HEADER    MEMBRANE PROTEIN                        12-DEC-19   6TP6              
TITLE     CRYSTAL STRUCTURE OF THE OREXIN-1 RECEPTOR IN COMPLEX WITH FILOREXANT 
CAVEAT     6TP6    PGW A 411 HAS WRONG CHIRALITY AT ATOM C05                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OREXIN RECEPTOR TYPE 1;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: OX1R,HYPOCRETIN RECEPTOR TYPE 1;                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: FILOREXANT BOUND IN THE ORTHOSTERIC SITE              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HCRTR1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    7TM, GPCR, MEMBRANE PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.RAPPAS,A.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,M.CONGREVE,         
AUTHOR   2 R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,A.JAZAYERI,          
AUTHOR   3 F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,B.G.TEHAN,M.WEIR,           
AUTHOR   4 J.A.CHRISTOPHER                                                      
REVDAT   4   29-JUL-20 6TP6    1       COMPND REMARK HETNAM SITE                
REVDAT   3   11-MAR-20 6TP6    1       JRNL                                     
REVDAT   2   29-JAN-20 6TP6    1       JRNL                                     
REVDAT   1   01-JAN-20 6TP6    0                                                
JRNL        AUTH   M.RAPPAS,A.A.E.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,       
JRNL        AUTH 2 M.CONGREVE,R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,  
JRNL        AUTH 3 A.JAZAYERI,F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,         
JRNL        AUTH 4 B.G.TEHAN,M.WEIR,J.A.CHRISTOPHER                             
JRNL        TITL   COMPARISON OF OREXIN 1 AND OREXIN 2 LIGAND BINDING MODES     
JRNL        TITL 2 USING X-RAY CRYSTALLOGRAPHY AND COMPUTATIONAL ANALYSIS.      
JRNL        REF    J.MED.CHEM.                   V.  63  1528 2020              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   31860301                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.9B01787                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 60.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 29373                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1464                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 34.9950 -  5.0321    0.95     4447   245  0.2291 0.2487        
REMARK   3     2  5.0321 -  3.9960    0.97     4528   225  0.1767 0.2030        
REMARK   3     3  3.9960 -  3.4914    0.96     4484   236  0.1978 0.2414        
REMARK   3     4  3.4914 -  3.1724    0.92     4251   248  0.2161 0.2544        
REMARK   3     5  3.1724 -  2.9451    0.79     3665   194  0.2349 0.2810        
REMARK   3     6  2.9451 -  2.7716    0.64     2986   125  0.2473 0.3118        
REMARK   3     7  2.7716 -  2.6328    0.43     1997   108  0.2853 0.3123        
REMARK   3     8  2.6328 -  2.5182    0.24     1094    55  0.3009 0.3405        
REMARK   3     9  2.5182 -  2.4213    0.08      374    21  0.2880 0.4301        
REMARK   3    10  2.4213 -  2.3380    0.02       83     7  0.2827 0.3609        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 25:376)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0351  -5.4999 100.5171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0104 T22:   0.3245                                     
REMARK   3      T33:   0.8255 T12:  -0.0002                                     
REMARK   3      T13:  -0.0600 T23:  -0.0659                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4572 L22:   5.6457                                     
REMARK   3      L33:   4.5142 L12:  -0.5372                                     
REMARK   3      L13:  -1.1388 L23:   2.6320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0877 S12:  -0.2893 S13:   0.1751                       
REMARK   3      S21:   0.1630 S22:   0.4832 S23:  -1.1237                       
REMARK   3      S31:  -0.1806 S32:   0.7481 S33:  -0.1702                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 43:377)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3102 -27.6120  75.7130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5092 T22:   0.1658                                     
REMARK   3      T33:   0.3306 T12:   0.0704                                     
REMARK   3      T13:   0.1617 T23:   0.0837                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7219 L22:   4.9738                                     
REMARK   3      L33:   2.5155 L12:  -0.5837                                     
REMARK   3      L13:  -0.4339 L23:   1.1699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1059 S12:   0.3354 S13:   0.0370                       
REMARK   3      S21:  -1.0582 S22:   0.0854 S23:  -0.3102                       
REMARK   3      S31:   0.0737 S32:  -0.0650 S33:  -0.0883                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND RESID 43 THROUGH 376)          
REMARK   3     SELECTION          : (CHAIN B AND (RESID 43 THROUGH 189 OR       
REMARK   3                          RESID 198 THROUGH 243 OR RESID 251          
REMARK   3                          THROUGH 376))                               
REMARK   3     ATOM PAIRS NUMBER  : 2638                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6TP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292105829.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JAN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 3.0-6.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96861                            
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : STARANISO                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29373                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.338                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.992                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 60.0                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 2.0                                
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6TO7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE 50MM SODIUM       
REMARK 280  CHLORIDE 50MM LITHIUM SULPHATE 15-34% PEG400, PH 4.3, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 284K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       73.10100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     ALA A   193                                                      
REMARK 465     ALA A   194                                                      
REMARK 465     ARG A   195                                                      
REMARK 465     THR A   196                                                      
REMARK 465     ARG A   197                                                      
REMARK 465     GLY A   244                                                      
REMARK 465     ARG A   245                                                      
REMARK 465     GLN A   246                                                      
REMARK 465     ILE A   247                                                      
REMARK 465     PRO A   248                                                      
REMARK 465     GLY A   249                                                      
REMARK 465     THR A   250                                                      
REMARK 465     ALA A   253                                                      
REMARK 465     LEU A   254                                                      
REMARK 465     VAL A   255                                                      
REMARK 465     ARG A   256                                                      
REMARK 465     ASN A   257                                                      
REMARK 465     TRP A   258                                                      
REMARK 465     LYS A   259                                                      
REMARK 465     ARG A   260                                                      
REMARK 465     PRO A   261                                                      
REMARK 465     SER A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     GLN A   264                                                      
REMARK 465     LEU A   265                                                      
REMARK 465     GLY A   266                                                      
REMARK 465     ASP A   267                                                      
REMARK 465     LEU A   268                                                      
REMARK 465     GLU A   269                                                      
REMARK 465     GLN A   270                                                      
REMARK 465     GLY A   271                                                      
REMARK 465     LEU A   272                                                      
REMARK 465     SER A   273                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     GLU A   275                                                      
REMARK 465     PRO A   276                                                      
REMARK 465     GLN A   277                                                      
REMARK 465     PRO A   278                                                      
REMARK 465     ARG A   279                                                      
REMARK 465     ALA A   280                                                      
REMARK 465     ARG A   281                                                      
REMARK 465     ALA A   282                                                      
REMARK 465     PHE A   283                                                      
REMARK 465     LEU A   284                                                      
REMARK 465     LEU A   377                                                      
REMARK 465     PRO A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     ALA A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     HIS A   384                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     HIS A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     HIS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     HIS A   391                                                      
REMARK 465     HIS A   392                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     ALA B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     GLU B    28                                                      
REMARK 465     ASP B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     PHE B    31                                                      
REMARK 465     LEU B    32                                                      
REMARK 465     ARG B    33                                                      
REMARK 465     TYR B    34                                                      
REMARK 465     LEU B    35                                                      
REMARK 465     TRP B    36                                                      
REMARK 465     ARG B    37                                                      
REMARK 465     ASP B    38                                                      
REMARK 465     TYR B    39                                                      
REMARK 465     LEU B    40                                                      
REMARK 465     TYR B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     ALA B   253                                                      
REMARK 465     LEU B   254                                                      
REMARK 465     VAL B   255                                                      
REMARK 465     ARG B   256                                                      
REMARK 465     ASN B   257                                                      
REMARK 465     TRP B   258                                                      
REMARK 465     LYS B   259                                                      
REMARK 465     ARG B   260                                                      
REMARK 465     PRO B   261                                                      
REMARK 465     SER B   262                                                      
REMARK 465     ASP B   263                                                      
REMARK 465     GLN B   264                                                      
REMARK 465     LEU B   265                                                      
REMARK 465     GLY B   266                                                      
REMARK 465     ASP B   267                                                      
REMARK 465     LEU B   268                                                      
REMARK 465     GLU B   269                                                      
REMARK 465     GLN B   270                                                      
REMARK 465     GLY B   271                                                      
REMARK 465     LEU B   272                                                      
REMARK 465     SER B   273                                                      
REMARK 465     GLY B   274                                                      
REMARK 465     GLU B   275                                                      
REMARK 465     PRO B   276                                                      
REMARK 465     GLN B   277                                                      
REMARK 465     PRO B   278                                                      
REMARK 465     ARG B   279                                                      
REMARK 465     ALA B   280                                                      
REMARK 465     ARG B   281                                                      
REMARK 465     ALA B   282                                                      
REMARK 465     PHE B   283                                                      
REMARK 465     LEU B   284                                                      
REMARK 465     PRO B   378                                                      
REMARK 465     GLY B   379                                                      
REMARK 465     LEU B   380                                                      
REMARK 465     ALA B   381                                                      
REMARK 465     ALA B   382                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     HIS B   384                                                      
REMARK 465     HIS B   385                                                      
REMARK 465     HIS B   386                                                      
REMARK 465     HIS B   387                                                      
REMARK 465     HIS B   388                                                      
REMARK 465     HIS B   389                                                      
REMARK 465     HIS B   390                                                      
REMARK 465     HIS B   391                                                      
REMARK 465     HIS B   392                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  39      -56.65   -135.89                                   
REMARK 500    TYR A 224      -74.05   -129.02                                   
REMARK 500    TYR B 224      -73.79   -129.45                                   
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     SOG A  407                                                       
REMARK 610     SOG A  409                                                       
REMARK 610     PG4 B  402                                                       
REMARK 610     SOG B  408                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6TO7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TOD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TOS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TOT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TP3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TP4   RELATED DB: PDB                                   
DBREF  6TP6 A   28   380  UNP    O43613   OX1R_HUMAN      28    380             
DBREF  6TP6 B   28   380  UNP    O43613   OX1R_HUMAN      28    380             
SEQADV 6TP6 ALA A   25  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 ALA A   26  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 SER A   27  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 ALA A   46  UNP  O43613    GLU    46 ENGINEERED MUTATION            
SEQADV 6TP6 LEU A   85  UNP  O43613    ILE    85 ENGINEERED MUTATION            
SEQADV 6TP6 ALA A   95  UNP  O43613    VAL    95 ENGINEERED MUTATION            
SEQADV 6TP6 LEU A  162  UNP  O43613    ARG   162 ENGINEERED MUTATION            
SEQADV 6TP6 ALA A  194  UNP  O43613    ASN   194 ENGINEERED MUTATION            
SEQADV 6TP6 ALA A  198  UNP  O43613    LEU   198 ENGINEERED MUTATION            
SEQADV 6TP6 ALA A  211  UNP  O43613    TYR   211 ENGINEERED MUTATION            
SEQADV 6TP6 VAL A  304  UNP  O43613    LEU   304 ENGINEERED MUTATION            
SEQADV 6TP6 ALA A  339  UNP  O43613    CYS   339 ENGINEERED MUTATION            
SEQADV 6TP6 TRP A  375  UNP  O43613    CYS   375 ENGINEERED MUTATION            
SEQADV 6TP6 TRP A  376  UNP  O43613    CYS   376 ENGINEERED MUTATION            
SEQADV 6TP6 ALA A  381  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 ALA A  382  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 ALA A  383  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS A  384  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS A  385  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS A  386  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS A  387  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS A  388  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS A  389  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS A  390  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS A  391  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS A  392  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 ALA B   25  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 ALA B   26  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 SER B   27  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 ALA B   46  UNP  O43613    GLU    46 ENGINEERED MUTATION            
SEQADV 6TP6 LEU B   85  UNP  O43613    ILE    85 ENGINEERED MUTATION            
SEQADV 6TP6 ALA B   95  UNP  O43613    VAL    95 ENGINEERED MUTATION            
SEQADV 6TP6 LEU B  162  UNP  O43613    ARG   162 ENGINEERED MUTATION            
SEQADV 6TP6 ALA B  194  UNP  O43613    ASN   194 ENGINEERED MUTATION            
SEQADV 6TP6 ALA B  198  UNP  O43613    LEU   198 ENGINEERED MUTATION            
SEQADV 6TP6 ALA B  211  UNP  O43613    TYR   211 ENGINEERED MUTATION            
SEQADV 6TP6 VAL B  304  UNP  O43613    LEU   304 ENGINEERED MUTATION            
SEQADV 6TP6 ALA B  339  UNP  O43613    CYS   339 ENGINEERED MUTATION            
SEQADV 6TP6 TRP B  375  UNP  O43613    CYS   375 ENGINEERED MUTATION            
SEQADV 6TP6 TRP B  376  UNP  O43613    CYS   376 ENGINEERED MUTATION            
SEQADV 6TP6 ALA B  381  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 ALA B  382  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 ALA B  383  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS B  384  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS B  385  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS B  386  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS B  387  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS B  388  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS B  389  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS B  390  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS B  391  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TP6 HIS B  392  UNP  O43613              EXPRESSION TAG                 
SEQRES   1 A  368  ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG          
SEQRES   2 A  368  ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE          
SEQRES   3 A  368  ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY          
SEQRES   4 A  368  ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS          
SEQRES   5 A  368  MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER          
SEQRES   6 A  368  LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA          
SEQRES   7 A  368  SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY          
SEQRES   8 A  368  HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL          
SEQRES   9 A  368  SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA          
SEQRES  10 A  368  LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE          
SEQRES  11 A  368  LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY          
SEQRES  12 A  368  ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA          
SEQRES  13 A  368  ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA          
SEQRES  14 A  368  ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP          
SEQRES  15 A  368  ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE          
SEQRES  16 A  368  PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA          
SEQRES  17 A  368  MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG          
SEQRES  18 A  368  GLN ILE PRO GLY THR THR SER ALA LEU VAL ARG ASN TRP          
SEQRES  19 A  368  LYS ARG PRO SER ASP GLN LEU GLY ASP LEU GLU GLN GLY          
SEQRES  20 A  368  LEU SER GLY GLU PRO GLN PRO ARG ALA ARG ALA PHE LEU          
SEQRES  21 A  368  ALA GLU VAL LYS GLN MET ARG ALA ARG ARG LYS THR ALA          
SEQRES  22 A  368  LYS MET LEU MET VAL VAL VAL LEU VAL PHE ALA LEU CYS          
SEQRES  23 A  368  TYR LEU PRO ILE SER VAL LEU ASN VAL LEU LYS ARG VAL          
SEQRES  24 A  368  PHE GLY MET PHE ARG GLN ALA SER ASP ARG GLU ALA VAL          
SEQRES  25 A  368  TYR ALA ALA PHE THR PHE SER HIS TRP LEU VAL TYR ALA          
SEQRES  26 A  368  ASN SER ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER          
SEQRES  27 A  368  GLY LYS PHE ARG GLU GLN PHE LYS ALA ALA PHE SER TRP          
SEQRES  28 A  368  TRP LEU PRO GLY LEU ALA ALA ALA HIS HIS HIS HIS HIS          
SEQRES  29 A  368  HIS HIS HIS HIS                                              
SEQRES   1 B  368  ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG          
SEQRES   2 B  368  ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE          
SEQRES   3 B  368  ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY          
SEQRES   4 B  368  ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS          
SEQRES   5 B  368  MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER          
SEQRES   6 B  368  LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA          
SEQRES   7 B  368  SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY          
SEQRES   8 B  368  HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL          
SEQRES   9 B  368  SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA          
SEQRES  10 B  368  LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE          
SEQRES  11 B  368  LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY          
SEQRES  12 B  368  ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA          
SEQRES  13 B  368  ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA          
SEQRES  14 B  368  ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP          
SEQRES  15 B  368  ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE          
SEQRES  16 B  368  PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA          
SEQRES  17 B  368  MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG          
SEQRES  18 B  368  GLN ILE PRO GLY THR THR SER ALA LEU VAL ARG ASN TRP          
SEQRES  19 B  368  LYS ARG PRO SER ASP GLN LEU GLY ASP LEU GLU GLN GLY          
SEQRES  20 B  368  LEU SER GLY GLU PRO GLN PRO ARG ALA ARG ALA PHE LEU          
SEQRES  21 B  368  ALA GLU VAL LYS GLN MET ARG ALA ARG ARG LYS THR ALA          
SEQRES  22 B  368  LYS MET LEU MET VAL VAL VAL LEU VAL PHE ALA LEU CYS          
SEQRES  23 B  368  TYR LEU PRO ILE SER VAL LEU ASN VAL LEU LYS ARG VAL          
SEQRES  24 B  368  PHE GLY MET PHE ARG GLN ALA SER ASP ARG GLU ALA VAL          
SEQRES  25 B  368  TYR ALA ALA PHE THR PHE SER HIS TRP LEU VAL TYR ALA          
SEQRES  26 B  368  ASN SER ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER          
SEQRES  27 B  368  GLY LYS PHE ARG GLU GLN PHE LYS ALA ALA PHE SER TRP          
SEQRES  28 B  368  TRP LEU PRO GLY LEU ALA ALA ALA HIS HIS HIS HIS HIS          
SEQRES  29 B  368  HIS HIS HIS HIS                                              
HET    NT5  A 401      56                                                       
HET    PG4  A 402      13                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SOG  A 405      20                                                       
HET    SOG  A 406      20                                                       
HET    SOG  A 407      13                                                       
HET    SOG  A 408      20                                                       
HET    SOG  A 409       4                                                       
HET     CL  A 410       1                                                       
HET    PGW  A 411      51                                                       
HET    NT5  B 401      56                                                       
HET    PG4  B 402       9                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HET    SOG  B 405      20                                                       
HET    SOG  B 406      20                                                       
HET    SOG  B 407      20                                                       
HET    SOG  B 408       6                                                       
HET    PGW  B 409      51                                                       
HETNAM     NT5 [(2~{R},5~{R})-5-[(5-FLUORANYLPYRIDIN-2-YL)OXYMETHYL]-           
HETNAM   2 NT5  2-METHYL-PIPERIDIN-1-YL]-(5-METHYL-2-PYRIMIDIN-2-YL-            
HETNAM   3 NT5  PHENYL)METHANONE                                                
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     SO4 SULFATE ION                                                      
HETNAM     SOG OCTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE                              
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PGW (1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)            
HETNAM   2 PGW  PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL (9Z)-          
HETNAM   3 PGW  OCTADEC-9-ENOATE                                                
HETSYN     SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE                                   
HETSYN     PGW 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-[PHOSPHO-(1-                   
HETSYN   2 PGW  GLYCEROL)]; PHOSPHATIDYLGLYCEROL                                
FORMUL   3  NT5    2(C24 H25 F N4 O2)                                           
FORMUL   4  PG4    2(C8 H18 O5)                                                 
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   7  SOG    9(C14 H28 O5 S)                                              
FORMUL  12   CL    CL 1-                                                        
FORMUL  13  PGW    2(C40 H77 O10 P)                                             
FORMUL  23  HOH   *50(H2 O)                                                     
HELIX    1 AA1 ALA A   26  TYR A   39  1                                  14    
HELIX    2 AA2 TYR A   39  ASN A   74  1                                  36    
HELIX    3 AA3 HIS A   75  ARG A   78  5                                   4    
HELIX    4 AA4 THR A   79  ILE A   98  1                                  20    
HELIX    5 AA5 ILE A   98  GLU A  110  1                                  13    
HELIX    6 AA6 PHE A  114  CYS A  149  1                                  36    
HELIX    7 AA7 THR A  157  MET A  176  1                                  20    
HELIX    8 AA8 MET A  176  VAL A  182  1                                   7    
HELIX    9 AA9 ASP A  209  TYR A  224  1                                  16    
HELIX   10 AB1 TYR A  224  TRP A  243  1                                  20    
HELIX   11 AB2 SER A  252  VAL A  323  1                                  40    
HELIX   12 AB3 ASP A  332  SER A  362  1                                  31    
HELIX   13 AB4 SER A  362  TRP A  376  1                                  15    
HELIX   14 AB5 TYR B   45  ASN B   74  1                                  30    
HELIX   15 AB6 HIS B   75  ARG B   78  5                                   4    
HELIX   16 AB7 THR B   79  ILE B   98  1                                  20    
HELIX   17 AB8 ILE B   98  GLU B  110  1                                  13    
HELIX   18 AB9 PHE B  114  CYS B  149  1                                  36    
HELIX   19 AC1 THR B  157  MET B  176  1                                  20    
HELIX   20 AC2 MET B  176  VAL B  182  1                                   7    
HELIX   21 AC3 LEU B  189  ARG B  195  5                                   7    
HELIX   22 AC4 ASP B  209  TYR B  224  1                                  16    
HELIX   23 AC5 TYR B  224  TRP B  243  1                                  20    
HELIX   24 AC6 THR B  251  VAL B  323  1                                  41    
HELIX   25 AC7 ASP B  332  SER B  362  1                                  31    
HELIX   26 AC8 SER B  362  LEU B  377  1                                  16    
SHEET    1 AA1 2 MET A 183  VAL A 188  0                                        
SHEET    2 AA1 2 PHE A 199  GLU A 204 -1  O  PHE A 199   N  VAL A 188           
SHEET    1 AA2 2 MET B 183  SER B 187  0                                        
SHEET    2 AA2 2 SER B 200  GLU B 204 -1  O  ASP B 203   N  GLU B 184           
SSBOND   1 CYS A  119    CYS A  202                          1555   1555  2.03  
SSBOND   2 CYS B  119    CYS B  202                          1555   1555  2.03  
CRYST1   59.892  146.202   72.328  90.00 111.12  90.00 P 1 21 1      4          
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      0.016697  0.000000  0.006450        0.00000                         
SCALE2      0.000000  0.006840  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014822        0.00000                         
ATOM      1  N   ALA A  25       6.440  16.657 137.975  1.00127.31           N  
ANISOU    1  N   ALA A  25    23425  10086  14861   -281   7895   -554       N  
ATOM      2  CA  ALA A  25       7.233  15.645 138.663  1.00130.16           C  
ANISOU    2  CA  ALA A  25    24336  10348  14771   -453   7784   -457       C  
ATOM      3  C   ALA A  25       7.851  14.689 137.656  1.00131.89           C  
ANISOU    3  C   ALA A  25    24173  10828  15112   -415   7414   -484       C  
ATOM      4  O   ALA A  25       9.071  14.629 137.504  1.00129.75           O  
ANISOU    4  O   ALA A  25    24076  10680  14545   -359   6913   -441       O  
ATOM      5  CB  ALA A  25       6.378  14.884 139.664  1.00131.05           C  
ANISOU    5  CB  ALA A  25    24808  10143  14841   -684   8324   -445       C  
ATOM      6  N   ALA A  26       6.999  13.929 136.979  1.00134.92           N  
ANISOU    6  N   ALA A  26    24017  11287  15960   -453   7640   -583       N  
ATOM      7  CA  ALA A  26       7.423  13.097 135.865  1.00130.71           C  
ANISOU    7  CA  ALA A  26    23020  11012  15633   -400   7327   -620       C  
ATOM      8  C   ALA A  26       7.446  13.850 134.540  1.00130.58           C  
ANISOU    8  C   ALA A  26    22329  11283  16002   -160   7037   -688       C  
ATOM      9  O   ALA A  26       7.868  13.280 133.529  1.00125.85           O  
ANISOU    9  O   ALA A  26    21335  10901  15580    -96   6741   -709       O  
ATOM     10  CB  ALA A  26       6.515  11.870 135.746  1.00128.63           C  
ANISOU   10  CB  ALA A  26    22500  10700  15674   -573   7689   -710       C  
ATOM     11  N   SER A  27       6.990  15.106 134.513  1.00135.67           N  
ANISOU   11  N   SER A  27    22858  11926  16766    -16   7118   -715       N  
ATOM     12  CA  SER A  27       6.978  15.857 133.262  1.00132.37           C  
ANISOU   12  CA  SER A  27    21861  11768  16665    237   6845   -763       C  
ATOM     13  C   SER A  27       8.384  16.071 132.716  1.00132.54           C  
ANISOU   13  C   SER A  27    21993  11889  16477    300   6315   -674       C  
ATOM     14  O   SER A  27       8.576  16.103 131.494  1.00129.64           O  
ANISOU   14  O   SER A  27    21133  11746  16378    451   6041   -698       O  
ATOM     15  CB  SER A  27       6.284  17.203 133.469  1.00128.48           C  
ANISOU   15  CB  SER A  27    21346  11220  16252    391   7024   -794       C  
ATOM     16  OG  SER A  27       6.917  17.942 134.499  1.00126.20           O  
ANISOU   16  OG  SER A  27    21740  10698  15513    314   7023   -685       O  
ATOM     17  N   GLU A  28       9.375  16.222 133.597  1.00136.14           N  
ANISOU   17  N   GLU A  28    23074  12192  16462    184   6138   -588       N  
ATOM     18  CA  GLU A  28      10.749  16.380 133.136  1.00136.86           C  
ANISOU   18  CA  GLU A  28    23233  12378  16390    207   5589   -546       C  
ATOM     19  C   GLU A  28      11.256  15.115 132.458  1.00133.24           C  
ANISOU   19  C   GLU A  28    22521  12058  16047    168   5328   -551       C  
ATOM     20  O   GLU A  28      12.094  15.191 131.552  1.00132.13           O  
ANISOU   20  O   GLU A  28    22134  12057  16013    228   4911   -539       O  
ATOM     21  CB  GLU A  28      11.659  16.758 134.305  1.00143.88           C  
ANISOU   21  CB  GLU A  28    24806  13099  16764     89   5408   -497       C  
ATOM     22  CG  GLU A  28      13.066  17.173 133.901  1.00147.31           C  
ANISOU   22  CG  GLU A  28    25281  13614  17078     89   4833   -493       C  
ATOM     23  CD  GLU A  28      13.127  18.589 133.363  1.00153.26           C  
ANISOU   23  CD  GLU A  28    25892  14396  17943    190   4786   -501       C  
ATOM     24  OE1 GLU A  28      14.241  19.059 133.048  1.00153.18           O  
ANISOU   24  OE1 GLU A  28    25921  14426  17855    150   4377   -513       O  
ATOM     25  OE2 GLU A  28      12.063  19.234 133.261  1.00156.79           O  
ANISOU   25  OE2 GLU A  28    26195  14816  18562    304   5160   -502       O  
ATOM     26  N   ASP A  29      10.765  13.947 132.879  1.00129.44           N  
ANISOU   26  N   ASP A  29    22112  11520  15547     51   5584   -563       N  
ATOM     27  CA  ASP A  29      11.145  12.710 132.205  1.00122.06           C  
ANISOU   27  CA  ASP A  29    20930  10709  14738     18   5374   -567       C  
ATOM     28  C   ASP A  29      10.672  12.702 130.757  1.00108.63           C  
ANISOU   28  C   ASP A  29    18488   9236  13548    160   5352   -627       C  
ATOM     29  O   ASP A  29      11.386  12.225 129.867  1.00108.95           O  
ANISOU   29  O   ASP A  29    18272   9416  13711    197   4988   -606       O  
ATOM     30  CB  ASP A  29      10.574  11.507 132.956  1.00133.15           C  
ANISOU   30  CB  ASP A  29    22588  11986  16015   -150   5733   -573       C  
ATOM     31  CG  ASP A  29      11.326  11.208 134.234  1.00140.82           C  
ANISOU   31  CG  ASP A  29    24316  12774  16414   -252   5600   -498       C  
ATOM     32  OD1 ASP A  29      12.537  10.914 134.156  1.00139.88           O  
ANISOU   32  OD1 ASP A  29    24355  12706  16088   -224   5066   -458       O  
ATOM     33  OD2 ASP A  29      10.710  11.277 135.317  1.00145.64           O  
ANISOU   33  OD2 ASP A  29    25361  13183  16794   -354   6011   -482       O  
ATOM     34  N   GLU A  30       9.470  13.222 130.500  1.00101.88           N  
ANISOU   34  N   GLU A  30    17269   8438  13002    254   5701   -705       N  
ATOM     35  CA  GLU A  30       8.980  13.272 129.126  1.00101.48           C  
ANISOU   35  CA  GLU A  30    16496   8657  13405    435   5613   -772       C  
ATOM     36  C   GLU A  30       9.786  14.257 128.291  1.00 98.71           C  
ANISOU   36  C   GLU A  30    16043   8400  13063    613   5205   -710       C  
ATOM     37  O   GLU A  30      10.012  14.031 127.097  1.00101.13           O  
ANISOU   37  O   GLU A  30    15905   8906  13612    726   4951   -710       O  
ATOM     38  CB  GLU A  30       7.495  13.634 129.110  1.00106.17           C  
ANISOU   38  CB  GLU A  30    16706   9325  14308    513   5982   -890       C  
ATOM     39  CG  GLU A  30       6.862  13.664 127.726  1.00109.73           C  
ANISOU   39  CG  GLU A  30    16388  10108  15196    723   5824   -978       C  
ATOM     40  CD  GLU A  30       5.398  14.059 127.771  1.00121.04           C  
ANISOU   40  CD  GLU A  30    17438  11638  16912    819   6096  -1132       C  
ATOM     41  OE1 GLU A  30       4.774  13.894 128.840  1.00128.19           O  
ANISOU   41  OE1 GLU A  30    18595  12353  17760    648   6491  -1190       O  
ATOM     42  OE2 GLU A  30       4.874  14.543 126.745  1.00122.97           O  
ANISOU   42  OE2 GLU A  30    17156  12145  17423   1073   5895  -1204       O  
ATOM     43  N   PHE A  31      10.240  15.350 128.907  1.00 90.10           N  
ANISOU   43  N   PHE A  31    15378   7158  11697    618   5147   -656       N  
ATOM     44  CA  PHE A  31      11.049  16.328 128.187  1.00 81.42           C  
ANISOU   44  CA  PHE A  31    14247   6112  10577    732   4794   -604       C  
ATOM     45  C   PHE A  31      12.386  15.727 127.777  1.00 81.34           C  
ANISOU   45  C   PHE A  31    14286   6137  10484    623   4358   -552       C  
ATOM     46  O   PHE A  31      12.818  15.860 126.626  1.00 81.98           O  
ANISOU   46  O   PHE A  31    14035   6356  10757    717   4095   -530       O  
ATOM     47  CB  PHE A  31      11.256  17.568 129.060  1.00 86.60           C  
ANISOU   47  CB  PHE A  31    15386   6587  10933    709   4854   -573       C  
ATOM     48  CG  PHE A  31      12.312  18.505 128.548  1.00 87.68           C  
ANISOU   48  CG  PHE A  31    15620   6729  10965    728   4498   -529       C  
ATOM     49  CD1 PHE A  31      11.996  19.480 127.619  1.00 84.50           C  
ANISOU   49  CD1 PHE A  31    14963   6407  10737    933   4475   -522       C  
ATOM     50  CD2 PHE A  31      13.616  18.419 129.005  1.00 90.27           C  
ANISOU   50  CD2 PHE A  31    16299   6983  11017    535   4174   -509       C  
ATOM     51  CE1 PHE A  31      12.962  20.347 127.149  1.00 84.39           C  
ANISOU   51  CE1 PHE A  31    15077   6372  10614    911   4201   -486       C  
ATOM     52  CE2 PHE A  31      14.587  19.283 128.539  1.00 87.96           C  
ANISOU   52  CE2 PHE A  31    16064   6694  10663    504   3880   -502       C  
ATOM     53  CZ  PHE A  31      14.260  20.249 127.609  1.00 84.86           C  
ANISOU   53  CZ  PHE A  31    15451   6357  10437    674   3925   -486       C  
ATOM     54  N   LEU A  32      13.053  15.051 128.710  1.00 87.68           N  
ANISOU   54  N   LEU A  32    15504   6819  10992    432   4257   -530       N  
ATOM     55  CA  LEU A  32      14.333  14.427 128.410  1.00 86.12           C  
ANISOU   55  CA  LEU A  32    15339   6663  10720    333   3800   -493       C  
ATOM     56  C   LEU A  32      14.205  13.275 127.423  1.00 80.76           C  
ANISOU   56  C   LEU A  32    14207   6136  10343    366   3735   -488       C  
ATOM     57  O   LEU A  32      15.187  12.948 126.746  1.00 81.09           O  
ANISOU   57  O   LEU A  32    14099   6269  10443    334   3348   -450       O  
ATOM     58  CB  LEU A  32      14.987  13.959 129.707  1.00 91.73           C  
ANISOU   58  CB  LEU A  32    16613   7223  11018    172   3674   -483       C  
ATOM     59  CG  LEU A  32      15.491  15.102 130.589  1.00 97.78           C  
ANISOU   59  CG  LEU A  32    17830   7854  11466    122   3593   -497       C  
ATOM     60  CD1 LEU A  32      15.317  14.772 132.059  1.00101.23           C  
ANISOU   60  CD1 LEU A  32    18839   8115  11510     32   3754   -492       C  
ATOM     61  CD2 LEU A  32      16.948  15.382 130.275  1.00 98.90           C  
ANISOU   61  CD2 LEU A  32    18002   8028  11548     49   3071   -520       C  
ATOM     62  N   ARG A  33      13.034  12.644 127.327  1.00 79.40           N  
ANISOU   62  N   ARG A  33    13787   6009  10373    410   4109   -537       N  
ATOM     63  CA  ARG A  33      12.852  11.605 126.318  1.00 75.56           C  
ANISOU   63  CA  ARG A  33    12792   5735  10182    433   4031   -537       C  
ATOM     64  C   ARG A  33      12.743  12.210 124.925  1.00 77.78           C  
ANISOU   64  C   ARG A  33    12517   6265  10773    615   3856   -524       C  
ATOM     65  O   ARG A  33      13.355  11.717 123.971  1.00 75.28           O  
ANISOU   65  O   ARG A  33    11875   6151  10575    608   3516   -460       O  
ATOM     66  CB  ARG A  33      11.615  10.764 126.642  1.00 75.65           C  
ANISOU   66  CB  ARG A  33    12684   5730  10332    392   4503   -636       C  
ATOM     67  CG  ARG A  33      11.815   9.832 127.824  1.00 82.80           C  
ANISOU   67  CG  ARG A  33    14137   6416  10908    187   4631   -619       C  
ATOM     68  CD  ARG A  33      10.616   8.930 128.073  1.00 96.58           C  
ANISOU   68  CD  ARG A  33    15741   8157  12797     85   5125   -721       C  
ATOM     69  NE  ARG A  33      11.042   7.616 128.548  1.00109.58           N  
ANISOU   69  NE  ARG A  33    17732   9688  14215    -88   5093   -675       N  
ATOM     70  CZ  ARG A  33      11.444   7.360 129.789  1.00122.74           C  
ANISOU   70  CZ  ARG A  33    20067  11149  15418   -207   5105   -603       C  
ATOM     71  NH1 ARG A  33      11.475   8.331 130.692  1.00128.84           N  
ANISOU   71  NH1 ARG A  33    21229  11796  15928   -194   5171   -580       N  
ATOM     72  NH2 ARG A  33      11.817   6.134 130.126  1.00126.98           N  
ANISOU   72  NH2 ARG A  33    20898  11620  15730   -317   5036   -554       N  
ATOM     73  N   TYR A  34      11.958  13.280 124.784  1.00 84.38           N  
ANISOU   73  N   TYR A  34    13271   7067  11723    801   4090   -587       N  
ATOM     74  CA  TYR A  34      11.893  13.964 123.500  1.00 79.61           C  
ANISOU   74  CA  TYR A  34    12263   6644  11343   1015   3906   -570       C  
ATOM     75  C   TYR A  34      13.182  14.716 123.199  1.00 75.04           C  
ANISOU   75  C   TYR A  34    11911   6009  10591    965   3547   -476       C  
ATOM     76  O   TYR A  34      13.520  14.916 122.026  1.00 71.44           O  
ANISOU   76  O   TYR A  34    11162   5707  10276   1059   3305   -430       O  
ATOM     77  CB  TYR A  34      10.682  14.891 123.476  1.00 75.60           C  
ANISOU   77  CB  TYR A  34    11588   6199  10938   1214   4142   -634       C  
ATOM     78  CG  TYR A  34       9.397  14.109 123.419  1.00 82.45           C  
ANISOU   78  CG  TYR A  34    12021   7240  12064   1239   4388   -749       C  
ATOM     79  CD1 TYR A  34       9.235  13.091 122.489  1.00 91.97           C  
ANISOU   79  CD1 TYR A  34    12743   8681  13521   1246   4253   -777       C  
ATOM     80  CD2 TYR A  34       8.366  14.351 124.313  1.00 85.97           C  
ANISOU   80  CD2 TYR A  34    12540   7618  12507   1218   4746   -838       C  
ATOM     81  CE1 TYR A  34       8.074  12.354 122.430  1.00 93.49           C  
ANISOU   81  CE1 TYR A  34    12524   9049  13947   1215   4440   -905       C  
ATOM     82  CE2 TYR A  34       7.196  13.615 124.264  1.00 93.39           C  
ANISOU   82  CE2 TYR A  34    13059   8719  13706   1189   4955   -973       C  
ATOM     83  CZ  TYR A  34       7.057  12.617 123.318  1.00 96.30           C  
ANISOU   83  CZ  TYR A  34    12943   9332  14315   1178   4789  -1013       C  
ATOM     84  OH  TYR A  34       5.900  11.875 123.254  1.00102.89           O  
ANISOU   84  OH  TYR A  34    13358  10335  15402   1110   4962  -1171       O  
ATOM     85  N   LEU A  35      13.915  15.134 124.234  1.00 75.51           N  
ANISOU   85  N   LEU A  35    12503   5842  10345    806   3518   -466       N  
ATOM     86  CA  LEU A  35      15.236  15.708 124.005  1.00 72.30           C  
ANISOU   86  CA  LEU A  35    12274   5399   9799    695   3171   -424       C  
ATOM     87  C   LEU A  35      16.201  14.662 123.460  1.00 70.32           C  
ANISOU   87  C   LEU A  35    11777   5336   9603    557   2794   -377       C  
ATOM     88  O   LEU A  35      17.077  14.982 122.649  1.00 76.43           O  
ANISOU   88  O   LEU A  35    12414   6194  10433    518   2525   -356       O  
ATOM     89  CB  LEU A  35      15.775  16.316 125.301  1.00 78.70           C  
ANISOU   89  CB  LEU A  35    13647   5997  10260    537   3171   -451       C  
ATOM     90  CG  LEU A  35      17.211  16.847 125.276  1.00 80.12           C  
ANISOU   90  CG  LEU A  35    14025   6124  10292    368   2819   -469       C  
ATOM     91  CD1 LEU A  35      17.315  18.129 124.459  1.00 78.32           C  
ANISOU   91  CD1 LEU A  35    13725   5906  10129    442   2828   -464       C  
ATOM     92  CD2 LEU A  35      17.734  17.055 126.691  1.00 86.10           C  
ANISOU   92  CD2 LEU A  35    15294   6723  10696    204   2754   -517       C  
ATOM     93  N   TRP A  36      16.037  13.404 123.875  1.00 66.68           N  
ANISOU   93  N   TRP A  36    11276   4930   9131    483   2802   -369       N  
ATOM     94  CA  TRP A  36      16.858  12.316 123.357  1.00 61.38           C  
ANISOU   94  CA  TRP A  36    10369   4434   8518    388   2464   -325       C  
ATOM     95  C   TRP A  36      16.461  11.947 121.932  1.00 59.71           C  
ANISOU   95  C   TRP A  36     9589   4473   8625    506   2421   -288       C  
ATOM     96  O   TRP A  36      17.322  11.772 121.063  1.00 58.90           O  
ANISOU   96  O   TRP A  36     9262   4508   8609    469   2120   -253       O  
ATOM     97  CB  TRP A  36      16.738  11.102 124.281  1.00 59.08           C  
ANISOU   97  CB  TRP A  36    10302   4072   8072    294   2521   -325       C  
ATOM     98  CG  TRP A  36      17.276   9.840 123.692  1.00 60.34           C  
ANISOU   98  CG  TRP A  36    10190   4413   8323    247   2252   -279       C  
ATOM     99  CD1 TRP A  36      16.558   8.801 123.174  1.00 56.30           C  
ANISOU   99  CD1 TRP A  36     9356   4038   7998    271   2386   -261       C  
ATOM    100  CD2 TRP A  36      18.654   9.483 123.555  1.00 49.49           C  
ANISOU  100  CD2 TRP A  36     8831   3105   6870    169   1806   -269       C  
ATOM    101  NE1 TRP A  36      17.406   7.817 122.726  1.00 52.94           N  
ANISOU  101  NE1 TRP A  36     8788   3739   7588    219   2059   -215       N  
ATOM    102  CE2 TRP A  36      18.698   8.213 122.948  1.00 52.35           C  
ANISOU  102  CE2 TRP A  36     8901   3630   7361    170   1697   -222       C  
ATOM    103  CE3 TRP A  36      19.857  10.114 123.888  1.00 50.13           C  
ANISOU  103  CE3 TRP A  36     9122   3127   6799     94   1492   -322       C  
ATOM    104  CZ2 TRP A  36      19.897   7.562 122.667  1.00 53.45           C  
ANISOU  104  CZ2 TRP A  36     8957   3870   7480    129   1288   -216       C  
ATOM    105  CZ3 TRP A  36      21.045   9.467 123.609  1.00 54.85           C  
ANISOU  105  CZ3 TRP A  36     9591   3845   7404     42   1078   -342       C  
ATOM    106  CH2 TRP A  36      21.057   8.204 123.004  1.00 52.52           C  
ANISOU  106  CH2 TRP A  36     9010   3709   7238     74    980   -283       C  
ATOM    107  N   ARG A  37      15.158  11.818 121.680  1.00 61.99           N  
ANISOU  107  N   ARG A  37     9634   4823   9096    647   2721   -319       N  
ATOM    108  CA  ARG A  37      14.686  11.407 120.361  1.00 64.32           C  
ANISOU  108  CA  ARG A  37     9397   5359   9683    776   2659   -308       C  
ATOM    109  C   ARG A  37      14.936  12.484 119.311  1.00 69.46           C  
ANISOU  109  C   ARG A  37     9930   6049  10414    929   2520   -281       C  
ATOM    110  O   ARG A  37      15.305  12.175 118.171  1.00 66.47           O  
ANISOU  110  O   ARG A  37     9253   5831  10170    961   2298   -237       O  
ATOM    111  CB  ARG A  37      13.198  11.060 120.445  1.00 67.85           C  
ANISOU  111  CB  ARG A  37     9600   5863  10318    889   3012   -403       C  
ATOM    112  CG  ARG A  37      12.442  11.032 119.128  1.00 76.22           C  
ANISOU  112  CG  ARG A  37    10123   7154  11685   1101   2974   -443       C  
ATOM    113  CD  ARG A  37      10.954  10.786 119.377  1.00 86.62           C  
ANISOU  113  CD  ARG A  37    11179   8524  13207   1201   3342   -600       C  
ATOM    114  NE  ARG A  37      10.656   9.384 119.664  1.00 92.62           N  
ANISOU  114  NE  ARG A  37    11800   9353  14040   1004   3470   -650       N  
ATOM    115  CZ  ARG A  37       9.487   8.947 120.123  1.00 96.55           C  
ANISOU  115  CZ  ARG A  37    12132   9864  14690    972   3850   -811       C  
ATOM    116  NH1 ARG A  37       8.503   9.804 120.361  1.00 97.77           N  
ANISOU  116  NH1 ARG A  37    12211  10055  14884   1084   3986   -895       N  
ATOM    117  NH2 ARG A  37       9.301   7.653 120.349  1.00 97.08           N  
ANISOU  117  NH2 ARG A  37    12129   9956  14802    762   3991   -858       N  
ATOM    118  N   ASP A  38      14.742  13.749 119.675  1.00 73.41           N  
ANISOU  118  N   ASP A  38    10710   6374  10808   1023   2669   -307       N  
ATOM    119  CA  ASP A  38      14.760  14.840 118.711  1.00 72.74           C  
ANISOU  119  CA  ASP A  38    10592   6273  10772   1209   2614   -289       C  
ATOM    120  C   ASP A  38      16.180  15.311 118.431  1.00 67.02           C  
ANISOU  120  C   ASP A  38    10132   5439   9893   1044   2405   -250       C  
ATOM    121  O   ASP A  38      16.444  15.790 117.324  1.00 60.61           O  
ANISOU  121  O   ASP A  38     9330   4595   9106   1159   2361   -227       O  
ATOM    122  CB  ASP A  38      13.736  15.903 119.115  1.00 70.07           C  
ANISOU  122  CB  ASP A  38    10423   5788  10412   1437   2914   -351       C  
ATOM    123  CG  ASP A  38      12.315  15.394 119.037  1.00 75.60           C  
ANISOU  123  CG  ASP A  38    10737   6674  11316   1609   3087   -430       C  
ATOM    124  OD1 ASP A  38      12.106  14.289 118.490  1.00 78.39           O  
ANISOU  124  OD1 ASP A  38    10704   7214  11866   1597   3012   -446       O  
ATOM    125  OD2 ASP A  38      11.406  16.096 119.524  1.00 81.70           O  
ANISOU  125  OD2 ASP A  38    11570   7420  12051   1732   3283   -489       O  
ATOM    126  N   TYR A  39      17.102  15.193 119.383  1.00 61.66           N  
ANISOU  126  N   TYR A  39     9680   4695   9055    783   2279   -262       N  
ATOM    127  CA  TYR A  39      18.374  15.897 119.280  1.00 58.68           C  
ANISOU  127  CA  TYR A  39     9515   4218   8563    604   2103   -284       C  
ATOM    128  C   TYR A  39      19.550  15.013 119.653  1.00 56.31           C  
ANISOU  128  C   TYR A  39     9180   3998   8218    359   1812   -313       C  
ATOM    129  O   TYR A  39      20.486  14.847 118.863  1.00 58.06           O  
ANISOU  129  O   TYR A  39     9211   4319   8532    253   1597   -323       O  
ATOM    130  CB  TYR A  39      18.368  17.144 120.168  1.00 64.05           C  
ANISOU  130  CB  TYR A  39    10670   4635   9030    576   2281   -338       C  
ATOM    131  CG  TYR A  39      19.714  17.830 120.289  1.00 63.73           C  
ANISOU  131  CG  TYR A  39    10870   4479   8864    326   2117   -411       C  
ATOM    132  CD1 TYR A  39      20.273  18.507 119.212  1.00 65.46           C  
ANISOU  132  CD1 TYR A  39    11043   4677   9153    295   2083   -418       C  
ATOM    133  CD2 TYR A  39      20.416  17.818 121.489  1.00 62.38           C  
ANISOU  133  CD2 TYR A  39    10996   4207   8500    115   2009   -498       C  
ATOM    134  CE1 TYR A  39      21.498  19.144 119.324  1.00 66.25           C  
ANISOU  134  CE1 TYR A  39    11334   4668   9169     23   1982   -528       C  
ATOM    135  CE2 TYR A  39      21.642  18.453 121.609  1.00 60.85           C  
ANISOU  135  CE2 TYR A  39    10969   3928   8223   -129   1848   -615       C  
ATOM    136  CZ  TYR A  39      22.178  19.113 120.524  1.00 64.94           C  
ANISOU  136  CZ  TYR A  39    11387   4437   8850   -193   1854   -640       C  
ATOM    137  OH  TYR A  39      23.396  19.745 120.642  1.00 70.02           O  
ANISOU  137  OH  TYR A  39    12169   4994   9442   -479   1738   -798       O  
ATOM    138  N   LEU A  40      19.521  14.457 120.862  1.00 48.81           N  
ANISOU  138  N   LEU A  40     8442   2990   7116    282   1809   -339       N  
ATOM    139  CA  LEU A  40      20.691  13.747 121.359  1.00 54.70           C  
ANISOU  139  CA  LEU A  40     9239   3776   7768     95   1490   -390       C  
ATOM    140  C   LEU A  40      20.987  12.513 120.517  1.00 52.79           C  
ANISOU  140  C   LEU A  40     8581   3765   7711    102   1287   -341       C  
ATOM    141  O   LEU A  40      22.110  12.338 120.030  1.00 57.05           O  
ANISOU  141  O   LEU A  40     8955   4400   8319    -12   1014   -390       O  
ATOM    142  CB  LEU A  40      20.487  13.380 122.831  1.00 66.39           C  
ANISOU  142  CB  LEU A  40    11122   5108   8997     60   1536   -417       C  
ATOM    143  CG  LEU A  40      20.535  14.553 123.813  1.00 65.44           C  
ANISOU  143  CG  LEU A  40    11483   4740   8642      3   1657   -490       C  
ATOM    144  CD1 LEU A  40      20.060  14.118 125.187  1.00 65.01           C  
ANISOU  144  CD1 LEU A  40    11855   4515   8332      7   1784   -496       C  
ATOM    145  CD2 LEU A  40      21.942  15.133 123.892  1.00 60.94           C  
ANISOU  145  CD2 LEU A  40    11008   4146   8001   -187   1345   -614       C  
ATOM    146  N   TYR A  41      19.990  11.650 120.324  1.00 51.03           N  
ANISOU  146  N   TYR A  41     8172   3632   7584    223   1436   -267       N  
ATOM    147  CA  TYR A  41      20.226  10.447 119.529  1.00 44.12           C  
ANISOU  147  CA  TYR A  41     6932   2961   6871    225   1261   -221       C  
ATOM    148  C   TYR A  41      20.656  10.754 118.102  1.00 51.54           C  
ANISOU  148  C   TYR A  41     7536   4032   8014    244   1152   -203       C  
ATOM    149  O   TYR A  41      21.684  10.212 117.660  1.00 60.89           O  
ANISOU  149  O   TYR A  41     8552   5323   9262    147    894   -222       O  
ATOM    150  CB  TYR A  41      18.972   9.564 119.549  1.00 52.33           C  
ANISOU  150  CB  TYR A  41     7834   4057   7990    326   1492   -174       C  
ATOM    151  CG  TYR A  41      19.033   8.423 118.563  1.00 55.93           C  
ANISOU  151  CG  TYR A  41     7898   4720   8634    340   1358   -127       C  
ATOM    152  CD1 TYR A  41      19.758   7.273 118.846  1.00 55.88           C  
ANISOU  152  CD1 TYR A  41     7922   4752   8557    253   1142   -115       C  
ATOM    153  CD2 TYR A  41      18.368   8.497 117.346  1.00 57.61           C  
ANISOU  153  CD2 TYR A  41     7739   5076   9075    463   1430   -100       C  
ATOM    154  CE1 TYR A  41      19.818   6.226 117.944  1.00 59.81           C  
ANISOU  154  CE1 TYR A  41     8087   5421   9216    266   1036    -72       C  
ATOM    155  CE2 TYR A  41      18.423   7.455 116.438  1.00 60.25           C  
ANISOU  155  CE2 TYR A  41     7738   5587   9566    468   1307    -64       C  
ATOM    156  CZ  TYR A  41      19.149   6.323 116.743  1.00 65.63           C  
ANISOU  156  CZ  TYR A  41     8454   6300  10183    357   1127    -46       C  
ATOM    157  OH  TYR A  41      19.204   5.285 115.841  1.00 68.77           O  
ANISOU  157  OH  TYR A  41     8544   6857  10727    361   1021     -9       O  
ATOM    158  N   PRO A  42      19.932  11.568 117.327  1.00 54.85           N  
ANISOU  158  N   PRO A  42     7867   4441   8533    383   1335   -174       N  
ATOM    159  CA  PRO A  42      20.381  11.845 115.950  1.00 46.91           C  
ANISOU  159  CA  PRO A  42     6633   3517   7672    404   1241   -153       C  
ATOM    160  C   PRO A  42      21.764  12.467 115.867  1.00 54.29           C  
ANISOU  160  C   PRO A  42     7686   4381   8561    205   1093   -229       C  
ATOM    161  O   PRO A  42      22.522  12.166 114.936  1.00 65.10           O  
ANISOU  161  O   PRO A  42     8835   5847  10053    131    955   -237       O  
ATOM    162  CB  PRO A  42      19.291  12.776 115.405  1.00 44.99           C  
ANISOU  162  CB  PRO A  42     6419   3210   7465    632   1467   -125       C  
ATOM    163  CG  PRO A  42      18.615  13.344 116.620  1.00 48.42           C  
ANISOU  163  CG  PRO A  42     7150   3490   7758    674   1677   -160       C  
ATOM    164  CD  PRO A  42      18.692  12.280 117.669  1.00 54.06           C  
ANISOU  164  CD  PRO A  42     7899   4238   8405    548   1634   -173       C  
ATOM    165  N   LYS A  43      22.111  13.342 116.817  1.00 59.67           N  
ANISOU  165  N   LYS A  43     8706   4890   9076    100   1136   -308       N  
ATOM    166  CA  LYS A  43      23.446  13.937 116.841  1.00 62.98           C  
ANISOU  166  CA  LYS A  43     9213   5246   9470   -131   1001   -435       C  
ATOM    167  C   LYS A  43      24.497  12.917 117.255  1.00 57.86           C  
ANISOU  167  C   LYS A  43     8403   4731   8849   -275    684   -519       C  
ATOM    168  O   LYS A  43      25.635  12.955 116.775  1.00 62.97           O  
ANISOU  168  O   LYS A  43     8885   5438   9605   -441    528   -633       O  
ATOM    169  CB  LYS A  43      23.460  15.130 117.789  1.00 69.56           C  
ANISOU  169  CB  LYS A  43    10466   5855  10109   -205   1130   -514       C  
ATOM    170  CG  LYS A  43      24.764  15.899 117.808  1.00 83.55           C  
ANISOU  170  CG  LYS A  43    12334   7544  11867   -474   1036   -686       C  
ATOM    171  CD  LYS A  43      24.780  16.892 118.953  1.00 94.19           C  
ANISOU  171  CD  LYS A  43    14117   8676  12996   -564   1124   -778       C  
ATOM    172  CE  LYS A  43      26.054  17.714 118.952  1.00101.34           C  
ANISOU  172  CE  LYS A  43    15101   9496  13907   -866   1053   -991       C  
ATOM    173  NZ  LYS A  43      26.099  18.651 117.798  1.00100.14           N  
ANISOU  173  NZ  LYS A  43    14991   9225  13831   -910   1307   -983       N  
ATOM    174  N   GLN A  44      24.110  11.964 118.103  1.00 55.90           N  
ANISOU  174  N   GLN A  44     8204   4525   8508   -200    599   -476       N  
ATOM    175  CA  GLN A  44      25.009  10.893 118.509  1.00 59.68           C  
ANISOU  175  CA  GLN A  44     8578   5117   8981   -264    275   -543       C  
ATOM    176  C   GLN A  44      25.114   9.837 117.428  1.00 66.60           C  
ANISOU  176  C   GLN A  44     9057   6188  10061   -209    186   -473       C  
ATOM    177  O   GLN A  44      26.077   9.063 117.410  1.00 73.59           O  
ANISOU  177  O   GLN A  44     9776   7184  11001   -260    -94   -548       O  
ATOM    178  CB  GLN A  44      24.504  10.263 119.806  1.00 69.20           C  
ANISOU  178  CB  GLN A  44    10091   6241   9962   -188    256   -511       C  
ATOM    179  CG  GLN A  44      25.384   9.181 120.395  1.00 80.93           C  
ANISOU  179  CG  GLN A  44    11593   7793  11365   -198   -103   -580       C  
ATOM    180  CD  GLN A  44      24.818   8.642 121.696  1.00 92.94           C  
ANISOU  180  CD  GLN A  44    13545   9165  12603   -117    -71   -539       C  
ATOM    181  OE1 GLN A  44      24.776   9.344 122.707  1.00101.27           O  
ANISOU  181  OE1 GLN A  44    14993  10043  13440   -153    -34   -601       O  
ATOM    182  NE2 GLN A  44      24.350   7.398 121.668  1.00 92.52           N  
ANISOU  182  NE2 GLN A  44    13460   9156  12537    -20    -49   -438       N  
ATOM    183  N   TYR A  45      24.151   9.816 116.514  1.00 65.09           N  
ANISOU  183  N   TYR A  45     8711   6037   9982    -89    404   -346       N  
ATOM    184  CA  TYR A  45      24.142   8.849 115.430  1.00 58.72           C  
ANISOU  184  CA  TYR A  45     7554   5401   9356    -34    339   -276       C  
ATOM    185  C   TYR A  45      24.978   9.351 114.258  1.00 57.86           C  
ANISOU  185  C   TYR A  45     7250   5330   9404   -128    309   -329       C  
ATOM    186  O   TYR A  45      25.753   8.589 113.671  1.00 58.70           O  
ANISOU  186  O   TYR A  45     7100   5562   9640   -181    140   -360       O  
ATOM    187  CB  TYR A  45      22.687   8.603 115.031  1.00 57.84           C  
ANISOU  187  CB  TYR A  45     7371   5318   9288    141    567   -153       C  
ATOM    188  CG  TYR A  45      22.414   7.709 113.847  1.00 55.78           C  
ANISOU  188  CG  TYR A  45     6772   5219   9202    215    537    -80       C  
ATOM    189  CD1 TYR A  45      22.817   8.062 112.565  1.00 57.35           C  
ANISOU  189  CD1 TYR A  45     6799   5462   9530    213    517    -73       C  
ATOM    190  CD2 TYR A  45      21.677   6.547 114.004  1.00 57.59           C  
ANISOU  190  CD2 TYR A  45     6898   5532   9452    280    566    -25       C  
ATOM    191  CE1 TYR A  45      22.535   7.250 111.483  1.00 57.64           C  
ANISOU  191  CE1 TYR A  45     6564   5632   9702    289    485     -8       C  
ATOM    192  CE2 TYR A  45      21.388   5.736 112.936  1.00 59.07           C  
ANISOU  192  CE2 TYR A  45     6788   5862   9792    337    539     27       C  
ATOM    193  CZ  TYR A  45      21.816   6.088 111.678  1.00 60.19           C  
ANISOU  193  CZ  TYR A  45     6760   6056  10053    351    483     39       C  
ATOM    194  OH  TYR A  45      21.516   5.262 110.622  1.00 64.19           O  
ANISOU  194  OH  TYR A  45     7006   6695  10690    412    447     88       O  
ATOM    195  N   ALA A  46      24.830  10.631 113.909  1.00 59.30           N  
ANISOU  195  N   ALA A  46     7587   5380   9566   -150    498   -346       N  
ATOM    196  CA  ALA A  46      25.626  11.204 112.829  1.00 54.59           C  
ANISOU  196  CA  ALA A  46     6897   4758   9084   -269    537   -409       C  
ATOM    197  C   ALA A  46      27.108  11.237 113.181  1.00 57.11           C  
ANISOU  197  C   ALA A  46     7138   5100   9461   -516    353   -607       C  
ATOM    198  O   ALA A  46      27.959  11.080 112.297  1.00 62.84           O  
ANISOU  198  O   ALA A  46     7642   5886  10349   -636    324   -684       O  
ATOM    199  CB  ALA A  46      25.130  12.611 112.499  1.00 50.04           C  
ANISOU  199  CB  ALA A  46     6608   3983   8422   -230    799   -389       C  
ATOM    200  N   TRP A  47      27.439  11.445 114.460  1.00 61.72           N  
ANISOU  200  N   TRP A  47     7897   5635   9919   -593    228   -715       N  
ATOM    201  CA  TRP A  47      28.841  11.483 114.865  1.00 66.36           C  
ANISOU  201  CA  TRP A  47     8374   6266  10573   -808      1   -952       C  
ATOM    202  C   TRP A  47      29.497  10.120 114.691  1.00 74.11           C  
ANISOU  202  C   TRP A  47     9014   7455  11689   -767   -286   -988       C  
ATOM    203  O   TRP A  47      30.572  10.007 114.087  1.00 77.48           O  
ANISOU  203  O   TRP A  47     9155   7970  12313   -911   -375  -1149       O  
ATOM    204  CB  TRP A  47      28.955  11.951 116.316  1.00 69.09           C  
ANISOU  204  CB  TRP A  47     9023   6511  10718   -857   -113  -1059       C  
ATOM    205  CG  TRP A  47      30.345  12.366 116.718  1.00 80.58           C  
ANISOU  205  CG  TRP A  47    10392   7983  12242  -1100   -322  -1358       C  
ATOM    206  CD1 TRP A  47      30.834  13.639 116.771  1.00 88.94           C  
ANISOU  206  CD1 TRP A  47    11593   8900  13301  -1335   -177  -1533       C  
ATOM    207  CD2 TRP A  47      31.426  11.506 117.110  1.00 86.07           C  
ANISOU  207  CD2 TRP A  47    10824   8850  13030  -1127   -717  -1547       C  
ATOM    208  NE1 TRP A  47      32.146  13.627 117.179  1.00 92.51           N  
ANISOU  208  NE1 TRP A  47    11845   9441  13863  -1535   -454  -1843       N  
ATOM    209  CE2 TRP A  47      32.534  12.330 117.392  1.00 90.16           C  
ANISOU  209  CE2 TRP A  47    11283   9345  13627  -1389   -810  -1860       C  
ATOM    210  CE3 TRP A  47      31.562  10.122 117.252  1.00 86.74           C  
ANISOU  210  CE3 TRP A  47    10728   9096  13132   -945  -1004  -1498       C  
ATOM    211  CZ2 TRP A  47      33.761  11.817 117.807  1.00 91.30           C  
ANISOU  211  CZ2 TRP A  47    11143   9652  13895  -1452  -1212  -2145       C  
ATOM    212  CZ3 TRP A  47      32.782   9.614 117.664  1.00 85.06           C  
ANISOU  212  CZ3 TRP A  47    10287   9021  13010   -980  -1402  -1752       C  
ATOM    213  CH2 TRP A  47      33.864  10.460 117.937  1.00 87.38           C  
ANISOU  213  CH2 TRP A  47    10476   9318  13408  -1221  -1519  -2082       C  
ATOM    214  N   VAL A  48      28.872   9.072 115.234  1.00 79.94           N  
ANISOU  214  N   VAL A  48     9796   8255  12322   -576   -410   -854       N  
ATOM    215  CA  VAL A  48      29.421   7.725 115.092  1.00 74.07           C  
ANISOU  215  CA  VAL A  48     8794   7679  11671   -501   -675   -869       C  
ATOM    216  C   VAL A  48      29.504   7.332 113.624  1.00 71.18           C  
ANISOU  216  C   VAL A  48     8105   7414  11526   -505   -564   -804       C  
ATOM    217  O   VAL A  48      30.460   6.674 113.195  1.00 75.42           O  
ANISOU  217  O   VAL A  48     8351   8079  12228   -543   -744   -914       O  
ATOM    218  CB  VAL A  48      28.576   6.718 115.894  1.00 58.47           C  
ANISOU  218  CB  VAL A  48     7017   5695   9505   -308   -742   -717       C  
ATOM    219  CG1 VAL A  48      29.086   5.305 115.667  1.00 54.30           C  
ANISOU  219  CG1 VAL A  48     6273   5309   9049   -210   -988   -714       C  
ATOM    220  CG2 VAL A  48      28.587   7.072 117.369  1.00 57.47           C  
ANISOU  220  CG2 VAL A  48     7270   5440   9127   -303   -856   -792       C  
ATOM    221  N   LEU A  49      28.501   7.720 112.833  1.00 61.54           N  
ANISOU  221  N   LEU A  49     6942   6133  10306   -446   -279   -638       N  
ATOM    222  CA  LEU A  49      28.494   7.381 111.413  1.00 53.30           C  
ANISOU  222  CA  LEU A  49     5663   5159   9430   -430   -174   -568       C  
ATOM    223  C   LEU A  49      29.675   8.013 110.686  1.00 60.47           C  
ANISOU  223  C   LEU A  49     6426   6047  10504   -643   -123   -747       C  
ATOM    224  O   LEU A  49      30.386   7.343 109.929  1.00 67.07           O  
ANISOU  224  O   LEU A  49     6983   6988  11512   -686   -189   -803       O  
ATOM    225  CB  LEU A  49      27.173   7.824 110.779  1.00 53.65           C  
ANISOU  225  CB  LEU A  49     5841   5127   9415   -293     82   -389       C  
ATOM    226  CG  LEU A  49      26.903   7.409 109.330  1.00 63.31           C  
ANISOU  226  CG  LEU A  49     6891   6409  10757   -221    170   -291       C  
ATOM    227  CD1 LEU A  49      27.022   5.897 109.161  1.00 67.07           C  
ANISOU  227  CD1 LEU A  49     7118   7052  11315   -159     -9   -246       C  
ATOM    228  CD2 LEU A  49      25.532   7.897 108.883  1.00 63.61           C  
ANISOU  228  CD2 LEU A  49     7074   6379  10716    -35    355   -151       C  
ATOM    229  N   ILE A  50      29.906   9.307 110.912  1.00 62.49           N  
ANISOU  229  N   ILE A  50     6880   6152  10712   -796     26   -855       N  
ATOM    230  CA  ILE A  50      30.967  10.001 110.190  1.00 58.74           C  
ANISOU  230  CA  ILE A  50     6307   5619  10394  -1045    160  -1047       C  
ATOM    231  C   ILE A  50      32.337   9.581 110.704  1.00 61.85           C  
ANISOU  231  C   ILE A  50     6400   6149  10953  -1206   -103  -1322       C  
ATOM    232  O   ILE A  50      33.289   9.440 109.927  1.00 64.73           O  
ANISOU  232  O   ILE A  50     6522   6603  11470  -1325    -56  -1452       O  
ATOM    233  CB  ILE A  50      30.759  11.521 110.287  1.00 52.34           C  
ANISOU  233  CB  ILE A  50     5849   4575   9463  -1170    430  -1088       C  
ATOM    234  CG1 ILE A  50      29.398  11.888 109.694  1.00 47.06           C  
ANISOU  234  CG1 ILE A  50     5452   3785   8644   -943    651   -832       C  
ATOM    235  CG2 ILE A  50      31.880  12.255 109.573  1.00 43.73           C  
ANISOU  235  CG2 ILE A  50     4697   3389   8530  -1478    627  -1314       C  
ATOM    236  CD1 ILE A  50      28.943  13.280 110.028  1.00 52.05           C  
ANISOU  236  CD1 ILE A  50     6495   4182   9101   -968    877   -832       C  
ATOM    237  N   ALA A  51      32.466   9.385 112.016  1.00 62.45           N  
ANISOU  237  N   ALA A  51     6532   6273  10922  -1159   -381  -1400       N  
ATOM    238  CA  ALA A  51      33.736   8.919 112.563  1.00 64.83           C  
ANISOU  238  CA  ALA A  51     6542   6722  11367  -1245   -712  -1681       C  
ATOM    239  C   ALA A  51      34.081   7.522 112.060  1.00 63.40           C  
ANISOU  239  C   ALA A  51     6048   6738  11304  -1081   -898  -1635       C  
ATOM    240  O   ALA A  51      35.238   7.243 111.724  1.00 72.06           O  
ANISOU  240  O   ALA A  51     6923   8011  12445  -1090   -948  -1771       O  
ATOM    241  CB  ALA A  51      33.687   8.940 114.090  1.00 66.18           C  
ANISOU  241  CB  ALA A  51     6935   6882  11330  -1165  -1002  -1745       C  
ATOM    242  N   ALA A  52      33.092   6.627 112.005  1.00 55.95           N  
ANISOU  242  N   ALA A  52     5199   5806  10254   -853   -927  -1371       N  
ATOM    243  CA  ALA A  52      33.351   5.287 111.490  1.00 43.57           C  
ANISOU  243  CA  ALA A  52     3382   4392   8782   -703  -1075  -1316       C  
ATOM    244  C   ALA A  52      33.776   5.329 110.027  1.00 51.61           C  
ANISOU  244  C   ALA A  52     4300   5476   9836   -739   -782  -1270       C  
ATOM    245  O   ALA A  52      34.716   4.631 109.626  1.00 62.35           O  
ANISOU  245  O   ALA A  52     5512   6976  11200   -678   -846  -1339       O  
ATOM    246  CB  ALA A  52      32.116   4.406 111.670  1.00 39.62           C  
ANISOU  246  CB  ALA A  52     3073   3875   8105   -476  -1078  -1031       C  
ATOM    247  N   TYR A  53      33.090   6.133 109.210  1.00 53.92           N  
ANISOU  247  N   TYR A  53     4714   5630  10142   -829   -465  -1161       N  
ATOM    248  CA  TYR A  53      33.451   6.229 107.799  1.00 52.15           C  
ANISOU  248  CA  TYR A  53     4463   5421   9932   -866   -209  -1133       C  
ATOM    249  C   TYR A  53      34.812   6.888 107.609  1.00 55.47           C  
ANISOU  249  C   TYR A  53     4794   5880  10404  -1057   -120  -1379       C  
ATOM    250  O   TYR A  53      35.587   6.483 106.733  1.00 54.13           O  
ANISOU  250  O   TYR A  53     4510   5787  10268  -1059    -39  -1427       O  
ATOM    251  CB  TYR A  53      32.374   7.000 107.035  1.00 57.85           C  
ANISOU  251  CB  TYR A  53     5388   5950  10642   -892     80   -973       C  
ATOM    252  CG  TYR A  53      31.321   6.122 106.400  1.00 58.52           C  
ANISOU  252  CG  TYR A  53     5475   6057  10704   -687     77   -734       C  
ATOM    253  CD1 TYR A  53      30.175   5.760 107.096  1.00 55.07           C  
ANISOU  253  CD1 TYR A  53     5079   5603  10240   -554    -28   -585       C  
ATOM    254  CD2 TYR A  53      31.469   5.661 105.100  1.00 56.29           C  
ANISOU  254  CD2 TYR A  53     5176   5810  10403   -631    190   -670       C  
ATOM    255  CE1 TYR A  53      29.209   4.955 106.516  1.00 48.91           C  
ANISOU  255  CE1 TYR A  53     4286   4877   9419   -370    -20   -389       C  
ATOM    256  CE2 TYR A  53      30.508   4.857 104.511  1.00 52.43           C  
ANISOU  256  CE2 TYR A  53     4704   5345   9870   -452    168   -473       C  
ATOM    257  CZ  TYR A  53      29.381   4.507 105.223  1.00 48.19           C  
ANISOU  257  CZ  TYR A  53     4177   4823   9309   -324     62   -340       C  
ATOM    258  OH  TYR A  53      28.425   3.708 104.638  1.00 51.35           O  
ANISOU  258  OH  TYR A  53     4615   5273   9622   -160     49   -174       O  
ATOM    259  N   VAL A  54      35.128   7.897 108.422  1.00 62.26           N  
ANISOU  259  N   VAL A  54     5711   6673  11271  -1232   -123  -1548       N  
ATOM    260  CA  VAL A  54      36.407   8.590 108.281  1.00 61.78           C  
ANISOU  260  CA  VAL A  54     5552   6650  11272  -1437    -19  -1799       C  
ATOM    261  C   VAL A  54      37.555   7.704 108.748  1.00 63.48           C  
ANISOU  261  C   VAL A  54     5477   7080  11563  -1355   -310  -1972       C  
ATOM    262  O   VAL A  54      38.592   7.605 108.084  1.00 67.28           O  
ANISOU  262  O   VAL A  54     5788   7635  12138  -1418   -209  -2112       O  
ATOM    263  CB  VAL A  54      36.383   9.926 109.043  1.00 64.85           C  
ANISOU  263  CB  VAL A  54     6126   6897  11619  -1651     63  -1932       C  
ATOM    264  CG1 VAL A  54      37.777  10.532 109.082  1.00 64.42           C  
ANISOU  264  CG1 VAL A  54     5918   6912  11647  -1864    120  -2222       C  
ATOM    265  CG2 VAL A  54      35.399  10.877 108.397  1.00 65.69           C  
ANISOU  265  CG2 VAL A  54     6577   6752  11631  -1718    414  -1771       C  
ATOM    266  N   ALA A  55      37.393   7.053 109.901  1.00 62.68           N  
ANISOU  266  N   ALA A  55     5338   7056  11421  -1202   -673  -1978       N  
ATOM    267  CA  ALA A  55      38.450   6.179 110.396  1.00 61.37           C  
ANISOU  267  CA  ALA A  55     4944   7069  11303  -1076   -976  -2140       C  
ATOM    268  C   ALA A  55      38.758   5.066 109.399  1.00 67.18           C  
ANISOU  268  C   ALA A  55     5570   7888  12069   -930   -921  -2043       C  
ATOM    269  O   ALA A  55      39.927   4.726 109.179  1.00 72.07           O  
ANISOU  269  O   ALA A  55     5976   8615  12792   -928   -966  -2225       O  
ATOM    270  CB  ALA A  55      38.062   5.600 111.756  1.00 54.49           C  
ANISOU  270  CB  ALA A  55     4147   6220  10336   -894  -1382  -2131       C  
ATOM    271  N   VAL A  56      37.725   4.489 108.780  1.00 65.72           N  
ANISOU  271  N   VAL A  56     5531   7644  11797   -812   -822  -1773       N  
ATOM    272  CA  VAL A  56      37.956   3.457 107.772  1.00 58.04           C  
ANISOU  272  CA  VAL A  56     4509   6725  10819   -699   -752  -1676       C  
ATOM    273  C   VAL A  56      38.609   4.056 106.532  1.00 63.36           C  
ANISOU  273  C   VAL A  56     5120   7361  11593   -873   -429  -1768       C  
ATOM    274  O   VAL A  56      39.507   3.454 105.932  1.00 72.01           O  
ANISOU  274  O   VAL A  56     6070   8525  12765   -851   -408  -1861       O  
ATOM    275  CB  VAL A  56      36.637   2.739 107.431  1.00 52.39           C  
ANISOU  275  CB  VAL A  56     3981   5953   9972   -551   -725  -1379       C  
ATOM    276  CG1 VAL A  56      36.752   2.003 106.100  1.00 65.72           C  
ANISOU  276  CG1 VAL A  56     5678   7654  11639   -507   -562  -1277       C  
ATOM    277  CG2 VAL A  56      36.254   1.779 108.544  1.00 43.07           C  
ANISOU  277  CG2 VAL A  56     2848   4815   8702   -360  -1042  -1315       C  
ATOM    278  N   PHE A  57      38.156   5.241 106.118  1.00 61.95           N  
ANISOU  278  N   PHE A  57     5074   7046  11417  -1048   -160  -1751       N  
ATOM    279  CA  PHE A  57      38.725   5.896 104.944  1.00 64.04           C  
ANISOU  279  CA  PHE A  57     5342   7230  11760  -1224    181  -1846       C  
ATOM    280  C   PHE A  57      40.229   6.092 105.097  1.00 66.80           C  
ANISOU  280  C   PHE A  57     5441   7670  12272  -1354    177  -2160       C  
ATOM    281  O   PHE A  57      41.010   5.733 104.207  1.00 68.46           O  
ANISOU  281  O   PHE A  57     5535   7897  12582  -1379    316  -2256       O  
ATOM    282  CB  PHE A  57      38.021   7.234 104.718  1.00 60.82           C  
ANISOU  282  CB  PHE A  57     5174   6634  11300  -1393    456  -1799       C  
ATOM    283  CG  PHE A  57      38.494   7.977 103.506  1.00 57.92           C  
ANISOU  283  CG  PHE A  57     4901   6134  10973  -1574    846  -1886       C  
ATOM    284  CD1 PHE A  57      38.024   7.641 102.249  1.00 59.93           C  
ANISOU  284  CD1 PHE A  57     5293   6297  11180  -1504   1034  -1728       C  
ATOM    285  CD2 PHE A  57      39.392   9.024 103.624  1.00 61.46           C  
ANISOU  285  CD2 PHE A  57     5324   6532  11495  -1821   1037  -2138       C  
ATOM    286  CE1 PHE A  57      38.446   8.327 101.131  1.00 54.95           C  
ANISOU  286  CE1 PHE A  57     4802   5514  10563  -1668   1412  -1813       C  
ATOM    287  CE2 PHE A  57      39.818   9.713 102.507  1.00 67.34           C  
ANISOU  287  CE2 PHE A  57     6201   7127  12257  -1993   1438  -2228       C  
ATOM    288  CZ  PHE A  57      39.343   9.363 101.259  1.00 64.33           C  
ANISOU  288  CZ  PHE A  57     5988   6642  11813  -1912   1629  -2063       C  
ATOM    289  N   VAL A  58      40.654   6.663 106.225  1.00 65.01           N  
ANISOU  289  N   VAL A  58     5120   7494  12087  -1440     18  -2344       N  
ATOM    290  CA  VAL A  58      42.078   6.907 106.449  1.00 68.06           C  
ANISOU  290  CA  VAL A  58     5233   7975  12652  -1564     -4  -2678       C  
ATOM    291  C   VAL A  58      42.842   5.591 106.529  1.00 64.94           C  
ANISOU  291  C   VAL A  58     4594   7740  12340  -1359   -262  -2751       C  
ATOM    292  O   VAL A  58      43.835   5.383 105.822  1.00 67.27           O  
ANISOU  292  O   VAL A  58     4695   8069  12796  -1413   -129  -2932       O  
ATOM    293  CB  VAL A  58      42.288   7.749 107.718  1.00 70.12           C  
ANISOU  293  CB  VAL A  58     5461   8260  12920  -1682   -171  -2858       C  
ATOM    294  CG1 VAL A  58      43.771   7.873 108.029  1.00 71.35           C  
ANISOU  294  CG1 VAL A  58     5287   8543  13281  -1778   -251  -3229       C  
ATOM    295  CG2 VAL A  58      41.645   9.111 107.559  1.00 65.85           C  
ANISOU  295  CG2 VAL A  58     5193   7530  12295  -1913    133  -2809       C  
ATOM    296  N   VAL A  59      42.398   4.684 107.403  1.00 58.72           N  
ANISOU  296  N   VAL A  59     3833   7033  11445  -1122   -620  -2626       N  
ATOM    297  CA  VAL A  59      43.138   3.442 107.611  1.00 62.15           C  
ANISOU  297  CA  VAL A  59     4079   7599  11934   -912   -885  -2705       C  
ATOM    298  C   VAL A  59      43.227   2.639 106.318  1.00 73.85           C  
ANISOU  298  C   VAL A  59     5564   9059  13437   -860   -691  -2593       C  
ATOM    299  O   VAL A  59      44.265   2.041 106.014  1.00 76.15           O  
ANISOU  299  O   VAL A  59     5631   9428  13874   -816   -730  -2773       O  
ATOM    300  CB  VAL A  59      42.496   2.616 108.740  1.00 58.47           C  
ANISOU  300  CB  VAL A  59     3734   7177  11305   -663  -1267  -2565       C  
ATOM    301  CG1 VAL A  59      43.050   1.204 108.727  1.00 61.17           C  
ANISOU  301  CG1 VAL A  59     3975   7611  11656   -426  -1484  -2578       C  
ATOM    302  CG2 VAL A  59      42.730   3.280 110.083  1.00 60.82           C  
ANISOU  302  CG2 VAL A  59     3991   7513  11607   -691  -1529  -2755       C  
ATOM    303  N   ALA A  60      42.143   2.605 105.539  1.00 72.83           N  
ANISOU  303  N   ALA A  60     5684   8819  13170   -860   -492  -2312       N  
ATOM    304  CA  ALA A  60      42.162   1.842 104.292  1.00 66.83           C  
ANISOU  304  CA  ALA A  60     4958   8026  12408   -814   -323  -2202       C  
ATOM    305  C   ALA A  60      43.127   2.443 103.274  1.00 74.00           C  
ANISOU  305  C   ALA A  60     5728   8881  13508  -1013     -6  -2424       C  
ATOM    306  O   ALA A  60      43.787   1.709 102.529  1.00 78.93           O  
ANISOU  306  O   ALA A  60     6236   9525  14227   -976     53  -2492       O  
ATOM    307  CB  ALA A  60      40.754   1.758 103.705  1.00 53.52           C  
ANISOU  307  CB  ALA A  60     3566   6233  10536   -767   -199  -1880       C  
ATOM    308  N   LEU A  61      43.224   3.774 103.224  1.00 74.29           N  
ANISOU  308  N   LEU A  61     5790   8832  13603  -1238    225  -2553       N  
ATOM    309  CA  LEU A  61      44.092   4.407 102.235  1.00 75.02           C  
ANISOU  309  CA  LEU A  61     5796   8840  13866  -1453    588  -2779       C  
ATOM    310  C   LEU A  61      45.562   4.260 102.604  1.00 81.11           C  
ANISOU  310  C   LEU A  61     6198   9737  14883  -1500    500  -3147       C  
ATOM    311  O   LEU A  61      46.396   3.945 101.746  1.00 85.13           O  
ANISOU  311  O   LEU A  61     6559  10230  15556  -1552    685  -3317       O  
ATOM    312  CB  LEU A  61      43.729   5.882 102.080  1.00 74.55           C  
ANISOU  312  CB  LEU A  61     5929   8630  13769  -1690    895  -2809       C  
ATOM    313  CG  LEU A  61      42.461   6.194 101.283  1.00 76.60           C  
ANISOU  313  CG  LEU A  61     6551   8716  13838  -1680   1106  -2514       C  
ATOM    314  CD1 LEU A  61      42.342   7.691 101.055  1.00 77.89           C  
ANISOU  314  CD1 LEU A  61     6920   8703  13970  -1929   1458  -2596       C  
ATOM    315  CD2 LEU A  61      42.453   5.443  99.961  1.00 76.43           C  
ANISOU  315  CD2 LEU A  61     6593   8628  13818  -1611   1274  -2421       C  
ATOM    316  N   VAL A  62      45.903   4.488 103.873  1.00 82.30           N  
ANISOU  316  N   VAL A  62     6188  10008  15074  -1481    217  -3298       N  
ATOM    317  CA  VAL A  62      47.291   4.351 104.302  1.00 85.94           C  
ANISOU  317  CA  VAL A  62     6268  10604  15782  -1501     88  -3679       C  
ATOM    318  C   VAL A  62      47.729   2.892 104.243  1.00 84.12           C  
ANISOU  318  C   VAL A  62     5880  10483  15599  -1246   -164  -3670       C  
ATOM    319  O   VAL A  62      48.776   2.563 103.672  1.00 83.22           O  
ANISOU  319  O   VAL A  62     5510  10404  15707  -1279    -63  -3923       O  
ATOM    320  CB  VAL A  62      47.478   4.933 105.713  1.00 83.89           C  
ANISOU  320  CB  VAL A  62     5900  10442  15531  -1521   -196  -3838       C  
ATOM    321  CG1 VAL A  62      48.884   4.656 106.212  1.00 82.74           C  
ANISOU  321  CG1 VAL A  62     5337  10457  15643  -1488   -400  -4243       C  
ATOM    322  CG2 VAL A  62      47.186   6.423 105.712  1.00 82.56           C  
ANISOU  322  CG2 VAL A  62     5881  10153  15335  -1811     94  -3886       C  
ATOM    323  N   GLY A  63      46.938   1.996 104.838  1.00 79.56           N  
ANISOU  323  N   GLY A  63     5462   9951  14815   -996   -478  -3397       N  
ATOM    324  CA  GLY A  63      47.317   0.591 104.860  1.00 78.59           C  
ANISOU  324  CA  GLY A  63     5236   9920  14705   -749   -721  -3381       C  
ATOM    325  C   GLY A  63      47.465  -0.002 103.472  1.00 79.93           C  
ANISOU  325  C   GLY A  63     5422  10020  14929   -772   -452  -3315       C  
ATOM    326  O   GLY A  63      48.459  -0.666 103.169  1.00 83.41           O  
ANISOU  326  O   GLY A  63     5612  10526  15554   -712   -489  -3524       O  
ATOM    327  N   ASN A  64      46.476   0.230 102.605  1.00 79.64           N  
ANISOU  327  N   ASN A  64     5678   9845  14737   -850   -189  -3038       N  
ATOM    328  CA  ASN A  64      46.528  -0.355 101.269  1.00 74.47           C  
ANISOU  328  CA  ASN A  64     5079   9107  14110   -862     51  -2962       C  
ATOM    329  C   ASN A  64      47.632   0.264 100.422  1.00 75.28           C  
ANISOU  329  C   ASN A  64     4970   9148  14484  -1082    388  -3294       C  
ATOM    330  O   ASN A  64      48.144  -0.384  99.503  1.00 82.24           O  
ANISOU  330  O   ASN A  64     5772   9996  15478  -1075    528  -3360       O  
ATOM    331  CB  ASN A  64      45.173  -0.205 100.578  1.00 71.96           C  
ANISOU  331  CB  ASN A  64     5128   8654  13562   -878    223  -2613       C  
ATOM    332  CG  ASN A  64      44.135  -1.155 101.129  1.00 69.70           C  
ANISOU  332  CG  ASN A  64     5033   8419  13030   -655    -57  -2300       C  
ATOM    333  OD1 ASN A  64      44.376  -2.357 101.231  1.00 69.09           O  
ANISOU  333  OD1 ASN A  64     4898   8420  12932   -486   -245  -2264       O  
ATOM    334  ND2 ASN A  64      42.976  -0.623 101.502  1.00 75.15           N  
ANISOU  334  ND2 ASN A  64     5956   9059  13540   -658    -69  -2091       N  
ATOM    335  N   THR A  65      48.018   1.508 100.713  1.00 76.97           N  
ANISOU  335  N   THR A  65     5099   9337  14811  -1293    545  -3522       N  
ATOM    336  CA  THR A  65      49.176   2.074 100.031  1.00 78.99           C  
ANISOU  336  CA  THR A  65     5127   9540  15346  -1517    878  -3900       C  
ATOM    337  C   THR A  65      50.466   1.447 100.537  1.00 82.68           C  
ANISOU  337  C   THR A  65     5164  10177  16075  -1431    651  -4246       C  
ATOM    338  O   THR A  65      51.389   1.193  99.754  1.00 84.51           O  
ANISOU  338  O   THR A  65     5188  10384  16540  -1509    861  -4501       O  
ATOM    339  CB  THR A  65      49.215   3.589 100.215  1.00 78.04           C  
ANISOU  339  CB  THR A  65     5057   9338  15258  -1785   1136  -4059       C  
ATOM    340  OG1 THR A  65      48.052   4.178  99.617  1.00 77.53           O  
ANISOU  340  OG1 THR A  65     5401   9096  14960  -1855   1377  -3759       O  
ATOM    341  CG2 THR A  65      50.460   4.160  99.554  1.00 83.83           C  
ANISOU  341  CG2 THR A  65     5552  10012  16287  -2038   1515  -4493       C  
ATOM    342  N   LEU A  66      50.547   1.192 101.844  1.00 84.29           N  
ANISOU  342  N   LEU A  66     5234  10546  16248  -1263    221  -4278       N  
ATOM    343  CA  LEU A  66      51.724   0.538 102.401  1.00 86.72           C  
ANISOU  343  CA  LEU A  66     5140  11022  16788  -1128    -57  -4610       C  
ATOM    344  C   LEU A  66      51.893  -0.863 101.830  1.00 86.50           C  
ANISOU  344  C   LEU A  66     5081  11018  16768   -919   -151  -4513       C  
ATOM    345  O   LEU A  66      53.021  -1.320 101.605  1.00100.17           O  
ANISOU  345  O   LEU A  66     6465  12818  18776   -889   -163  -4848       O  
ATOM    346  CB  LEU A  66      51.616   0.485 103.922  1.00 87.29           C  
ANISOU  346  CB  LEU A  66     5159  11239  16769   -948   -527  -4621       C  
ATOM    347  CG  LEU A  66      51.770   1.821 104.650  1.00 89.71           C  
ANISOU  347  CG  LEU A  66     5391  11561  17133  -1153   -496  -4826       C  
ATOM    348  CD1 LEU A  66      51.824   1.607 106.152  1.00 91.12           C  
ANISOU  348  CD1 LEU A  66     5489  11886  17246   -941  -1006  -4886       C  
ATOM    349  CD2 LEU A  66      53.007   2.563 104.170  1.00 95.81           C  
ANISOU  349  CD2 LEU A  66     5811  12341  18251  -1413   -197  -5298       C  
ATOM    350  N   VAL A  67      50.782  -1.566 101.602  1.00 84.50           N  
ANISOU  350  N   VAL A  67     5168  10703  16234   -774   -215  -4090       N  
ATOM    351  CA  VAL A  67      50.857  -2.902 101.014  1.00 87.44           C  
ANISOU  351  CA  VAL A  67     5537  11074  16612   -591   -277  -4000       C  
ATOM    352  C   VAL A  67      51.518  -2.843  99.643  1.00 88.31           C  
ANISOU  352  C   VAL A  67     5529  11077  16950   -771    130  -4184       C  
ATOM    353  O   VAL A  67      52.414  -3.635  99.330  1.00 89.64           O  
ANISOU  353  O   VAL A  67     5432  11297  17330   -687     92  -4404       O  
ATOM    354  CB  VAL A  67      49.458  -3.536 100.931  1.00 82.32           C  
ANISOU  354  CB  VAL A  67     5294  10361  15622   -455   -356  -3525       C  
ATOM    355  CG1 VAL A  67      49.516  -4.811 100.107  1.00 72.57           C  
ANISOU  355  CG1 VAL A  67     4080   9099  14396   -325   -335  -3430       C  
ATOM    356  CG2 VAL A  67      48.914  -3.813 102.320  1.00 80.90           C  
ANISOU  356  CG2 VAL A  67     5220  10282  15236   -254   -762  -3380       C  
ATOM    357  N   CYS A  68      51.071  -1.914  98.795  1.00 88.04           N  
ANISOU  357  N   CYS A  68     5710  10878  16865  -1013    532  -4098       N  
ATOM    358  CA  CYS A  68      51.683  -1.769  97.479  1.00 98.70           C  
ANISOU  358  CA  CYS A  68     6999  12090  18413  -1204    964  -4284       C  
ATOM    359  C   CYS A  68      53.145  -1.367  97.592  1.00109.62           C  
ANISOU  359  C   CYS A  68     7940  13539  20171  -1343   1070  -4809       C  
ATOM    360  O   CYS A  68      53.969  -1.773  96.762  1.00110.66           O  
ANISOU  360  O   CYS A  68     7880  13624  20540  -1404   1285  -5046       O  
ATOM    361  CB  CYS A  68      50.913  -0.742  96.651  1.00101.21           C  
ANISOU  361  CB  CYS A  68     7672  12201  18583  -1425   1369  -4117       C  
ATOM    362  SG  CYS A  68      49.209  -1.210  96.291  1.00 98.60           S  
ANISOU  362  SG  CYS A  68     7825  11782  17856  -1273   1289  -3552       S  
ATOM    363  N   LEU A  69      53.487  -0.573  98.606  1.00113.27           N  
ANISOU  363  N   LEU A  69     8228  14110  20702  -1402    928  -5014       N  
ATOM    364  CA  LEU A  69      54.878  -0.177  98.798  1.00114.14           C  
ANISOU  364  CA  LEU A  69     7880  14304  21184  -1534   1002  -5552       C  
ATOM    365  C   LEU A  69      55.720  -1.335  99.320  1.00114.24           C  
ANISOU  365  C   LEU A  69     7514  14505  21388  -1268    610  -5770       C  
ATOM    366  O   LEU A  69      56.832  -1.572  98.836  1.00119.27           O  
ANISOU  366  O   LEU A  69     7796  15164  22355  -1330    755  -6162       O  
ATOM    367  CB  LEU A  69      54.958   1.011  99.753  1.00117.82           C  
ANISOU  367  CB  LEU A  69     8272  14831  21665  -1674    950  -5719       C  
ATOM    368  CG  LEU A  69      54.501   2.374  99.230  1.00121.12           C  
ANISOU  368  CG  LEU A  69     8962  15055  22003  -1995   1416  -5690       C  
ATOM    369  CD1 LEU A  69      54.158   3.290 100.393  1.00123.10           C  
ANISOU  369  CD1 LEU A  69     9245  15381  22146  -2042   1225  -5681       C  
ATOM    370  CD2 LEU A  69      55.572   3.003  98.354  1.00130.31           C  
ANISOU  370  CD2 LEU A  69     9915  16109  23486  -2303   1922  -6147       C  
ATOM    371  N   ALA A  70      55.208  -2.065 100.315  1.00109.13           N  
ANISOU  371  N   ALA A  70     6946  13986  20532   -965    120  -5534       N  
ATOM    372  CA  ALA A  70      55.986  -3.145 100.913  1.00111.48           C  
ANISOU  372  CA  ALA A  70     6923  14459  20974   -675   -289  -5740       C  
ATOM    373  C   ALA A  70      56.372  -4.194  99.876  1.00109.54           C  
ANISOU  373  C   ALA A  70     6596  14167  20856   -604   -152  -5762       C  
ATOM    374  O   ALA A  70      57.471  -4.759  99.934  1.00116.06           O  
ANISOU  374  O   ALA A  70     7021  15110  21968   -494   -282  -6128       O  
ATOM    375  CB  ALA A  70      55.199  -3.789 102.053  1.00109.12           C  
ANISOU  375  CB  ALA A  70     6847  14252  20363   -364   -783  -5423       C  
ATOM    376  N   VAL A  71      55.484  -4.476  98.923  1.00 99.31           N  
ANISOU  376  N   VAL A  71     5670  12709  19355   -657     99  -5384       N  
ATOM    377  CA  VAL A  71      55.827  -5.439  97.881  1.00100.67           C  
ANISOU  377  CA  VAL A  71     5786  12824  19640   -612    257  -5393       C  
ATOM    378  C   VAL A  71      56.751  -4.821  96.839  1.00108.58           C  
ANISOU  378  C   VAL A  71     6563  13716  20978   -913    746  -5770       C  
ATOM    379  O   VAL A  71      57.611  -5.511  96.281  1.00118.61           O  
ANISOU  379  O   VAL A  71     7559  15006  22503   -878    821  -6014       O  
ATOM    380  CB  VAL A  71      54.550  -6.003  97.234  1.00 92.98           C  
ANISOU  380  CB  VAL A  71     5284  11718  18327   -555    335  -4871       C  
ATOM    381  CG1 VAL A  71      54.912  -6.900  96.062  1.00 93.69           C  
ANISOU  381  CG1 VAL A  71     5329  11730  18538   -546    548  -4886       C  
ATOM    382  CG2 VAL A  71      53.731  -6.766  98.263  1.00 92.10           C  
ANISOU  382  CG2 VAL A  71     5370  11712  17913   -257   -127  -4549       C  
ATOM    383  N   TRP A  72      56.599  -3.525  96.560  1.00107.56           N  
ANISOU  383  N   TRP A  72     6555  13461  20854  -1214   1104  -5836       N  
ATOM    384  CA  TRP A  72      57.465  -2.885  95.576  1.00114.64           C  
ANISOU  384  CA  TRP A  72     7284  14220  22054  -1525   1621  -6214       C  
ATOM    385  C   TRP A  72      58.897  -2.759  96.083  1.00121.57           C  
ANISOU  385  C   TRP A  72     7582  15260  23350  -1559   1543  -6807       C  
ATOM    386  O   TRP A  72      59.848  -2.926  95.311  1.00123.93           O  
ANISOU  386  O   TRP A  72     7610  15508  23971  -1688   1837  -7166       O  
ATOM    387  CB  TRP A  72      56.908  -1.515  95.199  1.00114.99           C  
ANISOU  387  CB  TRP A  72     7651  14077  21963  -1826   2028  -6133       C  
ATOM    388  CG  TRP A  72      57.797  -0.756  94.262  1.00123.35           C  
ANISOU  388  CG  TRP A  72     8587  14969  23311  -2169   2601  -6549       C  
ATOM    389  CD1 TRP A  72      58.106  -1.089  92.976  1.00125.30           C  
ANISOU  389  CD1 TRP A  72     8905  15023  23681  -2292   3014  -6630       C  
ATOM    390  CD2 TRP A  72      58.484   0.472  94.534  1.00129.83           C  
ANISOU  390  CD2 TRP A  72     9211  15776  24343  -2450   2863  -6975       C  
ATOM    391  NE1 TRP A  72      58.948  -0.149  92.432  1.00129.68           N  
ANISOU  391  NE1 TRP A  72     9334  15429  24508  -2635   3533  -7088       N  
ATOM    392  CE2 TRP A  72      59.194   0.820  93.368  1.00133.82           C  
ANISOU  392  CE2 TRP A  72     9688  16065  25092  -2742   3456  -7310       C  
ATOM    393  CE3 TRP A  72      58.570   1.309  95.651  1.00134.11           C  
ANISOU  393  CE3 TRP A  72     9609  16456  24890  -2495   2670  -7115       C  
ATOM    394  CZ2 TRP A  72      59.978   1.968  93.286  1.00143.16           C  
ANISOU  394  CZ2 TRP A  72    10708  17168  26517  -3082   3877  -7788       C  
ATOM    395  CZ3 TRP A  72      59.348   2.448  95.567  1.00142.32           C  
ANISOU  395  CZ3 TRP A  72    10468  17431  26175  -2829   3066  -7580       C  
ATOM    396  CH2 TRP A  72      60.042   2.767  94.393  1.00147.86           C  
ANISOU  396  CH2 TRP A  72    11149  17918  27112  -3123   3672  -7916       C  
ATOM    397  N   ARG A  73      59.074  -2.458  97.370  1.00123.71           N  
ANISOU  397  N   ARG A  73     7650  15723  23629  -1445   1153  -6937       N  
ATOM    398  CA  ARG A  73      60.417  -2.316  97.925  1.00132.06           C  
ANISOU  398  CA  ARG A  73     8134  16956  25086  -1456   1030  -7526       C  
ATOM    399  C   ARG A  73      61.080  -3.674  98.135  1.00139.62           C  
ANISOU  399  C   ARG A  73     8765  18081  26203  -1125    650  -7668       C  
ATOM    400  O   ARG A  73      62.138  -3.959  97.562  1.00150.25           O  
ANISOU  400  O   ARG A  73     9727  19445  27915  -1190    831  -8082       O  
ATOM    401  CB  ARG A  73      60.370  -1.518  99.232  1.00132.33           C  
ANISOU  401  CB  ARG A  73     8080  17135  25063  -1440    726  -7621       C  
ATOM    402  CG  ARG A  73      60.151  -0.022  99.029  1.00135.27           C  
ANISOU  402  CG  ARG A  73     8617  17369  25411  -1822   1159  -7680       C  
ATOM    403  CD  ARG A  73      61.169   0.809  99.805  1.00146.48           C  
ANISOU  403  CD  ARG A  73     9580  18938  27137  -1964   1106  -8228       C  
ATOM    404  NE  ARG A  73      61.147   2.219  99.417  1.00150.19           N  
ANISOU  404  NE  ARG A  73    10178  19251  27637  -2376   1625  -8367       N  
ATOM    405  CZ  ARG A  73      60.493   3.171 100.076  1.00148.09           C  
ANISOU  405  CZ  ARG A  73    10142  18970  27155  -2477   1591  -8205       C  
ATOM    406  NH1 ARG A  73      59.802   2.870 101.167  1.00144.81           N  
ANISOU  406  NH1 ARG A  73     9856  18688  26479  -2203   1061  -7889       N  
ATOM    407  NH2 ARG A  73      60.533   4.426  99.647  1.00148.10           N  
ANISOU  407  NH2 ARG A  73    10266  18811  27195  -2858   2105  -8368       N  
ATOM    408  N   ASN A  74      60.471  -4.525  98.956  1.00134.50           N  
ANISOU  408  N   ASN A  74     8276  17549  25281   -766    135  -7337       N  
ATOM    409  CA  ASN A  74      61.056  -5.814  99.310  1.00129.45           C  
ANISOU  409  CA  ASN A  74     7370  17074  24743   -405   -279  -7456       C  
ATOM    410  C   ASN A  74      60.880  -6.784  98.147  1.00127.06           C  
ANISOU  410  C   ASN A  74     7211  16653  24412   -369    -55  -7240       C  
ATOM    411  O   ASN A  74      59.756  -7.185  97.825  1.00121.76           O  
ANISOU  411  O   ASN A  74     7005  15869  23390   -313    -28  -6724       O  
ATOM    412  CB  ASN A  74      60.403  -6.351 100.580  1.00126.43           C  
ANISOU  412  CB  ASN A  74     7187  16815  24035    -47   -862  -7166       C  
ATOM    413  CG  ASN A  74      61.148  -7.528 101.161  1.00130.97           C  
ANISOU  413  CG  ASN A  74     7466  17574  24723    352  -1340  -7376       C  
ATOM    414  OD1 ASN A  74      61.819  -8.268 100.442  1.00134.07           O  
ANISOU  414  OD1 ASN A  74     7622  17980  25337    412  -1241  -7554       O  
ATOM    415  ND2 ASN A  74      61.038  -7.709 102.471  1.00131.66           N  
ANISOU  415  ND2 ASN A  74     7581  17793  24649    639  -1863  -7361       N  
ATOM    416  N   HIS A  75      61.993  -7.161  97.511  1.00133.05           N  
ANISOU  416  N   HIS A  75     7560  17442  25552   -405    111  -7650       N  
ATOM    417  CA  HIS A  75      61.944  -8.053  96.359  1.00132.30           C  
ANISOU  417  CA  HIS A  75     7566  17233  25470   -391    356  -7489       C  
ATOM    418  C   HIS A  75      61.699  -9.509  96.732  1.00131.47           C  
ANISOU  418  C   HIS A  75     7530  17246  25177     37    -96  -7228       C  
ATOM    419  O   HIS A  75      61.275 -10.289  95.871  1.00126.61           O  
ANISOU  419  O   HIS A  75     7143  16524  24437     74     66  -6932       O  
ATOM    420  CB  HIS A  75      63.238  -7.932  95.555  1.00144.87           C  
ANISOU  420  CB  HIS A  75     8690  18806  27550   -592    720  -8039       C  
ATOM    421  CG  HIS A  75      63.507  -6.543  95.067  1.00148.94           C  
ANISOU  421  CG  HIS A  75     9174  19167  28249  -1038   1244  -8316       C  
ATOM    422  ND1 HIS A  75      63.070  -6.089  93.842  1.00146.40           N  
ANISOU  422  ND1 HIS A  75     9201  18567  27857  -1353   1821  -8145       N  
ATOM    423  CD2 HIS A  75      64.153  -5.503  95.647  1.00154.13           C  
ANISOU  423  CD2 HIS A  75     9523  19900  29138  -1218   1285  -8754       C  
ATOM    424  CE1 HIS A  75      63.442  -4.831  93.685  1.00148.51           C  
ANISOU  424  CE1 HIS A  75     9398  18734  28297  -1706   2212  -8465       C  
ATOM    425  NE2 HIS A  75      64.101  -4.452  94.765  1.00154.38           N  
ANISOU  425  NE2 HIS A  75     9730  19694  29232  -1643   1905  -8839       N  
ATOM    426  N   HIS A  76      61.959  -9.897  97.981  1.00135.50           N  
ANISOU  426  N   HIS A  76     7871  17961  25654    365   -648  -7338       N  
ATOM    427  CA  HIS A  76      61.637 -11.250  98.413  1.00136.01           C  
ANISOU  427  CA  HIS A  76     8084  18112  25484    786  -1075  -7065       C  
ATOM    428  C   HIS A  76      60.144 -11.444  98.610  1.00136.94           C  
ANISOU  428  C   HIS A  76     8803  18123  25104    841  -1147  -6445       C  
ATOM    429  O   HIS A  76      59.673 -12.586  98.613  1.00135.75           O  
ANISOU  429  O   HIS A  76     8879  17979  24723   1109  -1339  -6136       O  
ATOM    430  CB  HIS A  76      62.372 -11.590  99.712  1.00138.15           C  
ANISOU  430  CB  HIS A  76     8038  18608  25847   1143  -1654  -7389       C  
ATOM    431  CG  HIS A  76      63.858 -11.451  99.620  1.00146.02           C  
ANISOU  431  CG  HIS A  76     8392  19739  27348   1129  -1646  -8044       C  
ATOM    432  ND1 HIS A  76      64.484 -10.226  99.537  1.00149.33           N  
ANISOU  432  ND1 HIS A  76     8494  20161  28085    790  -1375  -8466       N  
ATOM    433  CD2 HIS A  76      64.842 -12.381  99.600  1.00151.44           C  
ANISOU  433  CD2 HIS A  76     8687  20566  28288   1413  -1867  -8370       C  
ATOM    434  CE1 HIS A  76      65.790 -10.409  99.469  1.00157.80           C  
ANISOU  434  CE1 HIS A  76     8985  21372  29599    852  -1424  -9041       C  
ATOM    435  NE2 HIS A  76      66.034 -11.706  99.506  1.00159.26           N  
ANISOU  435  NE2 HIS A  76     9106  21646  29757   1238  -1733  -8995       N  
ATOM    436  N   MET A  77      59.402 -10.354  98.775  1.00139.10           N  
ANISOU  436  N   MET A  77     9330  18303  25218    594   -986  -6276       N  
ATOM    437  CA  MET A  77      57.962 -10.380  98.975  1.00129.66           C  
ANISOU  437  CA  MET A  77     8676  17009  23581    612  -1027  -5729       C  
ATOM    438  C   MET A  77      57.180 -10.483  97.672  1.00124.19           C  
