779 5778 5780                                                           
CONECT 5780 5779                                                                
MASTER      500    0   12   38    4    0    0    6 5835    2  244   70          
END