ANISOU  438  C   MET A  77     8311  16122  22753    411   -594  -5385       C  
ATOM    439  O   MET A  77      55.945 -10.519  97.713  1.00124.24           O  
ANISOU  439  O   MET A  77     8754  16042  22409    414   -599  -4942       O  
ATOM    440  CB  MET A  77      57.531  -9.127  99.740  1.00125.97           C  
ANISOU  440  CB  MET A  77     8316  16534  23014    449  -1052  -5720       C  
ATOM    441  CG  MET A  77      57.943  -9.131 101.202  1.00126.06           C  
ANISOU  441  CG  MET A  77     8150  16722  23026    700  -1561  -5928       C  
ATOM    442  SD  MET A  77      57.104  -7.859 102.167  1.00122.76           S  
ANISOU  442  SD  MET A  77     7987  16278  22377    553  -1625  -5767       S  
ATOM    443  CE  MET A  77      55.569  -8.682 102.568  1.00116.90           C  
ANISOU  443  CE  MET A  77     7828  15463  21126    769  -1831  -5146       C  
ATOM    444  N   ARG A  78      57.857 -10.519  96.524  1.00115.01           N  
ANISOU  444  N   ARG A  78     6954  14882  21864    239   -220  -5592       N  
ATOM    445  CA  ARG A  78      57.179 -10.549  95.228  1.00104.93           C  
ANISOU  445  CA  ARG A  78     5997  13400  20470     41    207  -5302       C  
ATOM    446  C   ARG A  78      56.825 -11.985  94.838  1.00101.70           C  
ANISOU  446  C   ARG A  78     5741  13000  19899    289     88  -5014       C  
ATOM    447  O   ARG A  78      57.263 -12.522  93.821  1.00105.53           O  
ANISOU  447  O   ARG A  78     6136  13420  20540    248    340  -5082       O  
ATOM    448  CB  ARG A  78      58.044  -9.880  94.166  1.00107.40           C  
ANISOU  448  CB  ARG A  78     6082  13591  21133   -277    704  -5661       C  
ATOM    449  CG  ARG A  78      58.375  -8.425  94.461  1.00109.96           C  
ANISOU  449  CG  ARG A  78     6285  13884  21610   -552    889  -5952       C  
ATOM    450  CD  ARG A  78      59.064  -7.756  93.280  1.00113.59           C  
ANISOU  450  CD  ARG A  78     6631  14164  22364   -901   1468  -6262       C  
ATOM    451  NE  ARG A  78      59.447  -6.380  93.583  1.00116.70           N  
ANISOU  451  NE  ARG A  78     6900  14531  22911  -1169   1668  -6577       N  
ATOM    452  CZ  ARG A  78      59.957  -5.533  92.694  1.00119.95           C  
ANISOU  452  CZ  ARG A  78     7278  14758  23539  -1516   2212  -6862       C  
ATOM    453  NH1 ARG A  78      60.144  -5.919  91.440  1.00121.76           N  
ANISOU  453  NH1 ARG A  78     7599  14803  23860  -1636   2605  -6868       N  
ATOM    454  NH2 ARG A  78      60.276  -4.298  93.059  1.00122.87           N  
ANISOU  454  NH2 ARG A  78     7547  15114  24025  -1750   2382  -7145       N  
ATOM    455  N   THR A  79      56.013 -12.605  95.686  1.00 97.12           N  
ANISOU  455  N   THR A  79     5410  12494  18997    546   -288  -4695       N  
ATOM    456  CA  THR A  79      55.482 -13.932  95.421  1.00 94.20           C  
ANISOU  456  CA  THR A  79     5260  12123  18409    780   -401  -4375       C  
ATOM    457  C   THR A  79      54.172 -13.821  94.644  1.00 98.10           C  
ANISOU  457  C   THR A  79     6217  12445  18613    618   -139  -3942       C  
ATOM    458  O   THR A  79      53.586 -12.744  94.512  1.00 97.51           O  
ANISOU  458  O   THR A  79     6322  12267  18462    379     51  -3858       O  
ATOM    459  CB  THR A  79      55.268 -14.700  96.725  1.00 94.19           C  
ANISOU  459  CB  THR A  79     5325  12264  18198   1141   -912  -4270       C  
ATOM    460  OG1 THR A  79      54.174 -14.124  97.450  1.00 89.53           O  
ANISOU  460  OG1 THR A  79     5069  11639  17311   1092  -1022  -3998       O  
ATOM    461  CG2 THR A  79      56.519 -14.647  97.585  1.00101.18           C  
ANISOU  461  CG2 THR A  79     5768  13318  19358   1312  -1215  -4725       C  
ATOM    462  N   VAL A  80      53.714 -14.959  94.116  1.00 94.81           N  
ANISOU  462  N   VAL A  80     5991  11999  18032    765   -135  -3677       N  
ATOM    463  CA  VAL A  80      52.456 -14.961  93.374  1.00 86.93           C  
ANISOU  463  CA  VAL A  80     5418  10851  16761    638     78  -3287       C  
ATOM    464  C   VAL A  80      51.305 -14.523  94.268  1.00 79.57           C  
ANISOU  464  C   VAL A  80     4785   9925  15524    651   -120  -3023       C  
ATOM    465  O   VAL A  80      50.414 -13.778  93.839  1.00 75.67           O  
ANISOU  465  O   VAL A  80     4554   9306  14890    450     81  -2835       O  
ATOM    466  CB  VAL A  80      52.193 -16.348  92.765  1.00 84.29           C  
ANISOU  466  CB  VAL A  80     5218  10506  16302    821     83  -3072       C  
ATOM    467  CG1 VAL A  80      50.798 -16.401  92.163  1.00 79.87           C  
ANISOU  467  CG1 VAL A  80     5097   9812  15438    720    232  -2679       C  
ATOM    468  CG2 VAL A  80      53.244 -16.679  91.723  1.00 86.97           C  
ANISOU  468  CG2 VAL A  80     5294  10809  16943    770    353  -3314       C  
ATOM    469  N   THR A  81      51.295 -14.984  95.520  1.00 79.76           N  
ANISOU  469  N   THR A  81     4786  10083  15436    899   -513  -3011       N  
ATOM    470  CA  THR A  81      50.231 -14.592  96.438  1.00 75.35           C  
ANISOU  470  CA  THR A  81     4507   9524  14597    912   -691  -2779       C  
ATOM    471  C   THR A  81      50.244 -13.090  96.683  1.00 79.55           C  
ANISOU  471  C   THR A  81     4984  10023  15217    675   -581  -2912       C  
ATOM    472  O   THR A  81      49.200 -12.431  96.637  1.00 79.95           O  
ANISOU  472  O   THR A  81     5313   9989  15077    536   -476  -2686       O  
ATOM    473  CB  THR A  81      50.364 -15.344  97.760  1.00 76.75           C  
ANISOU  473  CB  THR A  81     4675   9829  14658   1229  -1120  -2788       C  
ATOM    474  OG1 THR A  81      50.289 -16.753  97.520  1.00 85.82           O  
ANISOU  474  OG1 THR A  81     5920  10990  15697   1463  -1200  -2642       O  
ATOM    475  CG2 THR A  81      49.257 -14.932  98.715  1.00 74.07           C  
ANISOU  475  CG2 THR A  81     4635   9473  14036   1227  -1271  -2558       C  
ATOM    476  N   ASN A  82      51.426 -12.530  96.953  1.00 83.46           N  
ANISOU  476  N   ASN A  82     5115  10589  16007    635   -603  -3296       N  
ATOM    477  CA  ASN A  82      51.508 -11.106  97.255  1.00 81.64           C  
ANISOU  477  CA  ASN A  82     4820  10335  15864    417   -498  -3448       C  
ATOM    478  C   ASN A  82      51.185 -10.245  96.041  1.00 87.58           C  
ANISOU  478  C   ASN A  82     5706  10913  16657    113    -44  -3396       C  
ATOM    479  O   ASN A  82      50.672  -9.131  96.196  1.00 95.31           O  
ANISOU  479  O   ASN A  82     6824  11830  17560    -55     69  -3342       O  
ATOM    480  CB  ASN A  82      52.891 -10.769  97.810  1.00 84.02           C  
ANISOU  480  CB  ASN A  82     4673  10759  16490    445   -625  -3912       C  
ATOM    481  CG  ASN A  82      53.126 -11.369  99.185  1.00 93.57           C  
ANISOU  481  CG  ASN A  82     5800  12128  17624    757  -1116  -3975       C  
ATOM    482  OD1 ASN A  82      52.213 -11.921  99.799  1.00 82.52           O  
ANISOU  482  OD1 ASN A  82     4707  10731  15917    926  -1335  -3665       O  
ATOM    483  ND2 ASN A  82      54.357 -11.265  99.675  1.00105.04           N  
ANISOU  483  ND2 ASN A  82     6845  13705  19359    839  -1289  -4397       N  
ATOM    484  N   TYR A  83      51.483 -10.725  94.830  1.00 82.70           N  
ANISOU  484  N   TYR A  83     5067  10205  16151     48    225  -3414       N  
ATOM    485  CA  TYR A  83      51.070  -9.982  93.644  1.00 76.95           C  
ANISOU  485  CA  TYR A  83     4544   9281  15412   -213    651  -3332       C  
ATOM    486  C   TYR A  83      49.553  -9.915  93.548  1.00 75.30           C  
ANISOU  486  C   TYR A  83     4769   8990  14852   -208    638  -2911       C  
ATOM    487  O   TYR A  83      48.994  -8.903  93.111  1.00 76.90           O  
ANISOU  487  O   TYR A  83     5175   9065  14980   -391    873  -2833       O  
ATOM    488  CB  TYR A  83      51.654 -10.616  92.382  1.00 79.52           C  
ANISOU  488  CB  TYR A  83     4793   9512  15907   -266    932  -3423       C  
ATOM    489  CG  TYR A  83      53.036 -10.127  92.023  1.00 89.74           C  
ANISOU  489  CG  TYR A  83     5719  10792  17588   -424   1171  -3877       C  
ATOM    490  CD1 TYR A  83      53.705  -9.215  92.828  1.00 95.52           C  
ANISOU  490  CD1 TYR A  83     6188  11607  18499   -504   1106  -4190       C  
ATOM    491  CD2 TYR A  83      53.667 -10.570  90.869  1.00 88.91           C  
ANISOU  491  CD2 TYR A  83     5526  10581  17675   -508   1481  -4010       C  
ATOM    492  CE1 TYR A  83      54.969  -8.766  92.498  1.00102.49           C  
ANISOU  492  CE1 TYR A  83     6711  12475  19754   -668   1344  -4645       C  
ATOM    493  CE2 TYR A  83      54.929 -10.126  90.530  1.00 98.22           C  
ANISOU  493  CE2 TYR A  83     6360  11735  19226   -673   1733  -4455       C  
ATOM    494  CZ  TYR A  83      55.575  -9.224  91.347  1.00107.10           C  
ANISOU  494  CZ  TYR A  83     7209  12950  20534   -756   1665  -4782       C  
ATOM    495  OH  TYR A  83      56.833  -8.782  91.010  1.00119.53           O  
ANISOU  495  OH  TYR A  83     8419  14500  22498   -938   1935  -5263       O  
ATOM    496  N   PHE A  84      48.868 -10.986  93.957  1.00 70.96           N  
ANISOU  496  N   PHE A  84     4367   8512  14082      7    372  -2654       N  
ATOM    497  CA  PHE A  84      47.410 -10.955  93.994  1.00 62.75           C  
ANISOU  497  CA  PHE A  84     3702   7413  12725     17    334  -2291       C  
ATOM    498  C   PHE A  84      46.904 -10.104  95.151  1.00 67.55           C  
ANISOU  498  C   PHE A  84     4374   8079  13215     14    155  -2251       C  
ATOM    499  O   PHE A  84      45.889  -9.409  95.020  1.00 70.72           O  
ANISOU  499  O   PHE A  84     5029   8397  13444    -80    248  -2057       O  
ATOM    500  CB  PHE A  84      46.854 -12.374  94.090  1.00 64.27           C  
ANISOU  500  CB  PHE A  84     4030   7658  12732    227    141  -2062       C  
ATOM    501  CG  PHE A  84      46.837 -13.106  92.781  1.00 68.31           C  
ANISOU  501  CG  PHE A  84     4616   8073  13264    202    364  -1984       C  
ATOM    502  CD1 PHE A  84      46.243 -12.539  91.668  1.00 65.60           C  
ANISOU  502  CD1 PHE A  84     4488   7564  12873     23    663  -1872       C  
ATOM    503  CD2 PHE A  84      47.412 -14.360  92.665  1.00 66.89           C  
ANISOU  503  CD2 PHE A  84     4308   7965  13144    376    272  -2024       C  
ATOM    504  CE1 PHE A  84      46.222 -13.205  90.461  1.00 58.47           C  
ANISOU  504  CE1 PHE A  84     3673   6561  11983      2    869  -1805       C  
ATOM    505  CE2 PHE A  84      47.395 -15.033  91.459  1.00 62.87           C  
ANISOU  505  CE2 PHE A  84     3874   7364  12651    353    489  -1952       C  
ATOM    506  CZ  PHE A  84      46.798 -14.454  90.355  1.00 60.26           C  
ANISOU  506  CZ  PHE A  84     3762   6860  12274    157    789  -1844       C  
ATOM    507  N   LEU A  85      47.591 -10.152  96.296  1.00 67.94           N  
ANISOU  507  N   LEU A  85     4197   8268  13351    130   -113  -2438       N  
ATOM    508  CA  LEU A  85      47.195  -9.308  97.417  1.00 67.35           C  
ANISOU  508  CA  LEU A  85     4172   8241  13176    120   -275  -2422       C  
ATOM    509  C   LEU A  85      47.317  -7.833  97.065  1.00 74.28           C  
ANISOU  509  C   LEU A  85     5026   9036  14161   -127     -6  -2548       C  
ATOM    510  O   LEU A  85      46.509  -7.016  97.521  1.00 73.24           O  
ANISOU  510  O   LEU A  85     5075   8880  13874   -188    -14  -2410       O  
ATOM    511  CB  LEU A  85      48.041  -9.630  98.651  1.00 68.28           C  
ANISOU  511  CB  LEU A  85     4040   8516  13388    300   -617  -2641       C  
ATOM    512  CG  LEU A  85      47.821 -10.989  99.318  1.00 64.16           C  
ANISOU  512  CG  LEU A  85     3600   8075  12702    583   -933  -2505       C  
ATOM    513  CD1 LEU A  85      48.628 -11.091 100.605  1.00 68.25           C  
ANISOU  513  CD1 LEU A  85     3907   8728  13297    771  -1289  -2740       C  
ATOM    514  CD2 LEU A  85      46.344 -11.224  99.587  1.00 61.75           C  
ANISOU  514  CD2 LEU A  85     3677   7715  12068    613   -971  -2137       C  
ATOM    515  N   VAL A  86      48.319  -7.471  96.261  1.00 81.30           N  
ANISOU  515  N   VAL A  86     5702   9875  15314   -274    253  -2818       N  
ATOM    516  CA  VAL A  86      48.425  -6.089  95.809  1.00 74.58           C  
ANISOU  516  CA  VAL A  86     4871   8915  14549   -525    570  -2941       C  
ATOM    517  C   VAL A  86      47.242  -5.730  94.921  1.00 66.23           C  
ANISOU  517  C   VAL A  86     4193   7698  13274   -613    801  -2637       C  
ATOM    518  O   VAL A  86      46.723  -4.608  94.978  1.00 64.41           O  
ANISOU  518  O   VAL A  86     4116   7402  12955   -740    931  -2583       O  
ATOM    519  CB  VAL A  86      49.766  -5.861  95.091  1.00 72.97           C  
ANISOU  519  CB  VAL A  86     4372   8671  14683   -677    842  -3321       C  
ATOM    520  CG1 VAL A  86      49.762  -4.518  94.381  1.00 72.00           C  
ANISOU  520  CG1 VAL A  86     4364   8385  14609   -955   1256  -3416       C  
ATOM    521  CG2 VAL A  86      50.921  -5.943  96.080  1.00 76.00           C  
ANISOU  521  CG2 VAL A  86     4346   9227  15302   -601    598  -3674       C  
ATOM    522  N   ASN A  87      46.793  -6.673  94.087  1.00 65.41           N  
ANISOU  522  N   ASN A  87     4244   7532  13077   -539    848  -2444       N  
ATOM    523  CA  ASN A  87      45.610  -6.429  93.268  1.00 59.40           C  
ANISOU  523  CA  ASN A  87     3837   6634  12100   -586   1016  -2160       C  
ATOM    524  C   ASN A  87      44.377  -6.237  94.139  1.00 62.19           C  
ANISOU  524  C   ASN A  87     4392   7043  12196   -493    783  -1902       C  
ATOM    525  O   ASN A  87      43.495  -5.432  93.816  1.00 69.75           O  
ANISOU  525  O   ASN A  87     5579   7911  13010   -567    913  -1752       O  
ATOM    526  CB  ASN A  87      45.398  -7.583  92.287  1.00 59.34           C  
ANISOU  526  CB  ASN A  87     3930   6567  12049   -511   1075  -2021       C  
ATOM    527  CG  ASN A  87      44.379  -7.255  91.212  1.00 57.72           C  
ANISOU  527  CG  ASN A  87     4046   6178  11705   -579   1307  -1819       C  
ATOM    528  OD1 ASN A  87      44.428  -6.189  90.598  1.00 63.21           O  
ANISOU  528  OD1 ASN A  87     4833   6715  12470   -740   1613  -1915       O  
ATOM    529  ND2 ASN A  87      43.443  -8.170  90.987  1.00 60.64           N  
ANISOU  529  ND2 ASN A  87     4595   6554  11889   -454   1175  -1559       N  
ATOM    530  N   LEU A  88      44.297  -6.974  95.250  1.00 59.93           N  
ANISOU  530  N   LEU A  88     4030   6897  11844   -326    448  -1857       N  
ATOM    531  CA  LEU A  88      43.197  -6.785  96.189  1.00 56.69           C  
ANISOU  531  CA  LEU A  88     3800   6532  11206   -251    247  -1648       C  
ATOM    532  C   LEU A  88      43.225  -5.386  96.789  1.00 64.52           C  
ANISOU  532  C   LEU A  88     4765   7527  12222   -370    292  -1744       C  
ATOM    533  O   LEU A  88      42.175  -4.762  96.986  1.00 66.95           O  
ANISOU  533  O   LEU A  88     5282   7800  12358   -391    301  -1564       O  
ATOM    534  CB  LEU A  88      43.274  -7.848  97.284  1.00 57.19           C  
ANISOU  534  CB  LEU A  88     3795   6729  11206    -56    -87  -1623       C  
ATOM    535  CG  LEU A  88      42.166  -7.977  98.330  1.00 59.87           C  
ANISOU  535  CG  LEU A  88     4330   7112  11307     43   -300  -1415       C  
ATOM    536  CD1 LEU A  88      40.800  -8.096  97.677  1.00 52.45           C  
ANISOU  536  CD1 LEU A  88     3678   6078  10173     21   -192  -1146       C  
ATOM    537  CD2 LEU A  88      42.449  -9.183  99.214  1.00 58.11           C  
ANISOU  537  CD2 LEU A  88     4048   6996  11037    244   -583  -1423       C  
ATOM    538  N   SER A  89      44.423  -4.879  97.094  1.00 72.83           N  
ANISOU  538  N   SER A  89     5548   8626  13496   -450    322  -2042       N  
ATOM    539  CA  SER A  89      44.543  -3.520  97.607  1.00 71.48           C  
ANISOU  539  CA  SER A  89     5341   8454  13363   -592    396  -2161       C  
ATOM    540  C   SER A  89      44.128  -2.487  96.569  1.00 67.47           C  
ANISOU  540  C   SER A  89     5021   7779  12836   -776    758  -2120       C  
ATOM    541  O   SER A  89      43.576  -1.439  96.924  1.00 63.76           O  
ANISOU  541  O   SER A  89     4665   7265  12298   -858    815  -2081       O  
ATOM    542  CB  SER A  89      45.976  -3.265  98.070  1.00 80.11           C  
ANISOU  542  CB  SER A  89     6079   9632  14726   -650    365  -2534       C  
ATOM    543  OG  SER A  89      46.261  -3.999  99.247  1.00 83.51           O  
ANISOU  543  OG  SER A  89     6363  10216  15152   -459    -11  -2581       O  
ATOM    544  N   LEU A  90      44.379  -2.759  95.286  1.00 66.36           N  
ANISOU  544  N   LEU A  90     4923   7515  12775   -837   1019  -2150       N  
ATOM    545  CA  LEU A  90      43.930  -1.833  94.253  1.00 61.20           C  
ANISOU  545  CA  LEU A  90     4492   6658  12103   -989   1384  -2122       C  
ATOM    546  C   LEU A  90      42.410  -1.769  94.195  1.00 62.35           C  
ANISOU  546  C   LEU A  90     4933   6757  11998   -895   1307  -1794       C  
ATOM    547  O   LEU A  90      41.834  -0.683  94.069  1.00 62.86           O  
ANISOU  547  O   LEU A  90     5167   6715  12003   -987   1476  -1756       O  
ATOM    548  CB  LEU A  90      44.497  -2.233  92.891  1.00 54.89           C  
ANISOU  548  CB  LEU A  90     3705   5717  11434  -1061   1688  -2226       C  
ATOM    549  CG  LEU A  90      46.002  -2.097  92.663  1.00 64.93           C  
ANISOU  549  CG  LEU A  90     4697   6976  12995  -1204   1888  -2603       C  
ATOM    550  CD1 LEU A  90      46.356  -2.613  91.280  1.00 71.11           C  
ANISOU  550  CD1 LEU A  90     5551   7595  13874  -1258   2195  -2659       C  
ATOM    551  CD2 LEU A  90      46.445  -0.652  92.830  1.00 62.88           C  
ANISOU  551  CD2 LEU A  90     4418   6641  12834  -1425   2152  -2842       C  
ATOM    552  N   ALA A  91      41.743  -2.922  94.284  1.00 63.05           N  
ANISOU  552  N   ALA A  91     5089   6922  11943   -717   1067  -1572       N  
ATOM    553  CA  ALA A  91      40.285  -2.925  94.329  1.00 56.37           C  
ANISOU  553  CA  ALA A  91     4484   6051  10882   -624    970  -1293       C  
ATOM    554  C   ALA A  91      39.768  -2.247  95.591  1.00 67.02           C  
ANISOU  554  C   ALA A  91     5842   7483  12140   -605    790  -1248       C  
ATOM    555  O   ALA A  91      38.758  -1.532  95.554  1.00 75.94           O  
ANISOU  555  O   ALA A  91     7143   8536  13176   -613    844  -1118       O  
ATOM    556  CB  ALA A  91      39.759  -4.356  94.236  1.00 49.08           C  
ANISOU  556  CB  ALA A  91     3621   5199   9829   -463    767  -1105       C  
ATOM    557  N   ASP A  92      40.438  -2.466  96.724  1.00 70.43           N  
ANISOU  557  N   ASP A  92     6088   8062  12610   -572    576  -1361       N  
ATOM    558  CA  ASP A  92      40.009  -1.819  97.960  1.00 68.73           C  
ANISOU  558  CA  ASP A  92     5881   7910  12322   -561    416  -1339       C  
ATOM    559  C   ASP A  92      40.202  -0.313  97.891  1.00 70.13           C  
ANISOU  559  C   ASP A  92     6055   7989  12601   -741    642  -1480       C  
ATOM    560  O   ASP A  92      39.367   0.451  98.392  1.00 72.12           O  
ANISOU  560  O   ASP A  92     6428   8208  12765   -755    627  -1385       O  
ATOM    561  CB  ASP A  92      40.771  -2.398  99.149  1.00 75.55           C  
ANISOU  561  CB  ASP A  92     6547   8935  13225   -478    144  -1457       C  
ATOM    562  CG  ASP A  92      40.339  -3.802  99.474  1.00 85.60           C  
ANISOU  562  CG  ASP A  92     7881  10274  14369   -293    -79  -1302       C  
ATOM    563  OD1 ASP A  92      39.203  -4.157  99.104  1.00 85.85           O  
ANISOU  563  OD1 ASP A  92     8127  10253  14239   -241    -61  -1079       O  
ATOM    564  OD2 ASP A  92      41.119  -4.542 100.108  1.00 92.91           O  
ANISOU  564  OD2 ASP A  92     8639  11292  15369   -199   -270  -1424       O  
ATOM    565  N   VAL A  93      41.301   0.133  97.282  1.00 70.69           N  
ANISOU  565  N   VAL A  93     5996   8004  12860   -894    879  -1721       N  
ATOM    566  CA  VAL A  93      41.534   1.565  97.145  1.00 68.78           C  
ANISOU  566  CA  VAL A  93     5790   7647  12694  -1099   1156  -1876       C  
ATOM    567  C   VAL A  93      40.507   2.187  96.210  1.00 64.87           C  
ANISOU  567  C   VAL A  93     5600   6966  12081  -1138   1411  -1704       C  
ATOM    568  O   VAL A  93      40.019   3.297  96.453  1.00 63.47           O  
ANISOU  568  O   VAL A  93     5564   6704  11847  -1231   1530  -1687       O  
ATOM    569  CB  VAL A  93      42.968   1.826  96.660  1.00 69.83           C  
ANISOU  569  CB  VAL A  93     5724   7749  13058  -1267   1395  -2205       C  
ATOM    570  CG1 VAL A  93      43.050   3.190  95.996  1.00 68.51           C  
ANISOU  570  CG1 VAL A  93     5725   7390  12918  -1499   1819  -2328       C  
ATOM    571  CG2 VAL A  93      43.934   1.730  97.822  1.00 73.77           C  
ANISOU  571  CG2 VAL A  93     5910   8423  13698  -1264   1156  -2431       C  
ATOM    572  N   LEU A  94      40.178   1.495  95.116  1.00 66.10           N  
ANISOU  572  N   LEU A  94     5874   7044  12198  -1068   1505  -1582       N  
ATOM    573  CA  LEU A  94      39.176   2.012  94.190  1.00 67.81           C  
ANISOU  573  CA  LEU A  94     6386   7079  12299  -1078   1731  -1417       C  
ATOM    574  C   LEU A  94      37.852   2.273  94.897  1.00 65.89           C  
ANISOU  574  C   LEU A  94     6255   6863  11916   -965   1531  -1197       C  
ATOM    575  O   LEU A  94      37.218   3.312  94.681  1.00 64.80           O  
ANISOU  575  O   LEU A  94     6330   6582  11709  -1033   1721  -1142       O  
ATOM    576  CB  LEU A  94      38.987   1.036  93.030  1.00 70.36           C  
ANISOU  576  CB  LEU A  94     6789   7340  12605   -990   1796  -1313       C  
ATOM    577  CG  LEU A  94      37.817   1.291  92.077  1.00 63.88           C  
ANISOU  577  CG  LEU A  94     6267   6354  11649   -944   1958  -1106       C  
ATOM    578  CD1 LEU A  94      37.989   2.587  91.286  1.00 68.88           C  
ANISOU  578  CD1 LEU A  94     7183   6763  12226  -1126   2398  -1195       C  
ATOM    579  CD2 LEU A  94      37.634   0.099  91.149  1.00 59.37           C  
ANISOU  579  CD2 LEU A  94     5719   5768  11070   -834   1934  -1002       C  
ATOM    580  N   ALA A  95      37.420   1.342  95.752  1.00 69.94           N  
ANISOU  580  N   ALA A  95     6662   7542  12369   -798   1170  -1075       N  
ATOM    581  CA  ALA A  95      36.162   1.528  96.468  1.00 65.49           C  
ANISOU  581  CA  ALA A  95     6192   7000  11691   -691    995   -890       C  
ATOM    582  C   ALA A  95      36.285   2.597  97.548  1.00 64.20           C  
ANISOU  582  C   ALA A  95     5992   6850  11549   -788    981   -988       C  
ATOM    583  O   ALA A  95      35.350   3.378  97.764  1.00 63.03           O  
ANISOU  583  O   ALA A  95     5980   6615  11354   -787   1027   -889       O  
ATOM    584  CB  ALA A  95      35.702   0.206  97.080  1.00 65.83           C  
ANISOU  584  CB  ALA A  95     6193   7197  11625   -512    668   -751       C  
ATOM    585  N   THR A  96      37.423   2.643  98.243  1.00 68.55           N  
ANISOU  585  N   THR A  96     6355   7505  12188   -870    914  -1191       N  
ATOM    586  CA  THR A  96      37.580   3.596  99.339  1.00 69.32           C  
ANISOU  586  CA  THR A  96     6403   7624  12311   -968    873  -1300       C  
ATOM    587  C   THR A  96      37.654   5.031  98.830  1.00 69.33           C  
ANISOU  587  C   THR A  96     6562   7443  12337  -1175   1224  -1395       C  
ATOM    588  O   THR A  96      36.974   5.921  99.354  1.00 73.20           O  
ANISOU  588  O   THR A  96     7188   7857  12767  -1218   1255  -1342       O  
ATOM    589  CB  THR A  96      38.828   3.260 100.150  1.00 68.18           C  
ANISOU  589  CB  THR A  96     5999   7631  12274   -999    706  -1517       C  
ATOM    590  OG1 THR A  96      38.693   1.951 100.715  1.00 70.69           O  
ANISOU  590  OG1 THR A  96     6247   8091  12521   -801    394  -1413       O  
ATOM    591  CG2 THR A  96      39.017   4.278 101.262  1.00 61.56           C  
ANISOU  591  CG2 THR A  96     5110   6810  11472  -1116    660  -1652       C  
ATOM    592  N   ALA A  97      38.481   5.276  97.815  1.00 68.87           N  
ANISOU  592  N   ALA A  97     6525   7290  12351  -1311   1519  -1542       N  
ATOM    593  CA  ALA A  97      38.676   6.640  97.334  1.00 71.02           C  
ANISOU  593  CA  ALA A  97     7014   7367  12603  -1528   1901  -1654       C  
ATOM    594  C   ALA A  97      37.399   7.206  96.723  1.00 69.49           C  
ANISOU  594  C   ALA A  97     7194   6978  12233  -1482   2061  -1424       C  
ATOM    595  O   ALA A  97      37.000   8.337  97.027  1.00 69.91           O  
ANISOU  595  O   ALA A  97     7476   6899  12188  -1575   2198  -1412       O  
ATOM    596  CB  ALA A  97      39.820   6.680  96.323  1.00 69.41           C  
ANISOU  596  CB  ALA A  97     6783   7087  12503  -1676   2217  -1869       C  
ATOM    597  N   ILE A  98      36.744   6.436  95.859  1.00 68.72           N  
ANISOU  597  N   ILE A  98     7182   6846  12081  -1330   2042  -1241       N  
ATOM    598  CA  ILE A  98      35.615   6.944  95.084  1.00 67.23           C  
ANISOU  598  CA  ILE A  98     7378   6448  11720  -1272   2208  -1035       C  
ATOM    599  C   ILE A  98      34.284   6.627  95.751  1.00 64.44           C  
ANISOU  599  C   ILE A  98     7004   6146  11336  -1074   1917   -813       C  
ATOM    600  O   ILE A  98      33.478   7.523  96.015  1.00 65.26           O  
ANISOU  600  O   ILE A  98     7365   6104  11327  -1058   1969   -717       O  
ATOM    601  CB  ILE A  98      35.667   6.369  93.653  1.00 66.50           C  
ANISOU  601  CB  ILE A  98     7429   6258  11579  -1233   2386   -978       C  
ATOM    602  CG1 ILE A  98      36.942   6.813  92.939  1.00 64.68           C  
ANISOU  602  CG1 ILE A  98     7266   5932  11376  -1440   2749  -1216       C  
ATOM    603  CG2 ILE A  98      34.441   6.794  92.867  1.00 62.81           C  
ANISOU  603  CG2 ILE A  98     7404   5576  10883  -1119   2480   -742       C  
ATOM    604  CD1 ILE A  98      36.979   8.294  92.632  1.00 71.34           C  
ANISOU  604  CD1 ILE A  98     8530   6540  12037  -1600   3113  -1271       C  
ATOM    605  N   CYS A  99      34.036   5.347  96.035  1.00 67.76           N  
ANISOU  605  N   CYS A  99     7149   6757  11840   -909   1614   -734       N  
ATOM    606  CA  CYS A  99      32.713   4.915  96.471  1.00 66.73           C  
ANISOU  606  CA  CYS A  99     6995   6664  11697   -714   1377   -525       C  
ATOM    607  C   CYS A  99      32.428   5.277  97.926  1.00 58.57           C  
ANISOU  607  C   CYS A  99     5857   5716  10680   -703   1188   -542       C  
ATOM    608  O   CYS A  99      31.306   5.682  98.252  1.00 59.20           O  
ANISOU  608  O   CYS A  99     6046   5706  10742   -617   1152   -404       O  
ATOM    609  CB  CYS A  99      32.560   3.409  96.255  1.00 64.06           C  
ANISOU  609  CB  CYS A  99     6469   6487  11384   -550   1140   -442       C  
ATOM    610  SG  CYS A  99      32.906   2.845  94.568  1.00 62.21           S  
ANISOU  610  SG  CYS A  99     6341   6151  11145   -562   1350   -426       S  
ATOM    611  N   LEU A 100      33.412   5.137  98.816  1.00 52.90           N  
ANISOU  611  N   LEU A 100     4951   5151   9998   -781   1064   -709       N  
ATOM    612  CA  LEU A 100      33.156   5.393 100.233  1.00 54.43           C  
ANISOU  612  CA  LEU A 100     5070   5422  10190   -768    872   -724       C  
ATOM    613  C   LEU A 100      32.616   6.793 100.488  1.00 61.98           C  
ANISOU  613  C   LEU A 100     6246   6182  11122   -873   1059   -717       C  
ATOM    614  O   LEU A 100      31.590   6.920 101.178  1.00 65.01           O  
ANISOU  614  O   LEU A 100     6671   6533  11498   -774    949   -596       O  
ATOM    615  CB  LEU A 100      34.428   5.139 101.048  1.00 57.87           C  
ANISOU  615  CB  LEU A 100     5304   6015  10667   -850    732   -926       C  
ATOM    616  CG  LEU A 100      34.303   5.279 102.570  1.00 53.60           C  
ANISOU  616  CG  LEU A 100     4688   5558  10121   -837    504   -964       C  
ATOM    617  CD1 LEU A 100      35.330   4.407 103.274  1.00 56.23           C  
ANISOU  617  CD1 LEU A 100     4815   6074  10475   -799    261  -1093       C  
ATOM    618  CD2 LEU A 100      34.451   6.730 103.011  1.00 57.01           C  
ANISOU  618  CD2 LEU A 100     5221   5862  10577  -1037    672  -1088       C  
ATOM    619  N   PRO A 101      33.226   7.868  99.984  1.00 58.83           N  
ANISOU  619  N   PRO A 101     6046   5627  10681  -1064   1354   -838       N  
ATOM    620  CA  PRO A 101      32.649   9.201 100.231  1.00 52.60           C  
ANISOU  620  CA  PRO A 101     5594   4611   9780  -1129   1534   -808       C  
ATOM    621  C   PRO A 101      31.228   9.341  99.716  1.00 50.53           C  
ANISOU  621  C   PRO A 101     5622   4164   9415   -919   1566   -568       C  
ATOM    622  O   PRO A 101      30.401  10.001 100.353  1.00 53.89           O  
ANISOU  622  O   PRO A 101     6242   4467   9766   -832   1547   -492       O  
ATOM    623  CB  PRO A 101      33.611  10.147  99.503  1.00 56.42           C  
ANISOU  623  CB  PRO A 101     6291   4960  10186  -1347   1872   -969       C  
ATOM    624  CG  PRO A 101      34.872   9.364  99.319  1.00 58.69           C  
ANISOU  624  CG  PRO A 101     6234   5444  10622  -1431   1823  -1148       C  
ATOM    625  CD  PRO A 101      34.442   7.941  99.155  1.00 58.24           C  
ANISOU  625  CD  PRO A 101     5951   5546  10630  -1216   1560  -1008       C  
ATOM    626  N   ALA A 102      30.918   8.738  98.563  1.00 55.91           N  
ANISOU  626  N   ALA A 102     6359   4811  10072   -799   1600   -453       N  
ATOM    627  CA  ALA A 102      29.554   8.796  98.048  1.00 53.95           C  
ANISOU  627  CA  ALA A 102     6384   4412   9703   -523   1559   -236       C  
ATOM    628  C   ALA A 102      28.589   8.047  98.957  1.00 57.73           C  
ANISOU  628  C   ALA A 102     6593   5076  10266   -316   1245   -127       C  
ATOM    629  O   ALA A 102      27.483   8.530  99.232  1.00 60.50           O  
ANISOU  629  O   ALA A 102     7131   5397  10459    -84   1176    -19       O  
ATOM    630  CB  ALA A 102      29.505   8.236  96.628  1.00 58.24           C  
ANISOU  630  CB  ALA A 102     7043   4913  10172   -435   1619   -157       C  
ATOM    631  N   SER A 103      28.985   6.862  99.427  1.00 52.86           N  
ANISOU  631  N   SER A 103     5548   4703   9833   -370   1046   -163       N  
ATOM    632  CA  SER A 103      28.126   6.091 100.319  1.00 49.41           C  
ANISOU  632  CA  SER A 103     4895   4482   9395   -191    772    -71       C  
ATOM    633  C   SER A 103      27.861   6.841 101.618  1.00 56.03           C  
ANISOU  633  C   SER A 103     5805   5309  10174   -202    739   -107       C  
ATOM    634  O   SER A 103      26.770   6.743 102.190  1.00 58.07           O  
ANISOU  634  O   SER A 103     6078   5638  10348    -10    627    -10       O  
ATOM    635  CB  SER A 103      28.760   4.728 100.606  1.00 47.01           C  
ANISOU  635  CB  SER A 103     4219   4393   9248   -250    590   -117       C  
ATOM    636  OG  SER A 103      27.997   3.997 101.548  1.00 44.18           O  
ANISOU  636  OG  SER A 103     3792   4200   8796   -101    363    -42       O  
ATOM    637  N   LEU A 104      28.852   7.593 102.103  1.00 60.25           N  
ANISOU  637  N   LEU A 104     6379   5752  10761   -440    850   -269       N  
ATOM    638  CA  LEU A 104      28.668   8.338 103.344  1.00 56.51           C  
ANISOU  638  CA  LEU A 104     6008   5247  10215   -468    821   -317       C  
ATOM    639  C   LEU A 104      27.579   9.397 103.203  1.00 57.38           C  
ANISOU  639  C   LEU A 104     6499   5182  10120   -286    956   -205       C  
ATOM    640  O   LEU A 104      26.739   9.553 104.097  1.00 51.77           O  
ANISOU  640  O   LEU A 104     5834   4512   9325   -145    872   -147       O  
ATOM    641  CB  LEU A 104      29.991   8.977 103.766  1.00 53.53           C  
ANISOU  641  CB  LEU A 104     5595   4799   9944   -782    917   -551       C  
ATOM    642  CG  LEU A 104      29.949   9.989 104.908  1.00 46.90           C  
ANISOU  642  CG  LEU A 104     4942   3868   9008   -861    937   -632       C  
ATOM    643  CD1 LEU A 104      29.369   9.353 106.161  1.00 47.51           C  
ANISOU  643  CD1 LEU A 104     4903   4111   9037   -710    665   -569       C  
ATOM    644  CD2 LEU A 104      31.345  10.526 105.172  1.00 47.95           C  
ANISOU  644  CD2 LEU A 104     5000   4013   9204  -1158   1004   -891       C  
ATOM    645  N   LEU A 105      27.572  10.136 102.088  1.00 52.24           N  
ANISOU  645  N   LEU A 105     6156   4317   9374   -270   1176   -180       N  
ATOM    646  CA  LEU A 105      26.537  11.149 101.894  1.00 55.00           C  
ANISOU  646  CA  LEU A 105     6904   4484   9509    -37   1277    -79       C  
ATOM    647  C   LEU A 105      25.162  10.520 101.698  1.00 60.36           C  
ANISOU  647  C   LEU A 105     7484   5309  10140    317   1083     72       C  
ATOM    648  O   LEU A 105      24.161  11.043 102.198  1.00 61.56           O  
ANISOU  648  O   LEU A 105     7762   5440  10189    533   1057    122       O  
ATOM    649  CB  LEU A 105      26.887  12.055 100.713  1.00 54.25           C  
ANISOU  649  CB  LEU A 105     7245   4087   9283    -81   1556    -90       C  
ATOM    650  CG  LEU A 105      27.605  13.360 101.078  1.00 63.43           C  
ANISOU  650  CG  LEU A 105     8713   5075  10313   -324   1794   -220       C  
ATOM    651  CD1 LEU A 105      29.108  13.159 101.216  1.00 74.41           C  
ANISOU  651  CD1 LEU A 105     9847   6557  11869   -719   1878   -425       C  
ATOM    652  CD2 LEU A 105      27.285  14.472 100.084  1.00 67.05           C  
ANISOU  652  CD2 LEU A 105     9715   5327  10433   -195   1981   -156       C  
ATOM    653  N   VAL A 106      25.088   9.396 100.980  1.00 62.03           N  
ANISOU  653  N   VAL A 106     7456   5673  10440    376    954    124       N  
ATOM    654  CA  VAL A 106      23.792   8.761 100.755  1.00 52.68           C  
ANISOU  654  CA  VAL A 106     6139   4640   9236    679    773    225       C  
ATOM    655  C   VAL A 106      23.220   8.252 102.069  1.00 51.46           C  
ANISOU  655  C   VAL A 106     5716   4678   9159    700    646    218       C  
ATOM    656  O   VAL A 106      22.012   8.343 102.318  1.00 48.02           O  
ANISOU  656  O   VAL A 106     5272   4330   8645    916    582    249       O  
ATOM    657  CB  VAL A 106      23.914   7.634  99.714  1.00 47.24           C  
ANISOU  657  CB  VAL A 106     5267   4060   8622    696    675    264       C  
ATOM    658  CG1 VAL A 106      22.574   6.939  99.539  1.00 36.62           C  
ANISOU  658  CG1 VAL A 106     3780   2989   7147    905    459    310       C  
ATOM    659  CG2 VAL A 106      24.411   8.194  98.392  1.00 55.00           C  
ANISOU  659  CG2 VAL A 106     6599   4809   9489    689    837    273       C  
ATOM    660  N   ASP A 107      24.079   7.715 102.934  1.00 54.56           N  
ANISOU  660  N   ASP A 107     5913   5160   9656    463    605    154       N  
ATOM    661  CA  ASP A 107      23.622   7.185 104.209  1.00 57.17           C  
ANISOU  661  CA  ASP A 107     6075   5629  10018    470    504    149       C  
ATOM    662  C   ASP A 107      23.240   8.284 105.189  1.00 56.47           C  
ANISOU  662  C   ASP A 107     6211   5423   9821    499    602    122       C  
ATOM    663  O   ASP A 107      22.618   7.987 106.215  1.00 50.47           O  
ANISOU  663  O   ASP A 107     5384   4739   9052    544    566    124       O  
ATOM    664  CB  ASP A 107      24.692   6.279 104.807  1.00 58.89           C  
ANISOU  664  CB  ASP A 107     6083   5953  10339    257    392     85       C  
ATOM    665  CG  ASP A 107      24.752   4.937 104.116  1.00 69.61           C  
ANISOU  665  CG  ASP A 107     7195   7456  11796    278    279    129       C  
ATOM    666  OD1 ASP A 107      23.674   4.375 103.826  1.00 71.09           O  
ANISOU  666  OD1 ASP A 107     7399   7768  11844    380    231    196       O  
ATOM    667  OD2 ASP A 107      25.869   4.457 103.842  1.00 76.47           O  
ANISOU  667  OD2 ASP A 107     7942   8353  12759    131    235     70       O  
ATOM    668  N   ILE A 108      23.612   9.531 104.915  1.00 58.40           N  
ANISOU  668  N   ILE A 108     6756   5462   9973    460    753     89       N  
ATOM    669  CA  ILE A 108      23.189  10.641 105.760  1.00 55.51           C  
ANISOU  669  CA  ILE A 108     6649   4957   9485    509    865     67       C  
ATOM    670  C   ILE A 108      21.911  11.276 105.237  1.00 59.43           C  
ANISOU  670  C   ILE A 108     7320   5379   9881    840    923    138       C  
ATOM    671  O   ILE A 108      20.920  11.393 105.960  1.00 54.50           O  
ANISOU  671  O   ILE A 108     6672   4799   9237   1006    925    146       O  
ATOM    672  CB  ILE A 108      24.313  11.694 105.864  1.00 52.86           C  
ANISOU  672  CB  ILE A 108     6575   4416   9094    264   1016    -34       C  
ATOM    673  CG1 ILE A 108      25.523  11.145 106.619  1.00 59.85           C  
ANISOU  673  CG1 ILE A 108     7244   5401  10096    -33    911   -158       C  
ATOM    674  CG2 ILE A 108      23.782  12.955 106.530  1.00 48.73           C  
ANISOU  674  CG2 ILE A 108     6398   3706   8412    346   1161    -43       C  
ATOM    675  CD1 ILE A 108      26.729  12.059 106.566  1.00 53.29           C  
ANISOU  675  CD1 ILE A 108     6575   4401   9271   -321   1059   -315       C  
ATOM    676  N   THR A 109      21.924  11.695 103.974  1.00 60.27           N  
ANISOU  676  N   THR A 109     7620   5362   9919    955    972    175       N  
ATOM    677  CA  THR A 109      20.788  12.368 103.362  1.00 58.38           C  
ANISOU  677  CA  THR A 109     7593   5080   9507   1296    957    218       C  
ATOM    678  C   THR A 109      19.782  11.421 102.723  1.00 59.39           C  
ANISOU  678  C   THR A 109     7439   5493   9632   1498    729    237       C  
ATOM    679  O   THR A 109      18.621  11.809 102.538  1.00 56.42           O  
ANISOU  679  O   THR A 109     7117   5192   9129   1774    631    211       O  
ATOM    680  CB  THR A 109      21.274  13.358 102.301  1.00 60.53           C  
ANISOU  680  CB  THR A 109     8312   5110   9576   1305   1077    228       C  
ATOM    681  OG1 THR A 109      21.813  12.635 101.187  1.00 63.83           O  
ANISOU  681  OG1 THR A 109     8655   5559  10038   1233   1031    252       O  
ATOM    682  CG2 THR A 109      22.347  14.269 102.878  1.00 61.77           C  
ANISOU  682  CG2 THR A 109     8747   5021   9702   1013   1319    164       C  
ATOM    683  N   GLU A 110      20.189  10.199 102.382  1.00 56.39           N  
ANISOU  683  N   GLU A 110     6765   5280   9382   1355    631    250       N  
ATOM    684  CA  GLU A 110      19.328   9.274 101.646  1.00 55.98           C  
ANISOU  684  CA  GLU A 110     6505   5491   9274   1484    433    245       C  
ATOM    685  C   GLU A 110      18.879   9.891 100.323  1.00 62.24           C  
ANISOU  685  C   GLU A 110     7586   6193   9870   1750    352    247       C  
ATOM    686  O   GLU A 110      17.737   9.724  99.891  1.00 59.67           O  
ANISOU  686  O   GLU A 110     7198   6036   9436   1994    179    192       O  
ATOM    687  CB  GLU A 110      18.123   8.851 102.488  1.00 54.72           C  
ANISOU  687  CB  GLU A 110     6110   5563   9117   1562    364    187       C  
ATOM    688  CG  GLU A 110      18.484   8.271 103.845  1.00 57.96           C  
ANISOU  688  CG  GLU A 110     6328   6011   9685   1332    442    183       C  
ATOM    689  CD  GLU A 110      19.235   6.958 103.749  1.00 67.62           C  
ANISOU  689  CD  GLU A 110     7344   7349  10998   1094    372    204       C  
ATOM    690  OE1 GLU A 110      19.173   6.306 102.685  1.00 69.99           O  
ANISOU  690  OE1 GLU A 110     7597   7762  11234   1098    267    213       O  
ATOM    691  OE2 GLU A 110      19.888   6.578 104.742  1.00 73.02           O  
ANISOU  691  OE2 GLU A 110     7946   7998  11802    924    412    204       O  
ATOM    692  N   SER A 111      19.796  10.611  99.677  1.00 71.23           N  
ANISOU  692  N   SER A 111     9068   7048  10949   1694    486    287       N  
ATOM    693  CA  SER A 111      19.552  11.249  98.391  1.00 68.03           C  
ANISOU  693  CA  SER A 111     9025   6481  10343   1905    417    293       C  
ATOM    694  C   SER A 111      20.862  11.293  97.616  1.00 63.68           C  
ANISOU  694  C   SER A 111     8712   5710   9772   1679    612    339       C  
ATOM    695  O   SER A 111      21.945  11.117  98.182  1.00 61.29           O  
ANISOU  695  O   SER A 111     8312   5346   9628   1372    808    332       O  
ATOM    696  CB  SER A 111      18.970  12.659  98.563  1.00 65.79           C  
ANISOU  696  CB  SER A 111     9063   6022   9911   2092    452    273       C  
ATOM    697  OG  SER A 111      19.947  13.562  99.046  1.00 66.80           O  
ANISOU  697  OG  SER A 111     9503   5906   9971   1879    742    298       O  
ATOM    698  N   TRP A 112      20.753  11.524  96.307  1.00 62.02           N  
ANISOU  698  N   TRP A 112     8794   5383   9390   1811    554    358       N  
ATOM    699  CA  TRP A 112      21.905  11.564  95.410  1.00 60.43           C  
ANISOU  699  CA  TRP A 112     8864   4979   9119   1598    765    383       C  
ATOM    700  C   TRP A 112      22.222  13.008  95.046  1.00 65.65           C  
ANISOU  700  C   TRP A 112    10069   5363   9511   1575    986    383       C  
ATOM    701  O   TRP A 112      21.386  13.700  94.455  1.00 67.26           O  
ANISOU  701  O   TRP A 112    10547   5517   9490   1849    880    407       O  
ATOM    702  CB  TRP A 112      21.648  10.741  94.148  1.00 53.73           C  
ANISOU  702  CB  TRP A 112     7998   4192   8225   1720    589    408       C  
ATOM    703  CG  TRP A 112      22.885  10.512  93.350  1.00 50.21           C  
ANISOU  703  CG  TRP A 112     7739   3584   7755   1459    828    419       C  
ATOM    704  CD1 TRP A 112      23.230  11.105  92.171  1.00 51.05           C  
ANISOU  704  CD1 TRP A 112     8314   3478   7605   1455    967    435       C  
ATOM    705  CD2 TRP A 112      23.967   9.643  93.694  1.00 47.97           C  
ANISOU  705  CD2 TRP A 112     7145   3358   7725   1138    984    393       C  
ATOM    706  NE1 TRP A 112      24.454  10.643  91.750  1.00 58.75           N  
ANISOU  706  NE1 TRP A 112     9292   4376   8656   1144   1211    407       N  
ATOM    707  CE2 TRP A 112      24.928   9.746  92.671  1.00 54.85           C  
ANISOU  707  CE2 TRP A 112     8300   4046   8493    948   1214    374       C  
ATOM    708  CE3 TRP A 112      24.213   8.781  94.768  1.00 47.73           C  
ANISOU  708  CE3 TRP A 112     6591   3536   8010    984    941    371       C  
ATOM    709  CZ2 TRP A 112      26.117   9.019  92.689  1.00 58.09           C  
ANISOU  709  CZ2 TRP A 112     8455   4486   9130    618   1399    313       C  
ATOM    710  CZ3 TRP A 112      25.391   8.061  94.784  1.00 48.45           C  
ANISOU  710  CZ3 TRP A 112     6437   3641   8330    674   1084    320       C  
ATOM    711  CH2 TRP A 112      26.329   8.184  93.752  1.00 51.56           C  
ANISOU  711  CH2 TRP A 112     7089   3863   8639    496   1312    282       C  
ATOM    712  N   LEU A 113      23.427  13.455  95.403  1.00 65.94           N  
ANISOU  712  N   LEU A 113    10235   5244   9574   1231   1302    338       N  
ATOM    713  CA  LEU A 113      23.874  14.824  95.183  1.00 72.22           C  
ANISOU  713  CA  LEU A 113    11530   5798  10111   1132   1571    314       C  
ATOM    714  C   LEU A 113      25.010  14.924  94.168  1.00 73.29           C  
ANISOU  714  C   LEU A 113    11927   5778  10140    866   1853    276       C  
ATOM    715  O   LEU A 113      25.633  15.987  94.056  1.00 86.78           O  
ANISOU  715  O   LEU A 113    14005   7302  11663    690   2152    225       O  
ATOM    716  CB  LEU A 113      24.307  15.447  96.514  1.00 67.74           C  
ANISOU  716  CB  LEU A 113    10899   5193   9644    917   1732    243       C  
ATOM    717  CG  LEU A 113      23.255  15.393  97.626  1.00 64.65           C  
ANISOU  717  CG  LEU A 113    10266   4947   9352   1148   1515    268       C  
ATOM    718  CD1 LEU A 113      23.850  15.693  99.001  1.00 70.41           C  
ANISOU  718  CD1 LEU A 113    10865   5655  10232    879   1663    188       C  
ATOM    719  CD2 LEU A 113      22.110  16.339  97.315  1.00 63.51           C  
ANISOU  719  CD2 LEU A 113    10439   4753   8940   1510   1409    317       C  
ATOM    720  N   PHE A 114      25.308  13.849  93.437  1.00 62.63           N  
ANISOU  720  N   PHE A 114    10392   4505   8899    821   1791    288       N  
ATOM    721  CA  PHE A 114      26.458  13.808  92.539  1.00 59.80           C  
ANISOU  721  CA  PHE A 114    10207   4030   8485    540   2085    230       C  
ATOM    722  C   PHE A 114      26.081  13.820  91.061  1.00 59.96           C  
ANISOU  722  C   PHE A 114    10624   3951   8207    750   2053    304       C  
ATOM    723  O   PHE A 114      26.961  13.667  90.205  1.00 66.38           O  
ANISOU  723  O   PHE A 114    11589   4674   8957    545   2300    261       O  
ATOM    724  CB  PHE A 114      27.324  12.588  92.854  1.00 63.33           C  
ANISOU  724  CB  PHE A 114    10136   4633   9293    269   2103    157       C  
ATOM    725  CG  PHE A 114      27.670  12.458  94.306  1.00 68.21           C  
ANISOU  725  CG  PHE A 114    10337   5375  10205     81   2087     73       C  
ATOM    726  CD1 PHE A 114      27.022  11.539  95.111  1.00 72.07           C  
ANISOU  726  CD1 PHE A 114    10395   6061  10928    222   1802    125       C  
ATOM    727  CD2 PHE A 114      28.624  13.285  94.874  1.00 70.37           C  
ANISOU  727  CD2 PHE A 114    10654   5578  10507   -232   2354    -72       C  
ATOM    728  CE1 PHE A 114      27.338  11.431  96.452  1.00 67.45           C  
ANISOU  728  CE1 PHE A 114     9458   5580  10590     54   1779     45       C  
ATOM    729  CE2 PHE A 114      28.945  13.181  96.212  1.00 66.07           C  
ANISOU  729  CE2 PHE A 114     9739   5154  10210   -399   2297   -168       C  
ATOM    730  CZ  PHE A 114      28.301  12.254  97.003  1.00 61.99           C  
ANISOU  730  CZ  PHE A 114     8828   4812   9913   -253   2006   -103       C  
ATOM    731  N   GLY A 115      24.805  13.996  90.738  1.00 54.00           N  
ANISOU  731  N   GLY A 115    10025   3224   7268   1153   1757    394       N  
ATOM    732  CA  GLY A 115      24.386  14.119  89.356  1.00 55.21           C  
ANISOU  732  CA  GLY A 115    10601   3281   7096   1376   1701    449       C  
ATOM    733  C   GLY A 115      24.149  12.790  88.656  1.00 55.20           C  
ANISOU  733  C   GLY A 115    10341   3417   7215   1466   1465    479       C  
ATOM    734  O   GLY A 115      24.377  11.700  89.187  1.00 52.64           O  
ANISOU  734  O   GLY A 115     9512   3260   7228   1341   1366    463       O  
ATOM    735  N   HIS A 116      23.671  12.907  87.414  1.00 66.16           N  
ANISOU  735  N   HIS A 116    12128   4724   8285   1696   1377    521       N  
ATOM    736  CA  HIS A 116      23.256  11.727  86.663  1.00 66.51           C  
ANISOU  736  CA  HIS A 116    11982   4896   8392   1830   1113    546       C  
ATOM    737  C   HIS A 116      24.438  10.834  86.294  1.00 67.58           C  
ANISOU  737  C   HIS A 116    11984   5005   8689   1497   1343    522       C  
ATOM    738  O   HIS A 116      24.338   9.605  86.381  1.00 74.63           O  
ANISOU  738  O   HIS A 116    12448   6067   9840   1486   1152    528       O  
ATOM    739  CB  HIS A 116      22.495  12.151  85.410  1.00 74.36           C  
ANISOU  739  CB  HIS A 116    13494   5798   8962   2157    967    575       C  
ATOM    740  CG  HIS A 116      21.271  12.962  85.695  1.00 89.56           C  
ANISOU  740  CG  HIS A 116    15522   7778  10728   2519    710    575       C  
ATOM    741  ND1 HIS A 116      21.283  14.339  85.734  1.00 98.55           N  
ANISOU  741  ND1 HIS A 116    17167   8725  11553   2588    894    578       N  
ATOM    742  CD2 HIS A 116      19.997  12.588  85.963  1.00 93.67           C  
ANISOU  742  CD2 HIS A 116    15687   8535  11368   2821    303    553       C  
ATOM    743  CE1 HIS A 116      20.067  14.779  86.008  1.00100.43           C  
ANISOU  743  CE1 HIS A 116    17366   9071  11722   2941    591    564       C  
ATOM    744  NE2 HIS A 116      19.269  13.737  86.153  1.00 96.02           N  
ANISOU  744  NE2 HIS A 116    16267   8783  11435   3078    236    539       N  
ATOM    745  N   ALA A 117      25.565  11.424  85.887  1.00 65.88           N  
ANISOU  745  N   ALA A 117    12113   4591   8328   1218   1773    480       N  
ATOM    746  CA  ALA A 117      26.680  10.618  85.395  1.00 59.17           C  
ANISOU  746  CA  ALA A 117    11143   3727   7612    916   2019    432       C  
ATOM    747  C   ALA A 117      27.281   9.765  86.507  1.00 58.21           C  
ANISOU  747  C   ALA A 117    10373   3790   7955    665   2018    373       C  
ATOM    748  O   ALA A 117      27.485   8.557  86.338  1.00 65.64           O  
ANISOU  748  O   ALA A 117    10985   4853   9101    609   1923    374       O  
ATOM    749  CB  ALA A 117      27.745  11.518  84.768  1.00 62.66           C  
ANISOU  749  CB  ALA A 117    12060   3940   7807    662   2524    361       C  
ATOM    750  N   LEU A 118      27.572  10.378  87.656  1.00 62.18           N  
ANISOU  750  N   LEU A 118    10702   4314   8609    518   2124    316       N  
ATOM    751  CA  LEU A 118      28.146   9.639  88.775  1.00 59.26           C  
ANISOU  751  CA  LEU A 118     9739   4126   8652    291   2117    246       C  
ATOM    752  C   LEU A 118      27.167   8.626  89.356  1.00 62.51           C  
ANISOU  752  C   LEU A 118     9738   4749   9262    523   1708    326       C  
ATOM    753  O   LEU A 118      27.598   7.680  90.027  1.00 61.99           O  
ANISOU  753  O   LEU A 118     9176   4856   9520    370   1676    287       O  
ATOM    754  CB  LEU A 118      28.626  10.614  89.851  1.00 54.80           C  
ANISOU  754  CB  LEU A 118     9129   3529   8163     94   2309    152       C  
ATOM    755  CG  LEU A 118      29.784  11.514  89.405  1.00 53.47           C  
ANISOU  755  CG  LEU A 118     9259   3194   7864   -204   2767     21       C  
ATOM    756  CD1 LEU A 118      30.153  12.497  90.500  1.00 50.82           C  
ANISOU  756  CD1 LEU A 118     8880   2836   7593   -381   2917    -83       C  
ATOM    757  CD2 LEU A 118      30.991  10.678  88.996  1.00 49.95           C  
ANISOU  757  CD2 LEU A 118     8520   2826   7632   -486   2982   -110       C  
ATOM    758  N   CYS A 119      25.866   8.804  89.116  1.00 62.57           N  
ANISOU  758  N   CYS A 119     9908   4775   9089    892   1399    415       N  
ATOM    759  CA  CYS A 119      24.881   7.802  89.508  1.00 61.17           C  
ANISOU  759  CA  CYS A 119     9330   4832   9080   1121   1022    460       C  
ATOM    760  C   CYS A 119      25.110   6.477  88.799  1.00 61.02           C  
ANISOU  760  C   CYS A 119     9123   4902   9160   1079    953    476       C  
ATOM    761  O   CYS A 119      24.702   5.430  89.314  1.00 62.29           O  
ANISOU  761  O   CYS A 119     8833   5300   9533   1129    744    488       O  
ATOM    762  CB  CYS A 119      23.475   8.330  89.202  1.00 63.29           C  
ANISOU  762  CB  CYS A 119     9780   5125   9141   1509    718    499       C  
ATOM    763  SG  CYS A 119      22.067   7.228  89.546  1.00 63.54           S  
ANISOU  763  SG  CYS A 119     9291   5489   9363   1788    247    496       S  
ATOM    764  N   LYS A 120      25.751   6.502  87.631  1.00 58.00           N  
ANISOU  764  N   LYS A 120     9079   4352   8608    978   1145    471       N  
ATOM    765  CA  LYS A 120      26.140   5.285  86.930  1.00 56.58           C  
ANISOU  765  CA  LYS A 120     8758   4226   8515    897   1141    476       C  
ATOM    766  C   LYS A 120      27.565   4.862  87.259  1.00 53.95           C  
ANISOU  766  C   LYS A 120     8152   3915   8431    515   1469    392       C  
ATOM    767  O   LYS A 120      27.830   3.669  87.440  1.00 62.84           O  
ANISOU  767  O   LYS A 120     8870   5205   9801    434   1407    385       O  
ATOM    768  CB  LYS A 120      26.016   5.473  85.413  1.00 56.22           C  
ANISOU  768  CB  LYS A 120     9220   4006   8136   1011   1167    505       C  
ATOM    769  CG  LYS A 120      24.615   5.771  84.916  1.00 53.51           C  
ANISOU  769  CG  LYS A 120     9086   3682   7563   1400    814    558       C  
ATOM    770  CD  LYS A 120      24.444   5.332  83.468  1.00 56.45           C  
ANISOU  770  CD  LYS A 120     9788   3974   7686   1512    757    584       C  
ATOM    771  CE  LYS A 120      22.978   5.276  83.072  1.00 59.64           C  
ANISOU  771  CE  LYS A 120    10224   4497   7939   1896    340    603       C  
ATOM    772  NZ  LYS A 120      22.396   3.928  83.303  1.00 61.50           N  
ANISOU  772  NZ  LYS A 120     9947   4978   8444   1956     50    601       N  
ATOM    773  N   VAL A 121      28.491   5.819  87.337  1.00 56.98           N  
ANISOU  773  N   VAL A 121     8720   4163   8766    281   1813    305       N  
ATOM    774  CA  VAL A 121      29.897   5.482  87.553  1.00 54.68           C  
ANISOU  774  CA  VAL A 121     8131   3925   8718    -69   2117    165       C  
ATOM    775  C   VAL A 121      30.094   4.838  88.919  1.00 54.57           C  
ANISOU  775  C   VAL A 121     7493   4148   9092   -164   1979    114       C  
ATOM    776  O   VAL A 121      30.539   3.689  89.026  1.00 55.33           O  
ANISOU  776  O   VAL A 121     7182   4410   9430   -240   1923     79       O  
ATOM    777  CB  VAL A 121      30.783   6.728  87.392  1.00 57.64           C  
ANISOU  777  CB  VAL A 121     8810   4133   8957   -286   2510     44       C  
ATOM    778  CG1 VAL A 121      32.231   6.366  87.655  1.00 55.36           C  
ANISOU  778  CG1 VAL A 121     8132   3950   8953   -609   2785   -158       C  
ATOM    779  CG2 VAL A 121      30.620   7.320  86.005  1.00 59.84           C  
ANISOU  779  CG2 VAL A 121     9724   4182   8832   -188   2669     96       C  
ATOM    780  N   ILE A 122      29.776   5.578  89.985  1.00 52.94           N  
ANISOU  780  N   ILE A 122     7221   3961   8933   -150   1916    105       N  
ATOM    781  CA  ILE A 122      30.079   5.099  91.335  1.00 51.75           C  
ANISOU  781  CA  ILE A 122     6514   4025   9122   -261   1794     33       C  
ATOM    782  C   ILE A 122      29.440   3.742  91.612  1.00 51.03           C  
ANISOU  782  C   ILE A 122     6037   4136   9216   -108   1479    128       C  
ATOM    783  O   ILE A 122      30.146   2.836  92.080  1.00 50.12           O  
ANISOU  783  O   ILE A 122     5492   4205   9347   -234   1429     48       O  
ATOM    784  CB  ILE A 122      29.680   6.155  92.377  1.00 55.46           C  
ANISOU  784  CB  ILE A 122     7056   4455   9563   -241   1766     26       C  
ATOM    785  CG1 ILE A 122      30.661   7.330  92.341  1.00 52.02           C  
ANISOU  785  CG1 ILE A 122     6856   3881   9026   -485   2098   -125       C  
ATOM    786  CG2 ILE A 122      29.622   5.537  93.762  1.00 54.82           C  
ANISOU  786  CG2 ILE A 122     6454   4598   9778   -267   1539     -2       C  
ATOM    787  CD1 ILE A 122      30.067   8.632  92.819  1.00 61.23           C  
ANISOU  787  CD1 ILE A 122     8367   4899   9998   -407   2129    -89       C  
ATOM    788  N   PRO A 123      28.140   3.540  91.379  1.00 47.90           N  
ANISOU  788  N   PRO A 123     5755   3762   8681    182   1232    270       N  
ATOM    789  CA  PRO A 123      27.585   2.186  91.556  1.00 40.59           C  
ANISOU  789  CA  PRO A 123     4456   3073   7892    294    951    332       C  
ATOM    790  C   PRO A 123      28.288   1.150  90.701  1.00 47.28           C  
ANISOU  790  C   PRO A 123     5222   3930   8813    189   1028    313       C  
ATOM    791  O   PRO A 123      28.446  -0.003  91.123  1.00 43.14           O  
ANISOU  791  O   PRO A 123     4309   3590   8493    153    891    309       O  
ATOM    792  CB  PRO A 123      26.116   2.366  91.169  1.00 37.47           C  
ANISOU  792  CB  PRO A 123     4269   2734   7233    603    707    426       C  
ATOM    793  CG  PRO A 123      25.829   3.800  91.499  1.00 39.48           C  
ANISOU  793  CG  PRO A 123     4835   2827   7338    682    790    421       C  
ATOM    794  CD  PRO A 123      27.086   4.521  91.075  1.00 45.57           C  
ANISOU  794  CD  PRO A 123     5885   3346   8083    435   1154    348       C  
ATOM    795  N   TYR A 124      28.702   1.527  89.489  1.00 52.81           N  
ANISOU  795  N   TYR A 124     6324   4430   9312    150   1249    301       N  
ATOM    796  CA  TYR A 124      29.436   0.597  88.636  1.00 51.31           C  
ANISOU  796  CA  TYR A 124     6086   4242   9168     44   1364    268       C  
ATOM    797  C   TYR A 124      30.805   0.270  89.221  1.00 49.89           C  
ANISOU  797  C   TYR A 124     5524   4176   9257   -200   1532    107       C  
ATOM    798  O   TYR A 124      31.216  -0.896  89.250  1.00 57.90           O  
ANISOU  798  O   TYR A 124     6230   5341  10430   -210   1453     77       O  
ATOM    799  CB  TYR A 124      29.564   1.179  87.229  1.00 55.34           C  
ANISOU  799  CB  TYR A 124     7168   4508   9350     61   1571    279       C  
ATOM    800  CG  TYR A 124      30.589   0.488  86.357  1.00 56.71           C  
ANISOU  800  CG  TYR A 124     7337   4654   9556   -101   1802    205       C  
ATOM    801  CD1 TYR A 124      30.291  -0.706  85.715  1.00 55.63           C  
ANISOU  801  CD1 TYR A 124     7146   4575   9417     -9   1660    271       C  
ATOM    802  CD2 TYR A 124      31.846   1.044  86.155  1.00 51.34           C  
ANISOU  802  CD2 TYR A 124     6708   3899   8901   -333   2170     49       C  
ATOM    803  CE1 TYR A 124      31.221  -1.335  84.909  1.00 47.08           C  
ANISOU  803  CE1 TYR A 124     6075   3458   8354   -141   1884    201       C  
ATOM    804  CE2 TYR A 124      32.779   0.424  85.349  1.00 49.93           C  
ANISOU  804  CE2 TYR A 124     6509   3704   8759   -450   2396    -43       C  
ATOM    805  CZ  TYR A 124      32.464  -0.763  84.729  1.00 43.52           C  
ANISOU  805  CZ  TYR A 124     5660   2936   7941   -351   2256     42       C  
ATOM    806  OH  TYR A 124      33.403  -1.371  83.929  1.00 55.33           O  
ANISOU  806  OH  TYR A 124     7148   4402   9471   -457   2500    -54       O  
ATOM    807  N   LEU A 125      31.531   1.291  89.684  1.00 43.94           N  
ANISOU  807  N   LEU A 125     4808   3377   8512   -351   1728    -24       N  
ATOM    808  CA  LEU A 125      32.860   1.058  90.243  1.00 45.13           C  
ANISOU  808  CA  LEU A 125     4634   3672   8841   -496   1802   -233       C  
ATOM    809  C   LEU A 125      32.797   0.204  91.504  1.00 51.22           C  
ANISOU  809  C   LEU A 125     5025   4692   9745   -392   1441   -242       C  
ATOM    810  O   LEU A 125      33.691  -0.614  91.752  1.00 57.23           O  
ANISOU  810  O   LEU A 125     5623   5575  10547   -400   1341   -351       O  
ATOM    811  CB  LEU A 125      33.553   2.391  90.526  1.00 48.14           C  
ANISOU  811  CB  LEU A 125     5163   3955   9175   -668   2046   -385       C  
ATOM    812  CG  LEU A 125      34.045   3.132  89.281  1.00 51.26           C  
ANISOU  812  CG  LEU A 125     5983   4112   9381   -792   2440   -441       C  
ATOM    813  CD1 LEU A 125      34.692   4.456  89.651  1.00 49.38           C  
ANISOU  813  CD1 LEU A 125     5882   3779   9099   -970   2685   -602       C  
ATOM    814  CD2 LEU A 125      35.010   2.258  88.492  1.00 54.77           C  
ANISOU  814  CD2 LEU A 125     6308   4584   9919   -851   2587   -559       C  
ATOM    815  N   GLN A 126      31.748   0.370  92.312  1.00 54.00           N  
ANISOU  815  N   GLN A 126     5328   5096  10095   -287   1228   -122       N  
ATOM    816  CA  GLN A 126      31.615  -0.463  93.503  1.00 52.63           C  
ANISOU  816  CA  GLN A 126     4989   5129   9878   -195    883   -111       C  
ATOM    817  C   GLN A 126      31.421  -1.927  93.132  1.00 54.85           C  
ANISOU  817  C   GLN A 126     5267   5499  10075   -114    710    -34       C  
ATOM    818  O   GLN A 126      32.038  -2.815  93.732  1.00 61.34           O  
ANISOU  818  O   GLN A 126     6044   6466  10797   -121    560    -88       O  
ATOM    819  CB  GLN A 126      30.452   0.031  94.365  1.00 53.36           C  
ANISOU  819  CB  GLN A 126     5086   5242   9948   -116    735     -4       C  
ATOM    820  CG  GLN A 126      30.205  -0.807  95.609  1.00 51.12           C  
ANISOU  820  CG  GLN A 126     4785   5162   9475    -70    440     16       C  
ATOM    821  CD  GLN A 126      31.367  -0.759  96.589  1.00 52.82           C  
ANISOU  821  CD  GLN A 126     4920   5475   9674   -145    401   -133       C  
ATOM    822  OE1 GLN A 126      31.704   0.295  97.124  1.00 52.35           O  
ANISOU  822  OE1 GLN A 126     4817   5374   9699   -216    482   -222       O  
ATOM    823  NE2 GLN A 126      31.984  -1.911  96.829  1.00 51.42           N  
ANISOU  823  NE2 GLN A 126     4713   5422   9400   -134    281   -164       N  
ATOM    824  N   ALA A 127      30.568  -2.199  92.141  1.00 48.71           N  
ANISOU  824  N   ALA A 127     4544   4630   9336    -46    745     96       N  
ATOM    825  CA  ALA A 127      30.387  -3.570  91.679  1.00 45.94           C  
ANISOU  825  CA  ALA A 127     4212   4354   8889     -9    612    156       C  
ATOM    826  C   ALA A 127      31.670  -4.120  91.067  1.00 46.93           C  
ANISOU  826  C   ALA A 127     4308   4452   9072    -64    757     42       C  
ATOM    827  O   ALA A 127      32.009  -5.293  91.268  1.00 49.31           O  
ANISOU  827  O   ALA A 127     4593   4867   9276    -55    619     33       O  
ATOM    828  CB  ALA A 127      29.239  -3.639  90.672  1.00 49.15           C  
ANISOU  828  CB  ALA A 127     4653   4680   9341     51    621    302       C  
ATOM    829  N   VAL A 128      32.396  -3.290  90.314  1.00 47.37           N  
ANISOU  829  N   VAL A 128     4387   4366   9247   -147   1073    -56       N  
ATOM    830  CA  VAL A 128      33.664  -3.732  89.740  1.00 44.91           C  
ANISOU  830  CA  VAL A 128     4052   4029   8983   -229   1240   -199       C  
ATOM    831  C   VAL A 128      34.657  -4.073  90.843  1.00 46.91           C  
ANISOU  831  C   VAL A 128     4155   4440   9229   -265   1070   -333       C  
ATOM    832  O   VAL A 128      35.417  -5.044  90.738  1.00 54.58           O  
ANISOU  832  O   VAL A 128     5050   5469  10218   -264   1024   -393       O  
ATOM    833  CB  VAL A 128      34.222  -2.655  88.789  1.00 47.40           C  
ANISOU  833  CB  VAL A 128     4532   4161   9317   -371   1656   -298       C  
ATOM    834  CG1 VAL A 128      35.695  -2.909  88.497  1.00 45.86           C  
ANISOU  834  CG1 VAL A 128     4261   3950   9215   -482   1832   -511       C  
ATOM    835  CG2 VAL A 128      33.416  -2.603  87.497  1.00 57.84           C  
ANISOU  835  CG2 VAL A 128     6152   5322  10502   -355   1819   -143       C  
ATOM    836  N   SER A 129      34.665  -3.286  91.924  1.00 49.58           N  
ANISOU  836  N   SER A 129     4446   4848   9543   -292    982   -377       N  
ATOM    837  CA  SER A 129      35.610  -3.541  93.007  1.00 48.55           C  
ANISOU  837  CA  SER A 129     4168   4870   9407   -319    832   -503       C  
ATOM    838  C   SER A 129      35.321  -4.869  93.694  1.00 48.31           C  
ANISOU  838  C   SER A 129     4131   4997   9227   -211    551   -405       C  
ATOM    839  O   SER A 129      36.248  -5.597  94.071  1.00 49.88           O  
ANISOU  839  O   SER A 129     4213   5292   9446   -206    472   -497       O  
ATOM    840  CB  SER A 129      35.578  -2.397  94.020  1.00 61.40           C  
ANISOU  840  CB  SER A 129     5763   6526  11040   -370    808   -563       C  
ATOM    841  OG  SER A 129      36.250  -2.764  95.213  1.00 74.21           O  
ANISOU  841  OG  SER A 129     7249   8310  12638   -359    608   -647       O  
ATOM    842  N   VAL A 130      34.041  -5.206  93.863  1.00 49.67           N  
ANISOU  842  N   VAL A 130     4429   5192   9250   -132    422   -234       N  
ATOM    843  CA  VAL A 130      33.691  -6.463  94.516  1.00 45.41           C  
ANISOU  843  CA  VAL A 130     3927   4787   8538    -62    224   -158       C  
ATOM    844  C   VAL A 130      34.089  -7.648  93.645  1.00 47.29           C  
ANISOU  844  C   VAL A 130     4156   5005   8808    -45    255   -152       C  
ATOM    845  O   VAL A 130      34.635  -8.643  94.137  1.00 52.83           O  
ANISOU  845  O   VAL A 130     4783   5756   9532    -10    158   -190       O  
ATOM    846  CB  VAL A 130      32.190  -6.484  94.855  1.00 44.75           C  
ANISOU  846  CB  VAL A 130     3975   4722   8308    -17    130    -16       C  
ATOM    847  CG1 VAL A 130      31.855  -7.704  95.695  1.00 37.51           C  
ANISOU  847  CG1 VAL A 130     3073   3863   7318     26    -15     28       C  
ATOM    848  CG2 VAL A 130      31.794  -5.204  95.570  1.00 50.46           C  
ANISOU  848  CG2 VAL A 130     4698   5433   9041    -33    132    -24       C  
ATOM    849  N   SER A 131      33.831  -7.560  92.339  1.00 41.66           N  
ANISOU  849  N   SER A 131     3492   4161   8174    -60    403   -111       N  
ATOM    850  CA  SER A 131      34.211  -8.641  91.434  1.00 38.68           C  
ANISOU  850  CA  SER A 131     3108   3744   7844    -49    458   -107       C  
ATOM    851  C   SER A 131      35.715  -8.881  91.460  1.00 38.96           C  
ANISOU  851  C   SER A 131     2990   3799   8013    -84    528   -273       C  
ATOM    852  O   SER A 131      36.172 -10.023  91.598  1.00 45.18           O  
ANISOU  852  O   SER A 131     3725   4659   8781    -43    446   -287       O  
ATOM    853  CB  SER A 131      33.741  -8.325  90.015  1.00 48.09           C  
ANISOU  853  CB  SER A 131     4370   4756   9146    -58    649    -49       C  
ATOM    854  OG  SER A 131      34.151  -9.341  89.117  1.00 53.06           O  
ANISOU  854  OG  SER A 131     4993   5327   9839    -53    732    -51       O  
ATOM    855  N   VAL A 132      36.503  -7.812  91.317  1.00 34.34           N  
ANISOU  855  N   VAL A 132     2320   3148   7578   -166    695   -418       N  
ATOM    856  CA  VAL A 132      37.959  -7.947  91.338  1.00 40.21           C  
ANISOU  856  CA  VAL A 132     2882   3915   8480   -218    774   -616       C  
ATOM    857  C   VAL A 132      38.421  -8.602  92.635  1.00 46.27           C  
ANISOU  857  C   VAL A 132     3519   4867   9194   -146    520   -657       C  
ATOM    858  O   VAL A 132      39.274  -9.498  92.630  1.00 59.01           O  
ANISOU  858  O   VAL A 132     4995   6520  10906   -107    484   -748       O  
ATOM    859  CB  VAL A 132      38.622  -6.573  91.135  1.00 46.03           C  
ANISOU  859  CB  VAL A 132     3560   4557   9371   -347   1009   -790       C  
ATOM    860  CG1 VAL A 132      40.131  -6.670  91.301  1.00 48.04           C  
ANISOU  860  CG1 VAL A 132     3585   4858   9809   -413   1071  -1034       C  
ATOM    861  CG2 VAL A 132      38.262  -6.011  89.771  1.00 42.74           C  
ANISOU  861  CG2 VAL A 132     3305   3925   9009   -412   1328   -768       C  
ATOM    862  N   ALA A 133      37.856  -8.172  93.766  1.00 48.34           N  
ANISOU  862  N   ALA A 133     3810   5194   9363   -115    360   -608       N  
ATOM    863  CA  ALA A 133      38.297  -8.693  95.056  1.00 43.39           C  
ANISOU  863  CA  ALA A 133     3060   4684   8744    -38    142   -672       C  
ATOM    864  C   ALA A 133      38.022 -10.186  95.175  1.00 48.06           C  
ANISOU  864  C   ALA A 133     3695   5316   9248     71      8   -576       C  
ATOM    865  O   ALA A 133      38.922 -10.973  95.489  1.00 56.49           O  
ANISOU  865  O   ALA A 133     4615   6453  10396    144    -82   -678       O  
ATOM    866  CB  ALA A 133      37.605  -7.933  96.188  1.00 38.60           C  
ANISOU  866  CB  ALA A 133     2515   4118   8032    -31     25   -621       C  
ATOM    867  N   VAL A 134      36.778 -10.597  94.927  1.00 47.73           N  
ANISOU  867  N   VAL A 134     3848   5237   9049     87     -4   -392       N  
ATOM    868  CA  VAL A 134      36.432 -12.005  95.077  1.00 43.30           C  
ANISOU  868  CA  VAL A 134     3342   4711   8398    171   -106   -305       C  
ATOM    869  C   VAL A 134      37.145 -12.853  94.033  1.00 45.65           C  
ANISOU  869  C   VAL A 134     3575   4982   8788    186    -15   -345       C  
ATOM    870  O   VAL A 134      37.560 -13.984  94.316  1.00 58.67           O  
ANISOU  870  O   VAL A 134     5169   6691  10433    283   -108   -361       O  
ATOM    871  CB  VAL A 134      34.907 -12.190  95.015  1.00 36.17           C  
ANISOU  871  CB  VAL A 134     2638   3774   7330    158   -116   -131       C  
ATOM    872  CG1 VAL A 134      34.411 -12.033  93.588  1.00 37.09           C  
ANISOU  872  CG1 VAL A 134     2845   3799   7448    103     33    -62       C  
ATOM    873  CG2 VAL A 134      34.520 -13.544  95.583  1.00 32.62           C  
ANISOU  873  CG2 VAL A 134     2236   3376   6781    235   -229    -65       C  
ATOM    874  N   LEU A 135      37.307 -12.332  92.812  1.00 39.81           N  
ANISOU  874  N   LEU A 135     2850   4149   8128    104    179   -364       N  
ATOM    875  CA  LEU A 135      38.073 -13.076  91.817  1.00 47.93           C  
ANISOU  875  CA  LEU A 135     3807   5141   9262    109    297   -420       C  
ATOM    876  C   LEU A 135      39.544 -13.171  92.196  1.00 47.89           C  
ANISOU  876  C   LEU A 135     3556   5201   9439    139    280   -625       C  
ATOM    877  O   LEU A 135      40.202 -14.164  91.868  1.00 50.20           O  
ANISOU  877  O   LEU A 135     3756   5518   9801    207    285   -674       O  
ATOM    878  CB  LEU A 135      37.935 -12.436  90.435  1.00 47.55           C  
ANISOU  878  CB  LEU A 135     3836   4941   9290     14    541   -411       C  
ATOM    879  CG  LEU A 135      36.657 -12.728  89.655  1.00 49.50           C  
ANISOU  879  CG  LEU A 135     4274   5088   9444     16    574   -233       C  
ATOM    880  CD1 LEU A 135      36.699 -12.005  88.322  1.00 45.36           C  
ANISOU  880  CD1 LEU A 135     3799   4362   9072    -54    850   -256       C  
ATOM    881  CD2 LEU A 135      36.496 -14.227  89.456  1.00 51.34           C  
ANISOU  881  CD2 LEU A 135     4530   5344   9631     80    507   -160       C  
ATOM    882  N   THR A 136      40.074 -12.160  92.889  1.00 43.82           N  
ANISOU  882  N   THR A 136     2917   4721   9010     98    256   -758       N  
ATOM    883  CA  THR A 136      41.469 -12.220  93.310  1.00 52.04           C  
ANISOU  883  CA  THR A 136     3688   5839  10246    129    215   -987       C  
ATOM    884  C   THR A 136      41.669 -13.271  94.390  1.00 55.58           C  
ANISOU  884  C   THR A 136     4066   6419  10635    310    -54   -985       C  
ATOM    885  O   THR A 136      42.643 -14.031  94.354  1.00 52.32           O  
ANISOU  885  O   THR A 136     3471   6065  10342    408   -101  -1112       O  
ATOM    886  CB  THR A 136      41.935 -10.854  93.805  1.00 56.66           C  
ANISOU  886  CB  THR A 136     4159   6431  10939     30    254  -1145       C  
ATOM    887  OG1 THR A 136      41.953  -9.931  92.708  1.00 54.77           O  
ANISOU  887  OG1 THR A 136     3982   6059  10771   -127    546  -1179       O  
ATOM    888  CG2 THR A 136      43.331 -10.958  94.389  1.00 59.63           C  
ANISOU  888  CG2 THR A 136     4226   6906  11524     74    165  -1409       C  
ATOM    889  N   LEU A 137      40.768 -13.313  95.371  1.00 51.85           N  
ANISOU  889  N   LEU A 137     3736   5988   9976    367   -224   -853       N  
ATOM    890  CA  LEU A 137      40.849 -14.344  96.399  1.00 52.07           C  
ANISOU  890  CA  LEU A 137     3754   6119   9911    556   -462   -832       C  
ATOM    891  C   LEU A 137      40.667 -15.730  95.796  1.00 54.67           C  
ANISOU  891  C   LEU A 137     4164   6439  10170    656   -445   -729       C  
ATOM    892  O   LEU A 137      41.268 -16.705  96.263  1.00 55.56           O  
ANISOU  892  O   LEU A 137     4201   6627  10282    846   -591   -775       O  
ATOM    893  CB  LEU A 137      39.801 -14.094  97.480  1.00 46.92           C  
ANISOU  893  CB  LEU A 137     3275   5486   9067    575   -593   -703       C  
ATOM    894  CG  LEU A 137      39.932 -12.799  98.285  1.00 47.99           C  
ANISOU  894  CG  LEU A 137     3346   5643   9245    508   -641   -794       C  
ATOM    895  CD1 LEU A 137      38.709 -12.591  99.165  1.00 46.11           C  
ANISOU  895  CD1 LEU A 137     3308   5400   8810    512   -719   -640       C  
ATOM    896  CD2 LEU A 137      41.202 -12.802  99.123  1.00 46.72           C  
ANISOU  896  CD2 LEU A 137     2952   5582   9218    621   -823  -1008       C  
ATOM    897  N   SER A 138      39.831 -15.843  94.765  1.00 53.16           N  
ANISOU  897  N   SER A 138     4135   6151   9914    551   -278   -590       N  
ATOM    898  CA  SER A 138      39.640 -17.133  94.115  1.00 47.03           C  
ANISOU  898  CA  SER A 138     3437   5356   9076    632   -243   -500       C  
ATOM    899  C   SER A 138      40.934 -17.626  93.480  1.00 54.86           C  
ANISOU  899  C   SER A 138     4229   6366  10249    701   -177   -647       C  
ATOM    900  O   SER A 138      41.341 -18.777  93.682  1.00 57.41           O  
ANISOU  900  O   SER A 138     4522   6746  10546    890   -272   -652       O  
ATOM    901  CB  SER A 138      38.521 -17.029  93.079  1.00 39.94           C  
ANISOU  901  CB  SER A 138     2732   4345   8098    494    -83   -350       C  
ATOM    902  OG  SER A 138      37.253 -17.054  93.711  1.00 47.09           O  
ANISOU  902  OG  SER A 138     3813   5251   8828    480   -166   -211       O  
ATOM    903  N   PHE A 139      41.600 -16.762  92.711  1.00 57.58           N  
ANISOU  903  N   PHE A 139     4442   6654  10780    563      1   -777       N  
ATOM    904  CA  PHE A 139      42.832 -17.170  92.048  1.00 55.94           C  
ANISOU  904  CA  PHE A 139     4026   6452  10776    602    106   -943       C  
ATOM    905  C   PHE A 139      43.937 -17.455  93.057  1.00 61.07           C  
ANISOU  905  C   PHE A 139     4426   7238  11539    775   -100  -1127       C  
ATOM    906  O   PHE A 139      44.834 -18.262  92.784  1.00 66.18           O  
ANISOU  906  O   PHE A 139     4914   7928  12305    908   -101  -1235       O  
ATOM    907  CB  PHE A 139      43.272 -16.093  91.057  1.00 57.83           C  
ANISOU  907  CB  PHE A 139     4198   6580  11195    397    378  -1062       C  
ATOM    908  CG  PHE A 139      42.451 -16.053  89.795  1.00 67.54           C  
ANISOU  908  CG  PHE A 139     5646   7636  12380    277    603   -920       C  
ATOM    909  CD1 PHE A 139      41.106 -16.396  89.807  1.00 66.92           C  
ANISOU  909  CD1 PHE A 139     5814   7527  12087    292    527   -693       C  
ATOM    910  CD2 PHE A 139      43.028 -15.674  88.596  1.00 76.57           C  
ANISOU  910  CD2 PHE A 139     6742   8616  13734    146    906  -1040       C  
ATOM    911  CE1 PHE A 139      40.355 -16.355  88.644  1.00 65.09           C  
ANISOU  911  CE1 PHE A 139     5755   7116  11858    198    716   -580       C  
ATOM    912  CE2 PHE A 139      42.284 -15.633  87.433  1.00 75.44           C  
ANISOU  912  CE2 PHE A 139     6813   8275  13578     55   1124   -918       C  
ATOM    913  CZ  PHE A 139      40.946 -15.974  87.456  1.00 69.98           C  
ANISOU  913  CZ  PHE A 139     6344   7566  12679     91   1012   -684       C  
ATOM    914  N   ILE A 140      43.890 -16.814  94.226  1.00 63.40           N  
ANISOU  914  N   ILE A 140     4687   7602  11802    794   -284  -1172       N  
ATOM    915  CA  ILE A 140      44.854 -17.129  95.275  1.00 62.95           C  
ANISOU  915  CA  ILE A 140     4418   7670  11830    990   -529  -1344       C  
ATOM    916  C   ILE A 140      44.604 -18.526  95.825  1.00 66.17           C  
ANISOU  916  C   ILE A 140     4956   8128  12057   1259   -723  -1213       C  
ATOM    917  O   ILE A 140      45.528 -19.337  95.946  1.00 68.08           O  
ANISOU  917  O   ILE A 140     5045   8432  12392   1469   -832  -1329       O  
ATOM    918  CB  ILE A 140      44.804 -16.070  96.388  1.00 61.06           C  
ANISOU  918  CB  ILE A 140     4140   7474  11585    942   -675  -1421       C  
ATOM    919  CG1 ILE A 140      45.351 -14.742  95.870  1.00 65.10           C  
ANISOU  919  CG1 ILE A 140     4482   7937  12314    713   -475  -1608       C  
ATOM    920  CG2 ILE A 140      45.584 -16.545  97.603  1.00 63.07           C  
ANISOU  920  CG2 ILE A 140     4247   7848  11869   1187   -990  -1566       C  
ATOM    921  CD1 ILE A 140      44.972 -13.564  96.720  1.00 70.73           C  
ANISOU  921  CD1 ILE A 140     5237   8658  12980    619   -543  -1622       C  
ATOM    922  N   ALA A 141      43.350 -18.830  96.166  1.00 59.03           N  
ANISOU  922  N   ALA A 141     4344   7187  10897   1267   -760   -979       N  
ATOM    923  CA  ALA A 141      43.031 -20.172  96.644  1.00 56.85           C  
ANISOU  923  CA  ALA A 141     4245   6923  10433   1519   -898   -843       C  
ATOM    924  C   ALA A 141      43.324 -21.214  95.573  1.00 64.59           C  
ANISOU  924  C   ALA A 141     5227   7868  11445   1604   -760   -813       C  
ATOM    925  O   ALA A 141      43.806 -22.311  95.877  1.00 72.33           O  
ANISOU  925  O   ALA A 141     6225   8870  12388   1878   -877   -812       O  
ATOM    926  CB  ALA A 141      41.569 -20.242  97.086  1.00 44.66           C  
ANISOU  926  CB  ALA A 141     3006   5327   8635   1469   -903   -622       C  
ATOM    927  N   LEU A 142      43.037 -20.887  94.309  1.00 63.85           N  
ANISOU  927  N   LEU A 142     5142   7701  11417   1389   -509   -786       N  
ATOM    928  CA  LEU A 142      43.327 -21.811  93.218  1.00 60.75           C  
ANISOU  928  CA  LEU A 142     4754   7258  11068   1453   -357   -771       C  
ATOM    929  C   LEU A 142      44.826 -22.044  93.085  1.00 67.41           C  
ANISOU  929  C   LEU A 142     5299   8169  12143   1592   -371   -990       C  
ATOM    930  O   LEU A 142      45.273 -23.176  92.868  1.00 66.14           O  
ANISOU  930  O   LEU A 142     5135   8002  11992   1818   -389   -994       O  
ATOM    931  CB  LEU A 142      42.743 -21.267  91.911  1.00 58.09           C  
ANISOU  931  CB  LEU A 142     4488   6790  10794   1178    -92   -721       C  
ATOM    932  CG  LEU A 142      42.678 -22.150  90.664  1.00 63.38           C  
ANISOU  932  CG  LEU A 142     5226   7333  11520   1184     96   -676       C  
ATOM    933  CD1 LEU A 142      41.592 -23.203  90.817  1.00 58.84           C  
ANISOU  933  CD1 LEU A 142     4925   6699  10734   1289     28   -484       C  
ATOM    934  CD2 LEU A 142      42.416 -21.295  89.432  1.00 64.23           C  
ANISOU  934  CD2 LEU A 142     5352   7293  11759    906    365   -677       C  
ATOM    935  N   ASP A 143      45.621 -20.978  93.207  1.00 73.02           N  
ANISOU  935  N   ASP A 143     5746   8919  13078   1461   -360  -1201       N  
ATOM    936  CA  ASP A 143      47.069 -21.123  93.122  1.00 62.92           C  
ANISOU  936  CA  ASP A 143     4132   7709  12065   1571   -378  -1462       C  
ATOM    937  C   ASP A 143      47.609 -21.955  94.278  1.00 68.40           C  
ANISOU  937  C   ASP A 143     4766   8505  12716   1915   -701  -1515       C  
ATOM    938  O   ASP A 143      48.464 -22.826  94.080  1.00 77.77           O  
ANISOU  938  O   ASP A 143     5814   9726  14010   2138   -734  -1616       O  
ATOM    939  CB  ASP A 143      47.726 -19.745  93.088  1.00 67.11           C  
ANISOU  939  CB  ASP A 143     4409   8245  12844   1341   -293  -1701       C  
ATOM    940  CG  ASP A 143      49.220 -19.811  93.280  1.00 82.86           C  
ANISOU  940  CG  ASP A 143     6015  10335  15135   1458   -367  -2027       C  
ATOM    941  OD1 ASP A 143      49.686 -19.529  94.402  1.00 88.11           O  
ANISOU  941  OD1 ASP A 143     6528  11100  15851   1570   -634  -2179       O  
ATOM    942  OD2 ASP A 143      49.925 -20.190  92.321  1.00 87.74           O  
ANISOU  942  OD2 ASP A 143     6477  10924  15937   1450   -166  -2143       O  
ATOM    943  N   ARG A 144      47.123 -21.700  95.497  1.00 67.71           N  
ANISOU  943  N   ARG A 144     4802   8450  12473   1977   -940  -1452       N  
ATOM    944  CA  ARG A 144      47.558 -22.492  96.644  1.00 71.69           C  
ANISOU  944  CA  ARG A 144     5322   9010  12907   2317  -1263  -1491       C  
ATOM    945  C   ARG A 144      47.088 -23.934  96.529  1.00 76.68           C  
ANISOU  945  C   ARG A 144     6243   9568  13323   2565  -1265  -1267       C  
ATOM    946  O   ARG A 144      47.813 -24.863  96.901  1.00 82.65           O  
ANISOU  946  O   ARG A 144     6967  10334  14102   2880  -1438  -1335       O  
ATOM    947  CB  ARG A 144      47.025 -21.879  97.937  1.00 67.12           C  
ANISOU  947  CB  ARG A 144     4872   8448  12183   2308  -1487  -1456       C  
ATOM    948  CG  ARG A 144      47.525 -20.482  98.240  1.00 66.60           C  
ANISOU  948  CG  ARG A 144     4547   8444  12313   2108  -1514  -1686       C  
ATOM    949  CD  ARG A 144      49.020 -20.454  98.509  1.00 70.48           C  
ANISOU  949  CD  ARG A 144     4660   9036  13083   2257  -1687  -2036       C  
ATOM    950  NE  ARG A 144      49.802 -20.456  97.276  1.00 73.44           N  
ANISOU  950  NE  ARG A 144     4766   9416  13724   2151  -1434  -2191       N  
ATOM    951  CZ  ARG A 144      51.035 -20.939  97.173  1.00 81.18           C  
ANISOU  951  CZ  ARG A 144     5438  10471  14937   2337  -1523  -2453       C  
ATOM    952  NH1 ARG A 144      51.636 -21.459  98.235  1.00 81.42           N  
ANISOU  952  NH1 ARG A 144     5399  10579  14957   2657  -1893  -2596       N  
ATOM    953  NH2 ARG A 144      51.672 -20.898  96.011  1.00 81.13           N  
ANISOU  953  NH2 ARG A 144     5201  10452  15174   2210  -1246  -2589       N  
ATOM    954  N   TRP A 145      45.874 -24.139  96.015  1.00 68.67           N  
ANISOU  954  N   TRP A 145     5524   8464  12103   2435  -1078  -1014       N  
ATOM    955  CA  TRP A 145      45.323 -25.487  95.930  1.00 63.46           C  
ANISOU  955  CA  TRP A 145     5171   7687  11252   2653  -1067   -822       C  
ATOM    956  C   TRP A 145      46.147 -26.366  94.997  1.00 66.98           C  
ANISOU  956  C   TRP A 145     5506   8109  11833   2815   -951   -895       C  
ATOM    957  O   TRP A 145      46.431 -27.527  95.318  1.00 74.88           O  
ANISOU  957  O   TRP A 145     6645   9038  12769   3132  -1058   -850       O  
ATOM    958  CB  TRP A 145      43.865 -25.417  95.475  1.00 59.60           C  
ANISOU  958  CB  TRP A 145     4969   7101  10574   2444   -893   -609       C  
ATOM    959  CG  TRP A 145      43.116 -26.711  95.579  1.00 59.98           C  
ANISOU  959  CG  TRP A 145     5385   6993  10413   2639   -886   -416       C  
ATOM    960  CD1 TRP A 145      42.638 -27.295  96.716  1.00 60.63           C  
ANISOU  960  CD1 TRP A 145     5745   6977  10313   2821  -1052   -297       C  
ATOM    961  CD2 TRP A 145      42.734 -27.567  94.498  1.00 59.60           C  
ANISOU  961  CD2 TRP A 145     5503   6823  10321   2653   -689   -330       C  
ATOM    962  NE1 TRP A 145      41.995 -28.471  96.411  1.00 62.69           N  
ANISOU  962  NE1 TRP A 145     6343   7045  10432   2938   -944   -134       N  
ATOM    963  CE2 TRP A 145      42.039 -28.659  95.054  1.00 62.49           C  
ANISOU  963  CE2 TRP A 145     6253   7013  10476   2848   -729   -155       C  
ATOM    964  CE3 TRP A 145      42.918 -27.518  93.113  1.00 56.59           C  
ANISOU  964  CE3 TRP A 145     5004   6424  10071   2508   -474   -394       C  
ATOM    965  CZ2 TRP A 145      41.528 -29.693  94.273  1.00 63.72           C  
ANISOU  965  CZ2 TRP A 145     6687   6989  10534   2907   -563    -49       C  
ATOM    966  CZ3 TRP A 145      42.412 -28.545  92.340  1.00 55.03           C  
ANISOU  966  CZ3 TRP A 145     5065   6063   9783   2572   -338   -296       C  
ATOM    967  CH2 TRP A 145      41.725 -29.618  92.921  1.00 58.29           C  
ANISOU  967  CH2 TRP A 145     5869   6315   9963   2776   -390   -133       C  
ATOM    968  N   TYR A 146      46.530 -25.839  93.831  1.00 65.19           N  
ANISOU  968  N   TYR A 146     5059   7909  11802   2600   -718  -1009       N  
ATOM    969  CA  TYR A 146      47.395 -26.581  92.921  1.00 66.18           C  
ANISOU  969  CA  TYR A 146     5044   8013  12089   2739   -584  -1112       C  
ATOM    970  C   TYR A 146      48.840 -26.644  93.393  1.00 76.01           C  
ANISOU  970  C   TYR A 146     5940   9373  13567   2950   -753  -1368       C  
ATOM    971  O   TYR A 146      49.558 -27.580  93.027  1.00 78.12           O  
ANISOU  971  O   TYR A 146     6140   9620  13922   3198   -731  -1433       O  
ATOM    972  CB  TYR A 146      47.346 -25.957  91.521  1.00 61.76           C  
ANISOU  972  CB  TYR A 146     4377   7403  11688   2418   -263  -1174       C  
ATOM    973  CG  TYR A 146      46.148 -26.374  90.701  1.00 57.70           C  
ANISOU  973  CG  TYR A 146     4193   6733  10999   2298    -84   -966       C  
ATOM    974  CD1 TYR A 146      46.069 -27.648  90.162  1.00 58.27           C  
ANISOU  974  CD1 TYR A 146     4457   6695  10987   2508     -6   -885       C  
ATOM    975  CD2 TYR A 146      45.101 -25.494  90.459  1.00 53.65           C  
ANISOU  975  CD2 TYR A 146     3803   6164  10419   1981      3   -864       C  
ATOM    976  CE1 TYR A 146      44.982 -28.040  89.409  1.00 54.95           C  
ANISOU  976  CE1 TYR A 146     4333   6110  10434   2384    143   -726       C  
ATOM    977  CE2 TYR A 146      44.006 -25.878  89.704  1.00 50.45           C  
ANISOU  977  CE2 TYR A 146     3668   5603   9897   1864    144   -697       C  
ATOM    978  CZ  TYR A 146      43.953 -27.154  89.181  1.00 51.13           C  
ANISOU  978  CZ  TYR A 146     3930   5579   9918   2054    211   -636       C  
ATOM    979  OH  TYR A 146      42.873 -27.555  88.429  1.00 50.29           O  
ANISOU  979  OH  TYR A 146     4089   5296   9722   1922    349   -484       O  
ATOM    980  N   ALA A 147      49.280 -25.677  94.198  1.00 79.22           N  
ANISOU  980  N   ALA A 147     6124   9893  14084   2866   -929  -1534       N  
ATOM    981  CA  ALA A 147      50.655 -25.686  94.677  1.00 82.74           C  
ANISOU  981  CA  ALA A 147     6205  10450  14784   3059  -1130  -1840       C  
ATOM    982  C   ALA A 147      50.868 -26.699  95.790  1.00 85.54           C  
ANISOU  982  C   ALA A 147     6708  10796  14997   3473  -1478  -1812       C  
ATOM    983  O   ALA A 147      51.953 -27.284  95.892  1.00101.41           O  
ANISOU  983  O   ALA A 147     8498  12856  17175   3749  -1621  -2018       O  
ATOM    984  CB  ALA A 147      51.057 -24.294  95.161  1.00 77.45           C  
ANISOU  984  CB  ALA A 147     5251   9870  14305   2828  -1215  -2084       C  
ATOM    985  N   ILE A 148      49.859 -26.924  96.622  1.00 78.99           N  
ANISOU  985  N   ILE A 148     6260   9884  13869   3525  -1616  -1579       N  
ATOM    986  CA  ILE A 148      49.988 -27.777  97.793  1.00 79.48           C  
ANISOU  986  CA  ILE A 148     6535   9890  13773   3893  -1967  -1571       C  
ATOM    987  C   ILE A 148      49.312 -29.125  97.586  1.00 78.28           C  
ANISOU  987  C   ILE A 148     6810   9541  13393   4092  -1889  -1309       C  
ATOM    988  O   ILE A 148      49.890 -30.170  97.886  1.00 89.35           O  
ANISOU  988  O   ILE A 148     8303  10873  14772   4447  -2066  -1363       O  
ATOM    989  CB  ILE A 148      49.433 -27.056  99.041  1.00 78.20           C  
ANISOU  989  CB  ILE A 148     6522   9742  13449   3824  -2205  -1553       C  
ATOM    990  CG1 ILE A 148      50.248 -25.789  99.326  1.00 80.50           C  
ANISOU  990  CG1 ILE A 148     6390  10201  13996   3672  -2321  -1869       C  
ATOM    991  CG2 ILE A 148      49.428 -27.999 100.233  1.00 81.20           C  
ANISOU  991  CG2 ILE A 148     7233  10016  13602   4203  -2564  -1536       C  
ATOM    992  CD1 ILE A 148      49.521 -24.746 100.153  1.00 91.33           C  
ANISOU  992  CD1 ILE A 148     7874  11581  15245   3467  -2404  -1823       C  
ATOM    993  N   CYS A 149      48.079 -29.121  97.077  1.00 80.46           N  
ANISOU  993  N   CYS A 149     7364   9708  13498   3870  -1630  -1044       N  
ATOM    994  CA  CYS A 149      47.316 -30.359  96.971  1.00 82.61           C  
ANISOU  994  CA  CYS A 149     8081   9755  13553   4023  -1547   -803       C  
ATOM    995  C   CYS A 149      47.644 -31.142  95.702  1.00 87.92           C  
ANISOU  995  C   CYS A 149     8722  10359  14325   4095  -1278   -775       C  
ATOM    996  O   CYS A 149      47.769 -32.372  95.750  1.00 98.72           O  
ANISOU  996  O   CYS A 149    10337  11552  15621   4371  -1309   -706       O  
ATOM    997  CB  CYS A 149      45.818 -30.058  97.042  1.00 72.97           C  
ANISOU  997  CB  CYS A 149     7174   8437  12116   3768  -1405   -564       C  
ATOM    998  SG  CYS A 149      45.265 -29.350  98.616  1.00 72.53           S  
ANISOU  998  SG  CYS A 149     7265   8398  11893   3724  -1697   -562       S  
ATOM    999  N   HIS A 150      47.787 -30.468  94.561  1.00 78.48           N  
ANISOU  999  N   HIS A 150     7264   9273  13284   3851  -1018   -843       N  
ATOM   1000  CA  HIS A 150      47.996 -31.142  93.276  1.00 75.53           C  
ANISOU 1000  CA  HIS A 150     6902   8823  12972   3895   -738   -826       C  
ATOM   1001  C   HIS A 150      49.187 -30.558  92.523  1.00 79.44           C  
ANISOU 1001  C   HIS A 150     6919   9481  13783   3821   -641  -1102       C  
ATOM   1002  O   HIS A 150      49.030 -29.832  91.534  1.00 76.01           O  
ANISOU 1002  O   HIS A 150     6354   9080  13446   3512   -402  -1158       O  
ATOM   1003  CB  HIS A 150      46.726 -31.080  92.428  1.00 70.21           C  
ANISOU 1003  CB  HIS A 150     6514   8042  12119   3642   -481   -642       C  
ATOM   1004  CG  HIS A 150      45.539 -31.716  93.083  1.00 73.70           C  
ANISOU 1004  CG  HIS A 150     7422   8295  12287   3691   -526   -392       C  
ATOM   1005  ND1 HIS A 150      45.268 -33.065  92.986  1.00 77.01           N  
ANISOU 1005  ND1 HIS A 150     8207   8459  12594   3902   -442   -237       N  
ATOM   1006  CD2 HIS A 150      44.554 -31.189  93.847  1.00 73.25           C  
ANISOU 1006  CD2 HIS A 150     7523   8230  12079   3527   -621   -284       C  
ATOM   1007  CE1 HIS A 150      44.164 -33.338  93.659  1.00 77.32           C  
ANISOU 1007  CE1 HIS A 150     8599   8326  12454   3832   -481    -55       C  
ATOM   1008  NE2 HIS A 150      43.711 -32.218  94.191  1.00 72.28           N  
ANISOU 1008  NE2 HIS A 150     7842   7851  11771   3627   -590    -80       N  
ATOM   1009  N   PRO A 151      50.397 -30.856  92.982  1.00 82.76           N  
ANISOU 1009  N   PRO A 151     7074   9981  14391   4089   -831  -1305       N  
ATOM   1010  CA  PRO A 151      51.600 -30.286  92.367  1.00 82.55           C  
ANISOU 1010  CA  PRO A 151     6552  10104  14709   4012   -742  -1613       C  
ATOM   1011  C   PRO A 151      51.868 -30.812  90.960  1.00 82.96           C  
ANISOU 1011  C   PRO A 151     6578  10082  14863   4004   -396  -1632       C  
ATOM   1012  O   PRO A 151      51.419 -31.889  90.558  1.00 84.53           O  
ANISOU 1012  O   PRO A 151     7120  10118  14880   4188   -282  -1441       O  
ATOM   1013  CB  PRO A 151      52.716 -30.701  93.332  1.00 88.68           C  
ANISOU 1013  CB  PRO A 151     7108  10965  15621   4372  -1090  -1827       C  
ATOM   1014  CG  PRO A 151      52.012 -30.910  94.635  1.00 89.60           C  
ANISOU 1014  CG  PRO A 151     7566  11015  15462   4502  -1405  -1667       C  
ATOM   1015  CD  PRO A 151      50.709 -31.535  94.248  1.00 88.05           C  
ANISOU 1015  CD  PRO A 151     7863  10613  14977   4437  -1193  -1316       C  
ATOM   1016  N   LEU A 152      52.612 -30.007  90.204  1.00 84.54           N  
ANISOU 1016  N   LEU A 152     6384  10375  15365   3766   -209  -1884       N  
ATOM   1017  CA  LEU A 152      53.115 -30.365  88.881  1.00 86.09           C  
ANISOU 1017  CA  LEU A 152     6473  10506  15732   3731    126  -1987       C  
ATOM   1018  C   LEU A 152      52.027 -30.573  87.827  1.00 81.16           C  
ANISOU 1018  C   LEU A 152     6227   9701  14911   3528    417  -1771       C  
ATOM   1019  O   LEU A 152      52.199 -31.383  86.913  1.00 87.34           O  
ANISOU 1019  O   LEU A 152     7115  10370  15701   3638    635  -1766       O  
ATOM   1020  CB  LEU A 152      53.972 -31.629  88.974  1.00 91.18           C  
ANISOU 1020  CB  LEU A 152     7074  11138  16432   4195     48  -2049       C  
ATOM   1021  CG  LEU A 152      54.986 -31.655  90.120  1.00 96.65           C  
ANISOU 1021  CG  LEU A 152     7445  11982  17297   4473   -323  -2267       C  
ATOM   1022  CD1 LEU A 152      55.470 -33.076  90.388  1.00102.40           C  
ANISOU 1022  CD1 LEU A 152     8303  12628  17977   4978   -458  -2231       C  
ATOM   1023  CD2 LEU A 152      56.154 -30.723  89.846  1.00100.83           C  
ANISOU 1023  CD2 LEU A 152     7393  12674  18243   4285   -260  -2666       C  
ATOM   1024  N   LEU A 153      50.900 -29.871  87.920  1.00 79.73           N  
ANISOU 1024  N   LEU A 153     6257   9477  14561   3236    417  -1608       N  
ATOM   1025  CA  LEU A 153      49.950 -29.839  86.813  1.00 80.96           C  
ANISOU 1025  CA  LEU A 153     6687   9452  14620   2966    692  -1473       C  
ATOM   1026  C   LEU A 153      50.001 -28.513  86.066  1.00 87.26           C  
ANISOU 1026  C   LEU A 153     7284  10219  15652   2509    938  -1594       C  
ATOM   1027  O   LEU A 153      50.050 -28.488  84.832  1.00 92.14           O  
ANISOU 1027  O   LEU A 153     7933  10678  16398   2312   1275  -1631       O  
ATOM   1028  CB  LEU A 153      48.522 -30.116  87.296  1.00 77.08           C  
ANISOU 1028  CB  LEU A 153     6626   8876  13783   2963    555  -1195       C  
ATOM   1029  CG  LEU A 153      48.291 -31.334  88.190  1.00 71.77           C  
ANISOU 1029  CG  LEU A 153     6257   8170  12841   3383    334  -1036       C  
ATOM   1030  CD1 LEU A 153      46.839 -31.390  88.647  1.00 66.96           C  
ANISOU 1030  CD1 LEU A 153     6045   7463  11934   3287    243   -802       C  
ATOM   1031  CD2 LEU A 153      48.675 -32.609  87.456  1.00 75.56           C  
ANISOU 1031  CD2 LEU A 153     6910   8513  13287   3659    481  -1037       C  
ATOM   1032  N   PHE A 154      49.991 -27.409  86.806  1.00 83.99           N  
ANISOU 1032  N   PHE A 154     6706   9919  15287   2341    795  -1651       N  
ATOM   1033  CA  PHE A 154      50.008 -26.064  86.252  1.00 85.33           C  
ANISOU 1033  CA  PHE A 154     6743  10031  15647   1929   1015  -1756       C  
ATOM   1034  C   PHE A 154      51.088 -25.263  86.958  1.00 92.41           C  
ANISOU 1034  C   PHE A 154     7239  11091  16780   1914    894  -2026       C  
ATOM   1035  O   PHE A 154      51.149 -25.250  88.191  1.00 93.63           O  
ANISOU 1035  O   PHE A 154     7335  11402  16840   2098    558  -2021       O  
ATOM   1036  CB  PHE A 154      48.644 -25.391  86.413  1.00 77.61           C  
ANISOU 1036  CB  PHE A 154     6053   8982  14454   1702    977  -1531       C  
ATOM   1037  CG  PHE A 154      47.520 -26.151  85.772  1.00 74.44           C  
ANISOU 1037  CG  PHE A 154     6026   8414  13845   1698   1074  -1288       C  
ATOM   1038  CD1 PHE A 154      47.280 -26.039  84.414  1.00 74.91           C  
ANISOU 1038  CD1 PHE A 154     6207   8254  14003   1465   1433  -1260       C  
ATOM   1039  CD2 PHE A 154      46.709 -26.985  86.525  1.00 69.61           C  
ANISOU 1039  CD2 PHE A 154     5669   7832  12947   1922    827  -1097       C  
ATOM   1040  CE1 PHE A 154      46.248 -26.738  83.818  1.00 73.83           C  
ANISOU 1040  CE1 PHE A 154     6412   7949  13691   1453   1523  -1045       C  
ATOM   1041  CE2 PHE A 154      45.676 -27.687  85.934  1.00 69.49           C  
ANISOU 1041  CE2 PHE A 154     5993   7644  12766   1898    922   -902       C  
ATOM   1042  CZ  PHE A 154      45.445 -27.563  84.579  1.00 70.48           C  
ANISOU 1042  CZ  PHE A 154     6209   7569  13003   1662   1260   -876       C  
ATOM   1043  N   LYS A 155      51.941 -24.608  86.178  1.00 97.87           N  
ANISOU 1043  N   LYS A 155     7675  11722  17790   1688   1183  -2276       N  
ATOM   1044  CA  LYS A 155      53.005 -23.776  86.723  1.00103.74           C  
ANISOU 1044  CA  LYS A 155     8019  12591  18806   1625   1116  -2587       C  
ATOM   1045  C   LYS A 155      52.473 -22.372  86.987  1.00101.68           C  
ANISOU 1045  C   LYS A 155     7827  12288  18518   1307   1140  -2572       C  
ATOM   1046  O   LYS A 155      51.797 -21.786  86.134  1.00101.08           O  
ANISOU 1046  O   LYS A 155     7984  12018  18404   1024   1421  -2464       O  
ATOM   1047  CB  LYS A 155      54.186 -23.734  85.753  1.00106.70           C  
ANISOU 1047  CB  LYS A 155     8091  12896  19553   1517   1456  -2896       C  
ATOM   1048  CG  LYS A 155      55.516 -23.336  86.368  1.00116.61           C  
ANISOU 1048  CG  LYS A 155     8855  14317  21133   1573   1339  -3280       C  
ATOM   1049  CD  LYS A 155      56.547 -23.069  85.281  1.00127.20           C  
ANISOU 1049  CD  LYS A 155     9926  15543  22862   1360   1766  -3603       C  
ATOM   1050  CE  LYS A 155      57.826 -22.481  85.854  1.00137.59           C  
ANISOU 1050  CE  LYS A 155    10728  17007  24541   1345   1683  -4039       C  
ATOM   1051  NZ  LYS A 155      58.861 -22.278  84.800  1.00146.66           N  
ANISOU 1051  NZ  LYS A 155    11602  18034  26089   1131   2129  -4386       N  
ATOM   1052  N   SER A 156      52.777 -21.839  88.169  1.00 98.63           N  
ANISOU 1052  N   SER A 156     7261  12068  18148   1373    847  -2682       N  
ATOM   1053  CA  SER A 156      52.359 -20.499  88.569  1.00 96.67           C  
ANISOU 1053  CA  SER A 156     7065  11796  17870   1114    844  -2689       C  
ATOM   1054  C   SER A 156      53.605 -19.640  88.744  1.00 96.25           C  
ANISOU 1054  C   SER A 156     6600  11798  18173    989    911  -3091       C  
ATOM   1055  O   SER A 156      54.414 -19.886  89.646  1.00 98.85           O  
ANISOU 1055  O   SER A 156     6631  12307  18621   1204    629  -3292       O  
ATOM   1056  CB  SER A 156      51.532 -20.542  89.854  1.00 99.41           C  
ANISOU 1056  CB  SER A 156     7596  12263  17911   1273    461  -2472       C  
ATOM   1057  OG  SER A 156      52.364 -20.646  90.997  1.00108.67           O  
ANISOU 1057  OG  SER A 156     8484  13607  19199   1490    140  -2684       O  
ATOM   1058  N   THR A 157      53.761 -18.641  87.881  1.00 96.42           N  
ANISOU 1058  N   THR A 157     6617  11645  18374    648   1290  -3230       N  
ATOM   1059  CA  THR A 157      54.868 -17.702  87.951  1.00101.01           C  
ANISOU 1059  CA  THR A 157     6840  12238  19301    470   1427  -3635       C  
ATOM   1060  C   THR A 157      54.324 -16.294  88.142  1.00 99.68           C  
ANISOU 1060  C   THR A 157     6837  11975  19063    201   1522  -3613       C  
ATOM   1061  O   THR A 157      53.183 -15.999  87.774  1.00 97.71           O  
ANISOU 1061  O   THR A 157     6978  11585  18562     94   1618  -3316       O  
ATOM   1062  CB  THR A 157      55.735 -17.756  86.684  1.00106.44           C  
ANISOU 1062  CB  THR A 157     7367  12763  20311    292   1878  -3894       C  
ATOM   1063  OG1 THR A 157      54.921 -17.487  85.535  1.00102.89           O  
ANISOU 1063  OG1 THR A 157     7315  12039  19741     59   2252  -3685       O  
ATOM   1064  CG2 THR A 157      56.379 -19.127  86.538  1.00108.76           C  
ANISOU 1064  CG2 THR A 157     7455  13168  20700    585   1784  -3948       C  
ATOM   1065  N   ALA A 158      55.147 -15.423  88.731  1.00102.66           N  
ANISOU 1065  N   ALA A 158     6908  12430  19670    106   1492  -3946       N  
ATOM   1066  CA  ALA A 158      54.732 -14.035  88.893  1.00 95.74           C  
ANISOU 1066  CA  ALA A 158     6174  11455  18747   -146   1619  -3961       C  
ATOM   1067  C   ALA A 158      54.450 -13.387  87.546  1.00 99.57           C  
ANISOU 1067  C   ALA A 158     6921  11638  19274   -453   2138  -3948       C  
ATOM   1068  O   ALA A 158      53.579 -12.515  87.443  1.00 99.85           O  
ANISOU 1068  O   ALA A 158     7273  11544  19121   -599   2244  -3774       O  
ATOM   1069  CB  ALA A 158      55.798 -13.248  89.653  1.00 94.55           C  
ANISOU 1069  CB  ALA A 158     5609  11412  18903   -213   1551  -4400       C  
ATOM   1070  N   ARG A 159      55.173 -13.801  86.503  1.00109.54           N  
ANISOU 1070  N   ARG A 159     8073  12770  20776   -542   2474  -4135       N  
ATOM   1071  CA  ARG A 159      54.896 -13.287  85.167  1.00122.31           C  
ANISOU 1071  CA  ARG A 159    10004  14058  22412   -818   2992  -4115       C  
ATOM   1072  C   ARG A 159      53.488 -13.649  84.721  1.00120.15           C  
ANISOU 1072  C   ARG A 159    10209  13667  21776   -757   2962  -3658       C  
ATOM   1073  O   ARG A 159      52.796 -12.830  84.103  1.00118.27           O  
ANISOU 1073  O   ARG A 159    10329  13195  21413   -943   3234  -3548       O  
ATOM   1074  CB  ARG A 159      55.922 -13.835  84.178  1.00136.27           C  
ANISOU 1074  CB  ARG A 159    11578  15707  24492   -900   3346  -4386       C  
ATOM   1075  CG  ARG A 159      55.630 -13.521  82.723  1.00141.36           C  
ANISOU 1075  CG  ARG A 159    12611  15971  25127  -1158   3899  -4341       C  
ATOM   1076  CD  ARG A 159      56.544 -14.332  81.821  1.00151.07           C  
ANISOU 1076  CD  ARG A 159    13670  17103  26626  -1187   4197  -4547       C  
ATOM   1077  NE  ARG A 159      56.251 -15.763  81.864  1.00154.45           N  
ANISOU 1077  NE  ARG A 159    14078  17681  26923   -886   3917  -4293       N  
ATOM   1078  CZ  ARG A 159      55.379 -16.372  81.069  1.00151.08           C  
ANISOU 1078  CZ  ARG A 159    14051  17087  26268   -854   4030  -3965       C  
ATOM   1079  NH1 ARG A 159      54.709 -15.678  80.160  1.00148.96           N  
ANISOU 1079  NH1 ARG A 159    14239  16488  25871  -1087   4402  -3846       N  
ATOM   1080  NH2 ARG A 159      55.180 -17.678  81.178  1.00148.12           N  
ANISOU 1080  NH2 ARG A 159    13636  16860  25782   -574   3781  -3769       N  
ATOM   1081  N   ARG A 160      53.043 -14.872  85.025  1.00119.52           N  
ANISOU 1081  N   ARG A 160    10150  13741  21522   -486   2641  -3406       N  
ATOM   1082  CA  ARG A 160      51.689 -15.269  84.665  1.00114.78           C  
ANISOU 1082  CA  ARG A 160     9969  13046  20596   -427   2593  -3002       C  
ATOM   1083  C   ARG A 160      50.644 -14.794  85.665  1.00103.96           C  
ANISOU 1083  C   ARG A 160     8765  11797  18939   -353   2257  -2761       C  
ATOM   1084  O   ARG A 160      49.459 -14.734  85.317  1.00101.58           O  
ANISOU 1084  O   ARG A 160     8819  11381  18396   -371   2278  -2473       O  
ATOM   1085  CB  ARG A 160      51.594 -16.787  84.512  1.00122.57           C  
ANISOU 1085  CB  ARG A 160    10945  14119  21505   -185   2440  -2842       C  
ATOM   1086  CG  ARG A 160      52.426 -17.348  83.379  1.00135.44           C  
ANISOU 1086  CG  ARG A 160    12485  15598  23377   -252   2806  -3019       C  
ATOM   1087  CD  ARG A 160      51.801 -16.943  82.056  1.00140.46           C  
ANISOU 1087  CD  ARG A 160    13532  15882  23952   -488   3249  -2901       C  
ATOM   1088  NE  ARG A 160      50.402 -17.344  81.956  1.00139.11           N  
ANISOU 1088  NE  ARG A 160    13733  15669  23454   -397   3105  -2514       N  
ATOM   1089  CZ  ARG A 160      49.982 -18.506  81.473  1.00137.39           C  
ANISOU 1089  CZ  ARG A 160    13657  15418  23125   -262   3095  -2319       C  
ATOM   1090  NH1 ARG A 160      50.860 -19.399  81.045  1.00139.01           N  
ANISOU 1090  NH1 ARG A 160    13678  15634  23504   -181   3217  -2458       N  
ATOM   1091  NH2 ARG A 160      48.684 -18.773  81.423  1.00131.74           N  
ANISOU 1091  NH2 ARG A 160    13262  14662  22133   -204   2971  -1999       N  
ATOM   1092  N   ALA A 161      51.049 -14.446  86.888  1.00 97.73           N  
ANISOU 1092  N   ALA A 161     7728  11225  18180   -270   1960  -2884       N  
ATOM   1093  CA  ALA A 161      50.105 -13.837  87.818  1.00 88.02           C  
ANISOU 1093  CA  ALA A 161     6669  10079  16697   -238   1701  -2683       C  
ATOM   1094  C   ALA A 161      49.730 -12.434  87.370  1.00 87.37           C  
ANISOU 1094  C   ALA A 161     6784   9802  16610   -490   1992  -2712       C  
ATOM   1095  O   ALA A 161      48.592 -11.997  87.581  1.00 87.92           O  
ANISOU 1095  O   ALA A 161     7133   9842  16430   -489   1905  -2461       O  
ATOM   1096  CB  ALA A 161      50.689 -13.810  89.231  1.00 88.03           C  
ANISOU 1096  CB  ALA A 161     6375  10334  16737    -87   1334  -2825       C  
ATOM   1097  N   LEU A 162      50.670 -11.722  86.747  1.00 89.87           N  
ANISOU 1097  N   LEU A 162     6968   9978  17201   -701   2356  -3031       N  
ATOM   1098  CA  LEU A 162      50.362 -10.406  86.204  1.00 87.25           C  
ANISOU 1098  CA  LEU A 162     6872   9424  16854   -936   2700  -3077       C  
ATOM   1099  C   LEU A 162      49.378 -10.503  85.046  1.00 85.33           C  
ANISOU 1099  C   LEU A 162     7061   8930  16430   -981   2953  -2824       C  
ATOM   1100  O   LEU A 162      48.591  -9.576  84.824  1.00 91.27           O  
ANISOU 1100  O   LEU A 162     8110   9547  17022  -1067   3091  -2710       O  
ATOM   1101  CB  LEU A 162      51.649  -9.713  85.748  1.00 92.77           C  
ANISOU 1101  CB  LEU A 162     7353  10003  17891  -1164   3085  -3509       C  
ATOM   1102  CG  LEU A 162      51.584  -8.206  85.490  1.00 97.72           C  
ANISOU 1102  CG  LEU A 162     8168  10440  18523  -1408   3433  -3647       C  
ATOM   1103  CD1 LEU A 162      51.739  -7.433  86.792  1.00101.97           C  
ANISOU 1103  CD1 LEU A 162     8489  11185  19069  -1396   3162  -3751       C  
ATOM   1104  CD2 LEU A 162      52.634  -7.778  84.473  1.00104.53           C  
ANISOU 1104  CD2 LEU A 162     8990  11056  19669  -1666   3980  -4022       C  
ATOM   1105  N   GLY A 163      49.407 -11.610  84.298  1.00 78.93           N  
ANISOU 1105  N   GLY A 163     6295   8054  15640   -912   3022  -2743       N  
ATOM   1106  CA  GLY A 163      48.435 -11.805  83.237  1.00 77.48           C  
ANISOU 1106  CA  GLY A 163     6523   7638  15276   -930   3232  -2498       C  
ATOM   1107  C   GLY A 163      47.080 -12.215  83.756  1.00 82.01           C  
ANISOU 1107  C   GLY A 163     7275   8334  15553   -752   2871  -2135       C  
ATOM   1108  O   GLY A 163      46.055 -11.885  83.152  1.00 95.14           O  
ANISOU 1108  O   GLY A 163     9284   9831  17035   -772   2998  -1939       O  
ATOM   1109  N   SER A 164      47.053 -12.942  84.871  1.00 76.87           N  
ANISOU 1109  N   SER A 164     6405   7962  14839   -567   2435  -2056       N  
ATOM   1110  CA  SER A 164      45.785 -13.255  85.513  1.00 74.36           C  
ANISOU 1110  CA  SER A 164     6255   7762  14237   -421   2101  -1747       C  
ATOM   1111  C   SER A 164      45.156 -11.999  86.099  1.00 72.44           C  
ANISOU 1111  C   SER A 164     6120   7532  13872   -482   2039  -1698       C  
ATOM   1112  O   SER A 164      43.939 -11.799  86.001  1.00 63.13           O  
ANISOU 1112  O   SER A 164     5196   6302  12487   -453   1984  -1464       O  
ATOM   1113  CB  SER A 164      45.996 -14.307  86.600  1.00 74.14           C  
ANISOU 1113  CB  SER A 164     6016   8004  14149   -210   1701  -1706       C  
ATOM   1114  OG  SER A 164      46.463 -15.528  86.051  1.00 78.58           O  
ANISOU 1114  OG  SER A 164     6501   8560  14798   -119   1752  -1725       O  
ATOM   1115  N   ILE A 165      45.975 -11.147  86.720  1.00 75.73           N  
ANISOU 1115  N   ILE A 165     6329   8020  14424   -563   2049  -1929       N  
ATOM   1116  CA  ILE A 165      45.462  -9.908  87.295  1.00 68.25           C  
ANISOU 1116  CA  ILE A 165     5475   7083  13375   -628   2015  -1902       C  
ATOM   1117  C   ILE A 165      44.797  -9.051  86.226  1.00 74.35           C  
ANISOU 1117  C   ILE A 165     6573   7597  14082   -753   2371  -1837       C  
ATOM   1118  O   ILE A 165      43.736  -8.460  86.460  1.00 81.88           O  
ANISOU 1118  O   ILE A 165     7721   8545  14843   -724   2290  -1651       O  
ATOM   1119  CB  ILE A 165      46.595  -9.145  88.006  1.00 67.03           C  
ANISOU 1119  CB  ILE A 165     5028   7019  13421   -719   2028  -2209       C  
ATOM   1120  CG1 ILE A 165      46.863  -9.766  89.376  1.00 65.52           C  
ANISOU 1120  CG1 ILE A 165     4593   7107  13195   -543   1592  -2205       C  
ATOM   1121  CG2 ILE A 165      46.246  -7.669  88.127  1.00 70.62           C  
ANISOU 1121  CG2 ILE A 165     5622   7384  13827   -861   2187  -2245       C  
ATOM   1122  CD1 ILE A 165      48.220  -9.435  89.950  1.00 72.46           C  
ANISOU 1122  CD1 ILE A 165     5102   8090  14338   -591   1581  -2556       C  
ATOM   1123  N   LEU A 166      45.405  -8.964  85.038  1.00 79.79           N  
ANISOU 1123  N   LEU A 166     7342   8059  14916   -885   2788  -1996       N  
ATOM   1124  CA  LEU A 166      44.796  -8.180  83.966  1.00 76.72           C  
ANISOU 1124  CA  LEU A 166     7331   7405  14414   -980   3169  -1939       C  
ATOM   1125  C   LEU A 166      43.494  -8.810  83.487  1.00 71.97           C  
ANISOU 1125  C   LEU A 166     6993   6763  13591   -837   3069  -1620       C  
ATOM   1126  O   LEU A 166      42.547  -8.098  83.132  1.00 73.41           O  
ANISOU 1126  O   LEU A 166     7457   6852  13582   -827   3179  -1480       O  
ATOM   1127  CB  LEU A 166      45.778  -8.017  82.804  1.00 80.07           C  
ANISOU 1127  CB  LEU A 166     7840   7573  15010  -1153   3674  -2196       C  
ATOM   1128  CG  LEU A 166      46.867  -6.964  83.022  1.00 83.85           C  
ANISOU 1128  CG  LEU A 166     8170   8009  15682  -1353   3921  -2542       C  
ATOM   1129  CD1 LEU A 166      47.869  -6.974  81.879  1.00 89.26           C  
ANISOU 1129  CD1 LEU A 166     8931   8429  16553  -1531   4428  -2817       C  
ATOM   1130  CD2 LEU A 166      46.249  -5.584  83.188  1.00 83.31           C  
ANISOU 1130  CD2 LEU A 166     8344   7879  15433  -1422   4045  -2503       C  
ATOM   1131  N   GLY A 167      43.425 -10.142  83.472  1.00 71.43           N  
ANISOU 1131  N   GLY A 167     6830   6772  13539   -721   2868  -1510       N  
ATOM   1132  CA  GLY A 167      42.182 -10.797  83.105  1.00 70.50           C  
ANISOU 1132  CA  GLY A 167     6924   6631  13232   -592   2754  -1226       C  
ATOM   1133  C   GLY A 167      41.094 -10.589  84.140  1.00 65.84           C  
ANISOU 1133  C   GLY A 167     6322   6229  12466   -485   2371  -1026       C  
ATOM   1134  O   GLY A 167      39.914 -10.462  83.800  1.00 60.97           O  
ANISOU 1134  O   GLY A 167     5914   5563  11689   -421   2359   -830       O  
ATOM   1135  N   ILE A 168      41.474 -10.553  85.419  1.00 69.17           N  
ANISOU 1135  N   ILE A 168     6505   6871  12905   -457   2065  -1083       N  
ATOM   1136  CA  ILE A 168      40.499 -10.281  86.471  1.00 63.54           C  
ANISOU 1136  CA  ILE A 168     5814   6319  12010   -372   1738   -917       C  
ATOM   1137  C   ILE A 168      39.847  -8.924  86.254  1.00 62.01           C  
ANISOU 1137  C   ILE A 168     5793   6018  11750   -434   1901   -886       C  
ATOM   1138  O   ILE A 168      38.629  -8.769  86.411  1.00 63.74           O  
ANISOU 1138  O   ILE A 168     6142   6260  11816   -359   1763   -691       O  
ATOM   1139  CB  ILE A 168      41.174 -10.363  87.851  1.00 64.84           C  
ANISOU 1139  CB  ILE A 168     5735   6713  12187   -336   1457  -1018       C  
ATOM   1140  CG1 ILE A 168      41.539 -11.810  88.171  1.00 61.14           C  
ANISOU 1140  CG1 ILE A 168     5143   6377  11712   -219   1256   -996       C  
ATOM   1141  CG2 ILE A 168      40.267  -9.780  88.919  1.00 67.03           C  
ANISOU 1141  CG2 ILE A 168     6078   7111  12280   -287   1213   -889       C  
ATOM   1142  CD1 ILE A 168      42.342 -11.957  89.432  1.00 61.15           C  
ANISOU 1142  CD1 ILE A 168     4907   6588  11739   -152   1020  -1121       C  
ATOM   1143  N   TRP A 169      40.646  -7.917  85.895  1.00 62.80           N  
ANISOU 1143  N   TRP A 169     5896   6001  11962   -576   2213  -1091       N  
ATOM   1144  CA  TRP A 169      40.092  -6.589  85.656  1.00 56.72           C  
ANISOU 1144  CA  TRP A 169     5329   5124  11098   -643   2417  -1072       C  
ATOM   1145  C   TRP A 169      39.227  -6.555  84.401  1.00 61.07           C  
ANISOU 1145  C   TRP A 169     6202   5504  11498   -614   2668   -920       C  
ATOM   1146  O   TRP A 169      38.155  -5.939  84.398  1.00 67.65           O  
ANISOU 1146  O   TRP A 169     7207   6339  12158   -575   2634   -754       O  
ATOM   1147  CB  TRP A 169      41.216  -5.562  85.572  1.00 51.42           C  
ANISOU 1147  CB  TRP A 169     4618   4361  10557   -825   2727  -1349       C  
ATOM   1148  CG  TRP A 169      41.718  -5.154  86.916  1.00 55.92           C  
ANISOU 1148  CG  TRP A 169     4923   5118  11205   -849   2479  -1463       C  
ATOM   1149  CD1 TRP A 169      42.792  -5.666  87.584  1.00 56.46           C  
ANISOU 1149  CD1 TRP A 169     4683   5329  11440   -857   2324  -1640       C  
ATOM   1150  CD2 TRP A 169      41.155  -4.150  87.769  1.00 54.64           C  
ANISOU 1150  CD2 TRP A 169     4790   5027  10945   -857   2361  -1409       C  
ATOM   1151  NE1 TRP A 169      42.935  -5.038  88.799  1.00 55.14           N  
ANISOU 1151  NE1 TRP A 169     4362   5316  11271   -866   2120  -1701       N  
ATOM   1152  CE2 TRP A 169      41.943  -4.103  88.936  1.00 51.52           C  
ANISOU 1152  CE2 TRP A 169     4111   4810  10656   -874   2144  -1560       C  
ATOM   1153  CE3 TRP A 169      40.062  -3.283  87.657  1.00 50.43           C  
ANISOU 1153  CE3 TRP A 169     4498   4421  10242   -848   2425  -1251       C  
ATOM   1154  CZ2 TRP A 169      41.674  -3.225  89.984  1.00 46.86           C  
ANISOU 1154  CZ2 TRP A 169     3483   4314  10009   -891   2002  -1558       C  
ATOM   1155  CZ3 TRP A 169      39.797  -2.411  88.699  1.00 50.56           C  
ANISOU 1155  CZ3 TRP A 169     4464   4528  10217   -867   2283  -1249       C  
ATOM   1156  CH2 TRP A 169      40.599  -2.389  89.847  1.00 45.09           C  
ANISOU 1156  CH2 TRP A 169     3498   4002   9632   -893   2078  -1402       C  
ATOM   1157  N   ALA A 170      39.676  -7.198  83.321  1.00 58.94           N  
ANISOU 1157  N   ALA A 170     6036   5096  11262   -636   2924   -971       N  
ATOM   1158  CA  ALA A 170      38.892  -7.195  82.091  1.00 55.80           C  
ANISOU 1158  CA  ALA A 170     5998   4574  10628   -612   3163   -815       C  
ATOM   1159  C   ALA A 170      37.530  -7.843  82.300  1.00 56.62           C  
ANISOU 1159  C   ALA A 170     6108   4808  10596   -463   2821   -538       C  
ATOM   1160  O   ALA A 170      36.515  -7.354  81.792  1.00 61.45           O  
ANISOU 1160  O   ALA A 170     7034   5382  10931   -461   2818   -356       O  
ATOM   1161  CB  ALA A 170      39.658  -7.911  80.978  1.00 52.95           C  
ANISOU 1161  CB  ALA A 170     5746   4058  10315   -652   3481   -923       C  
ATOM   1162  N   VAL A 171      37.487  -8.948  83.046  1.00 54.58           N  
ANISOU 1162  N   VAL A 171     5574   4677  10488   -355   2486   -501       N  
ATOM   1163  CA  VAL A 171      36.218  -9.626  83.297  1.00 57.40           C  
ANISOU 1163  CA  VAL A 171     5915   5148  10747   -226   2177   -274       C  
ATOM   1164  C   VAL A 171      35.324  -8.779  84.194  1.00 58.77           C  
ANISOU 1164  C   VAL A 171     6057   5423  10851   -195   1946   -180       C  
ATOM   1165  O   VAL A 171      34.146  -8.559  83.893  1.00 56.40           O  
ANISOU 1165  O   VAL A 171     5911   5131  10388   -166   1864     -7       O  
ATOM   1166  CB  VAL A 171      36.468 -11.017  83.902  1.00 57.32           C  
ANISOU 1166  CB  VAL A 171     5712   5224  10844   -154   1894   -260       C  
ATOM   1167  CG1 VAL A 171      35.164 -11.624  84.385  1.00 53.77           C  
ANISOU 1167  CG1 VAL A 171     5255   4889  10288    -52   1562    -58       C  
ATOM   1168  CG2 VAL A 171      37.143 -11.918  82.886  1.00 54.75           C  
ANISOU 1168  CG2 VAL A 171     5436   4770  10594   -168   2138   -320       C  
ATOM   1169  N   SER A 172      35.871  -8.287  85.309  1.00 57.52           N  
ANISOU 1169  N   SER A 172     5742   5343  10770   -225   1807   -291       N  
ATOM   1170  CA  SER A 172      35.078  -7.471  86.225  1.00 50.36           C  
ANISOU 1170  CA  SER A 172     4817   4525   9795   -196   1610   -216       C  
ATOM   1171  C   SER A 172      34.552  -6.218  85.536  1.00 45.64           C  
ANISOU 1171  C   SER A 172     4447   3805   9091   -260   1868   -169       C  
ATOM   1172  O   SER A 172      33.387  -5.843  85.717  1.00 50.47           O  
ANISOU 1172  O   SER A 172     5138   4434   9603   -205   1717    -12       O  
ATOM   1173  CB  SER A 172      35.910  -7.099  87.451  1.00 53.22           C  
ANISOU 1173  CB  SER A 172     5021   5006  10194   -249   1468   -357       C  
ATOM   1174  OG  SER A 172      36.312  -8.255  88.166  1.00 58.53           O  
ANISOU 1174  OG  SER A 172     5567   5832  10839   -204   1209   -364       O  
ATOM   1175  N   LEU A 173      35.393  -5.553  84.738  1.00 49.70           N  
ANISOU 1175  N   LEU A 173     5150   4169   9566   -394   2240   -298       N  
ATOM   1176  CA  LEU A 173      34.938  -4.351  84.048  1.00 50.25           C  
ANISOU 1176  CA  LEU A 173     5642   4070   9381   -469   2450   -233       C  
ATOM   1177  C   LEU A 173      33.800  -4.656  83.083  1.00 48.50           C  
ANISOU 1177  C   LEU A 173     5814   3746   8869   -368   2331    -21       C  
ATOM   1178  O   LEU A 173      32.912  -3.818  82.885  1.00 53.62           O  
ANISOU 1178  O   LEU A 173     6820   4284   9269   -296   2238     89       O  
ATOM   1179  CB  LEU A 173      36.101  -3.693  83.302  1.00 58.33           C  
ANISOU 1179  CB  LEU A 173     6860   4930  10374   -630   2890   -427       C  
ATOM   1180  CG  LEU A 173      37.171  -2.984  84.138  1.00 59.77           C  
ANISOU 1180  CG  LEU A 173     6795   5145  10768   -745   3003   -674       C  
ATOM   1181  CD1 LEU A 173      38.342  -2.565  83.261  1.00 55.49           C  
ANISOU 1181  CD1 LEU A 173     6424   4424  10235   -907   3466   -899       C  
ATOM   1182  CD2 LEU A 173      36.582  -1.779  84.855  1.00 55.96           C  
ANISOU 1182  CD2 LEU A 173     6408   4667  10186   -769   2929   -618       C  
ATOM   1183  N   ALA A 174      33.807  -5.842  82.473  1.00 49.96           N  
ANISOU 1183  N   ALA A 174     5977   3950   9057   -323   2292     19       N  
ATOM   1184  CA  ALA A 174      32.775  -6.184  81.500  1.00 53.99           C  
ANISOU 1184  CA  ALA A 174     6897   4355   9261   -201   2126    179       C  
ATOM   1185  C   ALA A 174      31.470  -6.602  82.169  1.00 55.79           C  
ANISOU 1185  C   ALA A 174     6976   4714   9509    -37   1697    312       C  
ATOM   1186  O   ALA A 174      30.401  -6.083  81.837  1.00 57.94           O  
ANISOU 1186  O   ALA A 174     7575   4899   9540    112   1500    402       O  
ATOM   1187  CB  ALA A 174      33.276  -7.297  80.580  1.00 56.49           C  
ANISOU 1187  CB  ALA A 174     7268   4637   9559   -224   2254    157       C  
ATOM   1188  N   ILE A 175      31.533  -7.545  83.113  1.00 53.78           N  
ANISOU 1188  N   ILE A 175     6230   4668   9536    -35   1540    306       N  
ATOM   1189  CA  ILE A 175      30.310  -8.136  83.646  1.00 55.27           C  
ANISOU 1189  CA  ILE A 175     6268   4996   9736    101   1166    412       C  
ATOM   1190  C   ILE A 175      29.505  -7.158  84.495  1.00 57.18           C  
ANISOU 1190  C   ILE A 175     6464   5293   9969    179    988    447       C  
ATOM   1191  O   ILE A 175      28.320  -7.402  84.748  1.00 57.47           O  
ANISOU 1191  O   ILE A 175     6453   5443   9938    316    689    510       O  
ATOM   1192  CB  ILE A 175      30.632  -9.413  84.443  1.00 57.80           C  
ANISOU 1192  CB  ILE A 175     6135   5507  10318     75   1064    396       C  
ATOM   1193  CG1 ILE A 175      31.485  -9.093  85.669  1.00 59.27           C  
ANISOU 1193  CG1 ILE A 175     5996   5771  10753     60   1096    289       C  
ATOM   1194  CG2 ILE A 175      31.324 -10.435  83.545  1.00 61.11           C  
ANISOU 1194  CG2 ILE A 175     6632   5864  10724     39   1225    365       C  
ATOM   1195  CD1 ILE A 175      31.674 -10.276  86.580  1.00 52.80           C  
ANISOU 1195  CD1 ILE A 175     5152   5059   9850     44    824    279       C  
ATOM   1196  N   MET A 176      30.105  -6.058  84.949  1.00 55.15           N  
ANISOU 1196  N   MET A 176     6208   4978   9769     92   1170    383       N  
ATOM   1197  CA  MET A 176      29.390  -5.076  85.756  1.00 49.24           C  
ANISOU 1197  CA  MET A 176     5447   4263   9000    167   1028    413       C  
ATOM   1198  C   MET A 176      28.745  -3.973  84.924  1.00 52.01           C  
ANISOU 1198  C   MET A 176     6329   4409   9024    295   1043    456       C  
ATOM   1199  O   MET A 176      28.159  -3.045  85.499  1.00 51.95           O  
ANISOU 1199  O   MET A 176     6370   4403   8965    385    947    474       O  
ATOM   1200  CB  MET A 176      30.336  -4.463  86.796  1.00 43.87           C  
ANISOU 1200  CB  MET A 176     4493   3627   8549     17   1186    307       C  
ATOM   1201  CG  MET A 176      30.785  -5.468  87.835  1.00 44.94           C  
ANISOU 1201  CG  MET A 176     4176   3961   8938     21   1039    251       C  
ATOM   1202  SD  MET A 176      29.379  -6.381  88.502  1.00 47.05           S  
ANISOU 1202  SD  MET A 176     4420   4414   9043     66    619    382       S  
ATOM   1203  CE  MET A 176      30.210  -7.504  89.610  1.00 46.70           C  
ANISOU 1203  CE  MET A 176     4377   4543   8823     37    460    285       C  
ATOM   1204  N   VAL A 177      28.844  -4.051  83.593  1.00 50.74           N  
ANISOU 1204  N   VAL A 177     6596   4063   8620    322   1150    469       N  
ATOM   1205  CA  VAL A 177      28.172  -3.064  82.740  1.00 51.79           C  
ANISOU 1205  CA  VAL A 177     7295   3984   8399    493   1099    510       C  
ATOM   1206  C   VAL A 177      26.668  -3.052  82.956  1.00 47.04           C  
ANISOU 1206  C   VAL A 177     6683   3471   7718    787    687    574       C  
ATOM   1207  O   VAL A 177      26.084  -1.963  83.037  1.00 50.77           O  
ANISOU 1207  O   VAL A 177     7399   3863   8029    943    597    584       O  
ATOM   1208  CB  VAL A 177      28.560  -3.287  81.270  1.00 55.51           C  
ANISOU 1208  CB  VAL A 177     8210   4261   8619    469   1252    506       C  
ATOM   1209  CG1 VAL A 177      27.695  -2.407  80.371  1.00 57.70           C  
ANISOU 1209  CG1 VAL A 177     9044   4356   8525    698   1102    552       C  
ATOM   1210  CG2 VAL A 177      30.025  -2.980  81.065  1.00 47.81           C  
ANISOU 1210  CG2 VAL A 177     7253   3212   7699    196   1706    406       C  
ATOM   1211  N   PRO A 178      25.980  -4.192  83.032  1.00 46.32           N  
ANISOU 1211  N   PRO A 178     6308   3565   7728    876    426    596       N  
ATOM   1212  CA  PRO A 178      24.524  -4.148  83.251  1.00 41.75           C  
ANISOU 1212  CA  PRO A 178     5641   3142   7080   1143     38    602       C  
ATOM   1213  C   PRO A 178      24.152  -3.406  84.512  1.00 47.31           C  
ANISOU 1213  C   PRO A 178     6072   4026   7877   1154    -25    578       C  
ATOM   1214  O   PRO A 178      23.099  -2.758  84.556  1.00 52.49           O  
ANISOU 1214  O   PRO A 178     6830   4734   8379   1394   -241    562       O  
ATOM   1215  CB  PRO A 178      24.136  -5.630  83.333  1.00 40.76           C  
ANISOU 1215  CB  PRO A 178     5137   3253   7095   1094   -143    585       C  
ATOM   1216  CG  PRO A 178      25.235  -6.358  82.640  1.00 42.65           C  
ANISOU 1216  CG  PRO A 178     5498   3331   7376    920    112    606       C  
ATOM   1217  CD  PRO A 178      26.476  -5.579  82.942  1.00 44.45           C  
ANISOU 1217  CD  PRO A 178     5791   3435   7661    728    470    589       C  
ATOM   1218  N   GLN A 179      24.986  -3.487  85.555  1.00 51.66           N  
ANISOU 1218  N   GLN A 179     6283   4680   8665    914    155    563       N  
ATOM   1219  CA  GLN A 179      24.736  -2.715  86.767  1.00 51.07           C  
ANISOU 1219  CA  GLN A 179     6012   4734   8658    904    124    541       C  
ATOM   1220  C   GLN A 179      24.692  -1.223  86.458  1.00 55.31           C  
ANISOU 1220  C   GLN A 179     6991   5015   9009   1035    225    554       C  
ATOM   1221  O   GLN A 179      23.776  -0.512  86.887  1.00 64.09           O  
ANISOU 1221  O   GLN A 179     8136   6198  10018   1219     56    543       O  
ATOM   1222  CB  GLN A 179      25.806  -3.026  87.807  1.00 45.05           C  
ANISOU 1222  CB  GLN A 179     4889   4059   8170    641    298    515       C  
ATOM   1223  CG  GLN A 179      25.546  -2.390  89.158  1.00 48.75           C  
ANISOU 1223  CG  GLN A 179     5156   4669   8698    606    244    489       C  
ATOM   1224  CD  GLN A 179      24.263  -2.893  89.802  1.00 53.47           C  
ANISOU 1224  CD  GLN A 179     5597   5557   9163    657    -18    462       C  
ATOM   1225  OE1 GLN A 179      24.150  -4.064  90.164  1.00 65.62           O  
ANISOU 1225  OE1 GLN A 179     6978   7264  10690    527    -89    436       O  
ATOM   1226  NE2 GLN A 179      23.286  -2.003  89.943  1.00 48.82           N  
ANISOU 1226  NE2 GLN A 179     5126   4991   8431    842   -123    448       N  
ATOM   1227  N   ALA A 180      25.686  -0.729  85.715  1.00 48.68           N  
ANISOU 1227  N   ALA A 180     6521   3889   8085    917    523    555       N  
ATOM   1228  CA  ALA A 180      25.682   0.674  85.311  1.00 50.48           C  
ANISOU 1228  CA  ALA A 180     7254   3866   8059    995    638    553       C  
ATOM   1229  C   ALA A 180      24.482   1.003  84.432  1.00 56.60           C  
ANISOU 1229  C   ALA A 180     8380   4567   8558   1329    332    581       C  
ATOM   1230  O   ALA A 180      23.901   2.088  84.544  1.00 65.98           O  
ANISOU 1230  O   ALA A 180     9765   5698   9608   1486    258    583       O  
ATOM   1231  CB  ALA A 180      26.980   1.011  84.581  1.00 45.98           C  
ANISOU 1231  CB  ALA A 180     6983   3081   7406    741   1035    512       C  
ATOM   1232  N   ALA A 181      24.097   0.082  83.544  1.00 54.72           N  
ANISOU 1232  N   ALA A 181     8176   4348   8266   1429    162    598       N  
ATOM   1233  CA  ALA A 181      23.024   0.373  82.597  1.00 55.66           C  
ANISOU 1233  CA  ALA A 181     8567   4449   8133   1709    -76    615       C  
ATOM   1234  C   ALA A 181      21.702   0.649  83.306  1.00 58.32           C  
ANISOU 1234  C   ALA A 181     8601   5035   8524   1941   -368    599       C  
ATOM   1235  O   ALA A 181      20.925   1.505  82.871  1.00 66.25           O  
ANISOU 1235  O   ALA A 181     9883   6023   9265   2163   -510    577       O  
ATOM   1236  CB  ALA A 181      22.866  -0.792  81.620  1.00 55.53           C  
ANISOU 1236  CB  ALA A 181     8586   4457   8054   1744   -190    622       C  
ATOM   1237  N   VAL A 182      21.427  -0.061  84.405  1.00 61.50           N  
ANISOU 1237  N   VAL A 182     8464   5712   9191   1897   -407    603       N  
ATOM   1238  CA  VAL A 182      20.136   0.076  85.085  1.00 53.63           C  
ANISOU 1238  CA  VAL A 182     7161   5043   8172   2051   -636    547       C  
ATOM   1239  C   VAL A 182      20.047   1.281  86.007  1.00 50.71           C  
ANISOU 1239  C   VAL A 182     6796   4637   7833   2083   -536    562       C  
ATOM   1240  O   VAL A 182      18.938   1.656  86.407  1.00 54.99           O  
ANISOU 1240  O   VAL A 182     7173   5376   8343   2221   -708    511       O  
ATOM   1241  CB  VAL A 182      19.811  -1.195  85.895  1.00 53.63           C  
ANISOU 1241  CB  VAL A 182     6648   5422   8306   1900   -739    461       C  
ATOM   1242  CG1 VAL A 182      19.663  -2.381  84.964  1.00 51.76           C  
ANISOU 1242  CG1 VAL A 182     6376   5224   8065   1878   -878    435       C  
ATOM   1243  CG2 VAL A 182      20.894  -1.455  86.931  1.00 50.89           C  
ANISOU 1243  CG2 VAL A 182     6093   5093   8151   1603   -551    450       C  
ATOM   1244  N   MET A 183      21.173   1.895  86.356  1.00 49.10           N  
ANISOU 1244  N   MET A 183     6752   4177   7729   1914   -284    593       N  
ATOM   1245  CA  MET A 183      21.151   3.048  87.244  1.00 44.77           C  
ANISOU 1245  CA  MET A 183     6223   3559   7230   1897   -285    542       C  
ATOM   1246  C   MET A 183      20.434   4.218  86.586  1.00 59.41           C  
ANISOU 1246  C   MET A 183     8494   5299   8782   2143   -343    552       C  
ATOM   1247  O   MET A 183      20.660   4.517  85.410  1.00 65.81           O  
ANISOU 1247  O   MET A 183     9780   5918   9305   2206   -308    562       O  
ATOM   1248  CB  MET A 183      22.571   3.457  87.630  1.00 46.47           C  
ANISOU 1248  CB  MET A 183     6683   3585   7387   1664      7    517       C  
ATOM   1249  CG  MET A 183      23.351   2.360  88.326  1.00 54.69           C  
ANISOU 1249  CG  MET A 183     7265   4828   8687   1378    158    523       C  
ATOM   1250  SD  MET A 183      22.341   1.518  89.561  1.00 48.65           S  
ANISOU 1250  SD  MET A 183     5900   4525   8058   1381    -92    476       S  
ATOM   1251  CE  MET A 183      22.088   2.829  90.756  1.00 42.45           C  
ANISOU 1251  CE  MET A 183     5139   3720   7271   1423    -37    458       C  
ATOM   1252  N   GLU A 184      19.565   4.877  87.346  1.00 60.03           N  
ANISOU 1252  N   GLU A 184     8422   5509   8879   2278   -433    531       N  
ATOM   1253  CA  GLU A 184      18.879   6.073  86.883  1.00 62.63           C  
ANISOU 1253  CA  GLU A 184     9143   5743   8911   2524   -523    504       C  
ATOM   1254  C   GLU A 184      18.854   7.099  88.001  1.00 66.66           C  
ANISOU 1254  C   GLU A 184     9626   6214   9486   2511   -415    496       C  
ATOM   1255  O   GLU A 184      18.661   6.754  89.170  1.00 64.27           O  
ANISOU 1255  O   GLU A 184     8866   6091   9463   2416   -408    487       O  
ATOM   1256  CB  GLU A 184      17.438   5.770  86.435  1.00 77.50           C  
ANISOU 1256  CB  GLU A 184    10871   7869  10707   2789   -851    436       C  
ATOM   1257  CG  GLU A 184      17.311   5.208  85.035  1.00 99.91           C  
ANISOU 1257  CG  GLU A 184    13968  10668  13325   2902  -1015    411       C  
ATOM   1258  CD  GLU A 184      18.076   6.037  84.027  1.00114.07           C  
ANISOU 1258  CD  GLU A 184    16465  12114  14763   2943   -861    454       C  
ATOM   1259  OE1 GLU A 184      17.899   7.273  84.030  1.00119.50           O  
ANISOU 1259  OE1 GLU A 184    17519  12664  15223   3090   -820    448       O  
ATOM   1260  OE2 GLU A 184      18.841   5.455  83.229  1.00114.98           O  
ANISOU 1260  OE2 GLU A 184    16789  12095  14802   2820   -753    491       O  
ATOM   1261  N   CYS A 185      19.045   8.359  87.630  1.00 79.14           N  
ANISOU 1261  N   CYS A 185    11739   7560  10772   2602   -305    502       N  
ATOM   1262  CA  CYS A 185      18.955   9.484  88.551  1.00 80.74           C  
ANISOU 1262  CA  CYS A 185    12021   7698  10959   2624   -202    491       C  
ATOM   1263  C   CYS A 185      17.629  10.164  88.247  1.00 86.39           C  
ANISOU 1263  C   CYS A 185    12859   8492  11471   2980   -437    450       C  
ATOM   1264  O   CYS A 185      17.448  10.725  87.162  1.00 89.20           O  
ANISOU 1264  O   CYS A 185    13718   8706  11469   3177   -491    447       O  
ATOM   1265  CB  CYS A 185      20.132  10.447  88.391  1.00 77.92           C  
ANISOU 1265  CB  CYS A 185    12186   7028  10391   2444    144    521       C  
ATOM   1266  SG  CYS A 185      20.473  11.501  89.837  1.00 78.29           S  
ANISOU 1266  SG  CYS A 185    12220   7003  10525   2311    356    503       S  
ATOM   1267  N   SER A 186      16.703  10.115  89.193  1.00 86.97           N  
ANISOU 1267  N   SER A 186    12497   8790  11758   3063   -568    403       N  
ATOM   1268  CA  SER A 186      15.374  10.661  88.982  1.00 89.67           C  
ANISOU 1268  CA  SER A 186    12867   9241  11961   3396   -805    330       C  
ATOM   1269  C   SER A 186      15.131  11.748  90.009  1.00 87.15           C  
ANISOU 1269  C   SER A 186    12584   8869  11661   3452   -702    319       C  
ATOM   1270  O   SER A 186      15.458  11.586  91.188  1.00 81.23           O  
ANISOU 1270  O   SER A 186    11515   8169  11178   3243   -555    333       O  
ATOM   1271  CB  SER A 186      14.295   9.580  89.110  1.00 92.83           C  
ANISOU 1271  CB  SER A 186    12699   9984  12589   3446  -1038    253       C  
ATOM   1272  OG  SER A 186      14.593   8.456  88.304  1.00 93.95           O  
ANISOU 1272  OG  SER A 186    12767  10188  12742   3349  -1110    264       O  
ATOM   1273  N   SER A 187      14.563  12.856  89.551  1.00 92.06           N  
ANISOU 1273  N   SER A 187    13628   9377  11974   3748   -785    287       N  
ATOM   1274  CA  SER A 187      14.218  13.925  90.463  1.00 95.81           C  
ANISOU 1274  CA  SER A 187    14164   9800  12438   3842   -703    271       C  
ATOM   1275  C   SER A 187      12.924  13.578  91.176  1.00 96.17           C  
ANISOU 1275  C   SER A 187    13651  10136  12754   3975   -890    176       C  
ATOM   1276  O   SER A 187      12.057  12.888  90.635  1.00 95.90           O  
ANISOU 1276  O   SER A 187    13359  10309  12769   4115  -1136     96       O  
ATOM   1277  CB  SER A 187      14.080  15.251  89.717  1.00101.13           C  
ANISOU 1277  CB  SER A 187    15532  10239  12656   4123   -705    273       C  
ATOM   1278  OG  SER A 187      14.292  16.342  90.594  1.00103.50           O  
ANISOU 1278  OG  SER A 187    16031  10393  12900   4097   -496    299       O  
ATOM   1279  N   VAL A 188      12.803  14.061  92.404  1.00 99.07           N  
ANISOU 1279  N   VAL A 188    13845  10511  13287   3915   -752    170       N  
ATOM   1280  CA  VAL A 188      11.625  13.840  93.225  1.00104.08           C  
ANISOU 1280  CA  VAL A 188    13979  11387  14179   4009   -845     80       C  
ATOM   1281  C   VAL A 188      11.041  15.206  93.536  1.00101.89           C  
ANISOU 1281  C   VAL A 188    13985  10994  13735   4285   -847     37       C  
ATOM   1282  O   VAL A 188      11.744  16.083  94.050  1.00 97.61           O  
ANISOU 1282  O   VAL A 188    13776  10234  13076   4208   -638     96       O  
ATOM   1283  CB  VAL A 188      11.957  13.054  94.505  1.00101.19           C  
ANISOU 1283  CB  VAL A 188    13134  11142  14173   3684   -656    107       C  
ATOM   1284  CG1 VAL A 188      10.701  12.830  95.319  1.00107.75           C  
ANISOU 1284  CG1 VAL A 188    13502  12209  15229   3772   -691     19       C  
ATOM   1285  CG2 VAL A 188      12.608  11.726  94.144  1.00 89.52           C  
ANISOU 1285  CG2 VAL A 188    11438   9764  12811   3431   -644    163       C  
ATOM   1286  N   LEU A 189       9.764  15.383  93.231  1.00106.06           N  
ANISOU 1286  N   LEU A 189    14386  11668  14243   4605  -1081    -78       N  
ATOM   1287  CA  LEU A 189       9.113  16.658  93.473  1.00113.27           C  
ANISOU 1287  CA  LEU A 189    15559  12483  14995   4915  -1109   -130       C  
ATOM   1288  C   LEU A 189       8.128  16.544  94.628  1.00114.90           C  
ANISOU 1288  C   LEU A 189    15230  12884  15542   4939  -1078   -225       C  
ATOM   1289  O   LEU A 189       7.030  16.016  94.468  1.00118.08           O  
ANISOU 1289  O   LEU A 189    15237  13527  16101   5087  -1270   -351       O  
ATOM   1290  CB  LEU A 189       8.388  17.132  92.209  1.00116.19           C  
ANISOU 1290  CB  LEU A 189    16274  12838  15036   5332  -1414   -216       C  
ATOM   1291  CG  LEU A 189       9.212  17.589  91.003  1.00111.22           C  
ANISOU 1291  CG  LEU A 189    16351  11952  13954   5403  -1423   -135       C  
ATOM   1292  CD1 LEU A 189       9.518  16.419  90.074  1.00108.12           C  
ANISOU 1292  CD1 LEU A 189    15844  11654  13583   5275  -1550   -134       C  
ATOM   1293  CD2 LEU A 189       8.482  18.691  90.255  1.00113.40           C  
ANISOU 1293  CD2 LEU A 189    17138  12118  13831   5880  -1633   -215       C  
ATOM   1294  N   ALA A 198      13.078  18.695  93.888  1.00 93.55           N  
ANISOU 1294  N   ALA A 198    14569   9115  11861   4274   -251    226       N  
ATOM   1295  CA  ALA A 198      13.982  19.458  94.740  1.00 92.59           C  
ANISOU 1295  CA  ALA A 198    14714   8788  11676   4043     67    282       C  
ATOM   1296  C   ALA A 198      15.226  18.650  95.095  1.00 98.69           C  
ANISOU 1296  C   ALA A 198    15307   9544  12646   3616    252    324       C  
ATOM   1297  O   ALA A 198      16.303  19.211  95.295  1.00105.86           O  
ANISOU 1297  O   ALA A 198    16571  10236  13416   3372    537    372       O  
ATOM   1298  CB  ALA A 198      13.264  19.898  96.007  1.00 88.89           C  
ANISOU 1298  CB  ALA A 198    13990   8399  11386   4126     86    224       C  
ATOM   1299  N   PHE A 199      15.065  17.334  95.215  1.00 95.87           N  
ANISOU 1299  N   PHE A 199    14388   9419  12618   3516    103    294       N  
ATOM   1300  CA  PHE A 199      16.185  16.443  95.479  1.00 90.26           C  
ANISOU 1300  CA  PHE A 199    13486   8714  12096   3156    229    322       C  
ATOM   1301  C   PHE A 199      16.131  15.274  94.504  1.00 83.01           C  
ANISOU 1301  C   PHE A 199    12343   7931  11265   3155     50    329       C  
ATOM   1302  O   PHE A 199      15.060  14.897  94.022  1.00 86.14           O  
ANISOU 1302  O   PHE A 199    12525   8504  11699   3388   -190    289       O  
ATOM   1303  CB  PHE A 199      16.197  15.952  96.932  1.00 86.56           C  
ANISOU 1303  CB  PHE A 199    12559   8383  11946   2983    272    275       C  
ATOM   1304  CG  PHE A 199      15.153  14.925  97.238  1.00 84.64           C  
ANISOU 1304  CG  PHE A 199    11717   8434  12006   3071     56    208       C  
ATOM   1305  CD1 PHE A 199      15.486  13.584  97.303  1.00 81.02           C  
ANISOU 1305  CD1 PHE A 199    10859   8135  11789   2872     -5    199       C  
ATOM   1306  CD2 PHE A 199      13.841  15.299  97.467  1.00 86.07           C  
ANISOU 1306  CD2 PHE A 199    11742   8729  12233   3332    -53    148       C  
ATOM   1307  CE1 PHE A 199      14.529  12.633  97.590  1.00 82.98           C  
ANISOU 1307  CE1 PHE A 199    10579   8642  12306   2896   -117    158       C  
ATOM   1308  CE2 PHE A 199      12.878  14.353  97.753  1.00 86.92           C  
ANISOU 1308  CE2 PHE A 199    11299   9099  12626   3357   -165     92       C  
ATOM   1309  CZ  PHE A 199      13.223  13.017  97.815  1.00 88.87           C  
ANISOU 1309  CZ  PHE A 199    11178   9500  13089   3125   -163    117       C  
ATOM   1310  N   SER A 200      17.301  14.719  94.205  1.00 71.32           N  
ANISOU 1310  N   SER A 200    10923   6364   9810   2883    185    370       N  
ATOM   1311  CA  SER A 200      17.459  13.577  93.315  1.00 68.66           C  
ANISOU 1311  CA  SER A 200    10411   6125   9551   2837     60    384       C  
ATOM   1312  C   SER A 200      17.692  12.291  94.105  1.00 72.18           C  
ANISOU 1312  C   SER A 200    10285   6775  10367   2623     14    358       C  
ATOM   1313  O   SER A 200      18.139  12.313  95.254  1.00 69.26           O  
ANISOU 1313  O   SER A 200     9772   6412  10130   2455    124    331       O  
ATOM   1314  CB  SER A 200      18.619  13.805  92.340  1.00 72.77           C  
ANISOU 1314  CB  SER A 200    11419   6397   9832   2681    266    438       C  
ATOM   1315  OG  SER A 200      18.266  14.731  91.328  1.00 83.08           O  
ANISOU 1315  OG  SER A 200    13269   7546  10753   2916    256    458       O  
ATOM   1316  N   VAL A 201      17.381  11.161  93.465  1.00 72.52           N  
ANISOU 1316  N   VAL A 201    10040   6986  10529   2638   -149    362       N  
ATOM   1317  CA  VAL A 201      17.657   9.836  94.011  1.00 67.62           C  
ANISOU 1317  CA  VAL A 201     8931   6550  10213   2431   -192    341       C  
ATOM   1318  C   VAL A 201      18.287   8.983  92.917  1.00 61.95           C  
ANISOU 1318  C   VAL A 201     8277   5802   9461   2346   -212    383       C  
ATOM   1319  O   VAL A 201      17.871   9.042  91.755  1.00 62.02           O  
ANISOU 1319  O   VAL A 201     8500   5787   9276   2514   -289    418       O  
ATOM   1320  CB  VAL A 201      16.378   9.155  94.542  1.00 65.59           C  
ANISOU 1320  CB  VAL A 201     8187   6632  10104   2502   -232    367       C  
ATOM   1321  CG1 VAL A 201      15.841   9.890  95.762  1.00 67.20           C  
ANISOU 1321  CG1 VAL A 201     8300   6857  10376   2535   -183    310       C  
ATOM   1322  CG2 VAL A 201      15.324   9.075  93.442  1.00 65.51           C  
ANISOU 1322  CG2 VAL A 201     8216   6719   9955   2763   -433    355       C  
ATOM   1323  N   CYS A 202      19.291   8.190  93.291  1.00 53.97           N  
ANISOU 1323  N   CYS A 202     7210   4841   8457   2144   -206    317       N  
ATOM   1324  CA  CYS A 202      19.927   7.228  92.396  1.00 54.07           C  
ANISOU 1324  CA  CYS A 202     7266   4859   8420   2065   -196    348       C  
ATOM   1325  C   CYS A 202      19.419   5.832  92.744  1.00 62.33           C  
ANISOU 1325  C   CYS A 202     7887   6334   9460   2049   -228    361       C  
ATOM   1326  O   CYS A 202      19.648   5.347  93.858  1.00 66.55           O  
ANISOU 1326  O   CYS A 202     8059   7040  10186   1794   -168    344       O  
ATOM   1327  CB  CYS A 202      21.452   7.314  92.511  1.00 59.03           C  
ANISOU 1327  CB  CYS A 202     8022   5303   9103   1744    174    424       C  
ATOM   1328  SG  CYS A 202      22.430   6.332  91.335  1.00 66.53           S  
ANISOU 1328  SG  CYS A 202     9027   6170  10082   1565    286    464       S  
ATOM   1329  N   ASP A 203      18.729   5.194  91.801  1.00 64.50           N  
ANISOU 1329  N   ASP A 203     8117   6745   9646   2201   -298    420       N  
ATOM   1330  CA  ASP A 203      18.192   3.860  92.030  1.00 67.42           C  
ANISOU 1330  CA  ASP A 203     8050   7455  10111   2061   -430    358       C  
ATOM   1331  C   ASP A 203      18.151   3.100  90.713  1.00 60.37           C  
ANISOU 1331  C   ASP A 203     7210   6547   9182   2107   -509    400       C  
ATOM   1332  O   ASP A 203      18.332   3.668  89.634  1.00 57.40           O  
ANISOU 1332  O   ASP A 203     7147   5890   8773   2238   -475    497       O  
ATOM   1333  CB  ASP A 203      16.797   3.919  92.663  1.00 80.14           C  
ANISOU 1333  CB  ASP A 203     9398   9320  11730   2162   -500    323       C  
ATOM   1334  CG  ASP A 203      15.811   4.728  91.837  1.00 96.47           C  
ANISOU 1334  CG  ASP A 203    11571  11275  13809   2423   -588    384       C  
ATOM   1335  OD1 ASP A 203      15.583   4.376  90.660  1.00101.80           O  
ANISOU 1335  OD1 ASP A 203    12320  11907  14453   2493   -748    369       O  
ATOM   1336  OD2 ASP A 203      15.257   5.714  92.367  1.00104.65           O  
ANISOU 1336  OD2 ASP A 203    12627  12251  14885   2540   -569    380       O  
ATOM   1337  N   GLU A 204      17.899   1.798  90.816  1.00 52.68           N  
ANISOU 1337  N   GLU A 204     5919   5820   8278   1932   -603    329       N  
ATOM   1338  CA  GLU A 204      17.878   0.939  89.642  1.00 51.02           C  
ANISOU 1338  CA  GLU A 204     5736   5604   8045   1949   -700    342       C  
ATOM   1339  C   GLU A 204      16.536   1.034  88.925  1.00 50.45           C  
ANISOU 1339  C   GLU A 204     5622   5615   7931   2158   -896    317       C  
ATOM   1340  O   GLU A 204      15.476   1.047  89.557  1.00 50.23           O  
ANISOU 1340  O   GLU A 204     5346   5793   7946   2177   -962    243       O  
ATOM   1341  CB  GLU A 204      18.169  -0.510  90.038  1.00 48.30           C  
ANISOU 1341  CB  GLU A 204     5100   5441   7811   1649   -698    276       C  
ATOM   1342  CG  GLU A 204      19.520  -0.709  90.726  1.00 54.88           C  
ANISOU 1342  CG  GLU A 204     5895   6173   8784   1371   -533    304       C  
ATOM   1343  CD  GLU A 204      19.713  -2.126  91.235  1.00 60.53           C  
ANISOU 1343  CD  GLU A 204     6374   7045   9579   1090   -506    270       C  
ATOM   1344  OE1 GLU A 204      18.887  -2.994  90.887  1.00 59.02           O  
ANISOU 1344  OE1 GLU A 204     6087   7000   9337   1105   -603    217       O  
ATOM   1345  OE2 GLU A 204      20.703  -2.379  91.955  1.00 63.31           O  
ANISOU 1345  OE2 GLU A 204     6671   7349  10036    867   -381    299       O  
ATOM   1346  N   ARG A 205      16.588   1.098  87.597  1.00 50.83           N  
ANISOU 1346  N   ARG A 205     5937   5481   7897   2297  -1018    337       N  
ATOM   1347  CA  ARG A 205      15.395   1.154  86.759  1.00 54.00           C  
ANISOU 1347  CA  ARG A 205     6360   5946   8212   2505  -1306    229       C  
ATOM   1348  C   ARG A 205      15.200  -0.213  86.109  1.00 57.13           C  
ANISOU 1348  C   ARG A 205     6598   6478   8630   2417  -1442    156       C  
ATOM   1349  O   ARG A 205      16.008  -0.629  85.273  1.00 63.65           O  
ANISOU 1349  O   ARG A 205     7656   7137   9391   2392  -1426    210       O  
ATOM   1350  CB  ARG A 205      15.532   2.259  85.713  1.00 66.29           C  
ANISOU 1350  CB  ARG A 205     8447   7205   9535   2754  -1397    245       C  
ATOM   1351  CG  ARG A 205      14.347   2.403  84.781  1.00 85.57           C  
ANISOU 1351  CG  ARG A 205    11001   9715  11797   3034  -1738     95       C  
ATOM   1352  CD  ARG A 205      14.740   2.121  83.339  1.00 98.80           C  
ANISOU 1352  CD  ARG A 205    13112  11202  13225   3138  -1859     92       C  
ATOM   1353  NE  ARG A 205      15.951   2.832  82.935  1.00105.56           N  
ANISOU 1353  NE  ARG A 205    14496  11711  13900   3106  -1619    230       N  
ATOM   1354  CZ  ARG A 205      17.092   2.234  82.609  1.00103.77           C  
ANISOU 1354  CZ  ARG A 205    14399  11325  13702   2902  -1412    328       C  
ATOM   1355  NH1 ARG A 205      17.178   0.911  82.635  1.00 98.53           N  
ANISOU 1355  NH1 ARG A 205    13391  10822  13226   2749  -1448    317       N  
ATOM   1356  NH2 ARG A 205      18.146   2.956  82.251  1.00105.53           N  
ANISOU 1356  NH2 ARG A 205    15109  11227  13759   2834  -1146    420       N  
ATOM   1357  N   TRP A 206      14.135  -0.914  86.501  1.00 53.54           N  
ANISOU 1357  N   TRP A 206     5770   6298   8274   2355  -1553     26       N  
ATOM   1358  CA  TRP A 206      13.825  -2.243  85.985  1.00 56.43           C  
ANISOU 1358  CA  TRP A 206     5960   6794   8687   2245  -1674    -72       C  
ATOM   1359  C   TRP A 206      12.484  -2.217  85.267  1.00 67.01           C  
ANISOU 1359  C   TRP A 206     7239   8231   9989   2453  -1988   -262       C  
ATOM   1360  O   TRP A 206      11.482  -1.765  85.832  1.00 69.33           O  
ANISOU 1360  O   TRP A 206     7334   8661  10349   2527  -2039   -362       O  
ATOM   1361  CB  TRP A 206      13.809  -3.287  87.108  1.00 52.22           C  
ANISOU 1361  CB  TRP A 206     5072   6467   8301   1934  -1493    -93       C  
ATOM   1362  CG  TRP A 206      15.156  -3.519  87.719  1.00 48.63           C  
ANISOU 1362  CG  TRP A 206     4686   5932   7859   1733  -1249     29       C  
ATOM   1363  CD1 TRP A 206      15.622  -3.003  88.891  1.00 47.64           C  
ANISOU 1363  CD1 TRP A 206     4539   5813   7747   1634  -1060     79       C  
ATOM   1364  CD2 TRP A 206      16.215  -4.326  87.185  1.00 52.13           C  
ANISOU 1364  CD2 TRP A 206     5232   6262   8314   1610  -1197     80       C  
ATOM   1365  NE1 TRP A 206      16.907  -3.436  89.121  1.00 46.81           N  
ANISOU 1365  NE1 TRP A 206     4504   5606   7674   1444   -917    136       N  
ATOM   1366  CE2 TRP A 206      17.294  -4.250  88.089  1.00 50.82           C  
ANISOU 1366  CE2 TRP A 206     5077   6038   8193   1426   -982    147       C  
ATOM   1367  CE3 TRP A 206      16.356  -5.104  86.031  1.00 56.68           C  
ANISOU 1367  CE3 TRP A 206     5894   6763   8880   1638  -1326     64       C  
ATOM   1368  CZ2 TRP A 206      18.497  -4.922  87.876  1.00 45.76           C  
ANISOU 1368  CZ2 TRP A 206     4494   5270   7621   1259   -879    202       C  
ATOM   1369  CZ3 TRP A 206      17.553  -5.772  85.821  1.00 49.61           C  
ANISOU 1369  CZ3 TRP A 206     5080   5734   8036   1489  -1205    138       C  
ATOM   1370  CH2 TRP A 206      18.606  -5.677  86.738  1.00 39.49           C  
ANISOU 1370  CH2 TRP A 206     3772   4402   6830   1298   -976    207       C  
ATOM   1371  N   ALA A 207      12.474  -2.693  84.020  1.00 68.42           N  
ANISOU 1371  N   ALA A 207     7605   8336  10056   2562  -2206   -330       N  
ATOM   1372  CA  ALA A 207      11.251  -2.718  83.225  1.00 62.98           C  
ANISOU 1372  CA  ALA A 207     6888   7736   9304   2787  -2548   -551       C  
ATOM   1373  C   ALA A 207      10.222  -3.716  83.739  1.00 66.49           C  
ANISOU 1373  C   ALA A 207     6841   8452   9968   2615  -2582   -730       C  
ATOM   1374  O   ALA A 207       9.033  -3.565  83.440  1.00 71.27           O  
ANISOU 1374  O   ALA A 207     7313   9176  10593   2792  -2826   -945       O  
ATOM   1375  CB  ALA A 207      11.578  -3.032  81.763  1.00 63.09           C  
ANISOU 1375  CB  ALA A 207     7285   7582   9103   2944  -2771   -580       C  
ATOM   1376  N   ASP A 208      10.639  -4.729  84.496  1.00 72.54           N  
ANISOU 1376  N   ASP A 208     7367   9308  10888   2284  -2339   -665       N  
ATOM   1377  CA  ASP A 208       9.701  -5.734  84.973  1.00 72.86           C  
ANISOU 1377  CA  ASP A 208     7012   9563  11108   2098  -2328   -833       C  
ATOM   1378  C   ASP A 208      10.173  -6.283  86.311  1.00 64.99           C  
ANISOU 1378  C   ASP A 208     5847   8627  10219   1776  -1979   -713       C  
ATOM   1379  O   ASP A 208      11.325  -6.099  86.712  1.00 68.91           O  
ANISOU 1379  O   ASP A 208     6513   9014  10656   1685  -1780   -521       O  
ATOM   1380  CB  ASP A 208       9.530  -6.865  83.953  1.00 81.33           C  
ANISOU 1380  CB  ASP A 208     8063  10655  12184   2064  -2519   -967       C  
ATOM   1381  CG  ASP A 208      10.759  -7.736  83.845  1.00 89.28           C  
ANISOU 1381  CG  ASP A 208     9194  11554  13175   1854  -2352   -808       C  
ATOM   1382  OD1 ASP A 208      11.806  -7.232  83.387  1.00 93.81           O  
ANISOU 1382  OD1 ASP A 208    10094  11932  13615   1952  -2332   -645       O  
ATOM   1383  OD2 ASP A 208      10.680  -8.922  84.227  1.00 95.19           O  
ANISOU 1383  OD2 ASP A 208     9728  12395  14046   1595  -2230   -853       O  
ATOM   1384  N   ASP A 209       9.250  -6.959  87.003  1.00 57.18           N  
ANISOU 1384  N   ASP A 209     4543   7803   9378   1616  -1914   -853       N  
ATOM   1385  CA  ASP A 209       9.535  -7.484  88.335  1.00 65.31           C  
ANISOU 1385  CA  ASP A 209     5468   8878  10471   1340  -1606   -770       C  
ATOM   1386  C   ASP A 209      10.500  -8.664  88.310  1.00 61.73           C  
ANISOU 1386  C   ASP A 209     5101   8363   9990   1109  -1467   -679       C  
ATOM   1387  O   ASP A 209      11.197  -8.911  89.299  1.00 64.63           O  
ANISOU 1387  O   ASP A 209     5524   8693  10341    936  -1236   -569       O  
ATOM   1388  CB  ASP A 209       8.232  -7.915  89.014  1.00 74.53           C  
ANISOU 1388  CB  ASP A 209     6306  10193  11821   1248  -1584   -987       C  
ATOM   1389  CG  ASP A 209       7.354  -6.742  89.395  1.00 88.75           C  
ANISOU 1389  CG  ASP A 209     7990  12048  13685   1451  -1663  -1087       C  
ATOM   1390  OD1 ASP A 209       7.043  -5.912  88.517  1.00 98.13           O  
ANISOU 1390  OD1 ASP A 209     9257  13227  14800   1728  -1900  -1122       O  
ATOM   1391  OD2 ASP A 209       6.962  -6.661  90.578  1.00 93.83           O  
ANISOU 1391  OD2 ASP A 209     8478  12731  14441   1346  -1489  -1139       O  
ATOM   1392  N   LEU A 210      10.561  -9.404  87.202  1.00 53.24           N  
ANISOU 1392  N   LEU A 210     4053   7261   8915   1119  -1625   -746       N  
ATOM   1393  CA  LEU A 210      11.357 -10.629  87.193  1.00 54.02           C  
ANISOU 1393  CA  LEU A 210     4203   7304   9018    899  -1495   -685       C  
ATOM   1394  C   LEU A 210      12.846 -10.353  87.002  1.00 58.25           C  
ANISOU 1394  C   LEU A 210     5007   7668   9456    915  -1411   -489       C  
ATOM   1395  O   LEU A 210      13.682 -10.990  87.654  1.00 62.60           O  
ANISOU 1395  O   LEU A 210     5613   8164  10006    728  -1206   -395       O  
ATOM   1396  CB  LEU A 210      10.849 -11.580  86.112  1.00 59.22           C  
ANISOU 1396  CB  LEU A 210     4775   7995   9732    890  -1693   -847       C  
ATOM   1397  CG  LEU A 210      11.440 -12.993  86.115  1.00 58.24           C  
ANISOU 1397  CG  LEU A 210     4660   7824   9645    649  -1562   -821       C  
ATOM   1398  CD1 LEU A 210      11.289 -13.630  87.485  1.00 60.26           C  
ANISOU 1398  CD1 LEU A 210     4807   8134   9955    408  -1283   -806       C  
ATOM   1399  CD2 LEU A 210      10.771 -13.856  85.055  1.00 53.91           C  
ANISOU 1399  CD2 LEU A 210     4002   7325   9155    641  -1779  -1017       C  
ATOM   1400  N   ALA A 211      13.198  -9.422  86.119  1.00 56.87           N  
ANISOU 1400  N   ALA A 211     5019   7386   9201   1146  -1569   -438       N  
ATOM   1401  CA  ALA A 211      14.605  -9.143  85.835  1.00 50.42           C  
ANISOU 1401  CA  ALA A 211     4451   6379   8326   1164  -1486   -272       C  
ATOM   1402  C   ALA A 211      15.423  -8.825  87.079  1.00 55.11           C  
ANISOU 1402  C   ALA A 211     5072   6950   8916   1020  -1218   -155       C  
ATOM   1403  O   ALA A 211      16.486  -9.439  87.260  1.00 59.72           O  
ANISOU 1403  O   ALA A 211     5727   7434   9528    866  -1078    -75       O  
ATOM   1404  CB  ALA A 211      14.693  -8.000  84.812  1.00 49.26           C  
ANISOU 1404  CB  ALA A 211     4558   6094   8065   1467  -1681   -239       C  
ATOM   1405  N   PRO A 212      15.024  -7.899  87.951  1.00 56.46           N  
ANISOU 1405  N   PRO A 212     5202   7192   9059   1068  -1156   -150       N  
ATOM   1406  CA  PRO A 212      15.821  -7.661  89.165  1.00 46.52           C  
ANISOU 1406  CA  PRO A 212     3990   5899   7786    926   -939    -69       C  
ATOM   1407  C   PRO A 212      15.968  -8.896  90.039  1.00 39.42           C  
ANISOU 1407  C   PRO A 212     3017   5040   6919    683   -795    -87       C  
ATOM   1408  O   PRO A 212      17.016  -9.075  90.672  1.00 40.14           O  
ANISOU 1408  O   PRO A 212     3210   5022   7020    561   -664    -14       O  
ATOM   1409  CB  PRO A 212      15.031  -6.561  89.900  1.00 41.38           C  
ANISOU 1409  CB  PRO A 212     3273   5337   7112   1038   -939    -94       C  
ATOM   1410  CG  PRO A 212      13.649  -6.625  89.324  1.00 46.04           C  
ANISOU 1410  CG  PRO A 212     3702   6048   7744   1164  -1117   -213       C  
ATOM   1411  CD  PRO A 212      13.823  -7.046  87.898  1.00 52.06           C  
ANISOU 1411  CD  PRO A 212     4554   6733   8495   1257  -1296   -232       C  
ATOM   1412  N   LYS A 213      14.955  -9.759  90.075  1.00 46.35           N  
ANISOU 1412  N   LYS A 213     3725   6029   7858    619   -832   -193       N  
ATOM   1413  CA  LYS A 213      15.060 -10.974  90.869  1.00 38.56           C  
ANISOU 1413  CA  LYS A 213     2694   5020   6937    414   -701   -215       C  
ATOM   1414  C   LYS A 213      16.096 -11.925  90.285  1.00 43.37           C  
ANISOU 1414  C   LYS A 213     3429   5531   7517    334   -666   -142       C  
ATOM   1415  O   LYS A 213      16.907 -12.500  91.020  1.00 53.10           O  
ANISOU 1415  O   LYS A 213     4748   6662   8767    220   -539    -80       O  
ATOM   1416  CB  LYS A 213      13.699 -11.661  90.954  1.00 39.46           C  
ANISOU 1416  CB  LYS A 213     2585   5270   7139    354   -734   -365       C  
ATOM   1417  CG  LYS A 213      12.654 -10.889  91.728  1.00 44.01           C  
ANISOU 1417  CG  LYS A 213     3002   5932   7787    406   -730   -456       C  
ATOM   1418  CD  LYS A 213      11.331 -11.634  91.699  1.00 46.44           C  
ANISOU 1418  CD  LYS A 213     3062   6362   8220    328   -754   -638       C  
ATOM   1419  CE  LYS A 213      10.297 -10.981  92.600  1.00 47.68           C  
ANISOU 1419  CE  LYS A 213     3037   6592   8486    355   -711   -753       C  
ATOM   1420  NZ  LYS A 213       8.917 -11.475  92.326  1.00 63.14           N  
ANISOU 1420  NZ  LYS A 213     4716   8677  10596    319   -773   -982       N  
ATOM   1421  N   ILE A 214      16.085 -12.102  88.962  1.00 41.24           N  
ANISOU 1421  N   ILE A 214     3160   5238   7271    410   -806   -161       N  
ATOM   1422  CA  ILE A 214      17.062 -12.977  88.323  1.00 34.04           C  
ANISOU 1422  CA  ILE A 214     2344   4189   6402    343   -785    -98       C  
ATOM   1423  C   ILE A 214      18.462 -12.381  88.408  1.00 37.91           C  
ANISOU 1423  C   ILE A 214     3003   4524   6878    358   -694     39       C  
ATOM   1424  O   ILE A 214      19.435 -13.091  88.686  1.00 44.79           O  
ANISOU 1424  O   ILE A 214     3948   5295   7776    254   -578    110       O  
ATOM   1425  CB  ILE A 214      16.651 -13.266  86.867  1.00 42.33           C  
ANISOU 1425  CB  ILE A 214     3353   5226   7504    436   -994   -166       C  
ATOM   1426  CG1 ILE A 214      15.356 -14.075  86.838  1.00 45.82           C  
ANISOU 1426  CG1 ILE A 214     3598   5823   7990    364  -1068   -331       C  
ATOM   1427  CG2 ILE A 214      17.743 -14.025  86.136  1.00 38.94           C  
ANISOU 1427  CG2 ILE A 214     3028   4623   7145    387   -974    -79       C  
ATOM   1428  CD1 ILE A 214      14.798 -14.270  85.449  1.00 47.54           C  
ANISOU 1428  CD1 ILE A 214     3774   6049   8241    475  -1335   -448       C  
ATOM   1429  N   TYR A 215      18.593 -11.073  88.175  1.00 45.16           N  
ANISOU 1429  N   TYR A 215     3979   5414   7766    492   -743     70       N  
ATOM   1430  CA  TYR A 215      19.916 -10.458  88.203  1.00 42.74           C  
ANISOU 1430  CA  TYR A 215     3800   4955   7484    483   -642    180       C  
ATOM   1431  C   TYR A 215      20.530 -10.520  89.594  1.00 45.81           C  
ANISOU 1431  C   TYR A 215     4217   5348   7842    349   -485    210       C  
ATOM   1432  O   TYR A 215      21.668 -10.972  89.765  1.00 47.93           O  
ANISOU 1432  O   TYR A 215     4547   5515   8148    262   -388    271       O  
ATOM   1433  CB  TYR A 215      19.837  -9.008  87.734  1.00 35.68           C  
ANISOU 1433  CB  TYR A 215     2981   4013   6564    671   -716    200       C  
ATOM   1434  CG  TYR A 215      21.143  -8.279  87.909  1.00 39.45           C  
ANISOU 1434  CG  TYR A 215     3556   4333   7101    634   -574    296       C  
ATOM   1435  CD1 TYR A 215      22.220  -8.548  87.078  1.00 43.95           C  
ANISOU 1435  CD1 TYR A 215     4203   4723   7771    618   -496    372       C  
ATOM   1436  CD2 TYR A 215      21.305  -7.334  88.912  1.00 38.37           C  
ANISOU 1436  CD2 TYR A 215     3419   4215   6945    611   -498    302       C  
ATOM   1437  CE1 TYR A 215      23.421  -7.891  87.235  1.00 36.69           C  
ANISOU 1437  CE1 TYR A 215     3331   3659   6950    567   -321    437       C  
ATOM   1438  CE2 TYR A 215      22.502  -6.669  89.074  1.00 33.35           C  
ANISOU 1438  CE2 TYR A 215     2834   3434   6405    558   -363    369       C  
ATOM   1439  CZ  TYR A 215      23.557  -6.951  88.235  1.00 36.85           C  
ANISOU 1439  CZ  TYR A 215     3322   3711   6968    530   -264    429       C  
ATOM   1440  OH  TYR A 215      24.747  -6.286  88.402  1.00 49.04           O  
ANISOU 1440  OH  TYR A 215     4875   5107   8650    464    -81    468       O  
ATOM   1441  N   HIS A 216      19.793 -10.058  90.603  1.00 47.19           N  
ANISOU 1441  N   HIS A 216     4347   5633   7948    355   -476    162       N  
ATOM   1442  CA  HIS A 216      20.351 -10.007  91.947  1.00 46.36           C  
ANISOU 1442  CA  HIS A 216     4273   5465   7877    262   -376    196       C  
ATOM   1443  C   HIS A 216      20.517 -11.397  92.548  1.00 48.80           C  
ANISOU 1443  C   HIS A 216     4580   5744   8218    163   -322    200       C  
ATOM   1444  O   HIS A 216      21.289 -11.559  93.498  1.00 45.72           O  
ANISOU 1444  O   HIS A 216     4244   5279   7847    117   -261    245       O  
ATOM   1445  CB  HIS A 216      19.487  -9.105  92.830  1.00 38.24           C  
ANISOU 1445  CB  HIS A 216     3179   4504   6846    305   -387    152       C  
ATOM   1446  CG  HIS A 216      19.705  -7.639  92.585  1.00 44.92           C  
ANISOU 1446  CG  HIS A 216     4069   5339   7658    409   -407    175       C  
ATOM   1447  ND1 HIS A 216      20.827  -6.970  93.025  1.00 43.80           N  
ANISOU 1447  ND1 HIS A 216     4008   5096   7537    367   -332    235       N  
ATOM   1448  CD2 HIS A 216      18.954  -6.720  91.929  1.00 45.23           C  
ANISOU 1448  CD2 HIS A 216     4089   5454   7640    579   -495    144       C  
ATOM   1449  CE1 HIS A 216      20.753  -5.702  92.661  1.00 44.26           C  
ANISOU 1449  CE1 HIS A 216     4092   5145   7578    485   -354    242       C  
ATOM   1450  NE2 HIS A 216      19.627  -5.524  91.994  1.00 50.42           N  
ANISOU 1450  NE2 HIS A 216     4829   6014   8313    636   -461    196       N  
ATOM   1451  N   SER A 217      19.815 -12.402  92.024  1.00 40.32           N  
ANISOU 1451  N   SER A 217     3441   4734   7144    143   -353    149       N  
ATOM   1452  CA  SER A 217      20.114 -13.772  92.424  1.00 35.30           C  
ANISOU 1452  CA  SER A 217     2822   4061   6530     61   -291    163       C  
ATOM   1453  C   SER A 217      21.468 -14.209  91.876  1.00 37.32           C  
ANISOU 1453  C   SER A 217     3182   4207   6791     58   -264    242       C  
ATOM   1454  O   SER A 217      22.291 -14.779  92.602  1.00 43.39           O  
ANISOU 1454  O   SER A 217     4003   4906   7578     32   -210    287       O  
ATOM   1455  CB  SER A 217      19.005 -14.712  91.954  1.00 34.90           C  
ANISOU 1455  CB  SER A 217     2657   4118   6486     15   -318     71       C  
ATOM   1456  OG  SER A 217      17.803 -14.475  92.666  1.00 41.52           O  
ANISOU 1456  OG  SER A 217     3367   5061   7347     -7   -309    -20       O  
ATOM   1457  N   CYS A 218      21.720 -13.934  90.594  1.00 38.80           N  
ANISOU 1457  N   CYS A 218     3380   4371   6991     96   -306    256       N  
ATOM   1458  CA  CYS A 218      23.015 -14.258  90.003  1.00 38.24           C  
ANISOU 1458  CA  CYS A 218     3370   4169   6991     87   -258    327       C  
ATOM   1459  C   CYS A 218      24.139 -13.447  90.640  1.00 42.24           C  
ANISOU 1459  C   CYS A 218     3937   4628   7482     88   -195    360       C  
ATOM   1460  O   CYS A 218      25.239 -13.966  90.866  1.00 43.89           O  
ANISOU 1460  O   CYS A 218     4177   4775   7726     70   -142    385       O  
ATOM   1461  CB  CYS A 218      22.973 -14.016  88.496  1.00 36.78           C  
ANISOU 1461  CB  CYS A 218     3155   3922   6899    131   -313    344       C  
ATOM   1462  SG  CYS A 218      21.789 -15.044  87.603  1.00 45.70           S  
ANISOU 1462  SG  CYS A 218     4189   5099   8074    133   -434    279       S  
ATOM   1463  N   PHE A 219      23.889 -12.166  90.926  1.00 47.10           N  
ANISOU 1463  N   PHE A 219     4551   5279   8064    116   -209    347       N  
ATOM   1464  CA  PHE A 219      24.908 -11.335  91.562  1.00 40.88           C  
ANISOU 1464  CA  PHE A 219     3789   4430   7312    104   -156    365       C  
ATOM   1465  C   PHE A 219      25.363 -11.941  92.886  1.00 46.64           C  
ANISOU 1465  C   PHE A 219     4521   5140   8058     75   -149    367       C  
ATOM   1466  O   PHE A 219      26.565 -12.056  93.154  1.00 45.45           O  
ANISOU 1466  O   PHE A 219     4373   4940   7956     68   -120    366       O  
ATOM   1467  CB  PHE A 219      24.365  -9.921  91.777  1.00 32.76           C  
ANISOU 1467  CB  PHE A 219     2748   3438   6262    141   -175    351       C  
ATOM   1468  CG  PHE A 219      25.417  -8.908  92.133  1.00 32.16           C  
ANISOU 1468  CG  PHE A 219     2682   3291   6245    126   -112    358       C  
ATOM   1469  CD1 PHE A 219      25.828  -8.750  93.447  1.00 30.38           C  
ANISOU 1469  CD1 PHE A 219     2453   3057   6034     99   -110    346       C  
ATOM   1470  CD2 PHE A 219      25.980  -8.099  91.158  1.00 41.89           C  
ANISOU 1470  CD2 PHE A 219     3885   4396   7637    138    -46    388       C  
ATOM   1471  CE1 PHE A 219      26.793  -7.813  93.780  1.00 30.46           C  
ANISOU 1471  CE1 PHE A 219     2452   3019   6102     87    -61    324       C  
ATOM   1472  CE2 PHE A 219      26.944  -7.162  91.486  1.00 47.03           C  
ANISOU 1472  CE2 PHE A 219     4513   4950   8406    111     44    376       C  
ATOM   1473  CZ  PHE A 219      27.350  -7.019  92.797  1.00 39.39           C  
ANISOU 1473  CZ  PHE A 219     3557   4045   7366     86     22    330       C  
ATOM   1474  N   PHE A 220      24.406 -12.342  93.728  1.00 45.43           N  
ANISOU 1474  N   PHE A 220     4350   5040   7873     70   -177    354       N  
ATOM   1475  CA  PHE A 220      24.751 -12.904  95.030  1.00 40.77           C  
ANISOU 1475  CA  PHE A 220     3762   4441   7287     59   -174    359       C  
ATOM   1476  C   PHE A 220      25.556 -14.189  94.894  1.00 45.87           C  
ANISOU 1476  C   PHE A 220     4420   5055   7953     57   -166    375       C  
ATOM   1477  O   PHE A 220      26.546 -14.388  95.606  1.00 47.51           O  
ANISOU 1477  O   PHE A 220     4624   5248   8182     72   -179    373       O  
ATOM   1478  CB  PHE A 220      23.477 -13.150  95.835  1.00 42.01           C  
ANISOU 1478  CB  PHE A 220     3883   4661   7418     49   -172    334       C  
ATOM   1479  CG  PHE A 220      23.694 -13.939  97.088  1.00 40.65           C  
ANISOU 1479  CG  PHE A 220     3713   4486   7245     42   -158    343       C  
ATOM   1480  CD1 PHE A 220      24.438 -13.423  98.132  1.00 38.85           C  
ANISOU 1480  CD1 PHE A 220     3497   4244   7019     61   -180    351       C  
ATOM   1481  CD2 PHE A 220      23.149 -15.205  97.219  1.00 37.51           C  
ANISOU 1481  CD2 PHE A 220     3287   4093   6872     14   -124    339       C  
ATOM   1482  CE1 PHE A 220      24.634 -14.154  99.288  1.00 32.48           C  
ANISOU 1482  CE1 PHE A 220     2672   3413   6258     72   -189    369       C  
ATOM   1483  CE2 PHE A 220      23.340 -15.939  98.368  1.00 39.72           C  
ANISOU 1483  CE2 PHE A 220     3532   4285   7274     10   -104    378       C  
ATOM   1484  CZ  PHE A 220      24.084 -15.414  99.406  1.00 38.12           C  
ANISOU 1484  CZ  PHE A 220     3339   4056   7088     50   -149    400       C  
ATOM   1485  N   ILE A 221      25.147 -15.073  93.983  1.00 46.50           N  
ANISOU 1485  N   ILE A 221     4502   5140   8028     48   -154    380       N  
ATOM   1486  CA  ILE A 221      25.828 -16.355  93.832  1.00 48.51           C  
ANISOU 1486  CA  ILE A 221     4762   5359   8311     52   -139    399       C  
ATOM   1487  C   ILE A 221      27.188 -16.171  93.167  1.00 48.08           C  
ANISOU 1487  C   ILE A 221     4711   5262   8296     71   -119    397       C  
ATOM   1488  O   ILE A 221      28.178 -16.793  93.569  1.00 49.33           O  
ANISOU 1488  O   ILE A 221     4844   5400   8498     99   -124    392       O  
ATOM   1489  CB  ILE A 221      24.938 -17.339  93.048  1.00 50.91           C  
ANISOU 1489  CB  ILE A 221     5035   5638   8671     25   -127    407       C  
ATOM   1490  CG1 ILE A 221      23.870 -17.933  93.969  1.00 43.61           C  
ANISOU 1490  CG1 ILE A 221     4059   4732   7778    -11   -111    390       C  
ATOM   1491  CG2 ILE A 221      25.778 -18.437  92.415  1.00 46.87           C  
ANISOU 1491  CG2 ILE A 221     4516   5027   8265     33    -99    448       C  
ATOM   1492  CD1 ILE A 221      22.548 -18.221  93.282  1.00 49.90           C  
ANISOU 1492  CD1 ILE A 221     4790   5599   8570    -67   -108    324       C  
ATOM   1493  N   VAL A 222      27.262 -15.320  92.144  1.00 44.92           N  
ANISOU 1493  N   VAL A 222     4315   4840   7911     66    -93    394       N  
ATOM   1494  CA  VAL A 222      28.502 -15.200  91.384  1.00 42.84           C  
ANISOU 1494  CA  VAL A 222     4032   4518   7728     75    -34    382       C  
ATOM   1495  C   VAL A 222      29.569 -14.455  92.177  1.00 44.02           C  
ANISOU 1495  C   VAL A 222     4136   4666   7925     85    -34    333       C  
ATOM   1496  O   VAL A 222      30.738 -14.858  92.194  1.00 46.12           O  
ANISOU 1496  O   VAL A 222     4343   4921   8261    106    -13    288       O  
ATOM   1497  CB  VAL A 222      28.233 -14.522  90.031  1.00 45.10           C  
ANISOU 1497  CB  VAL A 222     4314   4733   8090     67     15    405       C  
ATOM   1498  CG1 VAL A 222      29.542 -14.070  89.421  1.00 36.25           C  
ANISOU 1498  CG1 VAL A 222     3151   3514   7110     67    125    380       C  
ATOM   1499  CG2 VAL A 222      27.505 -15.477  89.110  1.00 45.69           C  
ANISOU 1499  CG2 VAL A 222     4383   4772   8204     63      4    444       C  
ATOM   1500  N   THR A 223      29.197 -13.357  92.834  1.00 43.93           N  
ANISOU 1500  N   THR A 223     4127   4671   7893     76    -60    325       N  
ATOM   1501  CA  THR A 223      30.163 -12.561  93.577  1.00 39.85           C  
ANISOU 1501  CA  THR A 223     3551   4154   7436     82    -65    264       C  
ATOM   1502  C   THR A 223      30.338 -13.005  95.024  1.00 45.83           C  
ANISOU 1502  C   THR A 223     4280   4967   8168    109   -155    243       C  
ATOM   1503  O   THR A 223      31.294 -12.566  95.671  1.00 45.81           O  
ANISOU 1503  O   THR A 223     4200   4986   8220    128   -188    170       O  
ATOM   1504  CB  THR A 223      29.775 -11.080  93.544  1.00 45.76           C  
ANISOU 1504  CB  THR A 223     4315   4891   8183     65    -38    261       C  
ATOM   1505  OG1 THR A 223      28.503 -10.897  94.182  1.00 48.39           O  
ANISOU 1505  OG1 THR A 223     4692   5265   8427     66    -93    304       O  
ATOM   1506  CG2 THR A 223      29.709 -10.583  92.102  1.00 42.72           C  
ANISOU 1506  CG2 THR A 223     3952   4456   7822     58     55    276       C  
ATOM   1507  N   TYR A 224      29.460 -13.856  95.554  1.00 48.54           N  
ANISOU 1507  N   TYR A 224     4668   5339   8435    116   -195    292       N  
ATOM   1508  CA  TYR A 224      29.607 -14.243  96.952  1.00 41.15           C  
ANISOU 1508  CA  TYR A 224     3712   4455   7466    159   -275    275       C  
ATOM   1509  C   TYR A 224      29.585 -15.750  97.167  1.00 42.58           C  
ANISOU 1509  C   TYR A 224     3907   4658   7613    210   -303    299       C  
ATOM   1510  O   TYR A 224      30.625 -16.361  97.433  1.00 40.52           O  
ANISOU 1510  O   TYR A 224     3602   4425   7369    298   -362    257       O  
ATOM   1511  CB  TYR A 224      28.518 -13.591  97.806  1.00 36.23           C  
ANISOU 1511  CB  TYR A 224     3125   3852   6788    137   -282    301       C  
ATOM   1512  CG  TYR A 224      28.741 -13.769  99.294  1.00 42.91           C  
ANISOU 1512  CG  TYR A 224     3955   4749   7599    194   -363    280       C  
ATOM   1513  CD1 TYR A 224      29.515 -12.865 100.014  1.00 34.73           C  
ANISOU 1513  CD1 TYR A 224     2872   3739   6586    221   -425    220       C  
ATOM   1514  CD2 TYR A 224      28.186 -14.844  99.978  1.00 44.40           C  
ANISOU 1514  CD2 TYR A 224     4156   4912   7804    229   -389    325       C  
ATOM   1515  CE1 TYR A 224      29.726 -13.025 101.375  1.00 27.25           C  
ANISOU 1515  CE1 TYR A 224     1916   2833   5606    303   -530    200       C  
ATOM   1516  CE2 TYR A 224      28.391 -15.011 101.336  1.00 44.82           C  
ANISOU 1516  CE2 TYR A 224     4193   4939   7898    314   -493    326       C  
ATOM   1517  CZ  TYR A 224      29.162 -14.099 102.030  1.00 43.00           C  
ANISOU 1517  CZ  TYR A 224     3938   4761   7637    360   -578    260       C  
ATOM   1518  OH  TYR A 224      29.366 -14.266 103.381  1.00 49.41           O  
ANISOU 1518  OH  TYR A 224     4768   5532   8472    483   -722    255       O  
ATOM   1519  N   LEU A 225      28.401 -16.353  97.059  1.00 40.38           N  
ANISOU 1519  N   LEU A 225     3672   4351   7320    173   -265    358       N  
ATOM   1520  CA  LEU A 225      28.212 -17.707  97.569  1.00 39.05           C  
ANISOU 1520  CA  LEU A 225     3484   4112   7241    216   -291    408       C  
ATOM   1521  C   LEU A 225      29.138 -18.704  96.881  1.00 45.15           C  
ANISOU 1521  C   LEU A 225     4244   4859   8053    282   -298    403       C  
ATOM   1522  O   LEU A 225      29.899 -19.419  97.544  1.00 53.74           O  
ANISOU 1522  O   LEU A 225     5336   5936   9147    423   -382    390       O  
ATOM   1523  CB  LEU A 225      26.751 -18.125  97.398  1.00 46.03           C  
ANISOU 1523  CB  LEU A 225     4365   4934   8191    138   -216    463       C  
ATOM   1524  CG  LEU A 225      26.312 -19.382  98.147  1.00 50.30           C  
ANISOU 1524  CG  LEU A 225     4863   5349   8900    171   -197    532       C  
ATOM   1525  CD1 LEU A 225      26.256 -19.120  99.645  1.00 50.46           C  
ANISOU 1525  CD1 LEU A 225     4892   5331   8949    247   -248    549       C  
ATOM   1526  CD2 LEU A 225      24.969 -19.868  97.634  1.00 51.22           C  
ANISOU 1526  CD2 LEU A 225     4926   5418   9119     60    -75    543       C  
ATOM   1527  N   ALA A 226      29.096 -18.764  95.551  1.00 45.15           N  
ANISOU 1527  N   ALA A 226     4248   4840   8067    221   -222    409       N  
ATOM   1528  CA  ALA A 226      29.868 -19.787  94.849  1.00 40.41           C  
ANISOU 1528  CA  ALA A 226     3628   4197   7530    281   -204    412       C  
ATOM   1529  C   ALA A 226      31.368 -19.680  95.083  1.00 50.24           C  
ANISOU 1529  C   ALA A 226     4824   5506   8761    397   -263    327       C  
ATOM   1530  O   ALA A 226      31.980 -20.679  95.498  1.00 56.02           O  
ANISOU 1530  O   ALA A 226     5564   6223   9499    550   -326    317       O  
ATOM   1531  CB  ALA A 226      29.541 -19.724  93.353  1.00 29.00           C  
ANISOU 1531  CB  ALA A 226     2193   2705   6121    197   -112    434       C  
ATOM   1532  N   PRO A 227      32.021 -18.538  94.844  1.00 47.62           N  
ANISOU 1532  N   PRO A 227     4444   5232   8417    360   -247    256       N  
ATOM   1533  CA  PRO A 227      33.475 -18.477  95.080  1.00 43.13           C  
ANISOU 1533  CA  PRO A 227     3773   4728   7888    467   -299    153       C  
ATOM   1534  C   PRO A 227      33.889 -18.749  96.515  1.00 53.02           C  
ANISOU 1534  C   PRO A 227     5010   6045   9091    620   -454    115       C  
ATOM   1535  O   PRO A 227      34.888 -19.443  96.743  1.00 64.29           O  
ANISOU 1535  O   PRO A 227     6383   7504  10540    789   -533     56       O  
ATOM   1536  CB  PRO A 227      33.844 -17.051  94.643  1.00 48.25           C  
ANISOU 1536  CB  PRO A 227     4353   5356   8624    363   -235     96       C  
ATOM   1537  CG  PRO A 227      32.555 -16.295  94.608  1.00 45.24           C  
ANISOU 1537  CG  PRO A 227     4076   4937   8177    259   -200    174       C  
ATOM   1538  CD  PRO A 227      31.493 -17.289  94.274  1.00 44.91           C  
ANISOU 1538  CD  PRO A 227     4130   4878   8055    245   -179    264       C  
ATOM   1539  N   LEU A 228      33.157 -18.211  97.497  1.00 52.86           N  
ANISOU 1539  N   LEU A 228     5043   6035   9006    593   -506    145       N  
ATOM   1540  CA  LEU A 228      33.531 -18.430  98.892  1.00 46.26           C  
ANISOU 1540  CA  LEU A 228     4221   5231   8126    762   -670    117       C  
ATOM   1541  C   LEU A 228      33.293 -19.872  99.314  1.00 43.19           C  
ANISOU 1541  C   LEU A 228     3968   4747   7694    940   -740    184       C  
ATOM   1542  O   LEU A 228      34.055 -20.424 100.116  1.00 48.03           O  
ANISOU 1542  O   LEU A 228     4635   5359   8253   1173   -889    152       O  
ATOM   1543  CB  LEU A 228      32.773 -17.473  99.810  1.00 47.66           C  
ANISOU 1543  CB  LEU A 228     4431   5411   8265    688   -695    137       C  
ATOM   1544  CG  LEU A 228      33.168 -16.003  99.690  1.00 49.17           C  
ANISOU 1544  CG  LEU A 228     4530   5663   8489    577   -658     64       C  
ATOM   1545  CD1 LEU A 228      32.112 -15.096 100.308  1.00 53.27           C  
ANISOU 1545  CD1 LEU A 228     5111   6168   8959    486   -632    110       C  
ATOM   1546  CD2 LEU A 228      34.520 -15.791 100.345  1.00 43.37           C  
ANISOU 1546  CD2 LEU A 228     3672   4995   7812    701   -798    -57       C  
ATOM   1547  N   GLY A 229      32.238 -20.501  98.791  1.00 37.06           N  
ANISOU 1547  N   GLY A 229     3275   3863   6941    854   -637    282       N  
ATOM   1548  CA  GLY A 229      32.018 -21.906  99.093  1.00 36.38           C  
ANISOU 1548  CA  GLY A 229     3386   3624   6812   1029   -668    356       C  
ATOM   1549  C   GLY A 229      33.101 -22.790  98.511  1.00 49.16           C  
ANISOU 1549  C   GLY A 229     5020   5247   8410   1200   -689    314       C  
ATOM   1550  O   GLY A 229      33.541 -23.752  99.145  1.00 58.98           O  
ANISOU 1550  O   GLY A 229     6471   6396   9545   1461   -784    333       O  
ATOM   1551  N   LEU A 230      33.541 -22.479  97.289  1.00 49.03           N  
ANISOU 1551  N   LEU A 230     4829   5311   8489   1072   -589    265       N  
ATOM   1552  CA  LEU A 230      34.664 -23.199  96.700  1.00 43.62           C  
ANISOU 1552  CA  LEU A 230     4111   4639   7825   1230   -594    208       C  
ATOM   1553  C   LEU A 230      35.963 -22.893  97.435  1.00 46.62           C  
ANISOU 1553  C   LEU A 230     4379   5142   8193   1414   -738     98       C  
ATOM   1554  O   LEU A 230      36.794 -23.785  97.639  1.00 52.08           O  
ANISOU 1554  O   LEU A 230     5118   5817   8854   1667   -816     76       O  
ATOM   1555  CB  LEU A 230      34.785 -22.844  95.219  1.00 45.84           C  
ANISOU 1555  CB  LEU A 230     4250   4935   8232   1037   -434    186       C  
ATOM   1556  CG  LEU A 230      33.647 -23.361  94.339  1.00 43.36           C  
ANISOU 1556  CG  LEU A 230     4027   4492   7956    891   -299    298       C  
ATOM   1557  CD1 LEU A 230      33.596 -22.618  93.012  1.00 43.21           C  
ANISOU 1557  CD1 LEU A 230     3899   4479   8040    688   -158    289       C  
ATOM   1558  CD2 LEU A 230      33.806 -24.854  94.118  1.00 42.97           C  
ANISOU 1558  CD2 LEU A 230     4143   4308   7876   1073   -281    340       C  
ATOM   1559  N   MET A 231      36.155 -21.634  97.840  1.00 54.75           N  
ANISOU 1559  N   MET A 231     5263   6280   9258   1294   -772     31       N  
ATOM   1560  CA  MET A 231      37.364 -21.273  98.573  1.00 55.04           C  
ANISOU 1560  CA  MET A 231     5160   6422   9330   1438   -919    -85       C  
ATOM   1561  C   MET A 231      37.432 -21.994  99.912  1.00 58.95           C  
ANISOU 1561  C   MET A 231     5830   6861   9706   1706  -1118    -48       C  
ATOM   1562  O   MET A 231      38.501 -22.464 100.320  1.00 66.98           O  
ANISOU 1562  O   MET A 231     6796   7904  10750   1928  -1264   -123       O  
ATOM   1563  CB  MET A 231      37.426 -19.761  98.783  1.00 56.93           C  
ANISOU 1563  CB  MET A 231     5257   6744   9629   1245   -904   -158       C  
ATOM   1564  CG  MET A 231      37.882 -18.975  97.567  1.00 58.86           C  
ANISOU 1564  CG  MET A 231     5327   6989  10047   1048   -748   -240       C  
ATOM   1565  SD  MET A 231      38.206 -17.240  97.932  1.00 68.68           S  
ANISOU 1565  SD  MET A 231     6423   8255  11417    883   -752   -358       S  
ATOM   1566  CE  MET A 231      36.670 -16.499  97.383  1.00 69.16           C  
ANISOU 1566  CE  MET A 231     6658   8223  11398    658   -589   -214       C  
ATOM   1567  N   ALA A 232      36.305 -22.073 100.621  1.00 54.22           N  
ANISOU 1567  N   ALA A 232     5455   6158   8990   1691  -1134     59       N  
ATOM   1568  CA  ALA A 232      36.286 -22.790 101.892  1.00 52.17           C  
ANISOU 1568  CA  ALA A 232     5460   5769   8592   1945  -1309    111       C  
ATOM   1569  C   ALA A 232      36.689 -24.247 101.701  1.00 59.06           C  
ANISOU 1569  C   ALA A 232     6530   6511   9399   2185  -1322    165       C  
ATOM   1570  O   ALA A 232      37.485 -24.790 102.475  1.00 68.90           O  
ANISOU 1570  O   ALA A 232     7878   7709  10592   2431  -1520    120       O  
ATOM   1571  CB  ALA A 232      34.898 -22.693 102.528  1.00 46.93           C  
ANISOU 1571  CB  ALA A 232     5046   4958   7827   1864  -1267    227       C  
ATOM   1572  N   MET A 233      36.149 -24.899 100.667  1.00 55.21           N  
ANISOU 1572  N   MET A 233     6118   5945   8915   2115  -1132    241       N  
ATOM   1573  CA  MET A 233      36.515 -26.288 100.409  1.00 54.06           C  
ANISOU 1573  CA  MET A 233     6184   5646   8710   2332  -1107    301       C  
ATOM   1574  C   MET A 233      37.965 -26.419  99.964  1.00 58.26           C  
ANISOU 1574  C   MET A 233     6452   6318   9366   2473  -1180    179       C  
ATOM   1575  O   MET A 233      38.607 -27.437 100.247  1.00 61.69           O  
ANISOU 1575  O   MET A 233     7033   6642   9765   2724  -1274    183       O  
ATOM   1576  CB  MET A 233      35.572 -26.891  99.367  1.00 54.17           C  
ANISOU 1576  CB  MET A 233     6350   5527   8706   2202   -887    388       C  
ATOM   1577  CG  MET A 233      34.143 -27.028  99.859  1.00 62.03           C  
ANISOU 1577  CG  MET A 233     7658   6311   9599   2080   -810    500       C  
ATOM   1578  SD  MET A 233      33.044 -27.838  98.686  1.00 69.66           S  
ANISOU 1578  SD  MET A 233     8820   7067  10581   1884   -589    568       S  
ATOM   1579  CE  MET A 233      32.733 -26.505  97.534  1.00 65.03           C  
ANISOU 1579  CE  MET A 233     7703   6740  10264   1525   -525    497       C  
ATOM   1580  N   ALA A 234      38.500 -25.412  99.273  1.00 54.99           N  
ANISOU 1580  N   ALA A 234     5670   6113   9109   2302  -1137     54       N  
ATOM   1581  CA  ALA A 234      39.902 -25.471  98.876  1.00 52.70           C  
ANISOU 1581  CA  ALA A 234     5114   5936   8972   2418  -1191    -87       C  
ATOM   1582  C   ALA A 234      40.818 -25.354 100.088  1.00 56.71           C  
ANISOU 1582  C   ALA A 234     5560   6488   9499   2622  -1472   -203       C  
ATOM   1583  O   ALA A 234      41.743 -26.155 100.262  1.00 68.94           O  
ANISOU 1583  O   ALA A 234     7104   8008  11081   2881  -1608   -275       O  
ATOM   1584  CB  ALA A 234      40.210 -24.374  97.856  1.00 53.38           C  
ANISOU 1584  CB  ALA A 234     4879   6172   9232   2147  -1050   -201       C  
ATOM   1585  N   TYR A 235      40.575 -24.356 100.940  1.00 57.01           N  
ANISOU 1585  N   TYR A 235     5559   6587   9517   2517  -1584   -246       N  
ATOM   1586  CA  TYR A 235      41.408 -24.179 102.125  1.00 65.65           C  
ANISOU 1586  CA  TYR A 235     6616   7714  10615   2708  -1892   -395       C  
ATOM   1587  C   TYR A 235      41.235 -25.314 103.126  1.00 71.18           C  
ANISOU 1587  C   TYR A 235     7724   8224  11098   3004  -2099   -334       C  
ATOM   1588  O   TYR A 235      42.165 -25.609 103.885  1.00 74.33           O  
ANISOU 1588  O   TYR A 235     8138   8629  11475   3263  -2390   -491       O  
ATOM   1589  CB  TYR A 235      41.126 -22.824 102.768  1.00 63.00           C  
ANISOU 1589  CB  TYR A 235     6177   7462  10297   2519  -1947   -455       C  
ATOM   1590  CG  TYR A 235      41.784 -21.696 102.014  1.00 62.21           C  
ANISOU 1590  CG  TYR A 235     5690   7526  10421   2295  -1830   -600       C  
ATOM   1591  CD1 TYR A 235      43.169 -21.612 101.935  1.00 62.61           C  
ANISOU 1591  CD1 TYR A 235     5452   7674  10662   2400  -1953   -822       C  
ATOM   1592  CD2 TYR A 235      41.030 -20.734 101.359  1.00 61.00           C  
ANISOU 1592  CD2 TYR A 235     5483   7405  10291   1984  -1596   -535       C  
ATOM   1593  CE1 TYR A 235      43.785 -20.593 101.239  1.00 64.95           C  
ANISOU 1593  CE1 TYR A 235     5420   8065  11193   2186  -1836   -989       C  
ATOM   1594  CE2 TYR A 235      41.638 -19.711 100.660  1.00 67.68           C  
ANISOU 1594  CE2 TYR A 235     6043   8329  11344   1783  -1491   -685       C  
ATOM   1595  CZ  TYR A 235      43.015 -19.645 100.603  1.00 68.87           C  
ANISOU 1595  CZ  TYR A 235     5915   8548  11706   1877  -1600   -914       C  
ATOM   1596  OH  TYR A 235      43.621 -18.625  99.906  1.00 70.97           O  
ANISOU 1596  OH  TYR A 235     5911   8850  12204   1669  -1468  -1084       O  
ATOM   1597  N   PHE A 236      40.061 -25.948 103.165  1.00 65.66           N  
ANISOU 1597  N   PHE A 236     7392   7336  10221   2975  -1966   -135       N  
ATOM   1598  CA  PHE A 236      39.907 -27.115 104.028  1.00 65.87           C  
ANISOU 1598  CA  PHE A 236     7899   7131   9999   3241  -2128    -87       C  
ATOM   1599  C   PHE A 236      40.805 -28.256 103.568  1.00 71.09           C  
ANISOU 1599  C   PHE A 236     8586   7744  10681   3488  -2179   -136       C  
ATOM   1600  O   PHE A 236      41.413 -28.949 104.393  1.00 76.15           O  
ANISOU 1600  O   PHE A 236     9480   8300  11154   3794  -2453   -232       O  
ATOM   1601  CB  PHE A 236      38.449 -27.573 104.061  1.00 63.20           C  
ANISOU 1601  CB  PHE A 236     7962   6566   9485   3113  -1922    119       C  
ATOM   1602  CG  PHE A 236      38.249 -28.899 104.745  1.00 75.64           C  
ANISOU 1602  CG  PHE A 236    10122   7864  10754   3341  -2012    169       C  
ATOM   1603  CD1 PHE A 236      38.247 -28.983 106.126  1.00 82.70           C  
ANISOU 1603  CD1 PHE A 236    11417   8647  11356   3521  -2255    114       C  
ATOM   1604  CD2 PHE A 236      38.072 -30.063 104.008  1.00 82.29           C  
ANISOU 1604  CD2 PHE A 236    11170   8543  11552   3374  -1844    257       C  
ATOM   1605  CE1 PHE A 236      38.068 -30.196 106.766  1.00 83.83           C  
ANISOU 1605  CE1 PHE A 236    12193   8529  11128   3730  -2310    148       C  
ATOM   1606  CE2 PHE A 236      37.891 -31.282 104.644  1.00 82.70           C  
ANISOU 1606  CE2 PHE A 236    11830   8335  11256   3567  -1901    288       C  
ATOM   1607  CZ  PHE A 236      37.889 -31.347 106.025  1.00 81.75           C  
ANISOU 1607  CZ  PHE A 236    12142   8114  10807   3747  -2124    235       C  
ATOM   1608  N   GLN A 237      40.889 -28.476 102.255  1.00 71.03           N  
ANISOU 1608  N   GLN A 237     8356   7782  10848   3379  -1926    -82       N  
ATOM   1609  CA  GLN A 237      41.816 -29.478 101.743  1.00 69.19           C  
ANISOU 1609  CA  GLN A 237     8099   7515  10676   3613  -1958   -141       C  
ATOM   1610  C   GLN A 237      43.261 -29.045 101.948  1.00 69.86           C  
ANISOU 1610  C   GLN A 237     7805   7804  10935   3775  -2196   -387       C  
ATOM   1611  O   GLN A 237      44.130 -29.878 102.235  1.00 73.42           O  
ANISOU 1611  O   GLN A 237     8333   8211  11353   4092  -2403   -499       O  
ATOM   1612  CB  GLN A 237      41.543 -29.747 100.263  1.00 67.59           C  
ANISOU 1612  CB  GLN A 237     7766   7304  10612   3453  -1615    -35       C  
ATOM   1613  CG  GLN A 237      40.286 -30.559 100.001  1.00 71.73           C  
ANISOU 1613  CG  GLN A 237     8704   7570  10980   3360  -1410    167       C  
ATOM   1614  CD  GLN A 237      40.318 -31.260  98.655  1.00 77.12           C  
ANISOU 1614  CD  GLN A 237     9356   8180  11768   3332  -1150    230       C  
ATOM   1615  OE1 GLN A 237      40.808 -30.710  97.669  1.00 81.73           O  
ANISOU 1615  OE1 GLN A 237     9589   8950  12513   3252  -1018    166       O  
ATOM   1616  NE2 GLN A 237      39.800 -32.483  98.610  1.00 76.65           N  
ANISOU 1616  NE2 GLN A 237     9709   7837  11579   3389  -1086    326       N  
ATOM   1617  N   ILE A 238      43.539 -27.748 101.806  1.00 69.58           N  
ANISOU 1617  N   ILE A 238     7373   7982  11083   3563  -2175   -496       N  
ATOM   1618  CA  ILE A 238      44.893 -27.264 102.051  1.00 72.19           C  
ANISOU 1618  CA  ILE A 238     7335   8489  11605   3683  -2399   -767       C  
ATOM   1619  C   ILE A 238      45.264 -27.442 103.516  1.00 81.81           C  
ANISOU 1619  C   ILE A 238     8768   9663  12653   3967  -2808   -903       C  
ATOM   1620  O   ILE A 238      46.410 -27.768 103.847  1.00 90.00           O  
ANISOU 1620  O   ILE A 238     9675  10760  13760   4246  -3076  -1126       O  
ATOM   1621  CB  ILE A 238      45.025 -25.798 101.606  1.00 68.88           C  
ANISOU 1621  CB  ILE A 238     6514   8262  11396   3354  -2263   -863       C  
ATOM   1622  CG1 ILE A 238      45.091 -25.719 100.080  1.00 66.86           C  
ANISOU 1622  CG1 ILE A 238     6037   8060  11307   3157  -1923   -824       C  
ATOM   1623  CG2 ILE A 238      46.254 -25.159 102.235  1.00 69.25           C  
ANISOU 1623  CG2 ILE A 238     6243   8456  11615   3458  -2541  -1168       C  
ATOM   1624  CD1 ILE A 238      44.694 -24.376  99.525  1.00 67.18           C  
ANISOU 1624  CD1 ILE A 238     5883   8200  11442   2781  -1717   -832       C  
ATOM   1625  N   PHE A 239      44.303 -27.224 104.415  1.00 81.69           N  
ANISOU 1625  N   PHE A 239     9100   9539  12401   3916  -2872   -792       N  
ATOM   1626  CA  PHE A 239      44.551 -27.425 105.838  1.00 84.03           C  
ANISOU 1626  CA  PHE A 239     9708   9758  12462   4202  -3259   -916       C  
ATOM   1627  C   PHE A 239      44.875 -28.883 106.144  1.00 89.15           C  
ANISOU 1627  C   PHE A 239    10763  10231  12877   4584  -3434   -921       C  
ATOM   1628  O   PHE A 239      45.755 -29.171 106.963  1.00 94.93           O  
ANISOU 1628  O   PHE A 239    11584  10973  13512   4922  -3806  -1136       O  
ATOM   1629  CB  PHE A 239      43.334 -26.956 106.637  1.00 81.52           C  
ANISOU 1629  CB  PHE A 239     9735   9323  11915   4053  -3229   -770       C  
ATOM   1630  CG  PHE A 239      43.302 -27.453 108.051  1.00 86.83           C  
ANISOU 1630  CG  PHE A 239    10936   9828  12226   4361  -3564   -834       C  
ATOM   1631  CD1 PHE A 239      43.923 -26.740 109.063  1.00 92.41           C  
ANISOU 1631  CD1 PHE A 239    11581  10618  12913   4490  -3901  -1058       C  
ATOM   1632  CD2 PHE A 239      42.634 -28.623 108.372  1.00 88.92           C  
ANISOU 1632  CD2 PHE A 239    11813   9833  12141   4515  -3529   -681       C  
ATOM   1633  CE1 PHE A 239      43.887 -27.191 110.369  1.00 98.60           C  
ANISOU 1633  CE1 PHE A 239    12917  11229  13319   4794  -4215  -1126       C  
ATOM   1634  CE2 PHE A 239      42.595 -29.078 109.675  1.00 95.45           C  
ANISOU 1634  CE2 PHE A 239    13219  10480  12569   4801  -3812   -744       C  
ATOM   1635  CZ  PHE A 239      43.222 -28.361 110.675  1.00 99.15           C  
ANISOU 1635  CZ  PHE A 239    13635  11033  13005   4952  -4163   -965       C  
ATOM   1636  N   ARG A 240      44.176 -29.817 105.494  1.00 88.29           N  
ANISOU 1636  N   ARG A 240    10930   9952  12663   4547  -3177   -704       N  
ATOM   1637  CA  ARG A 240      44.438 -31.231 105.737  1.00 85.34           C  
ANISOU 1637  CA  ARG A 240    11003   9387  12037   4897  -3309   -702       C  
ATOM   1638  C   ARG A 240      45.851 -31.617 105.316  1.00 89.70           C  
ANISOU 1638  C   ARG A 240    11212  10069  12800   5164  -3476   -912       C  
ATOM   1639  O   ARG A 240      46.505 -32.430 105.980  1.00 99.72           O  
ANISOU 1639  O   ARG A 240    12766  11259  13865   5561  -3785  -1047       O  
ATOM   1640  CB  ARG A 240      43.411 -32.085 104.994  1.00 86.18           C  
ANISOU 1640  CB  ARG A 240    11431   9282  12030   4751  -2958   -445       C  
ATOM   1641  CG  ARG A 240      42.009 -32.043 105.573  1.00 91.73           C  
ANISOU 1641  CG  ARG A 240    12612   9793  12447   4566  -2823   -263       C  
ATOM   1642  CD  ARG A 240      41.878 -32.960 106.779  1.00109.51           C  
ANISOU 1642  CD  ARG A 240    15595  11805  14211   4871  -3040   -282       C  
ATOM   1643  NE  ARG A 240      40.482 -33.248 107.096  1.00120.96           N  
ANISOU 1643  NE  ARG A 240    17585  13013  15362   4674  -2798    -89       N  
ATOM   1644  CZ  ARG A 240      39.841 -34.343 106.700  1.00131.37           C  
ANISOU 1644  CZ  ARG A 240    19343  14099  16471   4636  -2554     50       C  
ATOM   1645  NH1 ARG A 240      40.470 -35.252 105.968  1.00136.92           N  
ANISOU 1645  NH1 ARG A 240    20018  14777  17230   4801  -2534     30       N  
ATOM   1646  NH2 ARG A 240      38.570 -34.527 107.032  1.00131.39           N  
ANISOU 1646  NH2 ARG A 240    19823  13890  16210   4421  -2310    194       N  
ATOM   1647  N   LYS A 241      46.338 -31.049 104.213  1.00 87.45           N  
ANISOU 1647  N   LYS A 241    10345   9978  12906   4963  -3269   -955       N  
ATOM   1648  CA  LYS A 241      47.668 -31.401 103.726  1.00 87.75           C  
ANISOU 1648  CA  LYS A 241    10027  10137  13178   5195  -3381  -1165       C  
ATOM   1649  C   LYS A 241      48.760 -30.826 104.623  1.00 91.18           C  
ANISOU 1649  C   LYS A 241    10209  10741  13694   5408  -3795  -1494       C  
ATOM   1650  O   LYS A 241      49.710 -31.527 104.990  1.00 98.23           O  
ANISOU 1650  O   LYS A 241    11135  11635  14552   5802  -4099  -1695       O  
ATOM   1651  CB  LYS A 241      47.840 -30.914 102.287  1.00 83.20           C  
ANISOU 1651  CB  LYS A 241     8954   9699  12961   4901  -3007  -1128       C  
ATOM   1652  CG  LYS A 241      48.748 -31.785 101.439  1.00 90.15           C  
ANISOU 1652  CG  LYS A 241     9661  10581  14010   5117  -2947  -1208       C  
ATOM   1653  CD  LYS A 241      47.952 -32.843 100.687  1.00 90.73           C  
ANISOU 1653  CD  LYS A 241    10100  10424  13950   5096  -2652   -942       C  
ATOM   1654  CE  LYS A 241      48.852 -33.949 100.151  1.00 92.96           C  
ANISOU 1654  CE  LYS A 241    10355  10649  14318   5415  -2670  -1025       C  
ATOM   1655  NZ  LYS A 241      49.656 -33.493  98.984  1.00 95.05           N  
ANISOU 1655  NZ  LYS A 241    10058  11094  14963   5299  -2442  -1142       N  
ATOM   1656  N   LEU A 242      48.643 -29.544 104.983  1.00 89.32           N  
ANISOU 1656  N   LEU A 242     9724  10644  13568   5160  -3820  -1572       N  
ATOM   1657  CA  LEU A 242      49.714 -28.879 105.720  1.00 94.65           C  
ANISOU 1657  CA  LEU A 242    10093  11489  14383   5315  -4184  -1918       C  
ATOM   1658  C   LEU A 242      49.766 -29.323 107.177  1.00105.87           C  
ANISOU 1658  C   LEU A 242    11995  12788  15444   5691  -4632  -2025       C  
ATOM   1659  O   LEU A 242      50.852 -29.437 107.756  1.00119.76           O  
ANISOU 1659  O   LEU A 242    13627  14629  17247   6024  -5020  -2338       O  
ATOM   1660  CB  LEU A 242      49.542 -27.363 105.631  1.00 90.73           C  
ANISOU 1660  CB  LEU A 242     9225  11149  14102   4920  -4046  -1967       C  
ATOM   1661  CG  LEU A 242      49.744 -26.764 104.240  1.00 87.85           C  
ANISOU 1661  CG  LEU A 242     8374  10920  14087   4577  -3651  -1950       C  
ATOM   1662  CD1 LEU A 242      49.326 -25.303 104.219  1.00 84.19           C  
ANISOU 1662  CD1 LEU A 242     7701  10553  13737   4180  -3492  -1949       C  
ATOM   1663  CD2 LEU A 242      51.193 -26.920 103.809  1.00 93.20           C  
ANISOU 1663  CD2 LEU A 242     8593  11744  15073   4754  -3763  -2265       C  
ATOM   1664  N   TRP A 243      48.615 -29.578 107.787  1.00 99.49           N  
ANISOU 1664  N   TRP A 243    11758  11774  14267   5656  -4590  -1792       N  
ATOM   1665  CA  TRP A 243      48.591 -29.935 109.202  1.00 99.64           C  
ANISOU 1665  CA  TRP A 243    12322  11647  13888   5999  -4989  -1891       C  
ATOM   1666  C   TRP A 243      48.203 -31.393 109.421  1.00101.53           C  
ANISOU 1666  C   TRP A 243    13242  11621  13716   6295  -5014  -1742       C  
ATOM   1667  O   TRP A 243      47.230 -31.879 108.849  1.00 97.52           O  
ANISOU 1667  O   TRP A 243    12990  10964  13101   6097  -4660  -1454       O  
ATOM   1668  CB  TRP A 243      47.638 -29.016 109.967  1.00 98.31           C  
ANISOU 1668  CB  TRP A 243    12362  11425  13564   5761  -4957  -1792       C  
ATOM   1669  CG  TRP A 243      48.181 -27.633 110.178  1.00105.60           C  
ANISOU 1669  CG  TRP A 243    12763  12570  14789   5592  -5072  -2014       C  
ATOM   1670  CD1 TRP A 243      49.009 -27.227 111.184  1.00113.08           C  
ANISOU 1670  CD1 TRP A 243    13667  13582  15716   5846  -5507  -2330       C  
ATOM   1671  CD2 TRP A 243      47.933 -26.474 109.372  1.00 99.51           C  
ANISOU 1671  CD2 TRP A 243    11478  11967  14363   5137  -4744  -1952       C  
ATOM   1672  NE1 TRP A 243      49.293 -25.890 111.054  1.00109.41           N  
ANISOU 1672  NE1 TRP A 243    12678  13313  15581   5560  -5456  -2469       N  
ATOM   1673  CE2 TRP A 243      48.644 -25.404 109.950  1.00100.88           C  
ANISOU 1673  CE2 TRP A 243    11322  12295  14715   5123  -4985  -2237       C  
ATOM   1674  CE3 TRP A 243      47.179 -26.237 108.218  1.00 93.23           C  
ANISOU 1674  CE3 TRP A 243    10504  11195  13726   4754  -4278  -1698       C  
ATOM   1675  CZ2 TRP A 243      48.625 -24.118 109.416  1.00 96.84           C  
ANISOU 1675  CZ2 TRP A 243    10334  11944  14515   4728  -4751  -2266       C  
ATOM   1676  CZ3 TRP A 243      47.161 -24.958 107.689  1.00 87.33           C  
ANISOU 1676  CZ3 TRP A 243     9299  10614  13269   4383  -4066  -1728       C  
ATOM   1677  CH2 TRP A 243      47.879 -23.916 108.288  1.00 89.02           C  
ANISOU 1677  CH2 TRP A 243     9217  10966  13640   4367  -4291  -2005       C  
ATOM   1678  N   THR A 251      62.790 -34.617 105.196  1.00168.92           N  
ANISOU 1678  N   THR A 251    16455  21978  25748   9368  -6978  -5350       N  
ATOM   1679  CA  THR A 251      63.651 -33.706 104.456  1.00170.61           C  
ANISOU 1679  CA  THR A 251    15816  22450  26556   9070  -6773  -5678       C  
ATOM   1680  C   THR A 251      63.621 -32.326 105.111  1.00169.65           C  
ANISOU 1680  C   THR A 251    15450  22462  26547   8759  -6900  -5887       C  
ATOM   1681  O   THR A 251      62.548 -31.789 105.382  1.00162.76           O  
ANISOU 1681  O   THR A 251    14945  21477  25418   8429  -6736  -5562       O  
ATOM   1682  CB  THR A 251      63.198 -33.608 102.983  1.00164.10           C  
ANISOU 1682  CB  THR A 251    14812  21586  25954   8603  -6079  -5366       C  
ATOM   1683  OG1 THR A 251      63.248 -34.908 102.379  1.00165.27           O  
ANISOU 1683  OG1 THR A 251    15194  21594  26007   8908  -5954  -5179       O  
ATOM   1684  CG2 THR A 251      64.077 -32.643 102.203  1.00166.22           C  
ANISOU 1684  CG2 THR A 251    14255  22090  26810   8277  -5839  -5735       C  
ATOM   1685  N   SER A 252      64.802 -31.753 105.365  1.00176.86           N  
ANISOU 1685  N   SER A 252    15734  23611  27854   8867  -7187  -6446       N  
ATOM   1686  CA  SER A 252      64.860 -30.449 106.020  1.00176.76           C  
ANISOU 1686  CA  SER A 252    15479  23717  27966   8596  -7323  -6686       C  
ATOM   1687  C   SER A 252      64.327 -29.323 105.141  1.00173.97           C  
ANISOU 1687  C   SER A 252    14855  23389  27856   7900  -6731  -6510       C  
ATOM   1688  O   SER A 252      63.814 -28.326 105.664  1.00169.48           O  
ANISOU 1688  O   SER A 252    14368  22815  27210   7603  -6727  -6467       O  
ATOM   1689  CB  SER A 252      66.292 -30.139 106.452  1.00186.86           C  
ANISOU 1689  CB  SER A 252    16119  25239  29639   8880  -7759  -7367       C  
ATOM   1690  OG  SER A 252      66.348 -28.909 107.154  1.00187.14           O  
ANISOU 1690  OG  SER A 252    15957  25371  29778   8645  -7909  -7607       O  
ATOM   1691  N   ALA A 285      64.426 -29.456 103.816  1.00178.06           N  
ANISOU 1691  N   ALA A 285    15087  23918  28649   7645  -6228  -6407       N  
ATOM   1692  CA  ALA A 285      63.881 -28.426 102.938  1.00160.54           C  
ANISOU 1692  CA  ALA A 285    12692  21692  26612   7005  -5662  -6230       C  
ATOM   1693  C   ALA A 285      62.363 -28.494 102.867  1.00151.09           C  
ANISOU 1693  C   ALA A 285    12147  20282  24977   6763  -5391  -5622       C  
ATOM   1694  O   ALA A 285      61.690 -27.457 102.860  1.00145.73           O  
ANISOU 1694  O   ALA A 285    11512  19584  24275   6327  -5169  -5485       O  
ATOM   1695  CB  ALA A 285      64.494 -28.546 101.541  1.00161.70           C  
ANISOU 1695  CB  ALA A 285    12362  21901  27176   6823  -5209  -6338       C  
ATOM   1696  N   GLU A 286      61.809 -29.705 102.819  1.00149.29           N  
ANISOU 1696  N   GLU A 286    12430  19887  24405   7044  -5403  -5271       N  
ATOM   1697  CA  GLU A 286      60.360 -29.858 102.780  1.00143.14           C  
ANISOU 1697  CA  GLU A 286    12268  18901  23218   6834  -5155  -4723       C  
ATOM   1698  C   GLU A 286      59.708 -29.405 104.077  1.00148.59           C  
ANISOU 1698  C   GLU A 286    13357  19533  23568   6857  -5476  -4653       C  
ATOM   1699  O   GLU A 286      58.581 -28.897 104.057  1.00145.84           O  
ANISOU 1699  O   GLU A 286    13308  19083  23022   6506  -5223  -4313       O  
ATOM   1700  CB  GLU A 286      60.004 -31.309 102.458  1.00143.21           C  
ANISOU 1700  CB  GLU A 286    12726  18728  22958   7147  -5096  -4413       C  
ATOM   1701  CG  GLU A 286      60.202 -31.666 100.995  1.00147.23           C  
ANISOU 1701  CG  GLU A 286    12976  19233  23733   6995  -4612  -4317       C  
ATOM   1702  CD  GLU A 286      60.048 -33.145 100.705  1.00153.00           C  
ANISOU 1702  CD  GLU A 286    14105  19785  24244   7361  -4584  -4080       C  
ATOM   1703  OE1 GLU A 286      58.905 -33.650 100.647  1.00149.98           O  
ANISOU 1703  OE1 GLU A 286    14293  19184  23507   7292  -4411  -3658       O  
ATOM   1704  OE2 GLU A 286      61.094 -33.803 100.537  1.00160.38           O  
ANISOU 1704  OE2 GLU A 286    14772  20790  25377   7728  -4744  -4351       O  
ATOM   1705  N   VAL A 287      60.394 -29.572 105.211  1.00155.80           N  
ANISOU 1705  N   VAL A 287    14286  20505  24405   7276  -6034  -4982       N  
ATOM   1706  CA  VAL A 287      59.858 -29.054 106.464  1.00145.06           C  
ANISOU 1706  CA  VAL A 287    13288  19090  22740   7298  -6339  -4957       C  
ATOM   1707  C   VAL A 287      59.927 -27.533 106.482  1.00143.28           C  
ANISOU 1707  C   VAL A 287    12641  19003  22798   6857  -6209  -5136       C  
ATOM   1708  O   VAL A 287      59.011 -26.862 106.971  1.00138.26           O  
ANISOU 1708  O   VAL A 287    12300  18287  21946   6607  -6140  -4915       O  
ATOM   1709  CB  VAL A 287      60.602 -29.671 107.660  1.00153.35           C  
ANISOU 1709  CB  VAL A 287    14515  20146  23607   7909  -6998  -5293       C  
ATOM   1710  CG1 VAL A 287      60.102 -29.066 108.967  1.00152.90           C  
ANISOU 1710  CG1 VAL A 287    14830  20021  23244   7939  -7319  -5312       C  
ATOM   1711  CG2 VAL A 287      60.434 -31.183 107.670  1.00155.04           C  
ANISOU 1711  CG2 VAL A 287    15252  20178  23478   8351  -7115  -5099       C  
ATOM   1712  N   LYS A 288      61.013 -26.968 105.953  1.00147.66           N  
ANISOU 1712  N   LYS A 288    12507  19755  23841   6753  -6160  -5549       N  
ATOM   1713  CA  LYS A 288      61.107 -25.519 105.826  1.00146.10           C  
ANISOU 1713  CA  LYS A 288    11908  19667  23934   6298  -5965  -5726       C  
ATOM   1714  C   LYS A 288      60.044 -24.981 104.877  1.00137.26           C  
ANISOU 1714  C   LYS A 288    10920  18450  22783   5763  -5376  -5307       C  
ATOM   1715  O   LYS A 288      59.512 -23.883 105.085  1.00134.37           O  
ANISOU 1715  O   LYS A 288    10573  18076  22407   5410  -5239  -5242       O  
ATOM   1716  CB  LYS A 288      62.504 -25.133 105.345  1.00153.05           C  
ANISOU 1716  CB  LYS A 288    12036  20758  25360   6287  -5976  -6271       C  
ATOM   1717  CG  LYS A 288      62.767 -23.643 105.282  1.00152.92           C  
ANISOU 1717  CG  LYS A 288    11588  20847  25668   5847  -5800  -6536       C  
ATOM   1718  CD  LYS A 288      64.194 -23.372 104.835  1.00160.73           C  
ANISOU 1718  CD  LYS A 288    11834  22032  27204   5857  -5811  -7117       C  
ATOM   1719  CE  LYS A 288      64.465 -21.884 104.705  1.00160.84           C  
ANISOU 1719  CE  LYS A 288    11435  22126  27551   5390  -5578  -7394       C  
ATOM   1720  NZ  LYS A 288      65.841 -21.606 104.207  1.00168.68           N  
ANISOU 1720  NZ  LYS A 288    11689  23296  29104   5354  -5527  -7985       N  
ATOM   1721  N   GLN A 289      59.721 -25.741 103.828  1.00134.18           N  
ANISOU 1721  N   GLN A 289    10633  17979  22371   5715  -5030  -5025       N  
ATOM   1722  CA  GLN A 289      58.676 -25.327 102.897  1.00127.11           C  
ANISOU 1722  CA  GLN A 289     9903  16980  21414   5253  -4497  -4628       C  
ATOM   1723  C   GLN A 289      57.304 -25.349 103.560  1.00124.41           C  
ANISOU 1723  C   GLN A 289    10176  16479  20615   5197  -4521  -4204       C  
ATOM   1724  O   GLN A 289      56.510 -24.414 103.403  1.00124.70           O  
ANISOU 1724  O   GLN A 289    10287  16481  20612   4801  -4260  -4024       O  
ATOM   1725  CB  GLN A 289      58.694 -26.232 101.664  1.00129.64           C  
ANISOU 1725  CB  GLN A 289    10211  17244  21803   5270  -4159  -4448       C  
ATOM   1726  CG  GLN A 289      57.745 -25.811 100.554  1.00127.43           C  
ANISOU 1726  CG  GLN A 289    10054  16867  21495   4811  -3608  -4097       C  
ATOM   1727  CD  GLN A 289      57.733 -26.798  99.399  1.00133.96           C  
ANISOU 1727  CD  GLN A 289    10928  17621  22348   4875  -3299  -3910       C  
ATOM   1728  OE1 GLN A 289      57.813 -28.009  99.604  1.00137.24           O  
ANISOU 1728  OE1 GLN A 289    11572  17973  22599   5269  -3477  -3815       O  
ATOM   1729  NE2 GLN A 289      57.634 -26.283  98.178  1.00134.12           N  
ANISOU 1729  NE2 GLN A 289    10766  17631  22563   4498  -2829  -3863       N  
ATOM   1730  N   MET A 290      57.007 -26.416 104.307  1.00125.54           N  
ANISOU 1730  N   MET A 290    10780  16512  20406   5595  -4822  -4053       N  
ATOM   1731  CA  MET A 290      55.701 -26.531 104.950  1.00127.02           C  
ANISOU 1731  CA  MET A 290    11573  16529  20159   5549  -4823  -3668       C  
ATOM   1732  C   MET A 290      55.482 -25.420 105.968  1.00131.14           C  
ANISOU 1732  C   MET A 290    12118  17088  20621   5417  -5019  -3778       C  
ATOM   1733  O   MET A 290      54.430 -24.772 105.979  1.00132.05           O  
ANISOU 1733  O   MET A 290    12445  17133  20596   5089  -4785  -3506       O  
ATOM   1734  CB  MET A 290      55.554 -27.901 105.611  1.00132.24           C  
ANISOU 1734  CB  MET A 290    12749  17038  20457   6027  -5129  -3560       C  
ATOM   1735  CG  MET A 290      54.291 -28.027 106.449  1.00134.09           C  
ANISOU 1735  CG  MET A 290    13630  17079  20240   6015  -5184  -3251       C  
ATOM   1736  SD  MET A 290      54.095 -29.641 107.224  1.00143.42           S  
ANISOU 1736  SD  MET A 290    15518  18031  20945   6567  -5516  -3149       S  
ATOM   1737  CE  MET A 290      53.593 -30.637 105.823  1.00143.49           C  
ANISOU 1737  CE  MET A 290    15623  17922  20974   6456  -5035  -2803       C  
ATOM   1738  N   ARG A 291      56.468 -25.185 106.838  1.00131.53           N  
ANISOU 1738  N   ARG A 291    11951  17248  20778   5683  -5456  -4187       N  
ATOM   1739  CA  ARG A 291      56.289 -24.187 107.888  1.00127.14           C  
ANISOU 1739  CA  ARG A 291    11451  16710  20146   5605  -5678  -4307       C  
ATOM   1740  C   ARG A 291      56.093 -22.793 107.307  1.00118.42           C  
ANISOU 1740  C   ARG A 291     9993  15689  19313   5081  -5307  -4315       C  
ATOM   1741  O   ARG A 291      55.401 -21.964 107.908  1.00114.97           O  
ANISOU 1741  O   ARG A 291     9740  15207  18734   4887  -5296  -4201       O  
ATOM   1742  CB  ARG A 291      57.475 -24.214 108.852  1.00131.77           C  
ANISOU 1742  CB  ARG A 291    11833  17406  20828   6013  -6231  -4794       C  
ATOM   1743  CG  ARG A 291      57.494 -25.447 109.741  1.00137.52           C  
ANISOU 1743  CG  ARG A 291    13077  18003  21170   6569  -6678  -4790       C  
ATOM   1744  CD  ARG A 291      58.176 -25.175 111.070  1.00149.79           C  
ANISOU 1744  CD  ARG A 291    14654  19602  22657   6927  -7261  -5188       C  
ATOM   1745  NE  ARG A 291      58.204 -26.365 111.915  1.00158.65           N  
ANISOU 1745  NE  ARG A 291    16346  20571  23365   7487  -7695  -5196       N  
ATOM   1746  CZ  ARG A 291      57.241 -26.692 112.772  1.00158.87           C  
ANISOU 1746  CZ  ARG A 291    17098  20371  22895   7611  -7811  -4938       C  
ATOM   1747  NH1 ARG A 291      56.172 -25.918 112.895  1.00157.48           N  
ANISOU 1747  NH1 ARG A 291    17116  20114  22606   7216  -7533  -4652       N  
ATOM   1748  NH2 ARG A 291      57.345 -27.794 113.504  1.00161.67           N  
ANISOU 1748  NH2 ARG A 291    18006  20565  22855   8135  -8195  -4975       N  
ATOM   1749  N   ALA A 292      56.680 -22.515 106.140  1.00118.62           N  
ANISOU 1749  N   ALA A 292     9542  15813  19716   4853  -4994  -4455       N  
ATOM   1750  CA  ALA A 292      56.416 -21.240 105.483  1.00114.77           C  
ANISOU 1750  CA  ALA A 292     8805  15357  19445   4350  -4598  -4441       C  
ATOM   1751  C   ALA A 292      55.026 -21.227 104.856  1.00106.57           C  
ANISOU 1751  C   ALA A 292     8149  14175  18167   4055  -4195  -3943       C  
ATOM   1752  O   ALA A 292      54.291 -20.241 104.980  1.00102.33           O  
ANISOU 1752  O   ALA A 292     7714  13602  17566   3747  -4028  -3806       O  
ATOM   1753  CB  ALA A 292      57.488 -20.954 104.433  1.00118.30           C  
ANISOU 1753  CB  ALA A 292     8669  15924  20355   4198  -4371  -4769       C  
ATOM   1754  N   ARG A 293      54.648 -22.318 104.184  1.00106.31           N  
ANISOU 1754  N   ARG A 293     8330  14060  18003   4159  -4040  -3680       N  
ATOM   1755  CA  ARG A 293      53.310 -22.406 103.608  1.00 97.23           C  
ANISOU 1755  CA  ARG A 293     7546  12776  16620   3914  -3687  -3228       C  
ATOM   1756  C   ARG A 293      52.234 -22.364 104.684  1.00 94.07           C  
ANISOU 1756  C   ARG A 293     7628  12271  15843   3958  -3846  -2979       C  
ATOM   1757  O   ARG A 293      51.134 -21.850 104.443  1.00 90.60           O  
ANISOU 1757  O   ARG A 293     7390  11760  15273   3663  -3578  -2700       O  
ATOM   1758  CB  ARG A 293      53.182 -23.685 102.782  1.00 96.47           C  
ANISOU 1758  CB  ARG A 293     7595  12607  16451   4068  -3531  -3025       C  
ATOM   1759  CG  ARG A 293      53.821 -23.610 101.406  1.00 97.17           C  
ANISOU 1759  CG  ARG A 293     7292  12755  16872   3893  -3197  -3143       C  
ATOM   1760  CD  ARG A 293      53.957 -24.994 100.793  1.00 98.15           C  
ANISOU 1760  CD  ARG A 293     7533  12819  16940   4155  -3137  -3012       C  
ATOM   1761  NE  ARG A 293      54.200 -24.952  99.355  1.00 97.07           N  
ANISOU 1761  NE  ARG A 293     7152  12692  17039   3936  -2726  -3011       N  
ATOM   1762  CZ  ARG A 293      54.382 -26.030  98.599  1.00 97.84           C  
ANISOU 1762  CZ  ARG A 293     7294  12740  17143   4113  -2591  -2914       C  
ATOM   1763  NH1 ARG A 293      54.357 -27.239  99.146  1.00 99.78           N  
ANISOU 1763  NH1 ARG A 293     7821  12913  17176   4512  -2835  -2810       N  
ATOM   1764  NH2 ARG A 293      54.600 -25.901  97.298  1.00 96.93           N  
ANISOU 1764  NH2 ARG A 293     6970  12624  17236   3897  -2206  -2930       N  
ATOM   1765  N   ARG A 294      52.526 -22.897 105.872  1.00 98.06           N  
ANISOU 1765  N   ARG A 294     8339  12755  16164   4332  -4280  -3089       N  
ATOM   1766  CA  ARG A 294      51.556 -22.840 106.961  1.00 95.85           C  
ANISOU 1766  CA  ARG A 294     8541  12350  15530   4389  -4447  -2906       C  
ATOM   1767  C   ARG A 294      51.301 -21.406 107.403  1.00101.36           C  
ANISOU 1767  C   ARG A 294     9111  13101  16301   4100  -4413  -2975       C  
ATOM   1768  O   ARG A 294      50.165 -21.041 107.726  1.00101.59           O  
ANISOU 1768  O   ARG A 294     9457  13030  16113   3931  -4297  -2720       O  
ATOM   1769  CB  ARG A 294      52.053 -23.668 108.144  1.00101.64           C  
ANISOU 1769  CB  ARG A 294     9547  13027  16045   4886  -4959  -3085       C  
ATOM   1770  CG  ARG A 294      51.844 -25.169 108.035  1.00105.96           C  
ANISOU 1770  CG  ARG A 294    10487  13431  16342   5200  -5010  -2911       C  
ATOM   1771  CD  ARG A 294      52.468 -25.855 109.243  1.00115.28           C  
ANISOU 1771  CD  ARG A 294    11951  14555  17297   5716  -5552  -3149       C  
ATOM   1772  NE  ARG A 294      52.316 -27.306 109.222  1.00118.89           N  
ANISOU 1772  NE  ARG A 294    12849  14849  17473   6052  -5623  -3005       N  
ATOM   1773  CZ  ARG A 294      52.464 -28.082 110.292  1.00119.96           C  
ANISOU 1773  CZ  ARG A 294    13477  14846  17254   6501  -6038  -3100       C  
ATOM   1774  NH1 ARG A 294      52.762 -27.541 111.465  1.00119.01           N  
ANISOU 1774  NH1 ARG A 294    13458  14736  17024   6674  -6431  -3340       N  
ATOM   1775  NH2 ARG A 294      52.312 -29.395 110.191  1.00119.13           N  
ANISOU 1775  NH2 ARG A 294    13803  14576  16884   6786  -6058  -2961       N  
ATOM   1776  N   LYS A 295      52.348 -20.576 107.420  1.00103.02           N  
ANISOU 1776  N   LYS A 295     8854  13461  16826   4040  -4505  -3333       N  
ATOM   1777  CA  LYS A 295      52.182 -19.188 107.839  1.00 99.34           C  
ANISOU 1777  CA  LYS A 295     8264  13037  16444   3773  -4469  -3422       C  
ATOM   1778  C   LYS A 295      51.290 -18.426 106.870  1.00 95.43           C  
ANISOU 1778  C   LYS A 295     7758  12508  15994   3322  -3978  -3157       C  
ATOM   1779  O   LYS A 295      50.520 -17.549 107.279  1.00 93.32           O  
ANISOU 1779  O   LYS A 295     7639  12201  15617   3117  -3897  -3026       O  
ATOM   1780  CB  LYS A 295      53.546 -18.506 107.952  1.00104.09           C  
ANISOU 1780  CB  LYS A 295     8341  13800  17408   3794  -4639  -3896       C  
ATOM   1781  CG  LYS A 295      54.341 -18.874 109.192  1.00116.26           C  
ANISOU 1781  CG  LYS A 295     9902  15381  18891   4228  -5200  -4218       C  
ATOM   1782  CD  LYS A 295      55.783 -18.402 109.060  1.00126.63           C  
ANISOU 1782  CD  LYS A 295    10617  16876  20621   4259  -5332  -4715       C  
ATOM   1783  CE  LYS A 295      56.539 -18.510 110.375  1.00133.28           C  
ANISOU 1783  CE  LYS A 295    11454  17767  21418   4669  -5918  -5083       C  
ATOM   1784  NZ  LYS A 295      57.679 -17.552 110.429  1.00138.15           N  
ANISOU 1784  NZ  LYS A 295    11484  18560  22445   4572  -6004  -5567       N  
ATOM   1785  N   THR A 296      51.380 -18.747 105.577  1.00 91.73           N  
ANISOU 1785  N   THR A 296     7130  12043  15680   3183  -3657  -3089       N  
ATOM   1786  CA  THR A 296      50.549 -18.076 104.584  1.00 90.43           C  
ANISOU 1786  CA  THR A 296     6992  11827  15540   2789  -3213  -2861       C  
ATOM   1787  C   THR A 296      49.115 -18.594 104.608  1.00 90.12           C  
ANISOU 1787  C   THR A 296     7422  11662  15157   2762  -3089  -2436       C  
ATOM   1788  O   THR A 296      48.168 -17.804 104.537  1.00 93.15           O  
ANISOU 1788  O   THR A 296     7944  11999  15449   2502  -2890  -2253       O  
ATOM   1789  CB  THR A 296      51.154 -18.246 103.190  1.00 93.64           C  
ANISOU 1789  CB  THR A 296     7100  12263  16218   2661  -2920  -2953       C  
ATOM   1790  OG1 THR A 296      52.518 -17.804 103.203  1.00 93.02           O  
ANISOU 1790  OG1 THR A 296     6560  12300  16483   2688  -3027  -3386       O  
ATOM   1791  CG2 THR A 296      50.374 -17.435 102.166  1.00 95.24           C  
ANISOU 1791  CG2 THR A 296     7350  12395  16443   2265  -2486  -2763       C  
ATOM   1792  N   ALA A 297      48.935 -19.913 104.704  1.00 88.73           N  
ANISOU 1792  N   ALA A 297     7493  11426  14794   3033  -3196  -2288       N  
ATOM   1793  CA  ALA A 297      47.588 -20.471 104.762  1.00 83.00           C  
ANISOU 1793  CA  ALA A 297     7209  10572  13755   3012  -3069  -1913       C  
ATOM   1794  C   ALA A 297      46.815 -19.912 105.951  1.00 85.29           C  
ANISOU 1794  C   ALA A 297     7770  10800  13836   3000  -3230  -1845       C  
ATOM   1795  O   ALA A 297      45.631 -19.571 105.834  1.00 85.10           O  
ANISOU 1795  O   ALA A 297     7953  10707  13673   2792  -3019  -1601       O  
ATOM   1796  CB  ALA A 297      47.655 -21.997 104.829  1.00 84.56           C  
ANISOU 1796  CB  ALA A 297     7650  10684  13794   3346  -3200  -1826       C  
ATOM   1797  N   LYS A 298      47.470 -19.817 107.112  1.00 90.58           N  
ANISOU 1797  N   LYS A 298     8446  11489  14480   3240  -3620  -2082       N  
ATOM   1798  CA  LYS A 298      46.820 -19.249 108.288  1.00 92.37           C  
ANISOU 1798  CA  LYS A 298     8940  11646  14511   3249  -3797  -2052       C  
ATOM   1799  C   LYS A 298      46.375 -17.814 108.031  1.00 94.47           C  
ANISOU 1799  C   LYS A 298     9026  11964  14905   2874  -3553  -2021       C  
ATOM   1800  O   LYS A 298      45.299 -17.400 108.475  1.00 97.04           O  
ANISOU 1800  O   LYS A 298     9610  12207  15056   2758  -3487  -1838       O  
ATOM   1801  CB  LYS A 298      47.780 -19.314 109.478  1.00 99.49           C  
ANISOU 1801  CB  LYS A 298     9843  12571  15389   3582  -4276  -2368       C  
ATOM   1802  CG  LYS A 298      47.233 -18.811 110.800  1.00104.99           C  
ANISOU 1802  CG  LYS A 298    10863  13174  15855   3654  -4517  -2373       C  
ATOM   1803  CD  LYS A 298      48.300 -18.965 111.875  1.00115.04           C  
ANISOU 1803  CD  LYS A 298    12138  14470  17101   4024  -5016  -2720       C  
ATOM   1804  CE  LYS A 298      47.966 -18.191 113.137  1.00113.79           C  
ANISOU 1804  CE  LYS A 298    12218  14242  16777   4066  -5260  -2791       C  
ATOM   1805  NZ  LYS A 298      49.044 -18.321 114.158  1.00115.72           N  
ANISOU 1805  NZ  LYS A 298    12466  14509  16995   4446  -5769  -3156       N  
ATOM   1806  N   MET A 299      47.194 -17.043 107.311  1.00 92.70           N  
ANISOU 1806  N   MET A 299     8376  11863  14981   2686  -3411  -2211       N  
ATOM   1807  CA  MET A 299      46.833 -15.668 106.984  1.00 84.11           C  
ANISOU 1807  CA  MET A 299     7149  10804  14006   2336  -3160  -2192       C  
ATOM   1808  C   MET A 299      45.704 -15.619 105.961  1.00 77.70           C  
ANISOU 1808  C   MET A 299     6484   9930  13108   2080  -2761  -1874       C  
ATOM   1809  O   MET A 299      44.693 -14.938 106.167  1.00 70.21           O  
ANISOU 1809  O   MET A 299     5707   8929  12040   1910  -2641  -1710       O  
ATOM   1810  CB  MET A 299      48.062 -14.923 106.465  1.00 80.89           C  
ANISOU 1810  CB  MET A 299     6282  10509  13944   2219  -3108  -2516       C  
ATOM   1811  CG  MET A 299      47.851 -13.438 106.252  1.00 86.43           C  
ANISOU 1811  CG  MET A 299     6854  11217  14768   1892  -2886  -2558       C  
ATOM   1812  SD  MET A 299      49.239 -12.673 105.397  1.00 94.03           S  
ANISOU 1812  SD  MET A 299     7300  12267  16162   1721  -2732  -2949       S  
ATOM   1813  CE  MET A 299      48.970 -13.265 103.728  1.00 88.79           C  
ANISOU 1813  CE  MET A 299     6648  11533  15553   1578  -2340  -2771       C  
ATOM   1814  N   LEU A 300      45.860 -16.338 104.845  1.00 75.36           N  
ANISOU 1814  N   LEU A 300     6117   9626  12889   2068  -2578  -1822       N  
ATOM   1815  CA  LEU A 300      44.865 -16.270 103.780  1.00 71.52           C  
ANISOU 1815  CA  LEU A 300     5753   9076  12345   1836  -2227  -1577       C  
ATOM   1816  C   LEU A 300      43.501 -16.760 104.246  1.00 69.07           C  
ANISOU 1816  C   LEU A 300     5828   8683  11732   1872  -2212  -1276       C  
ATOM   1817  O   LEU A 300      42.471 -16.223 103.820  1.00 66.59           O  
ANISOU 1817  O   LEU A 300     5629   8325  11348   1654  -1985  -1108       O  
ATOM   1818  CB  LEU A 300      45.340 -17.078 102.571  1.00 77.78           C  
ANISOU 1818  CB  LEU A 300     6423   9869  13260   1857  -2070  -1588       C  
ATOM   1819  CG  LEU A 300      46.653 -16.612 101.938  1.00 84.24           C  
ANISOU 1819  CG  LEU A 300     6843  10756  14407   1791  -2015  -1893       C  
ATOM   1820  CD1 LEU A 300      47.057 -17.532 100.797  1.00 87.34           C  
ANISOU 1820  CD1 LEU A 300     7150  11139  14896   1839  -1860  -1883       C  
ATOM   1821  CD2 LEU A 300      46.539 -15.173 101.463  1.00 81.36           C  
ANISOU 1821  CD2 LEU A 300     6363  10371  14180   1470  -1779  -1958       C  
ATOM   1822  N   MET A 301      43.468 -17.767 105.122  1.00 70.11           N  
ANISOU 1822  N   MET A 301     6176   8767  11697   2157  -2462  -1239       N  
ATOM   1823  CA  MET A 301      42.184 -18.250 105.618  1.00 62.05           C  
ANISOU 1823  CA  MET A 301     5531   7623  10422   2196  -2453  -1004       C  
ATOM   1824  C   MET A 301      41.474 -17.187 106.443  1.00 62.73           C  
ANISOU 1824  C   MET A 301     5711   7683  10440   2070  -2488   -983       C  
ATOM   1825  O   MET A 301      40.239 -17.114 106.424  1.00 64.77           O  
ANISOU 1825  O   MET A 301     6175   7865  10571   1955  -2335   -784       O  
ATOM   1826  CB  MET A 301      42.383 -19.522 106.443  1.00 66.62           C  
ANISOU 1826  CB  MET A 301     6383   8103  10827   2550  -2734  -1007       C  
ATOM   1827  CG  MET A 301      42.767 -20.734 105.615  1.00 71.45           C  
ANISOU 1827  CG  MET A 301     6991   8697  11459   2687  -2661   -960       C  
ATOM   1828  SD  MET A 301      43.212 -22.157 106.626  1.00 82.86           S  
ANISOU 1828  SD  MET A 301     8788  10009  12685   3141  -3026  -1013       S  
ATOM   1829  CE  MET A 301      43.996 -23.198 105.398  1.00 84.68           C  
ANISOU 1829  CE  MET A 301     8832  10277  13064   3247  -2900  -1026       C  
ATOM   1830  N   VAL A 302      42.230 -16.359 107.166  1.00 64.45           N  
ANISOU 1830  N   VAL A 302     5772   7959  10756   2096  -2691  -1201       N  
ATOM   1831  CA  VAL A 302      41.619 -15.267 107.915  1.00 65.38           C  
ANISOU 1831  CA  VAL A 302     5963   8051  10829   1973  -2719  -1195       C  
ATOM   1832  C   VAL A 302      41.085 -14.202 106.967  1.00 65.64           C  
ANISOU 1832  C   VAL A 302     5849   8122  10969   1637  -2371  -1109       C  
ATOM   1833  O   VAL A 302      40.001 -13.646 107.183  1.00 64.47           O  
ANISOU 1833  O   VAL A 302     5851   7917  10727   1508  -2264   -969       O  
ATOM   1834  CB  VAL A 302      42.625 -14.672 108.915  1.00 67.60           C  
ANISOU 1834  CB  VAL A 302     6113   8381  11190   2101  -3042  -1478       C  
ATOM   1835  CG1 VAL A 302      42.028 -13.452 109.597  1.00 60.91           C  
ANISOU 1835  CG1 VAL A 302     5320   7506  10318   1955  -3048  -1477       C  
ATOM   1836  CG2 VAL A 302      43.035 -15.715 109.940  1.00 67.97           C  
ANISOU 1836  CG2 VAL A 302     6403   8359  11063   2474  -3425  -1565       C  
ATOM   1837  N   VAL A 303      41.844 -13.883 105.917  1.00 62.82           N  
ANISOU 1837  N   VAL A 303     5220   7845  10802   1505  -2198  -1205       N  
ATOM   1838  CA  VAL A 303      41.383 -12.902 104.938  1.00 58.54           C  
ANISOU 1838  CA  VAL A 303     4609   7301  10333   1216  -1880  -1137       C  
ATOM   1839  C   VAL A 303      40.073 -13.359 104.312  1.00 61.11           C  
ANISOU 1839  C   VAL A 303     5165   7555  10500   1135  -1672   -878       C  
ATOM   1840  O   VAL A 303      39.120 -12.583 104.182  1.00 66.02           O  
ANISOU 1840  O   VAL A 303     5883   8135  11065    969  -1520   -770       O  
ATOM   1841  CB  VAL A 303      42.465 -12.665 103.869  1.00 55.89           C  
ANISOU 1841  CB  VAL A 303     3983   6994  10259   1124  -1756  -1329       C  
ATOM   1842  CG1 VAL A 303      41.916 -11.814 102.735  1.00 52.92           C  
ANISOU 1842  CG1 VAL A 303     3617   6551   9941    862  -1433  -1252       C  
ATOM   1843  CG2 VAL A 303      43.689 -12.020 104.492  1.00 62.67           C  
ANISOU 1843  CG2 VAL A 303     4576   7930  11306   1165  -1937  -1625       C  
ATOM   1844  N   VAL A 304      40.006 -14.630 103.912  1.00 60.43           N  
ANISOU 1844  N   VAL A 304     5163   7452  10346   1260  -1669   -790       N  
ATOM   1845  CA  VAL A 304      38.782 -15.143 103.309  1.00 54.82           C  
ANISOU 1845  CA  VAL A 304     4654   6678   9496   1188  -1484   -573       C  
ATOM   1846  C   VAL A 304      37.647 -15.160 104.327  1.00 58.06           C  
ANISOU 1846  C   VAL A 304     5296   7018   9747   1227  -1560   -451       C  
ATOM   1847  O   VAL A 304      36.484 -14.919 103.983  1.00 59.44           O  
ANISOU 1847  O   VAL A 304     5581   7145   9858   1084  -1390   -319       O  
ATOM   1848  CB  VAL A 304      39.028 -16.540 102.713  1.00 48.44           C  
ANISOU 1848  CB  VAL A 304     3886   5858   8661   1331  -1473   -523       C  
ATOM   1849  CG1 VAL A 304      37.740 -17.103 102.142  1.00 42.67           C  
ANISOU 1849  CG1 VAL A 304     3359   5053   7800   1257  -1301   -329       C  
ATOM   1850  CG2 VAL A 304      40.115 -16.481 101.650  1.00 55.62           C  
ANISOU 1850  CG2 VAL A 304     4547   6798   9789   1281  -1395   -673       C  
ATOM   1851  N   LEU A 305      37.963 -15.442 105.594  1.00 58.90           N  
ANISOU 1851  N   LEU A 305     5490   7093   9798   1432  -1834   -513       N  
ATOM   1852  CA  LEU A 305      36.925 -15.468 106.621  1.00 58.31           C  
ANISOU 1852  CA  LEU A 305     5671   6907   9578   1490  -1923   -412       C  
ATOM   1853  C   LEU A 305      36.413 -14.067 106.929  1.00 64.00           C  
ANISOU 1853  C   LEU A 305     6333   7638  10344   1305  -1860   -426       C  
ATOM   1854  O   LEU A 305      35.199 -13.854 107.035  1.00 66.15           O  
ANISOU 1854  O   LEU A 305     6737   7838  10558   1214  -1746   -295       O  
ATOM   1855  CB  LEU A 305      37.453 -16.130 107.892  1.00 63.41           C  
ANISOU 1855  CB  LEU A 305     6512   7477  10105   1786  -2264   -490       C  
ATOM   1856  CG  LEU A 305      36.505 -16.135 109.093  1.00 67.84           C  
ANISOU 1856  CG  LEU A 305     7422   7877  10478   1880  -2391   -404       C  
ATOM   1857  CD1 LEU A 305      35.338 -17.078 108.846  1.00 62.03           C  
ANISOU 1857  CD1 LEU A 305     6964   6989   9615   1891  -2224   -193       C  
ATOM   1858  CD2 LEU A 305      37.255 -16.530 110.351  1.00 68.14           C  
ANISOU 1858  CD2 LEU A 305     7691   7840  10360   2174  -2766   -540       C  
ATOM   1859  N   VAL A 306      37.319 -13.099 107.080  1.00 63.01           N  
ANISOU 1859  N   VAL A 306     6007   7593  10342   1252  -1930   -595       N  
ATOM   1860  CA  VAL A 306      36.889 -11.729 107.341  1.00 59.99           C  
ANISOU 1860  CA  VAL A 306     5579   7208  10008   1084  -1860   -613       C  
ATOM   1861  C   VAL A 306      36.134 -11.171 106.141  1.00 61.87           C  
ANISOU 1861  C   VAL A 306     5787   7452  10270    851  -1531   -497       C  
ATOM   1862  O   VAL A 306      35.173 -10.408 106.293  1.00 63.45           O  
ANISOU 1862  O   VAL A 306     6059   7605  10445    740  -1431   -418       O  
ATOM   1863  CB  VAL A 306      38.096 -10.850 107.710  1.00 59.78           C  
ANISOU 1863  CB  VAL A 306     5339   7252  10124   1080  -2001   -843       C  
ATOM   1864  CG1 VAL A 306      37.674  -9.396 107.792  1.00 55.48           C  
ANISOU 1864  CG1 VAL A 306     4744   6694   9640    890  -1884   -856       C  
ATOM   1865  CG2 VAL A 306      38.706 -11.310 109.025  1.00 60.88           C  
ANISOU 1865  CG2 VAL A 306     5560   7368  10202   1335  -2381   -980       C  
ATOM   1866  N   PHE A 307      36.554 -11.543 104.930  1.00 58.28           N  
ANISOU 1866  N   PHE A 307     5247   7040   9858    794  -1375   -493       N  
ATOM   1867  CA  PHE A 307      35.847 -11.109 103.730  1.00 52.18           C  
ANISOU 1867  CA  PHE A 307     4507   6238   9080    613  -1110   -396       C  
ATOM   1868  C   PHE A 307      34.418 -11.640 103.714  1.00 58.81           C  
ANISOU 1868  C   PHE A 307     5536   7020   9787    597  -1030   -224       C  
ATOM   1869  O   PHE A 307      33.468 -10.893 103.458  1.00 63.02           O  
ANISOU 1869  O   PHE A 307     6135   7517  10292    475   -896   -153       O  
ATOM   1870  CB  PHE A 307      36.604 -11.571 102.484  1.00 46.84           C  
ANISOU 1870  CB  PHE A 307     3719   5550   8530    587  -1019   -454       C  
ATOM   1871  CG  PHE A 307      36.039 -11.046 101.195  1.00 56.68           C  
ANISOU 1871  CG  PHE A 307     5006   6712   9817    425   -791   -390       C  
ATOM   1872  CD1 PHE A 307      35.072 -11.758 100.504  1.00 55.09           C  
ANISOU 1872  CD1 PHE A 307     4945   6457   9528    400   -695   -248       C  
ATOM   1873  CD2 PHE A 307      36.474  -9.838 100.676  1.00 58.05           C  
ANISOU 1873  CD2 PHE A 307     5086   6854  10114    312   -679   -478       C  
ATOM   1874  CE1 PHE A 307      34.552 -11.274  99.313  1.00 53.10           C  
ANISOU 1874  CE1 PHE A 307     4747   6122   9305    284   -521   -192       C  
ATOM   1875  CE2 PHE A 307      35.962  -9.352  99.486  1.00 54.89           C  
ANISOU 1875  CE2 PHE A 307     4757   6364   9733    204   -486   -412       C  
ATOM   1876  CZ  PHE A 307      34.999 -10.068  98.805  1.00 54.60           C  
ANISOU 1876  CZ  PHE A 307     4868   6276   9602    201   -422   -266       C  
ATOM   1877  N   ALA A 308      34.250 -12.938 103.982  1.00 51.69           N  
ANISOU 1877  N   ALA A 308     4720   6092   8827    731  -1118   -169       N  
ATOM   1878  CA  ALA A 308      32.914 -13.525 103.982  1.00 43.57           C  
ANISOU 1878  CA  ALA A 308     3841   4983   7730    708  -1043    -30       C  
ATOM   1879  C   ALA A 308      32.022 -12.881 105.036  1.00 48.52           C  
ANISOU 1879  C   ALA A 308     4540   5547   8348    694  -1086     11       C  
ATOM   1880  O   ALA A 308      30.813 -12.727 104.826  1.00 50.44           O  
ANISOU 1880  O   ALA A 308     4833   5740   8592    588   -949    104       O  
ATOM   1881  CB  ALA A 308      33.008 -15.034 104.221  1.00 34.27           C  
ANISOU 1881  CB  ALA A 308     2767   3750   6504    890  -1147     14       C  
ATOM   1882  N   LEU A 309      32.598 -12.496 106.177  1.00 52.88           N  
ANISOU 1882  N   LEU A 309     5094   6093   8905    806  -1288    -67       N  
ATOM   1883  CA  LEU A 309      31.804 -11.866 107.230  1.00 52.38           C  
ANISOU 1883  CA  LEU A 309     5117   5945   8839    812  -1350    -32       C  
ATOM   1884  C   LEU A 309      31.468 -10.423 106.880  1.00 50.83           C  
ANISOU 1884  C   LEU A 309     4814   5792   8709    625  -1195    -49       C  
ATOM   1885  O   LEU A 309      30.323  -9.986 107.037  1.00 51.08           O  
ANISOU 1885  O   LEU A 309     4887   5766   8756    550  -1088     35       O  
ATOM   1886  CB  LEU A 309      32.544 -11.935 108.563  1.00 49.86           C  
ANISOU 1886  CB  LEU A 309     4899   5578   8468   1018  -1660   -124       C  
ATOM   1887  CG  LEU A 309      32.748 -13.321 109.174  1.00 54.59           C  
ANISOU 1887  CG  LEU A 309     5755   6068   8921   1270  -1850    -92       C  
ATOM   1888  CD1 LEU A 309      33.854 -13.288 110.221  1.00 57.64           C  
ANISOU 1888  CD1 LEU A 309     6225   6451   9224   1474  -2182   -246       C  
ATOM   1889  CD2 LEU A 309      31.451 -13.836 109.773  1.00 52.71           C  
ANISOU 1889  CD2 LEU A 309     5839   5607   8582   1332  -1805     68       C  
ATOM   1890  N   CYS A 310      32.455  -9.666 106.396  1.00 46.72           N  
ANISOU 1890  N   CYS A 310     4162   5353   8237    563  -1175   -159       N  
ATOM   1891  CA  CYS A 310      32.212  -8.266 106.071  1.00 54.22           C  
ANISOU 1891  CA  CYS A 310     5062   6306   9235    421  -1038   -175       C  
ATOM   1892  C   CYS A 310      31.169  -8.121 104.971  1.00 58.40           C  
ANISOU 1892  C   CYS A 310     5660   6818   9709    311   -806    -61       C  
ATOM   1893  O   CYS A 310      30.414  -7.142 104.953  1.00 64.09           O  
ANISOU 1893  O   CYS A 310     6407   7507  10436    242   -711    -25       O  
ATOM   1894  CB  CYS A 310      33.522  -7.596 105.655  1.00 59.42           C  
ANISOU 1894  CB  CYS A 310     5570   7024   9982    381  -1046   -320       C  
ATOM   1895  SG  CYS A 310      34.621  -7.165 107.029  1.00 64.87           S  
ANISOU 1895  SG  CYS A 310     6147   7736  10764    476  -1333   -511       S  
ATOM   1896  N   TYR A 311      31.116  -9.071 104.040  1.00 49.89           N  
ANISOU 1896  N   TYR A 311     4617   5759   8581    310   -733    -15       N  
ATOM   1897  CA  TYR A 311      30.211  -8.967 102.906  1.00 34.02           C  
ANISOU 1897  CA  TYR A 311     2677   3725   6524    226   -564     64       C  
ATOM   1898  C   TYR A 311      28.897  -9.711 103.095  1.00 39.74           C  
ANISOU 1898  C   TYR A 311     3479   4421   7200    226   -524    160       C  
ATOM   1899  O   TYR A 311      27.984  -9.531 102.281  1.00 39.49           O  
ANISOU 1899  O   TYR A 311     3494   4375   7137    169   -414    208       O  
ATOM   1900  CB  TYR A 311      30.906  -9.476 101.639  1.00 34.06           C  
ANISOU 1900  CB  TYR A 311     2646   3699   6598    208   -519     44       C  
ATOM   1901  CG  TYR A 311      31.880  -8.474 101.077  1.00 42.11           C  
ANISOU 1901  CG  TYR A 311     3573   4699   7729    166   -479    -47       C  
ATOM   1902  CD1 TYR A 311      33.144  -8.325 101.629  1.00 43.89           C  
ANISOU 1902  CD1 TYR A 311     3669   4978   8031    201   -574   -174       C  
ATOM   1903  CD2 TYR A 311      31.533  -7.668 100.002  1.00 45.92           C  
ANISOU 1903  CD2 TYR A 311     4087   5115   8245    103   -349    -19       C  
ATOM   1904  CE1 TYR A 311      34.033  -7.405 101.127  1.00 42.08           C  
ANISOU 1904  CE1 TYR A 311     3328   4734   7926    142   -510   -282       C  
ATOM   1905  CE2 TYR A 311      32.420  -6.747  99.489  1.00 46.41           C  
ANISOU 1905  CE2 TYR A 311     4065   5155   8415     61   -281   -110       C  
ATOM   1906  CZ  TYR A 311      33.669  -6.621 100.056  1.00 50.15           C  
ANISOU 1906  CZ  TYR A 311     4395   5681   8980     66   -347   -248       C  
ATOM   1907  OH  TYR A 311      34.563  -5.706  99.554  1.00 69.50           O  
ANISOU 1907  OH  TYR A 311     6738   8112  11558     -3   -250   -366       O  
ATOM   1908  N   LEU A 312      28.776 -10.542 104.128  1.00 43.41           N  
ANISOU 1908  N   LEU A 312     3943   4846   7705    300   -628    182       N  
ATOM   1909  CA  LEU A 312      27.518 -11.258 104.328  1.00 47.85           C  
ANISOU 1909  CA  LEU A 312     4538   5342   8303    285   -564    269       C  
ATOM   1910  C   LEU A 312      26.339 -10.321 104.553  1.00 50.51           C  
ANISOU 1910  C   LEU A 312     4868   5665   8658    219   -456    296       C  
ATOM   1911  O   LEU A 312      25.306 -10.494 103.884  1.00 55.95           O  
ANISOU 1911  O   LEU A 312     5567   6362   9328    162   -336    325       O  
ATOM   1912  CB  LEU A 312      27.665 -12.251 105.485  1.00 38.78           C  
ANISOU 1912  CB  LEU A 312     3423   4094   7219    425   -710    301       C  
ATOM   1913  CG  LEU A 312      26.426 -13.107 105.755  1.00 43.62           C  
ANISOU 1913  CG  LEU A 312     4060   4571   7943    428   -609    405       C  
ATOM   1914  CD1 LEU A 312      26.200 -14.047 104.591  1.00 43.85           C  
ANISOU 1914  CD1 LEU A 312     4063   4622   7977    358   -507    430       C  
ATOM   1915  CD2 LEU A 312      26.564 -13.882 107.055  1.00 49.75           C  
ANISOU 1915  CD2 LEU A 312     5076   5111   8716    643   -744    465       C  
ATOM   1916  N   PRO A 313      26.404  -9.341 105.463  1.00 47.57           N  
ANISOU 1916  N   PRO A 313     4473   5275   8325    237   -502    273       N  
ATOM   1917  CA  PRO A 313      25.199  -8.534 105.739  1.00 45.71           C  
ANISOU 1917  CA  PRO A 313     4220   5022   8127    194   -384    297       C  
ATOM   1918  C   PRO A 313      24.623  -7.815 104.529  1.00 48.55           C  
ANISOU 1918  C   PRO A 313     4615   5456   8378    142   -276    284       C  
ATOM   1919  O   PRO A 313      23.404  -7.861 104.312  1.00 51.78           O  
ANISOU 1919  O   PRO A 313     5011   5880   8782    124   -180    293       O  
ATOM   1920  CB  PRO A 313      25.691  -7.551 106.810  1.00 44.75           C  
ANISOU 1920  CB  PRO A 313     4072   4863   8068    236   -481    264       C  
ATOM   1921  CG  PRO A 313      26.792  -8.280 107.494  1.00 41.36           C  
ANISOU 1921  CG  PRO A 313     3662   4397   7655    340   -690    235       C  
ATOM   1922  CD  PRO A 313      27.500  -9.020 106.394  1.00 48.01           C  
ANISOU 1922  CD  PRO A 313     4514   5318   8410    320   -683    213       C  
ATOM   1923  N   ILE A 314      25.455  -7.150 103.727  1.00 52.95           N  
ANISOU 1923  N   ILE A 314     5200   6049   8869    134   -296    250       N  
ATOM   1924  CA  ILE A 314      24.920  -6.433 102.573  1.00 48.64           C  
ANISOU 1924  CA  ILE A 314     4686   5534   8262    119   -225    251       C  
ATOM   1925  C   ILE A 314      24.377  -7.407 101.535  1.00 49.87           C  
ANISOU 1925  C   ILE A 314     4852   5684   8410    109   -200    277       C  
ATOM   1926  O   ILE A 314      23.337  -7.159 100.914  1.00 57.22           O  
ANISOU 1926  O   ILE A 314     5772   6636   9335    114   -162    278       O  
ATOM   1927  CB  ILE A 314      25.984  -5.503 101.969  1.00 40.20           C  
ANISOU 1927  CB  ILE A 314     3606   4426   7240    107   -235    221       C  
ATOM   1928  CG1 ILE A 314      25.326  -4.548 100.972  1.00 29.24           C  
ANISOU 1928  CG1 ILE A 314     2230   3019   5859    112   -172    238       C  
ATOM   1929  CG2 ILE A 314      27.070  -6.317 101.294  1.00 42.37           C  
ANISOU 1929  CG2 ILE A 314     3868   4678   7551     97   -264    205       C  
ATOM   1930  CD1 ILE A 314      24.209  -3.709 101.563  1.00 34.11           C  
ANISOU 1930  CD1 ILE A 314     2836   3663   6461    143   -142    243       C  
ATOM   1931  N   SER A 315      25.076  -8.524 101.320  1.00 49.17           N  
ANISOU 1931  N   SER A 315     4773   5582   8326    104   -232    284       N  
ATOM   1932  CA  SER A 315      24.613  -9.512 100.351  1.00 45.90           C  
ANISOU 1932  CA  SER A 315     4369   5163   7908     92   -208    305       C  
ATOM   1933  C   SER A 315      23.247 -10.063 100.735  1.00 49.75           C  
ANISOU 1933  C   SER A 315     4830   5695   8377     83   -161    301       C  
ATOM   1934  O   SER A 315      22.371 -10.230  99.876  1.00 54.27           O  
ANISOU 1934  O   SER A 315     5378   6292   8951     75   -137    287       O  
ATOM   1935  CB  SER A 315      25.630 -10.645 100.225  1.00 44.51           C  
ANISOU 1935  CB  SER A 315     4200   4969   7743     98   -247    311       C  
ATOM   1936  OG  SER A 315      26.769 -10.240  99.484  1.00 42.53           O  
ANISOU 1936  OG  SER A 315     3940   4683   7536     97   -261    290       O  
ATOM   1937  N   VAL A 316      23.053 -10.370 102.020  1.00 50.16           N  
ANISOU 1937  N   VAL A 316     4853   5731   8475     83   -147    307       N  
ATOM   1938  CA  VAL A 316      21.753 -10.850 102.478  1.00 45.95           C  
ANISOU 1938  CA  VAL A 316     4245   5189   8024     51    -56    292       C  
ATOM   1939  C   VAL A 316      20.699  -9.760 102.330  1.00 48.08           C  
ANISOU 1939  C   VAL A 316     4480   5544   8245     56    -14    236       C  
ATOM   1940  O   VAL A 316      19.583 -10.013 101.865  1.00 46.98           O  
ANISOU 1940  O   VAL A 316     4275   5478   8097     34     34    178       O  
ATOM   1941  CB  VAL A 316      21.840 -11.349 103.931  1.00 43.24           C  
ANISOU 1941  CB  VAL A 316     3842   4723   7864     45    -15    331       C  
ATOM   1942  CG1 VAL A 316      20.445 -11.606 104.487  1.00 44.90           C  
ANISOU 1942  CG1 VAL A 316     3963   4916   8182    -29    171    281       C  
ATOM   1943  CG2 VAL A 316      22.694 -12.602 104.016  1.00 38.83           C  
ANISOU 1943  CG2 VAL A 316     3285   4073   7397     68    -72    391       C  
ATOM   1944  N   LEU A 317      21.035  -8.529 102.725  1.00 47.88           N  
ANISOU 1944  N   LEU A 317     4475   5514   8202     89    -40    243       N  
ATOM   1945  CA  LEU A 317      20.064  -7.443 102.636  1.00 41.06           C  
ANISOU 1945  CA  LEU A 317     3565   4715   7321    117     -7    198       C  
ATOM   1946  C   LEU A 317      19.655  -7.174 101.193  1.00 47.22           C  
ANISOU 1946  C   LEU A 317     4328   5542   8073    147    -51    178       C  
ATOM   1947  O   LEU A 317      18.487  -6.872 100.920  1.00 49.48           O  
ANISOU 1947  O   LEU A 317     4519   5905   8375    179    -34    117       O  
ATOM   1948  CB  LEU A 317      20.624  -6.174 103.277  1.00 41.58           C  
ANISOU 1948  CB  LEU A 317     3654   4732   7412    147    -23    218       C  
ATOM   1949  CG  LEU A 317      20.626  -6.111 104.804  1.00 44.51           C  
ANISOU 1949  CG  LEU A 317     3980   5014   7917    137     29    231       C  
ATOM   1950  CD1 LEU A 317      21.260  -4.814 105.264  1.00 43.59           C  
ANISOU 1950  CD1 LEU A 317     3882   4855   7825    166     -7    241       C  
ATOM   1951  CD2 LEU A 317      19.212  -6.240 105.349  1.00 47.28           C  
ANISOU 1951  CD2 LEU A 317     4232   5378   8356    121    169    177       C  
ATOM   1952  N   ASN A 318      20.592  -7.287 100.249  1.00 51.27           N  
ANISOU 1952  N   ASN A 318     4904   6003   8572    146   -106    219       N  
ATOM   1953  CA  ASN A 318      20.235  -7.066  98.849  1.00 47.62           C  
ANISOU 1953  CA  ASN A 318     4421   5569   8103    182   -147    205       C  
ATOM   1954  C   ASN A 318      19.328  -8.172  98.321  1.00 43.48           C  
ANISOU 1954  C   ASN A 318     3824   5110   7588    167   -151    158       C  
ATOM   1955  O   ASN A 318      18.429  -7.911  97.512  1.00 49.59           O  
ANISOU 1955  O   ASN A 318     4518   5966   8360    220   -193    104       O  
ATOM   1956  CB  ASN A 318      21.495  -6.955  97.995  1.00 50.27           C  
ANISOU 1956  CB  ASN A 318     4834   5828   8437    171   -172    254       C  
ATOM   1957  CG  ASN A 318      22.084  -5.562  98.009  1.00 50.12           C  
ANISOU 1957  CG  ASN A 318     4844   5775   8425    197   -164    267       C  
ATOM   1958  OD1 ASN A 318      21.358  -4.568  98.008  1.00 58.81           O  
ANISOU 1958  OD1 ASN A 318     5915   6921   9510    263   -166    247       O  
ATOM   1959  ND2 ASN A 318      23.409  -5.481  98.026  1.00 47.20           N  
ANISOU 1959  ND2 ASN A 318     4517   5332   8085    157   -152    287       N  
ATOM   1960  N   VAL A 319      19.545  -9.412  98.764  1.00 33.44           N  
ANISOU 1960  N   VAL A 319     2567   3814   6325    106   -115    168       N  
ATOM   1961  CA  VAL A 319      18.694 -10.511  98.316  1.00 39.38           C  
ANISOU 1961  CA  VAL A 319     3239   4629   7094     68    -98    110       C  
ATOM   1962  C   VAL A 319      17.288 -10.368  98.885  1.00 47.95           C  
ANISOU 1962  C   VAL A 319     4183   5818   8218     51    -41     12       C  
ATOM   1963  O   VAL A 319      16.294 -10.579  98.179  1.00 51.86           O  
ANISOU 1963  O   VAL A 319     4554   6410   8740     53    -65    -73       O  
ATOM   1964  CB  VAL A 319      19.323 -11.862  98.697  1.00 35.11           C  
ANISOU 1964  CB  VAL A 319     2753   4035   6551      8    -56    146       C  
ATOM   1965  CG1 VAL A 319      18.306 -12.982  98.547  1.00 31.77           C  
ANISOU 1965  CG1 VAL A 319     2233   3684   6152    -69      5     68       C  
ATOM   1966  CG2 VAL A 319      20.553 -12.130  97.849  1.00 24.66           C  
ANISOU 1966  CG2 VAL A 319     1526   2633   5210     30   -113    216       C  
ATOM   1967  N   LEU A 320      17.179 -10.019 100.171  1.00 47.15           N  
ANISOU 1967  N   LEU A 320     4080   5704   8130     32     38     11       N  
ATOM   1968  CA  LEU A 320      15.864  -9.840 100.781  1.00 48.68           C  
ANISOU 1968  CA  LEU A 320     4129   5987   8379      4    128    -92       C  
ATOM   1969  C   LEU A 320      15.104  -8.695 100.126  1.00 56.40           C  
ANISOU 1969  C   LEU A 320     5003   7051   9374    110     50   -147       C  
ATOM   1970  O   LEU A 320      13.885  -8.776  99.931  1.00 65.90           O  
ANISOU 1970  O   LEU A 320     6033   8363  10643    109     67   -261       O  
ATOM   1971  CB  LEU A 320      16.014  -9.582 102.281  1.00 40.40           C  
ANISOU 1971  CB  LEU A 320     3106   4857   7386    -31    245    -74       C  
ATOM   1972  CG  LEU A 320      16.722 -10.653 103.111  1.00 44.24           C  
ANISOU 1972  CG  LEU A 320     3658   5191   7960   -115    338    -22       C  
ATOM   1973  CD1 LEU A 320      16.958 -10.162 104.530  1.00 46.07           C  
ANISOU 1973  CD1 LEU A 320     3905   5299   8301   -122    447      7       C  
ATOM   1974  CD2 LEU A 320      15.909 -11.933 103.112  1.00 42.47           C  
ANISOU 1974  CD2 LEU A 320     3358   4967   7809   -249    484   -113       C  
ATOM   1975  N   LYS A 321      15.813  -7.622  99.773  1.00 48.92           N  
ANISOU 1975  N   LYS A 321     4150   6060   8377    203    -33    -76       N  
ATOM   1976  CA  LYS A 321      15.173  -6.469  99.149  1.00 43.48           C  
ANISOU 1976  CA  LYS A 321     3385   5451   7683    335   -110   -115       C  
ATOM   1977  C   LYS A 321      14.832  -6.739  97.689  1.00 46.79           C  
ANISOU 1977  C   LYS A 321     3751   5939   8087    398   -226   -149       C  
ATOM   1978  O   LYS A 321      13.689  -6.546  97.259  1.00 47.91           O  
ANISOU 1978  O   LYS A 321     3731   6205   8269    481   -281   -244       O  
ATOM   1979  CB  LYS A 321      16.094  -5.256  99.269  1.00 45.67           C  
ANISOU 1979  CB  LYS A 321     3797   5649   7907    400   -134    -30       C  
ATOM   1980  CG  LYS A 321      15.668  -4.033  98.482  1.00 44.70           C  
ANISOU 1980  CG  LYS A 321     3647   5588   7748    572   -217    -46       C  
ATOM   1981  CD  LYS A 321      16.842  -3.074  98.369  1.00 52.19           C  
ANISOU 1981  CD  LYS A 321     4755   6432   8644    601   -222     43       C  
ATOM   1982  CE  LYS A 321      16.521  -1.867  97.510  1.00 60.59           C  
ANISOU 1982  CE  LYS A 321     5845   7532   9643    811   -294     42       C  
ATOM   1983  NZ  LYS A 321      17.711  -0.982  97.353  1.00 60.85           N  
ANISOU 1983  NZ  LYS A 321     6033   7433   9655    824   -269    117       N  
ATOM   1984  N   ARG A 322      15.816  -7.194  96.911  1.00 47.77           N  
ANISOU 1984  N   ARG A 322     3999   5987   8164    369   -269    -77       N  
ATOM   1985  CA  ARG A 322      15.646  -7.290  95.466  1.00 40.79           C  
ANISOU 1985  CA  ARG A 322     3097   5155   7249    450   -384    -93       C  
ATOM   1986  C   ARG A 322      14.935  -8.566  95.027  1.00 42.82           C  
ANISOU 1986  C   ARG A 322     3234   5486   7551    381   -401   -174       C  
ATOM   1987  O   ARG A 322      14.167  -8.533  94.060  1.00 52.93           O  
ANISOU 1987  O   ARG A 322     4408   6867   8835    471   -514   -242       O  
ATOM   1988  CB  ARG A 322      17.006  -7.167  94.777  1.00 45.56           C  
ANISOU 1988  CB  ARG A 322     3874   5640   7796    446   -399     10       C  
ATOM   1989  CG  ARG A 322      17.638  -5.795  94.943  1.00 45.96           C  
ANISOU 1989  CG  ARG A 322     4020   5630   7810    521   -389     68       C  
ATOM   1990  CD  ARG A 322      16.961  -4.787  94.025  1.00 53.19           C  
ANISOU 1990  CD  ARG A 322     4920   6625   8666    733   -492     43       C  
ATOM   1991  NE  ARG A 322      17.341  -3.410  94.324  1.00 64.89           N  
ANISOU 1991  NE  ARG A 322     6495   8054  10107    835   -465     87       N  
ATOM   1992  CZ  ARG A 322      16.874  -2.349  93.673  1.00 66.94           C  
ANISOU 1992  CZ  ARG A 322     6804   8327  10304   1074   -539     91       C  
ATOM   1993  NH1 ARG A 322      16.006  -2.503  92.682  1.00 64.80           N  
ANISOU 1993  NH1 ARG A 322     6487   8133   9999   1235   -664     60       N  
ATOM   1994  NH2 ARG A 322      17.270  -1.131  94.016  1.00 68.50           N  
ANISOU 1994  NH2 ARG A 322     7104   8415  10508   1163   -500    129       N  
ATOM   1995  N   VAL A 323      15.165  -9.687  95.705  1.00 38.33           N  
ANISOU 1995  N   VAL A 323     2681   4870   7014    235   -298   -170       N  
ATOM   1996  CA  VAL A 323      14.604 -10.967  95.291  1.00 37.78           C  
ANISOU 1996  CA  VAL A 323     2512   4857   6984    146   -290   -245       C  
ATOM   1997  C   VAL A 323      13.323 -11.303  96.045  1.00 43.56           C  
ANISOU 1997  C   VAL A 323     3051   5687   7813     69   -206   -377       C  
ATOM   1998  O   VAL A 323      12.409 -11.900  95.476  1.00 45.50           O  
ANISOU 1998  O   VAL A 323     3136   6030   8124     30   -239   -494       O  
ATOM   1999  CB  VAL A 323      15.652 -12.088  95.456  1.00 38.02           C  
ANISOU 1999  CB  VAL A 323     2684   4774   6986     43   -219   -163       C  
ATOM   2000  CG1 VAL A 323      15.092 -13.414  94.963  1.00 34.88           C  
ANISOU 2000  CG1 VAL A 323     2196   4437   6621    -60   -201   -239       C  
ATOM   2001  CG2 VAL A 323      16.927 -11.736  94.709  1.00 38.26           C  
ANISOU 2001  CG2 VAL A 323     2880   4701   6957    106   -281    -50       C  
ATOM   2002  N   PHE A 324      13.240 -10.944  97.324  1.00 44.23           N  
ANISOU 2002  N   PHE A 324     3141   5740   7924     33    -87   -373       N  
ATOM   2003  CA  PHE A 324      12.083 -11.277  98.143  1.00 48.81           C  
ANISOU 2003  CA  PHE A 324     3548   6385   8612    -65     43   -506       C  
ATOM   2004  C   PHE A 324      11.168 -10.086  98.406  1.00 61.27           C  
ANISOU 2004  C   PHE A 324     4975   8046  10257     44     20   -589       C  
ATOM   2005  O   PHE A 324      10.206 -10.217  99.169  1.00 69.56           O  
ANISOU 2005  O   PHE A 324     5872   9138  11420    -34    151   -715       O  
ATOM   2006  CB  PHE A 324      12.544 -11.908  99.459  1.00 43.20           C  
ANISOU 2006  CB  PHE A 324     2950   5574   7889   -200    230   -459       C  
ATOM   2007  CG  PHE A 324      13.188 -13.254  99.283  1.00 51.31           C  
ANISOU 2007  CG  PHE A 324     4087   6536   8872   -314    275   -410       C  
ATOM   2008  CD1 PHE A 324      12.410 -14.398  99.185  1.00 53.61           C  
ANISOU 2008  CD1 PHE A 324     4278   6856   9236   -473    382   -526       C  
ATOM   2009  CD2 PHE A 324      14.565 -13.378  99.198  1.00 50.64           C  
ANISOU 2009  CD2 PHE A 324     4197   6349   8696   -266    217   -264       C  
ATOM   2010  CE1 PHE A 324      12.991 -15.638  99.010  1.00 55.32           C  
ANISOU 2010  CE1 PHE A 324     4596   6977   9445   -580    439   -493       C  
ATOM   2011  CE2 PHE A 324      15.154 -14.619  99.026  1.00 48.46           C  
ANISOU 2011  CE2 PHE A 324     4000   5989   8422   -349    259   -228       C  
ATOM   2012  CZ  PHE A 324      14.365 -15.750  98.931  1.00 51.15           C  
ANISOU 2012  CZ  PHE A 324     4253   6343   8840   -507    374   -338       C  
ATOM   2013  N   GLY A 325      11.447  -8.932  97.802  1.00 57.72           N  
ANISOU 2013  N   GLY A 325     4571   7613   9746    222   -125   -528       N  
ATOM   2014  CA  GLY A 325      10.548  -7.791  97.898  1.00 62.27           C  
ANISOU 2014  CA  GLY A 325     5002   8277  10379    364   -170   -605       C  
ATOM   2015  C   GLY A 325      10.325  -7.258  99.296  1.00 60.20           C  
ANISOU 2015  C   GLY A 325     4724   7987  10161    332    -12   -616       C  
ATOM   2016  O   GLY A 325       9.243  -6.735  99.584  1.00 64.14           O  
ANISOU 2016  O   GLY A 325     5032   8571  10767    394     14   -740       O  
ATOM   2017  N   MET A 326      11.311  -7.393 100.183  1.00 54.96           N  
ANISOU 2017  N   MET A 326     4250   7204   9430    244     93   -503       N  
ATOM   2018  CA  MET A 326      11.192  -6.909 101.553  1.00 54.49           C  
ANISOU 2018  CA  MET A 326     4202   7102   9398    212    247   -505       C  
ATOM   2019  C   MET A 326      11.538  -5.420 101.655  1.00 61.21           C  
ANISOU 2019  C   MET A 326     5127   7942  10189    377    179   -433       C  
ATOM   2020  O   MET A 326      12.023  -4.792 100.711  1.00 63.52           O  
ANISOU 2020  O   MET A 326     5495   8236  10404    502     29   -368       O  
ATOM   2021  CB  MET A 326      12.082  -7.719 102.497  1.00 56.72           C  
ANISOU 2021  CB  MET A 326     4652   7255   9643     64    376   -424       C  
ATOM   2022  CG  MET A 326      11.598  -9.139 102.766  1.00 66.74           C  
ANISOU 2022  CG  MET A 326     5855   8496  11009   -117    527   -519       C  
ATOM   2023  SD  MET A 326      12.440  -9.900 104.175  1.00 77.93           S  
ANISOU 2023  SD  MET A 326     7442   9684  12486   -265    745   -464       S  
ATOM   2024  CE  MET A 326      12.041 -11.631 103.939  1.00 85.27           C  
ANISOU 2024  CE  MET A 326     8350  10587  13463   -460    884   -557       C  
ATOM   2025  N   PHE A 327      11.274  -4.864 102.838  1.00 65.34           N  
ANISOU 2025  N   PHE A 327     5634   8436  10755    370    316   -454       N  
ATOM   2026  CA  PHE A 327      11.597  -3.477 103.182  1.00 64.46           C  
ANISOU 2026  CA  PHE A 327     5596   8282  10615    507    294   -400       C  
ATOM   2027  C   PHE A 327      10.871  -2.463 102.302  1.00 68.58           C  
ANISOU 2027  C   PHE A 327     6018   8933  11106    729    167   -435       C  
ATOM   2028  O   PHE A 327      11.408  -1.394 102.002  1.00 65.01           O  
ANISOU 2028  O   PHE A 327     5688   8445  10566    875     88   -356       O  
ATOM   2029  CB  PHE A 327      13.106  -3.213 103.127  1.00 49.27           C  
ANISOU 2029  CB  PHE A 327     3902   6231   8587    496    225   -252       C  
ATOM   2030  CG  PHE A 327      13.954  -4.373 103.568  1.00 47.46           C  
ANISOU 2030  CG  PHE A 327     3774   5893   8365    330    277   -196       C  
ATOM   2031  CD1 PHE A 327      13.874  -4.853 104.863  1.00 49.44           C  
ANISOU 2031  CD1 PHE A 327     4011   6034   8741    219    455   -222       C  
ATOM   2032  CD2 PHE A 327      14.870  -4.949 102.700  1.00 50.83           C  
ANISOU 2032  CD2 PHE A 327     4318   6309   8686    305    167   -120       C  
ATOM   2033  CE1 PHE A 327      14.664  -5.908 105.277  1.00 58.58           C  
ANISOU 2033  CE1 PHE A 327     5261   7079   9917    107    501   -164       C  
ATOM   2034  CE2 PHE A 327      15.668  -6.005 103.109  1.00 52.95           C  
ANISOU 2034  CE2 PHE A 327     4673   6479   8968    192    203    -68       C  
ATOM   2035  CZ  PHE A 327      15.564  -6.484 104.401  1.00 56.38           C  
ANISOU 2035  CZ  PHE A 327     5083   6809   9530    106    357    -84       C  
ATOM   2036  N   ARG A 328       9.653  -2.777 101.864  1.00 74.09           N  
ANISOU 2036  N   ARG A 328     6487   9750  11915    765    146   -570       N  
ATOM   2037  CA  ARG A 328       8.875  -1.789 101.127  1.00 82.74           C  
ANISOU 2037  CA  ARG A 328     7466  10943  13029   1013     18   -618       C  
ATOM   2038  C   ARG A 328       8.064  -0.884 102.043  1.00 95.36           C  
ANISOU 2038  C   ARG A 328     8953  12575  14704   1121    133   -691       C  
ATOM   2039  O   ARG A 328       7.806   0.273 101.688  1.00103.40           O  
ANISOU 2039  O   ARG A 328     9982  13620  15685   1372     48   -667       O  
ATOM   2040  CB  ARG A 328       7.949  -2.484 100.121  1.00 86.88           C  
ANISOU 2040  CB  ARG A 328     7775  11576  13658   1030   -101   -754       C  
ATOM   2041  CG  ARG A 328       8.668  -2.995  98.880  1.00 86.53           C  
ANISOU 2041  CG  ARG A 328     7856  11511  13513   1028   -262   -673       C  
ATOM   2042  CD  ARG A 328       7.840  -4.038  98.145  1.00 99.72           C  
ANISOU 2042  CD  ARG A 328     9320  13270  15299    962   -338   -827       C  
ATOM   2043  NE  ARG A 328       8.528  -4.578  96.975  1.00108.26           N  
ANISOU 2043  NE  ARG A 328    10529  14324  16280    957   -477   -751       N  
ATOM   2044  CZ  ARG A 328       8.146  -5.680  96.337  1.00115.66           C  
ANISOU 2044  CZ  ARG A 328    11353  15309  17284    857   -529   -854       C  
ATOM   2045  NH1 ARG A 328       8.820  -6.114  95.280  1.00115.17           N  
ANISOU 2045  NH1 ARG A 328    11423  15214  17122    865   -646   -774       N  
ATOM   2046  NH2 ARG A 328       7.086  -6.353  96.763  1.00119.30           N  
ANISOU 2046  NH2 ARG A 328    11565  15846  17918    741   -448  -1050       N  
ATOM   2047  N   GLN A 329       7.661  -1.384 103.211  1.00 96.64           N  
ANISOU 2047  N   GLN A 329     9021  12701  14997    946    343   -791       N  
ATOM   2048  CA  GLN A 329       6.885  -0.586 104.152  1.00105.72           C  
ANISOU 2048  CA  GLN A 329    10051  13845  16271   1024    492   -899       C  
ATOM   2049  C   GLN A 329       7.724   0.534 104.759  1.00106.04           C  
ANISOU 2049  C   GLN A 329    10309  13758  16224   1125    526   -778       C  
ATOM   2050  O   GLN A 329       8.896   0.347 105.100  1.00100.58           O  
ANISOU 2050  O   GLN A 329     9829  12930  15458   1003    547   -657       O  
ATOM   2051  CB  GLN A 329       6.308  -1.478 105.253  1.00114.27           C  
ANISOU 2051  CB  GLN A 329    11011  14877  17531    777    760  -1054       C  
ATOM   2052  CG  GLN A 329       5.171  -2.390 104.793  1.00125.35           C  
ANISOU 2052  CG  GLN A 329    12142  16405  19082    688    772  -1250       C  
ATOM   2053  CD  GLN A 329       5.613  -3.467 103.823  1.00133.65           C  
ANISOU 2053  CD  GLN A 329    13245  17486  20051    588    628  -1190       C  
ATOM   2054  OE1 GLN A 329       5.041  -3.614 102.743  1.00136.58           O  
ANISOU 2054  OE1 GLN A 329    13455  17979  20461    679    451  -1269       O  
ATOM   2055  NE2 GLN A 329       6.627  -4.232 104.206  1.00136.39           N  
ANISOU 2055  NE2 GLN A 329    13808  17700  20313    409    705  -1074       N  
ATOM   2056  N   ALA A 330       7.108   1.710 104.882  1.00113.54           N  
ANISOU 2056  N   ALA A 330    11200  14741  17200   1361    529   -822       N  
ATOM   2057  CA  ALA A 330       7.751   2.921 105.377  1.00118.08           C  
ANISOU 2057  CA  ALA A 330    11979  15188  17696   1499    561   -731       C  
ATOM   2058  C   ALA A 330       7.699   3.086 106.894  1.00115.17           C  
ANISOU 2058  C   ALA A 330    11627  14684  17446   1376    831   -793       C  
ATOM   2059  O   ALA A 330       8.195   4.097 107.400  1.00111.10           O  
ANISOU 2059  O   ALA A 330    11286  14039  16890   1481    881   -732       O  
ATOM   2060  CB  ALA A 330       7.122   4.154 104.717  1.00124.86           C  
ANISOU 2060  CB  ALA A 330    12819  16117  18506   1858    444   -733       C  
ATOM   2061  N   SER A 331       7.119   2.144 107.639  1.00115.57           N  
ANISOU 2061  N   SER A 331    11534  14730  17648   1155   1035   -918       N  
ATOM   2062  CA  SER A 331       7.046   2.321 109.089  1.00115.96           C  
ANISOU 2062  CA  SER A 331    11641  14613  17806   1038   1345   -976       C  
ATOM   2063  C   SER A 331       8.409   2.131 109.747  1.00110.36           C  
ANISOU 2063  C   SER A 331    11204  13683  17045    886   1420   -822       C  
ATOM   2064  O   SER A 331       8.821   2.937 110.589  1.00111.78           O  
ANISOU 2064  O   SER A 331    11546  13698  17227    927   1562   -775       O  
ATOM   2065  CB  SER A 331       6.022   1.357 109.684  1.00119.67           C  
ANISOU 2065  CB  SER A 331    11917  15105  18449    831   1593  -1170       C  
ATOM   2066  OG  SER A 331       6.429   0.012 109.507  1.00118.81           O  
ANISOU 2066  OG  SER A 331    11842  14965  18334    597   1596  -1146       O  
ATOM   2067  N   ASP A 332       9.112   1.064 109.389  1.00104.55           N  
ANISOU 2067  N   ASP A 332    10522  12933  16270    723   1335   -744       N  
ATOM   2068  CA  ASP A 332      10.453   0.769 109.878  1.00 97.88           C  
ANISOU 2068  CA  ASP A 332     9899  11901  15388    606   1364   -595       C  
ATOM   2069  C   ASP A 332      11.553   1.475 109.079  1.00 83.50           C  
ANISOU 2069  C   ASP A 332     8211  10076  13438    732   1096   -437       C  
ATOM   2070  O   ASP A 332      12.691   0.991 109.061  1.00 77.51           O  
ANISOU 2070  O   ASP A 332     7575   9230  12645    635   1026   -320       O  
ATOM   2071  CB  ASP A 332      10.675  -0.743 109.900  1.00106.12           C  
ANISOU 2071  CB  ASP A 332    10946  12922  16452    392   1415   -597       C  
ATOM   2072  CG  ASP A 332      10.354  -1.394 108.574  1.00115.19           C  
ANISOU 2072  CG  ASP A 332    11967  14268  17533    407   1178   -618       C  
ATOM   2073  OD1 ASP A 332       9.701  -0.742 107.730  1.00119.40           O  
ANISOU 2073  OD1 ASP A 332    12374  14966  18028    577   1022   -663       O  
ATOM   2074  OD2 ASP A 332      10.752  -2.561 108.381  1.00116.79           O  
ANISOU 2074  OD2 ASP A 332    12211  14448  17716    265   1166   -589       O  
ATOM   2075  N   ARG A 333      11.222   2.592 108.423  1.00 74.78           N  
ANISOU 2075  N   ARG A 333     7092   9055  12265    951    965   -445       N  
ATOM   2076  CA  ARG A 333      12.157   3.272 107.529  1.00 72.31           C  
ANISOU 2076  CA  ARG A 333     6927   8724  11822   1062    753   -324       C  
ATOM   2077  C   ARG A 333      13.537   3.464 108.156  1.00 69.10           C  
ANISOU 2077  C   ARG A 333     6709   8114  11431    960    793   -200       C  
ATOM   2078  O   ARG A 333      14.554   3.094 107.562  1.00 67.65           O  
ANISOU 2078  O   ARG A 333     6600   7916  11188    883    651   -108       O  
ATOM   2079  CB  ARG A 333      11.571   4.629 107.128  1.00 78.75           C  
ANISOU 2079  CB  ARG A 333     7766   9576  12579   1342    702   -361       C  
ATOM   2080  CG  ARG A 333      12.292   5.330 105.987  1.00 83.26           C  
ANISOU 2080  CG  ARG A 333     8503  10125  13007   1488    510   -267       C  
ATOM   2081  CD  ARG A 333      11.550   6.590 105.548  1.00 98.47           C  
ANISOU 2081  CD  ARG A 333    10484  12076  14854   1821    463   -313       C  
ATOM   2082  NE  ARG A 333      11.552   7.635 106.569  1.00113.05           N  
ANISOU 2082  NE  ARG A 333    12459  13752  16741   1900    622   -328       N  
ATOM   2083  CZ  ARG A 333      12.302   8.731 106.516  1.00119.25           C  
ANISOU 2083  CZ  ARG A 333    13521  14333  17453   2001    622   -257       C  
ATOM   2084  NH1 ARG A 333      13.119   8.928 105.491  1.00122.20           N  
ANISOU 2084  NH1 ARG A 333    14061  14644  17724   2031    484   -173       N  
ATOM   2085  NH2 ARG A 333      12.235   9.630 107.489  1.00116.40           N  
ANISOU 2085  NH2 ARG A 333    13300  13805  17121   2058    790   -275       N  
ATOM   2086  N   GLU A 334      13.600   4.036 109.363  1.00 65.37           N  
ANISOU 2086  N   GLU A 334     6318   7478  11042    964    997   -206       N  
ATOM   2087  CA  GLU A 334      14.906   4.330 109.951  1.00 55.52           C  
ANISOU 2087  CA  GLU A 334     5247   6033   9814    907   1021   -103       C  
ATOM   2088  C   GLU A 334      15.675   3.060 110.290  1.00 53.03           C  
ANISOU 2088  C   GLU A 334     4912   5687   9550    730   1007    -56       C  
ATOM   2089  O   GLU A 334      16.898   3.009 110.118  1.00 59.58           O  
ANISOU 2089  O   GLU A 334     5813   6455  10370    687    866     26       O  
ATOM   2090  CB  GLU A 334      14.748   5.217 111.186  1.00 56.59           C  
ANISOU 2090  CB  GLU A 334     5536   5971   9995    976   1268   -136       C  
ATOM   2091  CG  GLU A 334      14.377   6.652 110.868  1.00 59.84           C  
ANISOU 2091  CG  GLU A 334     6054   6351  10330   1174   1257   -151       C  
ATOM   2092  CD  GLU A 334      15.428   7.346 110.011  1.00 66.71           C  
ANISOU 2092  CD  GLU A 334     7070   7156  11122   1216   1074    -58       C  
ATOM   2093  OE1 GLU A 334      16.624   7.000 110.126  1.00 69.16           O  
ANISOU 2093  OE1 GLU A 334     7441   7370  11467   1082   1013      7       O  
ATOM   2094  OE2 GLU A 334      15.061   8.243 109.223  1.00 67.80           O  
ANISOU 2094  OE2 GLU A 334     7273   7322  11167   1394   1000    -65       O  
ATOM   2095  N   ALA A 335      14.988   2.024 110.775  1.00 54.61           N  
ANISOU 2095  N   ALA A 335     5020   5918   9810    630   1160   -122       N  
ATOM   2096  CA  ALA A 335      15.687   0.778 111.071  1.00 55.27           C  
ANISOU 2096  CA  ALA A 335     5112   5955   9933    496   1160    -75       C  
ATOM   2097  C   ALA A 335      16.252   0.154 109.802  1.00 54.13           C  
ANISOU 2097  C   ALA A 335     4930   5950   9685    450    867    -13       C  
ATOM   2098  O   ALA A 335      17.335  -0.443 109.823  1.00 54.93           O  
ANISOU 2098  O   ALA A 335     5078   6007   9788    393    753     62       O  
ATOM   2099  CB  ALA A 335      14.754  -0.198 111.783  1.00 50.87           C  
ANISOU 2099  CB  ALA A 335     4524   5376   9427    370   1444   -174       C  
ATOM   2100  N   VAL A 336      15.532   0.279 108.685  1.00 53.16           N  
ANISOU 2100  N   VAL A 336     4739   5992   9466    499    753    -57       N  
ATOM   2101  CA  VAL A 336      16.039  -0.238 107.419  1.00 49.12           C  
ANISOU 2101  CA  VAL A 336     4251   5584   8827    476    538    -11       C  
ATOM   2102  C   VAL A 336      17.254   0.564 106.970  1.00 49.35           C  
ANISOU 2102  C   VAL A 336     4395   5555   8802    509    407     75       C  
ATOM   2103  O   VAL A 336      18.243   0.001 106.490  1.00 48.83           O  
ANISOU 2103  O   VAL A 336     4386   5485   8681    435    295    128       O  
ATOM   2104  CB  VAL A 336      14.929  -0.245 106.353  1.00 56.77           C  
ANISOU 2104  CB  VAL A 336     5121   6730   9720    557    473    -92       C  
ATOM   2105  CG1 VAL A 336      15.511  -0.583 104.994  1.00 61.45           C  
ANISOU 2105  CG1 VAL A 336     5775   7396  10176    561    292    -41       C  
ATOM   2106  CG2 VAL A 336      13.843  -1.236 106.736  1.00 54.31           C  
ANISOU 2106  CG2 VAL A 336     4669   6481   9486    476    604   -200       C  
ATOM   2107  N   TYR A 337      17.199   1.892 107.117  1.00 50.45           N  
ANISOU 2107  N   TYR A 337     4572   5633   8965    619    444     75       N  
ATOM   2108  CA  TYR A 337      18.355   2.720 106.786  1.00 42.77           C  
ANISOU 2108  CA  TYR A 337     3699   4563   7988    629    373    135       C  
ATOM   2109  C   TYR A 337      19.542   2.387 107.679  1.00 46.82           C  
ANISOU 2109  C   TYR A 337     4231   4964   8594    521    358    168       C  
ATOM   2110  O   TYR A 337      20.688   2.337 107.215  1.00 52.16           O  
ANISOU 2110  O   TYR A 337     4929   5620   9270    452    250    192       O  
ATOM   2111  CB  TYR A 337      18.008   4.200 106.962  1.00 46.90           C  
ANISOU 2111  CB  TYR A 337     4295   4991   8532    785    458    120       C  
ATOM   2112  CG  TYR A 337      17.072   4.818 105.952  1.00 45.46           C  
ANISOU 2112  CG  TYR A 337     4124   4900   8248    966    416     85       C  
ATOM   2113  CD1 TYR A 337      16.841   4.229 104.719  1.00 48.21           C  
ANISOU 2113  CD1 TYR A 337     4430   5388   8498    984    286     78       C  
ATOM   2114  CD2 TYR A 337      16.413   6.006 106.245  1.00 46.27           C  
ANISOU 2114  CD2 TYR A 337     4306   4933   8342   1154    500     50       C  
ATOM   2115  CE1 TYR A 337      15.985   4.813 103.799  1.00 53.60           C  
ANISOU 2115  CE1 TYR A 337     5129   6149   9087   1206    220     36       C  
ATOM   2116  CE2 TYR A 337      15.555   6.594 105.336  1.00 52.12           C  
ANISOU 2116  CE2 TYR A 337     5070   5755   8977   1382    426      6       C  
ATOM   2117  CZ  TYR A 337      15.343   5.996 104.115  1.00 62.35           C  
ANISOU 2117  CZ  TYR A 337     6307   7199  10184   1418    276     -1       C  
ATOM   2118  OH  TYR A 337      14.487   6.587 103.214  1.00 74.75           O  
ANISOU 2118  OH  TYR A 337     7916   8844  11641   1696    185    -47       O  
ATOM   2119  N   ALA A 338      19.284   2.154 108.967  1.00 40.74           N  
ANISOU 2119  N   ALA A 338     3447   4111   7923    523    474    149       N  
ATOM   2120  CA  ALA A 338      20.356   1.798 109.890  1.00 45.09           C  
ANISOU 2120  CA  ALA A 338     4114   4567   8451    432    398    161       C  
ATOM   2121  C   ALA A 338      20.990   0.461 109.530  1.00 52.29           C  
ANISOU 2121  C   ALA A 338     4924   5550   9394    368    258    190       C  
ATOM   2122  O   ALA A 338      22.209   0.290 109.655  1.00 52.81           O  
ANISOU 2122  O   ALA A 338     5043   5598   9425    312     88    186       O  
ATOM   2123  CB  ALA A 338      19.821   1.766 111.320  1.00 49.69           C  
ANISOU 2123  CB  ALA A 338     4925   5050   8906    396    544    131       C  
ATOM   2124  N   ALA A 339      20.179  -0.503 109.085  1.00 49.30           N  
ANISOU 2124  N   ALA A 339     4474   5265   8991    346    315    193       N  
ATOM   2125  CA  ALA A 339      20.718  -1.813 108.731  1.00 40.29           C  
ANISOU 2125  CA  ALA A 339     3339   4173   7797    278    204    219       C  
ATOM   2126  C   ALA A 339      21.584  -1.736 107.481  1.00 46.19           C  
ANISOU 2126  C   ALA A 339     4145   4998   8407    245     55    228       C  
ATOM   2127  O   ALA A 339      22.708  -2.250 107.461  1.00 56.14           O  
ANISOU 2127  O   ALA A 339     5427   6251   9653    213    -70    232       O  
ATOM   2128  CB  ALA A 339      19.575  -2.814 108.542  1.00 37.99           C  
ANISOU 2128  CB  ALA A 339     3003   3937   7493    243    332    195       C  
ATOM   2129  N   PHE A 340      21.082  -1.084 106.428  1.00 44.19           N  
ANISOU 2129  N   PHE A 340     3911   4808   8071    273     79    218       N  
ATOM   2130  CA  PHE A 340      21.876  -0.943 105.212  1.00 43.62           C  
ANISOU 2130  CA  PHE A 340     3891   4763   7921    252      2    226       C  
ATOM   2131  C   PHE A 340      23.100  -0.065 105.442  1.00 48.28           C  
ANISOU 2131  C   PHE A 340     4475   5260   8607    224    -36    213       C  
ATOM   2132  O   PHE A 340      24.158  -0.302 104.848  1.00 56.96           O  
ANISOU 2132  O   PHE A 340     5589   6356   9696    174    -94    198       O  
ATOM   2133  CB  PHE A 340      21.022  -0.376 104.080  1.00 42.87           C  
ANISOU 2133  CB  PHE A 340     3800   4726   7763    322     30    220       C  
ATOM   2134  CG  PHE A 340      20.210  -1.407 103.358  1.00 47.35           C  
ANISOU 2134  CG  PHE A 340     4356   5406   8230    329     13    201       C  
ATOM   2135  CD1 PHE A 340      18.896  -1.653 103.717  1.00 49.98           C  
ANISOU 2135  CD1 PHE A 340     4609   5810   8571    368     67    154       C  
ATOM   2136  CD2 PHE A 340      20.760  -2.123 102.310  1.00 46.73           C  
ANISOU 2136  CD2 PHE A 340     4323   5354   8076    294    -42    215       C  
ATOM   2137  CE1 PHE A 340      18.148  -2.600 103.044  1.00 48.49           C  
ANISOU 2137  CE1 PHE A 340     4375   5727   8322    363     51    114       C  
ATOM   2138  CE2 PHE A 340      20.020  -3.071 101.635  1.00 48.83           C  
ANISOU 2138  CE2 PHE A 340     4567   5715   8270    300    -57    191       C  
ATOM   2139  CZ  PHE A 340      18.711  -3.310 102.001  1.00 53.49           C  
ANISOU 2139  CZ  PHE A 340     5065   6384   8874    331    -18    137       C  
ATOM   2140  N   THR A 341      22.978   0.952 106.301  1.00 49.23           N  
ANISOU 2140  N   THR A 341     4561   5297   8848    257     11    200       N  
ATOM   2141  CA  THR A 341      24.115   1.828 106.566  1.00 40.64           C  
ANISOU 2141  CA  THR A 341     3431   4109   7901    216    -21    153       C  
ATOM   2142  C   THR A 341      25.254   1.053 107.210  1.00 47.33           C  
ANISOU 2142  C   THR A 341     4239   4975   8768    149   -174     99       C  
ATOM   2143  O   THR A 341      26.409   1.149 106.778  1.00 47.13           O  
ANISOU 2143  O   THR A 341     4182   4951   8773     81   -235     30       O  
ATOM   2144  CB  THR A 341      23.698   2.998 107.458  1.00 39.10           C  
ANISOU 2144  CB  THR A 341     3223   3793   7839    292     73    136       C  
ATOM   2145  OG1 THR A 341      22.660   3.749 106.819  1.00 45.04           O  
ANISOU 2145  OG1 THR A 341     4053   4530   8532    402    200    172       O  
ATOM   2146  CG2 THR A 341      24.889   3.905 107.722  1.00 37.49           C  
ANISOU 2146  CG2 THR A 341     3117   3500   7627    164     45     44       C  
ATOM   2147  N   PHE A 342      24.950   0.277 108.254  1.00 49.39           N  
ANISOU 2147  N   PHE A 342     4494   5241   9029    186   -235    115       N  
ATOM   2148  CA  PHE A 342      25.994  -0.513 108.897  1.00 51.30           C  
ANISOU 2148  CA  PHE A 342     4711   5495   9288    176   -438     61       C  
ATOM   2149  C   PHE A 342      26.577  -1.536 107.930  1.00 54.18           C  
ANISOU 2149  C   PHE A 342     5117   5952   9517    149   -470     64       C  
ATOM   2150  O   PHE A 342      27.775  -1.834 107.981  1.00 55.11           O  
ANISOU 2150  O   PHE A 342     5202   6098   9639    138   -609    -19       O  
ATOM   2151  CB  PHE A 342      25.447  -1.206 110.146  1.00 52.45           C  
ANISOU 2151  CB  PHE A 342     5011   5578   9340    239   -468     93       C  
ATOM   2152  CG  PHE A 342      26.416  -2.170 110.779  1.00 54.05           C  
ANISOU 2152  CG  PHE A 342     5295   5775   9467    283   -711     46       C  
ATOM   2153  CD1 PHE A 342      27.488  -1.710 111.528  1.00 55.98           C  
ANISOU 2153  CD1 PHE A 342     5609   5996   9666    282   -928    -78       C  
ATOM   2154  CD2 PHE A 342      26.260  -3.539 110.616  1.00 49.09           C  
ANISOU 2154  CD2 PHE A 342     4684   5160   8807    340   -739    108       C  
ATOM   2155  CE1 PHE A 342      28.381  -2.595 112.109  1.00 57.43           C  
ANISOU 2155  CE1 PHE A 342     5866   6180   9773    380  -1205   -144       C  
ATOM   2156  CE2 PHE A 342      27.150  -4.428 111.193  1.00 55.70           C  
ANISOU 2156  CE2 PHE A 342     5642   5972   9550    432   -981     64       C  
ATOM   2157  CZ  PHE A 342      28.211  -3.955 111.941  1.00 59.79           C  
ANISOU 2157  CZ  PHE A 342     6217   6478  10022    473  -1233    -64       C  
ATOM   2158  N   SER A 343      25.741  -2.098 107.052  1.00 52.25           N  
ANISOU 2158  N   SER A 343     4936   5758   9160    151   -349    139       N  
ATOM   2159  CA  SER A 343      26.244  -3.063 106.079  1.00 44.92           C  
ANISOU 2159  CA  SER A 343     4048   4896   8122    136   -366    142       C  
ATOM   2160  C   SER A 343      27.123  -2.394 105.031  1.00 55.06           C  
ANISOU 2160  C   SER A 343     5323   6182   9416     96   -338     94       C  
ATOM   2161  O   SER A 343      28.107  -2.986 104.571  1.00 57.01           O  
ANISOU 2161  O   SER A 343     5555   6464   9641     85   -383     51       O  
ATOM   2162  CB  SER A 343      25.080  -3.789 105.404  1.00 44.26           C  
ANISOU 2162  CB  SER A 343     4018   4857   7942    143   -268    207       C  
ATOM   2163  OG  SER A 343      24.178  -4.318 106.359  1.00 44.50           O  
ANISOU 2163  OG  SER A 343     4022   4859   8027    165   -239    239       O  
ATOM   2164  N   HIS A 344      26.783  -1.163 104.633  1.00 59.39           N  
ANISOU 2164  N   HIS A 344     5862   6673  10030     82   -248     97       N  
ATOM   2165  CA  HIS A 344      27.641  -0.432 103.706  1.00 55.18           C  
ANISOU 2165  CA  HIS A 344     5295   6088   9583     38   -194     45       C  
ATOM   2166  C   HIS A 344      29.003  -0.171 104.330  1.00 60.82           C  
ANISOU 2166  C   HIS A 344     5909   6800  10398    -16   -269    -86       C  
ATOM   2167  O   HIS A 344      30.041  -0.346 103.682  1.00 61.14           O  
ANISOU 2167  O   HIS A 344     5904   6861  10466    -55   -256   -162       O  
ATOM   2168  CB  HIS A 344      26.993   0.897 103.309  1.00 55.09           C  
ANISOU 2168  CB  HIS A 344     5276   5974   9683     46    -76     72       C  
ATOM   2169  CG  HIS A 344      25.735   0.759 102.508  1.00 50.98           C  
ANISOU 2169  CG  HIS A 344     4823   5480   9067    116    -27    165       C  
ATOM   2170  ND1 HIS A 344      24.717   1.690 102.535  1.00 51.50           N  
ANISOU 2170  ND1 HIS A 344     4944   5628   8998    127    -55    199       N  
ATOM   2171  CD2 HIS A 344      25.329  -0.215 101.658  1.00 45.63           C  
ANISOU 2171  CD2 HIS A 344     4155   4777   8404    195     35    208       C  
ATOM   2172  CE1 HIS A 344      23.742   1.296 101.734  1.00 50.07           C  
ANISOU 2172  CE1 HIS A 344     4787   5482   8754    196    -31    243       C  
ATOM   2173  NE2 HIS A 344      24.089   0.144 101.190  1.00 48.69           N  
ANISOU 2173  NE2 HIS A 344     4590   5256   8655    253     17    247       N  
ATOM   2174  N   TRP A 345      29.013   0.240 105.598  1.00 62.02           N  
ANISOU 2174  N   TRP A 345     6011   6934  10618    -21   -355   -134       N  
ATOM   2175  CA  TRP A 345      30.269   0.495 106.290  1.00 60.87           C  
ANISOU 2175  CA  TRP A 345     5756   6808  10565    -76   -476   -296       C  
ATOM   2176  C   TRP A 345      31.088  -0.780 106.449  1.00 62.43           C  
ANISOU 2176  C   TRP A 345     5929   7103  10687    -23   -627   -339       C  
ATOM   2177  O   TRP A 345      32.321  -0.751 106.343  1.00 59.61           O  
ANISOU 2177  O   TRP A 345     5466   6793  10388    -60   -679   -483       O  
ATOM   2178  CB  TRP A 345      29.984   1.131 107.648  1.00 56.79           C  
ANISOU 2178  CB  TRP A 345     5203   6237  10138    -87   -582   -343       C  
ATOM   2179  CG  TRP A 345      31.208   1.372 108.433  1.00 51.63           C  
ANISOU 2179  CG  TRP A 345     4448   5613   9556   -146   -765   -543       C  
ATOM   2180  CD1 TRP A 345      32.054   2.433 108.325  1.00 47.10           C  
ANISOU 2180  CD1 TRP A 345     3795   5019   9080   -290   -707   -713       C  
ATOM   2181  CD2 TRP A 345      31.751   0.521 109.444  1.00 49.59           C  
ANISOU 2181  CD2 TRP A 345     4169   5410   9263    -55  -1050   -620       C  
ATOM   2182  NE1 TRP A 345      33.089   2.303 109.218  1.00 49.80           N  
ANISOU 2182  NE1 TRP A 345     4048   5427   9446   -300   -945   -904       N  
ATOM   2183  CE2 TRP A 345      32.926   1.135 109.917  1.00 48.98           C  
ANISOU 2183  CE2 TRP A 345     3985   5365   9261   -134  -1183   -849       C  
ATOM   2184  CE3 TRP A 345      31.355  -0.698 109.999  1.00 49.22           C  
ANISOU 2184  CE3 TRP A 345     4203   5376   9124     92  -1210   -529       C  
ATOM   2185  CZ2 TRP A 345      33.709   0.572 110.918  1.00 45.47           C  
ANISOU 2185  CZ2 TRP A 345     3514   4975   8788    -36  -1510   -993       C  
ATOM   2186  CZ3 TRP A 345      32.132  -1.256 110.992  1.00 43.59           C  
ANISOU 2186  CZ3 TRP A 345     3493   4687   8382    197  -1534   -657       C  
ATOM   2187  CH2 TRP A 345      33.297  -0.622 111.443  1.00 43.26           C  
ANISOU 2187  CH2 TRP A 345     3348   4688   8400    148  -1699   -890       C  
ATOM   2188  N   LEU A 346      30.425  -1.912 106.700  1.00 61.62           N  
ANISOU 2188  N   LEU A 346     5911   7027  10474     62   -682   -230       N  
ATOM   2189  CA  LEU A 346      31.158  -3.160 106.888  1.00 61.43           C  
ANISOU 2189  CA  LEU A 346     5873   7072  10398    130   -825   -267       C  
ATOM   2190  C   LEU A 346      31.946  -3.535 105.639  1.00 60.17           C  
ANISOU 2190  C   LEU A 346     5677   6966  10218    100   -731   -297       C  
ATOM   2191  O   LEU A 346      33.047  -4.087 105.733  1.00 57.80           O  
ANISOU 2191  O   LEU A 346     5288   6726   9948    135   -840   -401       O  
ATOM   2192  CB  LEU A 346      30.192  -4.285 107.267  1.00 60.22           C  
ANISOU 2192  CB  LEU A 346     5823   6906  10152    208   -855   -141       C  
ATOM   2193  CG  LEU A 346      30.311  -4.749 108.722  1.00 53.19           C  
ANISOU 2193  CG  LEU A 346     4949   5972   9288    323  -1106   -177       C  
ATOM   2194  CD1 LEU A 346      29.314  -5.852 109.044  1.00 54.01           C  
ANISOU 2194  CD1 LEU A 346     5162   6020   9338    403  -1101    -46       C  
ATOM   2195  CD2 LEU A 346      31.733  -5.197 109.027  1.00 50.23           C  
ANISOU 2195  CD2 LEU A 346     4516   5654   8915    401  -1326   -326       C  
ATOM   2196  N   VAL A 347      31.408  -3.237 104.456  1.00 56.39           N  
ANISOU 2196  N   VAL A 347     5261   6458   9705     50   -547   -217       N  
ATOM   2197  CA  VAL A 347      32.142  -3.519 103.226  1.00 56.11           C  
ANISOU 2197  CA  VAL A 347     5195   6441   9684     21   -460   -250       C  
ATOM   2198  C   VAL A 347      33.423  -2.699 103.180  1.00 59.56           C  
ANISOU 2198  C   VAL A 347     5477   6879  10276    -49   -446   -423       C  
ATOM   2199  O   VAL A 347      34.507  -3.216 102.890  1.00 57.72           O  
ANISOU 2199  O   VAL A 347     5137   6699  10094    -48   -475   -523       O  
ATOM   2200  CB  VAL A 347      31.256  -3.247 101.998  1.00 51.43           C  
ANISOU 2200  CB  VAL A 347     4706   5787   9050     -1   -302   -144       C  
ATOM   2201  CG1 VAL A 347      32.111  -3.139 100.752  1.00 46.63           C  
ANISOU 2201  CG1 VAL A 347     4045   5146   8527    -47   -194   -205       C  
ATOM   2202  CG2 VAL A 347      30.213  -4.335 101.852  1.00 49.20           C  
ANISOU 2202  CG2 VAL A 347     4539   5536   8617     50   -316    -23       C  
ATOM   2203  N   TYR A 348      33.313  -1.401 103.462  1.00 57.79           N  
ANISOU 2203  N   TYR A 348     5221   6592  10144   -121   -387   -476       N  
ATOM   2204  CA  TYR A 348      34.482  -0.531 103.454  1.00 47.50           C  
ANISOU 2204  CA  TYR A 348     3765   5287   8997   -228   -341   -672       C  
ATOM   2205  C   TYR A 348      35.445  -0.862 104.585  1.00 51.73           C  
ANISOU 2205  C   TYR A 348     4158   5917   9579   -199   -558   -828       C  
ATOM   2206  O   TYR A 348      36.658  -0.674 104.438  1.00 54.96           O  
ANISOU 2206  O   TYR A 348     4401   6371  10110   -263   -553  -1015       O  
ATOM   2207  CB  TYR A 348      34.026   0.923 103.513  1.00 41.44           C  
ANISOU 2207  CB  TYR A 348     3022   4414   8309   -328   -205   -693       C  
ATOM   2208  CG  TYR A 348      33.175   1.287 102.323  1.00 37.74           C  
ANISOU 2208  CG  TYR A 348     2675   3833   7830   -330     -4   -563       C  
ATOM   2209  CD1 TYR A 348      33.693   1.226 101.036  1.00 36.16           C  
ANISOU 2209  CD1 TYR A 348     2471   3589   7679   -378    161   -596       C  
ATOM   2210  CD2 TYR A 348      31.847   1.654 102.480  1.00 35.31           C  
ANISOU 2210  CD2 TYR A 348     2476   3454   7486   -271     15   -417       C  
ATOM   2211  CE1 TYR A 348      32.920   1.544  99.938  1.00 45.45           C  
ANISOU 2211  CE1 TYR A 348     3759   4642   8866   -364    328   -486       C  
ATOM   2212  CE2 TYR A 348      31.065   1.973 101.388  1.00 39.59           C  
ANISOU 2212  CE2 TYR A 348     3105   3889   8049   -245    168   -309       C  
ATOM   2213  CZ  TYR A 348      31.605   1.916 100.121  1.00 47.08           C  
ANISOU 2213  CZ  TYR A 348     4058   4784   9047   -289    318   -341       C  
ATOM   2214  OH  TYR A 348      30.821   2.236  99.037  1.00 55.79           O  
ANISOU 2214  OH  TYR A 348     5244   5755  10198   -252    465   -234       O  
ATOM   2215  N   ALA A 349      34.929  -1.346 105.717  1.00 51.54           N  
ANISOU 2215  N   ALA A 349     4189   5914   9479    -98   -756   -772       N  
ATOM   2216  CA  ALA A 349      35.807  -1.757 106.808  1.00 54.88           C  
ANISOU 2216  CA  ALA A 349     4501   6411   9941    -24  -1016   -926       C  
ATOM   2217  C   ALA A 349      36.709  -2.909 106.390  1.00 64.23           C  
ANISOU 2217  C   ALA A 349     5604   7677  11123     58  -1083   -977       C  
ATOM   2218  O   ALA A 349      37.818  -3.053 106.918  1.00 73.50           O  
ANISOU 2218  O   ALA A 349     6620   8920  12387    103  -1258  -1170       O  
ATOM   2219  CB  ALA A 349      34.981  -2.148 108.033  1.00 53.02           C  
ANISOU 2219  CB  ALA A 349     4385   6142   9618     90  -1221   -846       C  
ATOM   2220  N   ASN A 350      36.250  -3.739 105.450  1.00 62.56           N  
ANISOU 2220  N   ASN A 350     5492   7458  10818     86   -957   -821       N  
ATOM   2221  CA  ASN A 350      37.070  -4.847 104.974  1.00 57.90           C  
ANISOU 2221  CA  ASN A 350     4828   6934  10239    159  -1001   -864       C  
ATOM   2222  C   ASN A 350      38.367  -4.345 104.353  1.00 60.53           C  
ANISOU 2222  C   ASN A 350     4946   7299  10754     70   -921  -1065       C  
ATOM   2223  O   ASN A 350      39.425  -4.961 104.526  1.00 56.20           O  
ANISOU 2223  O   ASN A 350     4238   6823  10292    145  -1053  -1212       O  
ATOM   2224  CB  ASN A 350      36.279  -5.680 103.964  1.00 54.06           C  
ANISOU 2224  CB  ASN A 350     4492   6420   9628    171   -856   -673       C  
ATOM   2225  CG  ASN A 350      37.040  -6.903 103.487  1.00 58.40           C  
ANISOU 2225  CG  ASN A 350     4971   7012  10208    253   -905   -712       C  
ATOM   2226  OD1 ASN A 350      37.231  -7.863 104.237  1.00 56.11           O  
ANISOU 2226  OD1 ASN A 350     4691   6774   9855    393  -1091   -713       O  
ATOM   2227  ND2 ASN A 350      37.484  -6.873 102.237  1.00 59.15           N  
ANISOU 2227  ND2 ASN A 350     4997   7060  10416    180   -741   -754       N  
ATOM   2228  N   SER A 351      38.311  -3.225 103.626  1.00 66.57           N  
ANISOU 2228  N   SER A 351     5697   8000  11595    -86   -700  -1093       N  
ATOM   2229  CA  SER A 351      39.532  -2.678 103.045  1.00 62.57           C  
ANISOU 2229  CA  SER A 351     4985   7503  11287   -200   -582  -1312       C  
ATOM   2230  C   SER A 351      40.518  -2.247 104.124  1.00 68.41           C  
ANISOU 2230  C   SER A 351     5512   8319  12161   -206   -766  -1562       C  
ATOM   2231  O   SER A 351      41.734  -2.356 103.933  1.00 73.23           O  
ANISOU 2231  O   SER A 351     5895   8986  12942   -228   -776  -1784       O  
ATOM   2232  CB  SER A 351      39.195  -1.507 102.122  1.00 61.38           C  
ANISOU 2232  CB  SER A 351     4901   7236  11185   -367   -292  -1300       C  
ATOM   2233  OG  SER A 351      38.315  -1.916 101.086  1.00 64.69           O  
ANISOU 2233  OG  SER A 351     5506   7581  11493   -338   -157  -1096       O  
ATOM   2234  N   ALA A 352      40.016  -1.779 105.271  1.00 70.66           N  
ANISOU 2234  N   ALA A 352     5857   8606  12386   -180   -925  -1550       N  
ATOM   2235  CA  ALA A 352      40.895  -1.435 106.384  1.00 65.18           C  
ANISOU 2235  CA  ALA A 352     4980   7986  11800   -163  -1155  -1797       C  
ATOM   2236  C   ALA A 352      41.378  -2.668 107.131  1.00 61.95           C  
ANISOU 2236  C   ALA A 352     4522   7659  11355     63  -1475  -1849       C  
ATOM   2237  O   ALA A 352      42.458  -2.640 107.732  1.00 69.08           O  
ANISOU 2237  O   ALA A 352     5216   8643  12387    113  -1675  -2108       O  
ATOM   2238  CB  ALA A 352      40.182  -0.488 107.350  1.00 59.63           C  
ANISOU 2238  CB  ALA A 352     4379   7237  11042   -214  -1227  -1778       C  
ATOM   2239  N   ALA A 353      40.594  -3.746 107.115  1.00 57.57           N  
ANISOU 2239  N   ALA A 353     4163   7081  10629    206  -1532  -1625       N  
ATOM   2240  CA  ALA A 353      40.984  -4.953 107.833  1.00 59.35           C  
ANISOU 2240  CA  ALA A 353     4394   7357  10798    437  -1831  -1665       C  
ATOM   2241  C   ALA A 353      42.178  -5.640 107.184  1.00 69.51           C  
ANISOU 2241  C   ALA A 353     5468   8720  12223    489  -1835  -1818       C  
ATOM   2242  O   ALA A 353      43.087  -6.102 107.885  1.00 78.75           O  
ANISOU 2242  O   ALA A 353     6504   9958  13458    653  -2115  -2018       O  
ATOM   2243  CB  ALA A 353      39.801  -5.916 107.918  1.00 46.42           C  
ANISOU 2243  CB  ALA A 353     3031   5659   8948    548  -1842  -1394       C  
ATOM   2244  N   ASN A 354      42.193  -5.735 105.856  1.00 65.18           N  
ANISOU 2244  N   ASN A 354     4892   8153  11721    372  -1548  -1741       N  
ATOM   2245  CA  ASN A 354      43.214  -6.537 105.180  1.00 63.84           C  
ANISOU 2245  CA  ASN A 354     4539   8039  11680    433  -1542  -1864       C  
ATOM   2246  C   ASN A 354      44.640  -6.141 105.533  1.00 69.28           C  
ANISOU 2246  C   ASN A 354     4897   8812  12614    438  -1672  -2221       C  
ATOM   2247  O   ASN A 354      45.418  -7.021 105.932  1.00 71.18           O  
ANISOU 2247  O   ASN A 354     5012   9125  12910    634  -1914  -2363       O  
ATOM   2248  CB  ASN A 354      43.000  -6.459 103.661  1.00 66.32           C  
ANISOU 2248  CB  ASN A 354     4875   8271  12051    281  -1203  -1777       C  
ATOM   2249  CG  ASN A 354      41.764  -7.203 103.210  1.00 71.98           C  
ANISOU 2249  CG  ASN A 354     5870   8917  12560    323  -1125  -1478       C  
ATOM   2250  OD1 ASN A 354      41.286  -8.106 103.896  1.00 70.08           O  
ANISOU 2250  OD1 ASN A 354     5767   8702  12160    482  -1308  -1357       O  
ATOM   2251  ND2 ASN A 354      41.239  -6.830 102.050  1.00 74.98           N  
ANISOU 2251  ND2 ASN A 354     6342   9204  12942    184   -851  -1372       N  
ATOM   2252  N   PRO A 355      45.052  -4.876 105.412  1.00 69.32           N  
ANISOU 2252  N   PRO A 355     4747   8812  12779    239  -1527  -2399       N  
ATOM   2253  CA  PRO A 355      46.423  -4.533 105.830  1.00 67.46           C  
ANISOU 2253  CA  PRO A 355     4167   8671  12794    241  -1665  -2782       C  
ATOM   2254  C   PRO A 355      46.697  -4.832 107.290  1.00 74.83           C  
ANISOU 2254  C   PRO A 355     5072   9680  13680    462  -2097  -2912       C  
ATOM   2255  O   PRO A 355      47.812  -5.241 107.639  1.00 82.53           O  
ANISOU 2255  O   PRO A 355     5793  10750  14813    602  -2322  -3196       O  
ATOM   2256  CB  PRO A 355      46.522  -3.028 105.525  1.00 73.54           C  
ANISOU 2256  CB  PRO A 355     4854   9397  13692    -42  -1399  -2906       C  
ATOM   2257  CG  PRO A 355      45.386  -2.740 104.593  1.00 72.21           C  
ANISOU 2257  CG  PRO A 355     4965   9102  13370   -172  -1086  -2599       C  
ATOM   2258  CD  PRO A 355      44.301  -3.696 104.954  1.00 73.21           C  
ANISOU 2258  CD  PRO A 355     5368   9213  13236     14  -1246  -2287       C  
ATOM   2259  N   ILE A 356      45.699  -4.647 108.157  1.00 75.97           N  
ANISOU 2259  N   ILE A 356     5480   9774  13610    515  -2230  -2730       N  
ATOM   2260  CA  ILE A 356      45.878  -4.978 109.567  1.00 77.56           C  
ANISOU 2260  CA  ILE A 356     5728  10012  13727    753  -2661  -2844       C  
ATOM   2261  C   ILE A 356      46.082  -6.475 109.739  1.00 85.93           C  
ANISOU 2261  C   ILE A 356     6869  11088  14691   1047  -2897  -2803       C  
ATOM   2262  O   ILE A 356      46.856  -6.919 110.596  1.00 91.96           O  
ANISOU 2262  O   ILE A 356     7552  11909  15479   1284  -3265  -3028       O  
ATOM   2263  CB  ILE A 356      44.683  -4.471 110.391  1.00 67.77           C  
ANISOU 2263  CB  ILE A 356     4787   8687  12277    736  -2723  -2651       C  
ATOM   2264  CG1 ILE A 356      44.651  -2.943 110.366  1.00 64.87           C  
ANISOU 2264  CG1 ILE A 356     4317   8313  12020    466  -2538  -2748       C  
ATOM   2265  CG2 ILE A 356      44.771  -4.980 111.819  1.00 68.55           C  
ANISOU 2265  CG2 ILE A 356     5027   8783  12235   1021  -3184  -2741       C  
ATOM   2266  CD1 ILE A 356      43.333  -2.356 110.800  1.00 61.16           C  
ANISOU 2266  CD1 ILE A 356     4128   7740  11370    393  -2482  -2520       C  
ATOM   2267  N   ILE A 357      45.376  -7.278 108.941  1.00 86.00           N  
ANISOU 2267  N   ILE A 357     7058  11041  14577   1048  -2702  -2523       N  
ATOM   2268  CA  ILE A 357      45.554  -8.725 108.994  1.00 81.46           C  
ANISOU 2268  CA  ILE A 357     6572  10472  13908   1309  -2884  -2474       C  
ATOM   2269  C   ILE A 357      46.961  -9.111 108.563  1.00 76.48           C  
ANISOU 2269  C   ILE A 357     5597   9942  13518   1388  -2953  -2761       C  
ATOM   2270  O   ILE A 357      47.598  -9.978 109.174  1.00 74.19           O  
ANISOU 2270  O   ILE A 357     5285   9692  13213   1674  -3283  -2908       O  
ATOM   2271  CB  ILE A 357      44.487  -9.426 108.136  1.00 73.01           C  
ANISOU 2271  CB  ILE A 357     5741   9326  12673   1253  -2623  -2127       C  
ATOM   2272  CG1 ILE A 357      43.104  -9.194 108.737  1.00 74.66           C  
ANISOU 2272  CG1 ILE A 357     6275   9437  12654   1226  -2613  -1884       C  
ATOM   2273  CG2 ILE A 357      44.789 -10.905 108.030  1.00 76.53           C  
ANISOU 2273  CG2 ILE A 357     6247   9780  13051   1498  -2766  -2094       C  
ATOM   2274  CD1 ILE A 357      41.980  -9.590 107.825  1.00 71.74           C  
ANISOU 2274  CD1 ILE A 357     6095   9005  12159   1115  -2316  -1578       C  
ATOM   2275  N   TYR A 358      47.468  -8.483 107.499  1.00 77.89           N  
ANISOU 2275  N   TYR A 358     5519  10152  13922   1150  -2644  -2862       N  
ATOM   2276  CA  TYR A 358      48.815  -8.805 107.042  1.00 83.55           C  
ANISOU 2276  CA  TYR A 358     5878  10963  14906   1205  -2679  -3167       C  
ATOM   2277  C   TYR A 358      49.860  -8.444 108.087  1.00 96.10           C  
ANISOU 2277  C   TYR A 358     7208  12653  16654   1341  -3028  -3555       C  
ATOM   2278  O   TYR A 358      50.933  -9.055 108.128  1.00102.39           O  
ANISOU 2278  O   TYR A 358     7748  13537  17618   1524  -3224  -3826       O  
ATOM   2279  CB  TYR A 358      49.139  -8.075 105.739  1.00 81.74           C  
ANISOU 2279  CB  TYR A 358     5441  10706  14912    907  -2266  -3254       C  
ATOM   2280  CG  TYR A 358      48.111  -8.187 104.638  1.00 79.90           C  
ANISOU 2280  CG  TYR A 358     5457  10352  14550    754  -1920  -2926       C  
ATOM   2281  CD1 TYR A 358      47.243  -9.266 104.565  1.00 77.43           C  
ANISOU 2281  CD1 TYR A 358     5431   9992  13999    899  -1969  -2624       C  
ATOM   2282  CD2 TYR A 358      48.038  -7.219 103.645  1.00 83.33           C  
ANISOU 2282  CD2 TYR A 358     5845  10713  15104    469  -1544  -2941       C  
ATOM   2283  CE1 TYR A 358      46.311  -9.364 103.545  1.00 73.22           C  
ANISOU 2283  CE1 TYR A 358     5105   9356  13358    763  -1673  -2355       C  
ATOM   2284  CE2 TYR A 358      47.117  -7.308 102.625  1.00 81.18           C  
ANISOU 2284  CE2 TYR A 358     5811  10324  14711    355  -1260  -2663       C  
ATOM   2285  CZ  TYR A 358      46.255  -8.380 102.577  1.00 77.19           C  
ANISOU 2285  CZ  TYR A 358     5561   9788  13978    502  -1336  -2377       C  
ATOM   2286  OH  TYR A 358      45.337  -8.466 101.556  1.00 78.03           O  
ANISOU 2286  OH  TYR A 358     5890   9786  13973    394  -1074  -2127       O  
ATOM   2287  N   ASN A 359      49.567  -7.458 108.937  1.00 96.79           N  
ANISOU 2287  N   ASN A 359     7350  12731  16694   1264  -3123  -3602       N  
ATOM   2288  CA  ASN A 359      50.535  -7.022 109.939  1.00 97.94           C  
ANISOU 2288  CA  ASN A 359     7250  12975  16986   1379  -3463  -3988       C  
ATOM   2289  C   ASN A 359      50.715  -8.067 111.034  1.00101.66           C  
ANISOU 2289  C   ASN A 359     7877  13459  17290   1790  -3959  -4046       C  
ATOM   2290  O   ASN A 359      51.844  -8.366 111.440  1.00114.57           O  
ANISOU 2290  O   ASN A 359     9248  15197  19088   1997  -4260  -4399       O  
ATOM   2291  CB  ASN A 359      50.088  -5.687 110.538  1.00 94.04           C  
ANISOU 2291  CB  ASN A 359     6813  12458  16462   1178  -3422  -3998       C  
ATOM   2292  CG  ASN A 359      51.076  -5.135 111.544  1.00 99.86           C  
ANISOU 2292  CG  ASN A 359     7286  13303  17355   1265  -3760  -4410       C  
ATOM   2293  OD1 ASN A 359      52.107  -4.578 111.172  1.00104.12           O  
ANISOU 2293  OD1 ASN A 359     7422  13937  18200   1122  -3662  -4749       O  
ATOM   2294  ND2 ASN A 359      50.760  -5.275 112.828  1.00104.06           N  
ANISOU 2294  ND2 ASN A 359     8054  13811  17675   1497  -4159  -4400       N  
ATOM   2295  N   PHE A 360      49.613  -8.629 111.531  1.00 94.92           N  
ANISOU 2295  N   PHE A 360     7467  12491  16107   1924  -4053  -3723       N  
ATOM   2296  CA  PHE A 360      49.701  -9.575 112.636  1.00 98.06           C  
ANISOU 2296  CA  PHE A 360     8111  12855  16293   2325  -4520  -3771       C  
ATOM   2297  C   PHE A 360      50.049 -10.991 112.187  1.00100.00           C  
ANISOU 2297  C   PHE A 360     8387  13104  16505   2569  -4593  -3737       C  
ATOM   2298  O   PHE A 360      50.693 -11.730 112.941  1.00111.08           O  
ANISOU 2298  O   PHE A 360     9837  14522  17846   2930  -5007  -3936       O  
ATOM   2299  CB  PHE A 360      48.390  -9.577 113.418  1.00 95.94           C  
ANISOU 2299  CB  PHE A 360     8335  12438  15681   2369  -4585  -3470       C  
ATOM   2300  CG  PHE A 360      48.042  -8.245 114.020  1.00100.74           C  
ANISOU 2300  CG  PHE A 360     8948  13035  16296   2179  -4575  -3513       C  
ATOM   2301  CD1 PHE A 360      48.957  -7.575 114.817  1.00105.81           C  
ANISOU 2301  CD1 PHE A 360     9371  13761  17070   2248  -4870  -3871       C  
ATOM   2302  CD2 PHE A 360      46.807  -7.661 113.793  1.00 97.54           C  
ANISOU 2302  CD2 PHE A 360     8755  12538  15770   1938  -4282  -3211       C  
ATOM   2303  CE1 PHE A 360      48.649  -6.352 115.379  1.00103.77           C  
ANISOU 2303  CE1 PHE A 360     9124  13493  16810   2066  -4863  -3913       C  
ATOM   2304  CE2 PHE A 360      46.492  -6.435 114.352  1.00 98.36           C  
ANISOU 2304  CE2 PHE A 360     8867  12627  15878   1771  -4279  -3255       C  
ATOM   2305  CZ  PHE A 360      47.416  -5.780 115.147  1.00 99.13           C  
ANISOU 2305  CZ  PHE A 360     8764  12807  16096   1827  -4564  -3599       C  
ATOM   2306  N   LEU A 361      49.638 -11.393 110.985  1.00 89.62           N  
ANISOU 2306  N   LEU A 361     7070  11768  15215   2400  -4216  -3497       N  
ATOM   2307  CA  LEU A 361      49.842 -12.759 110.517  1.00 89.62           C  
ANISOU 2307  CA  LEU A 361     7134  11759  15160   2616  -4256  -3424       C  
ATOM   2308  C   LEU A 361      50.966 -12.896 109.498  1.00 97.69           C  
ANISOU 2308  C   LEU A 361     7709  12897  16511   2558  -4113  -3655       C  
ATOM   2309  O   LEU A 361      51.192 -14.001 108.995  1.00 98.93           O  
ANISOU 2309  O   LEU A 361     7883  13054  16652   2723  -4118  -3602       O  
ATOM   2310  CB  LEU A 361      48.545 -13.316 109.923  1.00 82.04           C  
ANISOU 2310  CB  LEU A 361     6523  10681  13966   2512  -3965  -2987       C  
ATOM   2311  CG  LEU A 361      47.359 -13.418 110.882  1.00 78.58           C  
ANISOU 2311  CG  LEU A 361     6557  10107  13192   2595  -4089  -2750       C  
ATOM   2312  CD1 LEU A 361      46.075 -13.738 110.128  1.00 75.91           C  
ANISOU 2312  CD1 LEU A 361     6463   9679  12699   2415  -3733  -2360       C  
ATOM   2313  CD2 LEU A 361      47.639 -14.465 111.947  1.00 83.03           C  
ANISOU 2313  CD2 LEU A 361     7406  10607  13536   3023  -4536  -2840       C  
ATOM   2314  N   SER A 362      51.673 -11.816 109.177  1.00101.82           N  
ANISOU 2314  N   SER A 362     7845  13510  17333   2327  -3975  -3918       N  
ATOM   2315  CA  SER A 362      52.798 -11.882 108.248  1.00 99.28           C  
ANISOU 2315  CA  SER A 362     7084  13288  17351   2261  -3830  -4190       C  
ATOM   2316  C   SER A 362      53.933 -11.039 108.808  1.00108.92           C  
ANISOU 2316  C   SER A 362     7896  14632  18858   2258  -4027  -4663       C  
ATOM   2317  O   SER A 362      53.805  -9.816 108.916  1.00106.68           O  
ANISOU 2317  O   SER A 362     7528  14349  18656   1992  -3875  -4726       O  
ATOM   2318  CB  SER A 362      52.398 -11.403 106.852  1.00 91.42           C  
ANISOU 2318  CB  SER A 362     6033  12228  16474   1896  -3306  -4035       C  
ATOM   2319  OG  SER A 362      53.525 -11.365 105.994  1.00 95.55           O  
ANISOU 2319  OG  SER A 362     6126  12819  17358   1819  -3158  -4363       O  
ATOM   2320  N   GLY A 363      55.041 -11.690 109.165  1.00118.62           N  
ANISOU 2320  N   GLY A 363     8865  15966  20240   2560  -4369  -5011       N  
ATOM   2321  CA  GLY A 363      56.179 -10.949 109.677  1.00114.73           C  
ANISOU 2321  CA  GLY A 363     7937  15608  20048   2571  -4575  -5508       C  
ATOM   2322  C   GLY A 363      56.891 -10.134 108.616  1.00116.42           C  
ANISOU 2322  C   GLY A 363     7694  15882  20659   2217  -4168  -5765       C  
ATOM   2323  O   GLY A 363      57.499  -9.106 108.926  1.00120.05           O  
ANISOU 2323  O   GLY A 363     7848  16423  21344   2059  -4173  -6093       O  
ATOM   2324  N   LYS A 364      56.834 -10.576 107.356  1.00114.23           N  
ANISOU 2324  N   LYS A 364     7375  15549  20477   2085  -3808  -5646       N  
ATOM   2325  CA  LYS A 364      57.468  -9.814 106.283  1.00124.53           C  
ANISOU 2325  CA  LYS A 364     8301  16866  22149   1740  -3381  -5898       C  
ATOM   2326  C   LYS A 364      56.730  -8.508 106.011  1.00122.80           C  
ANISOU 2326  C   LYS A 364     8237  16550  21873   1342  -3004  -5721       C  
ATOM   2327  O   LYS A 364      57.363  -7.472 105.772  1.00128.65           O  
ANISOU 2327  O   LYS A 364     8664  17324  22894   1078  -2791  -6038       O  
ATOM   2328  CB  LYS A 364      57.567 -10.668 105.019  1.00114.82           C  
ANISOU 2328  CB  LYS A 364     7037  15583  21008   1720  -3102  -5801       C  
ATOM   2329  CG  LYS A 364      58.779 -11.591 105.013  1.00121.66           C  
ANISOU 2329  CG  LYS A 364     7522  16578  22126   2014  -3360  -6179       C  
ATOM   2330  CD  LYS A 364      58.470 -12.945 104.396  1.00119.33           C  
ANISOU 2330  CD  LYS A 364     7429  16229  21681   2216  -3343  -5902       C  
ATOM   2331  CE  LYS A 364      59.581 -13.943 104.701  1.00126.33           C  
ANISOU 2331  CE  LYS A 364     8006  17252  22743   2607  -3718  -6249       C  
ATOM   2332  NZ  LYS A 364      59.400 -15.248 104.003  1.00124.69           N  
ANISOU 2332  NZ  LYS A 364     7953  16996  22427   2794  -3663  -6011       N  
ATOM   2333  N   PHE A 365      55.394  -8.532 106.038  1.00114.47           N  
ANISOU 2333  N   PHE A 365     7662  15372  20460   1294  -2910  -5233       N  
ATOM   2334  CA  PHE A 365      54.638  -7.285 105.953  1.00107.13           C  
ANISOU 2334  CA  PHE A 365     6906  14357  19442    971  -2623  -5063       C  
ATOM   2335  C   PHE A 365      54.831  -6.449 107.210  1.00104.41           C  
ANISOU 2335  C   PHE A 365     6491  14097  19085    990  -2903  -5246       C  
ATOM   2336  O   PHE A 365      54.996  -5.226 107.134  1.00104.14           O  
ANISOU 2336  O   PHE A 365     6317  14059  19193    705  -2685  -5404       O  
ATOM   2337  CB  PHE A 365      53.151  -7.578 105.737  1.00 99.76           C  
ANISOU 2337  CB  PHE A 365     6479  13288  18137    950  -2494  -4524       C  
ATOM   2338  CG  PHE A 365      52.771  -7.783 104.299  1.00 92.00           C  
ANISOU 2338  CG  PHE A 365     5590  12191  17177    769  -2069  -4331       C  
ATOM   2339  CD1 PHE A 365      52.804  -6.729 103.401  1.00 88.96           C  
ANISOU 2339  CD1 PHE A 365     5136  11724  16941    429  -1640  -4393       C  
ATOM   2340  CD2 PHE A 365      52.350  -9.024 103.853  1.00 87.23           C  
ANISOU 2340  CD2 PHE A 365     5174  11545  16423    941  -2096  -4083       C  
ATOM   2341  CE1 PHE A 365      52.442  -6.914 102.079  1.00 86.04           C  
ANISOU 2341  CE1 PHE A 365     4892  11229  16570    281  -1266  -4220       C  
ATOM   2342  CE2 PHE A 365      51.987  -9.215 102.533  1.00 84.32           C  
ANISOU 2342  CE2 PHE A 365     4905  11069  16065    780  -1722  -3907       C  
ATOM   2343  CZ  PHE A 365      52.033  -8.158 101.645  1.00 83.58           C  
ANISOU 2343  CZ  PHE A 365     4751  10888  16117    456  -1316  -3977       C  
ATOM   2344  N   ARG A 366      54.813  -7.098 108.376  1.00106.50           N  
ANISOU 2344  N   ARG A 366     6867  14415  19183   1334  -3390  -5254       N  
ATOM   2345  CA  ARG A 366      55.005  -6.391 109.635  1.00110.57           C  
ANISOU 2345  CA  ARG A 366     7331  14993  19688   1400  -3717  -5468       C  
ATOM   2346  C   ARG A 366      56.308  -5.602 109.628  1.00114.81           C  
ANISOU 2346  C   ARG A 366     7335  15663  20626   1266  -3707  -6004       C  
ATOM   2347  O   ARG A 366      56.356  -4.456 110.090  1.00116.03           O  
ANISOU 2347  O   ARG A 366     7402  15838  20845   1068  -3675  -6153       O  
ATOM   2348  CB  ARG A 366      54.981  -7.391 110.789  1.00114.53           C  
ANISOU 2348  CB  ARG A 366     8031  15516  19969   1847  -4268  -5460       C  
ATOM   2349  CG  ARG A 366      55.058  -6.777 112.171  1.00122.17           C  
ANISOU 2349  CG  ARG A 366     9041  16521  20859   1965  -4659  -5640       C  
ATOM   2350  CD  ARG A 366      54.271  -7.617 113.170  1.00130.38           C  
ANISOU 2350  CD  ARG A 366    10575  17463  21502   2315  -5037  -5381       C  
ATOM   2351  NE  ARG A 366      54.500  -9.047 112.974  1.00141.61           N  
ANISOU 2351  NE  ARG A 366    12085  18875  22844   2640  -5210  -5335       N  
ATOM   2352  CZ  ARG A 366      53.837 -10.003 113.615  1.00145.85           C  
ANISOU 2352  CZ  ARG A 366    13086  19301  23029   2949  -5472  -5095       C  
ATOM   2353  NH1 ARG A 366      52.905  -9.678 114.500  1.00143.72           N  
ANISOU 2353  NH1 ARG A 366    13224  18916  22465   2973  -5591  -4888       N  
ATOM   2354  NH2 ARG A 366      54.104 -11.280 113.377  1.00148.08           N  
ANISOU 2354  NH2 ARG A 366    13441  19575  23249   3232  -5605  -5071       N  
ATOM   2355  N   GLU A 367      57.380  -6.203 109.107  1.00122.22           N  
ANISOU 2355  N   GLU A 367     7900  16693  21845   1364  -3727  -6318       N  
ATOM   2356  CA  GLU A 367      58.660  -5.509 109.046  1.00129.31           C  
ANISOU 2356  CA  GLU A 367     8249  17723  23162   1228  -3694  -6876       C  
ATOM   2357  C   GLU A 367      58.544  -4.217 108.245  1.00126.30           C  
ANISOU 2357  C   GLU A 367     7786  17269  22933    743  -3143  -6901       C  
ATOM   2358  O   GLU A 367      58.967  -3.148 108.700  1.00129.10           O  
ANISOU 2358  O   GLU A 367     7918  17683  23450    558  -3132  -7201       O  
ATOM   2359  CB  GLU A 367      59.710  -6.434 108.432  1.00136.90           C  
ANISOU 2359  CB  GLU A 367     8842  18772  24403   1394  -3734  -7176       C  
ATOM   2360  CG  GLU A 367      60.591  -7.150 109.437  1.00144.89           C  
ANISOU 2360  CG  GLU A 367     9620  19940  25492   1830  -4335  -7536       C  
ATOM   2361  CD  GLU A 367      61.468  -8.194 108.780  1.00150.80           C  
ANISOU 2361  CD  GLU A 367    10058  20757  26481   2030  -4375  -7779       C  
ATOM   2362  OE1 GLU A 367      60.913  -9.122 108.155  1.00146.66           O  
ANISOU 2362  OE1 GLU A 367     9812  20135  25777   2123  -4260  -7426       O  
ATOM   2363  OE2 GLU A 367      62.708  -8.086 108.886  1.00158.57           O  
ANISOU 2363  OE2 GLU A 367    10509  21896  27843   2093  -4522  -8337       O  
ATOM   2364  N   GLN A 368      57.971  -4.298 107.040  1.00123.88           N  
ANISOU 2364  N   GLN A 368     7679  16823  22566    537  -2683  -6596       N  
ATOM   2365  CA  GLN A 368      57.841  -3.111 106.202  1.00124.54           C  
ANISOU 2365  CA  GLN A 368     7750  16803  22766    100  -2144  -6617       C  
ATOM   2366  C   GLN A 368      56.871  -2.095 106.793  1.00118.18           C  
ANISOU 2366  C   GLN A 368     7264  15926  21714    -58  -2106  -6368       C  
ATOM   2367  O   GLN A 368      57.066  -0.886 106.623  1.00118.82           O  
ANISOU 2367  O   GLN A 368     7234  15977  21935   -380  -1811  -6553       O  
ATOM   2368  CB  GLN A 368      57.394  -3.512 104.796  1.00125.03           C  
ANISOU 2368  CB  GLN A 368     8000  16708  22798    -30  -1709  -6359       C  
ATOM   2369  CG  GLN A 368      58.361  -4.442 104.082  1.00131.01           C  
ANISOU 2369  CG  GLN A 368     8428  17513  23838     82  -1680  -6635       C  
ATOM   2370  CD  GLN A 368      59.475  -3.694 103.377  1.00140.62           C  
ANISOU 2370  CD  GLN A 368     9210  18738  25483   -217  -1306  -7136       C  
ATOM   2371  OE1 GLN A 368      59.340  -3.306 102.217  1.00138.88           O  
ANISOU 2371  OE1 GLN A 368     9081  18360  25327   -503   -796  -7082       O  
ATOM   2372  NE2 GLN A 368      60.583  -3.486 104.077  1.00153.07           N  
ANISOU 2372  NE2 GLN A 368    10318  20487  27353   -154  -1553  -7646       N  
ATOM   2373  N   PHE A 369      55.828  -2.555 107.487  1.00112.54           N  
ANISOU 2373  N   PHE A 369     6948  15175  20637    156  -2381  -5969       N  
ATOM   2374  CA  PHE A 369      54.904  -1.612 108.107  1.00111.19           C  
ANISOU 2374  CA  PHE A 369     7064  14939  20242     20  -2365  -5752       C  
ATOM   2375  C   PHE A 369      55.561  -0.874 109.264  1.00116.57           C  
ANISOU 2375  C   PHE A 369     7497  15745  21051     24  -2666  -6126       C  
ATOM   2376  O   PHE A 369      55.309   0.318 109.470  1.00112.86           O  
ANISOU 2376  O   PHE A 369     7068  15240  20575   -243  -2494  -6153       O  
ATOM   2377  CB  PHE A 369      53.649  -2.340 108.584  1.00102.92           C  
ANISOU 2377  CB  PHE A 369     6487  13817  18799    249  -2579  -5274       C  
ATOM   2378  CG  PHE A 369      52.806  -2.888 107.471  1.00 94.55           C  
ANISOU 2378  CG  PHE A 369     5712  12629  17582    198  -2260  -4876       C  
ATOM   2379  CD1 PHE A 369      53.010  -2.486 106.161  1.00 94.07           C  
ANISOU 2379  CD1 PHE A 369     5565  12494  17685    -71  -1788  -4909       C  
ATOM   2380  CD2 PHE A 369      51.805  -3.805 107.738  1.00 89.90           C  
ANISOU 2380  CD2 PHE A 369     5493  11985  16679    418  -2429  -4487       C  
ATOM   2381  CE1 PHE A 369      52.231  -2.992 105.140  1.00 90.26           C  
ANISOU 2381  CE1 PHE A 369     5358  11891  17047   -102  -1526  -4554       C  
ATOM   2382  CE2 PHE A 369      51.025  -4.313 106.723  1.00 88.16           C  
ANISOU 2382  CE2 PHE A 369     5519  11658  16318    368  -2150  -4141       C  
ATOM   2383  CZ  PHE A 369      51.237  -3.907 105.423  1.00 87.31           C  
ANISOU 2383  CZ  PHE A 369     5321  11486  16368    116  -1715  -4171       C  
ATOM   2384  N   LYS A 370      56.411  -1.565 110.027  1.00123.51           N  
ANISOU 2384  N   LYS A 370     8123  16767  22039    331  -3126  -6426       N  
ATOM   2385  CA  LYS A 370      57.168  -0.893 111.074  1.00124.03           C  
ANISOU 2385  CA  LYS A 370     7902  16965  22258    347  -3436  -6842       C  
ATOM   2386  C   LYS A 370      58.187   0.072 110.485  1.00128.51           C  
ANISOU 2386  C   LYS A 370     8008  17594  23226      1  -3093  -7297       C  
ATOM   2387  O   LYS A 370      58.465   1.120 111.080  1.00131.66           O  
ANISOU 2387  O   LYS A 370     8262  18047  23717   -185  -3120  -7544       O  
ATOM   2388  CB  LYS A 370      57.847  -1.927 111.974  1.00128.93           C  
ANISOU 2388  CB  LYS A 370     8380  17714  22892    802  -4031  -7072       C  
ATOM   2389  CG  LYS A 370      58.105  -1.448 113.396  1.00136.42           C  
ANISOU 2389  CG  LYS A 370     9283  18754  23795    943  -4507  -7313       C  
ATOM   2390  CD  LYS A 370      58.678  -2.565 114.257  1.00143.86           C  
ANISOU 2390  CD  LYS A 370    10178  19788  24693   1451  -5118  -7505       C  
ATOM   2391  CE  LYS A 370      57.567  -3.443 114.815  1.00136.60           C  
ANISOU 2391  CE  LYS A 370     9847  18732  23322   1758  -5367  -7035       C  
ATOM   2392  NZ  LYS A 370      58.081  -4.572 115.638  1.00143.13           N  
ANISOU 2392  NZ  LYS A 370    10716  19609  24058   2278  -5952  -7206       N  
ATOM   2393  N   ALA A 371      58.759  -0.265 109.326  1.00129.84           N  
ANISOU 2393  N   ALA A 371     7950  17748  23634   -101  -2760  -7431       N  
ATOM   2394  CA  ALA A 371      59.683   0.652 108.671  1.00134.88           C  
ANISOU 2394  CA  ALA A 371     8186  18411  24653   -461  -2357  -7871       C  
ATOM   2395  C   ALA A 371      58.976   1.904 108.168  1.00135.34           C  
ANISOU 2395  C   ALA A 371     8503  18309  24612   -880  -1851  -7676       C  
ATOM   2396  O   ALA A 371      59.593   2.972 108.094  1.00136.94           O  
ANISOU 2396  O   ALA A 371     8448  18529  25052  -1196  -1594  -8042       O  
ATOM   2397  CB  ALA A 371      60.399  -0.051 107.518  1.00137.11           C  
ANISOU 2397  CB  ALA A 371     8212  18685  25198   -468  -2099  -8046       C  
ATOM   2398  N   ALA A 372      57.690   1.798 107.820  1.00131.14           N  
ANISOU 2398  N   ALA A 372     8480  17617  23732   -886  -1699  -7123       N  
ATOM   2399  CA  ALA A 372      56.964   2.967 107.332  1.00128.81           C  
ANISOU 2399  CA  ALA A 372     8463  17159  23319  -1246  -1238  -6929       C  
ATOM   2400  C   ALA A 372      56.654   3.940 108.461  1.00129.76           C  
ANISOU 2400  C   ALA A 372     8662  17316  23324  -1337  -1429  -6955       C  
ATOM   2401  O   ALA A 372      56.837   5.153 108.310  1.00134.03           O  
ANISOU 2401  O   ALA A 372     9152  17806  23969  -1687  -1099  -7141       O  
ATOM   2402  CB  ALA A 372      55.677   2.532 106.630  1.00125.31           C  
ANISOU 2402  CB  ALA A 372     8515  16547  22552  -1198  -1055  -6358       C  
ATOM   2403  N   PHE A 373      56.186   3.431 109.604  1.00125.05           N  
ANISOU 2403  N   PHE A 373     8219  16793  22503  -1033  -1947  -6781       N  
ATOM   2404  CA  PHE A 373      55.901   4.318 110.725  1.00121.84           C  
ANISOU 2404  CA  PHE A 373     7900  16415  21977  -1111  -2158  -6815       C  
ATOM   2405  C   PHE A 373      57.170   4.956 111.271  1.00127.46           C  
ANISOU 2405  C   PHE A 373     8132  17283  23015  -1232  -2282  -7397       C  
ATOM   2406  O   PHE A 373      57.128   6.083 111.779  1.00129.00           O  
ANISOU 2406  O   PHE A 373     8341  17471  23203  -1484  -2221  -7515       O  
ATOM   2407  CB  PHE A 373      55.174   3.551 111.829  1.00116.26           C  
ANISOU 2407  CB  PHE A 373     7479  15734  20958   -738  -2691  -6534       C  
ATOM   2408  CG  PHE A 373      53.834   3.019 111.413  1.00113.95           C  
ANISOU 2408  CG  PHE A 373     7662  15292  20342   -647  -2570  -5978       C  
ATOM   2409  CD1 PHE A 373      52.888   3.860 110.855  1.00108.91           C  
ANISOU 2409  CD1 PHE A 373     7320  14499  19560   -928  -2159  -5692       C  
ATOM   2410  CD2 PHE A 373      53.522   1.678 111.573  1.00106.12           C  
ANISOU 2410  CD2 PHE A 373     6824  14308  19190   -280  -2862  -5762       C  
ATOM   2411  CE1 PHE A 373      51.654   3.379 110.469  1.00 96.65           C  
ANISOU 2411  CE1 PHE A 373     6171  12821  17732   -839  -2060  -5215       C  
ATOM   2412  CE2 PHE A 373      52.288   1.191 111.187  1.00 99.22           C  
ANISOU 2412  CE2 PHE A 373     6366  13302  18033   -216  -2737  -5279       C  
ATOM   2413  CZ  PHE A 373      51.353   2.043 110.634  1.00 94.54           C  
ANISOU 2413  CZ  PHE A 373     6027  12574  17321   -494  -2344  -5012       C  
ATOM   2414  N   SER A 374      58.303   4.257 111.184  1.00133.18           N  
ANISOU 2414  N   SER A 374     8424  18150  24029  -1060  -2460  -7783       N  
ATOM   2415  CA  SER A 374      59.556   4.846 111.640  1.00143.13           C  
ANISOU 2415  CA  SER A 374     9172  19571  25638  -1179  -2567  -8388       C  
ATOM   2416  C   SER A 374      60.004   5.988 110.736  1.00148.19           C  
ANISOU 2416  C   SER A 374     9633  20139  26535  -1672  -1938  -8651       C  
ATOM   2417  O   SER A 374      60.569   6.978 111.215  1.00153.34           O  
ANISOU 2417  O   SER A 374    10047  20858  27355  -1917  -1907  -9022       O  
ATOM   2418  CB  SER A 374      60.641   3.774 111.711  1.00148.18           C  
ANISOU 2418  CB  SER A 374     9383  20379  26541   -853  -2907  -8755       C  
ATOM   2419  OG  SER A 374      60.396   2.871 112.772  1.00147.64           O  
ANISOU 2419  OG  SER A 374     9467  20383  26246   -393  -3541  -8619       O  
ATOM   2420  N   TRP A 375      59.775   5.866 109.427  1.00146.67           N  
ANISOU 2420  N   TRP A 375     9570  19794  26364  -1826  -1425  -8479       N  
ATOM   2421  CA  TRP A 375      60.226   6.907 108.508  1.00149.85           C  
ANISOU 2421  CA  TRP A 375     9851  20091  26993  -2283   -791  -8747       C  
ATOM   2422  C   TRP A 375      59.276   8.097 108.441  1.00149.27           C  
ANISOU 2422  C   TRP A 375    10215  19838  26664  -2598   -444  -8457       C  
ATOM   2423  O   TRP A 375      59.694   9.245 108.629  1.00153.30           O  
ANISOU 2423  O   TRP A 375    10600  20339  27306  -2936   -213  -8767       O  
ATOM   2424  CB  TRP A 375      60.420   6.312 107.115  1.00145.88           C  
ANISOU 2424  CB  TRP A 375     9336  19477  26614  -2317   -377  -8717       C  
ATOM   2425  CG  TRP A 375      61.795   5.805 106.905  1.00152.70           C  
ANISOU 2425  CG  TRP A 375     9622  20489  27908  -2263   -427  -9274       C  
ATOM   2426  CD1 TRP A 375      62.166   4.530 106.600  1.00154.42           C  
ANISOU 2426  CD1 TRP A 375     9673  20778  28223  -1952   -642  -9291       C  
ATOM   2427  CD2 TRP A 375      63.001   6.564 107.005  1.00159.46           C  
ANISOU 2427  CD2 TRP A 375     9971  21447  29170  -2531   -259  -9927       C  
ATOM   2428  NE1 TRP A 375      63.533   4.451 106.491  1.00161.98           N  
ANISOU 2428  NE1 TRP A 375    10038  21875  29632  -2000   -625  -9920       N  
ATOM   2429  CE2 TRP A 375      64.069   5.688 106.737  1.00166.19           C  
ANISOU 2429  CE2 TRP A 375    10341  22434  30371  -2356   -388 -10330       C  
ATOM   2430  CE3 TRP A 375      63.283   7.904 107.291  1.00163.09           C  
ANISOU 2430  CE3 TRP A 375    10336  21894  29736  -2913      0 -10224       C  
ATOM   2431  CZ2 TRP A 375      65.397   6.106 106.745  1.00175.98           C  
ANISOU 2431  CZ2 TRP A 375    10983  23804  32079  -2546   -270 -11037       C  
ATOM   2432  CZ3 TRP A 375      64.601   8.318 107.299  1.00172.48           C  
ANISOU 2432  CZ3 TRP A 375    10947  23209  31378  -3116    131 -10919       C  
ATOM   2433  CH2 TRP A 375      65.642   7.422 107.028  1.00178.94           C  
ANISOU 2433  CH2 TRP A 375    11265  24169  32557  -2931     -5 -11328       C  
ATOM   2434  N   TRP A 376      57.999   7.849 108.180  1.00146.22           N  
ANISOU 2434  N   TRP A 376    10340  19302  25914  -2497   -401  -7880       N  
ATOM   2435  CA  TRP A 376      57.046   8.944 108.053  1.00143.55           C  
ANISOU 2435  CA  TRP A 376    10435  18780  25327  -2771    -71  -7598       C  
ATOM   2436  C   TRP A 376      56.089   9.006 109.236  1.00138.60           C  
ANISOU 2436  C   TRP A 376    10102  18180  24379  -2603   -511  -7268       C  
ATOM   2437  O   TRP A 376      56.496   9.275 110.364  1.00140.55           O  
ANISOU 2437  O   TRP A 376    10160  18566  24677  -2571   -885  -7504       O  
ATOM   2438  CB  TRP A 376      56.265   8.825 106.742  1.00137.76           C  
ANISOU 2438  CB  TRP A 376    10086  17826  24432  -2837    394  -7227       C  
ATOM   2439  CG  TRP A 376      57.018   8.142 105.629  1.00139.13           C  
ANISOU 2439  CG  TRP A 376    10030  17982  24850  -2825    653  -7422       C  
ATOM   2440  CD1 TRP A 376      56.618   7.036 104.938  1.00131.65           C  
ANISOU 2440  CD1 TRP A 376     9225  16990  23807  -2587    619  -7124       C  
ATOM   2441  CD2 TRP A 376      58.294   8.514 105.084  1.00147.19           C  
ANISOU 2441  CD2 TRP A 376    10645  19021  26258  -3075    997  -7976       C  
ATOM   2442  NE1 TRP A 376      57.558   6.698 103.996  1.00136.55           N  
ANISOU 2442  NE1 TRP A 376     9568  17593  24722  -2670    909  -7443       N  
ATOM   2443  CE2 TRP A 376      58.597   7.588 104.065  1.00147.74           C  
ANISOU 2443  CE2 TRP A 376    10640  19047  26447  -2967   1153  -7977       C  
ATOM   2444  CE3 TRP A 376      59.207   9.538 105.357  1.00149.13           C  
ANISOU 2444  CE3 TRP A 376    10582  19312  26768  -3394   1202  -8487       C  
ATOM   2445  CZ2 TRP A 376      59.773   7.654 103.319  1.00148.72           C  
ANISOU 2445  CZ2 TRP A 376    10394  19163  26949  -3164   1512  -8476       C  
ATOM   2446  CZ3 TRP A 376      60.377   9.601 104.613  1.00151.61           C  
ANISOU 2446  CZ3 TRP A 376    10515  19626  27463  -3592   1569  -8995       C  
ATOM   2447  CH2 TRP A 376      60.647   8.665 103.607  1.00150.69           C  
ANISOU 2447  CH2 TRP A 376    10335  19458  27463  -3475   1723  -8989       C  
TER    2448      TRP A 376                                                      
ATOM   2449  N   LYS B  43      10.370 -50.484  76.635  1.00125.49           N  
ANISOU 2449  N   LYS B  43    16609  11875  19197  -3097   -563  -1199       N  
ATOM   2450  CA  LYS B  43      10.934 -49.471  75.750  1.00121.34           C  
ANISOU 2450  CA  LYS B  43    16175  11523  18407  -2860   -838  -1282       C  
ATOM   2451  C   LYS B  43      10.706 -49.825  74.287  1.00130.81           C  
ANISOU 2451  C   LYS B  43    17487  12696  19520  -2893  -1227  -1646       C  
ATOM   2452  O   LYS B  43      10.936 -50.962  73.873  1.00127.87           O  
ANISOU 2452  O   LYS B  43    17337  12085  19162  -2987  -1198  -1800       O  
ATOM   2453  CB  LYS B  43      12.423 -49.286  76.029  1.00110.58           C  
ANISOU 2453  CB  LYS B  43    15163  10156  16695  -2575   -625  -1053       C  
ATOM   2454  CG  LYS B  43      12.737 -48.070  76.879  1.00106.40           C  
ANISOU 2454  CG  LYS B  43    14517   9894  16016  -2379   -471   -763       C  
ATOM   2455  CD  LYS B  43      14.055 -48.226  77.612  1.00106.53           C  
ANISOU 2455  CD  LYS B  43    14808   9816  15853  -2188   -181   -515       C  
ATOM   2456  CE  LYS B  43      13.846 -48.854  78.978  1.00110.79           C  
ANISOU 2456  CE  LYS B  43    15295  10163  16638  -2334    138   -303       C  
ATOM   2457  NZ  LYS B  43      15.123 -48.941  79.734  1.00108.51           N  
ANISOU 2457  NZ  LYS B  43    15245   9879  16106  -2078    328    -45       N  
ATOM   2458  N   GLN B  44      10.140 -48.881  73.531  1.00143.53           N  
ANISOU 2458  N   GLN B  44    18934  14595  21005  -2804  -1574  -1777       N  
ATOM   2459  CA  GLN B  44       9.985 -49.038  72.093  1.00149.47           C  
ANISOU 2459  CA  GLN B  44    19844  15375  21574  -2778  -1983  -2107       C  
ATOM   2460  C   GLN B  44      11.018 -48.293  71.248  1.00145.41           C  
ANISOU 2460  C   GLN B  44    19693  15039  20518  -2445  -2080  -2065       C  
ATOM   2461  O   GLN B  44      11.222 -48.668  70.089  1.00152.07           O  
ANISOU 2461  O   GLN B  44    20814  15835  21133  -2404  -2320  -2319       O  
ATOM   2462  CB  GLN B  44       8.568 -48.608  71.687  1.00161.45           C  
ANISOU 2462  CB  GLN B  44    20954  17065  23325  -2909  -2366  -2323       C  
ATOM   2463  CG  GLN B  44       8.207 -48.842  70.242  1.00173.18           C  
ANISOU 2463  CG  GLN B  44    22568  18597  24633  -2898  -2826  -2685       C  
ATOM   2464  CD  GLN B  44       6.740 -48.552  69.978  1.00181.96           C  
ANISOU 2464  CD  GLN B  44    23225  19916  25997  -3011  -3139  -2863       C  
ATOM   2465  OE1 GLN B  44       6.033 -48.025  70.841  1.00183.38           O  
ANISOU 2465  OE1 GLN B  44    22991  20203  26484  -3081  -3036  -2724       O  
ATOM   2466  NE2 GLN B  44       6.265 -48.928  68.798  1.00186.86           N  
ANISOU 2466  NE2 GLN B  44    23914  20595  26489  -3022  -3502  -3170       N  
ATOM   2467  N   TYR B  45      11.656 -47.249  71.784  1.00130.06           N  
ANISOU 2467  N   TYR B  45    17761  13291  18366  -2216  -1892  -1767       N  
ATOM   2468  CA  TYR B  45      12.610 -46.414  71.054  1.00122.22           C  
ANISOU 2468  CA  TYR B  45    17075  12469  16892  -1914  -1939  -1701       C  
ATOM   2469  C   TYR B  45      14.074 -46.835  71.216  1.00112.13           C  
ANISOU 2469  C   TYR B  45    16152  11040  15412  -1773  -1610  -1577       C  
ATOM   2470  O   TYR B  45      14.965 -46.005  70.996  1.00108.05           O  
ANISOU 2470  O   TYR B  45    15813  10671  14571  -1528  -1523  -1439       O  
ATOM   2471  CB  TYR B  45      12.445 -44.950  71.472  1.00122.48           C  
ANISOU 2471  CB  TYR B  45    16899  12797  16840  -1746  -1943  -1474       C  
ATOM   2472  CG  TYR B  45      12.751 -44.665  72.926  1.00121.46           C  
ANISOU 2472  CG  TYR B  45    16592  12672  16887  -1741  -1568  -1171       C  
ATOM   2473  CD1 TYR B  45      13.997 -44.185  73.315  1.00119.15           C  
ANISOU 2473  CD1 TYR B  45    16501  12416  16354  -1529  -1300   -945       C  
ATOM   2474  CD2 TYR B  45      11.790 -44.855  73.909  1.00124.00           C  
ANISOU 2474  CD2 TYR B  45    16541  12962  17609  -1948  -1480  -1123       C  
ATOM   2475  CE1 TYR B  45      14.278 -43.910  74.642  1.00114.65           C  
ANISOU 2475  CE1 TYR B  45    15787  11859  15916  -1512   -997   -687       C  
ATOM   2476  CE2 TYR B  45      12.060 -44.584  75.235  1.00119.97           C  
ANISOU 2476  CE2 TYR B  45    15911  12462  17210  -1933  -1139   -850       C  
ATOM   2477  CZ  TYR B  45      13.303 -44.113  75.597  1.00112.82           C  
ANISOU 2477  CZ  TYR B  45    15230  11601  16036  -1709   -919   -637       C  
ATOM   2478  OH  TYR B  45      13.565 -43.844  76.921  1.00104.88           O  
ANISOU 2478  OH  TYR B  45    14121  10612  15118  -1685   -616   -386       O  
ATOM   2479  N   ALA B  46      14.354 -48.088  71.581  1.00104.81           N  
ANISOU 2479  N   ALA B  46    15324   9811  14687  -1914  -1425  -1626       N  
ATOM   2480  CA  ALA B  46      15.745 -48.480  71.802  1.00 95.58           C  
ANISOU 2480  CA  ALA B  46    14455   8495  13367  -1754  -1123  -1506       C  
ATOM   2481  C   ALA B  46      16.591 -48.366  70.535  1.00 97.96           C  
ANISOU 2481  C   ALA B  46    15123   8833  13266  -1559  -1207  -1664       C  
ATOM   2482  O   ALA B  46      17.775 -48.015  70.607  1.00 89.60           O  
ANISOU 2482  O   ALA B  46    14243   7807  11995  -1343   -984  -1522       O  
ATOM   2483  CB  ALA B  46      15.798 -49.908  72.347  1.00 89.06           C  
ANISOU 2483  CB  ALA B  46    13688   7305  12847  -1937   -944  -1546       C  
ATOM   2484  N   TRP B  47      16.008 -48.647  69.368  1.00106.34           N  
ANISOU 2484  N   TRP B  47    16302   9891  14214  -1631  -1521  -1969       N  
ATOM   2485  CA  TRP B  47      16.764 -48.518  68.124  1.00106.86           C  
ANISOU 2485  CA  TRP B  47    16755   9997  13849  -1446  -1586  -2125       C  
ATOM   2486  C   TRP B  47      17.104 -47.061  67.838  1.00104.13           C  
ANISOU 2486  C   TRP B  47    16441   9960  13164  -1215  -1602  -1947       C  
ATOM   2487  O   TRP B  47      18.259 -46.724  67.546  1.00102.25           O  
ANISOU 2487  O   TRP B  47    16453   9748  12648  -1011  -1382  -1865       O  
ATOM   2488  CB  TRP B  47      15.978 -49.122  66.959  1.00115.21           C  
ANISOU 2488  CB  TRP B  47    17945  10993  14835  -1575  -1956  -2504       C  
ATOM   2489  CG  TRP B  47      16.788 -49.332  65.702  1.00124.88           C  
ANISOU 2489  CG  TRP B  47    19638  12183  15629  -1415  -1973  -2710       C  
ATOM   2490  CD1 TRP B  47      17.378 -50.492  65.292  1.00133.07           C  
ANISOU 2490  CD1 TRP B  47    20856  13028  16676  -1416  -1802  -2877       C  
ATOM   2491  CD2 TRP B  47      17.076 -48.357  64.688  1.00127.31           C  
ANISOU 2491  CD2 TRP B  47    20199  12729  15444  -1200  -2098  -2721       C  
ATOM   2492  NE1 TRP B  47      18.020 -50.300  64.092  1.00138.38           N  
ANISOU 2492  NE1 TRP B  47    21874  13806  16897  -1225  -1807  -3002       N  
ATOM   2493  CE2 TRP B  47      17.849 -48.999  63.699  1.00134.49           C  
ANISOU 2493  CE2 TRP B  47    21474  13556  16071  -1099  -1989  -2913       C  
ATOM   2494  CE3 TRP B  47      16.757 -47.006  64.523  1.00122.32           C  
ANISOU 2494  CE3 TRP B  47    19484  12397  14595  -1067  -2251  -2553       C  
ATOM   2495  CZ2 TRP B  47      18.308 -48.335  62.563  1.00133.19           C  
ANISOU 2495  CZ2 TRP B  47    21643  13570  15392   -892  -2026  -2951       C  
ATOM   2496  CZ3 TRP B  47      17.213 -46.349  63.394  1.00122.95           C  
ANISOU 2496  CZ3 TRP B  47    19939  12618  14157   -861  -2318  -2596       C  
ATOM   2497  CH2 TRP B  47      17.981 -47.014  62.429  1.00128.81           C  
ANISOU 2497  CH2 TRP B  47    21117  13233  14591   -788  -2214  -2812       C  
ATOM   2498  N   VAL B  48      16.103 -46.183  67.912  1.00100.01           N  
ANISOU 2498  N   VAL B  48    15657   9658  12684  -1245  -1852  -1893       N  
ATOM   2499  CA  VAL B  48      16.335 -44.764  67.663  1.00 89.72           C  
ANISOU 2499  CA  VAL B  48    14383   8622  11085  -1029  -1879  -1714       C  
ATOM   2500  C   VAL B  48      17.347 -44.208  68.655  1.00 77.19           C  
ANISOU 2500  C   VAL B  48    12734   7065   9531   -900  -1487  -1406       C  
ATOM   2501  O   VAL B  48      18.180 -43.363  68.308  1.00 67.12           O  
ANISOU 2501  O   VAL B  48    11638   5904   7960   -698  -1358  -1287       O  
ATOM   2502  CB  VAL B  48      15.003 -43.994  67.728  1.00 83.15           C  
ANISOU 2502  CB  VAL B  48    13226   7990  10378  -1086  -2216  -1707       C  
ATOM   2503  CG1 VAL B  48      15.239 -42.502  67.546  1.00 76.90           C  
ANISOU 2503  CG1 VAL B  48    12470   7442   9308   -855  -2229  -1498       C  
ATOM   2504  CG2 VAL B  48      14.025 -44.535  66.702  1.00 88.86           C  
ANISOU 2504  CG2 VAL B  48    14000   8693  11072  -1201  -2654  -2042       C  
ATOM   2505  N   LEU B  49      17.291 -44.672  69.904  1.00 74.83           N  
ANISOU 2505  N   LEU B  49    12186   6656   9589  -1017  -1292  -1276       N  
ATOM   2506  CA  LEU B  49      18.213 -44.179  70.922  1.00 71.00           C  
ANISOU 2506  CA  LEU B  49    11631   6202   9143   -893   -961  -1001       C  
ATOM   2507  C   LEU B  49      19.660 -44.506  70.567  1.00 72.99           C  
ANISOU 2507  C   LEU B  49    12194   6341   9197   -734   -711  -1010       C  
ATOM   2508  O   LEU B  49      20.542 -43.643  70.652  1.00 73.77           O  
ANISOU 2508  O   LEU B  49    12341   6556   9133   -554   -536   -857       O  
ATOM   2509  CB  LEU B  49      17.844 -44.769  72.284  1.00 74.78           C  
ANISOU 2509  CB  LEU B  49    11847   6560  10007  -1050   -815   -878       C  
ATOM   2510  CG  LEU B  49      18.586 -44.236  73.508  1.00 76.36           C  
ANISOU 2510  CG  LEU B  49    11933   6813  10267   -937   -529   -596       C  
ATOM   2511  CD1 LEU B  49      18.472 -42.717  73.604  1.00 74.35           C  
ANISOU 2511  CD1 LEU B  49    11536   6836   9878   -807   -572   -450       C  
ATOM   2512  CD2 LEU B  49      18.034 -44.896  74.755  1.00 76.64           C  
ANISOU 2512  CD2 LEU B  49    11759   6719  10641  -1109   -414   -492       C  
ATOM   2513  N   ILE B  50      19.926 -45.749  70.162  1.00 74.71           N  
ANISOU 2513  N   ILE B  50    12611   6320   9454   -800   -683  -1202       N  
ATOM   2514  CA  ILE B  50      21.301 -46.150  69.876  1.00 74.07           C  
ANISOU 2514  CA  ILE B  50    12794   6111   9239   -642   -425  -1229       C  
ATOM   2515  C   ILE B  50      21.788 -45.533  68.574  1.00 77.49           C  
ANISOU 2515  C   ILE B  50    13515   6666   9263   -491   -451  -1339       C  
ATOM   2516  O   ILE B  50      22.948 -45.118  68.464  1.00 81.20           O  
ANISOU 2516  O   ILE B  50    14105   7163   9585   -314   -196  -1260       O  
ATOM   2517  CB  ILE B  50      21.414 -47.683  69.845  1.00 75.28           C  
ANISOU 2517  CB  ILE B  50    13082   5947   9576   -748   -379  -1410       C  
ATOM   2518  CG1 ILE B  50      20.987 -48.267  71.190  1.00 69.75           C  
ANISOU 2518  CG1 ILE B  50    12134   5103   9263   -892   -306  -1257       C  
ATOM   2519  CG2 ILE B  50      22.832 -48.101  69.492  1.00 71.72           C  
ANISOU 2519  CG2 ILE B  50    12888   5358   9004   -563   -114  -1463       C  
ATOM   2520  CD1 ILE B  50      20.752 -49.749  71.150  1.00 63.21           C  
ANISOU 2520  CD1 ILE B  50    11385   3971   8661  -1042   -310  -1427       C  
ATOM   2521  N   ALA B  51      20.919 -45.467  67.566  1.00 77.11           N  
ANISOU 2521  N   ALA B  51    13587   6687   9024   -556   -757  -1527       N  
ATOM   2522  CA  ALA B  51      21.310 -44.836  66.311  1.00 72.99           C  
ANISOU 2522  CA  ALA B  51    13389   6284   8058   -406   -789  -1611       C  
ATOM   2523  C   ALA B  51      21.622 -43.359  66.510  1.00 76.22           C  
ANISOU 2523  C   ALA B  51    13716   6921   8321   -257   -692  -1352       C  
ATOM   2524  O   ALA B  51      22.583 -42.837  65.935  1.00 79.15           O  
ANISOU 2524  O   ALA B  51    14324   7333   8417    -98   -475  -1315       O  
ATOM   2525  CB  ALA B  51      20.212 -45.023  65.266  1.00 71.09           C  
ANISOU 2525  CB  ALA B  51    13288   6087   7636   -495  -1199  -1857       C  
ATOM   2526  N   ALA B  52      20.813 -42.663  67.313  1.00 67.89           N  
ANISOU 2526  N   ALA B  52    12329   6004   7461   -314   -829  -1181       N  
ATOM   2527  CA  ALA B  52      21.084 -41.257  67.592  1.00 58.39           C  
ANISOU 2527  CA  ALA B  52    11033   4991   6161   -179   -733   -940       C  
ATOM   2528  C   ALA B  52      22.406 -41.081  68.329  1.00 64.42           C  
ANISOU 2528  C   ALA B  52    11750   5708   7018    -77   -335   -779       C  
ATOM   2529  O   ALA B  52      23.196 -40.187  68.001  1.00 71.16           O  
ANISOU 2529  O   ALA B  52    12724   6642   7670     66   -151   -677       O  
ATOM   2530  CB  ALA B  52      19.939 -40.649  68.399  1.00 58.64           C  
ANISOU 2530  CB  ALA B  52    10695   5157   6430   -262   -942   -814       C  
ATOM   2531  N   TYR B  53      22.664 -41.920  69.334  1.00 66.17           N  
ANISOU 2531  N   TYR B  53    11798   5791   7553   -147   -202   -754       N  
ATOM   2532  CA  TYR B  53      23.914 -41.810  70.078  1.00 65.92           C  
ANISOU 2532  CA  TYR B  53    11701   5714   7630    -35    126   -620       C  
ATOM   2533  C   TYR B  53      25.113 -42.165  69.208  1.00 72.26           C  
ANISOU 2533  C   TYR B  53    12798   6413   8243     87    355   -747       C  
ATOM   2534  O   TYR B  53      26.177 -41.546  69.325  1.00 71.79           O  
ANISOU 2534  O   TYR B  53    12733   6394   8151    220    612   -653       O  
ATOM   2535  CB  TYR B  53      23.869 -42.706  71.313  1.00 68.71           C  
ANISOU 2535  CB  TYR B  53    11850   5926   8330   -119    181   -563       C  
ATOM   2536  CG  TYR B  53      23.412 -42.016  72.578  1.00 69.00           C  
ANISOU 2536  CG  TYR B  53    11569   6087   8562   -152    167   -345       C  
ATOM   2537  CD1 TYR B  53      22.067 -41.966  72.927  1.00 70.82           C  
ANISOU 2537  CD1 TYR B  53    11611   6377   8918   -306    -48   -328       C  
ATOM   2538  CD2 TYR B  53      24.331 -41.426  73.431  1.00 65.07           C  
ANISOU 2538  CD2 TYR B  53    10949   5644   8133    -28    374   -178       C  
ATOM   2539  CE1 TYR B  53      21.655 -41.339  74.092  1.00 68.93           C  
ANISOU 2539  CE1 TYR B  53    11094   6250   8848   -330    -25   -141       C  
ATOM   2540  CE2 TYR B  53      23.932 -40.799  74.590  1.00 62.76           C  
ANISOU 2540  CE2 TYR B  53    10395   5462   7988    -50    365      1       C  
ATOM   2541  CZ  TYR B  53      22.595 -40.757  74.919  1.00 63.32           C  
ANISOU 2541  CZ  TYR B  53    10306   5591   8162   -199    182     23       C  
ATOM   2542  OH  TYR B  53      22.212 -40.127  76.081  1.00 61.54           O  
ANISOU 2542  OH  TYR B  53     9833   5476   8074   -215    208    190       O  
ATOM   2543  N   VAL B  54      24.964 -43.155  68.328  1.00 75.44           N  
ANISOU 2543  N   VAL B  54    13452   6675   8536     40    278   -981       N  
ATOM   2544  CA  VAL B  54      26.080 -43.549  67.472  1.00 72.98           C  
ANISOU 2544  CA  VAL B  54    13432   6256   8043    158    522  -1128       C  
ATOM   2545  C   VAL B  54      26.352 -42.480  66.422  1.00 75.48           C  
ANISOU 2545  C   VAL B  54    13981   6725   7972    262    590  -1114       C  
ATOM   2546  O   VAL B  54      27.505 -42.111  66.173  1.00 77.35           O  
ANISOU 2546  O   VAL B  54    14309   6957   8125    390    912  -1087       O  
ATOM   2547  CB  VAL B  54      25.809 -44.918  66.825  1.00 73.32           C  
ANISOU 2547  CB  VAL B  54    13698   6092   8070     78    421  -1404       C  
ATOM   2548  CG1 VAL B  54      26.865 -45.220  65.773  1.00 75.44           C  
ANISOU 2548  CG1 VAL B  54    14211   6340   8114    204    661  -1543       C  
ATOM   2549  CG2 VAL B  54      25.778 -46.002  67.883  1.00 63.14           C  
ANISOU 2549  CG2 VAL B  54    12195   4616   7179     -3    436  -1384       C  
ATOM   2550  N   ALA B  55      25.295 -41.969  65.785  1.00 75.65           N  
ANISOU 2550  N   ALA B  55    14104   6876   7762    212    289  -1132       N  
ATOM   2551  CA  ALA B  55      25.474 -40.932  64.774  1.00 74.02           C  
ANISOU 2551  CA  ALA B  55    14170   6802   7154    320    332  -1090       C  
ATOM   2552  C   ALA B  55      26.142 -39.692  65.358  1.00 74.32           C  
ANISOU 2552  C   ALA B  55    14032   6948   7258    412    576   -832       C  
ATOM   2553  O   ALA B  55      27.016 -39.091  64.721  1.00 76.40           O  
ANISOU 2553  O   ALA B  55    14509   7226   7295    519    855   -798       O  
ATOM   2554  CB  ALA B  55      24.127 -40.574  64.145  1.00 73.37           C  
ANISOU 2554  CB  ALA B  55    14182   6841   6853    270   -100  -1131       C  
ATOM   2555  N   VAL B  56      25.748 -39.291  66.570  1.00 70.30           N  
ANISOU 2555  N   VAL B  56    13142   6507   7061    363    494   -659       N  
ATOM   2556  CA  VAL B  56      26.380 -38.139  67.209  1.00 63.55           C  
ANISOU 2556  CA  VAL B  56    12102   5743   6302    440    710   -441       C  
ATOM   2557  C   VAL B  56      27.825 -38.454  67.573  1.00 66.30           C  
ANISOU 2557  C   VAL B  56    12395   5984   6811    511   1094   -456       C  
ATOM   2558  O   VAL B  56      28.720 -37.617  67.408  1.00 74.30           O  
ANISOU 2558  O   VAL B  56    13435   7029   7767    597   1370   -373       O  
ATOM   2559  CB  VAL B  56      25.572 -37.704  68.444  1.00 58.36           C  
ANISOU 2559  CB  VAL B  56    11064   5180   5930    372    524   -283       C  
ATOM   2560  CG1 VAL B  56      26.426 -36.842  69.364  1.00 65.09           C  
ANISOU 2560  CG1 VAL B  56    11687   6079   6967    440    775   -107       C  
ATOM   2561  CG2 VAL B  56      24.314 -36.964  68.025  1.00 56.74           C  
ANISOU 2561  CG2 VAL B  56    10880   5109   5568    350    198   -235       C  
ATOM   2562  N   PHE B  57      28.072 -39.661  68.084  1.00 64.45           N  
ANISOU 2562  N   PHE B  57    12071   5610   6808    480   1115   -564       N  
ATOM   2563  CA  PHE B  57      29.425 -40.061  68.458  1.00 63.90           C  
ANISOU 2563  CA  PHE B  57    11923   5429   6927    572   1437   -596       C  
ATOM   2564  C   PHE B  57      30.381 -39.937  67.278  1.00 71.04           C  
ANISOU 2564  C   PHE B  57    13105   6300   7588    662   1733   -708       C  
ATOM   2565  O   PHE B  57      31.461 -39.350  67.394  1.00 68.11           O  
ANISOU 2565  O   PHE B  57    12577   5993   7308    727   2006   -623       O  
ATOM   2566  CB  PHE B  57      29.402 -41.495  68.996  1.00 65.92           C  
ANISOU 2566  CB  PHE B  57    12113   5512   7423    535   1370   -705       C  
ATOM   2567  CG  PHE B  57      30.739 -42.004  69.457  1.00 64.65           C  
ANISOU 2567  CG  PHE B  57    11708   5358   7498    623   1590   -693       C  
ATOM   2568  CD1 PHE B  57      31.233 -41.662  70.704  1.00 68.34           C  
ANISOU 2568  CD1 PHE B  57    11832   5903   8233    664   1622   -537       C  
ATOM   2569  CD2 PHE B  57      31.488 -42.851  68.655  1.00 60.30           C  
ANISOU 2569  CD2 PHE B  57    11269   4739   6903    668   1732   -852       C  
ATOM   2570  CE1 PHE B  57      32.456 -42.138  71.137  1.00 65.58           C  
ANISOU 2570  CE1 PHE B  57    11263   5557   8097    755   1762   -549       C  
ATOM   2571  CE2 PHE B  57      32.712 -43.331  69.085  1.00 57.29           C  
ANISOU 2571  CE2 PHE B  57    10655   4350   6764    759   1898   -855       C  
ATOM   2572  CZ  PHE B  57      33.196 -42.973  70.327  1.00 56.98           C  
ANISOU 2572  CZ  PHE B  57    10281   4384   6987    805   1897   -707       C  
ATOM   2573  N   VAL B  58      29.997 -40.492  66.128  1.00 75.61           N  
ANISOU 2573  N   VAL B  58    14012   6839   7876    637   1650   -873       N  
ATOM   2574  CA  VAL B  58      30.860 -40.448  64.949  1.00 77.30           C  
ANISOU 2574  CA  VAL B  58    14429   7082   7860    695   1906   -934       C  
ATOM   2575  C   VAL B  58      31.061 -39.011  64.480  1.00 80.99           C  
ANISOU 2575  C   VAL B  58    15019   7656   8096    740   2063   -781       C  
ATOM   2576  O   VAL B  58      32.193 -38.540  64.322  1.00 82.77           O  
ANISOU 2576  O   VAL B  58    15145   7905   8400    781   2390   -706       O  
ATOM   2577  CB  VAL B  58      30.280 -41.324  63.827  1.00 80.99           C  
ANISOU 2577  CB  VAL B  58    15228   7498   8048    656   1735  -1139       C  
ATOM   2578  CG1 VAL B  58      31.091 -41.156  62.555  1.00 81.08           C  
ANISOU 2578  CG1 VAL B  58    15478   7541   7789    716   1998  -1178       C  
ATOM   2579  CG2 VAL B  58      30.246 -42.771  64.266  1.00 81.14           C  
ANISOU 2579  CG2 VAL B  58    15108   7384   8339    609   1638  -1288       C  
ATOM   2580  N   VAL B  59      29.960 -38.295  64.248  1.00 78.74           N  
ANISOU 2580  N   VAL B  59    14940   7434   7542    726   1817   -730       N  
ATOM   2581  CA  VAL B  59      30.060 -36.949  63.691  1.00 74.23           C  
ANISOU 2581  CA  VAL B  59    14524   6963   6719    773   1935   -561       C  
ATOM   2582  C   VAL B  59      30.849 -36.031  64.616  1.00 76.80           C  
ANISOU 2582  C   VAL B  59    14528   7312   7341    798   2198   -388       C  
ATOM   2583  O   VAL B  59      31.642 -35.199  64.157  1.00 78.37           O  
ANISOU 2583  O   VAL B  59    14743   7527   7508    819   2471   -270       O  
ATOM   2584  CB  VAL B  59      28.655 -36.386  63.408  1.00 65.30           C  
ANISOU 2584  CB  VAL B  59    13528   5944   5337    751   1515   -484       C  
ATOM   2585  CG1 VAL B  59      28.734 -34.893  63.151  1.00 62.79           C  
ANISOU 2585  CG1 VAL B  59    13303   5709   4846    812   1626   -258       C  
ATOM   2586  CG2 VAL B  59      28.026 -37.110  62.236  1.00 65.04           C  
ANISOU 2586  CG2 VAL B  59    13905   5889   4920    749   1290   -684       C  
ATOM   2587  N   ALA B  60      30.641 -36.155  65.928  1.00 69.65           N  
ANISOU 2587  N   ALA B  60    13223   6429   6813    759   2054   -326       N  
ATOM   2588  CA  ALA B  60      31.355 -35.293  66.865  1.00 59.64           C  
ANISOU 2588  CA  ALA B  60    11626   5195   5839    780   2251   -180       C  
ATOM   2589  C   ALA B  60      32.855 -35.571  66.860  1.00 67.79           C  
ANISOU 2589  C   ALA B  60    12510   6168   7078    811   2617   -238       C  
ATOM   2590  O   ALA B  60      33.664 -34.645  66.987  1.00 67.90           O  
ANISOU 2590  O   ALA B  60    12367   6213   7220    812   2849   -131       O  
ATOM   2591  CB  ALA B  60      30.785 -35.463  68.273  1.00 56.32           C  
ANISOU 2591  CB  ALA B  60    10821   4826   5751    731   1988   -103       C  
ATOM   2592  N   LEU B  61      33.247 -36.838  66.710  1.00 75.24           N  
ANISOU 2592  N   LEU B  61    13425   7055   8109    808   2617   -384       N  
ATOM   2593  CA  LEU B  61      34.668 -37.170  66.737  1.00 73.45           C  
ANISOU 2593  CA  LEU B  61    12963   6815   8128    826   2883   -426       C  
ATOM   2594  C   LEU B  61      35.363 -36.740  65.451  1.00 73.08           C  
ANISOU 2594  C   LEU B  61    13146   6744   7876    824   3171   -434       C  
ATOM   2595  O   LEU B  61      36.460 -36.170  65.493  1.00 74.20           O  
ANISOU 2595  O   LEU B  61    13092   6888   8212    817   3433   -388       O  
ATOM   2596  CB  LEU B  61      34.854 -38.667  66.977  1.00 75.37           C  
ANISOU 2596  CB  LEU B  61    13114   6993   8531    844   2786   -579       C  
ATOM   2597  CG  LEU B  61      34.617 -39.147  68.410  1.00 71.23           C  
ANISOU 2597  CG  LEU B  61    12268   6476   8319    850   2566   -543       C  
ATOM   2598  CD1 LEU B  61      35.021 -40.602  68.549  1.00 69.83           C  
ANISOU 2598  CD1 LEU B  61    12014   6209   8309    884   2519   -680       C  
ATOM   2599  CD2 LEU B  61      35.367 -38.280  69.410  1.00 69.53           C  
ANISOU 2599  CD2 LEU B  61    11684   6355   8379    871   2649   -421       C  
ATOM   2600  N   VAL B  62      34.743 -37.001  64.299  1.00 71.09           N  
ANISOU 2600  N   VAL B  62    13306   6464   7243    823   3108   -499       N  
ATOM   2601  CA  VAL B  62      35.341 -36.599  63.028  1.00 70.75           C  
ANISOU 2601  CA  VAL B  62    13517   6389   6977    824   3367   -495       C  
ATOM   2602  C   VAL B  62      35.355 -35.080  62.896  1.00 75.01           C  
ANISOU 2602  C   VAL B  62    14104   6947   7448    811   3477   -300       C  
ATOM   2603  O   VAL B  62      36.391 -34.475  62.592  1.00 76.82           O  
ANISOU 2603  O   VAL B  62    14255   7132   7802    793   3787   -252       O  
ATOM   2604  CB  VAL B  62      34.599 -37.257  61.852  1.00 64.94           C  
ANISOU 2604  CB  VAL B  62    13217   5632   5827    835   3216   -616       C  
ATOM   2605  CG1 VAL B  62      35.121 -36.718  60.532  1.00 64.19           C  
ANISOU 2605  CG1 VAL B  62    13419   5505   5464    846   3468   -585       C  
ATOM   2606  CG2 VAL B  62      34.745 -38.768  61.913  1.00 62.19           C  
ANISOU 2606  CG2 VAL B  62    12809   5228   5592    842   3152   -827       C  
ATOM   2607  N   GLY B  63      34.205 -34.440  63.116  1.00 75.58           N  
ANISOU 2607  N   GLY B  63    14298   7074   7343    819   3216   -196       N  
ATOM   2608  CA  GLY B  63      34.137 -32.995  62.957  1.00 72.92           C  
ANISOU 2608  CA  GLY B  63    14015   6746   6947    821   3285    -15       C  
ATOM   2609  C   GLY B  63      35.088 -32.253  63.878  1.00 68.96           C  
ANISOU 2609  C   GLY B  63    13114   6226   6862    789   3508     66       C  
ATOM   2610  O   GLY B  63      35.832 -31.370  63.444  1.00 72.70           O  
ANISOU 2610  O   GLY B  63    13591   6634   7398    769   3759    134       O  
ATOM   2611  N   ASN B  64      35.076 -32.600  65.168  1.00 61.18           N  
ANISOU 2611  N   ASN B  64    11778   5292   6176    782   3406     47       N  
ATOM   2612  CA  ASN B  64      35.918 -31.897  66.131  1.00 65.09           C  
ANISOU 2612  CA  ASN B  64    11871   5793   7069    751   3551    110       C  
ATOM   2613  C   ASN B  64      37.402 -32.175  65.931  1.00 72.20           C  
ANISOU 2613  C   ASN B  64    12570   6637   8224    716   3846     25       C  
ATOM   2614  O   ASN B  64      38.232 -31.339  66.306  1.00 75.75           O  
ANISOU 2614  O   ASN B  64    12773   7061   8947    671   4013     70       O  
ATOM   2615  CB  ASN B  64      35.482 -32.253  67.555  1.00 69.30           C  
ANISOU 2615  CB  ASN B  64    12091   6412   7829    764   3325    105       C  
ATOM   2616  CG  ASN B  64      34.188 -31.562  67.949  1.00 78.84           C  
ANISOU 2616  CG  ASN B  64    13407   7674   8876    789   3099    213       C  
ATOM   2617  OD1 ASN B  64      34.060 -30.348  67.803  1.00 80.12           O  
ANISOU 2617  OD1 ASN B  64    13606   7836   9000    782   3143    336       O  
ATOM   2618  ND2 ASN B  64      33.221 -32.331  68.440  1.00 84.40           N  
ANISOU 2618  ND2 ASN B  64    14134   8408   9526    815   2822    155       N  
ATOM   2619  N   THR B  65      37.762 -33.323  65.356  1.00 77.67           N  
ANISOU 2619  N   THR B  65    13353   7307   8850    735   3903   -115       N  
ATOM   2620  CA  THR B  65      39.157 -33.530  64.981  1.00 82.07           C  
ANISOU 2620  CA  THR B  65    13759   7807   9615    712   4206   -205       C  
ATOM   2621  C   THR B  65      39.519 -32.695  63.761  1.00 89.02           C  
ANISOU 2621  C   THR B  65    14931   8589  10303    678   4484   -150       C  
ATOM   2622  O   THR B  65      40.631 -32.162  63.673  1.00 95.25           O  
ANISOU 2622  O   THR B  65    15545   9315  11331    628   4762   -158       O  
ATOM   2623  CB  THR B  65      39.432 -35.011  64.716  1.00 83.08           C  
ANISOU 2623  CB  THR B  65    13899   7929   9739    760   4190   -383       C  
ATOM   2624  OG1 THR B  65      38.334 -35.587  64.003  1.00 88.40           O  
ANISOU 2624  OG1 THR B  65    14972   8595  10020    788   4015   -417       O  
ATOM   2625  CG2 THR B  65      39.644 -35.761  66.020  1.00 76.51           C  
ANISOU 2625  CG2 THR B  65    12666   7159   9246    799   3998   -449       C  
ATOM   2626  N   LEU B  66      38.593 -32.579  62.806  1.00 87.06           N  
ANISOU 2626  N   LEU B  66    15130   8324   9624    707   4397   -105       N  
ATOM   2627  CA  LEU B  66      38.840 -31.750  61.632  1.00 87.46           C  
ANISOU 2627  CA  LEU B  66    15496   8281   9452    694   4627    -39       C  
ATOM   2628  C   LEU B  66      39.038 -30.289  62.015  1.00 82.47           C  
ANISOU 2628  C   LEU B  66    14734   7605   8997    657   4716    101       C  
ATOM   2629  O   LEU B  66      39.848 -29.584  61.402  1.00 86.33           O  
ANISOU 2629  O   LEU B  66    15281   7985   9535    618   5023    125       O  
ATOM   2630  CB  LEU B  66      37.688 -31.884  60.639  1.00 85.54           C  
ANISOU 2630  CB  LEU B  66    15743   8059   8700    751   4424    -17       C  
ATOM   2631  CG  LEU B  66      37.587 -33.205  59.879  1.00 82.61           C  
ANISOU 2631  CG  LEU B  66    15603   7696   8089    781   4390   -180       C  
ATOM   2632  CD1 LEU B  66      36.517 -33.111  58.805  1.00 85.81           C  
ANISOU 2632  CD1 LEU B  66    16501   8120   7981    832   4181   -153       C  
ATOM   2633  CD2 LEU B  66      38.929 -33.572  59.268  1.00 78.25           C  
ANISOU 2633  CD2 LEU B  66    15009   7062   7662    757   4787   -284       C  
ATOM   2634  N   VAL B  67      38.302 -29.813  63.022  1.00 77.67           N  
ANISOU 2634  N   VAL B  67    13952   7068   8489    669   4461    183       N  
ATOM   2635  CA  VAL B  67      38.464 -28.429  63.464  1.00 76.76           C  
ANISOU 2635  CA  VAL B  67    13688   6912   8565    642   4524    290       C  
ATOM   2636  C   VAL B  67      39.900 -28.179  63.907  1.00 83.41           C  
ANISOU 2636  C   VAL B  67    14166   7680   9845    558   4813    231       C  
ATOM   2637  O   VAL B  67      40.528 -27.188  63.517  1.00 93.00           O  
ANISOU 2637  O   VAL B  67    15403   8782  11150    514   5060    265       O  
ATOM   2638  CB  VAL B  67      37.465 -28.101  64.587  1.00 73.05           C  
ANISOU 2638  CB  VAL B  67    13047   6551   8160    674   4198    358       C  
ATOM   2639  CG1 VAL B  67      37.793 -26.754  65.209  1.00 71.49           C  
ANISOU 2639  CG1 VAL B  67    12616   6317   8231    643   4272    426       C  
ATOM   2640  CG2 VAL B  67      36.044 -28.117  64.054  1.00 72.87           C  
ANISOU 2640  CG2 VAL B  67    13376   6602   7711    746   3907    418       C  
ATOM   2641  N   CYS B  68      40.434 -29.072  64.745  1.00 83.48           N  
ANISOU 2641  N   CYS B  68    13824   7758  10135    538   4769    130       N  
ATOM   2642  CA  CYS B  68      41.818 -28.947  65.189  1.00 84.46           C  
ANISOU 2642  CA  CYS B  68    13565   7842  10683    465   4989     44       C  
ATOM   2643  C   CYS B  68      42.795 -29.065  64.025  1.00 89.11           C  
ANISOU 2643  C   CYS B  68    14307   8311  11239    430   5359    -30       C  
ATOM   2644  O   CYS B  68      43.854 -28.428  64.037  1.00 91.79           O  
ANISOU 2644  O   CYS B  68    14451   8557  11869    354   5617    -67       O  
ATOM   2645  CB  CYS B  68      42.121 -30.004  66.253  1.00 81.04           C  
ANISOU 2645  CB  CYS B  68    12748   7536  10507    487   4808    -65       C  
ATOM   2646  SG  CYS B  68      41.149 -29.850  67.775  1.00 81.17           S  
ANISOU 2646  SG  CYS B  68    12529   7697  10616    518   4411     12       S  
ATOM   2647  N   LEU B  69      42.465 -29.873  63.015  1.00 87.33           N  
ANISOU 2647  N   LEU B  69    14431   8082  10667    482   5394    -66       N  
ATOM   2648  CA  LEU B  69      43.347 -29.990  61.857  1.00 86.06           C  
ANISOU 2648  CA  LEU B  69    14451   7810  10439    455   5764   -136       C  
ATOM   2649  C   LEU B  69      43.305 -28.732  60.998  1.00 89.09           C  
ANISOU 2649  C   LEU B  69    15149   8060  10641    425   5976    -16       C  
ATOM   2650  O   LEU B  69      44.349 -28.218  60.583  1.00 95.11           O  
ANISOU 2650  O   LEU B  69    15857   8697  11583    355   6333    -47       O  
ATOM   2651  CB  LEU B  69      42.973 -31.216  61.023  1.00 88.03           C  
ANISOU 2651  CB  LEU B  69    15003   8097  10350    524   5725   -223       C  
ATOM   2652  CG  LEU B  69      43.332 -32.592  61.587  1.00 83.86           C  
ANISOU 2652  CG  LEU B  69    14193   7655  10016    566   5623   -389       C  
ATOM   2653  CD1 LEU B  69      42.474 -33.669  60.943  1.00 81.61           C  
ANISOU 2653  CD1 LEU B  69    14253   7411   9343    642   5453   -455       C  
ATOM   2654  CD2 LEU B  69      44.808 -32.890  61.376  1.00 84.70           C  
ANISOU 2654  CD2 LEU B  69    14051   7699  10433    535   5964   -532       C  
ATOM   2655  N   ALA B  70      42.103 -28.222  60.719  1.00 88.51           N  
ANISOU 2655  N   ALA B  70    15402   8011  10216    484   5756    114       N  
ATOM   2656  CA  ALA B  70      41.984 -27.043  59.868  1.00 86.96           C  
ANISOU 2656  CA  ALA B  70    15530   7700   9808    484   5923    230       C  
ATOM   2657  C   ALA B  70      42.727 -25.851  60.461  1.00 88.20           C  
ANISOU 2657  C   ALA B  70    15396   7758  10357    404   6110    262       C  
ATOM   2658  O   ALA B  70      43.312 -25.047  59.726  1.00 88.80           O  
ANISOU 2658  O   ALA B  70    15633   7688  10418    363   6434    296       O  
ATOM   2659  CB  ALA B  70      40.512 -26.696  59.651  1.00 84.76           C  
ANISOU 2659  CB  ALA B  70    15575   7502   9128    577   5578    353       C  
ATOM   2660  N   VAL B  71      42.713 -25.713  61.787  1.00 93.46           N  
ANISOU 2660  N   VAL B  71    15643   8495  11370    380   5912    245       N  
ATOM   2661  CA  VAL B  71      43.437 -24.603  62.398  1.00 98.44           C  
ANISOU 2661  CA  VAL B  71    15982   9032  12390    299   6067    245       C  
ATOM   2662  C   VAL B  71      44.937 -24.865  62.413  1.00105.04           C  
ANISOU 2662  C   VAL B  71    16525   9777  13607    195   6398    105       C  
ATOM   2663  O   VAL B  71      45.736 -23.929  62.292  1.00105.59           O  
ANISOU 2663  O   VAL B  71    16510   9701  13910    114   6680     91       O  
ATOM   2664  CB  VAL B  71      42.897 -24.337  63.813  1.00 92.62           C  
ANISOU 2664  CB  VAL B  71    14911   8408  11874    312   5731    265       C  
ATOM   2665  CG1 VAL B  71      43.726 -23.266  64.497  1.00 94.77           C  
ANISOU 2665  CG1 VAL B  71    14854   8582  12571    221   5878    230       C  
ATOM   2666  CG2 VAL B  71      41.433 -23.938  63.752  1.00 87.32           C  
ANISOU 2666  CG2 VAL B  71    14511   7824  10845    415   5433    394       C  
ATOM   2667  N   TRP B  72      45.344 -26.126  62.567  1.00108.14           N  
ANISOU 2667  N   TRP B  72    16747  10258  14084    201   6367    -12       N  
ATOM   2668  CA  TRP B  72      46.765 -26.452  62.545  1.00105.68           C  
ANISOU 2668  CA  TRP B  72    16136   9882  14134    121   6664   -167       C  
ATOM   2669  C   TRP B  72      47.356 -26.275  61.152  1.00105.42           C  
ANISOU 2669  C   TRP B  72    16431   9691  13933     89   7097   -177       C  
ATOM   2670  O   TRP B  72      48.503 -25.837  61.009  1.00110.73           O  
ANISOU 2670  O   TRP B  72    16919  10233  14920     -5   7436   -260       O  
ATOM   2671  CB  TRP B  72      46.982 -27.882  63.035  1.00104.48           C  
ANISOU 2671  CB  TRP B  72    15730   9881  14086    170   6497   -298       C  
ATOM   2672  CG  TRP B  72      48.408 -28.336  62.951  1.00107.76           C  
ANISOU 2672  CG  TRP B  72    15838  10250  14855    121   6777   -477       C  
ATOM   2673  CD1 TRP B  72      49.466 -27.848  63.662  1.00105.03           C  
ANISOU 2673  CD1 TRP B  72    15049   9863  14995     37   6873   -579       C  
ATOM   2674  CD2 TRP B  72      48.933 -29.375  62.114  1.00115.85           C  
ANISOU 2674  CD2 TRP B  72    16965  11267  15786    160   6987   -596       C  
ATOM   2675  NE1 TRP B  72      50.616 -28.518  63.319  1.00111.20           N  
ANISOU 2675  NE1 TRP B  72    15638  10612  16001     27   7128   -752       N  
ATOM   2676  CE2 TRP B  72      50.316 -29.460  62.371  1.00118.61           C  
ANISOU 2676  CE2 TRP B  72    16905  11570  16591    105   7212   -763       C  
ATOM   2677  CE3 TRP B  72      48.368 -30.241  61.173  1.00120.14           C  
ANISOU 2677  CE3 TRP B  72    17903  11835  15908    241   6999   -595       C  
ATOM   2678  CZ2 TRP B  72      51.142 -30.376  61.721  1.00124.59           C  
ANISOU 2678  CZ2 TRP B  72    17630  12305  17402    136   7464   -921       C  
ATOM   2679  CZ3 TRP B  72      49.189 -31.150  60.529  1.00122.48           C  
ANISOU 2679  CZ3 TRP B  72    18182  12108  16245    267   7249   -755       C  
ATOM   2680  CH2 TRP B  72      50.561 -31.210  60.806  1.00124.48           C  
ANISOU 2680  CH2 TRP B  72    18018  12316  16964    219   7486   -912       C  
ATOM   2681  N   ARG B  73      46.586 -26.608  60.114  1.00102.01           N  
ANISOU 2681  N   ARG B  73    16489   9266  13004    166   7091   -102       N  
ATOM   2682  CA  ARG B  73      47.084 -26.512  58.745  1.00101.68           C  
ANISOU 2682  CA  ARG B  73    16809   9086  12740    148   7494   -107       C  
ATOM   2683  C   ARG B  73      47.150 -25.062  58.278  1.00105.01           C  
ANISOU 2683  C   ARG B  73    17443   9340  13117    101   7725     15       C  
ATOM   2684  O   ARG B  73      48.225 -24.548  57.947  1.00112.90           O  
ANISOU 2684  O   ARG B  73    18357  10181  14360      6   8132    -38       O  
ATOM   2685  CB  ARG B  73      46.194 -27.334  57.812  1.00 97.80           C  
ANISOU 2685  CB  ARG B  73    16788   8668  11705    252   7369    -76       C  
ATOM   2686  CG  ARG B  73      46.705 -27.424  56.386  1.00102.84           C  
ANISOU 2686  CG  ARG B  73    17817   9186  12072    245   7773    -98       C  
ATOM   2687  CD  ARG B  73      45.645 -27.993  55.454  1.00105.82           C  
ANISOU 2687  CD  ARG B  73    18717   9634  11855    354   7588    -50       C  
ATOM   2688  NE  ARG B  73      46.191 -28.339  54.144  1.00116.39           N  
ANISOU 2688  NE  ARG B  73    20409  10884  12930    356   7961   -108       N  
ATOM   2689  CZ  ARG B  73      45.452 -28.569  53.063  1.00122.33           C  
ANISOU 2689  CZ  ARG B  73    21700  11654  13128    439   7899    -60       C  
ATOM   2690  NH1 ARG B  73      44.130 -28.481  53.130  1.00119.23           N  
ANISOU 2690  NH1 ARG B  73    21536  11364  12402    525   7465     42       N  
ATOM   2691  NH2 ARG B  73      46.034 -28.881  51.913  1.00128.90           N  
ANISOU 2691  NH2 ARG B  73    22838  12403  13735    438   8265   -124       N  
ATOM   2692  N   ASN B  74      46.004 -24.389  58.240  1.00100.71           N  
ANISOU 2692  N   ASN B  74    17170   8827  12266    173   7474    171       N  
ATOM   2693  CA  ASN B  74      45.918 -23.028  57.723  1.00101.25           C  
ANISOU 2693  CA  ASN B  74    17495   8752  12225    159   7661    300       C  
ATOM   2694  C   ASN B  74      46.444 -22.058  58.775  1.00104.46           C  
ANISOU 2694  C   ASN B  74    17474   9092  13125     73   7695    276       C  
ATOM   2695  O   ASN B  74      45.835 -21.892  59.837  1.00104.60           O  
ANISOU 2695  O   ASN B  74    17248   9223  13271    103   7341    295       O  
ATOM   2696  CB  ASN B  74      44.476 -22.710  57.343  1.00100.13           C  
ANISOU 2696  CB  ASN B  74    17763   8696  11586    284   7336    461       C  
ATOM   2697  CG  ASN B  74      44.357 -21.449  56.529  1.00 99.57           C  
ANISOU 2697  CG  ASN B  74    18055   8482  11293    294   7546    606       C  
ATOM   2698  OD1 ASN B  74      45.190 -20.550  56.633  1.00100.72           O  
ANISOU 2698  OD1 ASN B  74    18058   8471  11741    203   7865    601       O  
ATOM   2699  ND2 ASN B  74      43.320 -21.373  55.705  1.00 98.55           N  
ANISOU 2699  ND2 ASN B  74    18402   8405  10637    406   7363    733       N  
ATOM   2700  N   HIS B  75      47.582 -21.419  58.488  1.00107.21           N  
ANISOU 2700  N   HIS B  75    17728   9253  13755    -38   8129    221       N  
ATOM   2701  CA  HIS B  75      48.177 -20.492  59.443  1.00104.50           C  
ANISOU 2701  CA  HIS B  75    16975   8829  13903   -133   8182    167       C  
ATOM   2702  C   HIS B  75      47.446 -19.159  59.513  1.00 98.10           C  
ANISOU 2702  C   HIS B  75    16343   7968  12961    -95   8101    316       C  
ATOM   2703  O   HIS B  75      47.597 -18.438  60.505  1.00 95.27           O  
ANISOU 2703  O   HIS B  75    15645   7596  12958   -142   8009    278       O  
ATOM   2704  CB  HIS B  75      49.649 -20.257  59.104  1.00114.77           C  
ANISOU 2704  CB  HIS B  75    18098   9935  15575   -273   8682     39       C  
ATOM   2705  CG  HIS B  75      50.473 -21.507  59.105  1.00119.30           C  
ANISOU 2705  CG  HIS B  75    18425  10565  16338   -309   8775   -129       C  
ATOM   2706  ND1 HIS B  75      51.130 -21.963  60.228  1.00118.26           N  
ANISOU 2706  ND1 HIS B  75    17731  10513  16688   -365   8629   -293       N  
ATOM   2707  CD2 HIS B  75      50.739 -22.401  58.124  1.00124.68           C  
ANISOU 2707  CD2 HIS B  75    19345  11247  16783   -286   8989   -165       C  
ATOM   2708  CE1 HIS B  75      51.769 -23.082  59.936  1.00120.00           C  
ANISOU 2708  CE1 HIS B  75    17840  10783  16970   -367   8748   -420       C  
ATOM   2709  NE2 HIS B  75      51.547 -23.370  58.665  1.00123.98           N  
ANISOU 2709  NE2 HIS B  75    18822  11237  17048   -322   8978   -350       N  
ATOM   2710  N   HIS B  76      46.663 -18.811  58.489  1.00 99.44           N  
ANISOU 2710  N   HIS B  76    17037   8119  12628     -7   8121    479       N  
ATOM   2711  CA  HIS B  76      45.861 -17.597  58.558  1.00101.75           C  
ANISOU 2711  CA  HIS B  76    17500   8397  12765     48   7996    632       C  
ATOM   2712  C   HIS B  76      44.671 -17.763  59.489  1.00102.50           C  
ANISOU 2712  C   HIS B  76    17458   8710  12776    147   7462    674       C  
ATOM   2713  O   HIS B  76      44.113 -16.762  59.952  1.00102.64           O  
ANISOU 2713  O   HIS B  76    17439   8744  12815    176   7317    759       O  
ATOM   2714  CB  HIS B  76      45.380 -17.195  57.164  1.00107.50           C  
ANISOU 2714  CB  HIS B  76    18835   9046  12964    118   8153    802       C  
ATOM   2715  CG  HIS B  76      46.487 -16.998  56.177  1.00116.45           C  
ANISOU 2715  CG  HIS B  76    20157   9956  14131     25   8710    777       C  
ATOM   2716  ND1 HIS B  76      47.225 -18.047  55.674  1.00119.18           N  
ANISOU 2716  ND1 HIS B  76    20509  10282  14493    -20   8934    659       N  
ATOM   2717  CD2 HIS B  76      46.977 -15.877  55.595  1.00120.89           C  
ANISOU 2717  CD2 HIS B  76    20914  10304  14714    -36   9107    857       C  
ATOM   2718  CE1 HIS B  76      48.126 -17.579  54.829  1.00123.46           C  
ANISOU 2718  CE1 HIS B  76    21232  10609  15068   -105   9451    661       C  
ATOM   2719  NE2 HIS B  76      47.997 -16.266  54.762  1.00125.60           N  
ANISOU 2719  NE2 HIS B  76    21629  10752  15342   -118   9570    784       N  
ATOM   2720  N   MET B  77      44.278 -19.003  59.769  1.00104.80           N  
ANISOU 2720  N   MET B  77    17674   9167  12980    197   7184    615       N  
ATOM   2721  CA  MET B  77      43.159 -19.311  60.646  1.00 98.42           C  
ANISOU 2721  CA  MET B  77    16734   8565  12095    284   6697    644       C  
ATOM   2722  C   MET B  77      43.533 -19.297  62.122  1.00 97.07           C  
ANISOU 2722  C   MET B  77    16018   8449  12416    224   6554    532       C  
ATOM   2723  O   MET B  77      42.655 -19.512  62.966  1.00100.92           O  
ANISOU 2723  O   MET B  77    16365   9103  12878    288   6174    551       O  
ATOM   2724  CB  MET B  77      42.571 -20.678  60.278  1.00 95.93           C  
ANISOU 2724  CB  MET B  77    16596   8387  11466    356   6479    626       C  
ATOM   2725  CG  MET B  77      41.776 -20.695  58.980  1.00 99.71           C  
ANISOU 2725  CG  MET B  77    17635   8871  11380    450   6446    747       C  
ATOM   2726  SD  MET B  77      40.785 -22.193  58.824  1.00100.88           S  
ANISOU 2726  SD  MET B  77    17942   9211  11178    544   6063    713       S  
ATOM   2727  CE  MET B  77      39.339 -21.735  59.774  1.00 99.62           C  
ANISOU 2727  CE  MET B  77    17662   9231  10957    628   5551    804       C  
ATOM   2728  N   ARG B  78      44.796 -19.038  62.456  1.00 95.57           N  
ANISOU 2728  N   ARG B  78    15520   8124  12669    102   6842    412       N  
ATOM   2729  CA  ARG B  78      45.250 -19.070  63.846  1.00 97.26           C  
ANISOU 2729  CA  ARG B  78    15213   8385  13356     39   6692    290       C  
ATOM   2730  C   ARG B  78      44.981 -17.724  64.522  1.00101.05           C  
ANISOU 2730  C   ARG B  78    15566   8832  13995     34   6630    327       C  
ATOM   2731  O   ARG B  78      45.878 -17.023  64.990  1.00107.68           O  
ANISOU 2731  O   ARG B  78    16127   9546  15240    -70   6817    228       O  
ATOM   2732  CB  ARG B  78      46.726 -19.443  63.907  1.00 98.82           C  
ANISOU 2732  CB  ARG B  78    15111   8471  13967    -92   6988    123       C  
ATOM   2733  CG  ARG B  78      47.044 -20.800  63.298  1.00 98.36           C  
ANISOU 2733  CG  ARG B  78    15133   8464  13774    -83   7058     70       C  
ATOM   2734  CD  ARG B  78      48.483 -21.207  63.565  1.00105.65           C  
ANISOU 2734  CD  ARG B  78    15661   9323  15157   -203   7290   -116       C  
ATOM   2735  NE  ARG B  78      48.824 -22.478  62.933  1.00112.21           N  
ANISOU 2735  NE  ARG B  78    16564  10208  15861   -183   7387   -179       N  
ATOM   2736  CZ  ARG B  78      49.977 -23.111  63.117  1.00114.36           C  
ANISOU 2736  CZ  ARG B  78    16493  10476  16483   -252   7543   -351       C  
ATOM   2737  NH1 ARG B  78      50.895 -22.590  63.918  1.00118.79           N  
ANISOU 2737  NH1 ARG B  78    16614  10979  17542   -352   7599   -481       N  
ATOM   2738  NH2 ARG B  78      50.211 -24.266  62.508  1.00112.65           N  
ANISOU 2738  NH2 ARG B  78    16362  10317  16124   -211   7630   -411       N  
ATOM   2739  N   THR B  79      43.700 -17.373  64.547  1.00 90.27           N  
ANISOU 2739  N   THR B  79    14408   7590  12300    146   6356    463       N  
ATOM   2740  CA  THR B  79      43.221 -16.188  65.236  1.00 77.15           C  
ANISOU 2740  CA  THR B  79    12631   5949  10735    161   6237    512       C  
ATOM   2741  C   THR B  79      42.880 -16.528  66.684  1.00 80.66           C  
ANISOU 2741  C   THR B  79    12685   6553  11409    178   5886    436       C  
ATOM   2742  O   THR B  79      42.809 -17.696  67.076  1.00 86.23           O  
ANISOU 2742  O   THR B  79    13271   7367  12125    194   5699    383       O  
ATOM   2743  CB  THR B  79      42.001 -15.604  64.523  1.00 72.23           C  
ANISOU 2743  CB  THR B  79    12411   5390   9644    267   6107    707       C  
ATOM   2744  OG1 THR B  79      40.875 -16.474  64.699  1.00 69.55           O  
ANISOU 2744  OG1 THR B  79    12147   5262   9017    370   5719    755       O  
ATOM   2745  CG2 THR B  79      42.278 -15.440  63.039  1.00 79.98           C  
ANISOU 2745  CG2 THR B  79    13835   6220  10336    265   6425    794       C  
ATOM   2746  N   VAL B  80      42.675 -15.485  67.489  1.00 84.46           N  
ANISOU 2746  N   VAL B  80    12976   7044  12072    169   5806    436       N  
ATOM   2747  CA  VAL B  80      42.305 -15.706  68.884  1.00 77.72           C  
ANISOU 2747  CA  VAL B  80    11776   6339  11414    188   5481    370       C  
ATOM   2748  C   VAL B  80      40.980 -16.450  68.976  1.00 74.56           C  
ANISOU 2748  C   VAL B  80    11517   6160  10651    306   5129    473       C  
ATOM   2749  O   VAL B  80      40.803 -17.332  69.824  1.00 76.57           O  
ANISOU 2749  O   VAL B  80    11563   6533  10996    323   4896    416       O  
ATOM   2750  CB  VAL B  80      42.247 -14.369  69.642  1.00 72.40           C  
ANISOU 2750  CB  VAL B  80    10913   5636  10959    161   5475    356       C  
ATOM   2751  CG1 VAL B  80      41.673 -14.584  71.031  1.00 70.70           C  
ANISOU 2751  CG1 VAL B  80    10399   5594  10868    197   5124    309       C  
ATOM   2752  CG2 VAL B  80      43.624 -13.742  69.718  1.00 79.45           C  
ANISOU 2752  CG2 VAL B  80    11600   6308  12281     28   5799    212       C  
ATOM   2753  N   THR B  81      40.025 -16.103  68.110  1.00 71.63           N  
ANISOU 2753  N   THR B  81    11504   5841   9872    381   5074    630       N  
ATOM   2754  CA  THR B  81      38.727 -16.768  68.140  1.00 70.00           C  
ANISOU 2754  CA  THR B  81    11428   5840   9330    477   4724    719       C  
ATOM   2755  C   THR B  81      38.863 -18.258  67.846  1.00 65.87           C  
ANISOU 2755  C   THR B  81    10971   5352   8705    494   4685    661       C  
ATOM   2756  O   THR B  81      38.302 -19.098  68.558  1.00 63.79           O  
ANISOU 2756  O   THR B  81    10572   5238   8429    532   4420    636       O  
ATOM   2757  CB  THR B  81      37.779 -16.109  67.140  1.00 77.25           C  
ANISOU 2757  CB  THR B  81    12733   6770   9849    539   4661    896       C  
ATOM   2758  OG1 THR B  81      37.633 -14.721  67.462  1.00 87.14           O  
ANISOU 2758  OG1 THR B  81    13919   7976  11214    520   4689    964       O  
ATOM   2759  CG2 THR B  81      36.417 -16.782  67.170  1.00 75.30           C  
ANISOU 2759  CG2 THR B  81    12597   6722   9290    625   4268    975       C  
ATOM   2760  N   ASN B  82      39.612 -18.605  66.798  1.00 72.64           N  
ANISOU 2760  N   ASN B  82    12042   6065   9492    461   4962    640       N  
ATOM   2761  CA  ASN B  82      39.740 -20.009  66.420  1.00 69.84           C  
ANISOU 2761  CA  ASN B  82    11779   5736   9022    471   4942    591       C  
ATOM   2762  C   ASN B  82      40.535 -20.814  67.441  1.00 67.41           C  
ANISOU 2762  C   ASN B  82    11078   5435   9099    405   4921    462       C  
ATOM   2763  O   ASN B  82      40.285 -22.014  67.607  1.00 68.17           O  
ANISOU 2763  O   ASN B  82    11160   5623   9117    429   4767    439       O  
ATOM   2764  CB  ASN B  82      40.375 -20.119  65.037  1.00 72.56           C  
ANISOU 2764  CB  ASN B  82    12447   5929   9192    444   5266    602       C  
ATOM   2765  CG  ASN B  82      39.467 -19.603  63.943  1.00 79.36           C  
ANISOU 2765  CG  ASN B  82    13758   6800   9593    523   5221    747       C  
ATOM   2766  OD1 ASN B  82      38.301 -19.293  64.187  1.00 74.77           O  
ANISOU 2766  OD1 ASN B  82    13236   6355   8817    595   4911    839       O  
ATOM   2767  ND2 ASN B  82      39.995 -19.505  62.729  1.00 88.08           N  
ANISOU 2767  ND2 ASN B  82    15180   7761  10524    504   5521    774       N  
ATOM   2768  N   TYR B  83      41.494 -20.189  68.129  1.00 68.93           N  
ANISOU 2768  N   TYR B  83    10951   5534   9706    314   5058    379       N  
ATOM   2769  CA  TYR B  83      42.207 -20.903  69.184  1.00 69.07           C  
ANISOU 2769  CA  TYR B  83    10571   5589  10083    238   4967    271       C  
ATOM   2770  C   TYR B  83      41.265 -21.293  70.315  1.00 67.93           C  
ANISOU 2770  C   TYR B  83    10273   5622   9914    298   4595    305       C  
ATOM   2771  O   TYR B  83      41.420 -22.358  70.923  1.00 68.54           O  
ANISOU 2771  O   TYR B  83    10160   5807  10077    273   4445    269       O  
ATOM   2772  CB  TYR B  83      43.357 -20.052  69.723  1.00 79.27           C  
ANISOU 2772  CB  TYR B  83    11545   6755  11818    120   5142    161       C  
ATOM   2773  CG  TYR B  83      44.655 -20.194  68.960  1.00 89.24           C  
ANISOU 2773  CG  TYR B  83    12784   7870  13254     22   5496     67       C  
ATOM   2774  CD1 TYR B  83      44.742 -21.006  67.837  1.00 92.63           C  
ANISOU 2774  CD1 TYR B  83    13486   8281  13427     47   5657     91       C  
ATOM   2775  CD2 TYR B  83      45.798 -19.523  69.373  1.00 96.09           C  
ANISOU 2775  CD2 TYR B  83    13345   8614  14549    -98   5672    -66       C  
ATOM   2776  CE1 TYR B  83      45.930 -21.137  67.142  1.00 96.29           C  
ANISOU 2776  CE1 TYR B  83    13920   8613  14053    -39   6005     -3       C  
ATOM   2777  CE2 TYR B  83      46.989 -19.649  68.686  1.00101.34           C  
ANISOU 2777  CE2 TYR B  83    13964   9145  15397   -187   6013   -167       C  
ATOM   2778  CZ  TYR B  83      47.050 -20.457  67.571  1.00100.90           C  
ANISOU 2778  CZ  TYR B  83    14182   9077  15078   -156   6188   -131       C  
ATOM   2779  OH  TYR B  83      48.234 -20.586  66.883  1.00107.29           O  
ANISOU 2779  OH  TYR B  83    14941   9752  16071   -243   6552   -237       O  
ATOM   2780  N   PHE B  84      40.282 -20.441  70.613  1.00 66.37           N  
ANISOU 2780  N   PHE B  84    10140   5488   9587    377   4448    373       N  
ATOM   2781  CA  PHE B  84      39.281 -20.797  71.612  1.00 59.37           C  
ANISOU 2781  CA  PHE B  84     9123   4804   8632    437   4104    409       C  
ATOM   2782  C   PHE B  84      38.317 -21.847  71.077  1.00 64.60           C  
ANISOU 2782  C   PHE B  84    10053   5559   8933    532   3966    466       C  
ATOM   2783  O   PHE B  84      37.875 -22.729  71.823  1.00 69.86           O  
ANISOU 2783  O   PHE B  84    10580   6377   9586    540   3730    469       O  
ATOM   2784  CB  PHE B  84      38.526 -19.551  72.069  1.00 58.76           C  
ANISOU 2784  CB  PHE B  84     9003   4800   8524    485   4008    454       C  
ATOM   2785  CG  PHE B  84      39.272 -18.730  73.080  1.00 57.98           C  
ANISOU 2785  CG  PHE B  84     8550   4684   8796    382   4007    380       C  
ATOM   2786  CD1 PHE B  84      39.766 -19.316  74.233  1.00 59.58           C  
ANISOU 2786  CD1 PHE B  84     8419   4971   9248    293   3824    313       C  
ATOM   2787  CD2 PHE B  84      39.485 -17.376  72.876  1.00 61.15           C  
ANISOU 2787  CD2 PHE B  84     8976   4962   9296    369   4196    375       C  
ATOM   2788  CE1 PHE B  84      40.452 -18.569  75.168  1.00 59.22           C  
ANISOU 2788  CE1 PHE B  84     8073   4891   9538    192   3807    223       C  
ATOM   2789  CE2 PHE B  84      40.173 -16.624  73.809  1.00 64.20           C  
ANISOU 2789  CE2 PHE B  84     9044   5319  10031    269   4190    282       C  
ATOM   2790  CZ  PHE B  84      40.657 -17.222  74.956  1.00 62.07           C  
ANISOU 2790  CZ  PHE B  84     8448   5135  10002    181   3980    196       C  
ATOM   2791  N   LEU B  85      37.971 -21.764  69.790  1.00 65.71           N  
ANISOU 2791  N   LEU B  85    10552   5673   8740    567   4057    524       N  
ATOM   2792  CA  LEU B  85      37.103 -22.779  69.202  1.00 66.12           C  
ANISOU 2792  CA  LEU B  85    10867   5817   8439    628   3899    563       C  
ATOM   2793  C   LEU B  85      37.760 -24.152  69.241  1.00 74.89           C  
ANISOU 2793  C   LEU B  85    11923   6884   9646    594   3960    489       C  
ATOM   2794  O   LEU B  85      37.080 -25.170  69.409  1.00 76.43           O  
ANISOU 2794  O   LEU B  85    12179   7173   9688    636   3773    490       O  
ATOM   2795  CB  LEU B  85      36.747 -22.399  67.765  1.00 60.43           C  
ANISOU 2795  CB  LEU B  85    10560   5047   7354    656   3981    641       C  
ATOM   2796  CG  LEU B  85      35.832 -21.186  67.588  1.00 61.28           C  
ANISOU 2796  CG  LEU B  85    10778   5219   7285    690   3840    765       C  
ATOM   2797  CD1 LEU B  85      35.459 -21.014  66.126  1.00 61.65           C  
ANISOU 2797  CD1 LEU B  85    11273   5207   6944    730   3885    853       C  
ATOM   2798  CD2 LEU B  85      34.588 -21.325  68.448  1.00 61.00           C  
ANISOU 2798  CD2 LEU B  85    10606   5380   7192    725   3457    814       C  
ATOM   2799  N   VAL B  86      39.083 -24.203  69.082  1.00 73.82           N  
ANISOU 2799  N   VAL B  86    11653   6628   9766    503   4216    423       N  
ATOM   2800  CA  VAL B  86      39.784 -25.477  69.206  1.00 69.01           C  
ANISOU 2800  CA  VAL B  86    10901   6054   9268    458   4250    344       C  
ATOM   2801  C   VAL B  86      39.684 -25.997  70.632  1.00 69.26           C  
ANISOU 2801  C   VAL B  86    10566   6239   9509    447   4002    321       C  
ATOM   2802  O   VAL B  86      39.556 -27.206  70.863  1.00 80.28           O  
ANISOU 2802  O   VAL B  86    11910   7746  10848    482   3875    273       O  
ATOM   2803  CB  VAL B  86      41.248 -25.327  68.757  1.00 63.78           C  
ANISOU 2803  CB  VAL B  86    10111   5274   8850    366   4567    250       C  
ATOM   2804  CG1 VAL B  86      42.047 -26.563  69.139  1.00 55.62           C  
ANISOU 2804  CG1 VAL B  86     8806   4331   7998    346   4550    126       C  
ATOM   2805  CG2 VAL B  86      41.317 -25.081  67.263  1.00 64.90           C  
ANISOU 2805  CG2 VAL B  86    10655   5284   8719    381   4822    277       C  
ATOM   2806  N   ASN B  87      39.746 -25.094  71.613  1.00 68.04           N  
ANISOU 2806  N   ASN B  87    10159   6104   9589    410   3919    337       N  
ATOM   2807  CA  ASN B  87      39.581 -25.510  73.001  1.00 66.08           C  
ANISOU 2807  CA  ASN B  87     9578   6038   9490    409   3653    313       C  
ATOM   2808  C   ASN B  87      38.186 -26.073  73.236  1.00 64.60           C  
ANISOU 2808  C   ASN B  87     9552   5968   9025    494   3424    401       C  
ATOM   2809  O   ASN B  87      38.011 -27.022  74.011  1.00 64.50           O  
ANISOU 2809  O   ASN B  87     9371   6105   9033    536   3209    345       O  
ATOM   2810  CB  ASN B  87      39.855 -24.332  73.932  1.00 65.28           C  
ANISOU 2810  CB  ASN B  87     9216   5931   9654    345   3610    306       C  
ATOM   2811  CG  ASN B  87      40.017 -24.759  75.368  1.00 58.61           C  
ANISOU 2811  CG  ASN B  87     8002   5282   8985    356   3332    220       C  
ATOM   2812  OD1 ASN B  87      40.736 -25.712  75.665  1.00 61.29           O  
ANISOU 2812  OD1 ASN B  87     8161   5692   9434    388   3260     98       O  
ATOM   2813  ND2 ASN B  87      39.344 -24.059  76.272  1.00 61.79           N  
ANISOU 2813  ND2 ASN B  87     8310   5762   9405    356   3159    269       N  
ATOM   2814  N   LEU B  88      37.181 -25.499  72.571  1.00 62.60           N  
ANISOU 2814  N   LEU B  88     9604   5674   8506    559   3404    480       N  
ATOM   2815  CA  LEU B  88      35.829 -26.040  72.650  1.00 59.23           C  
ANISOU 2815  CA  LEU B  88     9326   5380   7800    649   3170    511       C  
ATOM   2816  C   LEU B  88      35.771 -27.447  72.069  1.00 64.96           C  
ANISOU 2816  C   LEU B  88    10265   6065   8353    661   3204    495       C  
ATOM   2817  O   LEU B  88      35.080 -28.322  72.606  1.00 67.74           O  
ANISOU 2817  O   LEU B  88    10572   6533   8633    701   2985    466       O  
ATOM   2818  CB  LEU B  88      34.861 -25.110  71.914  1.00 56.74           C  
ANISOU 2818  CB  LEU B  88     9267   5079   7213    717   3132    558       C  
ATOM   2819  CG  LEU B  88      33.349 -25.346  71.956  1.00 53.45           C  
ANISOU 2819  CG  LEU B  88     8955   4816   6537    727   2772    648       C  
ATOM   2820  CD1 LEU B  88      32.866 -25.462  73.389  1.00 48.10           C  
ANISOU 2820  CD1 LEU B  88     7959   4276   6043    707   2526    660       C  
ATOM   2821  CD2 LEU B  88      32.618 -24.220  71.230  1.00 49.42           C  
ANISOU 2821  CD2 LEU B  88     8622   4321   5832    737   2678    746       C  
ATOM   2822  N   SER B  89      36.489 -27.684  70.967  1.00 63.88           N  
ANISOU 2822  N   SER B  89    10318   5798   8157    646   3416    446       N  
ATOM   2823  CA  SER B  89      36.534 -29.021  70.386  1.00 62.72           C  
ANISOU 2823  CA  SER B  89    10315   5665   7849    668   3412    360       C  
ATOM   2824  C   SER B  89      37.216 -30.022  71.306  1.00 65.81           C  
ANISOU 2824  C   SER B  89    10348   6152   8505    668   3313    246       C  
ATOM   2825  O   SER B  89      36.839 -31.200  71.325  1.00 64.39           O  
ANISOU 2825  O   SER B  89    10231   5999   8234    717   3169    175       O  
ATOM   2826  CB  SER B  89      37.245 -28.975  69.033  1.00 70.82           C  
ANISOU 2826  CB  SER B  89    11584   6565   8760    646   3673    322       C  
ATOM   2827  OG  SER B  89      36.445 -28.325  68.062  1.00 69.62           O  
ANISOU 2827  OG  SER B  89    11814   6361   8277    686   3661    393       O  
ATOM   2828  N   LEU B  90      38.223 -29.585  72.065  1.00 70.12           N  
ANISOU 2828  N   LEU B  90    10532   6727   9384    624   3354    208       N  
ATOM   2829  CA  LEU B  90      38.841 -30.488  73.029  1.00 67.11           C  
ANISOU 2829  CA  LEU B  90     9826   6432   9240    662   3192     94       C  
ATOM   2830  C   LEU B  90      37.861 -30.853  74.134  1.00 64.47           C  
ANISOU 2830  C   LEU B  90     9411   6206   8879    715   2867    132       C  
ATOM   2831  O   LEU B  90      37.774 -32.018  74.537  1.00 62.44           O  
ANISOU 2831  O   LEU B  90     9113   5971   8639    777   2698     70       O  
ATOM   2832  CB  LEU B  90      40.099 -29.854  73.619  1.00 64.44           C  
ANISOU 2832  CB  LEU B  90     9137   6101   9245    614   3266     25       C  
ATOM   2833  CG  LEU B  90      41.303 -29.640  72.702  1.00 68.04           C  
ANISOU 2833  CG  LEU B  90     9586   6441   9823    556   3582    -50       C  
ATOM   2834  CD1 LEU B  90      42.396 -28.924  73.471  1.00 69.83           C  
ANISOU 2834  CD1 LEU B  90     9441   6677  10413    503   3599   -133       C  
ATOM   2835  CD2 LEU B  90      41.817 -30.960  72.145  1.00 71.46           C  
ANISOU 2835  CD2 LEU B  90    10064   6854  10234    620   3641   -167       C  
ATOM   2836  N   ALA B  91      37.110 -29.870  74.634  1.00 62.91           N  
ANISOU 2836  N   ALA B  91     9196   6058   8647    692   2780    235       N  
ATOM   2837  CA  ALA B  91      36.084 -30.168  75.625  1.00 57.54           C  
ANISOU 2837  CA  ALA B  91     8461   5474   7928    730   2481    277       C  
ATOM   2838  C   ALA B  91      34.987 -31.043  75.033  1.00 61.22           C  
ANISOU 2838  C   ALA B  91     9219   5901   8142    759   2377    296       C  
ATOM   2839  O   ALA B  91      34.462 -31.936  75.707  1.00 62.96           O  
ANISOU 2839  O   ALA B  91     9393   6152   8376    780   2150    287       O  
ATOM   2840  CB  ALA B  91      35.505 -28.873  76.191  1.00 51.59           C  
ANISOU 2840  CB  ALA B  91     7630   4783   7190    699   2422    369       C  
ATOM   2841  N   ASP B  92      34.618 -30.799  73.774  1.00 68.63           N  
ANISOU 2841  N   ASP B  92    10483   6751   8842    754   2530    322       N  
ATOM   2842  CA  ASP B  92      33.602 -31.634  73.143  1.00 71.64           C  
ANISOU 2842  CA  ASP B  92    11165   7072   8982    771   2393    311       C  
ATOM   2843  C   ASP B  92      34.103 -33.058  72.944  1.00 74.09           C  
ANISOU 2843  C   ASP B  92    11494   7331   9326    792   2399    185       C  
ATOM   2844  O   ASP B  92      33.342 -34.019  73.110  1.00 75.48           O  
ANISOU 2844  O   ASP B  92    11749   7478   9450    790   2192    158       O  
ATOM   2845  CB  ASP B  92      33.184 -31.029  71.807  1.00 77.82           C  
ANISOU 2845  CB  ASP B  92    12348   7754   9465    780   2533    356       C  
ATOM   2846  CG  ASP B  92      32.395 -29.762  71.978  1.00 82.95           C  
ANISOU 2846  CG  ASP B  92    12984   8483  10050    753   2412    509       C  
ATOM   2847  OD1 ASP B  92      31.796 -29.590  73.057  1.00 76.69           O  
ANISOU 2847  OD1 ASP B  92    11924   7816   9398    730   2167    548       O  
ATOM   2848  OD2 ASP B  92      32.385 -28.938  71.042  1.00 88.24           O  
ANISOU 2848  OD2 ASP B  92    13875   9132  10520    755   2544    567       O  
ATOM   2849  N   VAL B  93      35.377 -33.214  72.578  1.00 75.51           N  
ANISOU 2849  N   VAL B  93    11587   7485   9617    798   2625    107       N  
ATOM   2850  CA  VAL B  93      35.930 -34.552  72.393  1.00 66.58           C  
ANISOU 2850  CA  VAL B  93    10448   6303   8546    832   2625    -17       C  
ATOM   2851  C   VAL B  93      35.994 -35.298  73.718  1.00 62.69           C  
ANISOU 2851  C   VAL B  93     9682   5859   8279    870   2387    -30       C  
ATOM   2852  O   VAL B  93      35.709 -36.499  73.784  1.00 60.50           O  
ANISOU 2852  O   VAL B  93     9475   5521   7991    896   2259    -86       O  
ATOM   2853  CB  VAL B  93      37.314 -34.477  71.727  1.00 60.33           C  
ANISOU 2853  CB  VAL B  93     9589   5475   7859    829   2910    -96       C  
ATOM   2854  CG1 VAL B  93      38.103 -35.741  72.031  1.00 62.01           C  
ANISOU 2854  CG1 VAL B  93     9638   5662   8263    893   2863   -225       C  
ATOM   2855  CG2 VAL B  93      37.175 -34.277  70.230  1.00 61.40           C  
ANISOU 2855  CG2 VAL B  93    10102   5526   7701    802   3128   -104       C  
ATOM   2856  N   LEU B  94      36.389 -34.607  74.791  1.00 60.62           N  
ANISOU 2856  N   LEU B  94     9128   5690   8216    874   2321     19       N  
ATOM   2857  CA  LEU B  94      36.454 -35.250  76.100  1.00 55.90           C  
ANISOU 2857  CA  LEU B  94     8318   5134   7786    925   2085     19       C  
ATOM   2858  C   LEU B  94      35.106 -35.840  76.495  1.00 57.37           C  
ANISOU 2858  C   LEU B  94     8641   5308   7849    902   1864     90       C  
ATOM   2859  O   LEU B  94      35.035 -36.968  76.997  1.00 65.12           O  
ANISOU 2859  O   LEU B  94     9615   6238   8889    938   1724     69       O  
ATOM   2860  CB  LEU B  94      36.928 -34.245  77.150  1.00 56.26           C  
ANISOU 2860  CB  LEU B  94     8086   5286   8004    927   2030     53       C  
ATOM   2861  CG  LEU B  94      36.858 -34.669  78.617  1.00 60.31           C  
ANISOU 2861  CG  LEU B  94     8432   5854   8630    988   1769     75       C  
ATOM   2862  CD1 LEU B  94      37.817 -35.821  78.908  1.00 62.21           C  
ANISOU 2862  CD1 LEU B  94     8585   6033   9017   1096   1710    -26       C  
ATOM   2863  CD2 LEU B  94      37.145 -33.476  79.514  1.00 62.63           C  
ANISOU 2863  CD2 LEU B  94     8511   6251   9035    976   1721     97       C  
ATOM   2864  N   ALA B  95      34.021 -35.092  76.273  1.00 58.73           N  
ANISOU 2864  N   ALA B  95     8937   5513   7865    838   1826    178       N  
ATOM   2865  CA  ALA B  95      32.695 -35.589  76.626  1.00 57.41           C  
ANISOU 2865  CA  ALA B  95     8865   5336   7613    788   1611    241       C  
ATOM   2866  C   ALA B  95      32.239 -36.693  75.679  1.00 64.21           C  
ANISOU 2866  C   ALA B  95     9991   6058   8347    765   1600    165       C  
ATOM   2867  O   ALA B  95      31.615 -37.668  76.111  1.00 73.37           O  
ANISOU 2867  O   ALA B  95    11176   7163   9539    731   1441    170       O  
ATOM   2868  CB  ALA B  95      31.688 -34.439  76.628  1.00 54.61           C  
ANISOU 2868  CB  ALA B  95     8536   5058   7154    731   1548    344       C  
ATOM   2869  N   THR B  96      32.534 -36.555  74.385  1.00 64.87           N  
ANISOU 2869  N   THR B  96    10294   6073   8279    775   1777     89       N  
ATOM   2870  CA  THR B  96      32.078 -37.542  73.412  1.00 65.91           C  
ANISOU 2870  CA  THR B  96    10719   6071   8254    752   1755    -15       C  
ATOM   2871  C   THR B  96      32.802 -38.873  73.582  1.00 69.40           C  
ANISOU 2871  C   THR B  96    11094   6435   8838    794   1768   -118       C  
ATOM   2872  O   THR B  96      32.171 -39.935  73.614  1.00 69.74           O  
ANISOU 2872  O   THR B  96    11239   6379   8881    754   1625   -162       O  
ATOM   2873  CB  THR B  96      32.273 -37.007  71.993  1.00 66.69           C  
ANISOU 2873  CB  THR B  96    11109   6127   8105    766   1951    -77       C  
ATOM   2874  OG1 THR B  96      31.495 -35.816  71.820  1.00 64.59           O  
ANISOU 2874  OG1 THR B  96    10950   5898   7695    744   1902     33       O  
ATOM   2875  CG2 THR B  96      31.846 -38.047  70.969  1.00 74.22           C  
ANISOU 2875  CG2 THR B  96    12384   6952   8863    744   1908   -223       C  
ATOM   2876  N   ALA B  97      34.131 -38.834  73.703  1.00 73.14           N  
ANISOU 2876  N   ALA B  97    11390   6941   9458    871   1927   -160       N  
ATOM   2877  CA  ALA B  97      34.904 -40.071  73.764  1.00 71.62           C  
ANISOU 2877  CA  ALA B  97    11144   6661   9408    938   1937   -265       C  
ATOM   2878  C   ALA B  97      34.580 -40.874  75.018  1.00 67.64           C  
ANISOU 2878  C   ALA B  97    10506   6130   9065    953   1707   -203       C  
ATOM   2879  O   ALA B  97      34.342 -42.084  74.951  1.00 64.12           O  
ANISOU 2879  O   ALA B  97    10163   5555   8645    953   1627   -260       O  
ATOM   2880  CB  ALA B  97      36.399 -39.756  73.702  1.00 69.76           C  
ANISOU 2880  CB  ALA B  97    10707   6468   9331   1018   2130   -324       C  
ATOM   2881  N   ILE B  98      34.569 -40.219  76.173  1.00 63.22           N  
ANISOU 2881  N   ILE B  98     9736   5682   8604    963   1606    -87       N  
ATOM   2882  CA  ILE B  98      34.451 -40.904  77.457  1.00 68.30           C  
ANISOU 2882  CA  ILE B  98    10264   6308   9381    997   1413    -16       C  
ATOM   2883  C   ILE B  98      33.015 -40.933  77.961  1.00 75.72           C  
ANISOU 2883  C   ILE B  98    11277   7255  10238    883   1257    100       C  
ATOM   2884  O   ILE B  98      32.471 -41.999  78.246  1.00 81.18           O  
ANISOU 2884  O   ILE B  98    12052   7834  10959    846   1152    116       O  
ATOM   2885  CB  ILE B  98      35.391 -40.245  78.490  1.00 72.18           C  
ANISOU 2885  CB  ILE B  98    10494   6910  10020   1089   1382     19       C  
ATOM   2886  CG1 ILE B  98      36.846 -40.383  78.036  1.00 82.18           C  
ANISOU 2886  CG1 ILE B  98    11650   8151  11422   1197   1517   -116       C  
ATOM   2887  CG2 ILE B  98      35.167 -40.850  79.860  1.00 67.98           C  
ANISOU 2887  CG2 ILE B  98     9903   6362   9566   1130   1174    111       C  
ATOM   2888  CD1 ILE B  98      37.782 -39.352  78.637  1.00 89.65           C  
ANISOU 2888  CD1 ILE B  98    12342   9220  12501   1251   1537   -125       C  
ATOM   2889  N   CYS B  99      32.385 -39.763  78.081  1.00 73.29           N  
ANISOU 2889  N   CYS B  99    10929   7071   9847    819   1248    180       N  
ATOM   2890  CA  CYS B  99      31.097 -39.681  78.761  1.00 64.95           C  
ANISOU 2890  CA  CYS B  99     9873   6048   8756    718   1100    293       C  
ATOM   2891  C   CYS B  99      29.950 -40.210  77.904  1.00 59.44           C  
ANISOU 2891  C   CYS B  99     9388   5237   7961    600   1054    259       C  
ATOM   2892  O   CYS B  99      29.041 -40.863  78.427  1.00 68.13           O  
ANISOU 2892  O   CYS B  99    10503   6278   9105    509    939    313       O  
ATOM   2893  CB  CYS B  99      30.819 -38.239  79.180  1.00 59.89           C  
ANISOU 2893  CB  CYS B  99     9102   5574   8080    701   1098    376       C  
ATOM   2894  SG  CYS B  99      32.134 -37.474  80.152  1.00 57.91           S  
ANISOU 2894  SG  CYS B  99     8610   5441   7953    820   1135    382       S  
ATOM   2895  N   LEU B 100      29.959 -39.932  76.599  1.00 52.05           N  
ANISOU 2895  N   LEU B 100     8632   4256   6888    593   1142    164       N  
ATOM   2896  CA  LEU B 100      28.837 -40.343  75.757  1.00 58.39           C  
ANISOU 2896  CA  LEU B 100     9670   4940   7576    481   1055    105       C  
ATOM   2897  C   LEU B 100      28.580 -41.841  75.823  1.00 62.45           C  
ANISOU 2897  C   LEU B 100    10260   5287   8180    425    984     34       C  
ATOM   2898  O   LEU B 100      27.422 -42.238  76.038  1.00 63.70           O  
ANISOU 2898  O   LEU B 100    10455   5373   8374    291    849     58       O  
ATOM   2899  CB  LEU B 100      29.077 -39.886  74.311  1.00 59.97           C  
ANISOU 2899  CB  LEU B 100    10117   5104   7564    513   1164     -7       C  
ATOM   2900  CG  LEU B 100      27.947 -40.170  73.312  1.00 54.35           C  
ANISOU 2900  CG  LEU B 100     9662   4319   6671    403   1010   -102       C  
ATOM   2901  CD1 LEU B 100      27.954 -39.168  72.162  1.00 53.38           C  
ANISOU 2901  CD1 LEU B 100     9697   4310   6275    433   1046   -127       C  
ATOM   2902  CD2 LEU B 100      28.029 -41.591  72.767  1.00 54.30           C  
ANISOU 2902  CD2 LEU B 100     9854   4105   6674    376   1007   -278       C  
ATOM   2903  N   PRO B 101      29.571 -42.716  75.634  1.00 64.26           N  
ANISOU 2903  N   PRO B 101    10510   5433   8472    513   1070    -57       N  
ATOM   2904  CA  PRO B 101      29.282 -44.156  75.739  1.00 57.60           C  
ANISOU 2904  CA  PRO B 101     9740   4411   7734    459    997   -115       C  
ATOM   2905  C   PRO B 101      28.717 -44.565  77.088  1.00 61.28           C  
ANISOU 2905  C   PRO B 101    10061   4871   8354    399    887     38       C  
ATOM   2906  O   PRO B 101      27.850 -45.447  77.151  1.00 68.30           O  
ANISOU 2906  O   PRO B 101    11024   5614   9311    272    805     24       O  
ATOM   2907  CB  PRO B 101      30.644 -44.810  75.473  1.00 55.22           C  
ANISOU 2907  CB  PRO B 101     9432   4052   7498    605   1118   -212       C  
ATOM   2908  CG  PRO B 101      31.467 -43.755  74.801  1.00 59.75           C  
ANISOU 2908  CG  PRO B 101     9994   4751   7957    692   1279   -255       C  
ATOM   2909  CD  PRO B 101      30.994 -42.455  75.365  1.00 64.44           C  
ANISOU 2909  CD  PRO B 101    10468   5510   8508    658   1240   -111       C  
ATOM   2910  N   ALA B 102      29.186 -43.951  78.174  1.00 60.06           N  
ANISOU 2910  N   ALA B 102     9710   4861   8249    480    889    173       N  
ATOM   2911  CA  ALA B 102      28.648 -44.273  79.490  1.00 55.29           C  
ANISOU 2911  CA  ALA B 102     9006   4264   7739    430    802    324       C  
ATOM   2912  C   ALA B 102      27.191 -43.845  79.610  1.00 62.54           C  
ANISOU 2912  C   ALA B 102     9917   5212   8632    255    739    390       C  
ATOM   2913  O   ALA B 102      26.356 -44.590  80.136  1.00 65.78           O  
ANISOU 2913  O   ALA B 102    10340   5521   9131    135    692    448       O  
ATOM   2914  CB  ALA B 102      29.493 -43.615  80.582  1.00 56.68           C  
ANISOU 2914  CB  ALA B 102     9007   4594   7934    561    802    424       C  
ATOM   2915  N   SER B 103      26.865 -42.643  79.129  1.00 65.70           N  
ANISOU 2915  N   SER B 103    10295   5738   8931    238    746    384       N  
ATOM   2916  CA  SER B 103      25.484 -42.175  79.187  1.00 65.14           C  
ANISOU 2916  CA  SER B 103    10207   5684   8859     83    675    437       C  
ATOM   2917  C   SER B 103      24.559 -43.073  78.377  1.00 67.64           C  
ANISOU 2917  C   SER B 103    10695   5794   9210    -81    605    320       C  
ATOM   2918  O   SER B 103      23.399 -43.280  78.751  1.00 66.75           O  
ANISOU 2918  O   SER B 103    10539   5623   9199   -252    545    360       O  
ATOM   2919  CB  SER B 103      25.397 -40.733  78.690  1.00 69.62           C  
ANISOU 2919  CB  SER B 103    10752   6397   9305    121    681    447       C  
ATOM   2920  OG  SER B 103      24.052 -40.297  78.640  1.00 75.28           O  
ANISOU 2920  OG  SER B 103    11431   7143  10029    -20    579    478       O  
ATOM   2921  N   LEU B 104      25.051 -43.607  77.256  1.00 62.99           N  
ANISOU 2921  N   LEU B 104    10297   5090   8546    -45    614    153       N  
ATOM   2922  CA  LEU B 104      24.226 -44.485  76.431  1.00 63.68           C  
ANISOU 2922  CA  LEU B 104    10564   4978   8653   -207    515     -9       C  
ATOM   2923  C   LEU B 104      23.854 -45.758  77.178  1.00 66.84           C  
ANISOU 2923  C   LEU B 104    10902   5230   9266   -312    510     26       C  
ATOM   2924  O   LEU B 104      22.704 -46.209  77.121  1.00 71.42           O  
ANISOU 2924  O   LEU B 104    11490   5690   9956   -521    421    -25       O  
ATOM   2925  CB  LEU B 104      24.960 -44.823  75.131  1.00 63.78           C  
ANISOU 2925  CB  LEU B 104    10804   4916   8512   -121    545   -208       C  
ATOM   2926  CG  LEU B 104      24.351 -45.927  74.268  1.00 60.99           C  
ANISOU 2926  CG  LEU B 104    10642   4359   8171   -262    435   -423       C  
ATOM   2927  CD1 LEU B 104      22.926 -45.571  73.889  1.00 61.63           C  
ANISOU 2927  CD1 LEU B 104    10660   4531   8226   -450    206   -484       C  
ATOM   2928  CD2 LEU B 104      25.192 -46.167  73.022  1.00 61.93           C  
ANISOU 2928  CD2 LEU B 104    10987   4444   8098   -146    500   -618       C  
ATOM   2929  N   LEU B 105      24.815 -46.355  77.885  1.00 60.71           N  
ANISOU 2929  N   LEU B 105    10065   4447   8557   -177    595    107       N  
ATOM   2930  CA  LEU B 105      24.525 -47.572  78.634  1.00 61.21           C  
ANISOU 2930  CA  LEU B 105    10110   4351   8798   -254    592    168       C  
ATOM   2931  C   LEU B 105      23.582 -47.298  79.801  1.00 65.66           C  
ANISOU 2931  C   LEU B 105    10524   4978   9447   -378    587    350       C  
ATOM   2932  O   LEU B 105      22.698 -48.112  80.094  1.00 80.48           O  
ANISOU 2932  O   LEU B 105    12401   6704  11474   -554    575    363       O  
ATOM   2933  CB  LEU B 105      25.831 -48.204  79.118  1.00 68.09           C  
ANISOU 2933  CB  LEU B 105    10983   5192   9694    -59    649    214       C  
ATOM   2934  CG  LEU B 105      26.717 -48.785  78.009  1.00 78.03           C  
ANISOU 2934  CG  LEU B 105    12384   6340  10922     45    683     21       C  
ATOM   2935  CD1 LEU B 105      28.034 -49.303  78.566  1.00 82.10           C  
ANISOU 2935  CD1 LEU B 105    12865   6831  11497    248    729     70       C  
ATOM   2936  CD2 LEU B 105      25.984 -49.887  77.256  1.00 85.90           C  
ANISOU 2936  CD2 LEU B 105    13531   7100  12006   -112    635   -140       C  
ATOM   2937  N   VAL B 106      23.747 -46.157  80.475  1.00 56.57           N  
ANISOU 2937  N   VAL B 106     9239   4047   8209   -295    612    480       N  
ATOM   2938  CA  VAL B 106      22.886 -45.834  81.611  1.00 52.62           C  
ANISOU 2938  CA  VAL B 106     8603   3627   7761   -398    633    643       C  
ATOM   2939  C   VAL B 106      21.448 -45.592  81.159  1.00 61.23           C  
ANISOU 2939  C   VAL B 106     9651   4666   8949   -635    596    583       C  
ATOM   2940  O   VAL B 106      20.498 -46.024  81.819  1.00 67.40           O  
ANISOU 2940  O   VAL B 106    10355   5385   9867   -807    630    652       O  
ATOM   2941  CB  VAL B 106      23.450 -44.620  82.376  1.00 48.79           C  
ANISOU 2941  CB  VAL B 106     7993   3393   7153   -245    659    758       C  
ATOM   2942  CG1 VAL B 106      22.520 -44.232  83.517  1.00 51.67           C  
ANISOU 2942  CG1 VAL B 106     8237   3850   7545   -348    700    903       C  
ATOM   2943  CG2 VAL B 106      24.850 -44.922  82.893  1.00 52.19           C  
ANISOU 2943  CG2 VAL B 106     8447   3852   7531    -38    670    790       C  
ATOM   2944  N   ASP B 107      21.263 -44.914  80.021  1.00 71.44           N  
ANISOU 2944  N   ASP B 107    11003   5973  10168   -656    523    443       N  
ATOM   2945  CA  ASP B 107      19.919 -44.569  79.567  1.00 77.07           C  
ANISOU 2945  CA  ASP B 107    11600   6724  10958   -860    407    354       C  
ATOM   2946  C   ASP B 107      19.139 -45.761  79.024  1.00 77.83           C  
ANISOU 2946  C   ASP B 107    11754   6595  11224  -1080    328    189       C  
ATOM   2947  O   ASP B 107      17.911 -45.677  78.901  1.00 83.87           O  
ANISOU 2947  O   ASP B 107    12328   7411  12129  -1273    220    116       O  
ATOM   2948  CB  ASP B 107      19.989 -43.463  78.521  1.00 82.90           C  
ANISOU 2948  CB  ASP B 107    12309   7687  11501   -759    256    251       C  
ATOM   2949  CG  ASP B 107      20.273 -42.117  79.133  1.00 89.69           C  
ANISOU 2949  CG  ASP B 107    13025   8784  12268   -618    312    404       C  
ATOM   2950  OD1 ASP B 107      19.689 -41.821  80.195  1.00 86.35           O  
ANISOU 2950  OD1 ASP B 107    12423   8429  11959   -679    381    535       O  
ATOM   2951  OD2 ASP B 107      21.084 -41.361  78.565  1.00 92.36           O  
ANISOU 2951  OD2 ASP B 107    13438   9229  12427   -452    308    387       O  
ATOM   2952  N   ILE B 108      19.813 -46.858  78.702  1.00 74.54           N  
ANISOU 2952  N   ILE B 108    11556   5943  10823  -1050    370    114       N  
ATOM   2953  CA  ILE B 108      19.134 -48.073  78.268  1.00 78.80           C  
ANISOU 2953  CA  ILE B 108    12139   6255  11548  -1254    304    -48       C  
ATOM   2954  C   ILE B 108      18.895 -49.012  79.439  1.00 81.56           C  
ANISOU 2954  C   ILE B 108    12392   6508  12090  -1322    422    121       C  
ATOM   2955  O   ILE B 108      17.773 -49.464  79.673  1.00 91.50           O  
ANISOU 2955  O   ILE B 108    13536   7671  13558  -1567    411     97       O  
ATOM   2956  CB  ILE B 108      19.948 -48.771  77.160  1.00 77.88           C  
ANISOU 2956  CB  ILE B 108    12253   6017  11322  -1148    247   -248       C  
ATOM   2957  CG1 ILE B 108      19.984 -47.913  75.893  1.00 80.20           C  
ANISOU 2957  CG1 ILE B 108    12662   6440  11371  -1099     84   -429       C  
ATOM   2958  CG2 ILE B 108      19.368 -50.147  76.871  1.00 77.19           C  
ANISOU 2958  CG2 ILE B 108    12197   5680  11452  -1334    198   -401       C  
ATOM   2959  CD1 ILE B 108      20.952 -48.424  74.847  1.00 88.17           C  
ANISOU 2959  CD1 ILE B 108    13945   7341  12214   -961     90   -611       C  
ATOM   2960  N   THR B 109      19.952 -49.313  80.196  1.00 74.62           N  
ANISOU 2960  N   THR B 109    11569   5659  11124  -1111    520    289       N  
ATOM   2961  CA  THR B 109      19.850 -50.246  81.308  1.00 70.99           C  
ANISOU 2961  CA  THR B 109    11106   5097  10769  -1150    609    456       C  
ATOM   2962  C   THR B 109      19.357 -49.585  82.587  1.00 68.85           C  
ANISOU 2962  C   THR B 109    10693   4999  10467  -1182    707    672       C  
ATOM   2963  O   THR B 109      18.849 -50.284  83.471  1.00 78.46           O  
ANISOU 2963  O   THR B 109    11908   6128  11774  -1293    797    794       O  
ATOM   2964  CB  THR B 109      21.198 -50.913  81.578  1.00 64.36           C  
ANISOU 2964  CB  THR B 109    10405   4199   9849   -913    639    517       C  
ATOM   2965  OG1 THR B 109      22.102 -49.957  82.147  1.00 67.44           O  
ANISOU 2965  OG1 THR B 109    10745   4823  10058   -691    666    638       O  
ATOM   2966  CG2 THR B 109      21.796 -51.449  80.282  1.00 51.74           C  
ANISOU 2966  CG2 THR B 109     8944   2462   8253   -851    574    288       C  
ATOM   2967  N   GLU B 110      19.499 -48.266  82.711  1.00 70.85           N  
ANISOU 2967  N   GLU B 110    10844   5489  10587  -1084    708    718       N  
ATOM   2968  CA  GLU B 110      19.145 -47.554  83.939  1.00 72.17           C  
ANISOU 2968  CA  GLU B 110    10885   5841  10696  -1079    809    902       C  
ATOM   2969  C   GLU B 110      19.902 -48.123  85.136  1.00 78.56           C  
ANISOU 2969  C   GLU B 110    11793   6647  11408   -935    882   1077       C  
ATOM   2970  O   GLU B 110      19.367 -48.236  86.241  1.00 86.53           O  
ANISOU 2970  O   GLU B 110    12775   7685  12419  -1006    993   1220       O  
ATOM   2971  CB  GLU B 110      17.634 -47.580  84.172  1.00 78.62           C  
ANISOU 2971  CB  GLU B 110    11544   6629  11697  -1359    874    895       C  
ATOM   2972  CG  GLU B 110      16.848 -47.048  82.986  1.00 90.30           C  
ANISOU 2972  CG  GLU B 110    12904   8098  13310  -1516    762    693       C  
ATOM   2973  CD  GLU B 110      15.351 -47.133  83.182  1.00101.36           C  
ANISOU 2973  CD  GLU B 110    14073   9481  14957  -1802    809    645       C  
ATOM   2974  OE1 GLU B 110      14.906 -47.231  84.345  1.00104.17           O  
ANISOU 2974  OE1 GLU B 110    14351   9899  15331  -1853    976    802       O  
ATOM   2975  OE2 GLU B 110      14.620 -47.104  82.170  1.00106.26           O  
ANISOU 2975  OE2 GLU B 110    14578  10036  15758  -1973    669    428       O  
ATOM   2976  N   SER B 111      21.162 -48.485  84.907  1.00 78.80           N  
ANISOU 2976  N   SER B 111    11943   6637  11359   -730    823   1054       N  
ATOM   2977  CA  SER B 111      22.027 -49.002  85.955  1.00 76.25           C  
ANISOU 2977  CA  SER B 111    11719   6297  10955   -568    851   1197       C  
ATOM   2978  C   SER B 111      23.464 -48.627  85.628  1.00 67.39           C  
ANISOU 2978  C   SER B 111    10617   5263   9726   -313    773   1139       C  
ATOM   2979  O   SER B 111      23.796 -48.293  84.487  1.00 63.71           O  
ANISOU 2979  O   SER B 111    10133   4812   9262   -276    723    984       O  
ATOM   2980  CB  SER B 111      21.889 -50.523  86.104  1.00 80.14           C  
ANISOU 2980  CB  SER B 111    12359   6511  11579   -649    881   1229       C  
ATOM   2981  OG  SER B 111      22.485 -51.202  85.012  1.00 79.59           O  
ANISOU 2981  OG  SER B 111    12375   6278  11588   -596    806   1071       O  
ATOM   2982  N   TRP B 112      24.318 -48.686  86.647  1.00 62.63           N  
ANISOU 2982  N   TRP B 112    10055   4709   9032   -142    767   1258       N  
ATOM   2983  CA  TRP B 112      25.735 -48.368  86.512  1.00 60.44           C  
ANISOU 2983  CA  TRP B 112     9769   4507   8689     96    696   1206       C  
ATOM   2984  C   TRP B 112      26.524 -49.669  86.528  1.00 66.12           C  
ANISOU 2984  C   TRP B 112    10627   5002   9493    200    665   1210       C  
ATOM   2985  O   TRP B 112      26.491 -50.406  87.520  1.00 70.97           O  
ANISOU 2985  O   TRP B 112    11345   5508  10112    214    678   1357       O  
ATOM   2986  CB  TRP B 112      26.210 -47.437  87.628  1.00 57.98           C  
ANISOU 2986  CB  TRP B 112     9391   4401   8237    227    681   1310       C  
ATOM   2987  CG  TRP B 112      27.577 -46.872  87.385  1.00 55.71           C  
ANISOU 2987  CG  TRP B 112     9041   4210   7915    441    608   1227       C  
ATOM   2988  CD1 TRP B 112      28.738 -47.242  87.999  1.00 60.56           C  
ANISOU 2988  CD1 TRP B 112     9697   4784   8530    637    538   1264       C  
ATOM   2989  CD2 TRP B 112      27.926 -45.835  86.460  1.00 56.24           C  
ANISOU 2989  CD2 TRP B 112     8987   4419   7961    476    604   1091       C  
ATOM   2990  NE1 TRP B 112      29.788 -46.502  87.513  1.00 59.80           N  
ANISOU 2990  NE1 TRP B 112     9489   4794   8440    783    494   1146       N  
ATOM   2991  CE2 TRP B 112      29.315 -45.630  86.569  1.00 56.52           C  
ANISOU 2991  CE2 TRP B 112     8981   4492   8001    683    549   1044       C  
ATOM   2992  CE3 TRP B 112      27.198 -45.059  85.552  1.00 57.53           C  
ANISOU 2992  CE3 TRP B 112     9080   4668   8111    356    640   1009       C  
ATOM   2993  CZ2 TRP B 112      29.991 -44.684  85.804  1.00 52.26           C  
ANISOU 2993  CZ2 TRP B 112     8329   4072   7455    757    561    918       C  
ATOM   2994  CZ3 TRP B 112      27.871 -44.120  84.795  1.00 48.76           C  
ANISOU 2994  CZ3 TRP B 112     7885   3676   6966    443    642    900       C  
ATOM   2995  CH2 TRP B 112      29.254 -43.941  84.925  1.00 51.30           C  
ANISOU 2995  CH2 TRP B 112     8164   4033   7294    633    619    856       C  
ATOM   2996  N   LEU B 113      27.230 -49.944  85.435  1.00 61.93           N  
ANISOU 2996  N   LEU B 113    10110   4393   9026    278    634   1049       N  
ATOM   2997  CA  LEU B 113      27.980 -51.180  85.271  1.00 65.15           C  
ANISOU 2997  CA  LEU B 113    10640   4571   9544    382    607   1018       C  
ATOM   2998  C   LEU B 113      29.489 -50.960  85.260  1.00 71.42           C  
ANISOU 2998  C   LEU B 113    11386   5420  10332    637    550    963       C  
ATOM   2999  O   LEU B 113      30.232 -51.880  84.903  1.00 83.49           O  
ANISOU 2999  O   LEU B 113    12986   6766  11972    747    527    894       O  
ATOM   3000  CB  LEU B 113      27.546 -51.883  83.981  1.00 55.84           C  
ANISOU 3000  CB  LEU B 113     9532   3210   8476    259    631    847       C  
ATOM   3001  CG  LEU B 113      26.047 -52.165  83.850  1.00 50.49           C  
ANISOU 3001  CG  LEU B 113     8880   2444   7860    -11    670    860       C  
ATOM   3002  CD1 LEU B 113      25.671 -52.514  82.418  1.00 55.23           C  
ANISOU 3002  CD1 LEU B 113     9529   2915   8540   -124    662    638       C  
ATOM   3003  CD2 LEU B 113      25.636 -53.280  84.797  1.00 53.46           C  
ANISOU 3003  CD2 LEU B 113     9369   2618   8327    -82    700   1018       C  
ATOM   3004  N   PHE B 114      29.965 -49.770  85.629  1.00 67.62           N  
ANISOU 3004  N   PHE B 114    10772   5171   9747    732    525    978       N  
ATOM   3005  CA  PHE B 114      31.381 -49.449  85.502  1.00 70.09           C  
ANISOU 3005  CA  PHE B 114    10999   5539  10091    953    475    893       C  
ATOM   3006  C   PHE B 114      32.113 -49.342  86.836  1.00 65.11           C  
ANISOU 3006  C   PHE B 114    10343   4954   9442   1122    378   1025       C  
ATOM   3007  O   PHE B 114      33.291 -48.966  86.853  1.00 70.39           O  
ANISOU 3007  O   PHE B 114    10903   5679  10162   1307    316    951       O  
ATOM   3008  CB  PHE B 114      31.558 -48.153  84.711  1.00 76.26           C  
ANISOU 3008  CB  PHE B 114    11644   6527  10804    947    523    768       C  
ATOM   3009  CG  PHE B 114      30.737 -48.091  83.457  1.00 79.03           C  
ANISOU 3009  CG  PHE B 114    12039   6856  11135    782    604    654       C  
ATOM   3010  CD1 PHE B 114      31.069 -48.850  82.348  1.00 82.03           C  
ANISOU 3010  CD1 PHE B 114    12504   7076  11586    798    645    500       C  
ATOM   3011  CD2 PHE B 114      29.641 -47.250  83.385  1.00 81.39           C  
ANISOU 3011  CD2 PHE B 114    12298   7285  11341    621    631    691       C  
ATOM   3012  CE1 PHE B 114      30.308 -48.782  81.195  1.00 84.70           C  
ANISOU 3012  CE1 PHE B 114    12913   7386  11885    653    701    383       C  
ATOM   3013  CE2 PHE B 114      28.883 -47.175  82.239  1.00 81.37           C  
ANISOU 3013  CE2 PHE B 114    12346   7247  11322    482    673    583       C  
ATOM   3014  CZ  PHE B 114      29.215 -47.940  81.143  1.00 82.60           C  
ANISOU 3014  CZ  PHE B 114    12612   7244  11529    496    703    426       C  
ATOM   3015  N   GLY B 115      31.461 -49.660  87.947  1.00 58.61           N  
ANISOU 3015  N   GLY B 115     9617   4103   8549   1066    365   1210       N  
ATOM   3016  CA  GLY B 115      32.131 -49.670  89.231  1.00 66.46           C  
ANISOU 3016  CA  GLY B 115    10633   5118   9500   1236    266   1344       C  
ATOM   3017  C   GLY B 115      32.199 -48.314  89.913  1.00 71.03           C  
ANISOU 3017  C   GLY B 115    11096   5951   9940   1271    236   1372       C  
ATOM   3018  O   GLY B 115      31.783 -47.278  89.392  1.00 74.94           O  
ANISOU 3018  O   GLY B 115    11477   6614  10382   1172    295   1289       O  
ATOM   3019  N   HIS B 116      32.747 -48.344  91.132  1.00 75.42           N  
ANISOU 3019  N   HIS B 116    11698   6525  10433   1428    134   1494       N  
ATOM   3020  CA  HIS B 116      32.758 -47.157  91.983  1.00 75.93           C  
ANISOU 3020  CA  HIS B 116    11694   6809  10346   1468     96   1535       C  
ATOM   3021  C   HIS B 116      33.653 -46.055  91.425  1.00 78.93           C  
ANISOU 3021  C   HIS B 116    11851   7338  10801   1567     45   1361       C  
ATOM   3022  O   HIS B 116      33.292 -44.873  91.480  1.00 85.53           O  
ANISOU 3022  O   HIS B 116    12593   8359  11545   1503     83   1328       O  
ATOM   3023  CB  HIS B 116      33.203 -47.536  93.394  1.00 78.24           C  
ANISOU 3023  CB  HIS B 116    12120   7072  10535   1635    -17   1697       C  
ATOM   3024  CG  HIS B 116      33.473 -46.359  94.279  1.00 90.12           C  
ANISOU 3024  CG  HIS B 116    13563   8791  11888   1730    -93   1708       C  
ATOM   3025  ND1 HIS B 116      34.733 -46.056  94.750  1.00 93.81           N  
ANISOU 3025  ND1 HIS B 116    13940   9308  12393   1971   -270   1663       N  
ATOM   3026  CD2 HIS B 116      32.645 -45.412  94.779  1.00 90.56           C  
ANISOU 3026  CD2 HIS B 116    13626   9016  11765   1622    -18   1746       C  
ATOM   3027  CE1 HIS B 116      34.668 -44.973  95.505  1.00 91.41           C  
ANISOU 3027  CE1 HIS B 116    13608   9197  11926   2005   -314   1668       C  
ATOM   3028  NE2 HIS B 116      33.413 -44.563  95.538  1.00 89.30           N  
ANISOU 3028  NE2 HIS B 116    13406   9001  11521   1799   -155   1720       N  
ATOM   3029  N   ALA B 117      34.822 -46.411  90.889  1.00 77.34           N  
ANISOU 3029  N   ALA B 117    11552   7048  10784   1724    -28   1243       N  
ATOM   3030  CA  ALA B 117      35.779 -45.389  90.474  1.00 74.44           C  
ANISOU 3030  CA  ALA B 117    10956   6808  10519   1827    -69   1076       C  
ATOM   3031  C   ALA B 117      35.252 -44.583  89.292  1.00 72.51           C  
ANISOU 3031  C   ALA B 117    10631   6663  10255   1662     76    948       C  
ATOM   3032  O   ALA B 117      35.251 -43.346  89.322  1.00 70.70           O  
ANISOU 3032  O   ALA B 117    10279   6607   9978   1641     95    898       O  
ATOM   3033  CB  ALA B 117      37.121 -46.038  90.132  1.00 70.61           C  
ANISOU 3033  CB  ALA B 117    10362   6189  10276   2023   -153    965       C  
ATOM   3034  N   LEU B 118      34.779 -45.264  88.247  1.00 70.40           N  
ANISOU 3034  N   LEU B 118    10445   6284  10020   1547    181    900       N  
ATOM   3035  CA  LEU B 118      34.254 -44.556  87.087  1.00 55.94           C  
ANISOU 3035  CA  LEU B 118     8563   4542   8147   1401    317    795       C  
ATOM   3036  C   LEU B 118      32.973 -43.801  87.414  1.00 56.59           C  
ANISOU 3036  C   LEU B 118     8670   4758   8072   1228    373    894       C  
ATOM   3037  O   LEU B 118      32.618 -42.864  86.690  1.00 52.82           O  
ANISOU 3037  O   LEU B 118     8115   4398   7556   1139    457    825       O  
ATOM   3038  CB  LEU B 118      34.030 -45.537  85.939  1.00 51.79           C  
ANISOU 3038  CB  LEU B 118     8141   3853   7682   1331    400    718       C  
ATOM   3039  CG  LEU B 118      35.331 -46.158  85.434  1.00 52.17           C  
ANISOU 3039  CG  LEU B 118     8143   3781   7899   1506    376    581       C  
ATOM   3040  CD1 LEU B 118      35.018 -47.166  84.353  1.00 52.44           C  
ANISOU 3040  CD1 LEU B 118     8309   3642   7973   1433    463    502       C  
ATOM   3041  CD2 LEU B 118      36.283 -45.083  84.926  1.00 54.56           C  
ANISOU 3041  CD2 LEU B 118     8256   4224   8251   1592    420    430       C  
ATOM   3042  N   CYS B 119      32.277 -44.194  88.485  1.00 58.53           N  
ANISOU 3042  N   CYS B 119     9023   4983   8232   1185    338   1053       N  
ATOM   3043  CA  CYS B 119      31.123 -43.441  88.963  1.00 62.66           C  
ANISOU 3043  CA  CYS B 119     9546   5640   8624   1042    394   1138       C  
ATOM   3044  C   CYS B 119      31.513 -42.043  89.409  1.00 58.14           C  
ANISOU 3044  C   CYS B 119     8837   5259   7996   1116    368   1108       C  
ATOM   3045  O   CYS B 119      30.663 -41.146  89.422  1.00 55.67           O  
ANISOU 3045  O   CYS B 119     8475   5072   7606   1004    435   1123       O  
ATOM   3046  CB  CYS B 119      30.457 -44.206  90.115  1.00 69.99           C  
ANISOU 3046  CB  CYS B 119    10628   6495   9471   1001    387   1312       C  
ATOM   3047  SG  CYS B 119      29.009 -43.429  90.910  1.00 82.64           S  
ANISOU 3047  SG  CYS B 119    12236   8241  10921    834    484   1423       S  
ATOM   3048  N   LYS B 120      32.773 -41.848  89.788  1.00 54.20           N  
ANISOU 3048  N   LYS B 120     8263   4772   7560   1307    264   1058       N  
ATOM   3049  CA  LYS B 120      33.296 -40.530  90.118  1.00 53.50           C  
ANISOU 3049  CA  LYS B 120     8022   4841   7464   1388    230    995       C  
ATOM   3050  C   LYS B 120      33.967 -39.869  88.922  1.00 55.65           C  
ANISOU 3050  C   LYS B 120     8133   5148   7863   1396    293    824       C  
ATOM   3051  O   LYS B 120      33.795 -38.665  88.700  1.00 63.96           O  
ANISOU 3051  O   LYS B 120     9077   6329   8894   1347    355    777       O  
ATOM   3052  CB  LYS B 120      34.302 -40.631  91.269  1.00 57.43           C  
ANISOU 3052  CB  LYS B 120     8504   5335   7980   1597     61   1022       C  
ATOM   3053  CG  LYS B 120      33.726 -41.195  92.547  1.00 57.31           C  
ANISOU 3053  CG  LYS B 120     8683   5301   7792   1610     12   1205       C  
ATOM   3054  CD  LYS B 120      34.500 -40.722  93.760  1.00 51.68           C  
ANISOU 3054  CD  LYS B 120     7951   4672   7013   1808   -151   1224       C  
ATOM   3055  CE  LYS B 120      33.719 -40.993  95.027  1.00 58.45           C  
ANISOU 3055  CE  LYS B 120     9038   5553   7619   1795   -155   1404       C  
ATOM   3056  NZ  LYS B 120      32.860 -39.840  95.394  1.00 66.71           N  
ANISOU 3056  NZ  LYS B 120    10076   6757   8514   1702    -63   1414       N  
ATOM   3057  N   VAL B 121      34.737 -40.636  88.148  1.00 56.19           N  
ANISOU 3057  N   VAL B 121     8191   5097   8060   1459    295    730       N  
ATOM   3058  CA  VAL B 121      35.486 -40.059  87.034  1.00 53.62           C  
ANISOU 3058  CA  VAL B 121     7727   4804   7842   1475    387    564       C  
ATOM   3059  C   VAL B 121      34.534 -39.524  85.972  1.00 50.88           C  
ANISOU 3059  C   VAL B 121     7418   4512   7404   1293    550    560       C  
ATOM   3060  O   VAL B 121      34.522 -38.325  85.668  1.00 56.78           O  
ANISOU 3060  O   VAL B 121     8058   5377   8138   1251    625    519       O  
ATOM   3061  CB  VAL B 121      36.459 -41.090  86.440  1.00 55.25           C  
ANISOU 3061  CB  VAL B 121     7933   4864   8196   1587    375    458       C  
ATOM   3062  CG1 VAL B 121      37.208 -40.485  85.266  1.00 60.48           C  
ANISOU 3062  CG1 VAL B 121     8466   5572   8943   1591    519    290       C  
ATOM   3063  CG2 VAL B 121      37.425 -41.593  87.500  1.00 53.49           C  
ANISOU 3063  CG2 VAL B 121     7652   4579   8095   1789    180    458       C  
ATOM   3064  N   ILE B 122      33.731 -40.413  85.381  1.00 50.64           N  
ANISOU 3064  N   ILE B 122     7538   4380   7322   1189    595    597       N  
ATOM   3065  CA  ILE B 122      32.895 -40.019  84.243  1.00 41.91           C  
ANISOU 3065  CA  ILE B 122     6478   3301   6145   1041    715    571       C  
ATOM   3066  C   ILE B 122      31.974 -38.852  84.588  1.00 48.16           C  
ANISOU 3066  C   ILE B 122     7216   4240   6843    945    725    641       C  
ATOM   3067  O   ILE B 122      31.944 -37.870  83.830  1.00 52.03           O  
ANISOU 3067  O   ILE B 122     7650   4807   7313    907    813    591       O  
ATOM   3068  CB  ILE B 122      32.127 -41.231  83.706  1.00 44.35           C  
ANISOU 3068  CB  ILE B 122     6956   3460   6434    949    720    586       C  
ATOM   3069  CG1 ILE B 122      33.082 -42.169  82.968  1.00 42.15           C  
ANISOU 3069  CG1 ILE B 122     6726   3038   6252   1042    756    471       C  
ATOM   3070  CG2 ILE B 122      31.000 -40.793  82.784  1.00 50.96           C  
ANISOU 3070  CG2 ILE B 122     7852   4326   7183    793    784    577       C  
ATOM   3071  CD1 ILE B 122      32.629 -43.604  82.941  1.00 42.05           C  
ANISOU 3071  CD1 ILE B 122     6869   2840   6270   1003    714    496       C  
ATOM   3072  N   PRO B 123      31.199 -38.893  85.674  1.00 55.17           N  
ANISOU 3072  N   PRO B 123     8126   5165   7671    904    656    757       N  
ATOM   3073  CA  PRO B 123      30.400 -37.709  86.036  1.00 54.26           C  
ANISOU 3073  CA  PRO B 123     7937   5194   7487    833    675    805       C  
ATOM   3074  C   PRO B 123      31.248 -36.467  86.247  1.00 59.17           C  
ANISOU 3074  C   PRO B 123     8412   5924   8144    924    690    748       C  
ATOM   3075  O   PRO B 123      30.809 -35.353  85.931  1.00 59.29           O  
ANISOU 3075  O   PRO B 123     8358   6034   8136    867    746    740       O  
ATOM   3076  CB  PRO B 123      29.694 -38.158  87.320  1.00 44.87           C  
ANISOU 3076  CB  PRO B 123     6810   4005   6235    806    621    931       C  
ATOM   3077  CG  PRO B 123      29.581 -39.651  87.167  1.00 45.82           C  
ANISOU 3077  CG  PRO B 123     7066   3959   6384    778    599    959       C  
ATOM   3078  CD  PRO B 123      30.898 -40.041  86.546  1.00 51.92           C  
ANISOU 3078  CD  PRO B 123     7826   4655   7248    906    583    854       C  
ATOM   3079  N   TYR B 124      32.454 -36.631  86.796  1.00 55.09           N  
ANISOU 3079  N   TYR B 124     7839   5386   7707   1070    626    703       N  
ATOM   3080  CA  TYR B 124      33.355 -35.497  86.979  1.00 56.69           C  
ANISOU 3080  CA  TYR B 124     7875   5673   7990   1152    630    617       C  
ATOM   3081  C   TYR B 124      33.822 -34.940  85.638  1.00 60.93           C  
ANISOU 3081  C   TYR B 124     8344   6213   8596   1107    771    513       C  
ATOM   3082  O   TYR B 124      33.828 -33.721  85.429  1.00 66.76           O  
ANISOU 3082  O   TYR B 124     8984   7032   9350   1067    842    484       O  
ATOM   3083  CB  TYR B 124      34.547 -35.923  87.834  1.00 59.61           C  
ANISOU 3083  CB  TYR B 124     8185   6006   8457   1328    493    568       C  
ATOM   3084  CG  TYR B 124      35.717 -34.968  87.800  1.00 62.43           C  
ANISOU 3084  CG  TYR B 124     8334   6424   8962   1415    488    419       C  
ATOM   3085  CD1 TYR B 124      35.721 -33.823  88.583  1.00 57.89           C  
ANISOU 3085  CD1 TYR B 124     7651   5954   8390   1439    443    400       C  
ATOM   3086  CD2 TYR B 124      36.825 -35.222  87.002  1.00 64.09           C  
ANISOU 3086  CD2 TYR B 124     8448   6585   9318   1469    538    283       C  
ATOM   3087  CE1 TYR B 124      36.792 -32.948  88.565  1.00 56.98           C  
ANISOU 3087  CE1 TYR B 124     7328   5892   8429   1500    437    242       C  
ATOM   3088  CE2 TYR B 124      37.902 -34.353  86.978  1.00 63.42           C  
ANISOU 3088  CE2 TYR B 124     8153   6565   9378   1527    553    136       C  
ATOM   3089  CZ  TYR B 124      37.880 -33.219  87.761  1.00 56.76           C  
ANISOU 3089  CZ  TYR B 124     7198   5825   8544   1535    497    114       C  
ATOM   3090  OH  TYR B 124      38.953 -32.356  87.735  1.00 48.16           O  
ANISOU 3090  OH  TYR B 124     5891   4799   7610   1569    522    -38       O  
ATOM   3091  N   LEU B 125      34.216 -35.822  84.716  1.00 59.69           N  
ANISOU 3091  N   LEU B 125     8253   5954   8473   1114    827    460       N  
ATOM   3092  CA  LEU B 125      34.687 -35.367  83.411  1.00 57.46           C  
ANISOU 3092  CA  LEU B 125     7945   5661   8227   1077    995    371       C  
ATOM   3093  C   LEU B 125      33.583 -34.655  82.642  1.00 51.46           C  
ANISOU 3093  C   LEU B 125     7273   4940   7339    949   1083    428       C  
ATOM   3094  O   LEU B 125      33.847 -33.702  81.901  1.00 50.75           O  
ANISOU 3094  O   LEU B 125     7147   4880   7257    918   1217    392       O  
ATOM   3095  CB  LEU B 125      35.228 -36.549  82.608  1.00 59.02           C  
ANISOU 3095  CB  LEU B 125     8229   5732   8465   1118   1046    299       C  
ATOM   3096  CG  LEU B 125      36.582 -37.078  83.081  1.00 58.73           C  
ANISOU 3096  CG  LEU B 125     8067   5654   8594   1270    980    203       C  
ATOM   3097  CD1 LEU B 125      37.022 -38.269  82.249  1.00 61.06           C  
ANISOU 3097  CD1 LEU B 125     8454   5814   8930   1312   1041    128       C  
ATOM   3098  CD2 LEU B 125      37.624 -35.971  83.041  1.00 60.82           C  
ANISOU 3098  CD2 LEU B 125     8118   6003   8987   1301   1055    100       C  
ATOM   3099  N   GLN B 126      32.336 -35.101  82.805  1.00 51.82           N  
ANISOU 3099  N   GLN B 126     7434   4977   7277    876   1006    515       N  
ATOM   3100  CA  GLN B 126      31.230 -34.419  82.140  1.00 50.30           C  
ANISOU 3100  CA  GLN B 126     7306   4824   6980    773   1037    559       C  
ATOM   3101  C   GLN B 126      31.067 -32.998  82.667  1.00 52.76           C  
ANISOU 3101  C   GLN B 126     7488   5257   7303    766   1044    590       C  
ATOM   3102  O   GLN B 126      30.882 -32.057  81.888  1.00 58.52           O  
ANISOU 3102  O   GLN B 126     8230   6011   7996    732   1125    587       O  
ATOM   3103  CB  GLN B 126      29.937 -35.216  82.319  1.00 51.08           C  
ANISOU 3103  CB  GLN B 126     7507   4888   7013    686    935    629       C  
ATOM   3104  CG  GLN B 126      28.708 -34.561  81.701  1.00 53.36           C  
ANISOU 3104  CG  GLN B 126     7841   5212   7222    590    918    669       C  
ATOM   3105  CD  GLN B 126      28.791 -34.454  80.184  1.00 60.99           C  
ANISOU 3105  CD  GLN B 126     8958   6106   8111    581    996    611       C  
ATOM   3106  OE1 GLN B 126      28.841 -35.460  79.476  1.00 61.51           O  
ANISOU 3106  OE1 GLN B 126     9177   6047   8147    569   1008    558       O  
ATOM   3107  NE2 GLN B 126      28.814 -33.225  79.681  1.00 67.52           N  
ANISOU 3107  NE2 GLN B 126     9769   6996   8890    591   1056    621       N  
ATOM   3108  N   ALA B 127      31.142 -32.821  83.990  1.00 46.10           N  
ANISOU 3108  N   ALA B 127     6542   4474   6500    807    960    622       N  
ATOM   3109  CA  ALA B 127      31.075 -31.479  84.557  1.00 42.09           C  
ANISOU 3109  CA  ALA B 127     5912   4063   6017    811    969    629       C  
ATOM   3110  C   ALA B 127      32.265 -30.633  84.122  1.00 45.88           C  
ANISOU 3110  C   ALA B 127     6285   4540   6606    845   1073    538       C  
ATOM   3111  O   ALA B 127      32.120 -29.435  83.853  1.00 49.49           O  
ANISOU 3111  O   ALA B 127     6691   5036   7077    806   1143    538       O  
ATOM   3112  CB  ALA B 127      31.000 -31.552  86.081  1.00 46.20           C  
ANISOU 3112  CB  ALA B 127     6383   4630   6540    869    865    669       C  
ATOM   3113  N   VAL B 128      33.455 -31.233  84.061  1.00 42.87           N  
ANISOU 3113  N   VAL B 128     5858   4107   6323    913   1086    456       N  
ATOM   3114  CA  VAL B 128      34.627 -30.489  83.608  1.00 40.92           C  
ANISOU 3114  CA  VAL B 128     5483   3853   6213    921   1203    354       C  
ATOM   3115  C   VAL B 128      34.442 -30.038  82.164  1.00 46.27           C  
ANISOU 3115  C   VAL B 128     6264   4484   6833    842   1398    371       C  
ATOM   3116  O   VAL B 128      34.838 -28.928  81.789  1.00 46.32           O  
ANISOU 3116  O   VAL B 128     6204   4491   6904    799   1527    349       O  
ATOM   3117  CB  VAL B 128      35.900 -31.340  83.779  1.00 41.26           C  
ANISOU 3117  CB  VAL B 128     5441   3850   6387   1018   1168    248       C  
ATOM   3118  CG1 VAL B 128      37.045 -30.754  82.969  1.00 36.49           C  
ANISOU 3118  CG1 VAL B 128     4717   3220   5927    991   1342    140       C  
ATOM   3119  CG2 VAL B 128      36.275 -31.449  85.247  1.00 39.08           C  
ANISOU 3119  CG2 VAL B 128     5055   3621   6173   1130    967    216       C  
ATOM   3120  N   SER B 129      33.834 -30.891  81.333  1.00 56.71           N  
ANISOU 3120  N   SER B 129     7773   5747   8025    825   1422    408       N  
ATOM   3121  CA  SER B 129      33.634 -30.543  79.931  1.00 55.82           C  
ANISOU 3121  CA  SER B 129     7821   5577   7812    779   1593    420       C  
ATOM   3122  C   SER B 129      32.678 -29.366  79.779  1.00 52.48           C  
ANISOU 3122  C   SER B 129     7438   5204   7298    731   1587    502       C  
ATOM   3123  O   SER B 129      32.883 -28.498  78.922  1.00 54.38           O  
ANISOU 3123  O   SER B 129     7747   5407   7509    710   1753    512       O  
ATOM   3124  CB  SER B 129      33.113 -31.755  79.161  1.00 64.56           C  
ANISOU 3124  CB  SER B 129     9140   6604   8786    779   1572    419       C  
ATOM   3125  OG  SER B 129      32.607 -31.370  77.895  1.00 84.16           O  
ANISOU 3125  OG  SER B 129    11836   9034  11106    744   1680    443       O  
ATOM   3126  N   VAL B 130      31.627 -29.319  80.601  1.00 53.53           N  
ANISOU 3126  N   VAL B 130     7536   5414   7391    715   1406    562       N  
ATOM   3127  CA  VAL B 130      30.671 -28.221  80.508  1.00 54.33           C  
ANISOU 3127  CA  VAL B 130     7645   5570   7428    680   1369    627       C  
ATOM   3128  C   VAL B 130      31.309 -26.913  80.957  1.00 55.81           C  
ANISOU 3128  C   VAL B 130     7684   5783   7740    684   1459    607       C  
ATOM   3129  O   VAL B 130      31.126 -25.868  80.321  1.00 52.64           O  
ANISOU 3129  O   VAL B 130     7329   5366   7307    666   1544    638       O  
ATOM   3130  CB  VAL B 130      29.405 -28.540  81.321  1.00 51.36           C  
ANISOU 3130  CB  VAL B 130     7239   5263   7012    654   1180    684       C  
ATOM   3131  CG1 VAL B 130      28.348 -27.482  81.076  1.00 43.07           C  
ANISOU 3131  CG1 VAL B 130     6195   4259   5911    629   1129    744       C  
ATOM   3132  CG2 VAL B 130      28.884 -29.921  80.966  1.00 58.81           C  
ANISOU 3132  CG2 VAL B 130     8312   6151   7883    628   1101    694       C  
ATOM   3133  N   SER B 131      32.067 -26.947  82.055  1.00 55.94           N  
ANISOU 3133  N   SER B 131     7529   5827   7897    709   1424    551       N  
ATOM   3134  CA  SER B 131      32.741 -25.740  82.523  1.00 44.46           C  
ANISOU 3134  CA  SER B 131     5922   4381   6589    695   1485    502       C  
ATOM   3135  C   SER B 131      33.695 -25.200  81.465  1.00 42.98           C  
ANISOU 3135  C   SER B 131     5751   4101   6479    656   1712    470       C  
ATOM   3136  O   SER B 131      33.680 -24.003  81.149  1.00 47.88           O  
ANISOU 3136  O   SER B 131     6368   4687   7139    614   1826    492       O  
ATOM   3137  CB  SER B 131      33.491 -26.028  83.823  1.00 45.10           C  
ANISOU 3137  CB  SER B 131     5837   4506   6793    743   1361    412       C  
ATOM   3138  OG  SER B 131      34.199 -24.879  84.248  1.00 55.61           O  
ANISOU 3138  OG  SER B 131     7014   5838   8279    719   1395    328       O  
ATOM   3139  N   VAL B 132      34.546 -26.071  80.917  1.00 46.59           N  
ANISOU 3139  N   VAL B 132     6231   4502   6968    668   1798    417       N  
ATOM   3140  CA  VAL B 132      35.480 -25.648  79.877  1.00 47.41           C  
ANISOU 3140  CA  VAL B 132     6363   4501   7149    620   2057    388       C  
ATOM   3141  C   VAL B 132      34.732 -25.043  78.695  1.00 53.93           C  
ANISOU 3141  C   VAL B 132     7431   5269   7792    605   2219    492       C  
ATOM   3142  O   VAL B 132      35.136 -24.010  78.148  1.00 64.50           O  
ANISOU 3142  O   VAL B 132     8793   6527   9186    558   2434    513       O  
ATOM   3143  CB  VAL B 132      36.363 -26.832  79.443  1.00 43.72           C  
ANISOU 3143  CB  VAL B 132     5900   3990   6722    649   2114    309       C  
ATOM   3144  CG1 VAL B 132      37.244 -26.444  78.269  1.00 44.39           C  
ANISOU 3144  CG1 VAL B 132     6047   3952   6867    589   2416    287       C  
ATOM   3145  CG2 VAL B 132      37.201 -27.321  80.610  1.00 53.13           C  
ANISOU 3145  CG2 VAL B 132     6851   5243   8094    700   1937    192       C  
ATOM   3146  N   ALA B 133      33.631 -25.676  78.281  1.00 52.95           N  
ANISOU 3146  N   ALA B 133     7500   5177   7443    648   2098    549       N  
ATOM   3147  CA  ALA B 133      32.898 -25.196  77.113  1.00 52.07           C  
ANISOU 3147  CA  ALA B 133     7641   5027   7116    658   2156    618       C  
ATOM   3148  C   ALA B 133      32.318 -23.806  77.351  1.00 57.25           C  
ANISOU 3148  C   ALA B 133     8246   5723   7783    648   2100    671       C  
ATOM   3149  O   ALA B 133      32.541 -22.884  76.559  1.00 57.43           O  
ANISOU 3149  O   ALA B 133     8379   5673   7767    647   2262    693       O  
ATOM   3150  CB  ALA B 133      31.787 -26.183  76.753  1.00 43.77           C  
ANISOU 3150  CB  ALA B 133     6765   4005   5859    675   1945    652       C  
ATOM   3151  N   VAL B 134      31.570 -23.633  78.444  1.00 60.57           N  
ANISOU 3151  N   VAL B 134     8514   6244   8256    646   1880    687       N  
ATOM   3152  CA  VAL B 134      30.927 -22.346  78.696  1.00 53.87           C  
ANISOU 3152  CA  VAL B 134     7623   5423   7424    643   1820    732       C  
ATOM   3153  C   VAL B 134      31.961 -21.265  78.989  1.00 48.95           C  
ANISOU 3153  C   VAL B 134     6866   4733   7001    612   2023    687       C  
ATOM   3154  O   VAL B 134      31.789 -20.106  78.593  1.00 52.72           O  
ANISOU 3154  O   VAL B 134     7395   5162   7475    611   2090    723       O  
ATOM   3155  CB  VAL B 134      29.902 -22.471  79.836  1.00 49.10           C  
ANISOU 3155  CB  VAL B 134     6891   4925   6840    649   1584    747       C  
ATOM   3156  CG1 VAL B 134      30.603 -22.585  81.183  1.00 50.84           C  
ANISOU 3156  CG1 VAL B 134     6899   5178   7239    639   1581    675       C  
ATOM   3157  CG2 VAL B 134      28.956 -21.284  79.817  1.00 45.28           C  
ANISOU 3157  CG2 VAL B 134     6416   4454   6335    661   1507    807       C  
ATOM   3158  N   LEU B 135      33.043 -21.614  79.690  1.00 46.25           N  
ANISOU 3158  N   LEU B 135     6343   4374   6854    574   2099    607       N  
ATOM   3159  CA  LEU B 135      34.100 -20.633  79.912  1.00 43.57           C  
ANISOU 3159  CA  LEU B 135     5856   3947   6752    503   2282    551       C  
ATOM   3160  C   LEU B 135      34.799 -20.269  78.613  1.00 50.03           C  
ANISOU 3160  C   LEU B 135     6806   4638   7564    487   2608    560       C  
ATOM   3161  O   LEU B 135      35.270 -19.136  78.459  1.00 61.38           O  
ANISOU 3161  O   LEU B 135     8203   5987   9133    448   2742    530       O  
ATOM   3162  CB  LEU B 135      35.117 -21.154  80.928  1.00 47.02           C  
ANISOU 3162  CB  LEU B 135     6068   4397   7402    465   2184    428       C  
ATOM   3163  CG  LEU B 135      34.737 -21.092  82.407  1.00 49.30           C  
ANISOU 3163  CG  LEU B 135     6203   4799   7728    498   1916    364       C  
ATOM   3164  CD1 LEU B 135      35.862 -21.661  83.257  1.00 54.08           C  
ANISOU 3164  CD1 LEU B 135     6614   5441   8492    513   1806    209       C  
ATOM   3165  CD2 LEU B 135      34.414 -19.665  82.820  1.00 48.04           C  
ANISOU 3165  CD2 LEU B 135     5987   4611   7654    462   1931    360       C  
ATOM   3166  N   THR B 136      34.877 -21.210  77.670  1.00 51.44           N  
ANISOU 3166  N   THR B 136     7170   4792   7584    529   2689    571       N  
ATOM   3167  CA  THR B 136      35.496 -20.910  76.385  1.00 49.91           C  
ANISOU 3167  CA  THR B 136     7166   4455   7344    539   2917    547       C  
ATOM   3168  C   THR B 136      34.638 -19.944  75.583  1.00 47.42           C  
ANISOU 3168  C   THR B 136     7089   4103   6825    599   2924    629       C  
ATOM   3169  O   THR B 136      35.148 -18.987  74.989  1.00 55.07           O  
ANISOU 3169  O   THR B 136     8133   4939   7850    585   3126    623       O  
ATOM   3170  CB  THR B 136      35.724 -22.194  75.593  1.00 52.08           C  
ANISOU 3170  CB  THR B 136     7612   4696   7479    561   2971    536       C  
ATOM   3171  OG1 THR B 136      36.702 -22.999  76.259  1.00 44.09           O  
ANISOU 3171  OG1 THR B 136     6390   3661   6700    460   2964    502       O  
ATOM   3172  CG2 THR B 136      36.218 -21.865  74.196  1.00 58.40           C  
ANISOU 3172  CG2 THR B 136     8683   5306   8199    583   3219    523       C  
ATOM   3173  N   LEU B 137      33.327 -20.191  75.540  1.00 47.41           N  
ANISOU 3173  N   LEU B 137     7205   4217   6592    628   2637    722       N  
ATOM   3174  CA  LEU B 137      32.430 -19.266  74.861  1.00 50.01           C  
ANISOU 3174  CA  LEU B 137     7726   4536   6741    651   2540    830       C  
ATOM   3175  C   LEU B 137      32.429 -17.904  75.538  1.00 60.00           C  
ANISOU 3175  C   LEU B 137     8833   5777   8186    628   2558    838       C  
ATOM   3176  O   LEU B 137      32.296 -16.873  74.870  1.00 67.05           O  
ANISOU 3176  O   LEU B 137     9874   6584   9018    637   2631    907       O  
ATOM   3177  CB  LEU B 137      31.016 -19.842  74.824  1.00 44.18           C  
ANISOU 3177  CB  LEU B 137     7078   3911   5798    685   2214    906       C  
ATOM   3178  CG  LEU B 137      30.821 -21.141  74.040  1.00 43.85           C  
ANISOU 3178  CG  LEU B 137     7236   3876   5548    703   2167    904       C  
ATOM   3179  CD1 LEU B 137      29.425 -21.694  74.275  1.00 43.05           C  
ANISOU 3179  CD1 LEU B 137     7145   3877   5335    720   1835    958       C  
ATOM   3180  CD2 LEU B 137      31.067 -20.924  72.553  1.00 47.70           C  
ANISOU 3180  CD2 LEU B 137     8053   4255   5816    728   2325    945       C  
ATOM   3181  N   SER B 138      32.573 -17.880  76.864  1.00 55.59           N  
ANISOU 3181  N   SER B 138     7995   5284   7843    599   2491    773       N  
ATOM   3182  CA  SER B 138      32.629 -16.611  77.580  1.00 45.37           C  
ANISOU 3182  CA  SER B 138     6549   3953   6737    570   2518    758       C  
ATOM   3183  C   SER B 138      33.842 -15.793  77.156  1.00 49.65           C  
ANISOU 3183  C   SER B 138     7072   4333   7458    524   2840    699       C  
ATOM   3184  O   SER B 138      33.730 -14.598  76.859  1.00 50.10           O  
ANISOU 3184  O   SER B 138     7202   4298   7537    517   2913    744       O  
ATOM   3185  CB  SER B 138      32.658 -16.871  79.086  1.00 48.08           C  
ANISOU 3185  CB  SER B 138     6616   4389   7264    536   2387    684       C  
ATOM   3186  OG  SER B 138      31.369 -17.198  79.574  1.00 56.51           O  
ANISOU 3186  OG  SER B 138     7698   5574   8197    583   2107    738       O  
ATOM   3187  N   PHE B 139      35.017 -16.423  77.134  1.00 58.92           N  
ANISOU 3187  N   PHE B 139     8143   5451   8792    494   3042    590       N  
ATOM   3188  CA  PHE B 139      36.233 -15.700  76.780  1.00 60.72           C  
ANISOU 3188  CA  PHE B 139     8324   5498   9251    440   3328    501       C  
ATOM   3189  C   PHE B 139      36.223 -15.245  75.327  1.00 63.65           C  
ANISOU 3189  C   PHE B 139     9023   5735   9427    472   3517    583       C  
ATOM   3190  O   PHE B 139      36.866 -14.244  74.991  1.00 67.73           O  
ANISOU 3190  O   PHE B 139     9556   6092  10088    429   3743    558       O  
ATOM   3191  CB  PHE B 139      37.455 -16.569  77.071  1.00 60.68           C  
ANISOU 3191  CB  PHE B 139     8141   5469   9445    347   3318    381       C  
ATOM   3192  CG  PHE B 139      37.809 -16.644  78.530  1.00 75.58           C  
ANISOU 3192  CG  PHE B 139     9689   7463  11563    233   3130    304       C  
ATOM   3193  CD1 PHE B 139      36.827 -16.564  79.507  1.00 74.24           C  
ANISOU 3193  CD1 PHE B 139     9454   7412  11342    248   2911    359       C  
ATOM   3194  CD2 PHE B 139      39.127 -16.778  78.923  1.00 89.73           C  
ANISOU 3194  CD2 PHE B 139    11311   9084  13698     96   3164    184       C  
ATOM   3195  CE1 PHE B 139      37.158 -16.626  80.848  1.00 77.43           C  
ANISOU 3195  CE1 PHE B 139     9614   7824  11982    166   2752    268       C  
ATOM   3196  CE2 PHE B 139      39.465 -16.841  80.261  1.00 90.28           C  
ANISOU 3196  CE2 PHE B 139    11091   9201  14012     27   3003     67       C  
ATOM   3197  CZ  PHE B 139      38.479 -16.765  81.226  1.00 83.92           C  
ANISOU 3197  CZ  PHE B 139    10234   8535  13118     65   2793    110       C  
ATOM   3198  N   ILE B 140      35.503 -15.954  74.454  1.00 55.01           N  
ANISOU 3198  N   ILE B 140     8198   4704   8000    528   3408    687       N  
ATOM   3199  CA  ILE B 140      35.367 -15.502  73.072  1.00 56.59           C  
ANISOU 3199  CA  ILE B 140     8739   4798   7963    547   3531    790       C  
ATOM   3200  C   ILE B 140      34.526 -14.233  73.007  1.00 63.46           C  
ANISOU 3200  C   ILE B 140     9701   5658   8751    561   3427    917       C  
ATOM   3201  O   ILE B 140      34.907 -13.247  72.365  1.00 71.53           O  
ANISOU 3201  O   ILE B 140    10863   6527   9787    541   3636    962       O  
ATOM   3202  CB  ILE B 140      34.770 -16.617  72.195  1.00 57.40           C  
ANISOU 3202  CB  ILE B 140     9105   4971   7735    603   3409    851       C  
ATOM   3203  CG1 ILE B 140      35.769 -17.758  72.037  1.00 59.63           C  
ANISOU 3203  CG1 ILE B 140     9351   5195   8110    589   3584    730       C  
ATOM   3204  CG2 ILE B 140      34.366 -16.079  70.831  1.00 60.00           C  
ANISOU 3204  CG2 ILE B 140     9812   5215   7769    637   3463    982       C  
ATOM   3205  CD1 ILE B 140      35.135 -19.024  71.544  1.00 58.12           C  
ANISOU 3205  CD1 ILE B 140     9345   5094   7643    636   3423    759       C  
ATOM   3206  N   ALA B 141      33.365 -14.240  73.668  1.00 67.76           N  
ANISOU 3206  N   ALA B 141    10175   6343   9225    596   3108    977       N  
ATOM   3207  CA  ALA B 141      32.530 -13.043  73.694  1.00 60.01           C  
ANISOU 3207  CA  ALA B 141     9261   5329   8209    621   2991   1088       C  
ATOM   3208  C   ALA B 141      33.257 -11.879  74.357  1.00 59.01           C  
ANISOU 3208  C   ALA B 141     8947   5086   8386    556   3183   1022       C  
ATOM   3209  O   ALA B 141      33.132 -10.729  73.918  1.00 57.62           O  
ANISOU 3209  O   ALA B 141     8908   4781   8204    559   3267   1109       O  
ATOM   3210  CB  ALA B 141      31.209 -13.339  74.407  1.00 47.28           C  
ANISOU 3210  CB  ALA B 141     7562   3871   6532    670   2627   1130       C  
ATOM   3211  N   LEU B 142      34.023 -12.157  75.416  1.00 56.60           N  
ANISOU 3211  N   LEU B 142     8333   4814   8360    497   3249    868       N  
ATOM   3212  CA  LEU B 142      34.796 -11.103  76.068  1.00 63.73           C  
ANISOU 3212  CA  LEU B 142     9033   5597   9584    422   3430    773       C  
ATOM   3213  C   LEU B 142      35.843 -10.538  75.120  1.00 68.79           C  
ANISOU 3213  C   LEU B 142     9798   6034  10304    376   3782    755       C  
ATOM   3214  O   LEU B 142      36.064  -9.322  75.073  1.00 72.23           O  
ANISOU 3214  O   LEU B 142    10245   6325  10874    334   3927    769       O  
ATOM   3215  CB  LEU B 142      35.463 -11.649  77.334  1.00 57.77           C  
ANISOU 3215  CB  LEU B 142     7922   4916   9113    368   3410    597       C  
ATOM   3216  CG  LEU B 142      36.114 -10.672  78.315  1.00 58.29           C  
ANISOU 3216  CG  LEU B 142     7711   4897   9540    280   3505    461       C  
ATOM   3217  CD1 LEU B 142      35.043  -9.917  79.083  1.00 55.35           C  
ANISOU 3217  CD1 LEU B 142     7314   4577   9139    293   3275    521       C  
ATOM   3218  CD2 LEU B 142      37.042 -11.409  79.272  1.00 56.51           C  
ANISOU 3218  CD2 LEU B 142     7168   4727   9574    205   3469    281       C  
ATOM   3219  N   ASP B 143      36.507 -11.413  74.364  1.00 68.83           N  
ANISOU 3219  N   ASP B 143     9903   6008  10241    381   3935    718       N  
ATOM   3220  CA  ASP B 143      37.500 -10.961  73.398  1.00 65.68           C  
ANISOU 3220  CA  ASP B 143     9648   5400   9907    336   4287    700       C  
ATOM   3221  C   ASP B 143      36.861 -10.137  72.287  1.00 68.02           C  
ANISOU 3221  C   ASP B 143    10313   5609   9921    371   4330    896       C  
ATOM   3222  O   ASP B 143      37.392  -9.090  71.897  1.00 68.17           O  
ANISOU 3222  O   ASP B 143    10406   5441  10055    319   4585    916       O  
ATOM   3223  CB  ASP B 143      38.239 -12.169  72.828  1.00 71.56           C  
ANISOU 3223  CB  ASP B 143    10443   6121  10624    340   4413    621       C  
ATOM   3224  CG  ASP B 143      39.059 -11.828  71.613  1.00 86.38           C  
ANISOU 3224  CG  ASP B 143    12554   7788  12479    301   4764    638       C  
ATOM   3225  OD1 ASP B 143      40.122 -11.194  71.772  1.00 95.37           O  
ANISOU 3225  OD1 ASP B 143    13536   8752  13949    212   5028    521       O  
ATOM   3226  OD2 ASP B 143      38.639 -12.203  70.499  1.00 89.01           O  
ANISOU 3226  OD2 ASP B 143    13229   8124  12465    353   4776    761       O  
ATOM   3227  N   ARG B 144      35.718 -10.589  71.764  1.00 69.34           N  
ANISOU 3227  N   ARG B 144    10719   5897   9731    461   4077   1042       N  
ATOM   3228  CA  ARG B 144      35.035  -9.822  70.728  1.00 66.41           C  
ANISOU 3228  CA  ARG B 144    10705   5438   9089    513   4066   1235       C  
ATOM   3229  C   ARG B 144      34.506  -8.501  71.269  1.00 64.15           C  
ANISOU 3229  C   ARG B 144    10360   5089   8926    510   3985   1307       C  
ATOM   3230  O   ARG B 144      34.541  -7.479  70.574  1.00 66.37           O  
ANISOU 3230  O   ARG B 144    10864   5196   9156    511   4139   1423       O  
ATOM   3231  CB  ARG B 144      33.889 -10.640  70.135  1.00 60.03           C  
ANISOU 3231  CB  ARG B 144    10126   4773   7910    613   3764   1349       C  
ATOM   3232  CG  ARG B 144      34.321 -11.906  69.426  1.00 56.84           C  
ANISOU 3232  CG  ARG B 144     9851   4404   7340    622   3845   1294       C  
ATOM   3233  CD  ARG B 144      35.145 -11.604  68.184  1.00 65.31           C  
ANISOU 3233  CD  ARG B 144    11221   5283   8309    603   4199   1330       C  
ATOM   3234  NE  ARG B 144      36.539 -11.308  68.502  1.00 73.07           N  
ANISOU 3234  NE  ARG B 144    12000   6122   9640    502   4559   1187       N  
ATOM   3235  CZ  ARG B 144      37.325 -10.537  67.758  1.00 73.57           C  
ANISOU 3235  CZ  ARG B 144    12230   5972   9751    453   4912   1214       C  
ATOM   3236  NH1 ARG B 144      36.852  -9.986  66.649  1.00 73.34           N  
ANISOU 3236  NH1 ARG B 144    12599   5854   9411    504   4954   1393       N  
ATOM   3237  NH2 ARG B 144      38.582 -10.319  68.118  1.00 73.50           N  
ANISOU 3237  NH2 ARG B 144    11991   5828  10108    352   5218   1060       N  
ATOM   3238  N   TRP B 145      34.015  -8.504  72.510  1.00 65.66           N  
ANISOU 3238  N   TRP B 145    10267   5402   9279    509   3753   1241       N  
ATOM   3239  CA  TRP B 145      33.418  -7.301  73.081  1.00 61.65           C  
ANISOU 3239  CA  TRP B 145     9705   4829   8889    516   3651   1298       C  
ATOM   3240  C   TRP B 145      34.447  -6.186  73.233  1.00 58.98           C  
ANISOU 3240  C   TRP B 145     9280   4284   8845    417   3978   1230       C  
ATOM   3241  O   TRP B 145      34.176  -5.025  72.903  1.00 63.99           O  
ANISOU 3241  O   TRP B 145    10073   4757   9481    426   4035   1344       O  
ATOM   3242  CB  TRP B 145      32.782  -7.642  74.429  1.00 59.87           C  
ANISOU 3242  CB  TRP B 145     9187   4773   8786    528   3368   1212       C  
ATOM   3243  CG  TRP B 145      31.920  -6.568  75.013  1.00 59.74           C  
ANISOU 3243  CG  TRP B 145     9140   4707   8854    564   3204   1268       C  
ATOM   3244  CD1 TRP B 145      30.664  -6.217  74.611  1.00 61.07           C  
ANISOU 3244  CD1 TRP B 145     9502   4871   8831    673   2961   1425       C  
ATOM   3245  CD2 TRP B 145      32.231  -5.731  76.133  1.00 65.07           C  
ANISOU 3245  CD2 TRP B 145     9564   5317   9842    498   3257   1151       C  
ATOM   3246  NE1 TRP B 145      30.180  -5.201  75.400  1.00 62.67           N  
ANISOU 3246  NE1 TRP B 145     9597   5000   9215    688   2875   1414       N  
ATOM   3247  CE2 TRP B 145      31.123  -4.886  76.343  1.00 64.98           C  
ANISOU 3247  CE2 TRP B 145     9627   5257   9807    577   3056   1246       C  
ATOM   3248  CE3 TRP B 145      33.342  -5.609  76.972  1.00 62.38           C  
ANISOU 3248  CE3 TRP B 145     8939   4945   9818    383   3444    962       C  
ATOM   3249  CZ2 TRP B 145      31.094  -3.933  77.358  1.00 63.24           C  
ANISOU 3249  CZ2 TRP B 145     9226   4956   9848    543   3053   1156       C  
ATOM   3250  CZ3 TRP B 145      33.312  -4.662  77.979  1.00 65.58           C  
ANISOU 3250  CZ3 TRP B 145     9159   5279  10480    339   3422    871       C  
ATOM   3251  CH2 TRP B 145      32.196  -3.836  78.164  1.00 65.43           C  
ANISOU 3251  CH2 TRP B 145     9240   5211  10411    418   3236    968       C  
ATOM   3252  N   TYR B 146      35.636  -6.518  73.744  1.00 57.60           N  
ANISOU 3252  N   TYR B 146     8845   4094   8945    323   4188   1039       N  
ATOM   3253  CA  TYR B 146      36.702  -5.526  73.845  1.00 63.40           C  
ANISOU 3253  CA  TYR B 146     9472   4620   9997    215   4513    945       C  
ATOM   3254  C   TYR B 146      37.331  -5.202  72.499  1.00 73.34           C  
ANISOU 3254  C   TYR B 146    11029   5683  11152    193   4845   1031       C  
ATOM   3255  O   TYR B 146      37.882  -4.110  72.334  1.00 79.09           O  
ANISOU 3255  O   TYR B 146    11781   6200  12068    119   5101   1031       O  
ATOM   3256  CB  TYR B 146      37.784  -6.018  74.809  1.00 61.83           C  
ANISOU 3256  CB  TYR B 146     8879   4455  10158    129   4605    691       C  
ATOM   3257  CG  TYR B 146      37.468  -5.796  76.269  1.00 59.70           C  
ANISOU 3257  CG  TYR B 146     8290   4287  10106    105   4383    576       C  
ATOM   3258  CD1 TYR B 146      37.533  -4.526  76.826  1.00 59.50           C  
ANISOU 3258  CD1 TYR B 146     8159   4128  10319     40   4438    533       C  
ATOM   3259  CD2 TYR B 146      37.108  -6.854  77.092  1.00 60.83           C  
ANISOU 3259  CD2 TYR B 146     8254   4646  10213    143   4124    510       C  
ATOM   3260  CE1 TYR B 146      37.249  -4.316  78.161  1.00 55.85           C  
ANISOU 3260  CE1 TYR B 146     7424   3750  10047     14   4234    413       C  
ATOM   3261  CE2 TYR B 146      36.821  -6.654  78.428  1.00 59.44           C  
ANISOU 3261  CE2 TYR B 146     7812   4556  10218    115   3928    407       C  
ATOM   3262  CZ  TYR B 146      36.893  -5.383  78.958  1.00 58.47           C  
ANISOU 3262  CZ  TYR B 146     7591   4302  10322     51   3979    351       C  
ATOM   3263  OH  TYR B 146      36.608  -5.181  80.289  1.00 59.82           O  
ANISOU 3263  OH  TYR B 146     7519   4550  10661     19   3775    232       O  
ATOM   3264  N   ALA B 147      37.265  -6.121  71.537  1.00 72.41           N  
ANISOU 3264  N   ALA B 147    11149   5622  10743    251   4856   1101       N  
ATOM   3265  CA  ALA B 147      37.849  -5.856  70.228  1.00 73.28           C  
ANISOU 3265  CA  ALA B 147    11574   5542  10725    232   5183   1186       C  
ATOM   3266  C   ALA B 147      36.989  -4.917  69.395  1.00 79.01           C  
ANISOU 3266  C   ALA B 147    12680   6163  11178    299   5140   1430       C  
ATOM   3267  O   ALA B 147      37.521  -4.145  68.592  1.00 86.32           O  
ANISOU 3267  O   ALA B 147    13828   6867  12103    257   5455   1507       O  
ATOM   3268  CB  ALA B 147      38.077  -7.165  69.473  1.00 68.54           C  
ANISOU 3268  CB  ALA B 147    11118   5022   9901    272   5211   1166       C  
ATOM   3269  N   ILE B 148      35.675  -4.970  69.564  1.00 73.84           N  
ANISOU 3269  N   ILE B 148    12105   5645  10305    405   4757   1555       N  
ATOM   3270  CA  ILE B 148      34.739  -4.227  68.733  1.00 68.90           C  
ANISOU 3270  CA  ILE B 148    11849   4928   9401    500   4644   1794       C  
ATOM   3271  C   ILE B 148      34.164  -3.024  69.475  1.00 74.70           C  
ANISOU 3271  C   ILE B 148    12482   5578  10321    506   4515   1846       C  
ATOM   3272  O   ILE B 148      34.097  -1.922  68.928  1.00 85.51           O  
ANISOU 3272  O   ILE B 148    14087   6735  11669    516   4645   1992       O  
ATOM   3273  CB  ILE B 148      33.614  -5.150  68.212  1.00 67.04           C  
ANISOU 3273  CB  ILE B 148    11811   4878   8785    632   4288   1901       C  
ATOM   3274  CG1 ILE B 148      34.215  -6.256  67.335  1.00 66.55           C  
ANISOU 3274  CG1 ILE B 148    11910   4857   8521    627   4449   1855       C  
ATOM   3275  CG2 ILE B 148      32.580  -4.330  67.461  1.00 73.27           C  
ANISOU 3275  CG2 ILE B 148    12944   5569   9325    749   4116   2140       C  
ATOM   3276  CD1 ILE B 148      33.354  -7.502  67.205  1.00 63.75           C  
ANISOU 3276  CD1 ILE B 148    11597   4725   7901    716   4106   1859       C  
ATOM   3277  N   CYS B 149      33.720  -3.228  70.718  1.00 74.09           N  
ANISOU 3277  N   CYS B 149    12075   5653  10423    506   4260   1731       N  
ATOM   3278  CA  CYS B 149      33.042  -2.170  71.459  1.00 72.76           C  
ANISOU 3278  CA  CYS B 149    11819   5411  10416    530   4101   1769       C  
ATOM   3279  C   CYS B 149      34.020  -1.233  72.170  1.00 75.05           C  
ANISOU 3279  C   CYS B 149    11882   5531  11101    394   4383   1631       C  
ATOM   3280  O   CYS B 149      33.818  -0.013  72.172  1.00 88.21           O  
ANISOU 3280  O   CYS B 149    13644   6999  12873    393   4435   1714       O  
ATOM   3281  CB  CYS B 149      32.057  -2.783  72.455  1.00 67.64           C  
ANISOU 3281  CB  CYS B 149    10944   4986   9769    597   3708   1706       C  
ATOM   3282  SG  CYS B 149      30.697  -3.723  71.701  1.00 66.63           S  
ANISOU 3282  SG  CYS B 149    11053   5033   9231    758   3325   1863       S  
ATOM   3283  N   HIS B 150      35.076  -1.770  72.786  1.00 72.72           N  
ANISOU 3283  N   HIS B 150    11284   5298  11050    283   4554   1413       N  
ATOM   3284  CA  HIS B 150      36.031  -0.983  73.576  1.00 72.68           C  
ANISOU 3284  CA  HIS B 150    11002   5152  11463    147   4785   1237       C  
ATOM   3285  C   HIS B 150      37.434  -1.351  73.099  1.00 70.59           C  
ANISOU 3285  C   HIS B 150    10676   4804  11339     42   5160   1114       C  
ATOM   3286  O   HIS B 150      38.183  -2.062  73.780  1.00 73.18           O  
ANISOU 3286  O   HIS B 150    10686   5233  11885    -18   5190    900       O  
ATOM   3287  CB  HIS B 150      35.796  -1.218  75.069  1.00 71.78           C  
ANISOU 3287  CB  HIS B 150    10510   5198  11565    129   4543   1058       C  
ATOM   3288  CG  HIS B 150      34.396  -0.891  75.505  1.00 70.58           C  
ANISOU 3288  CG  HIS B 150    10425   5111  11282    241   4192   1166       C  
ATOM   3289  ND1 HIS B 150      33.374  -1.815  75.475  1.00 69.82           N  
ANISOU 3289  ND1 HIS B 150    10393   5225  10909    359   3875   1245       N  
ATOM   3290  CD2 HIS B 150      33.842   0.265  75.947  1.00 70.69           C  
ANISOU 3290  CD2 HIS B 150    10453   4986  11420    258   4116   1201       C  
ATOM   3291  CE1 HIS B 150      32.257  -1.250  75.898  1.00 65.43           C  
ANISOU 3291  CE1 HIS B 150     9871   4663  10328    448   3621   1315       C  
ATOM   3292  NE2 HIS B 150      32.513   0.013  76.190  1.00 69.95           N  
ANISOU 3292  NE2 HIS B 150    10420   5022  11136    395   3758   1290       N  
ATOM   3293  N   PRO B 151      37.823  -0.839  71.928  1.00 71.47           N  
ANISOU 3293  N   PRO B 151    11097   4711  11348     24   5454   1243       N  
ATOM   3294  CA  PRO B 151      38.995  -1.367  71.192  1.00 74.47           C  
ANISOU 3294  CA  PRO B 151    11510   5014  11770    -45   5803   1161       C  
ATOM   3295  C   PRO B 151      40.376  -1.306  71.855  1.00 87.70           C  
ANISOU 3295  C   PRO B 151    12803   6599  13918   -192   6071    886       C  
ATOM   3296  O   PRO B 151      41.175  -2.217  71.606  1.00104.80           O  
ANISOU 3296  O   PRO B 151    14884   8799  16136   -216   6208    762       O  
ATOM   3297  CB  PRO B 151      38.976  -0.530  69.905  1.00 78.67           C  
ANISOU 3297  CB  PRO B 151    12478   5307  12105    -37   6060   1381       C  
ATOM   3298  CG  PRO B 151      37.550  -0.066  69.774  1.00 77.96           C  
ANISOU 3298  CG  PRO B 151    12636   5257  11730     94   5726   1609       C  
ATOM   3299  CD  PRO B 151      37.135   0.221  71.175  1.00 74.74           C  
ANISOU 3299  CD  PRO B 151    11876   4943  11578     80   5468   1486       C  
ATOM   3300  N   LEU B 152      40.712  -0.298  72.659  1.00 81.79           N  
ANISOU 3300  N   LEU B 152    11818   5724  13533   -289   6143    772       N  
ATOM   3301  CA  LEU B 152      42.107  -0.125  73.070  1.00 85.86           C  
ANISOU 3301  CA  LEU B 152    12006   6106  14512   -436   6433    509       C  
ATOM   3302  C   LEU B 152      42.344  -0.150  74.577  1.00 94.22           C  
ANISOU 3302  C   LEU B 152    12592   7270  15937   -488   6231    250       C  
ATOM   3303  O   LEU B 152      43.175   0.600  75.098  1.00103.52           O  
ANISOU 3303  O   LEU B 152    13513   8289  17532   -615   6407     58       O  
ATOM   3304  CB  LEU B 152      42.697   1.149  72.472  1.00 91.07           C  
ANISOU 3304  CB  LEU B 152    12807   6445  15351   -547   6824    557       C  
ATOM   3305  CG  LEU B 152      42.498   1.314  70.965  1.00 91.26           C  
ANISOU 3305  CG  LEU B 152    13333   6329  15013   -501   7052    823       C  
ATOM   3306  CD1 LEU B 152      42.770   2.748  70.539  1.00 92.62           C  
ANISOU 3306  CD1 LEU B 152    13676   6182  15333   -595   7370    920       C  
ATOM   3307  CD2 LEU B 152      43.381   0.332  70.203  1.00 88.33           C  
ANISOU 3307  CD2 LEU B 152    13005   5955  14601   -520   7294    748       C  
ATOM   3308  N   LEU B 153      41.645  -1.020  75.300  1.00 92.92           N  
ANISOU 3308  N   LEU B 153    12306   7370  15630   -397   5863    229       N  
ATOM   3309  CA  LEU B 153      41.928  -1.219  76.717  1.00 88.06           C  
ANISOU 3309  CA  LEU B 153    11256   6869  15334   -439   5665    -26       C  
ATOM   3310  C   LEU B 153      42.791  -2.449  76.987  1.00 83.43           C  
ANISOU 3310  C   LEU B 153    10421   6384  14895   -440   5650   -233       C  
ATOM   3311  O   LEU B 153      43.741  -2.378  77.771  1.00 83.19           O  
ANISOU 3311  O   LEU B 153    10030   6300  15280   -525   5684   -509       O  
ATOM   3312  CB  LEU B 153      40.617  -1.320  77.502  1.00 83.77           C  
ANISOU 3312  CB  LEU B 153    10718   6528  14582   -349   5267     67       C  
ATOM   3313  CG  LEU B 153      39.591  -0.228  77.196  1.00 81.73           C  
ANISOU 3313  CG  LEU B 153    10744   6167  14144   -310   5213    288       C  
ATOM   3314  CD1 LEU B 153      38.294  -0.480  77.950  1.00 73.79           C  
ANISOU 3314  CD1 LEU B 153     9737   5358  12942   -209   4811    360       C  
ATOM   3315  CD2 LEU B 153      40.155   1.147  77.525  1.00 84.16           C  
ANISOU 3315  CD2 LEU B 153    10936   6226  14814   -435   5417    181       C  
ATOM   3316  N   PHE B 154      42.479  -3.580  76.360  1.00 79.53           N  
ANISOU 3316  N   PHE B 154    10116   6019  14083   -343   5578   -117       N  
ATOM   3317  CA  PHE B 154      43.214  -4.820  76.577  1.00 84.58           C  
ANISOU 3317  CA  PHE B 154    10563   6731  14844   -331   5535   -291       C  
ATOM   3318  C   PHE B 154      43.607  -5.420  75.237  1.00 93.74           C  
ANISOU 3318  C   PHE B 154    12006   7802  15809   -313   5772   -190       C  
ATOM   3319  O   PHE B 154      42.761  -5.567  74.350  1.00 95.75           O  
ANISOU 3319  O   PHE B 154    12623   8114  15642   -232   5750     53       O  
ATOM   3320  CB  PHE B 154      42.372  -5.822  77.376  1.00 78.54           C  
ANISOU 3320  CB  PHE B 154     9712   6236  13894   -231   5147   -274       C  
ATOM   3321  CG  PHE B 154      41.920  -5.308  78.713  1.00 77.88           C  
ANISOU 3321  CG  PHE B 154     9368   6254  13967   -252   4905   -367       C  
ATOM   3322  CD1 PHE B 154      42.766  -5.348  79.808  1.00 75.71           C  
ANISOU 3322  CD1 PHE B 154     8725   5997  14045   -353   4752   -628       C  
ATOM   3323  CD2 PHE B 154      40.652  -4.777  78.872  1.00 77.67           C  
ANISOU 3323  CD2 PHE B 154     9505   6321  13685   -210   4724   -174       C  
ATOM   3324  CE1 PHE B 154      42.352  -4.874  81.039  1.00 74.67           C  
ANISOU 3324  CE1 PHE B 154     8379   5962  14029   -385   4510   -723       C  
ATOM   3325  CE2 PHE B 154      40.233  -4.300  80.098  1.00 77.15           C  
ANISOU 3325  CE2 PHE B 154     9222   6330  13762   -242   4505   -265       C  
ATOM   3326  CZ  PHE B 154      41.085  -4.349  81.183  1.00 75.04           C  
ANISOU 3326  CZ  PHE B 154     8563   6070  13879   -317   4453   -554       C  
ATOM   3327  N   LYS B 155      44.885  -5.768  75.090  1.00 96.12           N  
ANISOU 3327  N   LYS B 155    12143   7956  16421   -394   5980   -386       N  
ATOM   3328  CA  LYS B 155      45.370  -6.415  73.877  1.00 94.92           C  
ANISOU 3328  CA  LYS B 155    12232   7711  16121   -396   6219   -319       C  
ATOM   3329  C   LYS B 155      45.174  -7.921  73.974  1.00 94.09           C  
ANISOU 3329  C   LYS B 155    12125   7774  15850   -315   5974   -325       C  
ATOM   3330  O   LYS B 155      45.490  -8.531  75.000  1.00 90.37           O  
ANISOU 3330  O   LYS B 155    11341   7393  15603   -338   5722   -493       O  
ATOM   3331  CB  LYS B 155      46.843  -6.101  73.620  1.00 98.57           C  
ANISOU 3331  CB  LYS B 155    12523   7921  17010   -541   6573   -519       C  
ATOM   3332  CG  LYS B 155      47.235  -6.351  72.173  1.00105.34           C  
ANISOU 3332  CG  LYS B 155    13708   8639  17676   -561   6919   -399       C  
ATOM   3333  CD  LYS B 155      48.729  -6.276  71.948  1.00110.38           C  
ANISOU 3333  CD  LYS B 155    14141   9045  18752   -711   7261   -613       C  
ATOM   3334  CE  LYS B 155      49.072  -6.739  70.540  1.00113.40           C  
ANISOU 3334  CE  LYS B 155    14857   9318  18912   -722   7588   -494       C  
ATOM   3335  NZ  LYS B 155      50.524  -6.632  70.228  1.00120.55           N  
ANISOU 3335  NZ  LYS B 155    15571   9988  20245   -881   7968   -693       N  
ATOM   3336  N   SER B 156      44.662  -8.516  72.901  1.00 97.53           N  
ANISOU 3336  N   SER B 156    12921   8260  15877   -240   6017   -132       N  
ATOM   3337  CA  SER B 156      44.427  -9.954  72.826  1.00 94.29           C  
ANISOU 3337  CA  SER B 156    12557   7993  15275   -169   5814   -114       C  
ATOM   3338  C   SER B 156      45.335 -10.544  71.751  1.00 96.24           C  
ANISOU 3338  C   SER B 156    12948   8092  15528   -226   6109   -136       C  
ATOM   3339  O   SER B 156      45.188 -10.230  70.565  1.00 97.79           O  
ANISOU 3339  O   SER B 156    13494   8206  15458   -212   6350     12       O  
ATOM   3340  CB  SER B 156      42.958 -10.248  72.529  1.00 96.15           C  
ANISOU 3340  CB  SER B 156    13079   8440  15014    -33   5569    113       C  
ATOM   3341  OG  SER B 156      42.684 -10.104  71.147  1.00102.83           O  
ANISOU 3341  OG  SER B 156    14337   9220  15512     -3   5761    292       O  
ATOM   3342  N   THR B 157      46.271 -11.393  72.168  1.00 97.28           N  
ANISOU 3342  N   THR B 157    12814   8190  15959   -301   6079   -314       N  
ATOM   3343  CA  THR B 157      47.178 -12.079  71.260  1.00 95.82           C  
ANISOU 3343  CA  THR B 157    12705   7889  15812   -369   6341   -352       C  
ATOM   3344  C   THR B 157      46.985 -13.584  71.385  1.00 94.63           C  
ANISOU 3344  C   THR B 157    12538   7901  15518   -327   6091   -337       C  
ATOM   3345  O   THR B 157      46.531 -14.084  72.418  1.00 97.55           O  
ANISOU 3345  O   THR B 157    12718   8432  15916   -293   5730   -361       O  
ATOM   3346  CB  THR B 157      48.644 -11.720  71.548  1.00 96.24           C  
ANISOU 3346  CB  THR B 157    12417   7753  16398   -532   6573   -589       C  
ATOM   3347  OG1 THR B 157      48.963 -12.048  72.906  1.00 94.77           O  
ANISOU 3347  OG1 THR B 157    11812   7657  16540   -576   6252   -772       O  
ATOM   3348  CG2 THR B 157      48.880 -10.234  71.323  1.00 97.51           C  
ANISOU 3348  CG2 THR B 157    12612   7730  16708   -588   6871   -600       C  
ATOM   3349  N   ALA B 158      47.326 -14.308  70.316  1.00 93.05           N  
ANISOU 3349  N   ALA B 158    12545   7657  15152   -334   6298   -291       N  
ATOM   3350  CA  ALA B 158      47.237 -15.762  70.367  1.00 85.10           C  
ANISOU 3350  CA  ALA B 158    11512   6800  14022   -306   6099   -283       C  
ATOM   3351  C   ALA B 158      48.123 -16.330  71.467  1.00 98.71           C  
ANISOU 3351  C   ALA B 158    12758   8584  16162   -404   5925   -477       C  
ATOM   3352  O   ALA B 158      47.793 -17.363  72.062  1.00107.04           O  
ANISOU 3352  O   ALA B 158    13696   9834  17138   -367   5617   -466       O  
ATOM   3353  CB  ALA B 158      47.613 -16.364  69.014  1.00 72.30           C  
ANISOU 3353  CB  ALA B 158    10171   5103  12196   -311   6399   -234       C  
ATOM   3354  N   ARG B 159      49.253 -15.677  71.747  1.00104.47           N  
ANISOU 3354  N   ARG B 159    13201   9164  17328   -527   6111   -662       N  
ATOM   3355  CA  ARG B 159      50.109 -16.120  72.841  1.00109.46           C  
ANISOU 3355  CA  ARG B 159    13356   9878  18357   -608   5905   -874       C  
ATOM   3356  C   ARG B 159      49.389 -16.026  74.181  1.00106.66           C  
ANISOU 3356  C   ARG B 159    12828   9693  18004   -568   5472   -876       C  
ATOM   3357  O   ARG B 159      49.531 -16.909  75.034  1.00100.19           O  
ANISOU 3357  O   ARG B 159    11745   9073  17249   -559   5161   -952       O  
ATOM   3358  CB  ARG B 159      51.390 -15.290  72.858  1.00118.42           C  
ANISOU 3358  CB  ARG B 159    14225  10802  19966   -742   6189  -1090       C  
ATOM   3359  CG  ARG B 159      52.294 -15.547  74.042  1.00123.77           C  
ANISOU 3359  CG  ARG B 159    14389  11561  21077   -813   5951  -1347       C  
ATOM   3360  CD  ARG B 159      53.377 -14.491  74.102  1.00133.72           C  
ANISOU 3360  CD  ARG B 159    15410  12590  22809   -939   6221  -1567       C  
ATOM   3361  NE  ARG B 159      52.835 -13.176  74.429  1.00140.50           N  
ANISOU 3361  NE  ARG B 159    16356  13340  23686   -939   6239  -1541       N  
ATOM   3362  CZ  ARG B 159      52.681 -12.726  75.669  1.00142.85           C  
ANISOU 3362  CZ  ARG B 159    16404  13708  24166   -943   5925  -1666       C  
ATOM   3363  NH1 ARG B 159      53.031 -13.486  76.697  1.00142.89           N  
ANISOU 3363  NH1 ARG B 159    16068  13898  24327   -944   5554  -1820       N  
ATOM   3364  NH2 ARG B 159      52.180 -11.518  75.882  1.00141.39           N  
ANISOU 3364  NH2 ARG B 159    16309  13424  23991   -931   5980  -1643       N  
ATOM   3365  N   ARG B 160      48.613 -14.959  74.384  1.00108.44           N  
ANISOU 3365  N   ARG B 160    13198   9858  18147   -529   5453   -799       N  
ATOM   3366  CA  ARG B 160      47.839 -14.791  75.608  1.00104.24           C  
ANISOU 3366  CA  ARG B 160    12539   9474  17596   -491   5075   -793       C  
ATOM   3367  C   ARG B 160      46.537 -15.578  75.586  1.00 95.64           C  
ANISOU 3367  C   ARG B 160    11682   8611  16044   -368   4816   -573       C  
ATOM   3368  O   ARG B 160      45.953 -15.814  76.649  1.00 94.87           O  
ANISOU 3368  O   ARG B 160    11442   8708  15897   -347   4467   -561       O  
ATOM   3369  CB  ARG B 160      47.563 -13.298  75.824  1.00111.61           C  
ANISOU 3369  CB  ARG B 160    13481  10347  18579   -490   5142   -798       C  
ATOM   3370  CG  ARG B 160      48.828 -12.492  76.117  1.00122.54           C  
ANISOU 3370  CG  ARG B 160    14566  11524  20472   -618   5343  -1054       C  
ATOM   3371  CD  ARG B 160      49.152 -12.394  77.601  1.00127.00           C  
ANISOU 3371  CD  ARG B 160    14729  12191  21333   -676   5001  -1262       C  
ATOM   3372  NE  ARG B 160      48.179 -11.552  78.296  1.00126.06           N  
ANISOU 3372  NE  ARG B 160    14645  12196  21055   -623   4796  -1185       N  
ATOM   3373  CZ  ARG B 160      48.352 -10.248  78.500  1.00130.17           C  
ANISOU 3373  CZ  ARG B 160    15085  12598  21776   -659   4934  -1277       C  
ATOM   3374  NH1 ARG B 160      49.460  -9.653  78.072  1.00134.23           N  
ANISOU 3374  NH1 ARG B 160    15476  12864  22659   -753   5274  -1450       N  
ATOM   3375  NH2 ARG B 160      47.427  -9.539  79.134  1.00130.72           N  
ANISOU 3375  NH2 ARG B 160    15182  12782  21702   -608   4755  -1207       N  
ATOM   3376  N   ALA B 161      46.069 -15.988  74.404  1.00 93.59           N  
ANISOU 3376  N   ALA B 161    11782   8322  15455   -288   4988   -414       N  
ATOM   3377  CA  ALA B 161      44.911 -16.872  74.341  1.00 87.76           C  
ANISOU 3377  CA  ALA B 161    11244   7788  14311   -175   4746   -242       C  
ATOM   3378  C   ALA B 161      45.255 -18.281  74.807  1.00 90.57           C  
ANISOU 3378  C   ALA B 161    11405   8293  14715   -200   4560   -293       C  
ATOM   3379  O   ALA B 161      44.419 -18.952  75.423  1.00 98.67           O  
ANISOU 3379  O   ALA B 161    12422   9520  15548   -137   4264   -212       O  
ATOM   3380  CB  ALA B 161      44.344 -16.895  72.921  1.00 84.90           C  
ANISOU 3380  CB  ALA B 161    11326   7352  13581    -75   4971    -95       C  
ATOM   3381  N   LEU B 162      46.476 -18.743  74.530  1.00 88.56           N  
ANISOU 3381  N   LEU B 162    10967   7996  14687   -272   4718   -434       N  
ATOM   3382  CA  LEU B 162      46.894 -20.053  75.014  1.00 87.26           C  
ANISOU 3382  CA  LEU B 162    10564   8037  14556   -245   4516   -517       C  
ATOM   3383  C   LEU B 162      47.015 -20.075  76.531  1.00 78.99           C  
ANISOU 3383  C   LEU B 162     9148   7164  13699   -240   4159   -640       C  
ATOM   3384  O   LEU B 162      46.808 -21.123  77.153  1.00 75.63           O  
ANISOU 3384  O   LEU B 162     8612   6961  13164   -141   3878   -653       O  
ATOM   3385  CB  LEU B 162      48.221 -20.453  74.369  1.00 96.93           C  
ANISOU 3385  CB  LEU B 162    11655   9163  16012   -301   4782   -664       C  
ATOM   3386  CG  LEU B 162      48.239 -20.551  72.844  1.00102.71           C  
ANISOU 3386  CG  LEU B 162    12749   9736  16539   -300   5151   -569       C  
ATOM   3387  CD1 LEU B 162      49.667 -20.718  72.359  1.00106.08           C  
ANISOU 3387  CD1 LEU B 162    12981  10045  17278   -381   5444   -744       C  
ATOM   3388  CD2 LEU B 162      47.372 -21.705  72.366  1.00 99.99           C  
ANISOU 3388  CD2 LEU B 162    12668   9534  15789   -187   5039   -431       C  
ATOM   3389  N   GLY B 163      47.349 -18.934  77.140  1.00 79.38           N  
ANISOU 3389  N   GLY B 163     9026   7111  14025   -323   4162   -747       N  
ATOM   3390  CA  GLY B 163      47.391 -18.862  78.588  1.00 77.60           C  
ANISOU 3390  CA  GLY B 163     8490   7050  13943   -306   3809   -874       C  
ATOM   3391  C   GLY B 163      46.018 -18.789  79.205  1.00 77.28           C  
ANISOU 3391  C   GLY B 163     8595   7161  13607   -233   3555   -718       C  
ATOM   3392  O   GLY B 163      45.812 -19.262  80.327  1.00 79.46           O  
ANISOU 3392  O   GLY B 163     8697   7653  13842   -152   3214   -778       O  
ATOM   3393  N   SER B 164      45.064 -18.189  78.496  1.00 72.30           N  
ANISOU 3393  N   SER B 164     8295   6412  12762   -237   3714   -525       N  
ATOM   3394  CA  SER B 164      43.686 -18.217  78.963  1.00 63.38           C  
ANISOU 3394  CA  SER B 164     7312   5431  11340   -160   3494   -363       C  
ATOM   3395  C   SER B 164      43.119 -19.628  78.880  1.00 68.80           C  
ANISOU 3395  C   SER B 164     8093   6327  11721    -44   3323   -270       C  
ATOM   3396  O   SER B 164      42.414 -20.079  79.792  1.00 70.08           O  
ANISOU 3396  O   SER B 164     8197   6695  11734     42   3024   -250       O  
ATOM   3397  CB  SER B 164      42.830 -17.250  78.145  1.00 61.08           C  
ANISOU 3397  CB  SER B 164     7342   5019  10845   -131   3665   -199       C  
ATOM   3398  OG  SER B 164      43.252 -15.908  78.317  1.00 69.49           O  
ANISOU 3398  OG  SER B 164     8311   5964  12129   -187   3774   -297       O  
ATOM   3399  N   ILE B 165      43.416 -20.334  77.786  1.00 68.23           N  
ANISOU 3399  N   ILE B 165     8184   6188  11553    -29   3519   -228       N  
ATOM   3400  CA  ILE B 165      42.928 -21.699  77.619  1.00 69.22           C  
ANISOU 3400  CA  ILE B 165     8411   6475  11413     80   3385   -163       C  
ATOM   3401  C   ILE B 165      43.421 -22.593  78.750  1.00 73.76           C  
ANISOU 3401  C   ILE B 165     8687   7245  12092    161   3086   -311       C  
ATOM   3402  O   ILE B 165      42.669 -23.428  79.268  1.00 74.06           O  
ANISOU 3402  O   ILE B 165     8773   7443  11923    275   2841   -261       O  
ATOM   3403  CB  ILE B 165      43.348 -22.244  76.240  1.00 66.98           C  
ANISOU 3403  CB  ILE B 165     8338   6065  11047     74   3671   -135       C  
ATOM   3404  CG1 ILE B 165      42.425 -21.687  75.154  1.00 61.19           C  
ANISOU 3404  CG1 ILE B 165     8022   5181  10045     90   3858     44       C  
ATOM   3405  CG2 ILE B 165      43.338 -23.766  76.240  1.00 68.59           C  
ANISOU 3405  CG2 ILE B 165     8529   6422  11112    177   3532   -163       C  
ATOM   3406  CD1 ILE B 165      42.998 -21.749  73.753  1.00 69.82           C  
ANISOU 3406  CD1 ILE B 165     9350   6093  11085     76   4193     40       C  
ATOM   3407  N   LEU B 166      44.689 -22.444  79.148  1.00 75.71           N  
ANISOU 3407  N   LEU B 166     8640   7461  12666    122   3099   -503       N  
ATOM   3408  CA  LEU B 166      45.203 -23.246  80.257  1.00 72.18           C  
ANISOU 3408  CA  LEU B 166     7930   7179  12316    237   2794   -649       C  
ATOM   3409  C   LEU B 166      44.525 -22.873  81.569  1.00 71.24           C  
ANISOU 3409  C   LEU B 166     7742   7194  12132    295   2481   -652       C  
ATOM   3410  O   LEU B 166      44.284 -23.740  82.417  1.00 74.81           O  
ANISOU 3410  O   LEU B 166     8158   7799  12468    443   2198   -669       O  
ATOM   3411  CB  LEU B 166      46.722 -23.086  80.370  1.00 75.73           C  
ANISOU 3411  CB  LEU B 166     8070   7554  13152    187   2875   -868       C  
ATOM   3412  CG  LEU B 166      47.572 -23.875  79.370  1.00 74.44           C  
ANISOU 3412  CG  LEU B 166     7902   7313  13069    189   3106   -916       C  
ATOM   3413  CD1 LEU B 166      49.049 -23.521  79.504  1.00 77.63           C  
ANISOU 3413  CD1 LEU B 166     7973   7622  13901    120   3206  -1145       C  
ATOM   3414  CD2 LEU B 166      47.358 -25.369  79.554  1.00 69.41           C  
ANISOU 3414  CD2 LEU B 166     7307   6822  12242    369   2905   -894       C  
ATOM   3415  N   GLY B 167      44.205 -21.591  81.751  1.00 68.11           N  
ANISOU 3415  N   GLY B 167     7349   6723  11806    191   2541   -637       N  
ATOM   3416  CA  GLY B 167      43.485 -21.186  82.946  1.00 67.21           C  
ANISOU 3416  CA  GLY B 167     7196   6731  11611    246   2270   -642       C  
ATOM   3417  C   GLY B 167      42.062 -21.707  82.967  1.00 65.76           C  
ANISOU 3417  C   GLY B 167     7266   6656  11065    337   2153   -451       C  
ATOM   3418  O   GLY B 167      41.535 -22.060  84.027  1.00 64.79           O  
ANISOU 3418  O   GLY B 167     7125   6675  10818    448   1879   -460       O  
ATOM   3419  N   ILE B 168      41.419 -21.769  81.800  1.00 62.41           N  
ANISOU 3419  N   ILE B 168     7094   6151  10468    296   2364   -282       N  
ATOM   3420  CA  ILE B 168      40.074 -22.329  81.733  1.00 57.39           C  
ANISOU 3420  CA  ILE B 168     6687   5606   9513    376   2256   -119       C  
ATOM   3421  C   ILE B 168      40.072 -23.767  82.230  1.00 53.51           C  
ANISOU 3421  C   ILE B 168     6178   5237   8915    509   2040   -150       C  
ATOM   3422  O   ILE B 168      39.165 -24.188  82.959  1.00 51.98           O  
ANISOU 3422  O   ILE B 168     6052   5148   8550    593   1829    -94       O  
ATOM   3423  CB  ILE B 168      39.530 -22.233  80.297  1.00 55.75           C  
ANISOU 3423  CB  ILE B 168     6759   5279   9145    328   2524     44       C  
ATOM   3424  CG1 ILE B 168      39.239 -20.777  79.937  1.00 58.08           C  
ANISOU 3424  CG1 ILE B 168     7131   5439   9498    235   2711    118       C  
ATOM   3425  CG2 ILE B 168      38.293 -23.099  80.145  1.00 49.57           C  
ANISOU 3425  CG2 ILE B 168     6185   4592   8056    421   2402    172       C  
ATOM   3426  CD1 ILE B 168      38.853 -20.580  78.496  1.00 60.40           C  
ANISOU 3426  CD1 ILE B 168     7742   5574   9635    216   2996    275       C  
ATOM   3427  N   TRP B 169      41.080 -24.547  81.835  1.00 56.17           N  
ANISOU 3427  N   TRP B 169     6434   5544   9363    533   2106   -239       N  
ATOM   3428  CA  TRP B 169      41.160 -25.936  82.275  1.00 45.99           C  
ANISOU 3428  CA  TRP B 169     5138   4338   7997    674   1915   -270       C  
ATOM   3429  C   TRP B 169      41.468 -26.042  83.764  1.00 50.26           C  
ANISOU 3429  C   TRP B 169     5496   4985   8616    786   1624   -375       C  
ATOM   3430  O   TRP B 169      40.868 -26.863  84.469  1.00 63.88           O  
ANISOU 3430  O   TRP B 169     7305   6782  10183    909   1416   -327       O  
ATOM   3431  CB  TRP B 169      42.206 -26.683  81.453  1.00 43.79           C  
ANISOU 3431  CB  TRP B 169     4811   3990   7837    683   2072   -349       C  
ATOM   3432  CG  TRP B 169      41.694 -27.084  80.112  1.00 50.35           C  
ANISOU 3432  CG  TRP B 169     5902   4740   8490    640   2295   -236       C  
ATOM   3433  CD1 TRP B 169      41.845 -26.408  78.939  1.00 51.86           C  
ANISOU 3433  CD1 TRP B 169     6210   4806   8689    522   2605   -190       C  
ATOM   3434  CD2 TRP B 169      40.926 -28.252  79.807  1.00 52.11           C  
ANISOU 3434  CD2 TRP B 169     6331   4982   8487    720   2227   -158       C  
ATOM   3435  NE1 TRP B 169      41.225 -27.086  77.918  1.00 52.23           N  
ANISOU 3435  NE1 TRP B 169     6533   4809   8502    540   2723    -93       N  
ATOM   3436  CE2 TRP B 169      40.653 -28.223  78.426  1.00 52.64           C  
ANISOU 3436  CE2 TRP B 169     6630   4949   8420    653   2491    -83       C  
ATOM   3437  CE3 TRP B 169      40.445 -29.324  80.568  1.00 44.62           C  
ANISOU 3437  CE3 TRP B 169     5415   4100   7438    842   1974   -147       C  
ATOM   3438  CZ2 TRP B 169      39.922 -29.222  77.788  1.00 50.28           C  
ANISOU 3438  CZ2 TRP B 169     6577   4633   7895    701   2493    -21       C  
ATOM   3439  CZ3 TRP B 169      39.719 -30.317  79.933  1.00 47.78           C  
ANISOU 3439  CZ3 TRP B 169     6047   4464   7645    872   1991    -75       C  
ATOM   3440  CH2 TRP B 169      39.464 -30.258  78.557  1.00 51.36           C  
ANISOU 3440  CH2 TRP B 169     6710   4833   7972    801   2239    -25       C  
ATOM   3441  N   ALA B 170      42.404 -25.232  84.259  1.00 48.82           N  
ANISOU 3441  N   ALA B 170     5076   4795   8679    748   1612   -522       N  
ATOM   3442  CA  ALA B 170      42.750 -25.294  85.675  1.00 54.79           C  
ANISOU 3442  CA  ALA B 170     5667   5648   9502    872   1329   -636       C  
ATOM   3443  C   ALA B 170      41.549 -24.965  86.549  1.00 62.19           C  
ANISOU 3443  C   ALA B 170     6731   6665  10232    914   1166   -547       C  
ATOM   3444  O   ALA B 170      41.324 -25.608  87.580  1.00 66.05           O  
ANISOU 3444  O   ALA B 170     7243   7237  10617   1070    932   -547       O  
ATOM   3445  CB  ALA B 170      43.907 -24.346  85.977  1.00 54.97           C  
ANISOU 3445  CB  ALA B 170     5405   5629   9850    793   1354   -829       C  
ATOM   3446  N   VAL B 171      40.766 -23.959  86.156  1.00 61.21           N  
ANISOU 3446  N   VAL B 171     6702   6504  10052    786   1299   -465       N  
ATOM   3447  CA  VAL B 171      39.582 -23.601  86.930  1.00 45.53           C  
ANISOU 3447  CA  VAL B 171     4828   4587   7883    821   1171   -386       C  
ATOM   3448  C   VAL B 171      38.528 -24.698  86.832  1.00 45.15           C  
ANISOU 3448  C   VAL B 171     5000   4575   7579    897   1110   -228       C  
ATOM   3449  O   VAL B 171      37.974 -25.143  87.843  1.00 40.83           O  
ANISOU 3449  O   VAL B 171     4505   4098   6909   1010    925   -202       O  
ATOM   3450  CB  VAL B 171      39.026 -22.243  86.469  1.00 45.45           C  
ANISOU 3450  CB  VAL B 171     4860   4512   7899    677   1334   -336       C  
ATOM   3451  CG1 VAL B 171      37.673 -21.990  87.109  1.00 40.00           C  
ANISOU 3451  CG1 VAL B 171     4302   3890   7005    718   1226   -238       C  
ATOM   3452  CG2 VAL B 171      40.000 -21.128  86.808  1.00 48.51           C  
ANISOU 3452  CG2 VAL B 171     5023   4841   8567    598   1370   -511       C  
ATOM   3453  N   SER B 172      38.234 -25.149  85.611  1.00 52.07           N  
ANISOU 3453  N   SER B 172     6016   5387   8381    833   1276   -123       N  
ATOM   3454  CA  SER B 172      37.224 -26.188  85.432  1.00 43.96           C  
ANISOU 3454  CA  SER B 172     5190   4373   7142    878   1227     12       C  
ATOM   3455  C   SER B 172      37.599 -27.465  86.176  1.00 50.80           C  
ANISOU 3455  C   SER B 172     6047   5263   7992   1024   1046    -24       C  
ATOM   3456  O   SER B 172      36.750 -28.085  86.826  1.00 53.67           O  
ANISOU 3456  O   SER B 172     6530   5652   8210   1086    920     66       O  
ATOM   3457  CB  SER B 172      37.027 -26.471  83.944  1.00 47.06           C  
ANISOU 3457  CB  SER B 172     5728   4683   7471    800   1436     94       C  
ATOM   3458  OG  SER B 172      36.570 -25.312  83.270  1.00 53.88           O  
ANISOU 3458  OG  SER B 172     6648   5506   8319    698   1597    158       O  
ATOM   3459  N   LEU B 173      38.871 -27.868  86.105  1.00 54.06           N  
ANISOU 3459  N   LEU B 173     6322   5655   8563   1084   1039   -147       N  
ATOM   3460  CA  LEU B 173      39.297 -29.082  86.795  1.00 47.79           C  
ANISOU 3460  CA  LEU B 173     5530   4867   7762   1254    857   -176       C  
ATOM   3461  C   LEU B 173      39.122 -28.965  88.303  1.00 52.59           C  
ANISOU 3461  C   LEU B 173     6110   5547   8326   1386    625   -188       C  
ATOM   3462  O   LEU B 173      38.831 -29.962  88.974  1.00 60.54           O  
ANISOU 3462  O   LEU B 173     7237   6540   9227   1521    470   -120       O  
ATOM   3463  CB  LEU B 173      40.756 -29.390  86.455  1.00 49.68           C  
ANISOU 3463  CB  LEU B 173     5591   5078   8208   1305    895   -319       C  
ATOM   3464  CG  LEU B 173      41.047 -29.876  85.036  1.00 51.76           C  
ANISOU 3464  CG  LEU B 173     5910   5255   8503   1227   1119   -313       C  
ATOM   3465  CD1 LEU B 173      42.546 -29.953  84.785  1.00 52.97           C  
ANISOU 3465  CD1 LEU B 173     5839   5382   8903   1261   1182   -471       C  
ATOM   3466  CD2 LEU B 173      40.386 -31.220  84.789  1.00 53.11           C  
ANISOU 3466  CD2 LEU B 173     6296   5372   8511   1292   1071   -216       C  
ATOM   3467  N   ALA B 174      39.302 -27.763  88.852  1.00 51.88           N  
ANISOU 3467  N   ALA B 174     5879   5514   8318   1352    605   -270       N  
ATOM   3468  CA  ALA B 174      39.205 -27.568  90.294  1.00 54.00           C  
ANISOU 3468  CA  ALA B 174     6117   5852   8548   1490    394   -300       C  
ATOM   3469  C   ALA B 174      37.760 -27.485  90.771  1.00 55.84           C  
ANISOU 3469  C   ALA B 174     6539   6100   8577   1482    374   -157       C  
ATOM   3470  O   ALA B 174      37.363 -28.197  91.699  1.00 59.79           O  
ANISOU 3470  O   ALA B 174     7157   6604   8958   1627    221    -77       O  
ATOM   3471  CB  ALA B 174      39.961 -26.305  90.699  1.00 55.46           C  
ANISOU 3471  CB  ALA B 174     6067   6079   8927   1437    374   -474       C  
ATOM   3472  N   ILE B 175      36.953 -26.625  90.143  1.00 53.88           N  
ANISOU 3472  N   ILE B 175     6329   5851   8294   1315    537   -106       N  
ATOM   3473  CA  ILE B 175      35.624 -26.334  90.674  1.00 53.55           C  
ANISOU 3473  CA  ILE B 175     6415   5837   8094   1299    536     12       C  
ATOM   3474  C   ILE B 175      34.678 -27.522  90.565  1.00 57.49           C  
ANISOU 3474  C   ILE B 175     7125   6304   8414   1304    542    201       C  
ATOM   3475  O   ILE B 175      33.645 -27.546  91.244  1.00 59.60           O  
ANISOU 3475  O   ILE B 175     7509   6604   8532   1323    531    317       O  
ATOM   3476  CB  ILE B 175      35.018 -25.098  89.980  1.00 44.01           C  
ANISOU 3476  CB  ILE B 175     5191   4631   6901   1134    698     25       C  
ATOM   3477  CG1 ILE B 175      34.797 -25.358  88.488  1.00 42.30           C  
ANISOU 3477  CG1 ILE B 175     5057   4351   6663   1007    863    117       C  
ATOM   3478  CG2 ILE B 175      35.902 -23.875  90.208  1.00 44.44           C  
ANISOU 3478  CG2 ILE B 175     5053   4695   7138   1105    702   -152       C  
ATOM   3479  CD1 ILE B 175      34.028 -24.258  87.785  1.00 38.78           C  
ANISOU 3479  CD1 ILE B 175     4647   3888   6199    883   1000    177       C  
ATOM   3480  N   MET B 176      34.989 -28.513  89.731  1.00 55.71           N  
ANISOU 3480  N   MET B 176     6957   6015   8195   1283    575    233       N  
ATOM   3481  CA  MET B 176      34.131 -29.683  89.594  1.00 46.68           C  
ANISOU 3481  CA  MET B 176     6010   4826   6899   1264    579    392       C  
ATOM   3482  C   MET B 176      34.504 -30.817  90.537  1.00 50.05           C  
ANISOU 3482  C   MET B 176     6520   5219   7279   1416    415    431       C  
ATOM   3483  O   MET B 176      33.881 -31.886  90.473  1.00 55.23           O  
ANISOU 3483  O   MET B 176     7347   5820   7818   1387    418    558       O  
ATOM   3484  CB  MET B 176      34.152 -30.186  88.147  1.00 40.41           C  
ANISOU 3484  CB  MET B 176     5265   3968   6122   1162    706    402       C  
ATOM   3485  CG  MET B 176      33.508 -29.225  87.171  1.00 43.70           C  
ANISOU 3485  CG  MET B 176     5680   4403   6520   1024    858    424       C  
ATOM   3486  SD  MET B 176      31.893 -28.662  87.744  1.00 45.14           S  
ANISOU 3486  SD  MET B 176     5933   4651   6566    969    851    547       S  
ATOM   3487  CE  MET B 176      31.458 -27.545  86.421  1.00 45.02           C  
ANISOU 3487  CE  MET B 176     5907   4633   6566    852    995    549       C  
ATOM   3488  N   VAL B 177      35.499 -30.612  91.406  1.00 54.32           N  
ANISOU 3488  N   VAL B 177     6945   5783   7912   1577    260    322       N  
ATOM   3489  CA  VAL B 177      35.852 -31.645  92.385  1.00 57.43           C  
ANISOU 3489  CA  VAL B 177     7440   6143   8238   1744     71    382       C  
ATOM   3490  C   VAL B 177      34.677 -31.990  93.286  1.00 47.46           C  
ANISOU 3490  C   VAL B 177     6423   4913   6696   1743     61    575       C  
ATOM   3491  O   VAL B 177      34.455 -33.181  93.551  1.00 54.39           O  
ANISOU 3491  O   VAL B 177     7481   5723   7461   1760     16    701       O  
ATOM   3492  CB  VAL B 177      37.103 -31.225  93.168  1.00 57.11           C  
ANISOU 3492  CB  VAL B 177     7201   6143   8355   1922   -115    223       C  
ATOM   3493  CG1 VAL B 177      37.334 -32.190  94.327  1.00 50.64           C  
ANISOU 3493  CG1 VAL B 177     6541   5332   7367   2090   -336    316       C  
ATOM   3494  CG2 VAL B 177      38.310 -31.196  92.252  1.00 53.64           C  
ANISOU 3494  CG2 VAL B 177     6597   5702   8081   1961    -50     58       C  
ATOM   3495  N   PRO B 178      33.921 -31.031  93.825  1.00 43.61           N  
ANISOU 3495  N   PRO B 178     5958   4517   6095   1726    111    601       N  
ATOM   3496  CA  PRO B 178      32.777 -31.397  94.677  1.00 45.58           C  
ANISOU 3496  CA  PRO B 178     6444   4797   6076   1706    138    778       C  
ATOM   3497  C   PRO B 178      31.784 -32.292  93.975  1.00 46.28           C  
ANISOU 3497  C   PRO B 178     6657   4803   6124   1532    288    923       C  
ATOM   3498  O   PRO B 178      31.166 -33.147  94.624  1.00 53.36           O  
ANISOU 3498  O   PRO B 178     7752   5674   6849   1513    293   1065       O  
ATOM   3499  CB  PRO B 178      32.166 -30.041  95.043  1.00 44.33           C  
ANISOU 3499  CB  PRO B 178     6195   4777   5872   1620    202    703       C  
ATOM   3500  CG  PRO B 178      33.259 -29.052  94.841  1.00 43.60           C  
ANISOU 3500  CG  PRO B 178     5858   4721   5987   1669    123    484       C  
ATOM   3501  CD  PRO B 178      34.046 -29.570  93.679  1.00 52.29           C  
ANISOU 3501  CD  PRO B 178     6856   5700   7312   1673    163    450       C  
ATOM   3502  N   GLN B 179      31.597 -32.116  92.665  1.00 46.27           N  
ANISOU 3502  N   GLN B 179     6543   4770   6266   1386    404    872       N  
ATOM   3503  CA  GLN B 179      30.720 -33.013  91.920  1.00 54.39           C  
ANISOU 3503  CA  GLN B 179     7667   5734   7264   1225    497    958       C  
ATOM   3504  C   GLN B 179      31.205 -34.455  92.022  1.00 56.23           C  
ANISOU 3504  C   GLN B 179     8020   5860   7485   1270    413    997       C  
ATOM   3505  O   GLN B 179      30.420 -35.370  92.298  1.00 65.18           O  
ANISOU 3505  O   GLN B 179     9301   6942   8521   1191    444   1110       O  
ATOM   3506  CB  GLN B 179      30.638 -32.571  90.463  1.00 55.35           C  
ANISOU 3506  CB  GLN B 179     7675   5849   7507   1106    592    875       C  
ATOM   3507  CG  GLN B 179      29.631 -33.361  89.654  1.00 55.80           C  
ANISOU 3507  CG  GLN B 179     7818   5856   7529    953    657    934       C  
ATOM   3508  CD  GLN B 179      28.214 -33.191  90.174  1.00 56.26           C  
ANISOU 3508  CD  GLN B 179     7914   5963   7498    854    717   1034       C  
ATOM   3509  OE1 GLN B 179      27.646 -32.100  90.117  1.00 56.83           O  
ANISOU 3509  OE1 GLN B 179     7897   6111   7583    821    773   1026       O  
ATOM   3510  NE2 GLN B 179      27.636 -34.273  90.682  1.00 55.28           N  
ANISOU 3510  NE2 GLN B 179     7915   5784   7306    802    717   1125       N  
ATOM   3511  N   ALA B 180      32.501 -34.679  91.794  1.00 49.00           N  
ANISOU 3511  N   ALA B 180     7025   4898   6696   1393    313    895       N  
ATOM   3512  CA  ALA B 180      33.053 -36.021  91.937  1.00 49.75           C  
ANISOU 3512  CA  ALA B 180     7219   4877   6808   1467    219    928       C  
ATOM   3513  C   ALA B 180      32.909 -36.537  93.363  1.00 53.37           C  
ANISOU 3513  C   ALA B 180     7847   5335   7095   1564    113   1058       C  
ATOM   3514  O   ALA B 180      32.652 -37.727  93.576  1.00 49.21           O  
ANISOU 3514  O   ALA B 180     7479   4706   6512   1542    104   1162       O  
ATOM   3515  CB  ALA B 180      34.521 -36.033  91.519  1.00 47.25           C  
ANISOU 3515  CB  ALA B 180     6741   4520   6694   1601    128    774       C  
ATOM   3516  N   ALA B 181      33.088 -35.660  94.355  1.00 54.20           N  
ANISOU 3516  N   ALA B 181     7939   5552   7104   1678     33   1048       N  
ATOM   3517  CA  ALA B 181      33.069 -36.102  95.747  1.00 48.98           C  
ANISOU 3517  CA  ALA B 181     7474   4908   6228   1797    -83   1161       C  
ATOM   3518  C   ALA B 181      31.721 -36.698  96.134  1.00 50.72           C  
ANISOU 3518  C   ALA B 181     7907   5100   6265   1642     71   1334       C  
ATOM   3519  O   ALA B 181      31.661 -37.657  96.910  1.00 59.25           O  
ANISOU 3519  O   ALA B 181     9184   6117   7213   1682     27   1453       O  
ATOM   3520  CB  ALA B 181      33.410 -34.929  96.667  1.00 53.31           C  
ANISOU 3520  CB  ALA B 181     7982   5600   6675   1945   -199   1087       C  
ATOM   3521  N   VAL B 182      30.624 -36.143  95.616  1.00 49.30           N  
ANISOU 3521  N   VAL B 182     7674   4964   6095   1462    256   1344       N  
ATOM   3522  CA  VAL B 182      29.306 -36.621  96.027  1.00 46.78           C  
ANISOU 3522  CA  VAL B 182     7498   4628   5647   1304    413   1479       C  
ATOM   3523  C   VAL B 182      28.857 -37.875  95.282  1.00 54.29           C  
ANISOU 3523  C   VAL B 182     8488   5439   6703   1155    474   1522       C  
ATOM   3524  O   VAL B 182      27.906 -38.532  95.723  1.00 55.37           O  
ANISOU 3524  O   VAL B 182     8748   5528   6762   1035    584   1633       O  
ATOM   3525  CB  VAL B 182      28.254 -35.511  95.854  1.00 45.79           C  
ANISOU 3525  CB  VAL B 182     7272   4611   5517   1182    573   1464       C  
ATOM   3526  CG1 VAL B 182      28.579 -34.340  96.764  1.00 41.40           C  
ANISOU 3526  CG1 VAL B 182     6724   4181   4827   1339    526   1438       C  
ATOM   3527  CG2 VAL B 182      28.183 -35.068  94.402  1.00 40.82           C  
ANISOU 3527  CG2 VAL B 182     6438   3975   5097   1080    612   1355       C  
ATOM   3528  N   MET B 183      29.503 -38.232  94.170  1.00 49.76           N  
ANISOU 3528  N   MET B 183     7815   4788   6305   1158    419   1428       N  
ATOM   3529  CA  MET B 183      29.082 -39.411  93.423  1.00 52.66           C  
ANISOU 3529  CA  MET B 183     8233   5013   6762   1032    467   1451       C  
ATOM   3530  C   MET B 183      29.299 -40.669  94.261  1.00 60.10           C  
ANISOU 3530  C   MET B 183     9372   5827   7635   1095    415   1576       C  
ATOM   3531  O   MET B 183      30.362 -40.847  94.862  1.00 61.81           O  
ANISOU 3531  O   MET B 183     9637   6028   7821   1287    272   1585       O  
ATOM   3532  CB  MET B 183      29.848 -39.499  92.103  1.00 53.34           C  
ANISOU 3532  CB  MET B 183     8201   5046   7020   1054    425   1315       C  
ATOM   3533  CG  MET B 183      29.678 -38.282  91.183  1.00 55.82           C  
ANISOU 3533  CG  MET B 183     8342   5471   7394    993    487   1202       C  
ATOM   3534  SD  MET B 183      27.983 -37.676  91.017  1.00 60.16           S  
ANISOU 3534  SD  MET B 183     8857   6104   7897    786    625   1247       S  
ATOM   3535  CE  MET B 183      27.219 -39.046  90.158  1.00 63.51           C  
ANISOU 3535  CE  MET B 183     9368   6370   8394    626    661   1265       C  
ATOM   3536  N   GLU B 184      28.289 -41.544  94.303  1.00 53.70           N  
ANISOU 3536  N   GLU B 184     8669   4919   6816    936    525   1670       N  
ATOM   3537  CA  GLU B 184      28.389 -42.816  95.012  1.00 62.42           C  
ANISOU 3537  CA  GLU B 184     9975   5871   7871    974    505   1804       C  
ATOM   3538  C   GLU B 184      27.640 -43.893  94.230  1.00 64.55           C  
ANISOU 3538  C   GLU B 184    10279   5974   8274    796    596   1820       C  
ATOM   3539  O   GLU B 184      26.612 -43.619  93.604  1.00 59.27           O  
ANISOU 3539  O   GLU B 184     9519   5334   7666    609    706   1779       O  
ATOM   3540  CB  GLU B 184      27.845 -42.713  96.446  1.00 73.81           C  
ANISOU 3540  CB  GLU B 184    11580   7368   9095    981    573   1949       C  
ATOM   3541  CG  GLU B 184      28.782 -41.989  97.420  1.00 80.13           C  
ANISOU 3541  CG  GLU B 184    12426   8288   9730   1207    433   1950       C  
ATOM   3542  CD  GLU B 184      30.224 -42.455  97.329  1.00 86.64           C  
ANISOU 3542  CD  GLU B 184    13252   9041  10629   1424    218   1909       C  
ATOM   3543  OE1 GLU B 184      30.465 -43.679  97.364  1.00 86.94           O  
ANISOU 3543  OE1 GLU B 184    13413   8907  10713   1453    184   1991       O  
ATOM   3544  OE2 GLU B 184      31.120 -41.584  97.239  1.00 87.01           O  
ANISOU 3544  OE2 GLU B 184    13161   9194  10706   1569     84   1791       O  
ATOM   3545  N   CYS B 185      28.167 -45.125  94.262  1.00 68.07           N  
ANISOU 3545  N   CYS B 185    10854   6233   8777    863    537   1876       N  
ATOM   3546  CA  CYS B 185      27.576 -46.280  93.579  1.00 61.54           C  
ANISOU 3546  CA  CYS B 185    10088   5209   8086    715    608   1890       C  
ATOM   3547  C   CYS B 185      26.903 -47.210  94.590  1.00 66.33           C  
ANISOU 3547  C   CYS B 185    10901   5685   8615    645    705   2078       C  
ATOM   3548  O   CYS B 185      27.587 -47.842  95.403  1.00 75.53           O  
ANISOU 3548  O   CYS B 185    12231   6761   9707    799    633   2190       O  
ATOM   3549  CB  CYS B 185      28.651 -47.026  92.786  1.00 61.54           C  
ANISOU 3549  CB  CYS B 185    10086   5064   8233    841    494   1805       C  
ATOM   3550  SG  CYS B 185      28.050 -48.048  91.420  1.00 75.85           S  
ANISOU 3550  SG  CYS B 185    11908   6670  10241    665    563   1719       S  
ATOM   3551  N   SER B 186      25.565 -47.290  94.542  1.00 68.89           N  
ANISOU 3551  N   SER B 186    11216   5994   8965    415    871   2113       N  
ATOM   3552  CA  SER B 186      24.778 -48.109  95.464  1.00 76.10           C  
ANISOU 3552  CA  SER B 186    12310   6782   9821    310   1014   2287       C  
ATOM   3553  C   SER B 186      23.775 -49.005  94.736  1.00 79.40           C  
ANISOU 3553  C   SER B 186    12722   7015  10433     73   1131   2275       C  
ATOM   3554  O   SER B 186      23.124 -48.577  93.778  1.00 80.29           O  
ANISOU 3554  O   SER B 186    12659   7178  10669    -76   1159   2145       O  
ATOM   3555  CB  SER B 186      24.035 -47.226  96.479  1.00 83.69           C  
ANISOU 3555  CB  SER B 186    13272   7919  10607    257   1148   2359       C  
ATOM   3556  OG  SER B 186      23.505 -46.064  95.863  1.00 88.73           O  
ANISOU 3556  OG  SER B 186    13682   8738  11292    167   1178   2226       O  
ATOM   3557  N   SER B 187      23.661 -50.252  95.204  1.00 84.45           N  
ANISOU 3557  N   SER B 187    13561   7427  11101     42   1192   2411       N  
ATOM   3558  CA  SER B 187      22.669 -51.216  94.732  1.00 84.50           C  
ANISOU 3558  CA  SER B 187    13592   7221  11293   -195   1321   2420       C  
ATOM   3559  C   SER B 187      21.317 -51.001  95.411  1.00 87.81           C  
ANISOU 3559  C   SER B 187    13993   7686  11684   -410   1551   2506       C  
ATOM   3560  O   SER B 187      21.237 -50.466  96.521  1.00 89.28           O  
ANISOU 3560  O   SER B 187    14247   8004  11671   -349   1632   2614       O  
ATOM   3561  CB  SER B 187      23.146 -52.651  94.973  1.00 90.07           C  
ANISOU 3561  CB  SER B 187    14527   7639  12056   -134   1302   2536       C  
ATOM   3562  OG  SER B 187      22.515 -53.566  94.087  1.00 93.98           O  
ANISOU 3562  OG  SER B 187    15011   7910  12786   -329   1356   2468       O  
ATOM   3563  N   VAL B 188      20.244 -51.424  94.726  1.00 89.66           N  
ANISOU 3563  N   VAL B 188    14131   7805  12130   -665   1659   2441       N  
ATOM   3564  CA  VAL B 188      18.896 -51.280  95.282  1.00 89.96           C  
ANISOU 3564  CA  VAL B 188    14111   7871  12201   -892   1899   2500       C  
ATOM   3565  C   VAL B 188      18.838 -51.859  96.693  1.00 90.41           C  
ANISOU 3565  C   VAL B 188    14416   7839  12097   -861   2061   2724       C  
ATOM   3566  O   VAL B 188      18.325 -51.227  97.623  1.00 86.34           O  
ANISOU 3566  O   VAL B 188    13902   7469  11436   -883   2220   2800       O  
ATOM   3567  CB  VAL B 188      17.859 -51.946  94.359  1.00 86.06           C  
ANISOU 3567  CB  VAL B 188    13500   7201  11998  -1172   1973   2400       C  
ATOM   3568  CG1 VAL B 188      17.976 -53.465  94.416  1.00 91.37           C  
ANISOU 3568  CG1 VAL B 188    14387   7550  12781  -1224   2008   2491       C  
ATOM   3569  CG2 VAL B 188      16.446 -51.511  94.720  1.00 84.33           C  
ANISOU 3569  CG2 VAL B 188    13115   7064  11861  -1410   2202   2400       C  
ATOM   3570  N   LEU B 189      19.325 -53.084  96.861  1.00 98.26           N  
ANISOU 3570  N   LEU B 189    15637   8580  13118   -810   2037   2834       N  
ATOM   3571  CA  LEU B 189      19.486 -53.687  98.177  1.00100.40           C  
ANISOU 3571  CA  LEU B 189    16197   8745  13206   -732   2155   3065       C  
ATOM   3572  C   LEU B 189      20.989 -53.829  98.357  1.00121.89           C  
ANISOU 3572  C   LEU B 189    19073  11458  15783   -419   1912   3107       C  
ATOM   3573  O   LEU B 189      21.597 -54.734  97.765  1.00122.96           O  
ANISOU 3573  O   LEU B 189    19279  11385  16056   -358   1789   3089       O  
ATOM   3574  CB  LEU B 189      18.773 -55.040  98.303  1.00 90.62           C  
ANISOU 3574  CB  LEU B 189    15110   7190  12132   -933   2343   3179       C  
ATOM   3575  CG  LEU B 189      17.238 -55.032  98.390  1.00 85.59           C  
ANISOU 3575  CG  LEU B 189    14340   6533  11645  -1254   2630   3168       C  
ATOM   3576  CD1 LEU B 189      16.672 -56.233  97.655  1.00 83.41           C  
ANISOU 3576  CD1 LEU B 189    14063   5951  11679  -1481   2692   3129       C  
ATOM   3577  CD2 LEU B 189      16.763 -55.028  99.847  1.00 88.18           C  
ANISOU 3577  CD2 LEU B 189    14862   6879  11764  -1272   2894   3376       C  
ATOM   3578  N   PRO B 190      21.624 -52.997  99.185  1.00148.52           N  
ANISOU 3578  N   PRO B 190    22502  15037  18893   -211   1838   3155       N  
ATOM   3579  CA  PRO B 190      23.080 -52.804  99.060  1.00145.72           C  
ANISOU 3579  CA  PRO B 190    22173  14738  18458     80   1562   3112       C  
ATOM   3580  C   PRO B 190      23.865 -54.094  99.190  1.00142.39           C  
ANISOU 3580  C   PRO B 190    21981  14043  18078    217   1466   3230       C  
ATOM   3581  O   PRO B 190      24.924 -54.226  98.564  1.00143.61           O  
ANISOU 3581  O   PRO B 190    22081  14167  18318    392   1250   3137       O  
ATOM   3582  CB  PRO B 190      23.393 -51.850 100.225  1.00147.23           C  
ANISOU 3582  CB  PRO B 190    22444  15155  18341    242   1548   3183       C  
ATOM   3583  CG  PRO B 190      22.146 -51.073 100.411  1.00146.18           C  
ANISOU 3583  CG  PRO B 190    22180  15173  18187     30   1772   3151       C  
ATOM   3584  CD  PRO B 190      21.031 -52.053 100.153  1.00149.59           C  
ANISOU 3584  CD  PRO B 190    22636  15385  18817   -240   1994   3208       C  
ATOM   3585  N   GLU B 191      23.379 -55.056  99.971  1.00123.61           N  
ANISOU 3585  N   GLU B 191    19857  11453  15656    143   1632   3432       N  
ATOM   3586  CA  GLU B 191      24.071 -56.331 100.059  1.00104.55           C  
ANISOU 3586  CA  GLU B 191    17671   8749  13306    269   1546   3553       C  
ATOM   3587  C   GLU B 191      24.139 -57.032  98.707  1.00 90.77           C  
ANISOU 3587  C   GLU B 191    15794   6811  11882    179   1479   3403       C  
ATOM   3588  O   GLU B 191      25.013 -57.883  98.501  1.00 82.44           O  
ANISOU 3588  O   GLU B 191    14854   5553  10917    341   1338   3431       O  
ATOM   3589  CB  GLU B 191      23.387 -57.232 101.089  1.00112.04           C  
ANISOU 3589  CB  GLU B 191    18925   9485  14161    169   1776   3803       C  
ATOM   3590  CG  GLU B 191      23.339 -56.646 102.491  1.00124.69           C  
ANISOU 3590  CG  GLU B 191    20716  11250  15409    272   1856   3963       C  
ATOM   3591  CD  GLU B 191      22.377 -55.480 102.605  1.00131.02           C  
ANISOU 3591  CD  GLU B 191    21319  12319  16141     98   2028   3867       C  
ATOM   3592  OE1 GLU B 191      21.634 -55.231 101.632  1.00129.77           O  
ANISOU 3592  OE1 GLU B 191    20889  12196  16222   -124   2102   3702       O  
ATOM   3593  OE2 GLU B 191      22.368 -54.809 103.657  1.00135.01           O  
ANISOU 3593  OE2 GLU B 191    21945  12997  16356    191   2081   3950       O  
ATOM   3594  N   LEU B 192      23.235 -56.689  97.789  1.00 86.73           N  
ANISOU 3594  N   LEU B 192    15051   6356  11545    -67   1572   3237       N  
ATOM   3595  CA  LEU B 192      23.160 -57.330  96.481  1.00 83.60           C  
ANISOU 3595  CA  LEU B 192    14547   5778  11438   -177   1519   3075       C  
ATOM   3596  C   LEU B 192      24.353 -57.006  95.590  1.00 85.43           C  
ANISOU 3596  C   LEU B 192    14647   6087  11726     37   1272   2897       C  
ATOM   3597  O   LEU B 192      24.607 -57.739  94.629  1.00 90.38           O  
ANISOU 3597  O   LEU B 192    15258   6517  12564     23   1204   2783       O  
ATOM   3598  CB  LEU B 192      21.866 -56.910  95.783  1.00 81.59           C  
ANISOU 3598  CB  LEU B 192    14075   5597  11329   -484   1662   2936       C  
ATOM   3599  CG  LEU B 192      21.506 -57.418  94.386  1.00 78.96           C  
ANISOU 3599  CG  LEU B 192    13613   5105  11282   -652   1623   2738       C  
ATOM   3600  CD1 LEU B 192      21.269 -58.917  94.386  1.00 80.62           C  
ANISOU 3600  CD1 LEU B 192    14024   4935  11672   -758   1704   2823       C  
ATOM   3601  CD2 LEU B 192      20.267 -56.683  93.909  1.00 76.45           C  
ANISOU 3601  CD2 LEU B 192    13059   4938  11050   -915   1735   2612       C  
ATOM   3602  N   ALA B 193      25.078 -55.925  95.875  1.00 76.88           N  
ANISOU 3602  N   ALA B 193    13468   5275  10468    229   1148   2860       N  
ATOM   3603  CA  ALA B 193      26.145 -55.490  94.981  1.00 68.64           C  
ANISOU 3603  CA  ALA B 193    12262   4324   9494    406    947   2673       C  
ATOM   3604  C   ALA B 193      27.272 -56.509  94.894  1.00 74.69           C  
ANISOU 3604  C   ALA B 193    13160   4858  10361    622    808   2703       C  
ATOM   3605  O   ALA B 193      28.045 -56.487  93.930  1.00 79.83           O  
ANISOU 3605  O   ALA B 193    13685   5499  11148    728    684   2527       O  
ATOM   3606  CB  ALA B 193      26.687 -54.134  95.433  1.00 65.56           C  
ANISOU 3606  CB  ALA B 193    11751   4253   8906    559    855   2640       C  
ATOM   3607  N   ALA B 194      27.376 -57.408  95.871  1.00 75.33           N  
ANISOU 3607  N   ALA B 194    13498   4743  10381    695    837   2922       N  
ATOM   3608  CA  ALA B 194      28.408 -58.435  95.871  1.00 78.29           C  
ANISOU 3608  CA  ALA B 194    14011   4872  10865    913    704   2972       C  
ATOM   3609  C   ALA B 194      28.127 -59.549  94.874  1.00 84.76           C  
ANISOU 3609  C   ALA B 194    14859   5386  11961    784    752   2883       C  
ATOM   3610  O   ALA B 194      28.965 -60.445  94.722  1.00 93.30           O  
ANISOU 3610  O   ALA B 194    16037   6237  13177    960    648   2895       O  
ATOM   3611  CB  ALA B 194      28.566 -59.016  97.278  1.00 82.69           C  
ANISOU 3611  CB  ALA B 194    14863   5310  11245   1040    717   3253       C  
ATOM   3612  N   ARG B 195      26.968 -59.527  94.217  1.00 80.75           N  
ANISOU 3612  N   ARG B 195    14270   4862  11549    488    899   2789       N  
ATOM   3613  CA  ARG B 195      26.616 -60.500  93.189  1.00 80.57           C  
ANISOU 3613  CA  ARG B 195    14263   4562  11788    341    936   2666       C  
ATOM   3614  C   ARG B 195      26.541 -59.911  91.787  1.00 76.82           C  
ANISOU 3614  C   ARG B 195    13550   4215  11424    259    887   2377       C  
ATOM   3615  O   ARG B 195      26.958 -60.567  90.830  1.00 78.21           O  
ANISOU 3615  O   ARG B 195    13725   4205  11785    295    824   2221       O  
ATOM   3616  CB  ARG B 195      25.280 -61.164  93.538  1.00 83.70           C  
ANISOU 3616  CB  ARG B 195    14786   4772  12243     46   1146   2787       C  
ATOM   3617  CG  ARG B 195      25.242 -61.721  94.955  1.00 87.82           C  
ANISOU 3617  CG  ARG B 195    15576   5166  12623    107   1236   3089       C  
ATOM   3618  CD  ARG B 195      23.905 -62.362  95.269  1.00 91.20           C  
ANISOU 3618  CD  ARG B 195    16118   5405  13130   -204   1480   3200       C  
ATOM   3619  NE  ARG B 195      23.738 -63.630  94.568  1.00 94.44           N  
ANISOU 3619  NE  ARG B 195    16623   5440  13819   -315   1500   3143       N  
ATOM   3620  CZ  ARG B 195      22.677 -64.419  94.693  1.00 98.18           C  
ANISOU 3620  CZ  ARG B 195    17201   5669  14432   -590   1700   3217       C  
ATOM   3621  NH1 ARG B 195      21.679 -64.072  95.495  1.00 99.19           N  
ANISOU 3621  NH1 ARG B 195    17342   5895  14449   -781   1915   3352       N  
ATOM   3622  NH2 ARG B 195      22.613 -65.556  94.016  1.00101.17           N  
ANISOU 3622  NH2 ARG B 195    17667   5697  15075   -677   1694   3142       N  
ATOM   3623  N   THR B 196      26.031 -58.690  91.629  1.00 73.09           N  
ANISOU 3623  N   THR B 196    12889   4046  10837    158    917   2299       N  
ATOM   3624  CA  THR B 196      25.945 -58.064  90.315  1.00 69.77           C  
ANISOU 3624  CA  THR B 196    12265   3752  10492     89    871   2041       C  
ATOM   3625  C   THR B 196      26.016 -56.551  90.465  1.00 67.63           C  
ANISOU 3625  C   THR B 196    11810   3850  10038    136    843   2006       C  
ATOM   3626  O   THR B 196      25.821 -55.999  91.551  1.00 74.23           O  
ANISOU 3626  O   THR B 196    12664   4837  10702    155    887   2164       O  
ATOM   3627  CB  THR B 196      24.654 -58.446  89.572  1.00 70.69           C  
ANISOU 3627  CB  THR B 196    12354   3741  10766   -225    975   1940       C  
ATOM   3628  OG1 THR B 196      23.517 -58.223  90.418  1.00 71.58           O  
ANISOU 3628  OG1 THR B 196    12470   3911  10815   -427   1126   2091       O  
ATOM   3629  CG2 THR B 196      24.682 -59.896  89.141  1.00 77.70           C  
ANISOU 3629  CG2 THR B 196    13402   4251  11867   -271    980   1907       C  
ATOM   3630  N   ARG B 197      26.330 -55.886  89.356  1.00 67.23           N  
ANISOU 3630  N   ARG B 197    11596   3930  10018    162    774   1791       N  
ATOM   3631  CA  ARG B 197      26.080 -54.461  89.192  1.00 58.79           C  
ANISOU 3631  CA  ARG B 197    10339   3175   8822    131    773   1723       C  
ATOM   3632  C   ARG B 197      24.794 -54.191  88.414  1.00 57.98           C  
ANISOU 3632  C   ARG B 197    10141   3094   8795   -142    850   1615       C  
ATOM   3633  O   ARG B 197      24.509 -53.036  88.088  1.00 55.00           O  
ANISOU 3633  O   ARG B 197     9607   2949   8341   -179    844   1540       O  
ATOM   3634  CB  ARG B 197      27.268 -53.789  88.504  1.00 57.26           C  
ANISOU 3634  CB  ARG B 197    10031   3121   8603    339    660   1568       C  
ATOM   3635  CG  ARG B 197      28.586 -54.007  89.226  1.00 65.51           C  
ANISOU 3635  CG  ARG B 197    11130   4145   9615    613    560   1648       C  
ATOM   3636  CD  ARG B 197      29.768 -53.664  88.343  1.00 69.73           C  
ANISOU 3636  CD  ARG B 197    11550   4737  10207    796    473   1461       C  
ATOM   3637  NE  ARG B 197      31.010 -53.592  89.105  1.00 75.19           N  
ANISOU 3637  NE  ARG B 197    12231   5460  10879   1058    361   1526       N  
ATOM   3638  CZ  ARG B 197      32.197 -53.341  88.566  1.00 75.92           C  
ANISOU 3638  CZ  ARG B 197    12207   5588  11050   1248    283   1381       C  
ATOM   3639  NH1 ARG B 197      32.300 -53.144  87.259  1.00 74.00           N  
ANISOU 3639  NH1 ARG B 197    11881   5359  10875   1204    327   1172       N  
ATOM   3640  NH2 ARG B 197      33.280 -53.288  89.330  1.00 80.19           N  
ANISOU 3640  NH2 ARG B 197    12716   6148  11605   1482    165   1441       N  
ATOM   3641  N   ALA B 198      24.010 -55.234  88.120  1.00 60.88           N  
ANISOU 3641  N   ALA B 198    10597   3209   9325   -333    912   1604       N  
ATOM   3642  CA  ALA B 198      22.815 -55.085  87.290  1.00 60.71           C  
ANISOU 3642  CA  ALA B 198    10476   3173   9418   -597    954   1471       C  
ATOM   3643  C   ALA B 198      21.775 -54.172  87.926  1.00 59.59           C  
ANISOU 3643  C   ALA B 198    10207   3232   9201   -752   1050   1558       C  
ATOM   3644  O   ALA B 198      20.964 -53.568  87.214  1.00 58.32           O  
ANISOU 3644  O   ALA B 198     9902   3160   9100   -914   1048   1431       O  
ATOM   3645  CB  ALA B 198      22.194 -56.450  86.997  1.00 64.67           C  
ANISOU 3645  CB  ALA B 198    11098   3342  10131   -781   1001   1444       C  
ATOM   3646  N   PHE B 199      21.771 -54.059  89.252  1.00 66.97           N  
ANISOU 3646  N   PHE B 199    11200   4236  10009   -701   1135   1765       N  
ATOM   3647  CA  PHE B 199      20.789 -53.247  89.957  1.00 69.12           C  
ANISOU 3647  CA  PHE B 199    11362   4690  10208   -838   1258   1848       C  
ATOM   3648  C   PHE B 199      21.463 -52.127  90.741  1.00 73.40           C  
ANISOU 3648  C   PHE B 199    11866   5505  10518   -631   1226   1925       C  
ATOM   3649  O   PHE B 199      20.972 -51.707  91.790  1.00 85.68           O  
ANISOU 3649  O   PHE B 199    13424   7172  11960   -667   1344   2057       O  
ATOM   3650  CB  PHE B 199      19.943 -54.110  90.895  1.00 63.66           C  
ANISOU 3650  CB  PHE B 199    10787   3827   9574  -1008   1439   2015       C  
ATOM   3651  CG  PHE B 199      19.502 -55.421  90.298  1.00 70.63           C  
ANISOU 3651  CG  PHE B 199    11754   4389  10693  -1183   1464   1960       C  
ATOM   3652  CD1 PHE B 199      18.310 -55.517  89.598  1.00 73.23           C  
ANISOU 3652  CD1 PHE B 199    11945   4654  11226  -1468   1517   1827       C  
ATOM   3653  CD2 PHE B 199      20.271 -56.563  90.455  1.00 69.96           C  
ANISOU 3653  CD2 PHE B 199    11885   4056  10642  -1064   1427   2032       C  
ATOM   3654  CE1 PHE B 199      17.899 -56.725  89.057  1.00 71.52           C  
ANISOU 3654  CE1 PHE B 199    11805   4131  11238  -1641   1530   1755       C  
ATOM   3655  CE2 PHE B 199      19.866 -57.774  89.917  1.00 72.94           C  
ANISOU 3655  CE2 PHE B 199    12348   4119  11246  -1226   1452   1973       C  
ATOM   3656  CZ  PHE B 199      18.678 -57.855  89.217  1.00 73.91           C  
ANISOU 3656  CZ  PHE B 199    12336   4181  11566  -1520   1503   1829       C  
ATOM   3657  N   SER B 200      22.598 -51.651  90.242  1.00 63.41           N  
ANISOU 3657  N   SER B 200    10568   4339   9187   -418   1077   1833       N  
ATOM   3658  CA  SER B 200      23.328 -50.550  90.846  1.00 60.64           C  
ANISOU 3658  CA  SER B 200    10159   4236   8645   -225   1021   1867       C  
ATOM   3659  C   SER B 200      23.048 -49.273  90.067  1.00 65.33           C  
ANISOU 3659  C   SER B 200    10549   5046   9227   -265    991   1724       C  
ATOM   3660  O   SER B 200      22.736 -49.309  88.875  1.00 66.70           O  
ANISOU 3660  O   SER B 200    10653   5167   9523   -363    959   1577       O  
ATOM   3661  CB  SER B 200      24.831 -50.838  90.864  1.00 59.63           C  
ANISOU 3661  CB  SER B 200    10110   4069   8479     40    883   1857       C  
ATOM   3662  OG  SER B 200      25.145 -51.801  91.854  1.00 70.31           O  
ANISOU 3662  OG  SER B 200    11659   5257   9798    118    898   2027       O  
ATOM   3663  N   VAL B 201      23.157 -48.142  90.754  1.00 70.97           N  
ANISOU 3663  N   VAL B 201    11185   5991   9789   -183    999   1766       N  
ATOM   3664  CA  VAL B 201      23.007 -46.834  90.129  1.00 73.42           C  
ANISOU 3664  CA  VAL B 201    11312   6508  10076   -188    968   1650       C  
ATOM   3665  C   VAL B 201      24.086 -45.903  90.661  1.00 73.89           C  
ANISOU 3665  C   VAL B 201    11341   6751   9983     35    890   1654       C  
ATOM   3666  O   VAL B 201      24.461 -45.976  91.835  1.00 80.28           O  
ANISOU 3666  O   VAL B 201    12246   7585  10672    139    897   1774       O  
ATOM   3667  CB  VAL B 201      21.602 -46.247  90.365  1.00 76.77           C  
ANISOU 3667  CB  VAL B 201    11622   7021  10527   -390   1097   1674       C  
ATOM   3668  CG1 VAL B 201      20.563 -47.067  89.615  1.00 81.36           C  
ANISOU 3668  CG1 VAL B 201    12187   7418  11307   -627   1149   1622       C  
ATOM   3669  CG2 VAL B 201      21.289 -46.210  91.852  1.00 79.73           C  
ANISOU 3669  CG2 VAL B 201    12068   7449  10776   -385   1219   1836       C  
ATOM   3670  N   CYS B 202      24.582 -45.030  89.790  1.00 72.87           N  
ANISOU 3670  N   CYS B 202    11087   6738   9860    105    816   1521       N  
ATOM   3671  CA  CYS B 202      25.533 -43.987  90.155  1.00 72.01           C  
ANISOU 3671  CA  CYS B 202    10910   6806   9646    288    751   1496       C  
ATOM   3672  C   CYS B 202      24.767 -42.685  90.356  1.00 73.63           C  
ANISOU 3672  C   CYS B 202    10981   7201   9792    220    812   1490       C  
ATOM   3673  O   CYS B 202      24.171 -42.161  89.408  1.00 68.47           O  
ANISOU 3673  O   CYS B 202    10220   6588   9208    119    828   1406       O  
ATOM   3674  CB  CYS B 202      26.596 -43.827  89.068  1.00 72.04           C  
ANISOU 3674  CB  CYS B 202    10859   6803   9710    405    665   1352       C  
ATOM   3675  SG  CYS B 202      27.917 -42.628  89.397  1.00 71.62           S  
ANISOU 3675  SG  CYS B 202    10699   6927   9587    622    588   1296       S  
ATOM   3676  N   ASP B 203      24.781 -42.171  91.585  1.00 72.19           N  
ANISOU 3676  N   ASP B 203    10820   7126   9483    284    845   1579       N  
ATOM   3677  CA  ASP B 203      24.064 -40.944  91.903  1.00 72.43           C  
ANISOU 3677  CA  ASP B 203    10730   7327   9462    236    921   1575       C  
ATOM   3678  C   ASP B 203      24.764 -40.216  93.043  1.00 62.20           C  
ANISOU 3678  C   ASP B 203     9470   6153   8011    404    894   1617       C  
ATOM   3679  O   ASP B 203      25.688 -40.738  93.674  1.00 64.51           O  
ANISOU 3679  O   ASP B 203     9888   6393   8230    547    812   1666       O  
ATOM   3680  CB  ASP B 203      22.603 -41.230  92.260  1.00 83.53           C  
ANISOU 3680  CB  ASP B 203    12132   8701  10904     35   1074   1651       C  
ATOM   3681  CG  ASP B 203      21.663 -40.180  91.715  1.00 93.79           C  
ANISOU 3681  CG  ASP B 203    13242  10115  12280    -70   1135   1586       C  
ATOM   3682  OD1 ASP B 203      22.105 -39.024  91.546  1.00 90.31           O  
ANISOU 3682  OD1 ASP B 203    12702   9811  11799     37   1086   1524       O  
ATOM   3683  OD2 ASP B 203      20.489 -40.510  91.450  1.00101.19           O  
ANISOU 3683  OD2 ASP B 203    14119  10992  13337   -259   1231   1596       O  
ATOM   3684  N   GLU B 204      24.299 -38.994  93.302  1.00 53.44           N  
ANISOU 3684  N   GLU B 204     8249   5196   6858    395    956   1596       N  
ATOM   3685  CA  GLU B 204      24.879 -38.132  94.323  1.00 50.04           C  
ANISOU 3685  CA  GLU B 204     7847   4885   6280    552    934   1616       C  
ATOM   3686  C   GLU B 204      24.397 -38.520  95.716  1.00 47.71           C  
ANISOU 3686  C   GLU B 204     7722   4587   5820    545   1032   1750       C  
ATOM   3687  O   GLU B 204      23.217 -38.820  95.922  1.00 53.95           O  
ANISOU 3687  O   GLU B 204     8516   5354   6630    380   1191   1809       O  
ATOM   3688  CB  GLU B 204      24.500 -36.678  94.041  1.00 47.77           C  
ANISOU 3688  CB  GLU B 204     7385   4743   6023    542    983   1543       C  
ATOM   3689  CG  GLU B 204      24.947 -36.186  92.680  1.00 51.59           C  
ANISOU 3689  CG  GLU B 204     7721   5235   6647    549    904   1420       C  
ATOM   3690  CD  GLU B 204      24.342 -34.850  92.307  1.00 58.72           C  
ANISOU 3690  CD  GLU B 204     8456   6252   7602    514    966   1371       C  
ATOM   3691  OE1 GLU B 204      23.735 -34.192  93.180  1.00 53.07           O  
ANISOU 3691  OE1 GLU B 204     7725   5621   6820    514   1065   1420       O  
ATOM   3692  OE2 GLU B 204      24.441 -34.479  91.121  1.00 56.97           O  
ANISOU 3692  OE2 GLU B 204     8131   6029   7485    488    923   1287       O  
ATOM   3693  N   ARG B 205      25.326 -38.514  96.671  1.00 50.35           N  
ANISOU 3693  N   ARG B 205     8199   4941   5990    730    937   1794       N  
ATOM   3694  CA  ARG B 205      25.045 -38.795  98.075  1.00 65.75           C  
ANISOU 3694  CA  ARG B 205    10356   6900   7724    765   1012   1921       C  
ATOM   3695  C   ARG B 205      25.102 -37.479  98.846  1.00 62.06           C  
ANISOU 3695  C   ARG B 205     9883   6605   7094    872   1031   1889       C  
ATOM   3696  O   ARG B 205      26.173 -36.875  98.970  1.00 68.66           O  
ANISOU 3696  O   ARG B 205    10711   7501   7873   1062    862   1824       O  
ATOM   3697  CB  ARG B 205      26.035 -39.813  98.641  1.00 83.51           C  
ANISOU 3697  CB  ARG B 205    12810   9040   9878    916    865   2000       C  
ATOM   3698  CG  ARG B 205      27.496 -39.378  98.609  1.00 95.53           C  
ANISOU 3698  CG  ARG B 205    14302  10608  11387   1151    629   1915       C  
ATOM   3699  CD  ARG B 205      28.167 -39.587  99.963  1.00105.94           C  
ANISOU 3699  CD  ARG B 205    15851  11943  12458   1351    507   1999       C  
ATOM   3700  NE  ARG B 205      29.615 -39.717  99.833  1.00110.88           N  
ANISOU 3700  NE  ARG B 205    16445  12546  13140   1568    248   1929       N  
ATOM   3701  CZ  ARG B 205      30.447 -38.693  99.671  1.00110.73           C  
ANISOU 3701  CZ  ARG B 205    16274  12639  13159   1710     98   1789       C  
ATOM   3702  NH1 ARG B 205      29.975 -37.456  99.621  1.00112.72           N  
ANISOU 3702  NH1 ARG B 205    16421  13027  13380   1667    183   1718       N  
ATOM   3703  NH2 ARG B 205      31.750 -38.907  99.553  1.00109.25           N  
ANISOU 3703  NH2 ARG B 205    16022  12421  13067   1898   -132   1712       N  
ATOM   3704  N   TRP B 206      23.956 -37.042  99.369  1.00 59.68           N  
ANISOU 3704  N   TRP B 206     9575   6374   6727    755   1239   1924       N  
ATOM   3705  CA  TRP B 206      23.848 -35.790 100.110  1.00 59.82           C  
ANISOU 3705  CA  TRP B 206     9592   6550   6585    842   1297   1888       C  
ATOM   3706  C   TRP B 206      23.433 -36.074 101.547  1.00 69.24           C  
ANISOU 3706  C   TRP B 206    11030   7768   7511    859   1420   1992       C  
ATOM   3707  O   TRP B 206      22.437 -36.765 101.785  1.00 78.52           O  
ANISOU 3707  O   TRP B 206    12246   8878   8711    691   1613   2075       O  
ATOM   3708  CB  TRP B 206      22.845 -34.838  99.448  1.00 51.10           C  
ANISOU 3708  CB  TRP B 206     8239   5526   5650    702   1455   1813       C  
ATOM   3709  CG  TRP B 206      23.279 -34.356  98.096  1.00 49.42           C  
ANISOU 3709  CG  TRP B 206     7811   5306   5661    707   1335   1711       C  
ATOM   3710  CD1 TRP B 206      22.849 -34.811  96.884  1.00 53.26           C  
ANISOU 3710  CD1 TRP B 206     8149   5713   6376    561   1331   1677       C  
ATOM   3711  CD2 TRP B 206      24.248 -33.336  97.820  1.00 51.28           C  
ANISOU 3711  CD2 TRP B 206     7973   5609   5903    872   1199   1627       C  
ATOM   3712  NE1 TRP B 206      23.482 -34.132  95.870  1.00 56.39           N  
ANISOU 3712  NE1 TRP B 206     8396   6129   6901    621   1213   1578       N  
ATOM   3713  CE2 TRP B 206      24.347 -33.222  96.419  1.00 50.31           C  
ANISOU 3713  CE2 TRP B 206     7656   5441   6020    804   1142   1549       C  
ATOM   3714  CE3 TRP B 206      25.039 -32.506  98.622  1.00 51.00           C  
ANISOU 3714  CE3 TRP B 206     8026   5665   5689   1075   1113   1602       C  
ATOM   3715  CZ2 TRP B 206      25.204 -32.310  95.802  1.00 41.87           C  
ANISOU 3715  CZ2 TRP B 206     6465   4400   5043    917   1033   1454       C  
ATOM   3716  CZ3 TRP B 206      25.890 -31.602  98.007  1.00 47.20           C  
ANISOU 3716  CZ3 TRP B 206     7349   5238   5345   1159    955   1438       C  
ATOM   3717  CH2 TRP B 206      25.966 -31.512  96.612  1.00 42.52           C  
ANISOU 3717  CH2 TRP B 206     6562   4584   5010   1077    936   1378       C  
ATOM   3718  N   ALA B 207      24.205 -35.545 102.501  1.00 63.64           N  
ANISOU 3718  N   ALA B 207    10488   7150   6541   1065   1303   1979       N  
ATOM   3719  CA  ALA B 207      23.902 -35.746 103.913  1.00 62.60           C  
ANISOU 3719  CA  ALA B 207    10625   7053   6107   1106   1402   2066       C  
ATOM   3720  C   ALA B 207      22.635 -35.026 104.357  1.00 74.38           C  
ANISOU 3720  C   ALA B 207    12057   8646   7557    969   1696   2045       C  
ATOM   3721  O   ALA B 207      22.048 -35.406 105.376  1.00 80.50           O  
ANISOU 3721  O   ALA B 207    13025   9417   8143    926   1865   2131       O  
ATOM   3722  CB  ALA B 207      25.081 -35.293 104.777  1.00 66.18           C  
ANISOU 3722  CB  ALA B 207    11269   7596   6280   1378   1154   2022       C  
ATOM   3723  N   ASP B 208      22.205 -33.995 103.635  1.00 74.76           N  
ANISOU 3723  N   ASP B 208    11840   8781   7785    907   1770   1932       N  
ATOM   3724  CA  ASP B 208      21.021 -33.248 104.034  1.00 72.83           C  
ANISOU 3724  CA  ASP B 208    11497   8638   7539    792   2044   1887       C  
ATOM   3725  C   ASP B 208      20.334 -32.690 102.797  1.00 73.57           C  
ANISOU 3725  C   ASP B 208    11236   8741   7975    651   2119   1803       C  
ATOM   3726  O   ASP B 208      20.911 -32.634 101.707  1.00 73.35           O  
ANISOU 3726  O   ASP B 208    11070   8669   8130    675   1950   1768       O  
ATOM   3727  CB  ASP B 208      21.374 -32.124 105.012  1.00 77.06           C  
ANISOU 3727  CB  ASP B 208    12155   9338   7788    964   2032   1795       C  
ATOM   3728  CG  ASP B 208      22.131 -30.996 104.347  1.00 83.88           C  
ANISOU 3728  CG  ASP B 208    12863  10291   8718   1098   1867   1663       C  
ATOM   3729  OD1 ASP B 208      23.276 -31.224 103.904  1.00 93.24           O  
ANISOU 3729  OD1 ASP B 208    14085  11429   9914   1232   1600   1669       O  
ATOM   3730  OD2 ASP B 208      21.577 -29.880 104.267  1.00 85.18           O  
ANISOU 3730  OD2 ASP B 208    12855  10568   8943   1073   2010   1547       O  
ATOM   3731  N   ASP B 209      19.077 -32.282 102.985  1.00 84.65           N  
ANISOU 3731  N   ASP B 209    12490  10202   9472    509   2372   1765       N  
ATOM   3732  CA  ASP B 209      18.265 -31.774 101.885  1.00 87.06           C  
ANISOU 3732  CA  ASP B 209    12448  10519  10111    378   2438   1682       C  
ATOM   3733  C   ASP B 209      18.706 -30.402 101.390  1.00 72.53           C  
ANISOU 3733  C   ASP B 209    10440   8787   8331    498   2355   1559       C  
ATOM   3734  O   ASP B 209      18.443 -30.068 100.231  1.00 68.23           O  
ANISOU 3734  O   ASP B 209     9639   8224   8060    435   2310   1511       O  
ATOM   3735  CB  ASP B 209      16.798 -31.713 102.310  1.00104.02           C  
ANISOU 3735  CB  ASP B 209    14463  12702  12359    212   2720   1661       C  
ATOM   3736  CG  ASP B 209      16.186 -33.084 102.464  1.00121.17           C  
ANISOU 3736  CG  ASP B 209    16721  14744  14576     47   2829   1778       C  
ATOM   3737  OD1 ASP B 209      16.757 -34.050 101.921  1.00126.85           O  
ANISOU 3737  OD1 ASP B 209    17531  15337  15331     34   2672   1854       O  
ATOM   3738  OD2 ASP B 209      15.132 -33.195 103.122  1.00128.20           O  
ANISOU 3738  OD2 ASP B 209    17581  15653  15477    -70   3080   1786       O  
ATOM   3739  N   LEU B 210      19.363 -29.600 102.230  1.00 63.31           N  
ANISOU 3739  N   LEU B 210     9419   7729   6908    673   2328   1502       N  
ATOM   3740  CA  LEU B 210      19.680 -28.232 101.829  1.00 55.35           C  
ANISOU 3740  CA  LEU B 210     8217   6824   5989    771   2253   1340       C  
ATOM   3741  C   LEU B 210      20.894 -28.166 100.908  1.00 53.34           C  
ANISOU 3741  C   LEU B 210     7894   6520   5855    855   1924   1282       C  
ATOM   3742  O   LEU B 210      20.893 -27.401  99.935  1.00 60.28           O  
ANISOU 3742  O   LEU B 210     8514   7403   6986    834   1836   1169       O  
ATOM   3743  CB  LEU B 210      19.908 -27.356 103.059  1.00 60.25           C  
ANISOU 3743  CB  LEU B 210     8977   7580   6335    910   2288   1216       C  
ATOM   3744  CG  LEU B 210      20.059 -25.849 102.811  1.00 63.05           C  
ANISOU 3744  CG  LEU B 210     9094   8024   6839    982   2192    978       C  
ATOM   3745  CD1 LEU B 210      18.888 -25.296 102.013  1.00 66.04           C  
ANISOU 3745  CD1 LEU B 210     9144   8397   7551    859   2354    933       C  
ATOM   3746  CD2 LEU B 210      20.215 -25.089 104.123  1.00 63.46           C  
ANISOU 3746  CD2 LEU B 210     9317   8199   6596   1109   2244    841       C  
ATOM   3747  N   ALA B 211      21.939 -28.941 101.199  1.00 53.86           N  
ANISOU 3747  N   ALA B 211     8190   6528   5745    957   1751   1358       N  
ATOM   3748  CA  ALA B 211      23.156 -28.894 100.391  1.00 49.95           C  
ANISOU 3748  CA  ALA B 211     7614   5987   5379   1044   1465   1286       C  
ATOM   3749  C   ALA B 211      22.904 -29.114  98.906  1.00 51.11           C  
ANISOU 3749  C   ALA B 211     7546   6037   5835    920   1451   1302       C  
ATOM   3750  O   ALA B 211      23.381 -28.303  98.097  1.00 52.93           O  
ANISOU 3750  O   ALA B 211     7585   6283   6244    946   1328   1171       O  
ATOM   3751  CB  ALA B 211      24.152 -29.934 100.923  1.00 49.47           C  
ANISOU 3751  CB  ALA B 211     7830   5856   5111   1173   1303   1393       C  
ATOM   3752  N   PRO B 212      22.199 -30.164  98.481  1.00 45.63           N  
ANISOU 3752  N   PRO B 212     6890   5235   5212    784   1568   1449       N  
ATOM   3753  CA  PRO B 212      21.923 -30.311  97.046  1.00 38.12           C  
ANISOU 3753  CA  PRO B 212     5746   4206   4533    672   1528   1434       C  
ATOM   3754  C   PRO B 212      21.157 -29.132  96.464  1.00 42.21           C  
ANISOU 3754  C   PRO B 212     5994   4808   5236    616   1576   1316       C  
ATOM   3755  O   PRO B 212      21.375 -28.774  95.299  1.00 47.26           O  
ANISOU 3755  O   PRO B 212     6491   5416   6049    606   1461   1254       O  
ATOM   3756  CB  PRO B 212      21.103 -31.610  96.973  1.00 50.12           C  
ANISOU 3756  CB  PRO B 212     7341   5615   6087    514   1646   1559       C  
ATOM   3757  CG  PRO B 212      20.562 -31.800  98.358  1.00 47.91           C  
ANISOU 3757  CG  PRO B 212     7210   5387   5608    503   1813   1614       C  
ATOM   3758  CD  PRO B 212      21.592 -31.237  99.282  1.00 49.05           C  
ANISOU 3758  CD  PRO B 212     7537   5607   5491    712   1736   1608       C  
ATOM   3759  N   LYS B 213      20.274 -28.511  97.247  1.00 40.90           N  
ANISOU 3759  N   LYS B 213     5772   4739   5030    594   1748   1286       N  
ATOM   3760  CA  LYS B 213      19.542 -27.354  96.747  1.00 42.55           C  
ANISOU 3760  CA  LYS B 213     5723   5015   5431    572   1782   1171       C  
ATOM   3761  C   LYS B 213      20.468 -26.164  96.528  1.00 45.77           C  
ANISOU 3761  C   LYS B 213     6067   5462   5860    704   1624   1029       C  
ATOM   3762  O   LYS B 213      20.369 -25.474  95.507  1.00 61.17           O  
ANISOU 3762  O   LYS B 213     7850   7391   8002    698   1549    970       O  
ATOM   3763  CB  LYS B 213      18.415 -26.986  97.715  1.00 46.37           C  
ANISOU 3763  CB  LYS B 213     6154   5585   5878    532   2030   1155       C  
ATOM   3764  CG  LYS B 213      17.310 -28.020  97.795  1.00 48.62           C  
ANISOU 3764  CG  LYS B 213     6427   5819   6230    362   2233   1276       C  
ATOM   3765  CD  LYS B 213      16.254 -27.620  98.811  1.00 59.54           C  
ANISOU 3765  CD  LYS B 213     7750   7289   7584    325   2494   1232       C  
ATOM   3766  CE  LYS B 213      15.067 -28.566  98.771  1.00 61.27           C  
ANISOU 3766  CE  LYS B 213     7884   7449   7948    130   2617   1277       C  
ATOM   3767  NZ  LYS B 213      14.207 -28.414  99.977  1.00 66.10           N  
ANISOU 3767  NZ  LYS B 213     8512   8130   8472     91   2856   1238       N  
ATOM   3768  N   ILE B 214      21.373 -25.908  97.477  1.00 38.98           N  
ANISOU 3768  N   ILE B 214     5351   4651   4807    824   1568    972       N  
ATOM   3769  CA  ILE B 214      22.325 -24.812  97.319  1.00 36.64           C  
ANISOU 3769  CA  ILE B 214     4984   4375   4564    930   1422    817       C  
ATOM   3770  C   ILE B 214      23.323 -25.115  96.208  1.00 33.09           C  
ANISOU 3770  C   ILE B 214     4507   3830   4234    938   1254    825       C  
ATOM   3771  O   ILE B 214      23.650 -24.241  95.396  1.00 45.55           O  
ANISOU 3771  O   ILE B 214     5951   5377   5981    949   1198    739       O  
ATOM   3772  CB  ILE B 214      23.039 -24.520  98.653  1.00 40.37           C  
ANISOU 3772  CB  ILE B 214     5609   4928   4802   1054   1374    725       C  
ATOM   3773  CG1 ILE B 214      22.047 -23.978  99.688  1.00 43.19           C  
ANISOU 3773  CG1 ILE B 214     5989   5383   5039   1054   1573    679       C  
ATOM   3774  CG2 ILE B 214      24.194 -23.550  98.431  1.00 41.51           C  
ANISOU 3774  CG2 ILE B 214     5663   5066   5043   1143   1198    550       C  
ATOM   3775  CD1 ILE B 214      22.625 -23.823 101.091  1.00 50.36           C  
ANISOU 3775  CD1 ILE B 214     7110   6380   5645   1177   1533    596       C  
ATOM   3776  N   TYR B 215      23.828 -26.349  96.150  1.00 36.32           N  
ANISOU 3776  N   TYR B 215     5059   4179   4564    936   1193    930       N  
ATOM   3777  CA  TYR B 215      24.833 -26.680  95.144  1.00 39.48           C  
ANISOU 3777  CA  TYR B 215     5437   4487   5077    956   1059    920       C  
ATOM   3778  C   TYR B 215      24.266 -26.587  93.735  1.00 35.58           C  
ANISOU 3778  C   TYR B 215     4823   3927   4766    854   1090    948       C  
ATOM   3779  O   TYR B 215      24.833 -25.913  92.867  1.00 39.44           O  
ANISOU 3779  O   TYR B 215     5223   4380   5382    873   1038    875       O  
ATOM   3780  CB  TYR B 215      25.390 -28.079  95.389  1.00 46.29           C  
ANISOU 3780  CB  TYR B 215     6481   5279   5829    989    995   1028       C  
ATOM   3781  CG  TYR B 215      26.307 -28.533  94.281  1.00 46.92           C  
ANISOU 3781  CG  TYR B 215     6530   5253   6043   1004    896   1013       C  
ATOM   3782  CD1 TYR B 215      27.584 -28.005  94.153  1.00 46.72           C  
ANISOU 3782  CD1 TYR B 215     6428   5229   6096   1106    777    883       C  
ATOM   3783  CD2 TYR B 215      25.888 -29.470  93.346  1.00 46.98           C  
ANISOU 3783  CD2 TYR B 215     6575   5158   6119    908    934   1108       C  
ATOM   3784  CE1 TYR B 215      28.425 -28.407  93.138  1.00 41.82           C  
ANISOU 3784  CE1 TYR B 215     5770   4511   5609   1119    731    859       C  
ATOM   3785  CE2 TYR B 215      26.721 -29.879  92.325  1.00 44.26           C  
ANISOU 3785  CE2 TYR B 215     6221   4716   5880    927    868   1079       C  
ATOM   3786  CZ  TYR B 215      27.989 -29.344  92.225  1.00 43.51           C  
ANISOU 3786  CZ  TYR B 215     6050   4626   5855   1035    783    959       C  
ATOM   3787  OH  TYR B 215      28.821 -29.752  91.208  1.00 52.98           O  
ANISOU 3787  OH  TYR B 215     7224   5743   7163   1039    753    909       O  
ATOM   3788  N   HIS B 216      23.143 -27.262  93.485  1.00 36.48           N  
ANISOU 3788  N   HIS B 216     4943   4021   4895    744   1176   1051       N  
ATOM   3789  CA  HIS B 216      22.602 -27.300  92.133  1.00 39.29           C  
ANISOU 3789  CA  HIS B 216     5209   4318   5400    658   1158   1068       C  
ATOM   3790  C   HIS B 216      22.031 -25.955  91.700  1.00 43.48           C  
ANISOU 3790  C   HIS B 216     5576   4896   6049    669   1170    996       C  
ATOM   3791  O   HIS B 216      21.889 -25.716  90.495  1.00 46.66           O  
ANISOU 3791  O   HIS B 216     5930   5248   6549    645   1111    995       O  
ATOM   3792  CB  HIS B 216      21.557 -28.413  92.025  1.00 41.96           C  
ANISOU 3792  CB  HIS B 216     5575   4615   5753    528   1223   1169       C  
ATOM   3793  CG  HIS B 216      22.154 -29.784  91.909  1.00 47.13           C  
ANISOU 3793  CG  HIS B 216     6400   5159   6347    510   1186   1245       C  
ATOM   3794  ND1 HIS B 216      22.739 -30.244  90.748  1.00 49.18           N  
ANISOU 3794  ND1 HIS B 216     6698   5322   6665    505   1091   1230       N  
ATOM   3795  CD2 HIS B 216      22.273 -30.788  92.811  1.00 52.11           C  
ANISOU 3795  CD2 HIS B 216     7196   5745   6860    507   1240   1338       C  
ATOM   3796  CE1 HIS B 216      23.183 -31.474  90.937  1.00 54.82           C  
ANISOU 3796  CE1 HIS B 216     7544   5970   7314    491   1053   1251       C  
ATOM   3797  NE2 HIS B 216      22.913 -31.828  92.181  1.00 51.73           N  
ANISOU 3797  NE2 HIS B 216     7237   5598   6820    495   1133   1327       N  
ATOM   3798  N   SER B 217      21.703 -25.070  92.643  1.00 45.46           N  
ANISOU 3798  N   SER B 217     5762   5231   6280    716   1242    935       N  
ATOM   3799  CA  SER B 217      21.366 -23.704  92.259  1.00 39.57           C  
ANISOU 3799  CA  SER B 217     4876   4499   5661    757   1243    856       C  
ATOM   3800  C   SER B 217      22.601 -22.965  91.760  1.00 42.21           C  
ANISOU 3800  C   SER B 217     5227   4773   6036    827   1166    783       C  
ATOM   3801  O   SER B 217      22.560 -22.291  90.724  1.00 50.13           O  
ANISOU 3801  O   SER B 217     6182   5714   7152    832   1136    780       O  
ATOM   3802  CB  SER B 217      20.724 -22.968  93.435  1.00 36.41           C  
ANISOU 3802  CB  SER B 217     4409   4190   5236    795   1358    787       C  
ATOM   3803  OG  SER B 217      19.440 -23.497  93.721  1.00 41.43           O  
ANISOU 3803  OG  SER B 217     4980   4870   5893    715   1471    846       O  
ATOM   3804  N   CYS B 218      23.717 -23.090  92.482  1.00 39.99           N  
ANISOU 3804  N   CYS B 218     5018   4505   5673    882   1134    723       N  
ATOM   3805  CA  CYS B 218      24.958 -22.471  92.031  1.00 39.85           C  
ANISOU 3805  CA  CYS B 218     4982   4422   5739    928   1078    635       C  
ATOM   3806  C   CYS B 218      25.436 -23.081  90.718  1.00 46.11           C  
ANISOU 3806  C   CYS B 218     5818   5118   6582    889   1049    701       C  
ATOM   3807  O   CYS B 218      25.924 -22.369  89.832  1.00 47.37           O  
ANISOU 3807  O   CYS B 218     5949   5205   6844    885   1061    667       O  
ATOM   3808  CB  CYS B 218      26.034 -22.619  93.103  1.00 36.22           C  
ANISOU 3808  CB  CYS B 218     4563   4004   5195   1001   1013    539       C  
ATOM   3809  SG  CYS B 218      25.652 -21.798  94.658  1.00 45.27           S  
ANISOU 3809  SG  CYS B 218     5700   5262   6237   1063   1040    422       S  
ATOM   3810  N   PHE B 219      25.312 -24.402  90.576  1.00 39.60           N  
ANISOU 3810  N   PHE B 219     5084   4285   5676    852   1024    792       N  
ATOM   3811  CA  PHE B 219      25.716 -25.053  89.333  1.00 37.94           C  
ANISOU 3811  CA  PHE B 219     4936   3981   5496    817   1004    836       C  
ATOM   3812  C   PHE B 219      24.960 -24.475  88.141  1.00 37.67           C  
ANISOU 3812  C   PHE B 219     4881   3915   5516    769   1015    869       C  
ATOM   3813  O   PHE B 219      25.555 -24.151  87.107  1.00 43.41           O  
ANISOU 3813  O   PHE B 219     5633   4613   6250    741   1007    827       O  
ATOM   3814  CB  PHE B 219      25.490 -26.562  89.438  1.00 41.48           C  
ANISOU 3814  CB  PHE B 219     5492   4410   5859    777    979    921       C  
ATOM   3815  CG  PHE B 219      26.156 -27.356  88.350  1.00 46.03           C  
ANISOU 3815  CG  PHE B 219     6136   4921   6432    741    940    902       C  
ATOM   3816  CD1 PHE B 219      27.409 -27.915  88.547  1.00 44.32           C  
ANISOU 3816  CD1 PHE B 219     5953   4675   6214    797    907    850       C  
ATOM   3817  CD2 PHE B 219      25.528 -27.542  87.132  1.00 43.91           C  
ANISOU 3817  CD2 PHE B 219     5894   4628   6160    660    923    917       C  
ATOM   3818  CE1 PHE B 219      28.022 -28.647  87.544  1.00 44.55           C  
ANISOU 3818  CE1 PHE B 219     6034   4648   6247    768    894    815       C  
ATOM   3819  CE2 PHE B 219      26.132 -28.270  86.128  1.00 43.30           C  
ANISOU 3819  CE2 PHE B 219     5899   4496   6055    634    900    880       C  
ATOM   3820  CZ  PHE B 219      27.382 -28.825  86.332  1.00 45.80           C  
ANISOU 3820  CZ  PHE B 219     6240   4781   6380    685    903    830       C  
ATOM   3821  N   PHE B 220      23.639 -24.334  88.273  1.00 40.54           N  
ANISOU 3821  N   PHE B 220     5190   4325   5887    737   1014    916       N  
ATOM   3822  CA  PHE B 220      22.831 -23.825  87.170  1.00 36.10           C  
ANISOU 3822  CA  PHE B 220     4607   3733   5376    722    975    952       C  
ATOM   3823  C   PHE B 220      23.224 -22.399  86.800  1.00 41.10           C  
ANISOU 3823  C   PHE B 220     5212   4336   6069    776    997    902       C  
ATOM   3824  O   PHE B 220      23.353 -22.066  85.617  1.00 48.35           O  
ANISOU 3824  O   PHE B 220     6199   5215   6958    758    960    909       O  
ATOM   3825  CB  PHE B 220      21.350 -23.902  87.543  1.00 35.45           C  
ANISOU 3825  CB  PHE B 220     4413   3723   5334    682    960    978       C  
ATOM   3826  CG  PHE B 220      20.444 -23.202  86.576  1.00 36.90           C  
ANISOU 3826  CG  PHE B 220     4538   3890   5593    703    880    998       C  
ATOM   3827  CD1 PHE B 220      20.301 -23.662  85.277  1.00 45.31           C  
ANISOU 3827  CD1 PHE B 220     5698   4900   6619    677    772   1039       C  
ATOM   3828  CD2 PHE B 220      19.731 -22.083  86.969  1.00 36.87           C  
ANISOU 3828  CD2 PHE B 220     4397   3920   5690    767    900    969       C  
ATOM   3829  CE1 PHE B 220      19.462 -23.017  84.388  1.00 51.77           C  
ANISOU 3829  CE1 PHE B 220     6486   5705   7481    721    657   1061       C  
ATOM   3830  CE2 PHE B 220      18.892 -21.434  86.086  1.00 44.51           C  
ANISOU 3830  CE2 PHE B 220     5313   4863   6735    817    796    993       C  
ATOM   3831  CZ  PHE B 220      18.757 -21.901  84.793  1.00 50.70           C  
ANISOU 3831  CZ  PHE B 220     6202   5600   7462    798    660   1045       C  
ATOM   3832  N   ILE B 221      23.420 -21.540  87.803  1.00 47.37           N  
ANISOU 3832  N   ILE B 221     5922   5159   6918    823   1051    832       N  
ATOM   3833  CA  ILE B 221      23.737 -20.139  87.537  1.00 46.22           C  
ANISOU 3833  CA  ILE B 221     5749   4984   6828    830   1065    765       C  
ATOM   3834  C   ILE B 221      25.169 -19.985  87.040  1.00 38.49           C  
ANISOU 3834  C   ILE B 221     4829   3955   5841    788   1092    710       C  
ATOM   3835  O   ILE B 221      25.440 -19.208  86.117  1.00 43.46           O  
ANISOU 3835  O   ILE B 221     5501   4519   6493    770   1121    718       O  
ATOM   3836  CB  ILE B 221      23.477 -19.286  88.795  1.00 44.42           C  
ANISOU 3836  CB  ILE B 221     5419   4802   6656    873   1102    675       C  
ATOM   3837  CG1 ILE B 221      21.985 -18.987  88.934  1.00 40.86           C  
ANISOU 3837  CG1 ILE B 221     4877   4384   6264    916   1105    714       C  
ATOM   3838  CG2 ILE B 221      24.284 -17.995  88.747  1.00 40.43           C  
ANISOU 3838  CG2 ILE B 221     4907   4240   6216    857   1116    576       C  
ATOM   3839  CD1 ILE B 221      21.505 -18.903  90.365  1.00 42.16           C  
ANISOU 3839  CD1 ILE B 221     4953   4641   6427    952   1180    641       C  
ATOM   3840  N   VAL B 222      26.110 -20.712  87.642  1.00 39.50           N  
ANISOU 3840  N   VAL B 222     4955   4103   5949    785   1093    659       N  
ATOM   3841  CA  VAL B 222      27.515 -20.516  87.301  1.00 44.32           C  
ANISOU 3841  CA  VAL B 222     5566   4663   6611    754   1128    584       C  
ATOM   3842  C   VAL B 222      27.829 -21.080  85.920  1.00 45.15           C  
ANISOU 3842  C   VAL B 222     5771   4717   6666    716   1169    645       C  
ATOM   3843  O   VAL B 222      28.519 -20.439  85.119  1.00 50.00           O  
ANISOU 3843  O   VAL B 222     6407   5261   7330    686   1259    629       O  
ATOM   3844  CB  VAL B 222      28.412 -21.136  88.385  1.00 48.42           C  
ANISOU 3844  CB  VAL B 222     6036   5221   7139    793   1079    494       C  
ATOM   3845  CG1 VAL B 222      29.835 -21.268  87.877  1.00 47.24           C  
ANISOU 3845  CG1 VAL B 222     5862   5018   7069    764   1106    422       C  
ATOM   3846  CG2 VAL B 222      28.360 -20.296  89.645  1.00 38.57           C  
ANISOU 3846  CG2 VAL B 222     4704   4019   5933    840   1050    387       C  
ATOM   3847  N   THR B 223      27.325 -22.277  85.612  1.00 43.15           N  
ANISOU 3847  N   THR B 223     5592   4489   6314    716   1118    710       N  
ATOM   3848  CA  THR B 223      27.609 -22.919  84.336  1.00 47.18           C  
ANISOU 3848  CA  THR B 223     6219   4957   6752    688   1141    738       C  
ATOM   3849  C   THR B 223      26.610 -22.576  83.233  1.00 42.25           C  
ANISOU 3849  C   THR B 223     5692   4313   6047    682   1101    809       C  
ATOM   3850  O   THR B 223      26.896 -22.848  82.062  1.00 51.62           O  
ANISOU 3850  O   THR B 223     7009   5450   7153    670   1130    823       O  
ATOM   3851  CB  THR B 223      27.673 -24.443  84.511  1.00 50.53           C  
ANISOU 3851  CB  THR B 223     6690   5394   7115    685   1086    747       C  
ATOM   3852  OG1 THR B 223      26.399 -24.940  84.946  1.00 55.14           O  
ANISOU 3852  OG1 THR B 223     7277   6019   7654    675   1000    812       O  
ATOM   3853  CG2 THR B 223      28.734 -24.816  85.541  1.00 55.02           C  
ANISOU 3853  CG2 THR B 223     7184   5969   7753    722   1088    681       C  
ATOM   3854  N   TYR B 224      25.457 -21.986  83.556  1.00 45.09           N  
ANISOU 3854  N   TYR B 224     6003   4701   6429    705   1033    853       N  
ATOM   3855  CA  TYR B 224      24.482 -21.709  82.505  1.00 42.28           C  
ANISOU 3855  CA  TYR B 224     5740   4316   6010    722    950    926       C  
ATOM   3856  C   TYR B 224      23.976 -20.272  82.504  1.00 46.50           C  
ANISOU 3856  C   TYR B 224     6234   4826   6610    772    948    947       C  
ATOM   3857  O   TYR B 224      24.339 -19.479  81.629  1.00 50.13           O  
ANISOU 3857  O   TYR B 224     6795   5217   7033    783    989    966       O  
ATOM   3858  CB  TYR B 224      23.292 -22.661  82.612  1.00 35.85           C  
ANISOU 3858  CB  TYR B 224     4912   3527   5181    717    831    986       C  
ATOM   3859  CG  TYR B 224      22.350 -22.571  81.431  1.00 50.11           C  
ANISOU 3859  CG  TYR B 224     6828   5285   6927    750    705   1067       C  
ATOM   3860  CD1 TYR B 224      22.560 -23.334  80.288  1.00 46.63           C  
ANISOU 3860  CD1 TYR B 224     6575   4792   6349    728    661   1085       C  
ATOM   3861  CD2 TYR B 224      21.258 -21.713  81.454  1.00 46.75           C  
ANISOU 3861  CD2 TYR B 224     6323   4857   6582    827    620   1122       C  
ATOM   3862  CE1 TYR B 224      21.703 -23.253  79.204  1.00 41.06           C  
ANISOU 3862  CE1 TYR B 224     6006   4036   5559    784    516   1167       C  
ATOM   3863  CE2 TYR B 224      20.397 -21.624  80.376  1.00 47.34           C  
ANISOU 3863  CE2 TYR B 224     6498   4886   6605    894    461   1205       C  
ATOM   3864  CZ  TYR B 224      20.623 -22.394  79.255  1.00 49.06           C  
ANISOU 3864  CZ  TYR B 224     6931   5056   6655    874    399   1231       C  
ATOM   3865  OH  TYR B 224      19.761 -22.300  78.188  1.00 52.91           O  
ANISOU 3865  OH  TYR B 224     7523   5538   7042    930    186   1268       O  
ATOM   3866  N   LEU B 225      23.123 -19.934  83.472  1.00 52.77           N  
ANISOU 3866  N   LEU B 225     6887   5661   7502    808    915    948       N  
ATOM   3867  CA  LEU B 225      22.341 -18.709  83.360  1.00 53.95           C  
ANISOU 3867  CA  LEU B 225     7000   5779   7721    875    877    973       C  
ATOM   3868  C   LEU B 225      23.234 -17.481  83.254  1.00 49.82           C  
ANISOU 3868  C   LEU B 225     6509   5186   7234    869    981    930       C  
ATOM   3869  O   LEU B 225      23.115 -16.694  82.308  1.00 50.58           O  
ANISOU 3869  O   LEU B 225     6717   5202   7299    903    963    983       O  
ATOM   3870  CB  LEU B 225      21.400 -18.584  84.558  1.00 53.29           C  
ANISOU 3870  CB  LEU B 225     6732   5755   7760    917    869    951       C  
ATOM   3871  CG  LEU B 225      20.321 -17.508  84.443  1.00 56.01           C  
ANISOU 3871  CG  LEU B 225     7004   6076   8204   1008    802    969       C  
ATOM   3872  CD1 LEU B 225      19.280 -17.899  83.407  1.00 50.59           C  
ANISOU 3872  CD1 LEU B 225     6348   5371   7502   1068    635   1066       C  
ATOM   3873  CD2 LEU B 225      19.672 -17.280  85.793  1.00 50.22           C  
ANISOU 3873  CD2 LEU B 225     6076   5413   7594   1036    858    899       C  
ATOM   3874  N   ALA B 226      24.139 -17.298  84.215  1.00 44.35           N  
ANISOU 3874  N   ALA B 226     5730   4507   6614    829   1084    839       N  
ATOM   3875  CA  ALA B 226      24.943 -16.077  84.230  1.00 44.64           C  
ANISOU 3875  CA  ALA B 226     5766   4458   6738    812   1188    789       C  
ATOM   3876  C   ALA B 226      25.804 -15.902  82.988  1.00 45.88           C  
ANISOU 3876  C   ALA B 226     6063   4526   6842    780   1282    831       C  
ATOM   3877  O   ALA B 226      25.712 -14.844  82.340  1.00 51.14           O  
ANISOU 3877  O   ALA B 226     6811   5097   7524    804   1320    875       O  
ATOM   3878  CB  ALA B 226      25.810 -16.062  85.492  1.00 44.52           C  
ANISOU 3878  CB  ALA B 226     5631   4470   6816    772   1241    666       C  
ATOM   3879  N   PRO B 227      26.647 -16.863  82.600  1.00 45.46           N  
ANISOU 3879  N   PRO B 227     6055   4489   6727    736   1337    819       N  
ATOM   3880  CA  PRO B 227      27.488 -16.653  81.406  1.00 48.25           C  
ANISOU 3880  CA  PRO B 227     6547   4752   7033    712   1473    848       C  
ATOM   3881  C   PRO B 227      26.704 -16.438  80.123  1.00 53.78           C  
ANISOU 3881  C   PRO B 227     7448   5409   7575    760   1401    959       C  
ATOM   3882  O   PRO B 227      27.055 -15.555  79.330  1.00 63.34           O  
ANISOU 3882  O   PRO B 227     8781   6516   8771    764   1508   1002       O  
ATOM   3883  CB  PRO B 227      28.337 -17.931  81.347  1.00 44.18           C  
ANISOU 3883  CB  PRO B 227     6027   4274   6485    675   1522    804       C  
ATOM   3884  CG  PRO B 227      27.626 -18.928  82.221  1.00 36.30           C  
ANISOU 3884  CG  PRO B 227     4949   3385   5457    690   1363    793       C  
ATOM   3885  CD  PRO B 227      26.932 -18.138  83.276  1.00 41.23           C  
ANISOU 3885  CD  PRO B 227     5453   4040   6175    714   1299    774       C  
ATOM   3886  N   LEU B 228      25.636 -17.212  79.898  1.00 50.15           N  
ANISOU 3886  N   LEU B 228     7035   5014   7006    796   1217   1010       N  
ATOM   3887  CA  LEU B 228      24.871 -17.043  78.666  1.00 47.79           C  
ANISOU 3887  CA  LEU B 228     6935   4665   6557    850   1105   1117       C  
ATOM   3888  C   LEU B 228      24.103 -15.731  78.657  1.00 46.65           C  
ANISOU 3888  C   LEU B 228     6794   4456   6474    923   1036   1176       C  
ATOM   3889  O   LEU B 228      23.955 -15.110  77.597  1.00 55.94           O  
ANISOU 3889  O   LEU B 228     8162   5542   7550    967   1017   1266       O  
ATOM   3890  CB  LEU B 228      23.923 -18.223  78.448  1.00 47.37           C  
ANISOU 3890  CB  LEU B 228     6912   4679   6408    869    914   1152       C  
ATOM   3891  CG  LEU B 228      24.583 -19.568  78.130  1.00 47.65           C  
ANISOU 3891  CG  LEU B 228     7014   4742   6347    809    963   1112       C  
ATOM   3892  CD1 LEU B 228      23.609 -20.725  78.327  1.00 57.04           C  
ANISOU 3892  CD1 LEU B 228     8174   5988   7512    812    786   1130       C  
ATOM   3893  CD2 LEU B 228      25.149 -19.564  76.717  1.00 52.02           C  
ANISOU 3893  CD2 LEU B 228     7823   5221   6723    813   1046   1152       C  
ATOM   3894  N   GLY B 229      23.609 -15.291  79.816  1.00 37.94           N  
ANISOU 3894  N   GLY B 229     5496   3388   5530    945   1002   1126       N  
ATOM   3895  CA  GLY B 229      22.952 -13.996  79.868  1.00 34.45           C  
ANISOU 3895  CA  GLY B 229     5049   2868   5173   1023    954   1162       C  
ATOM   3896  C   GLY B 229      23.914 -12.855  79.602  1.00 41.42           C  
ANISOU 3896  C   GLY B 229     6008   3625   6105    992   1137   1161       C  
ATOM   3897  O   GLY B 229      23.569 -11.882  78.926  1.00 55.45           O  
ANISOU 3897  O   GLY B 229     7917   5287   7864   1055   1107   1244       O  
ATOM   3898  N   LEU B 230      25.135 -12.956  80.134  1.00 45.38           N  
ANISOU 3898  N   LEU B 230     6424   4132   6686    898   1326   1069       N  
ATOM   3899  CA  LEU B 230      26.150 -11.957  79.820  1.00 48.39           C  
ANISOU 3899  CA  LEU B 230     6862   4380   7143    853   1532   1063       C  
ATOM   3900  C   LEU B 230      26.573 -12.045  78.359  1.00 50.84           C  
ANISOU 3900  C   LEU B 230     7417   4614   7284    851   1616   1159       C  
ATOM   3901  O   LEU B 230      26.802 -11.016  77.712  1.00 62.81           O  
ANISOU 3901  O   LEU B 230     9071   5990   8803    862   1722   1224       O  
ATOM   3902  CB  LEU B 230      27.356 -12.121  80.743  1.00 52.28           C  
ANISOU 3902  CB  LEU B 230     7176   4891   7797    757   1696    929       C  
ATOM   3903  CG  LEU B 230      27.131 -11.771  82.214  1.00 49.91           C  
ANISOU 3903  CG  LEU B 230     6667   4632   7664    750   1641    820       C  
ATOM   3904  CD1 LEU B 230      28.230 -12.367  83.080  1.00 43.94           C  
ANISOU 3904  CD1 LEU B 230     5754   3925   7018    663   1716    693       C  
ATOM   3905  CD2 LEU B 230      27.053 -10.263  82.396  1.00 46.29           C  
ANISOU 3905  CD2 LEU B 230     6204   4035   7348    762   1700    806       C  
ATOM   3906  N   MET B 231      26.681 -13.263  77.821  1.00 51.68           N  
ANISOU 3906  N   MET B 231     7598   4801   7237    838   1581   1168       N  
ATOM   3907  CA  MET B 231      27.055 -13.412  76.418  1.00 54.09           C  
ANISOU 3907  CA  MET B 231     8160   5038   7354    842   1668   1248       C  
ATOM   3908  C   MET B 231      26.000 -12.814  75.495  1.00 56.80           C  
ANISOU 3908  C   MET B 231     8717   5316   7549    937   1500   1392       C  
ATOM   3909  O   MET B 231      26.333 -12.143  74.511  1.00 58.21           O  
ANISOU 3909  O   MET B 231     9116   5374   7629    953   1617   1478       O  
ATOM   3910  CB  MET B 231      27.285 -14.886  76.082  1.00 51.96           C  
ANISOU 3910  CB  MET B 231     7930   4862   6952    818   1646   1213       C  
ATOM   3911  CG  MET B 231      28.631 -15.435  76.532  1.00 54.54           C  
ANISOU 3911  CG  MET B 231     8126   5199   7398    741   1867   1093       C  
ATOM   3912  SD  MET B 231      28.980 -17.083  75.883  1.00 56.65           S  
ANISOU 3912  SD  MET B 231     8502   5524   7498    729   1876   1063       S  
ATOM   3913  CE  MET B 231      28.509 -18.093  77.282  1.00 53.03           C  
ANISOU 3913  CE  MET B 231     7792   5211   7147    714   1684    990       C  
ATOM   3914  N   ALA B 232      24.719 -13.053  75.791  1.00 56.32           N  
ANISOU 3914  N   ALA B 232     8596   5325   7479   1010   1227   1424       N  
ATOM   3915  CA  ALA B 232      23.657 -12.471  74.976  1.00 54.48           C  
ANISOU 3915  CA  ALA B 232     8534   5024   7141   1124   1027   1560       C  
ATOM   3916  C   ALA B 232      23.743 -10.951  74.962  1.00 62.13           C  
ANISOU 3916  C   ALA B 232     9552   5841   8214   1161   1112   1614       C  
ATOM   3917  O   ALA B 232      23.612 -10.323  73.904  1.00 73.89           O  
ANISOU 3917  O   ALA B 232    11286   7217   9571   1222   1101   1744       O  
ATOM   3918  CB  ALA B 232      22.290 -12.922  75.493  1.00 43.60           C  
ANISOU 3918  CB  ALA B 232     7011   3737   5819   1204    737   1559       C  
ATOM   3919  N   MET B 233      23.960 -10.341  76.129  1.00 57.75           N  
ANISOU 3919  N   MET B 233     8780   5273   7888   1128   1199   1518       N  
ATOM   3920  CA  MET B 233      24.079  -8.889  76.187  1.00 57.09           C  
ANISOU 3920  CA  MET B 233     8738   5026   7928   1155   1292   1554       C  
ATOM   3921  C   MET B 233      25.340  -8.398  75.489  1.00 58.71           C  
ANISOU 3921  C   MET B 233     9105   5105   8096   1075   1585   1584       C  
ATOM   3922  O   MET B 233      25.349  -7.295  74.931  1.00 63.03           O  
ANISOU 3922  O   MET B 233     9818   5483   8646   1113   1649   1684       O  
ATOM   3923  CB  MET B 233      24.056  -8.415  77.641  1.00 57.43           C  
ANISOU 3923  CB  MET B 233     8513   5088   8220   1134   1326   1420       C  
ATOM   3924  CG  MET B 233      22.728  -8.637  78.348  1.00 63.63           C  
ANISOU 3924  CG  MET B 233     9143   5965   9068   1235   1077   1389       C  
ATOM   3925  SD  MET B 233      22.694  -7.953  80.017  1.00 70.66           S  
ANISOU 3925  SD  MET B 233     9759   6869  10221   1221   1147   1226       S  
ATOM   3926  CE  MET B 233      23.616  -9.192  80.919  1.00 71.22           C  
ANISOU 3926  CE  MET B 233     9649   7111  10301   1082   1264   1092       C  
ATOM   3927  N   ALA B 234      26.411  -9.194  75.504  1.00 58.63           N  
ANISOU 3927  N   ALA B 234     9048   5161   8069    971   1775   1499       N  
ATOM   3928  CA  ALA B 234      27.626  -8.789  74.807  1.00 53.54           C  
ANISOU 3928  CA  ALA B 234     8539   4390   7412    900   2083   1512       C  
ATOM   3929  C   ALA B 234      27.422  -8.806  73.298  1.00 57.54           C  
ANISOU 3929  C   ALA B 234     9393   4826   7643    960   2077   1667       C  
ATOM   3930  O   ALA B 234      27.742  -7.833  72.607  1.00 70.01           O  
ANISOU 3930  O   ALA B 234    11169   6235   9196    969   2235   1762       O  
ATOM   3931  CB  ALA B 234      28.789  -9.696  75.208  1.00 51.64           C  
ANISOU 3931  CB  ALA B 234     8140   4230   7250    796   2275   1368       C  
ATOM   3932  N   TYR B 235      26.885  -9.906  72.767  1.00 54.00           N  
ANISOU 3932  N   TYR B 235     9039   4499   6981   1003   1899   1695       N  
ATOM   3933  CA  TYR B 235      26.672  -9.994  71.326  1.00 54.39           C  
ANISOU 3933  CA  TYR B 235     9436   4492   6737   1069   1877   1832       C  
ATOM   3934  C   TYR B 235      25.605  -9.019  70.844  1.00 60.00           C  
ANISOU 3934  C   TYR B 235    10314   5106   7379   1195   1667   1996       C  
ATOM   3935  O   TYR B 235      25.651  -8.581  69.689  1.00 66.03           O  
ANISOU 3935  O   TYR B 235    11395   5758   7937   1250   1725   2130       O  
ATOM   3936  CB  TYR B 235      26.326 -11.427  70.933  1.00 54.42           C  
ANISOU 3936  CB  TYR B 235     9491   4644   6541   1085   1720   1804       C  
ATOM   3937  CG  TYR B 235      27.540 -12.319  70.937  1.00 57.20           C  
ANISOU 3937  CG  TYR B 235     9801   5033   6899    984   1978   1677       C  
ATOM   3938  CD1 TYR B 235      28.585 -12.100  70.049  1.00 60.05           C  
ANISOU 3938  CD1 TYR B 235    10374   5273   7169    951   2291   1689       C  
ATOM   3939  CD2 TYR B 235      27.660 -13.357  71.847  1.00 57.53           C  
ANISOU 3939  CD2 TYR B 235     9589   5212   7057    931   1922   1547       C  
ATOM   3940  CE1 TYR B 235      29.705 -12.901  70.055  1.00 64.96           C  
ANISOU 3940  CE1 TYR B 235    10939   5906   7835    875   2534   1563       C  
ATOM   3941  CE2 TYR B 235      28.777 -14.164  71.860  1.00 59.49           C  
ANISOU 3941  CE2 TYR B 235     9792   5476   7336    859   2147   1433       C  
ATOM   3942  CZ  TYR B 235      29.797 -13.932  70.962  1.00 69.30           C  
ANISOU 3942  CZ  TYR B 235    11229   6592   8508    834   2452   1436       C  
ATOM   3943  OH  TYR B 235      30.915 -14.732  70.968  1.00 78.42           O  
ANISOU 3943  OH  TYR B 235    12325   7742   9730    775   2684   1313       O  
ATOM   3944  N   PHE B 236      24.633  -8.679  71.694  1.00 59.02           N  
ANISOU 3944  N   PHE B 236     9990   5014   7422   1255   1426   1988       N  
ATOM   3945  CA  PHE B 236      23.666  -7.657  71.310  1.00 63.67           C  
ANISOU 3945  CA  PHE B 236    10706   5484   8001   1391   1232   2135       C  
ATOM   3946  C   PHE B 236      24.345  -6.306  71.132  1.00 65.79           C  
ANISOU 3946  C   PHE B 236    11100   5539   8358   1369   1481   2200       C  
ATOM   3947  O   PHE B 236      24.027  -5.560  70.198  1.00 76.86           O  
ANISOU 3947  O   PHE B 236    12776   6800   9626   1464   1444   2368       O  
ATOM   3948  CB  PHE B 236      22.549  -7.557  72.350  1.00 65.95           C  
ANISOU 3948  CB  PHE B 236    10724   5834   8499   1465    959   2082       C  
ATOM   3949  CG  PHE B 236      21.636  -6.374  72.147  1.00 72.06           C  
ANISOU 3949  CG  PHE B 236    11573   6460   9346   1613    781   2207       C  
ATOM   3950  CD1 PHE B 236      20.650  -6.405  71.176  1.00 75.87           C  
ANISOU 3950  CD1 PHE B 236    12234   6935   9657   1767    507   2358       C  
ATOM   3951  CD2 PHE B 236      21.764  -5.232  72.926  1.00 82.52           C  
ANISOU 3951  CD2 PHE B 236    12788   7650  10915   1611    879   2166       C  
ATOM   3952  CE1 PHE B 236      19.807  -5.324  70.983  1.00 84.58           C  
ANISOU 3952  CE1 PHE B 236    13392   7896  10849   1923    328   2478       C  
ATOM   3953  CE2 PHE B 236      20.922  -4.145  72.737  1.00 85.30           C  
ANISOU 3953  CE2 PHE B 236    13213   7846  11352   1761    711   2277       C  
ATOM   3954  CZ  PHE B 236      19.943  -4.194  71.764  1.00 86.07           C  
ANISOU 3954  CZ  PHE B 236    13475   7934  11295   1920    432   2438       C  
ATOM   3955  N   GLN B 237      25.277  -5.967  72.027  1.00 64.15           N  
ANISOU 3955  N   GLN B 237    10695   5298   8381   1247   1734   2069       N  
ATOM   3956  CA  GLN B 237      26.047  -4.743  71.845  1.00 64.32           C  
ANISOU 3956  CA  GLN B 237    10825   5104   8508   1202   2010   2115       C  
ATOM   3957  C   GLN B 237      26.976  -4.852  70.644  1.00 68.46           C  
ANISOU 3957  C   GLN B 237    11638   5548   8828   1154   2286   2190       C  
ATOM   3958  O   GLN B 237      27.181  -3.871  69.919  1.00 76.12           O  
ANISOU 3958  O   GLN B 237    12857   6317   9748   1179   2431   2324       O  
ATOM   3959  CB  GLN B 237      26.844  -4.423  73.110  1.00 60.75           C  
ANISOU 3959  CB  GLN B 237    10070   4645   8368   1080   2206   1935       C  
ATOM   3960  CG  GLN B 237      26.005  -3.901  74.264  1.00 56.48           C  
ANISOU 3960  CG  GLN B 237     9304   4114   8043   1137   2004   1868       C  
ATOM   3961  CD  GLN B 237      26.822  -3.098  75.259  1.00 62.98           C  
ANISOU 3961  CD  GLN B 237     9928   4840   9162   1032   2230   1731       C  
ATOM   3962  OE1 GLN B 237      27.971  -3.432  75.550  1.00 67.99           O  
ANISOU 3962  OE1 GLN B 237    10438   5506   9889    899   2472   1613       O  
ATOM   3963  NE2 GLN B 237      26.234  -2.027  75.783  1.00 67.68           N  
ANISOU 3963  NE2 GLN B 237    10486   5308   9923   1097   2146   1735       N  
ATOM   3964  N   ILE B 238      27.547  -6.037  70.414  1.00 69.25           N  
ANISOU 3964  N   ILE B 238    11720   5784   8807   1090   2373   2103       N  
ATOM   3965  CA  ILE B 238      28.395  -6.222  69.242  1.00 70.68           C  
ANISOU 3965  CA  ILE B 238    12187   5886   8783   1058   2644   2156       C  
ATOM   3966  C   ILE B 238      27.574  -6.091  67.968  1.00 71.50           C  
ANISOU 3966  C   ILE B 238    12675   5940   8552   1195   2470   2355       C  
ATOM   3967  O   ILE B 238      28.042  -5.546  66.962  1.00 74.57           O  
ANISOU 3967  O   ILE B 238    13382   6168   8784   1207   2689   2470       O  
ATOM   3968  CB  ILE B 238      29.115  -7.579  69.309  1.00 60.98           C  
ANISOU 3968  CB  ILE B 238    10849   4807   7513    980   2751   2005       C  
ATOM   3969  CG1 ILE B 238      30.252  -7.528  70.331  1.00 57.50           C  
ANISOU 3969  CG1 ILE B 238    10088   4358   7401    847   3010   1823       C  
ATOM   3970  CG2 ILE B 238      29.642  -7.969  67.935  1.00 58.69           C  
ANISOU 3970  CG2 ILE B 238    10910   4454   6935    991   2945   2068       C  
ATOM   3971  CD1 ILE B 238      30.656  -8.887  70.850  1.00 57.39           C  
ANISOU 3971  CD1 ILE B 238     9859   4521   7426    796   2993   1662       C  
ATOM   3972  N   PHE B 239      26.343  -6.606  67.987  1.00 73.77           N  
ANISOU 3972  N   PHE B 239    12941   6360   8727   1306   2078   2396       N  
ATOM   3973  CA  PHE B 239      25.464  -6.479  66.830  1.00 76.18           C  
ANISOU 3973  CA  PHE B 239    13587   6631   8728   1459   1857   2578       C  
ATOM   3974  C   PHE B 239      25.142  -5.019  66.534  1.00 82.97           C  
ANISOU 3974  C   PHE B 239    14620   7276   9628   1546   1857   2751       C  
ATOM   3975  O   PHE B 239      25.093  -4.612  65.367  1.00 90.90           O  
ANISOU 3975  O   PHE B 239    16006   8162  10369   1631   1894   2916       O  
ATOM   3976  CB  PHE B 239      24.188  -7.287  67.066  1.00 75.24           C  
ANISOU 3976  CB  PHE B 239    13337   6695   8557   1559   1426   2562       C  
ATOM   3977  CG  PHE B 239      23.062  -6.939  66.138  1.00 79.38           C  
ANISOU 3977  CG  PHE B 239    14123   7182   8857   1747   1117   2741       C  
ATOM   3978  CD1 PHE B 239      22.937  -7.569  64.911  1.00 83.68           C  
ANISOU 3978  CD1 PHE B 239    15003   7769   9023   1819   1046   2803       C  
ATOM   3979  CD2 PHE B 239      22.115  -5.997  66.503  1.00 76.43           C  
ANISOU 3979  CD2 PHE B 239    13657   6730   8653   1867    883   2834       C  
ATOM   3980  CE1 PHE B 239      21.895  -7.256  64.059  1.00 89.04           C  
ANISOU 3980  CE1 PHE B 239    15924   8425   9483   2009    734   2958       C  
ATOM   3981  CE2 PHE B 239      21.071  -5.679  65.656  1.00 82.76           C  
ANISOU 3981  CE2 PHE B 239    14678   7502   9266   2062    578   2997       C  
ATOM   3982  CZ  PHE B 239      20.961  -6.310  64.432  1.00 89.17           C  
ANISOU 3982  CZ  PHE B 239    15826   8370   9686   2135    494   3059       C  
ATOM   3983  N   ARG B 240      24.921  -4.217  67.576  1.00 76.61           N  
ANISOU 3983  N   ARG B 240    13558   6406   9143   1533   1816   2715       N  
ATOM   3984  CA  ARG B 240      24.612  -2.808  67.359  1.00 69.80           C  
ANISOU 3984  CA  ARG B 240    12853   5317   8353   1619   1814   2873       C  
ATOM   3985  C   ARG B 240      25.771  -2.080  66.690  1.00 75.06           C  
ANISOU 3985  C   ARG B 240    13781   5773   8966   1534   2237   2945       C  
ATOM   3986  O   ARG B 240      25.559  -1.202  65.845  1.00 87.28           O  
ANISOU 3986  O   ARG B 240    15654   7131  10379   1630   2255   3142       O  
ATOM   3987  CB  ARG B 240      24.256  -2.138  68.687  1.00 71.11           C  
ANISOU 3987  CB  ARG B 240    12684   5445   8891   1609   1724   2779       C  
ATOM   3988  CG  ARG B 240      22.908  -2.537  69.262  1.00 74.83           C  
ANISOU 3988  CG  ARG B 240    12936   6057   9439   1734   1301   2747       C  
ATOM   3989  CD  ARG B 240      21.769  -1.780  68.591  1.00 92.92           C  
ANISOU 3989  CD  ARG B 240    15420   8225  11659   1944   1011   2947       C  
ATOM   3990  NE  ARG B 240      20.542  -1.834  69.380  1.00105.35           N  
ANISOU 3990  NE  ARG B 240    16711   9879  13440   2063    658   2890       N  
ATOM   3991  CZ  ARG B 240      20.149  -0.875  70.213  1.00112.16           C  
ANISOU 3991  CZ  ARG B 240    17406  10609  14601   2116    604   2853       C  
ATOM   3992  NH1 ARG B 240      20.890   0.215  70.366  1.00114.26           N  
ANISOU 3992  NH1 ARG B 240    17765  10658  14990   2052    869   2872       N  
ATOM   3993  NH2 ARG B 240      19.019  -1.005  70.894  1.00111.26           N  
ANISOU 3993  NH2 ARG B 240    17028  10572  14673   2234    298   2782       N  
ATOM   3994  N   LYS B 241      27.005  -2.430  67.053  1.00 71.81           N  
ANISOU 3994  N   LYS B 241    13228   5383   8673   1361   2584   2788       N  
ATOM   3995  CA  LYS B 241      28.166  -1.749  66.489  1.00 74.83           C  
ANISOU 3995  CA  LYS B 241    13813   5557   9064   1266   3023   2831       C  
ATOM   3996  C   LYS B 241      28.387  -2.133  65.027  1.00 78.72           C  
ANISOU 3996  C   LYS B 241    14732   6014   9163   1317   3140   2959       C  
ATOM   3997  O   LYS B 241      28.607  -1.265  64.174  1.00 84.08           O  
ANISOU 3997  O   LYS B 241    15753   6475   9719   1351   3327   3128       O  
ATOM   3998  CB  LYS B 241      29.408  -2.067  67.324  1.00 72.15           C  
ANISOU 3998  CB  LYS B 241    13157   5256   9000   1079   3342   2605       C  
ATOM   3999  CG  LYS B 241      30.438  -0.952  67.378  1.00 75.09           C  
ANISOU 3999  CG  LYS B 241    13550   5378   9601    966   3746   2602       C  
ATOM   4000  CD  LYS B 241      30.210  -0.051  68.586  1.00 86.40           C  
ANISOU 4000  CD  LYS B 241    14698   6740  11389    937   3669   2531       C  
ATOM   4001  CE  LYS B 241      30.963   1.268  68.462  1.00103.95           C  
ANISOU 4001  CE  LYS B 241    17021   8665  13811    853   4018   2580       C  
ATOM   4002  NZ  LYS B 241      32.427   1.105  68.669  1.00111.66           N  
ANISOU 4002  NZ  LYS B 241    17824   9602  15000    671   4438   2403       N  
ATOM   4003  N   LEU B 242      28.332  -3.433  64.718  1.00 78.67           N  
ANISOU 4003  N   LEU B 242    14731   6209   8950   1324   3040   2878       N  
ATOM   4004  CA  LEU B 242      28.688  -3.888  63.375  1.00 81.61           C  
ANISOU 4004  CA  LEU B 242    15506   6548   8952   1358   3194   2956       C  
ATOM   4005  C   LEU B 242      27.601  -3.577  62.352  1.00 91.73           C  
ANISOU 4005  C   LEU B 242    17177   7788   9887   1552   2900   3180       C  
ATOM   4006  O   LEU B 242      27.908  -3.253  61.199  1.00104.54           O  
ANISOU 4006  O   LEU B 242    19227   9266  11229   1598   3088   3320       O  
ATOM   4007  CB  LEU B 242      28.985  -5.387  63.392  1.00 76.63           C  
ANISOU 4007  CB  LEU B 242    14762   6128   8225   1307   3178   2783       C  
ATOM   4008  CG  LEU B 242      30.240  -5.805  64.159  1.00 73.83           C  
ANISOU 4008  CG  LEU B 242    14089   5797   8166   1132   3510   2568       C  
ATOM   4009  CD1 LEU B 242      30.313  -7.319  64.292  1.00 70.49           C  
ANISOU 4009  CD1 LEU B 242    13532   5585   7665   1109   3410   2410       C  
ATOM   4010  CD2 LEU B 242      31.481  -5.260  63.472  1.00 77.78           C  
ANISOU 4010  CD2 LEU B 242    14800   6078   8676   1047   4006   2587       C  
ATOM   4011  N   TRP B 243      26.333  -3.664  62.743  1.00 88.58           N  
ANISOU 4011  N   TRP B 243    16643   7508   9505   1676   2444   3215       N  
ATOM   4012  CA  TRP B 243      25.218  -3.465  61.826  1.00 91.55           C  
ANISOU 4012  CA  TRP B 243    17340   7869   9574   1883   2104   3407       C  
ATOM   4013  C   TRP B 243      24.505  -2.160  62.149  1.00100.63           C  
ANISOU 4013  C   TRP B 243    18466   8858  10910   1989   1939   3559       C  
ATOM   4014  O   TRP B 243      24.230  -1.868  63.317  1.00 99.63           O  
ANISOU 4014  O   TRP B 243    17959   8754  11142   1951   1838   3471       O  
ATOM   4015  CB  TRP B 243      24.239  -4.640  61.891  1.00 84.87           C  
ANISOU 4015  CB  TRP B 243    16367   7278   8603   1968   1684   3325       C  
ATOM   4016  CG  TRP B 243      24.751  -5.878  61.222  1.00 82.74           C  
ANISOU 4016  CG  TRP B 243    16257   7129   8050   1918   1790   3221       C  
ATOM   4017  CD1 TRP B 243      24.663  -6.184  59.897  1.00 86.89           C  
ANISOU 4017  CD1 TRP B 243    17236   7636   8144   2019   1763   3311       C  
ATOM   4018  CD2 TRP B 243      25.438  -6.973  61.842  1.00 78.31           C  
ANISOU 4018  CD2 TRP B 243    15424   6713   7617   1763   1938   3003       C  
ATOM   4019  NE1 TRP B 243      25.245  -7.403  59.652  1.00 85.26           N  
ANISOU 4019  NE1 TRP B 243    17052   7545   7798   1933   1891   3153       N  
ATOM   4020  CE2 TRP B 243      25.729  -7.908  60.830  1.00 80.00           C  
ANISOU 4020  CE2 TRP B 243    15940   6978   7478   1778   2000   2969       C  
ATOM   4021  CE3 TRP B 243      25.832  -7.254  63.154  1.00 73.38           C  
ANISOU 4021  CE3 TRP B 243    14343   6173   7364   1624   2018   2833       C  
ATOM   4022  CZ2 TRP B 243      26.396  -9.103  61.086  1.00 76.88           C  
ANISOU 4022  CZ2 TRP B 243    15395   6702   7113   1660   2141   2776       C  
ATOM   4023  CZ3 TRP B 243      26.495  -8.442  63.407  1.00 70.35           C  
ANISOU 4023  CZ3 TRP B 243    13815   5918   6998   1513   2149   2651       C  
ATOM   4024  CH2 TRP B 243      26.770  -9.352  62.377  1.00 77.23           C  
ANISOU 4024  CH2 TRP B 243    14984   6825   7535   1531   2211   2625       C  
ATOM   4025  N   GLY B 244      24.205  -1.388  61.115  1.00116.03           N  
ANISOU 4025  N   GLY B 244    20838  10636  12614   2132   1911   3786       N  
ATOM   4026  CA  GLY B 244      23.539  -0.100  61.290  1.00127.36           C  
ANISOU 4026  CA  GLY B 244    22302  11880  14209   2255   1760   3955       C  
ATOM   4027  C   GLY B 244      24.447   1.060  61.614  1.00137.77           C  
ANISOU 4027  C   GLY B 244    23638  12934  15775   2134   2161   3995       C  
ATOM   4028  O   GLY B 244      24.367   2.107  60.965  1.00142.82           O  
ANISOU 4028  O   GLY B 244    24609  13331  16324   2228   2228   4210       O  
ATOM   4029  N   ARG B 245      25.311   0.906  62.617  1.00145.35           N  
ANISOU 4029  N   ARG B 245    24247  13928  17052   1930   2426   3790       N  
ATOM   4030  CA  ARG B 245      26.219   1.982  62.999  1.00153.03           C  
ANISOU 4030  CA  ARG B 245    25195  14655  18295   1799   2813   3792       C  
ATOM   4031  C   ARG B 245      27.258   2.191  61.905  1.00151.71           C  
ANISOU 4031  C   ARG B 245    25429  14319  17896   1730   3253   3892       C  
ATOM   4032  O   ARG B 245      28.024   1.279  61.578  1.00152.00           O  
ANISOU 4032  O   ARG B 245    25487  14471  17796   1629   3475   3775       O  
ATOM   4033  CB  ARG B 245      26.886   1.669  64.337  1.00155.72           C  
ANISOU 4033  CB  ARG B 245    25052  15100  19015   1609   2962   3525       C  
ATOM   4034  CG  ARG B 245      25.989   1.953  65.533  1.00160.31           C  
ANISOU 4034  CG  ARG B 245    25274  15737  19901   1665   2629   3445       C  
ATOM   4035  CD  ARG B 245      26.691   1.699  66.858  1.00161.19           C  
ANISOU 4035  CD  ARG B 245    24945  15942  20360   1485   2788   3182       C  
ATOM   4036  NE  ARG B 245      25.905   2.206  67.979  1.00164.68           N  
ANISOU 4036  NE  ARG B 245    25100  16377  21094   1541   2530   3112       N  
ATOM   4037  CZ  ARG B 245      26.243   2.075  69.258  1.00166.01           C  
ANISOU 4037  CZ  ARG B 245    24885  16631  21561   1426   2583   2887       C  
ATOM   4038  NH1 ARG B 245      27.360   1.444  69.594  1.00165.70           N  
ANISOU 4038  NH1 ARG B 245    24678  16694  21588   1251   2865   2717       N  
ATOM   4039  NH2 ARG B 245      25.459   2.574  70.203  1.00166.53           N  
ANISOU 4039  NH2 ARG B 245    24738  16675  21861   1499   2350   2826       N  
ATOM   4040  N   GLN B 246      27.295   3.405  61.354  1.00136.16           N  
ANISOU 4040  N   GLN B 246    23780  12059  15898   1786   3396   4105       N  
ATOM   4041  CA  GLN B 246      28.126   3.726  60.193  1.00132.42           C  
ANISOU 4041  CA  GLN B 246    23761  11387  15166   1752   3802   4246       C  
ATOM   4042  C   GLN B 246      28.702   5.119  60.431  1.00127.98           C  
ANISOU 4042  C   GLN B 246    23247  10494  14887   1665   4132   4331       C  
ATOM   4043  O   GLN B 246      28.117   6.130  60.031  1.00121.44           O  
ANISOU 4043  O   GLN B 246    22696   9445  14002   1803   4023   4564       O  
ATOM   4044  CB  GLN B 246      27.320   3.652  58.901  1.00137.37           C  
ANISOU 4044  CB  GLN B 246    24884  12001  15309   1975   3560   4485       C  
ATOM   4045  CG  GLN B 246      26.569   2.338  58.721  1.00132.65           C  
ANISOU 4045  CG  GLN B 246    24219  11723  14457   2078   3164   4395       C  
ATOM   4046  CD  GLN B 246      25.530   2.398  57.614  1.00134.70           C  
ANISOU 4046  CD  GLN B 246    24913  11978  14290   2333   2809   4622       C  
ATOM   4047  OE1 GLN B 246      25.731   3.049  56.589  1.00141.53           O  
ANISOU 4047  OE1 GLN B 246    26265  12627  14883   2409   2986   4837       O  
ATOM   4048  NE2 GLN B 246      24.408   1.718  57.822  1.00129.70           N  
ANISOU 4048  NE2 GLN B 246    24104  11577  13600   2472   2305   4573       N  
ATOM   4049  N   ILE B 247      29.850   5.160  61.092  1.00126.24           N  
ANISOU 4049  N   ILE B 247    22748  10232  14985   1442   4526   4136       N  
ATOM   4050  CA  ILE B 247      30.472   6.441  61.441  1.00125.65           C  
ANISOU 4050  CA  ILE B 247    22659   9847  15237   1329   4856   4171       C  
ATOM   4051  C   ILE B 247      30.943   7.133  60.170  1.00129.75           C  
ANISOU 4051  C   ILE B 247    23721  10075  15505   1346   5213   4413       C  
ATOM   4052  O   ILE B 247      31.402   6.455  59.234  1.00129.26           O  
ANISOU 4052  O   ILE B 247    23926  10068  15121   1339   5409   4437       O  
ATOM   4053  CB  ILE B 247      31.633   6.212  62.407  1.00123.51           C  
ANISOU 4053  CB  ILE B 247    21946   9621  15362   1087   5188   3879       C  
ATOM   4054  CG1 ILE B 247      32.076   7.530  63.042  1.00126.27           C  
ANISOU 4054  CG1 ILE B 247    22180   9679  16119    975   5426   3869       C  
ATOM   4055  CG2 ILE B 247      32.787   5.530  61.687  1.00127.32           C  
ANISOU 4055  CG2 ILE B 247    22551  10120  15706    963   5618   3804       C  
ATOM   4056  CD1 ILE B 247      32.935   7.345  64.272  1.00121.39           C  
ANISOU 4056  CD1 ILE B 247    21039   9142  15942    771   5603   3555       C  
ATOM   4057  N   PRO B 248      30.834   8.459  60.074  1.00132.65           N  
ANISOU 4057  N   PRO B 248    24286  10119  15995   1375   5312   4599       N  
ATOM   4058  CA  PRO B 248      31.135   9.132  58.804  1.00140.36           C  
ANISOU 4058  CA  PRO B 248    25838  10809  16685   1420   5616   4871       C  
ATOM   4059  C   PRO B 248      32.579   8.940  58.366  1.00139.27           C  
ANISOU 4059  C   PRO B 248    25776  10571  16569   1208   6231   4776       C  
ATOM   4060  O   PRO B 248      33.502   8.905  59.184  1.00133.52           O  
ANISOU 4060  O   PRO B 248    24647   9846  16239    995   6517   4533       O  
ATOM   4061  CB  PRO B 248      30.824  10.605  59.100  1.00137.56           C  
ANISOU 4061  CB  PRO B 248    25565  10117  16584   1456   5615   5037       C  
ATOM   4062  CG  PRO B 248      29.908  10.573  60.284  1.00132.20           C  
ANISOU 4062  CG  PRO B 248    24450   9598  16183   1529   5135   4907       C  
ATOM   4063  CD  PRO B 248      30.354   9.398  61.098  1.00128.82           C  
ANISOU 4063  CD  PRO B 248    23541   9507  15899   1385   5127   4579       C  
ATOM   4064  N   GLY B 249      32.768   8.849  57.052  1.00142.81           N  
ANISOU 4064  N   GLY B 249    26750  10918  16592   1276   6436   4968       N  
ATOM   4065  CA  GLY B 249      34.090   8.899  56.443  1.00146.61           C  
ANISOU 4065  CA  GLY B 249    27410  11219  17075   1097   7068   4937       C  
ATOM   4066  C   GLY B 249      35.006   7.721  56.698  1.00141.32           C  
ANISOU 4066  C   GLY B 249    26414  10775  16505    938   7286   4633       C  
ATOM   4067  O   GLY B 249      36.220   7.909  56.840  1.00142.78           O  
ANISOU 4067  O   GLY B 249    26454  10812  16982    727   7798   4494       O  
ATOM   4068  N   THR B 250      34.461   6.510  56.742  1.00136.56           N  
ANISOU 4068  N   THR B 250    25691  10513  15683   1035   6913   4525       N  
ATOM   4069  CA  THR B 250      35.265   5.344  57.079  1.00133.44           C  
ANISOU 4069  CA  THR B 250    24957  10335  15410    899   7069   4231       C  
ATOM   4070  C   THR B 250      36.289   5.017  55.995  1.00139.73           C  
ANISOU 4070  C   THR B 250    26091  11002  15997    821   7585   4240       C  
ATOM   4071  O   THR B 250      36.052   5.195  54.797  1.00144.03           O  
ANISOU 4071  O   THR B 250    27201  11421  16103    939   7659   4475       O  
ATOM   4072  CB  THR B 250      34.373   4.132  57.318  1.00126.63           C  
ANISOU 4072  CB  THR B 250    23930   9842  14341   1029   6543   4136       C  
ATOM   4073  OG1 THR B 250      33.572   3.893  56.153  1.00130.04           O  
ANISOU 4073  OG1 THR B 250    24880  10300  14228   1233   6316   4358       O  
ATOM   4074  CG2 THR B 250      33.471   4.377  58.511  1.00121.68           C  
ANISOU 4074  CG2 THR B 250    22905   9346  13983   1078   6082   4084       C  
ATOM   4075  N   THR B 251      37.444   4.539  56.448  1.00139.43           N  
ANISOU 4075  N   THR B 251    25696  10988  16291    626   7942   3975       N  
ATOM   4076  CA  THR B 251      38.495   4.019  55.583  1.00138.70           C  
ANISOU 4076  CA  THR B 251    25813  10807  16079    536   8428   3913       C  
ATOM   4077  C   THR B 251      38.100   2.679  54.967  1.00136.72           C  
ANISOU 4077  C   THR B 251    25731  10814  15401    660   8184   3876       C  
ATOM   4078  O   THR B 251      37.428   1.853  55.593  1.00132.08           O  
ANISOU 4078  O   THR B 251    24854  10525  14806    732   7723   3756       O  
ATOM   4079  CB  THR B 251      39.797   3.852  56.368  1.00136.89           C  
ANISOU 4079  CB  THR B 251    25079  10541  16393    302   8818   3612       C  
ATOM   4080  OG1 THR B 251      40.204   5.118  56.896  1.00144.08           O  
ANISOU 4080  OG1 THR B 251    25844  11192  17706    176   9066   3633       O  
ATOM   4081  CG2 THR B 251      40.890   3.304  55.467  1.00140.89           C  
ANISOU 4081  CG2 THR B 251    25787  10938  16808    211   9330   3540       C  
ATOM   4082  N   SER B 252      38.540   2.463  53.723  1.00142.21           N  
ANISOU 4082  N   SER B 252    26911  11380  15742    680   8516   3976       N  
ATOM   4083  CA  SER B 252      38.231   1.215  53.035  1.00141.20           C  
ANISOU 4083  CA  SER B 252    26994  11465  15192    792   8325   3937       C  
ATOM   4084  C   SER B 252      38.796   0.015  53.781  1.00137.74           C  
ANISOU 4084  C   SER B 252    26043  11253  15039    685   8306   3611       C  
ATOM   4085  O   SER B 252      38.277  -1.095  53.630  1.00132.14           O  
ANISOU 4085  O   SER B 252    25347  10788  14072    784   7977   3541       O  
ATOM   4086  CB  SER B 252      38.784   1.237  51.606  1.00148.70           C  
ANISOU 4086  CB  SER B 252    28545  12203  15752    805   8767   4078       C  
ATOM   4087  OG  SER B 252      38.120   2.206  50.814  1.00156.30           O  
ANISOU 4087  OG  SER B 252    30052  12981  16355    946   8713   4404       O  
ATOM   4088  N   ALA B 285      39.847   0.206  54.578  1.00137.78           N  
ANISOU 4088  N   ALA B 285    25601  11173  15577    489   8642   3406       N  
ATOM   4089  CA  ALA B 285      40.337  -0.893  55.403  1.00128.16           C  
ANISOU 4089  CA  ALA B 285    23868  10168  14660    404   8572   3102       C  
ATOM   4090  C   ALA B 285      39.382  -1.174  56.553  1.00121.12           C  
ANISOU 4090  C   ALA B 285    22574   9551  13893    475   7995   3029       C  
ATOM   4091  O   ALA B 285      39.172  -2.334  56.927  1.00133.32           O  
ANISOU 4091  O   ALA B 285    23892  11349  15416    507   7722   2871       O  
ATOM   4092  CB  ALA B 285      41.736  -0.579  55.927  1.00129.27           C  
ANISOU 4092  CB  ALA B 285    23638  10128  15349    186   9074   2898       C  
ATOM   4093  N   GLU B 286      38.798  -0.122  57.129  1.00121.56           N  
ANISOU 4093  N   GLU B 286    22547   9548  14091    496   7816   3145       N  
ATOM   4094  CA  GLU B 286      37.834  -0.316  58.204  1.00114.55           C  
ANISOU 4094  CA  GLU B 286    21305   8905  13315    565   7279   3091       C  
ATOM   4095  C   GLU B 286      36.573  -1.012  57.706  1.00113.59           C  
ANISOU 4095  C   GLU B 286    21442   8996  12720    763   6787   3213       C  
ATOM   4096  O   GLU B 286      35.945  -1.770  58.457  1.00113.38           O  
ANISOU 4096  O   GLU B 286    21106   9231  12741    808   6379   3097       O  
ATOM   4097  CB  GLU B 286      37.483   1.032  58.832  1.00115.30           C  
ANISOU 4097  CB  GLU B 286    21302   8851  13656    549   7220   3201       C  
ATOM   4098  CG  GLU B 286      38.600   1.615  59.697  1.00115.24           C  
ANISOU 4098  CG  GLU B 286    20886   8695  14207    346   7588   3013       C  
ATOM   4099  CD  GLU B 286      38.255   2.999  60.213  1.00119.81           C  
ANISOU 4099  CD  GLU B 286    21425   9090  15007    329   7553   3131       C  
ATOM   4100  OE1 GLU B 286      37.455   3.066  61.166  1.00118.50           O  
ANISOU 4100  OE1 GLU B 286    20983   9079  14964    383   7138   3095       O  
ATOM   4101  OE2 GLU B 286      38.768   4.012  59.671  1.00122.57           O  
ANISOU 4101  OE2 GLU B 286    22029   9130  15413    260   7945   3258       O  
ATOM   4102  N   VAL B 287      36.179  -0.758  56.454  1.00118.27           N  
ANISOU 4102  N   VAL B 287    22605   9475  12858    885   6814   3445       N  
ATOM   4103  CA  VAL B 287      35.035  -1.462  55.880  1.00117.56           C  
ANISOU 4103  CA  VAL B 287    22780   9579  12308   1076   6352   3543       C  
ATOM   4104  C   VAL B 287      35.382  -2.922  55.636  1.00120.27           C  
ANISOU 4104  C   VAL B 287    23071  10107  12517   1057   6359   3352       C  
ATOM   4105  O   VAL B 287      34.556  -3.817  55.853  1.00118.27           O  
ANISOU 4105  O   VAL B 287    22713  10104  12120   1150   5919   3291       O  
ATOM   4106  CB  VAL B 287      34.567  -0.768  54.588  1.00124.43           C  
ANISOU 4106  CB  VAL B 287    24295  10264  12718   1221   6378   3840       C  
ATOM   4107  CG1 VAL B 287      33.436  -1.557  53.944  1.00124.18           C  
ANISOU 4107  CG1 VAL B 287    24536  10435  12209   1422   5894   3914       C  
ATOM   4108  CG2 VAL B 287      34.134   0.661  54.881  1.00126.63           C  
ANISOU 4108  CG2 VAL B 287    24616  10352  13146   1255   6326   4038       C  
ATOM   4109  N   LYS B 288      36.612  -3.189  55.191  1.00121.41           N  
ANISOU 4109  N   LYS B 288    23282  10118  12731    933   6865   3250       N  
ATOM   4110  CA  LYS B 288      37.060  -4.571  55.055  1.00121.53           C  
ANISOU 4110  CA  LYS B 288    23202  10281  12691    900   6904   3049       C  
ATOM   4111  C   LYS B 288      37.118  -5.258  56.411  1.00116.54           C  
ANISOU 4111  C   LYS B 288    21953   9864  12462    825   6687   2811       C  
ATOM   4112  O   LYS B 288      36.825  -6.454  56.526  1.00113.56           O  
ANISOU 4112  O   LYS B 288    21470   9696  11980    864   6437   2688       O  
ATOM   4113  CB  LYS B 288      38.426  -4.616  54.369  1.00129.53           C  
ANISOU 4113  CB  LYS B 288    24374  11075  13765    773   7521   2985       C  
ATOM   4114  CG  LYS B 288      38.915  -6.014  54.023  1.00131.52           C  
ANISOU 4114  CG  LYS B 288    24616  11438  13919    751   7599   2804       C  
ATOM   4115  CD  LYS B 288      40.243  -5.945  53.288  1.00138.62           C  
ANISOU 4115  CD  LYS B 288    25693  12090  14886    627   8233   2760       C  
ATOM   4116  CE  LYS B 288      40.786  -7.327  52.983  1.00136.48           C  
ANISOU 4116  CE  LYS B 288    25386  11909  14560    598   8327   2572       C  
ATOM   4117  NZ  LYS B 288      42.154  -7.270  52.398  1.00143.21           N  
ANISOU 4117  NZ  LYS B 288    26329  12518  15565    458   8964   2501       N  
ATOM   4118  N   GLN B 289      37.492  -4.513  57.453  1.00113.26           N  
ANISOU 4118  N   GLN B 289    21139   9390  12506    718   6778   2742       N  
ATOM   4119  CA  GLN B 289      37.522  -5.075  58.798  1.00102.17           C  
ANISOU 4119  CA  GLN B 289    19163   8182  11474    656   6561   2528       C  
ATOM   4120  C   GLN B 289      36.116  -5.387  59.294  1.00 95.91           C  
ANISOU 4120  C   GLN B 289    18284   7631  10526    787   5970   2583       C  
ATOM   4121  O   GLN B 289      35.881  -6.446  59.887  1.00 91.58           O  
ANISOU 4121  O   GLN B 289    17463   7303  10028    794   5717   2433       O  
ATOM   4122  CB  GLN B 289      38.234  -4.109  59.744  1.00101.80           C  
ANISOU 4122  CB  GLN B 289    18750   7999  11932    517   6796   2445       C  
ATOM   4123  CG  GLN B 289      38.462  -4.642  61.147  1.00 96.62           C  
ANISOU 4123  CG  GLN B 289    17509   7517  11684    444   6632   2207       C  
ATOM   4124  CD  GLN B 289      39.089  -3.603  62.058  1.00 98.78           C  
ANISOU 4124  CD  GLN B 289    17448   7650  12434    317   6832   2126       C  
ATOM   4125  OE1 GLN B 289      38.763  -2.417  61.979  1.00 97.98           O  
ANISOU 4125  OE1 GLN B 289    17492   7397  12339    325   6866   2283       O  
ATOM   4126  NE2 GLN B 289      39.999  -4.040  62.920  1.00 99.63           N  
ANISOU 4126  NE2 GLN B 289    17113   7794  12950    203   6958   1877       N  
ATOM   4127  N   MET B 290      35.172  -4.471  59.063  1.00 97.80           N  
ANISOU 4127  N   MET B 290    18750   7817  10591    893   5749   2800       N  
ATOM   4128  CA  MET B 290      33.802  -4.666  59.527  1.00 94.34           C  
ANISOU 4128  CA  MET B 290    18217   7583  10044   1019   5191   2857       C  
ATOM   4129  C   MET B 290      33.163  -5.889  58.879  1.00 93.54           C  
ANISOU 4129  C   MET B 290    18315   7669   9556   1128   4906   2845       C  
ATOM   4130  O   MET B 290      32.578  -6.736  59.565  1.00 88.80           O  
ANISOU 4130  O   MET B 290    17434   7295   9010   1150   4563   2732       O  
ATOM   4131  CB  MET B 290      32.974  -3.413  59.234  1.00 97.61           C  
ANISOU 4131  CB  MET B 290    18886   7861  10342   1126   5036   3106       C  
ATOM   4132  CG  MET B 290      31.488  -3.547  59.537  1.00 97.73           C  
ANISOU 4132  CG  MET B 290    18850   8053  10228   1280   4456   3187       C  
ATOM   4133  SD  MET B 290      30.572  -2.037  59.156  1.00114.96           S  
ANISOU 4133  SD  MET B 290    21335  10035  12308   1424   4282   3485       S  
ATOM   4134  CE  MET B 290      31.085  -0.974  60.507  1.00116.97           C  
ANISOU 4134  CE  MET B 290    21150  10162  13131   1276   4465   3404       C  
ATOM   4135  N   ARG B 291      33.265  -5.998  57.552  1.00 98.45           N  
ANISOU 4135  N   ARG B 291    19436   8191   9779   1197   5051   2957       N  
ATOM   4136  CA  ARG B 291      32.615  -7.100  56.849  1.00 98.41           C  
ANISOU 4136  CA  ARG B 291    19668   8346   9377   1310   4768   2947       C  
ATOM   4137  C   ARG B 291      33.187  -8.452  57.255  1.00 94.50           C  
ANISOU 4137  C   ARG B 291    18897   7998   9010   1220   4825   2702       C  
ATOM   4138  O   ARG B 291      32.470  -9.457  57.238  1.00 92.14           O  
ANISOU 4138  O   ARG B 291    18584   7893   8532   1290   4475   2640       O  
ATOM   4139  CB  ARG B 291      32.731  -6.897  55.338  1.00106.17           C  
ANISOU 4139  CB  ARG B 291    21265   9170   9903   1396   4955   3107       C  
ATOM   4140  CG  ARG B 291      31.863  -5.767  54.811  1.00111.92           C  
ANISOU 4140  CG  ARG B 291    22334   9787  10402   1542   4763   3373       C  
ATOM   4141  CD  ARG B 291      31.460  -6.001  53.366  1.00123.48           C  
ANISOU 4141  CD  ARG B 291    24405  11215  11299   1695   4689   3513       C  
ATOM   4142  NE  ARG B 291      30.640  -4.910  52.847  1.00133.22           N  
ANISOU 4142  NE  ARG B 291    25978  12330  12309   1853   4491   3779       N  
ATOM   4143  CZ  ARG B 291      29.315  -4.869  52.929  1.00136.90           C  
ANISOU 4143  CZ  ARG B 291    26445  12929  12642   2021   3937   3865       C  
ATOM   4144  NH1 ARG B 291      28.655  -5.860  53.511  1.00132.25           N  
ANISOU 4144  NH1 ARG B 291    25537  12596  12118   2040   3544   3705       N  
ATOM   4145  NH2 ARG B 291      28.649  -3.836  52.429  1.00143.51           N  
ANISOU 4145  NH2 ARG B 291    27600  13632  13296   2174   3780   4113       N  
ATOM   4146  N   ALA B 292      34.470  -8.503  57.623  1.00100.07           N  
ANISOU 4146  N   ALA B 292    19378   8606  10038   1067   5255   2558       N  
ATOM   4147  CA  ALA B 292      35.029  -9.756  58.119  1.00 97.80           C  
ANISOU 4147  CA  ALA B 292    18792   8445   9923    989   5293   2327       C  
ATOM   4148  C   ALA B 292      34.547 -10.047  59.536  1.00103.01           C  
ANISOU 4148  C   ALA B 292    18941   9301  10896    965   4964   2215       C  
ATOM   4149  O   ALA B 292      34.188 -11.187  59.855  1.00110.56           O  
ANISOU 4149  O   ALA B 292    19754  10441  11814    984   4716   2103       O  
ATOM   4150  CB  ALA B 292      36.555  -9.717  58.058  1.00 96.23           C  
ANISOU 4150  CB  ALA B 292    18499   8066   9997    845   5840   2205       C  
ATOM   4151  N   ARG B 293      34.535  -9.029  60.398  1.00100.20           N  
ANISOU 4151  N   ARG B 293    18323   8900  10849    920   4966   2245       N  
ATOM   4152  CA  ARG B 293      34.026  -9.211  61.752  1.00 89.25           C  
ANISOU 4152  CA  ARG B 293    16480   7691   9740    902   4655   2152       C  
ATOM   4153  C   ARG B 293      32.551  -9.590  61.743  1.00 86.94           C  
ANISOU 4153  C   ARG B 293    16260   7581   9192   1033   4140   2241       C  
ATOM   4154  O   ARG B 293      32.089 -10.314  62.633  1.00 84.61           O  
ANISOU 4154  O   ARG B 293    15651   7473   9024   1027   3866   2135       O  
ATOM   4155  CB  ARG B 293      34.245  -7.933  62.562  1.00 82.21           C  
ANISOU 4155  CB  ARG B 293    15356   6690   9191    838   4760   2179       C  
ATOM   4156  CG  ARG B 293      35.671  -7.739  63.059  1.00 77.66           C  
ANISOU 4156  CG  ARG B 293    14513   5988   9008    687   5186   2015       C  
ATOM   4157  CD  ARG B 293      35.882  -6.310  63.537  1.00 88.44           C  
ANISOU 4157  CD  ARG B 293    15772   7189  10643    629   5334   2072       C  
ATOM   4158  NE  ARG B 293      37.073  -6.163  64.368  1.00 87.46           N  
ANISOU 4158  NE  ARG B 293    15266   6991  10972    486   5628   1874       N  
ATOM   4159  CZ  ARG B 293      37.480  -5.009  64.887  1.00 89.00           C  
ANISOU 4159  CZ  ARG B 293    15310   7031  11475    405   5805   1866       C  
ATOM   4160  NH1 ARG B 293      36.797  -3.895  64.658  1.00 86.64           N  
ANISOU 4160  NH1 ARG B 293    15221   6622  11075    455   5731   2059       N  
ATOM   4161  NH2 ARG B 293      38.576  -4.967  65.632  1.00 91.02           N  
ANISOU 4161  NH2 ARG B 293    15204   7227  12152    278   6048   1661       N  
ATOM   4162  N   ARG B 294      31.796  -9.110  60.752  1.00 88.23           N  
ANISOU 4162  N   ARG B 294    16833   7684   9006   1154   4001   2433       N  
ATOM   4163  CA  ARG B 294      30.390  -9.487  60.657  1.00 86.07           C  
ANISOU 4163  CA  ARG B 294    16631   7573   8501   1288   3499   2507       C  
ATOM   4164  C   ARG B 294      30.236 -10.977  60.386  1.00 83.84           C  
ANISOU 4164  C   ARG B 294    16381   7450   8026   1304   3352   2381       C  
ATOM   4165  O   ARG B 294      29.326 -11.620  60.923  1.00 84.88           O  
ANISOU 4165  O   ARG B 294    16323   7762   8167   1345   2970   2335       O  
ATOM   4166  CB  ARG B 294      29.704  -8.684  59.552  1.00 91.40           C  
ANISOU 4166  CB  ARG B 294    17767   8133   8828   1431   3388   2736       C  
ATOM   4167  CG  ARG B 294      29.294  -7.270  59.922  1.00 93.66           C  
ANISOU 4167  CG  ARG B 294    18010   8297   9281   1467   3332   2893       C  
ATOM   4168  CD  ARG B 294      28.698  -6.580  58.703  1.00101.69           C  
ANISOU 4168  CD  ARG B 294    19534   9186   9918   1625   3236   3126       C  
ATOM   4169  NE  ARG B 294      28.275  -5.209  58.969  1.00106.36           N  
ANISOU 4169  NE  ARG B 294    20126   9632  10656   1678   3177   3296       N  
ATOM   4170  CZ  ARG B 294      27.435  -4.530  58.196  1.00112.50           C  
ANISOU 4170  CZ  ARG B 294    21255  10322  11169   1850   2955   3513       C  
ATOM   4171  NH1 ARG B 294      26.924  -5.099  57.112  1.00117.20           N  
ANISOU 4171  NH1 ARG B 294    22228  10975  11326   1985   2761   3577       N  
ATOM   4172  NH2 ARG B 294      27.101  -3.284  58.505  1.00115.42           N  
ANISOU 4172  NH2 ARG B 294    21604  10537  11713   1895   2916   3662       N  
ATOM   4173  N   LYS B 295      31.115 -11.542  59.555  1.00 79.11           N  
ANISOU 4173  N   LYS B 295    16024   6772   7261   1268   3662   2320       N  
ATOM   4174  CA  LYS B 295      31.024 -12.965  59.246  1.00 78.20           C  
ANISOU 4174  CA  LYS B 295    15970   6782   6960   1281   3545   2194       C  
ATOM   4175  C   LYS B 295      31.279 -13.814  60.483  1.00 79.14           C  
ANISOU 4175  C   LYS B 295    15611   7039   7420   1185   3495   2008       C  
ATOM   4176  O   LYS B 295      30.671 -14.877  60.652  1.00 83.26           O  
ANISOU 4176  O   LYS B 295    16071   7715   7851   1213   3212   1930       O  
ATOM   4177  CB  LYS B 295      32.015 -13.325  58.142  1.00 81.89           C  
ANISOU 4177  CB  LYS B 295    16787   7108   7220   1254   3935   2163       C  
ATOM   4178  CG  LYS B 295      31.591 -12.899  56.748  1.00 87.61           C  
ANISOU 4178  CG  LYS B 295    18071   7735   7480   1377   3909   2333       C  
ATOM   4179  CD  LYS B 295      32.764 -13.012  55.782  1.00 91.90           C  
ANISOU 4179  CD  LYS B 295    18928   8098   7891   1324   4398   2311       C  
ATOM   4180  CE  LYS B 295      32.331 -12.851  54.335  1.00 97.80           C  
ANISOU 4180  CE  LYS B 295    20278   8772   8111   1456   4353   2460       C  
ATOM   4181  NZ  LYS B 295      33.282 -13.521  53.403  1.00101.25           N  
ANISOU 4181  NZ  LYS B 295    21010   9102   8358   1412   4732   2382       N  
ATOM   4182  N   THR B 296      32.175 -13.360  61.360  1.00 78.93           N  
ANISOU 4182  N   THR B 296    15252   6951   7786   1074   3763   1933       N  
ATOM   4183  CA  THR B 296      32.469 -14.109  62.576  1.00 74.22           C  
ANISOU 4183  CA  THR B 296    14208   6476   7514    994   3718   1763       C  
ATOM   4184  C   THR B 296      31.367 -13.944  63.616  1.00 77.22           C  
ANISOU 4184  C   THR B 296    14304   7015   8022   1025   3317   1792       C  
ATOM   4185  O   THR B 296      30.961 -14.922  64.253  1.00 77.77           O  
ANISOU 4185  O   THR B 296    14167   7239   8144   1018   3093   1699       O  
ATOM   4186  CB  THR B 296      33.817 -13.670  63.146  1.00 69.67           C  
ANISOU 4186  CB  THR B 296    13376   5776   7318    876   4120   1661       C  
ATOM   4187  OG1 THR B 296      34.822 -13.780  62.130  1.00 79.58           O  
ANISOU 4187  OG1 THR B 296    14899   6862   8475    844   4511   1640       O  
ATOM   4188  CG2 THR B 296      34.206 -14.540  64.328  1.00 62.66           C  
ANISOU 4188  CG2 THR B 296    12060   5005   6743    810   4075   1481       C  
ATOM   4189  N   ALA B 297      30.875 -12.716  63.805  1.00 79.40           N  
ANISOU 4189  N   ALA B 297    14572   7239   8359   1057   3234   1923       N  
ATOM   4190  CA  ALA B 297      29.801 -12.488  64.764  1.00 76.40           C  
ANISOU 4190  CA  ALA B 297    13930   6986   8115   1091   2865   1954       C  
ATOM   4191  C   ALA B 297      28.569 -13.316  64.419  1.00 74.70           C  
ANISOU 4191  C   ALA B 297    13831   6913   7637   1190   2457   1988       C  
ATOM   4192  O   ALA B 297      27.933 -13.899  65.306  1.00 78.23           O  
ANISOU 4192  O   ALA B 297    13999   7506   8217   1183   2197   1923       O  
ATOM   4193  CB  ALA B 297      29.456 -11.000  64.819  1.00 79.65           C  
ANISOU 4193  CB  ALA B 297    14383   7277   8602   1128   2854   2102       C  
ATOM   4194  N   LYS B 298      28.214 -13.374  63.133  1.00 79.09           N  
ANISOU 4194  N   LYS B 298    14806   7422   7822   1286   2395   2085       N  
ATOM   4195  CA  LYS B 298      27.072 -14.181  62.720  1.00 81.19           C  
ANISOU 4195  CA  LYS B 298    15202   7816   7830   1385   1997   2098       C  
ATOM   4196  C   LYS B 298      27.271 -15.645  63.093  1.00 82.96           C  
ANISOU 4196  C   LYS B 298    15277   8161   8081   1320   1966   1926       C  
ATOM   4197  O   LYS B 298      26.324 -16.323  63.508  1.00 86.56           O  
ANISOU 4197  O   LYS B 298    15598   8754   8537   1351   1622   1892       O  
ATOM   4198  CB  LYS B 298      26.858 -14.029  61.212  1.00 89.10           C  
ANISOU 4198  CB  LYS B 298    16715   8735   8405   1498   1975   2207       C  
ATOM   4199  CG  LYS B 298      25.661 -14.769  60.641  1.00 92.93           C  
ANISOU 4199  CG  LYS B 298    17376   9340   8592   1619   1537   2214       C  
ATOM   4200  CD  LYS B 298      25.559 -14.502  59.145  1.00103.64           C  
ANISOU 4200  CD  LYS B 298    19263  10601   9515   1736   1535   2321       C  
ATOM   4201  CE  LYS B 298      24.603 -15.460  58.459  1.00107.35           C  
ANISOU 4201  CE  LYS B 298    19941  11188   9658   1843   1136   2271       C  
ATOM   4202  NZ  LYS B 298      24.540 -15.212  56.993  1.00112.26           N  
ANISOU 4202  NZ  LYS B 298    21102  11720   9832   1965   1129   2366       N  
ATOM   4203  N   MET B 299      28.502 -16.146  62.957  1.00 80.17           N  
ANISOU 4203  N   MET B 299    14945   7744   7771   1231   2329   1817       N  
ATOM   4204  CA  MET B 299      28.793 -17.528  63.323  1.00 78.15           C  
ANISOU 4204  CA  MET B 299    14556   7575   7562   1173   2331   1657       C  
ATOM   4205  C   MET B 299      28.759 -17.721  64.834  1.00 78.97           C  
ANISOU 4205  C   MET B 299    14184   7781   8039   1099   2253   1579       C  
ATOM   4206  O   MET B 299      28.090 -18.630  65.338  1.00 82.40           O  
ANISOU 4206  O   MET B 299    14483   8340   8486   1099   1995   1523       O  
ATOM   4207  CB  MET B 299      30.151 -17.940  62.755  1.00 74.09           C  
ANISOU 4207  CB  MET B 299    14184   6938   7027   1112   2753   1565       C  
ATOM   4208  CG  MET B 299      30.471 -19.414  62.926  1.00 68.69           C  
ANISOU 4208  CG  MET B 299    13439   6312   6350   1070   2766   1408       C  
ATOM   4209  SD  MET B 299      32.173 -19.795  62.481  1.00 76.28           S  
ANISOU 4209  SD  MET B 299    14465   7107   7411    993   3290   1292       S  
ATOM   4210  CE  MET B 299      33.042 -19.128  63.895  1.00 74.66           C  
ANISOU 4210  CE  MET B 299    13754   6883   7729    899   3492   1235       C  
ATOM   4211  N   LEU B 300      29.478 -16.873  65.577  1.00 76.18           N  
ANISOU 4211  N   LEU B 300    13585   7371   7988   1034   2476   1569       N  
ATOM   4212  CA  LEU B 300      29.556 -17.046  67.025  1.00 60.56           C  
ANISOU 4212  CA  LEU B 300    11173   5486   6352    967   2421   1482       C  
ATOM   4213  C   LEU B 300      28.183 -16.934  67.673  1.00 56.66           C  
ANISOU 4213  C   LEU B 300    10526   5112   5889   1014   2023   1546       C  
ATOM   4214  O   LEU B 300      27.889 -17.634  68.648  1.00 60.18           O  
ANISOU 4214  O   LEU B 300    10703   5669   6492    979   1877   1471       O  
ATOM   4215  CB  LEU B 300      30.501 -16.008  67.631  1.00 56.61           C  
ANISOU 4215  CB  LEU B 300    10470   4890   6148    902   2702   1460       C  
ATOM   4216  CG  LEU B 300      31.965 -16.005  67.197  1.00 65.59           C  
ANISOU 4216  CG  LEU B 300    11669   5885   7367    843   3129   1378       C  
ATOM   4217  CD1 LEU B 300      32.688 -14.843  67.850  1.00 69.73           C  
ANISOU 4217  CD1 LEU B 300    11978   6313   8202    782   3346   1361       C  
ATOM   4218  CD2 LEU B 300      32.630 -17.321  67.559  1.00 62.14           C  
ANISOU 4218  CD2 LEU B 300    11086   5495   7030    801   3211   1224       C  
ATOM   4219  N   MET B 301      27.325 -16.060  67.142  1.00 54.93           N  
ANISOU 4219  N   MET B 301    10478   4860   5534   1100   1847   1687       N  
ATOM   4220  CA  MET B 301      25.992 -15.916  67.713  1.00 58.00           C  
ANISOU 4220  CA  MET B 301    10712   5342   5984   1160   1472   1745       C  
ATOM   4221  C   MET B 301      25.171 -17.185  67.540  1.00 63.74           C  
ANISOU 4221  C   MET B 301    11481   6184   6554   1194   1190   1703       C  
ATOM   4222  O   MET B 301      24.357 -17.520  68.409  1.00 64.67           O  
ANISOU 4222  O   MET B 301    11348   6396   6826   1196    951   1682       O  
ATOM   4223  CB  MET B 301      25.279 -14.722  67.080  1.00 61.91           C  
ANISOU 4223  CB  MET B 301    11399   5755   6368   1268   1342   1907       C  
ATOM   4224  CG  MET B 301      25.859 -13.383  67.496  1.00 67.49           C  
ANISOU 4224  CG  MET B 301    12014   6339   7288   1234   1566   1952       C  
ATOM   4225  SD  MET B 301      25.154 -12.007  66.577  1.00 75.92           S  
ANISOU 4225  SD  MET B 301    13381   7270   8196   1370   1453   2162       S  
ATOM   4226  CE  MET B 301      26.330 -10.716  66.966  1.00 74.97           C  
ANISOU 4226  CE  MET B 301    13196   6972   8318   1278   1857   2168       C  
ATOM   4227  N   VAL B 302      25.372 -17.903  66.433  1.00 66.97           N  
ANISOU 4227  N   VAL B 302    12216   6572   6659   1220   1221   1683       N  
ATOM   4228  CA  VAL B 302      24.674 -19.169  66.233  1.00 62.99           C  
ANISOU 4228  CA  VAL B 302    11780   6159   5996   1243    962   1621       C  
ATOM   4229  C   VAL B 302      25.201 -20.231  67.189  1.00 63.74           C  
ANISOU 4229  C   VAL B 302    11618   6307   6291   1136   1066   1488       C  
ATOM   4230  O   VAL B 302      24.430 -21.017  67.753  1.00 68.08           O  
ANISOU 4230  O   VAL B 302    12024   6942   6901   1131    820   1451       O  
ATOM   4231  CB  VAL B 302      24.798 -19.621  64.768  1.00 55.84           C  
ANISOU 4231  CB  VAL B 302    11324   5202   4690   1302    974   1616       C  
ATOM   4232  CG1 VAL B 302      24.181 -21.000  64.582  1.00 53.84           C  
ANISOU 4232  CG1 VAL B 302    11155   5029   4274   1310    714   1517       C  
ATOM   4233  CG2 VAL B 302      24.144 -18.606  63.844  1.00 55.89           C  
ANISOU 4233  CG2 VAL B 302    11594   5162   4480   1429    816   1758       C  
ATOM   4234  N   VAL B 303      26.521 -20.284  67.374  1.00 55.71           N  
ANISOU 4234  N   VAL B 303    10545   5230   5391   1057   1429   1415       N  
ATOM   4235  CA  VAL B 303      27.100 -21.253  68.301  1.00 47.55           C  
ANISOU 4235  CA  VAL B 303     9265   4238   4562    973   1530   1294       C  
ATOM   4236  C   VAL B 303      26.552 -21.037  69.704  1.00 51.30           C  
ANISOU 4236  C   VAL B 303     9355   4804   5334    942   1368   1298       C  
ATOM   4237  O   VAL B 303      26.163 -21.987  70.393  1.00 58.46           O  
ANISOU 4237  O   VAL B 303    10109   5778   6326    912   1227   1245       O  
ATOM   4238  CB  VAL B 303      28.636 -21.165  68.279  1.00 50.75           C  
ANISOU 4238  CB  VAL B 303     9644   4551   5086    916   1940   1215       C  
ATOM   4239  CG1 VAL B 303      29.232 -22.015  69.390  1.00 42.30           C  
ANISOU 4239  CG1 VAL B 303     8273   3525   4273    849   2018   1100       C  
ATOM   4240  CG2 VAL B 303      29.171 -21.590  66.924  1.00 52.94           C  
ANISOU 4240  CG2 VAL B 303    10307   4730   5079    942   2120   1191       C  
ATOM   4241  N   VAL B 304      26.518 -19.780  70.152  1.00 59.72           N  
ANISOU 4241  N   VAL B 304    10276   5854   6559    950   1398   1357       N  
ATOM   4242  CA  VAL B 304      26.012 -19.492  71.489  1.00 53.74           C  
ANISOU 4242  CA  VAL B 304     9177   5170   6072    927   1265   1348       C  
ATOM   4243  C   VAL B 304      24.524 -19.805  71.585  1.00 55.73           C  
ANISOU 4243  C   VAL B 304     9409   5490   6276    988    909   1407       C  
ATOM   4244  O   VAL B 304      24.037 -20.254  72.629  1.00 58.28           O  
ANISOU 4244  O   VAL B 304     9484   5883   6778    962    790   1368       O  
ATOM   4245  CB  VAL B 304      26.305 -18.030  71.867  1.00 49.31           C  
ANISOU 4245  CB  VAL B 304     8511   4551   5673    928   1384   1388       C  
ATOM   4246  CG1 VAL B 304      25.717 -17.716  73.230  1.00 42.76           C  
ANISOU 4246  CG1 VAL B 304     7364   3790   5092    918   1245   1365       C  
ATOM   4247  CG2 VAL B 304      27.802 -17.762  71.845  1.00 55.31           C  
ANISOU 4247  CG2 VAL B 304     9257   5233   6524    867   1742   1316       C  
ATOM   4248  N   LEU B 305      23.775 -19.570  70.505  1.00 60.74           N  
ANISOU 4248  N   LEU B 305    10305   6099   6674   1081    731   1497       N  
ATOM   4249  CA  LEU B 305      22.345 -19.855  70.533  1.00 60.06           C  
ANISOU 4249  CA  LEU B 305    10190   6072   6559   1162    367   1541       C  
ATOM   4250  C   LEU B 305      22.085 -21.355  70.563  1.00 55.39           C  
ANISOU 4250  C   LEU B 305     9627   5528   5891   1128    244   1460       C  
ATOM   4251  O   LEU B 305      21.240 -21.830  71.332  1.00 53.31           O  
ANISOU 4251  O   LEU B 305     9162   5316   5777   1132     46   1445       O  
ATOM   4252  CB  LEU B 305      21.654 -19.221  69.327  1.00 64.70           C  
ANISOU 4252  CB  LEU B 305    11058   6626   6900   1289    175   1643       C  
ATOM   4253  CG  LEU B 305      20.162 -19.518  69.173  1.00 69.28           C  
ANISOU 4253  CG  LEU B 305    11619   7272   7432   1403   -251   1668       C  
ATOM   4254  CD1 LEU B 305      19.366 -18.799  70.251  1.00 65.43           C  
ANISOU 4254  CD1 LEU B 305    10787   6809   7263   1447   -371   1705       C  
ATOM   4255  CD2 LEU B 305      19.680 -19.120  67.790  1.00 74.30           C  
ANISOU 4255  CD2 LEU B 305    12592   7884   7755   1531   -445   1737       C  
ATOM   4256  N   VAL B 306      22.800 -22.116  69.732  1.00 59.69           N  
ANISOU 4256  N   VAL B 306    10434   6036   6210   1096    371   1404       N  
ATOM   4257  CA  VAL B 306      22.634 -23.565  69.737  1.00 58.41           C  
ANISOU 4257  CA  VAL B 306    10337   5885   5970   1055    269   1317       C  
ATOM   4258  C   VAL B 306      23.106 -24.155  71.059  1.00 57.82           C  
ANISOU 4258  C   VAL B 306     9950   5830   6191    954    415   1253       C  
ATOM   4259  O   VAL B 306      22.534 -25.129  71.561  1.00 61.90           O  
ANISOU 4259  O   VAL B 306    10391   6355   6774    924    257   1216       O  
ATOM   4260  CB  VAL B 306      23.378 -24.191  68.545  1.00 54.98           C  
ANISOU 4260  CB  VAL B 306    10276   5389   5226   1050    410   1258       C  
ATOM   4261  CG1 VAL B 306      23.356 -25.705  68.656  1.00 49.01           C  
ANISOU 4261  CG1 VAL B 306     9590   4614   4418    992    345   1155       C  
ATOM   4262  CG2 VAL B 306      22.765 -23.731  67.233  1.00 56.34           C  
ANISOU 4262  CG2 VAL B 306    10783   5555   5070   1160    210   1310       C  
ATOM   4263  N   PHE B 307      24.163 -23.585  71.641  1.00 58.22           N  
ANISOU 4263  N   PHE B 307     9825   5877   6421    902    700   1229       N  
ATOM   4264  CA  PHE B 307      24.632 -24.052  72.942  1.00 56.45           C  
ANISOU 4264  CA  PHE B 307     9295   5688   6464    825    804   1159       C  
ATOM   4265  C   PHE B 307      23.567 -23.845  74.013  1.00 58.24           C  
ANISOU 4265  C   PHE B 307     9261   5979   6888    832    607   1196       C  
ATOM   4266  O   PHE B 307      23.271 -24.755  74.795  1.00 56.22           O  
ANISOU 4266  O   PHE B 307     8868   5744   6747    788    548   1159       O  
ATOM   4267  CB  PHE B 307      25.927 -23.334  73.325  1.00 52.78           C  
ANISOU 4267  CB  PHE B 307     8702   5211   6139    791   1093   1114       C  
ATOM   4268  CG  PHE B 307      26.562 -23.858  74.583  1.00 49.91           C  
ANISOU 4268  CG  PHE B 307     8063   4891   6008    733   1182   1027       C  
ATOM   4269  CD1 PHE B 307      27.469 -24.903  74.534  1.00 50.10           C  
ANISOU 4269  CD1 PHE B 307     8123   4878   6034    706   1326    944       C  
ATOM   4270  CD2 PHE B 307      26.253 -23.304  75.815  1.00 49.72           C  
ANISOU 4270  CD2 PHE B 307     7767   4936   6190    721   1120   1026       C  
ATOM   4271  CE1 PHE B 307      28.061 -25.385  75.690  1.00 48.93           C  
ANISOU 4271  CE1 PHE B 307     7735   4768   6090    675   1377    873       C  
ATOM   4272  CE2 PHE B 307      26.839 -23.783  76.975  1.00 49.26           C  
ANISOU 4272  CE2 PHE B 307     7492   4923   6303    684   1180    949       C  
ATOM   4273  CZ  PHE B 307      27.744 -24.826  76.912  1.00 46.94           C  
ANISOU 4273  CZ  PHE B 307     7229   4597   6010    665   1294    878       C  
ATOM   4274  N   ALA B 308      22.985 -22.643  74.066  1.00 58.20           N  
ANISOU 4274  N   ALA B 308     9194   5988   6931    894    524   1270       N  
ATOM   4275  CA  ALA B 308      21.957 -22.359  75.064  1.00 55.68           C  
ANISOU 4275  CA  ALA B 308     8631   5716   6809    924    368   1301       C  
ATOM   4276  C   ALA B 308      20.746 -23.268  74.891  1.00 58.13           C  
ANISOU 4276  C   ALA B 308     8970   6040   7076    962     97   1315       C  
ATOM   4277  O   ALA B 308      20.110 -23.662  75.876  1.00 59.31           O  
ANISOU 4277  O   ALA B 308     8830   6277   7428    902     26   1255       O  
ATOM   4278  CB  ALA B 308      21.541 -20.889  74.981  1.00 47.26           C  
ANISOU 4278  CB  ALA B 308     7531   4635   5792   1005    320   1371       C  
ATOM   4279  N   LEU B 309      20.409 -23.614  73.645  1.00 59.99           N  
ANISOU 4279  N   LEU B 309     9466   6260   7067    999    -78   1314       N  
ATOM   4280  CA  LEU B 309      19.265 -24.490  73.410  1.00 57.92           C  
ANISOU 4280  CA  LEU B 309     9119   6083   6806    960   -388   1220       C  
ATOM   4281  C   LEU B 309      19.586 -25.932  73.781  1.00 54.60           C  
ANISOU 4281  C   LEU B 309     8630   5676   6439    807   -321   1095       C  
ATOM   4282  O   LEU B 309      18.779 -26.605  74.432  1.00 58.37           O  
ANISOU 4282  O   LEU B 309     8854   6219   7103    718   -445   1018       O  
ATOM   4283  CB  LEU B 309      18.825 -24.399  71.947  1.00 57.84           C  
ANISOU 4283  CB  LEU B 309     9431   6051   6494   1059   -632   1238       C  
ATOM   4284  CG  LEU B 309      18.240 -23.065  71.474  1.00 56.61           C  
ANISOU 4284  CG  LEU B 309     9365   5873   6271   1238   -791   1371       C  
ATOM   4285  CD1 LEU B 309      18.278 -22.956  69.954  1.00 58.88           C  
ANISOU 4285  CD1 LEU B 309    10107   6106   6161   1350   -937   1423       C  
ATOM   4286  CD2 LEU B 309      16.821 -22.896  71.989  1.00 51.00           C  
ANISOU 4286  CD2 LEU B 309     8307   5265   5807   1275  -1098   1325       C  
ATOM   4287  N   CYS B 310      20.758 -26.424  73.381  1.00 56.40           N  
ANISOU 4287  N   CYS B 310     9080   5827   6522    778   -106   1075       N  
ATOM   4288  CA  CYS B 310      21.106 -27.808  73.681  1.00 57.62           C  
ANISOU 4288  CA  CYS B 310     9198   5966   6731    657    -46    960       C  
ATOM   4289  C   CYS B 310      21.202 -28.057  75.181  1.00 54.12           C  
ANISOU 4289  C   CYS B 310     8439   5556   6567    584     73    957       C  
ATOM   4290  O   CYS B 310      20.869 -29.151  75.652  1.00 56.20           O  
ANISOU 4290  O   CYS B 310     8591   5823   6937    480     23    882       O  
ATOM   4291  CB  CYS B 310      22.424 -28.171  72.999  1.00 59.12           C  
ANISOU 4291  CB  CYS B 310     9665   6058   6740    666    191    934       C  
ATOM   4292  SG  CYS B 310      22.282 -28.544  71.236  1.00 68.71           S  
ANISOU 4292  SG  CYS B 310    11308   7227   7570    711     53    875       S  
ATOM   4293  N   TYR B 311      21.641 -27.062  75.947  1.00 50.88           N  
ANISOU 4293  N   TYR B 311     7902   5159   6270    636    229   1036       N  
ATOM   4294  CA  TYR B 311      21.863 -27.248  77.373  1.00 44.21           C  
ANISOU 4294  CA  TYR B 311     6810   4350   5638    587    347   1030       C  
ATOM   4295  C   TYR B 311      20.695 -26.802  78.241  1.00 42.68           C  
ANISOU 4295  C   TYR B 311     6352   4249   5616    577    233   1050       C  
ATOM   4296  O   TYR B 311      20.708 -27.069  79.448  1.00 43.95           O  
ANISOU 4296  O   TYR B 311     6331   4447   5922    529    321   1042       O  
ATOM   4297  CB  TYR B 311      23.138 -26.510  77.795  1.00 39.08           C  
ANISOU 4297  CB  TYR B 311     6164   3659   5025    640    589   1063       C  
ATOM   4298  CG  TYR B 311      24.392 -27.248  77.398  1.00 46.80           C  
ANISOU 4298  CG  TYR B 311     7254   4596   5933    609    734    979       C  
ATOM   4299  CD1 TYR B 311      24.869 -27.198  76.094  1.00 47.89           C  
ANISOU 4299  CD1 TYR B 311     7645   4667   5883    638    793    970       C  
ATOM   4300  CD2 TYR B 311      25.101 -27.995  78.327  1.00 48.00           C  
ANISOU 4300  CD2 TYR B 311     7272   4767   6198    570    815    913       C  
ATOM   4301  CE1 TYR B 311      26.012 -27.878  75.728  1.00 43.78           C  
ANISOU 4301  CE1 TYR B 311     7224   4090   5320    627    963    892       C  
ATOM   4302  CE2 TYR B 311      26.246 -28.672  77.971  1.00 46.30           C  
ANISOU 4302  CE2 TYR B 311     7142   4498   5950    573    945    839       C  
ATOM   4303  CZ  TYR B 311      26.698 -28.611  76.673  1.00 47.04           C  
ANISOU 4303  CZ  TYR B 311     7469   4516   5889    600   1035    825       C  
ATOM   4304  OH  TYR B 311      27.841 -29.290  76.328  1.00 57.74           O  
ANISOU 4304  OH  TYR B 311     8905   5798   7235    614   1203    747       O  
ATOM   4305  N   LEU B 312      19.707 -26.113  77.672  1.00 42.79           N  
ANISOU 4305  N   LEU B 312     6347   4298   5613    636     46   1075       N  
ATOM   4306  CA  LEU B 312      18.558 -25.695  78.471  1.00 46.09           C  
ANISOU 4306  CA  LEU B 312     6482   4802   6228    636    -48   1074       C  
ATOM   4307  C   LEU B 312      17.796 -26.874  79.058  1.00 48.62           C  
ANISOU 4307  C   LEU B 312     6625   5166   6683    496   -103   1001       C  
ATOM   4308  O   LEU B 312      17.521 -26.864  80.271  1.00 55.70           O  
ANISOU 4308  O   LEU B 312     7309   6112   7743    453      9   1004       O  
ATOM   4309  CB  LEU B 312      17.635 -24.807  77.629  1.00 48.04           C  
ANISOU 4309  CB  LEU B 312     6742   5066   6444    749   -275   1105       C  
ATOM   4310  CG  LEU B 312      16.395 -24.258  78.342  1.00 46.73           C  
ANISOU 4310  CG  LEU B 312     6258   4984   6513    778   -378   1090       C  
ATOM   4311  CD1 LEU B 312      16.808 -23.277  79.416  1.00 44.96           C  
ANISOU 4311  CD1 LEU B 312     5916   4763   6406    832   -163   1134       C  
ATOM   4312  CD2 LEU B 312      15.433 -23.605  77.360  1.00 45.71           C  
ANISOU 4312  CD2 LEU B 312     6146   4866   6356    905   -670   1104       C  
ATOM   4313  N   PRO B 313      17.416 -27.897  78.284  1.00 44.79           N  
ANISOU 4313  N   PRO B 313     6225   4654   6140    416   -257    929       N  
ATOM   4314  CA  PRO B 313      16.568 -28.959  78.857  1.00 41.76           C  
ANISOU 4314  CA  PRO B 313     5647   4287   5932    262   -298    858       C  
ATOM   4315  C   PRO B 313      17.167 -29.659  80.066  1.00 47.64           C  
ANISOU 4315  C   PRO B 313     6350   5001   6752    175    -57    884       C  
ATOM   4316  O   PRO B 313      16.474 -29.835  81.077  1.00 52.34           O  
ANISOU 4316  O   PRO B 313     6725   5639   7525     97     13    888       O  
ATOM   4317  CB  PRO B 313      16.380 -29.914  77.669  1.00 40.81           C  
ANISOU 4317  CB  PRO B 313     5699   4107   5698    199   -492    761       C  
ATOM   4318  CG  PRO B 313      16.518 -29.035  76.471  1.00 48.66           C  
ANISOU 4318  CG  PRO B 313     6898   5110   6481    349   -644    785       C  
ATOM   4319  CD  PRO B 313      17.608 -28.070  76.834  1.00 47.97           C  
ANISOU 4319  CD  PRO B 313     6903   5006   6317    459   -410    900       C  
ATOM   4320  N   ILE B 314      18.435 -30.065  80.003  1.00 43.97           N  
ANISOU 4320  N   ILE B 314     6092   4459   6155    196     78    904       N  
ATOM   4321  CA  ILE B 314      19.025 -30.762  81.144  1.00 46.57           C  
ANISOU 4321  CA  ILE B 314     6401   4752   6541    144    265    935       C  
ATOM   4322  C   ILE B 314      19.183 -29.818  82.330  1.00 50.16           C  
ANISOU 4322  C   ILE B 314     6712   5288   7058    212    401    999       C  
ATOM   4323  O   ILE B 314      18.950 -30.202  83.483  1.00 51.94           O  
ANISOU 4323  O   ILE B 314     6837   5532   7367    155    508   1027       O  
ATOM   4324  CB  ILE B 314      20.365 -31.407  80.753  1.00 49.28           C  
ANISOU 4324  CB  ILE B 314     6976   4992   6757    177    352    923       C  
ATOM   4325  CG1 ILE B 314      20.799 -32.399  81.831  1.00 46.69           C  
ANISOU 4325  CG1 ILE B 314     6646   4602   6494    125    482    951       C  
ATOM   4326  CG2 ILE B 314      21.430 -30.340  80.538  1.00 43.82           C  
ANISOU 4326  CG2 ILE B 314     6360   4316   5973    313    445    953       C  
ATOM   4327  CD1 ILE B 314      19.788 -33.502  82.099  1.00 43.28           C  
ANISOU 4327  CD1 ILE B 314     6153   4115   6177    -33    441    933       C  
ATOM   4328  N   SER B 315      19.585 -28.572  82.072  1.00 43.16           N  
ANISOU 4328  N   SER B 315     5839   4439   6122    333    409   1020       N  
ATOM   4329  CA  SER B 315      19.759 -27.610  83.156  1.00 48.95           C  
ANISOU 4329  CA  SER B 315     6445   5236   6916    399    527   1051       C  
ATOM   4330  C   SER B 315      18.448 -27.367  83.891  1.00 53.16           C  
ANISOU 4330  C   SER B 315     6748   5855   7596    357    514   1047       C  
ATOM   4331  O   SER B 315      18.409 -27.344  85.128  1.00 62.49           O  
ANISOU 4331  O   SER B 315     7837   7081   8824    344    648   1060       O  
ATOM   4332  CB  SER B 315      20.317 -26.298  82.602  1.00 50.40           C  
ANISOU 4332  CB  SER B 315     6687   5411   7053    520    534   1066       C  
ATOM   4333  OG  SER B 315      21.688 -26.428  82.274  1.00 43.03           O  
ANISOU 4333  OG  SER B 315     5917   4404   6027    553    629   1061       O  
ATOM   4334  N   VAL B 316      17.358 -27.182  83.143  1.00 48.44           N  
ANISOU 4334  N   VAL B 316     6056   5281   7069    345    351   1020       N  
ATOM   4335  CA  VAL B 316      16.055 -26.988  83.773  1.00 48.09           C  
ANISOU 4335  CA  VAL B 316     5747   5314   7211    303    346    994       C  
ATOM   4336  C   VAL B 316      15.624 -28.247  84.513  1.00 47.43           C  
ANISOU 4336  C   VAL B 316     5595   5218   7209    138    446    985       C  
ATOM   4337  O   VAL B 316      15.111 -28.180  85.637  1.00 54.45           O  
ANISOU 4337  O   VAL B 316     6329   6160   8200     98    602    993       O  
ATOM   4338  CB  VAL B 316      15.006 -26.566  82.729  1.00 45.78           C  
ANISOU 4338  CB  VAL B 316     5349   5045   7000    341    105    951       C  
ATOM   4339  CG1 VAL B 316      13.614 -26.611  83.338  1.00 46.02           C  
ANISOU 4339  CG1 VAL B 316     5058   5149   7279    273    102    896       C  
ATOM   4340  CG2 VAL B 316      15.317 -25.181  82.195  1.00 41.16           C  
ANISOU 4340  CG2 VAL B 316     4836   4456   6348    519     40    990       C  
ATOM   4341  N   LEU B 317      15.808 -29.415  83.890  1.00 48.09           N  
ANISOU 4341  N   LEU B 317     5811   5216   7246     39    377    967       N  
ATOM   4342  CA  LEU B 317      15.398 -30.662  84.529  1.00 55.47           C  
ANISOU 4342  CA  LEU B 317     6707   6097   8273   -130    482    968       C  
ATOM   4343  C   LEU B 317      16.167 -30.906  85.822  1.00 53.93           C  
ANISOU 4343  C   LEU B 317     6606   5887   7996   -119    712   1053       C  
ATOM   4344  O   LEU B 317      15.605 -31.409  86.802  1.00 55.45           O  
ANISOU 4344  O   LEU B 317     6717   6078   8274   -222    870   1086       O  
ATOM   4345  CB  LEU B 317      15.605 -31.835  83.571  1.00 58.66           C  
ANISOU 4345  CB  LEU B 317     7273   6381   8633   -222    362    921       C  
ATOM   4346  CG  LEU B 317      14.601 -32.021  82.434  1.00 53.99           C  
ANISOU 4346  CG  LEU B 317     6582   5790   8141   -289    115    810       C  
ATOM   4347  CD1 LEU B 317      15.002 -33.206  81.572  1.00 53.67           C  
ANISOU 4347  CD1 LEU B 317     6755   5618   8020   -373     22    748       C  
ATOM   4348  CD2 LEU B 317      13.202 -32.208  82.992  1.00 52.92           C  
ANISOU 4348  CD2 LEU B 317     6132   5696   8279   -428    137    762       C  
ATOM   4349  N   ASN B 318      17.454 -30.550  85.851  1.00 55.81           N  
ANISOU 4349  N   ASN B 318     7020   6113   8071      8    736   1085       N  
ATOM   4350  CA  ASN B 318      18.234 -30.738  87.071  1.00 54.00           C  
ANISOU 4350  CA  ASN B 318     6883   5880   7753     48    900   1150       C  
ATOM   4351  C   ASN B 318      17.782 -29.790  88.178  1.00 52.96           C  
ANISOU 4351  C   ASN B 318     6606   5865   7650     94   1021   1159       C  
ATOM   4352  O   ASN B 318      17.784 -30.161  89.358  1.00 57.71           O  
ANISOU 4352  O   ASN B 318     7245   6477   8205     69   1175   1211       O  
ATOM   4353  CB  ASN B 318      19.723 -30.560  86.776  1.00 58.77           C  
ANISOU 4353  CB  ASN B 318     7662   6446   8222    173    872   1150       C  
ATOM   4354  CG  ASN B 318      20.369 -31.829  86.245  1.00 57.78           C  
ANISOU 4354  CG  ASN B 318     7718   6186   8051    134    840   1154       C  
ATOM   4355  OD1 ASN B 318      20.043 -32.932  86.682  1.00 63.11           O  
ANISOU 4355  OD1 ASN B 318     8443   6781   8755     36    893   1195       O  
ATOM   4356  ND2 ASN B 318      21.294 -31.676  85.303  1.00 52.75           N  
ANISOU 4356  ND2 ASN B 318     7189   5506   7349    211    778   1112       N  
ATOM   4357  N   VAL B 319      17.395 -28.562  87.821  1.00 50.01           N  
ANISOU 4357  N   VAL B 319     6091   5570   7339    171    959   1109       N  
ATOM   4358  CA  VAL B 319      16.928 -27.617  88.831  1.00 50.69           C  
ANISOU 4358  CA  VAL B 319     6035   5756   7469    224   1081   1092       C  
ATOM   4359  C   VAL B 319      15.584 -28.053  89.400  1.00 56.55           C  
ANISOU 4359  C   VAL B 319     6597   6533   8358     98   1197   1090       C  
ATOM   4360  O   VAL B 319      15.368 -28.012  90.617  1.00 62.70           O  
ANISOU 4360  O   VAL B 319     7356   7361   9107     86   1393   1109       O  
ATOM   4361  CB  VAL B 319      16.854 -26.196  88.243  1.00 45.79           C  
ANISOU 4361  CB  VAL B 319     5318   5175   6904    349    984   1041       C  
ATOM   4362  CG1 VAL B 319      16.051 -25.283  89.161  1.00 42.61           C  
ANISOU 4362  CG1 VAL B 319     4726   4862   6602    393   1104    998       C  
ATOM   4363  CG2 VAL B 319      18.251 -25.639  88.017  1.00 33.67           C  
ANISOU 4363  CG2 VAL B 319     3948   3602   5243    459    956   1040       C  
ATOM   4364  N   LEU B 320      14.661 -28.478  88.534  1.00 57.94           N  
ANISOU 4364  N   LEU B 320     6637   6683   8695      0   1084   1055       N  
ATOM   4365  CA  LEU B 320      13.357 -28.925  89.014  1.00 58.90           C  
ANISOU 4365  CA  LEU B 320     6539   6827   9015   -143   1205   1031       C  
ATOM   4366  C   LEU B 320      13.490 -30.157  89.899  1.00 55.40           C  
ANISOU 4366  C   LEU B 320     6233   6308   8508   -282   1412   1113       C  
ATOM   4367  O   LEU B 320      12.765 -30.303  90.890  1.00 60.94           O  
ANISOU 4367  O   LEU B 320     6831   7039   9285   -367   1645   1130       O  
ATOM   4368  CB  LEU B 320      12.433 -29.214  87.831  1.00 65.45           C  
ANISOU 4368  CB  LEU B 320     7192   7633  10043   -224    994    953       C  
ATOM   4369  CG  LEU B 320      12.174 -28.048  86.878  1.00 67.70           C  
ANISOU 4369  CG  LEU B 320     7363   7977  10382    -73    759    890       C  
ATOM   4370  CD1 LEU B 320      11.391 -28.513  85.660  1.00 69.13           C  
ANISOU 4370  CD1 LEU B 320     7431   8131  10705   -144    497    810       C  
ATOM   4371  CD2 LEU B 320      11.450 -26.924  87.597  1.00 63.17           C  
ANISOU 4371  CD2 LEU B 320     6547   7503   9952     17    869    851       C  
ATOM   4372  N   LYS B 321      14.407 -31.060  89.551  1.00 55.00           N  
ANISOU 4372  N   LYS B 321     6429   6147   8321   -302   1345   1168       N  
ATOM   4373  CA  LYS B 321      14.608 -32.275  90.332  1.00 57.15           C  
ANISOU 4373  CA  LYS B 321     6875   6313   8526   -412   1519   1265       C  
ATOM   4374  C   LYS B 321      15.383 -31.998  91.616  1.00 60.48           C  
ANISOU 4374  C   LYS B 321     7475   6778   8725   -298   1679   1350       C  
ATOM   4375  O   LYS B 321      14.960 -32.398  92.706  1.00 64.19           O  
ANISOU 4375  O   LYS B 321     7987   7240   9163   -371   1913   1423       O  
ATOM   4376  CB  LYS B 321      15.324 -33.322  89.473  1.00 59.08           C  
ANISOU 4376  CB  LYS B 321     7319   6408   8720   -448   1376   1280       C  
ATOM   4377  CG  LYS B 321      15.755 -34.585  90.204  1.00 66.30           C  
ANISOU 4377  CG  LYS B 321     8470   7175   9548   -519   1524   1397       C  
ATOM   4378  CD  LYS B 321      16.771 -35.357  89.370  1.00 71.30           C  
ANISOU 4378  CD  LYS B 321     9316   7672  10103   -478   1368   1393       C  
ATOM   4379  CE  LYS B 321      17.304 -36.586  90.093  1.00 77.06           C  
ANISOU 4379  CE  LYS B 321    10277   8311  10691   -486   1409   1442       C  
ATOM   4380  NZ  LYS B 321      18.352 -37.270  89.281  1.00 77.27           N  
ANISOU 4380  NZ  LYS B 321    10477   8230  10651   -417   1248   1404       N  
ATOM   4381  N   ARG B 322      16.523 -31.314  91.508  1.00 59.37           N  
ANISOU 4381  N   ARG B 322     7449   6681   8427   -121   1559   1334       N  
ATOM   4382  CA  ARG B 322      17.417 -31.181  92.653  1.00 52.31           C  
ANISOU 4382  CA  ARG B 322     6745   5818   7314     -4   1646   1392       C  
ATOM   4383  C   ARG B 322      17.002 -30.060  93.599  1.00 57.53           C  
ANISOU 4383  C   ARG B 322     7299   6620   7940     65   1777   1347       C  
ATOM   4384  O   ARG B 322      17.162 -30.188  94.818  1.00 61.03           O  
ANISOU 4384  O   ARG B 322     7885   7092   8211     97   1930   1402       O  
ATOM   4385  CB  ARG B 322      18.846 -30.951  92.168  1.00 47.34           C  
ANISOU 4385  CB  ARG B 322     6248   5166   6574    145   1466   1365       C  
ATOM   4386  CG  ARG B 322      19.443 -32.140  91.448  1.00 47.68           C  
ANISOU 4386  CG  ARG B 322     6441   5062   6612    108   1369   1402       C  
ATOM   4387  CD  ARG B 322      19.866 -33.197  92.453  1.00 55.51           C  
ANISOU 4387  CD  ARG B 322     7630   6011   7450    113   1402   1451       C  
ATOM   4388  NE  ARG B 322      20.235 -34.462  91.825  1.00 77.09           N  
ANISOU 4388  NE  ARG B 322    10478   8613  10201     60   1304   1448       N  
ATOM   4389  CZ  ARG B 322      20.648 -35.529  92.500  1.00 85.51           C  
ANISOU 4389  CZ  ARG B 322    11722   9605  11164     67   1305   1502       C  
ATOM   4390  NH1 ARG B 322      20.745 -35.479  93.822  1.00 82.28           N  
ANISOU 4390  NH1 ARG B 322    11416   9244  10603    127   1390   1570       N  
ATOM   4391  NH2 ARG B 322      20.967 -36.645  91.859  1.00 91.75           N  
ANISOU 4391  NH2 ARG B 322    12602  10262  11995     23   1221   1493       N  
ATOM   4392  N   VAL B 323      16.480 -28.959  93.071  1.00 59.01           N  
ANISOU 4392  N   VAL B 323     7261   6888   8271    102   1718   1245       N  
ATOM   4393  CA  VAL B 323      16.169 -27.792  93.885  1.00 59.89           C  
ANISOU 4393  CA  VAL B 323     7271   7119   8366    190   1829   1176       C  
ATOM   4394  C   VAL B 323      14.699 -27.744  94.279  1.00 61.34           C  
ANISOU 4394  C   VAL B 323     7235   7350   8721     82   2028   1154       C  
ATOM   4395  O   VAL B 323      14.368 -27.312  95.383  1.00 65.84           O  
ANISOU 4395  O   VAL B 323     7800   7997   9221    111   2235   1132       O  
ATOM   4396  CB  VAL B 323      16.586 -26.507  93.143  1.00 59.13           C  
ANISOU 4396  CB  VAL B 323     7077   7056   8333    322   1658   1079       C  
ATOM   4397  CG1 VAL B 323      16.336 -25.295  94.018  1.00 55.88           C  
ANISOU 4397  CG1 VAL B 323     6578   6741   7911    421   1773    991       C  
ATOM   4398  CG2 VAL B 323      18.047 -26.589  92.736  1.00 48.65           C  
ANISOU 4398  CG2 VAL B 323     5937   5673   6875    407   1503   1090       C  
ATOM   4399  N   PHE B 324      13.805 -28.172  93.392  1.00 62.26           N  
ANISOU 4399  N   PHE B 324     7160   7424   9071    -40   1969   1139       N  
ATOM   4400  CA  PHE B 324      12.375 -28.100  93.649  1.00 59.53           C  
ANISOU 4400  CA  PHE B 324     6536   7122   8961   -146   2140   1089       C  
ATOM   4401  C   PHE B 324      11.755 -29.453  93.984  1.00 61.93           C  
ANISOU 4401  C   PHE B 324     6861   7342   9330   -359   2319   1161       C  
ATOM   4402  O   PHE B 324      10.533 -29.540  94.136  1.00 72.58           O  
ANISOU 4402  O   PHE B 324     7976   8716  10885   -468   2422   1086       O  
ATOM   4403  CB  PHE B 324      11.671 -27.460  92.448  1.00 61.07           C  
ANISOU 4403  CB  PHE B 324     6447   7340   9418   -118   1919    987       C  
ATOM   4404  CG  PHE B 324      12.026 -26.009  92.242  1.00 63.42           C  
ANISOU 4404  CG  PHE B 324     6703   7702   9692     85   1799    918       C  
ATOM   4405  CD1 PHE B 324      11.367 -25.016  92.948  1.00 65.36           C  
ANISOU 4405  CD1 PHE B 324     6765   8032  10038    164   1953    837       C  
ATOM   4406  CD2 PHE B 324      13.026 -25.641  91.354  1.00 65.81           C  
ANISOU 4406  CD2 PHE B 324     7159   7962   9883    193   1560    932       C  
ATOM   4407  CE1 PHE B 324      11.692 -23.681  92.769  1.00 62.97           C  
ANISOU 4407  CE1 PHE B 324     6437   7755   9733    349   1851    771       C  
ATOM   4408  CE2 PHE B 324      13.356 -24.307  91.170  1.00 61.92           C  
ANISOU 4408  CE2 PHE B 324     6644   7497   9388    363   1477    878       C  
ATOM   4409  CZ  PHE B 324      12.687 -23.327  91.880  1.00 61.83           C  
ANISOU 4409  CZ  PHE B 324     6454   7553   9484    442   1613    798       C  
ATOM   4410  N   GLY B 325      12.563 -30.507  94.101  1.00 62.96           N  
ANISOU 4410  N   GLY B 325     7287   7366   9268   -400   2293   1265       N  
ATOM   4411  CA  GLY B 325      12.056 -31.798  94.548  1.00 57.91           C  
ANISOU 4411  CA  GLY B 325     6740   6634   8627   -574   2412   1308       C  
ATOM   4412  C   GLY B 325      11.006 -32.421  93.656  1.00 60.35           C  
ANISOU 4412  C   GLY B 325     6794   6870   9265   -769   2377   1252       C  
ATOM   4413  O   GLY B 325      10.135 -33.145  94.152  1.00 72.13           O  
ANISOU 4413  O   GLY B 325     8236   8325  10846   -926   2538   1240       O  
ATOM   4414  N   MET B 326      11.047 -32.147  92.355  1.00 65.64           N  
ANISOU 4414  N   MET B 326     7296   7515  10129   -767   2167   1212       N  
ATOM   4415  CA  MET B 326      10.082 -32.701  91.415  1.00 66.39           C  
ANISOU 4415  CA  MET B 326     7139   7548  10536   -939   2051   1118       C  
ATOM   4416  C   MET B 326      10.487 -34.104  90.954  1.00 73.66           C  
ANISOU 4416  C   MET B 326     8273   8280  11433  -1082   1992   1173       C  
ATOM   4417  O   MET B 326      11.587 -34.593  91.226  1.00 74.68           O  
ANISOU 4417  O   MET B 326     8745   8334  11296  -1009   1993   1279       O  
ATOM   4418  CB  MET B 326       9.915 -31.774  90.209  1.00 70.05           C  
ANISOU 4418  CB  MET B 326     7411   8102  11102   -812   1712    988       C  
ATOM   4419  CG  MET B 326       9.166 -30.484  90.506  1.00 81.59           C  
ANISOU 4419  CG  MET B 326     8580   9715  12707   -701   1754    905       C  
ATOM   4420  SD  MET B 326       8.670 -29.624  88.998  1.00 91.28           S  
ANISOU 4420  SD  MET B 326     9564  11006  14113   -579   1337    765       S  
ATOM   4421  CE  MET B 326       8.267 -27.998  89.629  1.00 98.53           C  
ANISOU 4421  CE  MET B 326    10272  12068  15099   -376   1433    716       C  
ATOM   4422  N   PHE B 327       9.561 -34.750  90.241  1.00 84.96           N  
ANISOU 4422  N   PHE B 327     9487   9636  13159  -1274   1914   1072       N  
ATOM   4423  CA  PHE B 327       9.765 -36.064  89.623  1.00 88.43           C  
ANISOU 4423  CA  PHE B 327    10081   9878  13641  -1429   1827   1074       C  
ATOM   4424  C   PHE B 327      10.060 -37.164  90.642  1.00 90.46           C  
ANISOU 4424  C   PHE B 327    10645  10037  13691  -1486   2035   1182       C  
ATOM   4425  O   PHE B 327      10.797 -38.109  90.347  1.00 93.63           O  
ANISOU 4425  O   PHE B 327    11316  10287  13974  -1502   1959   1231       O  
ATOM   4426  CB  PHE B 327      10.885 -36.035  88.579  1.00 85.19           C  
ANISOU 4426  CB  PHE B 327     9909   9445  13014  -1271   1512   1055       C  
ATOM   4427  CG  PHE B 327      10.978 -34.751  87.804  1.00 80.60           C  
ANISOU 4427  CG  PHE B 327     9205   9034  12384  -1075   1252    965       C  
ATOM   4428  CD1 PHE B 327       9.945 -34.341  86.978  1.00 79.00           C  
ANISOU 4428  CD1 PHE B 327     8692   8905  12421  -1112   1046    813       C  
ATOM   4429  CD2 PHE B 327      12.121 -33.972  87.875  1.00 78.05           C  
ANISOU 4429  CD2 PHE B 327     9087   8783  11785   -851   1202   1031       C  
ATOM   4430  CE1 PHE B 327      10.043 -33.167  86.254  1.00 78.64           C  
ANISOU 4430  CE1 PHE B 327     8580   8991  12310   -914    803    756       C  
ATOM   4431  CE2 PHE B 327      12.226 -32.799  87.154  1.00 74.11           C  
ANISOU 4431  CE2 PHE B 327     8508   8407  11245   -680    992    966       C  
ATOM   4432  CZ  PHE B 327      11.185 -32.395  86.342  1.00 73.12           C  
ANISOU 4432  CZ  PHE B 327     8111   8342  11329   -705    794    842       C  
ATOM   4433  N   ARG B 328       9.499 -37.069  91.846  1.00 92.28           N  
ANISOU 4433  N   ARG B 328    10848  10347  13868  -1503   2283   1217       N  
ATOM   4434  CA  ARG B 328       9.666 -38.145  92.817  1.00102.84           C  
ANISOU 4434  CA  ARG B 328    12464  11581  15028  -1566   2464   1330       C  
ATOM   4435  C   ARG B 328       8.624 -39.243  92.667  1.00114.23           C  
ANISOU 4435  C   ARG B 328    13778  12890  16734  -1824   2553   1276       C  
ATOM   4436  O   ARG B 328       8.898 -40.398  93.010  1.00117.98           O  
ANISOU 4436  O   ARG B 328    14503  13209  17116  -1898   2621   1367       O  
ATOM   4437  CB  ARG B 328       9.617 -37.589  94.243  1.00106.21           C  
ANISOU 4437  CB  ARG B 328    12975  12133  15245  -1465   2696   1405       C  
ATOM   4438  CG  ARG B 328      10.887 -36.879  94.675  1.00105.45           C  
ANISOU 4438  CG  ARG B 328    13124  12123  14818  -1217   2619   1481       C  
ATOM   4439  CD  ARG B 328      10.632 -35.994  95.883  1.00112.54           C  
ANISOU 4439  CD  ARG B 328    14012  13174  15575  -1122   2815   1491       C  
ATOM   4440  NE  ARG B 328      11.830 -35.272  96.300  1.00111.32           N  
ANISOU 4440  NE  ARG B 328    14071  13102  15125   -892   2725   1537       N  
ATOM   4441  CZ  ARG B 328      11.822 -34.245  97.143  1.00109.12           C  
ANISOU 4441  CZ  ARG B 328    13781  12965  14713   -771   2831   1514       C  
ATOM   4442  NH1 ARG B 328      12.957 -33.642  97.472  1.00108.02           N  
ANISOU 4442  NH1 ARG B 328    13832  12886  14326   -573   2728   1540       N  
ATOM   4443  NH2 ARG B 328      10.677 -33.821  97.660  1.00106.75           N  
ANISOU 4443  NH2 ARG B 328    13273  12744  14542   -848   3038   1447       N  
ATOM   4444  N   GLN B 329       7.442 -38.907  92.161  1.00119.34           N  
ANISOU 4444  N   GLN B 329    14029  13592  17722  -1954   2538   1121       N  
ATOM   4445  CA  GLN B 329       6.376 -39.887  92.010  1.00123.17           C  
ANISOU 4445  CA  GLN B 329    14345  13960  18495  -2207   2616   1040       C  
ATOM   4446  C   GLN B 329       6.735 -40.916  90.946  1.00121.75           C  
ANISOU 4446  C   GLN B 329    14272  13585  18400  -2319   2401    994       C  
ATOM   4447  O   GLN B 329       7.312 -40.584  89.907  1.00121.02           O  
ANISOU 4447  O   GLN B 329    14183  13490  18311  -2242   2134    931       O  
ATOM   4448  CB  GLN B 329       5.064 -39.193  91.651  1.00128.32           C  
ANISOU 4448  CB  GLN B 329    14511  14738  19508  -2285   2590    852       C  
ATOM   4449  CG  GLN B 329       4.491 -38.333  92.769  1.00134.72           C  
ANISOU 4449  CG  GLN B 329    15197  15712  20279  -2206   2847    871       C  
ATOM   4450  CD  GLN B 329       5.340 -37.108  93.043  1.00138.33           C  
ANISOU 4450  CD  GLN B 329    15769  16320  20472  -1945   2800    934       C  
ATOM   4451  OE1 GLN B 329       5.737 -36.852  94.179  1.00142.05           O  
ANISOU 4451  OE1 GLN B 329    16465  16842  20664  -1841   3006   1051       O  
ATOM   4452  NE2 GLN B 329       5.632 -36.347  91.994  1.00137.39           N  
ANISOU 4452  NE2 GLN B 329    15499  16263  20440  -1838   2518    853       N  
ATOM   4453  N   ALA B 330       6.401 -42.177  91.215  1.00124.27           N  
ANISOU 4453  N   ALA B 330    14698  13729  18791  -2502   2527   1024       N  
ATOM   4454  CA  ALA B 330       6.721 -43.254  90.288  1.00124.64           C  
ANISOU 4454  CA  ALA B 330    14875  13567  18914  -2616   2345    971       C  
ATOM   4455  C   ALA B 330       5.676 -43.418  89.192  1.00123.69           C  
ANISOU 4455  C   ALA B 330    14384  13418  19194  -2815   2159    727       C  
ATOM   4456  O   ALA B 330       5.837 -44.289  88.331  1.00119.10           O  
ANISOU 4456  O   ALA B 330    13888  12663  18702  -2925   1983    638       O  
ATOM   4457  CB  ALA B 330       6.880 -44.576  91.049  1.00127.91           C  
ANISOU 4457  CB  ALA B 330    15584  13782  19233  -2712   2544   1115       C  
ATOM   4458  N   SER B 331       4.614 -42.609  89.202  1.00124.98           N  
ANISOU 4458  N   SER B 331    14138  13749  19599  -2850   2172    601       N  
ATOM   4459  CA  SER B 331       3.602 -42.683  88.153  1.00124.91           C  
ANISOU 4459  CA  SER B 331    13742  13745  19974  -3006   1933    344       C  
ATOM   4460  C   SER B 331       4.097 -42.059  86.850  1.00121.00           C  
ANISOU 4460  C   SER B 331    13192  13300  19484  -2892   1527    215       C  
ATOM   4461  O   SER B 331       3.949 -42.651  85.776  1.00120.60           O  
ANISOU 4461  O   SER B 331    13097  13140  19586  -3006   1251     40       O  
ATOM   4462  CB  SER B 331       2.315 -42.007  88.623  1.00125.22           C  
ANISOU 4462  CB  SER B 331    13355  13953  20272  -3044   2061    247       C  
ATOM   4463  OG  SER B 331       2.521 -40.621  88.837  1.00121.56           O  
ANISOU 4463  OG  SER B 331    12791  13699  19695  -2817   2036    280       O  
ATOM   4464  N   ASP B 332       4.688 -40.863  86.928  1.00116.67           N  
ANISOU 4464  N   ASP B 332    12658  12906  18764  -2664   1478    293       N  
ATOM   4465  CA  ASP B 332       5.262 -40.194  85.765  1.00112.49           C  
ANISOU 4465  CA  ASP B 332    12113  12413  18216  -2535   1109    209       C  
ATOM   4466  C   ASP B 332       6.664 -40.684  85.457  1.00102.72           C  
ANISOU 4466  C   ASP B 332    11328  11012  16690  -2460   1064    328       C  
ATOM   4467  O   ASP B 332       7.411 -40.019  84.728  1.00 95.73           O  
ANISOU 4467  O   ASP B 332    10581  10218  15575  -2244    803    320       O  
ATOM   4468  CB  ASP B 332       5.278 -38.678  85.978  1.00117.24           C  
ANISOU 4468  CB  ASP B 332    12525  13236  18784  -2320   1083    251       C  
ATOM   4469  CG  ASP B 332       5.997 -38.272  87.252  1.00121.76           C  
ANISOU 4469  CG  ASP B 332    13352  13866  19047  -2175   1429    486       C  
ATOM   4470  OD1 ASP B 332       6.254 -39.153  88.099  1.00124.48           O  
ANISOU 4470  OD1 ASP B 332    13965  14106  19227  -2245   1690    609       O  
ATOM   4471  OD2 ASP B 332       6.302 -37.069  87.405  1.00121.63           O  
ANISOU 4471  OD2 ASP B 332    13273  14001  18940  -1978   1410    539       O  
ATOM   4472  N   ARG B 333       7.016 -41.843  86.016  1.00103.17           N  
ANISOU 4472  N   ARG B 333    11685  10902  16614  -2548   1274    433       N  
ATOM   4473  CA  ARG B 333       8.353 -42.404  85.872  1.00100.43           C  
ANISOU 4473  CA  ARG B 333    11781  10401  15976  -2445   1258    551       C  
ATOM   4474  C   ARG B 333       8.802 -42.443  84.415  1.00 93.95           C  
ANISOU 4474  C   ARG B 333    11022   9493  15181  -2421    897    389       C  
ATOM   4475  O   ARG B 333       9.901 -41.987  84.080  1.00 90.81           O  
ANISOU 4475  O   ARG B 333    10887   9171  14447  -2172    776    453       O  
ATOM   4476  CB  ARG B 333       8.362 -43.804  86.483  1.00112.28           C  
ANISOU 4476  CB  ARG B 333    13515  11717  17430  -2577   1454    630       C  
ATOM   4477  CG  ARG B 333       9.720 -44.430  86.696  1.00118.10           C  
ANISOU 4477  CG  ARG B 333    14705  12320  17847  -2430   1484    787       C  
ATOM   4478  CD  ARG B 333       9.541 -45.731  87.463  1.00127.84           C  
ANISOU 4478  CD  ARG B 333    16108  13384  19080  -2557   1681    885       C  
ATOM   4479  NE  ARG B 333      10.696 -46.617  87.379  1.00131.72           N  
ANISOU 4479  NE  ARG B 333    16986  13699  19364  -2449   1629    974       N  
ATOM   4480  CZ  ARG B 333      11.674 -46.660  88.277  1.00133.10           C  
ANISOU 4480  CZ  ARG B 333    17429  13897  19247  -2245   1724   1174       C  
ATOM   4481  NH1 ARG B 333      11.645 -45.858  89.333  1.00133.20           N  
ANISOU 4481  NH1 ARG B 333    17400  14096  19113  -2138   1882   1301       N  
ATOM   4482  NH2 ARG B 333      12.682 -47.506  88.118  1.00132.82           N  
ANISOU 4482  NH2 ARG B 333    17690  13701  19075  -2140   1644   1226       N  
ATOM   4483  N   GLU B 334       7.960 -42.978  83.528  1.00 95.75           N  
ANISOU 4483  N   GLU B 334    11051   9645  15686  -2614    677    152       N  
ATOM   4484  CA  GLU B 334       8.391 -43.180  82.147  1.00 95.85           C  
ANISOU 4484  CA  GLU B 334    11229   9635  15553  -2534    296    -27       C  
ATOM   4485  C   GLU B 334       8.618 -41.857  81.424  1.00 91.14           C  
ANISOU 4485  C   GLU B 334    10596   9316  14718  -2259      1    -66       C  
ATOM   4486  O   GLU B 334       9.595 -41.711  80.681  1.00 88.24           O  
ANISOU 4486  O   GLU B 334    10533   8964  14031  -2070   -163    -67       O  
ATOM   4487  CB  GLU B 334       7.352 -44.018  81.400  1.00104.48           C  
ANISOU 4487  CB  GLU B 334    12101  10593  17004  -2810    100   -299       C  
ATOM   4488  CG  GLU B 334       7.273 -45.464  81.854  1.00117.32           C  
ANISOU 4488  CG  GLU B 334    13892  11976  18709  -3017    339   -271       C  
ATOM   4489  CD  GLU B 334       8.580 -46.209  81.679  1.00126.44           C  
ANISOU 4489  CD  GLU B 334    15525  12922  19592  -2921    383   -180       C  
ATOM   4490  OE1 GLU B 334       9.338 -45.874  80.747  1.00129.02           O  
ANISOU 4490  OE1 GLU B 334    16027  13253  19743  -2765    136   -263       O  
ATOM   4491  OE2 GLU B 334       8.849 -47.133  82.475  1.00131.02           O  
ANISOU 4491  OE2 GLU B 334    16321  13365  20094  -2965    645    -21       O  
ATOM   4492  N   ALA B 335       7.729 -40.882  81.626  1.00 89.24           N  
ANISOU 4492  N   ALA B 335     9991   9280  14637  -2229    -51    -97       N  
ATOM   4493  CA  ALA B 335       7.913 -39.578  80.998  1.00 83.09           C  
ANISOU 4493  CA  ALA B 335     9191   8737  13641  -1958   -314   -110       C  
ATOM   4494  C   ALA B 335       9.133 -38.853  81.553  1.00 83.67           C  
ANISOU 4494  C   ALA B 335     9542   8887  13363  -1715   -131    118       C  
ATOM   4495  O   ALA B 335       9.821 -38.131  80.820  1.00 84.44           O  
ANISOU 4495  O   ALA B 335     9820   9083  13179  -1493   -324    127       O  
ATOM   4496  CB  ALA B 335       6.658 -38.728  81.182  1.00 74.69           C  
ANISOU 4496  CB  ALA B 335     7658   7850  12870  -1971   -394   -193       C  
ATOM   4497  N   VAL B 336       9.411 -39.025  82.846  1.00 83.79           N  
ANISOU 4497  N   VAL B 336     9597   8852  13388  -1755    241    299       N  
ATOM   4498  CA  VAL B 336      10.541 -38.334  83.459  1.00 79.88           C  
ANISOU 4498  CA  VAL B 336     9333   8433  12585  -1531    395    491       C  
ATOM   4499  C   VAL B 336      11.862 -38.862  82.915  1.00 74.85           C  
ANISOU 4499  C   VAL B 336     9092   7679  11669  -1427    336    525       C  
ATOM   4500  O   VAL B 336      12.745 -38.087  82.530  1.00 72.54           O  
ANISOU 4500  O   VAL B 336     8957   7485  11121  -1208    246    565       O  
ATOM   4501  CB  VAL B 336      10.475 -38.468  84.990  1.00 80.26           C  
ANISOU 4501  CB  VAL B 336     9353   8453  12690  -1598    784    662       C  
ATOM   4502  CG1 VAL B 336      11.752 -37.942  85.624  1.00 79.42           C  
ANISOU 4502  CG1 VAL B 336     9518   8399  12258  -1375    908    835       C  
ATOM   4503  CG2 VAL B 336       9.257 -37.742  85.533  1.00 81.32           C  
ANISOU 4503  CG2 VAL B 336     9090   8732  13078  -1660    876    622       C  
ATOM   4504  N   TYR B 337      12.019 -40.186  82.868  1.00 75.36           N  
ANISOU 4504  N   TYR B 337     9316   7516  11800  -1584    402    502       N  
ATOM   4505  CA  TYR B 337      13.251 -40.746  82.320  1.00 84.23           C  
ANISOU 4505  CA  TYR B 337    10798   8513  12692  -1478    354    511       C  
ATOM   4506  C   TYR B 337      13.386 -40.458  80.831  1.00 80.98           C  
ANISOU 4506  C   TYR B 337    10458   8160  12149  -1390     31    336       C  
ATOM   4507  O   TYR B 337      14.496 -40.229  80.339  1.00 82.05           O  
ANISOU 4507  O   TYR B 337    10844   8306  12024  -1208     -5    360       O  
ATOM   4508  CB  TYR B 337      13.333 -42.242  82.612  1.00 99.54           C  
ANISOU 4508  CB  TYR B 337    12896  10167  14756  -1658    499    521       C  
ATOM   4509  CG  TYR B 337      13.577 -42.510  84.076  1.00113.67           C  
ANISOU 4509  CG  TYR B 337    14753  11883  16552  -1674    830    745       C  
ATOM   4510  CD1 TYR B 337      14.018 -41.494  84.913  1.00118.06           C  
ANISOU 4510  CD1 TYR B 337    15294  12623  16940  -1492    945    898       C  
ATOM   4511  CD2 TYR B 337      13.388 -43.772  84.619  1.00121.97           C  
ANISOU 4511  CD2 TYR B 337    15914  12701  17728  -1846   1004    797       C  
ATOM   4512  CE1 TYR B 337      14.246 -41.719  86.253  1.00119.95           C  
ANISOU 4512  CE1 TYR B 337    15629  12844  17102  -1472   1197   1081       C  
ATOM   4513  CE2 TYR B 337      13.619 -44.011  85.963  1.00125.57           C  
ANISOU 4513  CE2 TYR B 337    16472  13215  18022  -1778   1211    986       C  
ATOM   4514  CZ  TYR B 337      14.048 -42.979  86.774  1.00125.88           C  
ANISOU 4514  CZ  TYR B 337    16499  13458  17871  -1591   1296   1116       C  
ATOM   4515  OH  TYR B 337      14.281 -43.200  88.112  1.00130.97           O  
ANISOU 4515  OH  TYR B 337    17257  14157  18347  -1519   1466   1274       O  
ATOM   4516  N   ALA B 338      12.277 -40.468  80.092  1.00 75.16           N  
ANISOU 4516  N   ALA B 338     9510   7463  11586  -1512   -204    154       N  
ATOM   4517  CA  ALA B 338      12.358 -40.127  78.676  1.00 64.36           C  
ANISOU 4517  CA  ALA B 338     8245   6166  10044  -1407   -533     -5       C  
ATOM   4518  C   ALA B 338      12.845 -38.695  78.486  1.00 65.87           C  
ANISOU 4518  C   ALA B 338     8468   6566   9994  -1151   -590     93       C  
ATOM   4519  O   ALA B 338      13.579 -38.402  77.536  1.00 67.66           O  
ANISOU 4519  O   ALA B 338     8945   6815   9947   -999   -718     61       O  
ATOM   4520  CB  ALA B 338      11.003 -40.332  78.001  1.00 58.69           C  
ANISOU 4520  CB  ALA B 338     7263   5468   9569  -1570   -818   -225       C  
ATOM   4521  N   ALA B 339      12.442 -37.787  79.378  1.00 64.69           N  
ANISOU 4521  N   ALA B 339     8079   6556   9944  -1104   -473    210       N  
ATOM   4522  CA  ALA B 339      12.892 -36.401  79.282  1.00 54.05           C  
ANISOU 4522  CA  ALA B 339     6757   5378   8402   -871   -504    305       C  
ATOM   4523  C   ALA B 339      14.385 -36.287  79.567  1.00 55.33           C  
ANISOU 4523  C   ALA B 339     7209   5500   8315   -727   -306    439       C  
ATOM   4524  O   ALA B 339      15.117 -35.606  78.839  1.00 59.82           O  
ANISOU 4524  O   ALA B 339     7958   6120   8650   -558   -383    452       O  
ATOM   4525  CB  ALA B 339      12.091 -35.520  80.242  1.00 40.15           C  
ANISOU 4525  CB  ALA B 339     4668   3754   6834   -861   -405    375       C  
ATOM   4526  N   PHE B 340      14.855 -36.946  80.629  1.00 51.35           N  
ANISOU 4526  N   PHE B 340     6751   4898   7862   -789    -49    540       N  
ATOM   4527  CA  PHE B 340      16.275 -36.892  80.955  1.00 52.73           C  
ANISOU 4527  CA  PHE B 340     7162   5034   7838   -645    111    648       C  
ATOM   4528  C   PHE B 340      17.115 -37.560  79.874  1.00 57.00           C  
ANISOU 4528  C   PHE B 340     7985   5454   8220   -606     29    559       C  
ATOM   4529  O   PHE B 340      18.229 -37.111  79.579  1.00 57.32           O  
ANISOU 4529  O   PHE B 340     8194   5514   8072   -445     77    595       O  
ATOM   4530  CB  PHE B 340      16.525 -37.553  82.309  1.00 58.95           C  
ANISOU 4530  CB  PHE B 340     7961   5732   8707   -708    361    772       C  
ATOM   4531  CG  PHE B 340      16.227 -36.666  83.481  1.00 63.73           C  
ANISOU 4531  CG  PHE B 340     8386   6475   9353   -665    506    885       C  
ATOM   4532  CD1 PHE B 340      14.984 -36.696  84.090  1.00 64.37           C  
ANISOU 4532  CD1 PHE B 340     8221   6591   9646   -813    573    883       C  
ATOM   4533  CD2 PHE B 340      17.188 -35.801  83.972  1.00 59.16           C  
ANISOU 4533  CD2 PHE B 340     7875   5986   8616   -482    586    973       C  
ATOM   4534  CE1 PHE B 340      14.705 -35.881  85.170  1.00 56.94           C  
ANISOU 4534  CE1 PHE B 340     7130   5775   8728   -767    731    971       C  
ATOM   4535  CE2 PHE B 340      16.917 -34.984  85.050  1.00 60.87           C  
ANISOU 4535  CE2 PHE B 340     7946   6325   8856   -439    713   1051       C  
ATOM   4536  CZ  PHE B 340      15.673 -35.024  85.651  1.00 57.40           C  
ANISOU 4536  CZ  PHE B 340     7287   5922   8599   -576    793   1052       C  
ATOM   4537  N   THR B 341      16.594 -38.627  79.265  1.00 64.46           N  
ANISOU 4537  N   THR B 341     8974   6266   9252   -758    -82    426       N  
ATOM   4538  CA  THR B 341      17.339 -39.309  78.212  1.00 64.65           C  
ANISOU 4538  CA  THR B 341     9279   6165   9120   -722   -151    314       C  
ATOM   4539  C   THR B 341      17.526 -38.403  77.001  1.00 64.51           C  
ANISOU 4539  C   THR B 341     9369   6271   8871   -582   -327    245       C  
ATOM   4540  O   THR B 341      18.639 -38.265  76.483  1.00 66.09           O  
ANISOU 4540  O   THR B 341     9801   6447   8865   -446   -254    250       O  
ATOM   4541  CB  THR B 341      16.629 -40.605  77.814  1.00 62.93           C  
ANISOU 4541  CB  THR B 341     9078   5771   9060   -928   -250    157       C  
ATOM   4542  OG1 THR B 341      16.514 -41.461  78.956  1.00 62.96           O  
ANISOU 4542  OG1 THR B 341     9026   5627   9269  -1057    -46    251       O  
ATOM   4543  CG2 THR B 341      17.409 -41.328  76.724  1.00 58.62           C  
ANISOU 4543  CG2 THR B 341     8843   5088   8343   -882   -310     18       C  
ATOM   4544  N   PHE B 342      16.441 -37.778  76.533  1.00 63.03           N  
ANISOU 4544  N   PHE B 342     9020   6209   8721   -608   -554    182       N  
ATOM   4545  CA  PHE B 342      16.543 -36.895  75.375  1.00 57.14           C  
ANISOU 4545  CA  PHE B 342     8414   5567   7728   -461   -739    141       C  
ATOM   4546  C   PHE B 342      17.434 -35.694  75.663  1.00 60.10           C  
ANISOU 4546  C   PHE B 342     8839   6038   7958   -275   -574    303       C  
ATOM   4547  O   PHE B 342      18.205 -35.261  74.796  1.00 71.23           O  
ANISOU 4547  O   PHE B 342    10495   7452   9116   -145   -568    303       O  
ATOM   4548  CB  PHE B 342      15.148 -36.435  74.946  1.00 58.43           C  
ANISOU 4548  CB  PHE B 342     8364   5844   7992   -503  -1043     54       C  
ATOM   4549  CG  PHE B 342      15.159 -35.384  73.875  1.00 61.19           C  
ANISOU 4549  CG  PHE B 342     8864   6306   8080   -323  -1248     53       C  
ATOM   4550  CD1 PHE B 342      15.423 -35.716  72.556  1.00 62.84           C  
ANISOU 4550  CD1 PHE B 342     9390   6470   8016   -278  -1419    -73       C  
ATOM   4551  CD2 PHE B 342      14.915 -34.059  74.191  1.00 60.01           C  
ANISOU 4551  CD2 PHE B 342     8568   6292   7942   -191  -1257    183       C  
ATOM   4552  CE1 PHE B 342      15.434 -34.745  71.571  1.00 60.07           C  
ANISOU 4552  CE1 PHE B 342     9228   6210   7385   -103  -1595    -48       C  
ATOM   4553  CE2 PHE B 342      14.927 -33.084  73.213  1.00 60.14           C  
ANISOU 4553  CE2 PHE B 342     8755   6381   7713    -16  -1437    208       C  
ATOM   4554  CZ  PHE B 342      15.187 -33.428  71.901  1.00 62.30           C  
ANISOU 4554  CZ  PHE B 342     9368   6612   7693     29  -1604    104       C  
ATOM   4555  N   SER B 343      17.352 -35.147  76.878  1.00 59.37           N  
ANISOU 4555  N   SER B 343     8524   6013   8022   -266   -423    434       N  
ATOM   4556  CA  SER B 343      18.202 -34.017  77.236  1.00 60.82           C  
ANISOU 4556  CA  SER B 343     8734   6272   8104   -106   -268    565       C  
ATOM   4557  C   SER B 343      19.660 -34.433  77.365  1.00 53.19           C  
ANISOU 4557  C   SER B 343     7967   5208   7035    -45    -51    596       C  
ATOM   4558  O   SER B 343      20.557 -33.652  77.027  1.00 53.85           O  
ANISOU 4558  O   SER B 343     8168   5317   6975     85     41    641       O  
ATOM   4559  CB  SER B 343      17.708 -33.371  78.531  1.00 62.99           C  
ANISOU 4559  CB  SER B 343     8728   6640   8566   -114   -171    666       C  
ATOM   4560  OG  SER B 343      17.266 -34.349  79.455  1.00 74.87           O  
ANISOU 4560  OG  SER B 343    10105   8084  10260   -265    -83    665       O  
ATOM   4561  N   HIS B 344      19.922 -35.655  77.837  1.00 48.95           N  
ANISOU 4561  N   HIS B 344     7463   4545   6589   -135     38    569       N  
ATOM   4562  CA  HIS B 344      21.296 -36.144  77.851  1.00 50.90           C  
ANISOU 4562  CA  HIS B 344     7891   4687   6760    -57    211    573       C  
ATOM   4563  C   HIS B 344      21.858 -36.218  76.439  1.00 55.01           C  
ANISOU 4563  C   HIS B 344     8668   5160   7074      6    175    467       C  
ATOM   4564  O   HIS B 344      23.009 -35.834  76.199  1.00 59.55           O  
ANISOU 4564  O   HIS B 344     9357   5725   7546    125    328    485       O  
ATOM   4565  CB  HIS B 344      21.365 -37.518  78.517  1.00 61.12           C  
ANISOU 4565  CB  HIS B 344     9205   5824   8192   -153    281    563       C  
ATOM   4566  CG  HIS B 344      21.079 -37.497  79.984  1.00 60.34           C  
ANISOU 4566  CG  HIS B 344     8927   5754   8245   -190    380    691       C  
ATOM   4567  ND1 HIS B 344      20.469 -38.546  80.636  1.00 59.95           N  
ANISOU 4567  ND1 HIS B 344     8843   5588   8348   -333    408    709       N  
ATOM   4568  CD2 HIS B 344      21.336 -36.562  80.930  1.00 59.24           C  
ANISOU 4568  CD2 HIS B 344     8660   5736   8114   -104    471    804       C  
ATOM   4569  CE1 HIS B 344      20.354 -38.255  81.920  1.00 61.21           C  
ANISOU 4569  CE1 HIS B 344     8878   5804   8575   -327    524    841       C  
ATOM   4570  NE2 HIS B 344      20.874 -37.057  82.124  1.00 60.13           N  
ANISOU 4570  NE2 HIS B 344     8680   5817   8347   -185    551    889       N  
ATOM   4571  N   TRP B 345      21.058 -36.713  75.492  1.00 62.43           N  
ANISOU 4571  N   TRP B 345     9699   6069   7951    -77    -21    342       N  
ATOM   4572  CA  TRP B 345      21.496 -36.777  74.101  1.00 64.29           C  
ANISOU 4572  CA  TRP B 345    10222   6267   7938    -14    -65    231       C  
ATOM   4573  C   TRP B 345      21.708 -35.389  73.511  1.00 59.75           C  
ANISOU 4573  C   TRP B 345     9720   5815   7169    118    -65    307       C  
ATOM   4574  O   TRP B 345      22.638 -35.176  72.724  1.00 62.98           O  
ANISOU 4574  O   TRP B 345    10365   6189   7375    213     67    287       O  
ATOM   4575  CB  TRP B 345      20.474 -37.546  73.269  1.00 62.95           C  
ANISOU 4575  CB  TRP B 345    10128   6053   7738   -131   -325     64       C  
ATOM   4576  CG  TRP B 345      20.814 -37.602  71.815  1.00 64.53           C  
ANISOU 4576  CG  TRP B 345    10659   6226   7633    -62   -396    -64       C  
ATOM   4577  CD1 TRP B 345      21.667 -38.472  71.206  1.00 59.88           C  
ANISOU 4577  CD1 TRP B 345    10330   5497   6927    -44   -271   -186       C  
ATOM   4578  CD2 TRP B 345      20.313 -36.740  70.785  1.00 64.74           C  
ANISOU 4578  CD2 TRP B 345    10821   6366   7411     14   -600    -80       C  
ATOM   4579  NE1 TRP B 345      21.722 -38.213  69.856  1.00 66.79           N  
ANISOU 4579  NE1 TRP B 345    11504   6396   7475     28   -366   -285       N  
ATOM   4580  CE2 TRP B 345      20.900 -37.154  69.573  1.00 67.07           C  
ANISOU 4580  CE2 TRP B 345    11485   6587   7412     68   -579   -212       C  
ATOM   4581  CE3 TRP B 345      19.422 -35.663  70.770  1.00 56.65           C  
ANISOU 4581  CE3 TRP B 345     9655   5489   6380     58   -801      4       C  
ATOM   4582  CZ2 TRP B 345      20.626 -36.527  68.359  1.00 68.15           C  
ANISOU 4582  CZ2 TRP B 345    11885   6797   7213    161   -754   -247       C  
ATOM   4583  CZ3 TRP B 345      19.151 -35.042  69.564  1.00 57.47           C  
ANISOU 4583  CZ3 TRP B 345    10003   5656   6178    162   -997    -25       C  
ATOM   4584  CH2 TRP B 345      19.751 -35.476  68.375  1.00 66.41           C  
ANISOU 4584  CH2 TRP B 345    11533   6715   6983    211   -975   -143       C  
ATOM   4585  N   LEU B 346      20.846 -34.433  73.868  1.00 55.08           N  
ANISOU 4585  N   LEU B 346     8933   5350   6643    127   -192    394       N  
ATOM   4586  CA  LEU B 346      20.960 -33.088  73.314  1.00 49.70           C  
ANISOU 4586  CA  LEU B 346     8336   4756   5792    256   -204    481       C  
ATOM   4587  C   LEU B 346      22.291 -32.447  73.681  1.00 51.96           C  
ANISOU 4587  C   LEU B 346     8657   5023   6063    351     98    578       C  
ATOM   4588  O   LEU B 346      22.861 -31.687  72.891  1.00 55.47           O  
ANISOU 4588  O   LEU B 346     9301   5463   6311    447    187    617       O  
ATOM   4589  CB  LEU B 346      19.800 -32.220  73.803  1.00 53.66           C  
ANISOU 4589  CB  LEU B 346     8582   5379   6429    260   -382    553       C  
ATOM   4590  CG  LEU B 346      18.739 -31.835  72.768  1.00 57.52           C  
ANISOU 4590  CG  LEU B 346     9144   5929   6782    298   -706    503       C  
ATOM   4591  CD1 LEU B 346      17.640 -30.992  73.398  1.00 61.66           C  
ANISOU 4591  CD1 LEU B 346     9358   6564   7508    317   -856    567       C  
ATOM   4592  CD2 LEU B 346      19.379 -31.100  71.603  1.00 51.78           C  
ANISOU 4592  CD2 LEU B 346     8766   5187   5723    442   -680    550       C  
ATOM   4593  N   VAL B 347      22.802 -32.731  74.878  1.00 58.52           N  
ANISOU 4593  N   VAL B 347     9301   5836   7100    324    258    617       N  
ATOM   4594  CA  VAL B 347      24.096 -32.181  75.265  1.00 58.50           C  
ANISOU 4594  CA  VAL B 347     9293   5814   7121    410    515    674       C  
ATOM   4595  C   VAL B 347      25.184 -32.693  74.329  1.00 62.32           C  
ANISOU 4595  C   VAL B 347    10028   6193   7458    452    676    591       C  
ATOM   4596  O   VAL B 347      26.003 -31.922  73.818  1.00 63.43           O  
ANISOU 4596  O   VAL B 347    10279   6323   7500    528    851    620       O  
ATOM   4597  CB  VAL B 347      24.407 -32.520  76.734  1.00 58.55           C  
ANISOU 4597  CB  VAL B 347     9070   5822   7354    387    604    713       C  
ATOM   4598  CG1 VAL B 347      25.880 -32.309  77.017  1.00 60.18           C  
ANISOU 4598  CG1 VAL B 347     9280   5985   7602    473    835    714       C  
ATOM   4599  CG2 VAL B 347      23.548 -31.680  77.668  1.00 58.05           C  
ANISOU 4599  CG2 VAL B 347     8774   5874   7411    374    526    801       C  
ATOM   4600  N   TYR B 348      25.199 -34.005  74.084  1.00 60.33           N  
ANISOU 4600  N   TYR B 348     9873   5847   7202    397    642    478       N  
ATOM   4601  CA  TYR B 348      26.193 -34.584  73.185  1.00 58.79           C  
ANISOU 4601  CA  TYR B 348     9919   5543   6875    443    807    372       C  
ATOM   4602  C   TYR B 348      25.970 -34.158  71.739  1.00 62.43           C  
ANISOU 4602  C   TYR B 348    10677   6017   7028    474    763    333       C  
ATOM   4603  O   TYR B 348      26.934 -34.058  70.972  1.00 73.23           O  
ANISOU 4603  O   TYR B 348    12249   7325   8249    539    985    291       O  
ATOM   4604  CB  TYR B 348      26.186 -36.103  73.319  1.00 65.49           C  
ANISOU 4604  CB  TYR B 348    10805   6267   7813    382    770    254       C  
ATOM   4605  CG  TYR B 348      26.521 -36.547  74.719  1.00 57.29           C  
ANISOU 4605  CG  TYR B 348     9534   5194   7039    379    829    316       C  
ATOM   4606  CD1 TYR B 348      27.750 -36.237  75.289  1.00 54.63           C  
ANISOU 4606  CD1 TYR B 348     9100   4847   6809    482   1034    352       C  
ATOM   4607  CD2 TYR B 348      25.603 -37.250  75.483  1.00 50.81           C  
ANISOU 4607  CD2 TYR B 348     8595   4351   6359    274    678    337       C  
ATOM   4608  CE1 TYR B 348      28.059 -36.628  76.576  1.00 54.44           C  
ANISOU 4608  CE1 TYR B 348     8855   4846   6984    494   1032    400       C  
ATOM   4609  CE2 TYR B 348      25.904 -37.646  76.771  1.00 54.54           C  
ANISOU 4609  CE2 TYR B 348     8909   4786   7025    283    739    415       C  
ATOM   4610  CZ  TYR B 348      27.133 -37.332  77.313  1.00 55.11           C  
ANISOU 4610  CZ  TYR B 348     8881   4898   7160    403    891    444       C  
ATOM   4611  OH  TYR B 348      27.435 -37.725  78.595  1.00 56.90           O  
ANISOU 4611  OH  TYR B 348     8911   5180   7528    418    876    499       O  
ATOM   4612  N   ALA B 349      24.717 -33.912  71.347  1.00 59.96           N  
ANISOU 4612  N   ALA B 349    10395   5777   6610    436    481    341       N  
ATOM   4613  CA  ALA B 349      24.451 -33.433  69.995  1.00 62.79           C  
ANISOU 4613  CA  ALA B 349    11064   6155   6636    492    393    321       C  
ATOM   4614  C   ALA B 349      25.103 -32.082  69.747  1.00 69.13           C  
ANISOU 4614  C   ALA B 349    11950   6986   7330    593    597    463       C  
ATOM   4615  O   ALA B 349      25.441 -31.754  68.603  1.00 82.04           O  
ANISOU 4615  O   ALA B 349    13917   8590   8664    658    683    459       O  
ATOM   4616  CB  ALA B 349      22.946 -33.341  69.748  1.00 56.58           C  
ANISOU 4616  CB  ALA B 349    10238   5454   5806    452      5    304       C  
ATOM   4617  N   ASN B 350      25.276 -31.282  70.800  1.00 64.28           N  
ANISOU 4617  N   ASN B 350    11058   6418   6949    604    686    586       N  
ATOM   4618  CA  ASN B 350      25.926 -29.987  70.647  1.00 62.15           C  
ANISOU 4618  CA  ASN B 350    10841   6144   6628    680    898    712       C  
ATOM   4619  C   ASN B 350      27.351 -30.140  70.127  1.00 60.60           C  
ANISOU 4619  C   ASN B 350    10816   5847   6364    707   1261    663       C  
ATOM   4620  O   ASN B 350      27.810 -29.334  69.310  1.00 62.81           O  
ANISOU 4620  O   ASN B 350    11328   6086   6450    760   1445    730       O  
ATOM   4621  CB  ASN B 350      25.918 -29.245  71.982  1.00 62.83           C  
ANISOU 4621  CB  ASN B 350    10577   6285   7010    674    929    808       C  
ATOM   4622  CG  ASN B 350      26.509 -27.857  71.882  1.00 74.25           C  
ANISOU 4622  CG  ASN B 350    12014   7738   8459    728   1119    901       C  
ATOM   4623  OD1 ASN B 350      25.912 -26.958  71.290  1.00 82.82           O  
ANISOU 4623  OD1 ASN B 350    13211   8856   9403    775   1010    979       O  
ATOM   4624  ND2 ASN B 350      27.692 -27.676  72.455  1.00 75.80           N  
ANISOU 4624  ND2 ASN B 350    12018   7937   8847    712   1370    850       N  
ATOM   4625  N   SER B 351      28.068 -31.171  70.583  1.00 58.69           N  
ANISOU 4625  N   SER B 351    10462   5551   6287    677   1384    547       N  
ATOM   4626  CA  SER B 351      29.427 -31.380  70.092  1.00 64.36           C  
ANISOU 4626  CA  SER B 351    11299   6171   6984    712   1737    473       C  
ATOM   4627  C   SER B 351      29.445 -31.682  68.600  1.00 68.82           C  
ANISOU 4627  C   SER B 351    12288   6682   7180    737   1799    400       C  
ATOM   4628  O   SER B 351      30.396 -31.311  67.903  1.00 74.16           O  
ANISOU 4628  O   SER B 351    13145   7290   7743    774   2130    395       O  
ATOM   4629  CB  SER B 351      30.099 -32.505  70.878  1.00 72.22           C  
ANISOU 4629  CB  SER B 351    12090   7112   8240    702   1804    357       C  
ATOM   4630  OG  SER B 351      30.121 -32.196  72.261  1.00 75.80           O  
ANISOU 4630  OG  SER B 351    12195   7621   8986    693   1745    428       O  
ATOM   4631  N   ALA B 352      28.405 -32.345  68.090  1.00 64.06           N  
ANISOU 4631  N   ALA B 352    11850   6103   6386    713   1493    333       N  
ATOM   4632  CA  ALA B 352      28.311 -32.585  66.655  1.00 64.26           C  
ANISOU 4632  CA  ALA B 352    12316   6091   6010    747   1498    253       C  
ATOM   4633  C   ALA B 352      27.850 -31.349  65.896  1.00 60.65           C  
ANISOU 4633  C   ALA B 352    12108   5681   5255    810   1441    407       C  
ATOM   4634  O   ALA B 352      28.197 -31.184  64.722  1.00 57.94           O  
ANISOU 4634  O   ALA B 352    12169   5290   4554    864   1597    396       O  
ATOM   4635  CB  ALA B 352      27.361 -33.749  66.375  1.00 70.08           C  
ANISOU 4635  CB  ALA B 352    13135   6830   6662    695   1159     95       C  
ATOM   4636  N   ALA B 353      27.076 -30.476  66.544  1.00 62.62           N  
ANISOU 4636  N   ALA B 353    12145   6014   5635    814   1229    556       N  
ATOM   4637  CA  ALA B 353      26.569 -29.292  65.860  1.00 62.59           C  
ANISOU 4637  CA  ALA B 353    12377   6036   5369    896   1138    716       C  
ATOM   4638  C   ALA B 353      27.680 -28.296  65.549  1.00 74.76           C  
ANISOU 4638  C   ALA B 353    13902   7525   6980    920   1517    763       C  
ATOM   4639  O   ALA B 353      27.705 -27.712  64.459  1.00 84.15           O  
ANISOU 4639  O   ALA B 353    15356   8689   7929    976   1547    789       O  
ATOM   4640  CB  ALA B 353      25.481 -28.627  66.702  1.00 47.64           C  
ANISOU 4640  CB  ALA B 353    10181   4238   3684    900    821    826       C  
ATOM   4641  N   ASN B 354      28.597 -28.078  66.491  1.00 70.06           N  
ANISOU 4641  N   ASN B 354    12981   6906   6731    875   1784    763       N  
ATOM   4642  CA  ASN B 354      29.584 -27.008  66.345  1.00 69.26           C  
ANISOU 4642  CA  ASN B 354    12795   6757   6763    882   2095    794       C  
ATOM   4643  C   ASN B 354      30.397 -27.099  65.060  1.00 71.35           C  
ANISOU 4643  C   ASN B 354    13392   6905   6812    904   2367    739       C  
ATOM   4644  O   ASN B 354      30.455 -26.100  64.324  1.00 74.22           O  
ANISOU 4644  O   ASN B 354    13909   7234   7057    939   2434    817       O  
ATOM   4645  CB  ASN B 354      30.509 -27.017  67.571  1.00 70.03           C  
ANISOU 4645  CB  ASN B 354    12497   6847   7265    832   2308    753       C  
ATOM   4646  CG  ASN B 354      29.810 -26.545  68.832  1.00 72.97           C  
ANISOU 4646  CG  ASN B 354    12512   7336   7878    810   2071    821       C  
ATOM   4647  OD1 ASN B 354      28.808 -25.834  68.768  1.00 76.90           O  
ANISOU 4647  OD1 ASN B 354    13019   7903   8297    835   1824    914       O  
ATOM   4648  ND2 ASN B 354      30.339 -26.937  69.986  1.00 75.78           N  
ANISOU 4648  ND2 ASN B 354    12550   7709   8535    773   2139    769       N  
ATOM   4649  N   PRO B 355      31.038 -28.224  64.728  1.00 72.27           N  
ANISOU 4649  N   PRO B 355    13631   6949   6879    886   2538    613       N  
ATOM   4650  CA  PRO B 355      31.752 -28.287  63.441  1.00 65.29           C  
ANISOU 4650  CA  PRO B 355    13058   5955   5794    902   2782    568       C  
ATOM   4651  C   PRO B 355      30.847 -28.061  62.242  1.00 68.92           C  
ANISOU 4651  C   PRO B 355    13922   6441   5825    965   2552    614       C  
ATOM   4652  O   PRO B 355      31.268 -27.442  61.256  1.00 72.31           O  
ANISOU 4652  O   PRO B 355    14586   6793   6095    993   2732    660       O  
ATOM   4653  CB  PRO B 355      32.355 -29.701  63.439  1.00 65.54           C  
ANISOU 4653  CB  PRO B 355    13097   5938   5866    872   2915    409       C  
ATOM   4654  CG  PRO B 355      32.293 -30.159  64.871  1.00 71.45           C  
ANISOU 4654  CG  PRO B 355    13485   6741   6923    842   2842    383       C  
ATOM   4655  CD  PRO B 355      31.094 -29.497  65.460  1.00 75.02           C  
ANISOU 4655  CD  PRO B 355    13857   7307   7342    853   2510    507       C  
ATOM   4656  N   ILE B 356      29.601 -28.537  62.309  1.00 71.09           N  
ANISOU 4656  N   ILE B 356    14282   6816   5913    989   2143    604       N  
ATOM   4657  CA  ILE B 356      28.662 -28.310  61.215  1.00 75.01           C  
ANISOU 4657  CA  ILE B 356    15132   7348   6019   1063   1854    638       C  
ATOM   4658  C   ILE B 356      28.347 -26.828  61.075  1.00 83.55           C  
ANISOU 4658  C   ILE B 356    16198   8447   7102   1119   1808    813       C  
ATOM   4659  O   ILE B 356      28.177 -26.317  59.962  1.00 89.25           O  
ANISOU 4659  O   ILE B 356    17244   9136   7533   1190   1781    869       O  
ATOM   4660  CB  ILE B 356      27.387 -29.148  61.426  1.00 67.21           C  
ANISOU 4660  CB  ILE B 356    14179   6464   4893   1067   1388    566       C  
ATOM   4661  CG1 ILE B 356      27.720 -30.637  61.324  1.00 69.62           C  
ANISOU 4661  CG1 ILE B 356    14580   6730   5141   1014   1445    361       C  
ATOM   4662  CG2 ILE B 356      26.325 -28.767  60.408  1.00 66.21           C  
ANISOU 4662  CG2 ILE B 356    14346   6392   4417   1159   1019    603       C  
ATOM   4663  CD1 ILE B 356      26.653 -31.549  61.884  1.00 71.72           C  
ANISOU 4663  CD1 ILE B 356    14790   7076   5386    976   1044    254       C  
ATOM   4664  N   ILE B 357      28.249 -26.120  62.201  1.00 82.51           N  
ANISOU 4664  N   ILE B 357    15695   8362   7292   1092   1793    898       N  
ATOM   4665  CA  ILE B 357      28.017 -24.680  62.151  1.00 75.78           C  
ANISOU 4665  CA  ILE B 357    14798   7514   6481   1138   1777   1051       C  
ATOM   4666  C   ILE B 357      29.192 -23.969  61.494  1.00 76.40           C  
ANISOU 4666  C   ILE B 357    15016   7455   6556   1130   2201   1083       C  
ATOM   4667  O   ILE B 357      29.009 -23.054  60.680  1.00 77.82           O  
ANISOU 4667  O   ILE B 357    15437   7590   6541   1195   2203   1192       O  
ATOM   4668  CB  ILE B 357      27.744 -24.130  63.561  1.00 71.15           C  
ANISOU 4668  CB  ILE B 357    13760   7005   6267   1097   1693   1109       C  
ATOM   4669  CG1 ILE B 357      26.437 -24.708  64.103  1.00 67.51           C  
ANISOU 4669  CG1 ILE B 357    13188   6664   5798   1112   1254   1105       C  
ATOM   4670  CG2 ILE B 357      27.697 -22.615  63.535  1.00 79.12           C  
ANISOU 4670  CG2 ILE B 357    14719   7993   7352   1133   1742   1249       C  
ATOM   4671  CD1 ILE B 357      26.232 -24.468  65.577  1.00 62.72           C  
ANISOU 4671  CD1 ILE B 357    12130   6127   5574   1058   1198   1136       C  
ATOM   4672  N   TYR B 358      30.418 -24.373  61.836  1.00 78.99           N  
ANISOU 4672  N   TYR B 358    15196   7703   7112   1054   2566    990       N  
ATOM   4673  CA  TYR B 358      31.586 -23.742  61.232  1.00 81.80           C  
ANISOU 4673  CA  TYR B 358    15660   7912   7507   1034   2984   1007       C  
ATOM   4674  C   TYR B 358      31.640 -23.979  59.730  1.00 89.90           C  
ANISOU 4674  C   TYR B 358    17172   8861   8126   1086   3056   1010       C  
ATOM   4675  O   TYR B 358      32.208 -23.165  58.994  1.00 97.21           O  
ANISOU 4675  O   TYR B 358    18293   9670   8972   1097   3319   1084       O  
ATOM   4676  CB  TYR B 358      32.878 -24.263  61.867  1.00 76.10           C  
ANISOU 4676  CB  TYR B 358    14663   7115   7134    947   3327    889       C  
ATOM   4677  CG  TYR B 358      32.939 -24.228  63.377  1.00 67.89           C  
ANISOU 4677  CG  TYR B 358    13153   6152   6489    900   3262    860       C  
ATOM   4678  CD1 TYR B 358      32.201 -23.308  64.107  1.00 64.19           C  
ANISOU 4678  CD1 TYR B 358    12485   5779   6125    914   3045    956       C  
ATOM   4679  CD2 TYR B 358      33.757 -25.110  64.071  1.00 70.43           C  
ANISOU 4679  CD2 TYR B 358    13229   6448   7084    846   3419    740       C  
ATOM   4680  CE1 TYR B 358      32.268 -23.275  65.488  1.00 67.52           C  
ANISOU 4680  CE1 TYR B 358    12488   6276   6890    871   2988    926       C  
ATOM   4681  CE2 TYR B 358      33.831 -25.085  65.449  1.00 72.07           C  
ANISOU 4681  CE2 TYR B 358    13027   6724   7632    815   3354    716       C  
ATOM   4682  CZ  TYR B 358      33.085 -24.166  66.154  1.00 71.87           C  
ANISOU 4682  CZ  TYR B 358    12822   6803   7683    826   3140    805       C  
ATOM   4683  OH  TYR B 358      33.155 -24.137  67.529  1.00 74.38           O  
ANISOU 4683  OH  TYR B 358    12743   7198   8321    795   3072    778       O  
ATOM   4684  N   ASN B 359      31.053 -25.080  59.255  1.00 88.43           N  
ANISOU 4684  N   ASN B 359    17196   8731   7671   1117   2829    925       N  
ATOM   4685  CA  ASN B 359      31.101 -25.382  57.827  1.00 90.72           C  
ANISOU 4685  CA  ASN B 359    17955   8960   7555   1170   2880    906       C  
ATOM   4686  C   ASN B 359      30.222 -24.430  57.025  1.00 93.62           C  
ANISOU 4686  C   ASN B 359    18625   9346   7602   1276   2648   1053       C  
ATOM   4687  O   ASN B 359      30.639 -23.930  55.973  1.00101.03           O  
ANISOU 4687  O   ASN B 359    19901  10181   8306   1315   2860   1118       O  
ATOM   4688  CB  ASN B 359      30.679 -26.832  57.589  1.00 89.91           C  
ANISOU 4688  CB  ASN B 359    17977   8920   7265   1171   2668    749       C  
ATOM   4689  CG  ASN B 359      30.771 -27.237  56.131  1.00 94.40           C  
ANISOU 4689  CG  ASN B 359    19020   9436   7412   1222   2720    701       C  
ATOM   4690  OD1 ASN B 359      31.857 -27.510  55.622  1.00101.28           O  
ANISOU 4690  OD1 ASN B 359    19992  10199   8290   1184   3114    646       O  
ATOM   4691  ND2 ASN B 359      29.629 -27.285  55.452  1.00 95.53           N  
ANISOU 4691  ND2 ASN B 359    19446   9660   7191   1313   2313    714       N  
ATOM   4692  N   PHE B 360      29.003 -24.171  57.500  1.00 85.45           N  
ANISOU 4692  N   PHE B 360    17474   8436   6556   1328   2213   1111       N  
ATOM   4693  CA  PHE B 360      28.076 -23.330  56.754  1.00 84.54           C  
ANISOU 4693  CA  PHE B 360    17627   8345   6150   1447   1936   1246       C  
ATOM   4694  C   PHE B 360      28.315 -21.838  56.968  1.00 90.64           C  
ANISOU 4694  C   PHE B 360    18311   9050   7080   1461   2107   1420       C  
ATOM   4695  O   PHE B 360      28.058 -21.042  56.058  1.00 97.02           O  
ANISOU 4695  O   PHE B 360    19445   9801   7618   1555   2078   1547       O  
ATOM   4696  CB  PHE B 360      26.639 -23.691  57.126  1.00 75.41           C  
ANISOU 4696  CB  PHE B 360    16367   7344   4940   1503   1379   1225       C  
ATOM   4697  CG  PHE B 360      26.277 -25.116  56.819  1.00 86.63           C  
ANISOU 4697  CG  PHE B 360    17916   8825   6175   1491   1160   1045       C  
ATOM   4698  CD1 PHE B 360      26.479 -25.632  55.550  1.00 93.92           C  
ANISOU 4698  CD1 PHE B 360    19268   9699   6718   1536   1204    972       C  
ATOM   4699  CD2 PHE B 360      25.745 -25.943  57.796  1.00 89.07           C  
ANISOU 4699  CD2 PHE B 360    17926   9231   6684   1431    919    942       C  
ATOM   4700  CE1 PHE B 360      26.152 -26.941  55.253  1.00 92.14           C  
ANISOU 4700  CE1 PHE B 360    19156   9526   6327   1518    998    783       C  
ATOM   4701  CE2 PHE B 360      25.416 -27.256  57.506  1.00 90.18           C  
ANISOU 4701  CE2 PHE B 360    18193   9412   6660   1409    718    759       C  
ATOM   4702  CZ  PHE B 360      25.620 -27.755  56.231  1.00 91.92           C  
ANISOU 4702  CZ  PHE B 360    18825   9588   6514   1451    752    671       C  
ATOM   4703  N   LEU B 361      28.795 -21.435  58.145  1.00 86.90           N  
ANISOU 4703  N   LEU B 361    17414   8575   7028   1373   2277   1426       N  
ATOM   4704  CA  LEU B 361      28.956 -20.021  58.464  1.00 82.84           C  
ANISOU 4704  CA  LEU B 361    16779   8000   6694   1376   2407   1571       C  
ATOM   4705  C   LEU B 361      30.401 -19.538  58.412  1.00 90.49           C  
ANISOU 4705  C   LEU B 361    17721   8809   7852   1289   2939   1563       C  
ATOM   4706  O   LEU B 361      30.656 -18.367  58.710  1.00 97.41           O  
ANISOU 4706  O   LEU B 361    18490   9616   8906   1274   3085   1665       O  
ATOM   4707  CB  LEU B 361      28.362 -19.719  59.844  1.00 74.17           C  
ANISOU 4707  CB  LEU B 361    15220   7018   5944   1345   2181   1587       C  
ATOM   4708  CG  LEU B 361      26.861 -19.981  59.981  1.00 70.82           C  
ANISOU 4708  CG  LEU B 361    14773   6739   5398   1431   1650   1614       C  
ATOM   4709  CD1 LEU B 361      26.414 -19.895  61.436  1.00 71.43           C  
ANISOU 4709  CD1 LEU B 361    14367   6921   5853   1378   1487   1605       C  
ATOM   4710  CD2 LEU B 361      26.075 -19.011  59.111  1.00 75.73           C  
ANISOU 4710  CD2 LEU B 361    15689   7332   5754   1566   1440   1774       C  
ATOM   4711  N   SER B 362      31.350 -20.396  58.042  1.00 90.21           N  
ANISOU 4711  N   SER B 362    17771   8703   7802   1231   3232   1439       N  
ATOM   4712  CA  SER B 362      32.748 -19.989  57.918  1.00 90.23           C  
ANISOU 4712  CA  SER B 362    17742   8539   8002   1148   3743   1419       C  
ATOM   4713  C   SER B 362      33.313 -20.602  56.645  1.00 94.65           C  
ANISOU 4713  C   SER B 362    18715   8996   8252   1161   3979   1376       C  
ATOM   4714  O   SER B 362      33.434 -21.827  56.545  1.00 96.51           O  
ANISOU 4714  O   SER B 362    18966   9274   8429   1142   3950   1241       O  
ATOM   4715  CB  SER B 362      33.562 -20.417  59.141  1.00 81.35           C  
ANISOU 4715  CB  SER B 362    16135   7427   7345   1038   3908   1285       C  
ATOM   4716  OG  SER B 362      34.936 -20.124  58.963  1.00 79.90           O  
ANISOU 4716  OG  SER B 362    15912   7076   7371    957   4385   1243       O  
ATOM   4717  N   GLY B 363      33.656 -19.756  55.672  1.00 93.09           N  
ANISOU 4717  N   GLY B 363    18862   8657   7850   1191   4223   1492       N  
ATOM   4718  CA  GLY B 363      34.221 -20.266  54.435  1.00 97.05           C  
ANISOU 4718  CA  GLY B 363    19776   9055   8042   1202   4480   1459       C  
ATOM   4719  C   GLY B 363      35.634 -20.786  54.592  1.00 98.72           C  
ANISOU 4719  C   GLY B 363    19804   9156   8551   1079   4942   1324       C  
ATOM   4720  O   GLY B 363      36.057 -21.676  53.849  1.00107.95           O  
ANISOU 4720  O   GLY B 363    21192  10291   9532   1072   5095   1233       O  
ATOM   4721  N   LYS B 364      36.385 -20.240  55.550  1.00 91.57           N  
ANISOU 4721  N   LYS B 364    18485   8193   8115    983   5160   1301       N  
ATOM   4722  CA  LYS B 364      37.742 -20.722  55.781  1.00 90.19           C  
ANISOU 4722  CA  LYS B 364    18077   7912   8277    867   5568   1163       C  
ATOM   4723  C   LYS B 364      37.736 -22.120  56.388  1.00 95.57           C  
ANISOU 4723  C   LYS B 364    18509   8713   9092    843   5403   1001       C  
ATOM   4724  O   LYS B 364      38.572 -22.959  56.032  1.00 98.77           O  
ANISOU 4724  O   LYS B 364    18927   9059   9542    792   5659    887       O  
ATOM   4725  CB  LYS B 364      38.500 -19.725  56.656  1.00 86.01           C  
ANISOU 4725  CB  LYS B 364    17170   7290   8221    776   5801   1170       C  
ATOM   4726  CG  LYS B 364      39.058 -18.560  55.849  1.00 94.01           C  
ANISOU 4726  CG  LYS B 364    18452   8107   9159    755   6175   1286       C  
ATOM   4727  CD  LYS B 364      38.967 -17.239  56.591  1.00 96.87           C  
ANISOU 4727  CD  LYS B 364    18590   8435   9783    732   6164   1374       C  
ATOM   4728  CE  LYS B 364      39.208 -16.080  55.634  1.00104.38           C  
ANISOU 4728  CE  LYS B 364    19919   9197  10543    740   6466   1530       C  
ATOM   4729  NZ  LYS B 364      39.281 -14.759  56.316  1.00108.65           N  
ANISOU 4729  NZ  LYS B 364    20244   9669  11371    700   6524   1605       N  
ATOM   4730  N   PHE B 365      36.807 -22.391  57.310  1.00 95.25           N  
ANISOU 4730  N   PHE B 365    18237   8836   9118    878   4990    992       N  
ATOM   4731  CA  PHE B 365      36.633 -23.759  57.788  1.00 86.69           C  
ANISOU 4731  CA  PHE B 365    16990   7860   8087    869   4804    856       C  
ATOM   4732  C   PHE B 365      36.077 -24.650  56.687  1.00 90.04           C  
ANISOU 4732  C   PHE B 365    17845   8324   8043    936   4665    823       C  
ATOM   4733  O   PHE B 365      36.523 -25.789  56.514  1.00 95.31           O  
ANISOU 4733  O   PHE B 365    18513   8990   8711    907   4758    689       O  
ATOM   4734  CB  PHE B 365      35.705 -23.789  59.003  1.00 87.41           C  
ANISOU 4734  CB  PHE B 365    16767   8108   8335    889   4407    864       C  
ATOM   4735  CG  PHE B 365      36.400 -23.544  60.308  1.00 90.39           C  
ANISOU 4735  CG  PHE B 365    16644   8478   9221    811   4522    814       C  
ATOM   4736  CD1 PHE B 365      37.277 -24.480  60.830  1.00 91.58           C  
ANISOU 4736  CD1 PHE B 365    16531   8606   9660    745   4677    680       C  
ATOM   4737  CD2 PHE B 365      36.157 -22.386  61.024  1.00 87.01           C  
ANISOU 4737  CD2 PHE B 365    16006   8072   8981    809   4451    898       C  
ATOM   4738  CE1 PHE B 365      37.910 -24.258  62.039  1.00 86.20           C  
ANISOU 4738  CE1 PHE B 365    15392   7920   9442    681   4745    632       C  
ATOM   4739  CE2 PHE B 365      36.785 -22.157  62.232  1.00 83.43           C  
ANISOU 4739  CE2 PHE B 365    15102   7616   8981    742   4533    837       C  
ATOM   4740  CZ  PHE B 365      37.663 -23.094  62.741  1.00 82.59           C  
ANISOU 4740  CZ  PHE B 365    14744   7483   9155    681   4671    705       C  
ATOM   4741  N   ARG B 366      35.103 -24.138  55.932  1.00 94.04           N  
ANISOU 4741  N   ARG B 366    18715   8866   8149   1032   4427    937       N  
ATOM   4742  CA  ARG B 366      34.511 -24.900  54.839  1.00 93.56           C  
ANISOU 4742  CA  ARG B 366    19087   8846   7615   1106   4251    899       C  
ATOM   4743  C   ARG B 366      35.576 -25.367  53.854  1.00 96.34           C  
ANISOU 4743  C   ARG B 366    19688   9073   7845   1072   4672    825       C  
ATOM   4744  O   ARG B 366      35.542 -26.508  53.379  1.00 99.68           O  
ANISOU 4744  O   ARG B 366    20264   9534   8075   1082   4623    695       O  
ATOM   4745  CB  ARG B 366      33.456 -24.047  54.137  1.00 95.45           C  
ANISOU 4745  CB  ARG B 366    19675   9119   7473   1220   3967   1053       C  
ATOM   4746  CG  ARG B 366      32.675 -24.749  53.040  1.00104.04           C  
ANISOU 4746  CG  ARG B 366    21208  10268   8054   1315   3692   1012       C  
ATOM   4747  CD  ARG B 366      31.247 -24.212  52.961  1.00112.26           C  
ANISOU 4747  CD  ARG B 366    22370  11423   8862   1429   3182   1121       C  
ATOM   4748  NE  ARG B 366      31.201 -22.756  53.083  1.00122.27           N  
ANISOU 4748  NE  ARG B 366    23615  12630  10212   1460   3254   1313       N  
ATOM   4749  CZ  ARG B 366      30.080 -22.049  53.182  1.00127.71           C  
ANISOU 4749  CZ  ARG B 366    24325  13400  10799   1554   2862   1435       C  
ATOM   4750  NH1 ARG B 366      30.129 -20.727  53.292  1.00126.69           N  
ANISOU 4750  NH1 ARG B 366    24175  13199  10762   1577   2966   1606       N  
ATOM   4751  NH2 ARG B 366      28.906 -22.665  53.163  1.00130.73           N  
ANISOU 4751  NH2 ARG B 366    24741  13929  11003   1625   2361   1379       N  
ATOM   4752  N   GLU B 367      36.528 -24.491  53.526  1.00100.85           N  
ANISOU 4752  N   GLU B 367    20300   9489   8529   1027   5097    899       N  
ATOM   4753  CA  GLU B 367      37.593 -24.862  52.602  1.00110.30           C  
ANISOU 4753  CA  GLU B 367    21716  10558   9636    985   5541    833       C  
ATOM   4754  C   GLU B 367      38.379 -26.059  53.125  1.00112.99           C  
ANISOU 4754  C   GLU B 367    21732  10917  10281    903   5688    644       C  
ATOM   4755  O   GLU B 367      38.587 -27.044  52.406  1.00122.84           O  
ANISOU 4755  O   GLU B 367    23190  12172  11312    914   5768    528       O  
ATOM   4756  CB  GLU B 367      38.515 -23.663  52.382  1.00115.47           C  
ANISOU 4756  CB  GLU B 367    22384  11032  10456    929   5985    938       C  
ATOM   4757  CG  GLU B 367      38.234 -22.866  51.122  1.00129.19           C  
ANISOU 4757  CG  GLU B 367    24675  12682  11731   1008   6075   1090       C  
ATOM   4758  CD  GLU B 367      39.047 -21.590  51.062  1.00138.43           C  
ANISOU 4758  CD  GLU B 367    25827  13667  13104    945   6491   1204       C  
ATOM   4759  OE1 GLU B 367      38.904 -20.752  51.978  1.00135.42           O  
ANISOU 4759  OE1 GLU B 367    25131  13290  13033    920   6400   1268       O  
ATOM   4760  OE2 GLU B 367      39.830 -21.426  50.103  1.00146.23           O  
ANISOU 4760  OE2 GLU B 367    27117  14500  13942    918   6919   1222       O  
ATOM   4761  N   GLN B 368      38.824 -25.993  54.383  1.00103.34           N  
ANISOU 4761  N   GLN B 368    19995   9705   9563    827   5715    606       N  
ATOM   4762  CA  GLN B 368      39.602 -27.092  54.944  1.00102.22           C  
ANISOU 4762  CA  GLN B 368    19516   9583   9741    758   5839    436       C  
ATOM   4763  C   GLN B 368      38.764 -28.353  55.112  1.00101.57           C  
ANISOU 4763  C   GLN B 368    19461   9648   9483    810   5467    331       C  
ATOM   4764  O   GLN B 368      39.291 -29.465  54.984  1.00 99.29           O  
ANISOU 4764  O   GLN B 368    19113   9369   9245    788   5582    177       O  
ATOM   4765  CB  GLN B 368      40.211 -26.671  56.282  1.00103.63           C  
ANISOU 4765  CB  GLN B 368    19145   9746  10482    677   5905    427       C  
ATOM   4766  CG  GLN B 368      41.141 -25.470  56.177  1.00112.98           C  
ANISOU 4766  CG  GLN B 368    20258  10769  11899    607   6290    495       C  
ATOM   4767  CD  GLN B 368      42.556 -25.850  55.785  1.00120.73           C  
ANISOU 4767  CD  GLN B 368    21140  11631  13102    518   6757    379       C  
ATOM   4768  OE1 GLN B 368      43.394 -26.137  56.641  1.00122.98           O  
ANISOU 4768  OE1 GLN B 368    20967  11911  13848    441   6861    275       O  
ATOM   4769  NE2 GLN B 368      42.829 -25.853  54.486  1.00129.48           N  
ANISOU 4769  NE2 GLN B 368    22673  12646  13878    533   7034    392       N  
ATOM   4770  N   PHE B 369      37.467 -28.212  55.397  1.00100.34           N  
ANISOU 4770  N   PHE B 369    19385   9605   9135    877   5022    398       N  
ATOM   4771  CA  PHE B 369      36.624 -29.398  55.509  1.00 96.02           C  
ANISOU 4771  CA  PHE B 369    18886   9182   8414    916   4665    285       C  
ATOM   4772  C   PHE B 369      36.437 -30.068  54.155  1.00103.62           C  
ANISOU 4772  C   PHE B 369    20321  10140   8909    969   4667    204       C  
ATOM   4773  O   PHE B 369      36.370 -31.300  54.070  1.00108.24           O  
ANISOU 4773  O   PHE B 369    20918  10775   9433    969   4578     37       O  
ATOM   4774  CB  PHE B 369      35.271 -29.035  56.120  1.00 94.45           C  
ANISOU 4774  CB  PHE B 369    18648   9103   8137    967   4191    370       C  
ATOM   4775  CG  PHE B 369      35.345 -28.600  57.553  1.00 87.17           C  
ANISOU 4775  CG  PHE B 369    17252   8212   7658    921   4144    416       C  
ATOM   4776  CD1 PHE B 369      36.489 -28.814  58.305  1.00 82.04           C  
ANISOU 4776  CD1 PHE B 369    16219   7506   7445    842   4436    352       C  
ATOM   4777  CD2 PHE B 369      34.262 -27.983  58.152  1.00 85.94           C  
ANISOU 4777  CD2 PHE B 369    17019   8151   7482    960   3792    517       C  
ATOM   4778  CE1 PHE B 369      36.551 -28.411  59.627  1.00 77.51           C  
ANISOU 4778  CE1 PHE B 369    15222   6968   7262    807   4371    387       C  
ATOM   4779  CE2 PHE B 369      34.316 -27.580  59.468  1.00 79.24           C  
ANISOU 4779  CE2 PHE B 369    15746   7340   7021    922   3752    551       C  
ATOM   4780  CZ  PHE B 369      35.461 -27.793  60.208  1.00 74.95           C  
ANISOU 4780  CZ  PHE B 369    14849   6737   6892    847   4040    485       C  
ATOM   4781  N   LYS B 370      36.356 -29.274  53.084  1.00109.88           N  
ANISOU 4781  N   LYS B 370    21516  10871   9364   1019   4767    313       N  
ATOM   4782  CA  LYS B 370      36.295 -29.850  51.745  1.00114.48           C  
ANISOU 4782  CA  LYS B 370    22569  11442   9488   1072   4812    235       C  
ATOM   4783  C   LYS B 370      37.606 -30.536  51.387  1.00113.17           C  
ANISOU 4783  C   LYS B 370    22355  11187   9460   1009   5280     98       C  
ATOM   4784  O   LYS B 370      37.610 -31.569  50.707  1.00117.50           O  
ANISOU 4784  O   LYS B 370    23115  11763   9766   1034   5274    -61       O  
ATOM   4785  CB  LYS B 370      35.975 -28.759  50.725  1.00119.63           C  
ANISOU 4785  CB  LYS B 370    23664  12037   9755   1146   4837    403       C  
ATOM   4786  CG  LYS B 370      35.273 -29.241  49.468  1.00130.20           C  
ANISOU 4786  CG  LYS B 370    25529  13425  10516   1244   4622    351       C  
ATOM   4787  CD  LYS B 370      34.954 -28.069  48.552  1.00143.07           C  
ANISOU 4787  CD  LYS B 370    27582  14996  11783   1331   4634    543       C  
ATOM   4788  CE  LYS B 370      33.664 -27.372  48.949  1.00145.73           C  
ANISOU 4788  CE  LYS B 370    27895  15432  12044   1411   4130    673       C  
ATOM   4789  NZ  LYS B 370      33.376 -26.204  48.071  1.00153.85           N  
ANISOU 4789  NZ  LYS B 370    29329  16394  12732   1508   4141    870       N  
ATOM   4790  N   ALA B 371      38.730 -29.974  51.840  1.00106.35           N  
ANISOU 4790  N   ALA B 371    21195  10215   8999    927   5681    140       N  
ATOM   4791  CA  ALA B 371      40.024 -30.594  51.587  1.00101.66           C  
ANISOU 4791  CA  ALA B 371    20484   9540   8601    864   6127      2       C  
ATOM   4792  C   ALA B 371      40.177 -31.914  52.331  1.00 98.92           C  
ANISOU 4792  C   ALA B 371    19792   9279   8515    844   6008   -189       C  
ATOM   4793  O   ALA B 371      40.894 -32.806  51.863  1.00 99.93           O  
ANISOU 4793  O   ALA B 371    19940   9383   8646    837   6248   -354       O  
ATOM   4794  CB  ALA B 371      41.152 -29.633  51.964  1.00 99.92           C  
ANISOU 4794  CB  ALA B 371    19987   9186   8791    774   6543     82       C  
ATOM   4795  N   ALA B 372      39.516 -32.063  53.482  1.00100.05           N  
ANISOU 4795  N   ALA B 372    19623   9518   8875    843   5651   -176       N  
ATOM   4796  CA  ALA B 372      39.631 -33.308  54.234  1.00100.82           C  
ANISOU 4796  CA  ALA B 372    19402   9686   9221    832   5530   -349       C  
ATOM   4797  C   ALA B 372      38.873 -34.437  53.549  1.00106.89           C  
ANISOU 4797  C   ALA B 372    20490  10521   9604    895   5279   -502       C  
ATOM   4798  O   ALA B 372      39.384 -35.557  53.434  1.00107.89           O  
ANISOU 4798  O   ALA B 372    20539  10645   9810    898   5388   -696       O  
ATOM   4799  CB  ALA B 372      39.123 -33.110  55.661  1.00 92.59           C  
ANISOU 4799  CB  ALA B 372    17964   8718   8500    813   5235   -283       C  
ATOM   4800  N   PHE B 373      37.646 -34.166  53.098  1.00111.63           N  
ANISOU 4800  N   PHE B 373    21435  11181   9799    950   4923   -434       N  
ATOM   4801  CA  PHE B 373      36.884 -35.189  52.392  1.00116.18           C  
ANISOU 4801  CA  PHE B 373    22325  11818   9999   1002   4651   -599       C  
ATOM   4802  C   PHE B 373      37.517 -35.536  51.048  1.00130.64           C  
ANISOU 4802  C   PHE B 373    24526  13588  11522   1029   4960   -703       C  
ATOM   4803  O   PHE B 373      37.415 -36.682  50.594  1.00137.67           O  
ANISOU 4803  O   PHE B 373    25547  14503  12258   1053   4886   -917       O  
ATOM   4804  CB  PHE B 373      35.440 -34.725  52.199  1.00113.84           C  
ANISOU 4804  CB  PHE B 373    22290  11607   9357   1056   4173   -505       C  
ATOM   4805  CG  PHE B 373      34.696 -34.490  53.487  1.00110.32           C  
ANISOU 4805  CG  PHE B 373    21506  11232   9180   1034   3846   -428       C  
ATOM   4806  CD1 PHE B 373      34.641 -35.469  54.465  1.00105.89           C  
ANISOU 4806  CD1 PHE B 373    20611  10703   8918    993   3720   -564       C  
ATOM   4807  CD2 PHE B 373      34.054 -33.283  53.719  1.00110.94           C  
ANISOU 4807  CD2 PHE B 373    21604  11337   9210   1060   3672   -223       C  
ATOM   4808  CE1 PHE B 373      33.958 -35.252  55.648  1.00 93.50           C  
ANISOU 4808  CE1 PHE B 373    18755   9196   7575    972   3442   -492       C  
ATOM   4809  CE2 PHE B 373      33.371 -33.060  54.899  1.00101.76           C  
ANISOU 4809  CE2 PHE B 373    20134  10245   8286   1042   3388   -160       C  
ATOM   4810  CZ  PHE B 373      33.322 -34.045  55.865  1.00 91.85           C  
ANISOU 4810  CZ  PHE B 373    18569   9024   7307    994   3281   -292       C  
ATOM   4811  N   SER B 374      38.175 -34.569  50.402  1.00138.98           N  
ANISOU 4811  N   SER B 374    25759  14555  12491   1025   5316   -566       N  
ATOM   4812  CA  SER B 374      38.846 -34.851  49.136  1.00145.46           C  
ANISOU 4812  CA  SER B 374    26939  15308  13020   1047   5663   -658       C  
ATOM   4813  C   SER B 374      40.027 -35.792  49.323  1.00147.59           C  
ANISOU 4813  C   SER B 374    26923  15533  13622   1005   6021   -853       C  
ATOM   4814  O   SER B 374      40.307 -36.619  48.448  1.00150.10           O  
ANISOU 4814  O   SER B 374    27486  15840  13705   1039   6161  -1033       O  
ATOM   4815  CB  SER B 374      39.292 -33.546  48.478  1.00147.64           C  
ANISOU 4815  CB  SER B 374    27459  15479  13159   1044   5986   -456       C  
ATOM   4816  OG  SER B 374      38.178 -32.816  47.995  1.00150.53           O  
ANISOU 4816  OG  SER B 374    28194  15887  13113   1118   5649   -307       O  
ATOM   4817  N   TRP B 375      40.722 -35.685  50.453  1.00146.88           N  
ANISOU 4817  N   TRP B 375    26310  15421  14077    941   6154   -830       N  
ATOM   4818  CA  TRP B 375      41.833 -36.587  50.729  1.00147.68           C  
ANISOU 4818  CA  TRP B 375    26084  15489  14539    918   6445  -1019       C  
ATOM   4819  C   TRP B 375      41.310 -37.961  51.114  1.00146.54           C  
ANISOU 4819  C   TRP B 375    25835  15423  14422    962   6122  -1228       C  
ATOM   4820  O   TRP B 375      41.850 -38.988  50.684  1.00150.13           O  
ANISOU 4820  O   TRP B 375    26307  15855  14882    994   6284  -1445       O  
ATOM   4821  CB  TRP B 375      42.722 -36.006  51.828  1.00144.30           C  
ANISOU 4821  CB  TRP B 375    25121  15021  14686    845   6643   -936       C  
ATOM   4822  CG  TRP B 375      43.463 -37.033  52.630  1.00145.88           C  
ANISOU 4822  CG  TRP B 375    24853  15240  15336    847   6695  -1120       C  
ATOM   4823  CD1 TRP B 375      44.606 -37.690  52.273  1.00150.70           C  
ANISOU 4823  CD1 TRP B 375    25338  15794  16126    855   7058  -1297       C  
ATOM   4824  CD2 TRP B 375      43.119 -37.507  53.936  1.00143.70           C  
ANISOU 4824  CD2 TRP B 375    24170  15040  15391    854   6367  -1145       C  
ATOM   4825  NE1 TRP B 375      44.989 -38.550  53.275  1.00150.44           N  
ANISOU 4825  NE1 TRP B 375    24841  15800  16521    881   6949  -1431       N  
ATOM   4826  CE2 TRP B 375      44.093 -38.456  54.307  1.00144.42           C  
ANISOU 4826  CE2 TRP B 375    23908  15115  15850    879   6529  -1336       C  
ATOM   4827  CE3 TRP B 375      42.080 -37.224  54.827  1.00138.41           C  
ANISOU 4827  CE3 TRP B 375    23404  14446  14740    850   5955  -1027       C  
ATOM   4828  CZ2 TRP B 375      44.057 -39.122  55.531  1.00136.72           C  
ANISOU 4828  CZ2 TRP B 375    22509  14193  15245    908   6277  -1401       C  
ATOM   4829  CZ3 TRP B 375      42.046 -37.885  56.039  1.00129.64           C  
ANISOU 4829  CZ3 TRP B 375    21877  13388  13992    863   5736  -1093       C  
ATOM   4830  CH2 TRP B 375      43.028 -38.823  56.381  1.00129.83           C  
ANISOU 4830  CH2 TRP B 375    21574  13391  14365    895   5890  -1274       C  
ATOM   4831  N   TRP B 376      40.257 -37.994  51.928  1.00141.70           N  
ANISOU 4831  N   TRP B 376    25112  14889  13839    965   5672  -1173       N  
ATOM   4832  CA  TRP B 376      39.664 -39.258  52.338  1.00142.30           C  
ANISOU 4832  CA  TRP B 376    25098  15016  13953    995   5345  -1366       C  
ATOM   4833  C   TRP B 376      38.979 -39.952  51.167  1.00144.16           C  
ANISOU 4833  C   TRP B 376    25817  15270  13686   1046   5181  -1527       C  
ATOM   4834  O   TRP B 376      38.846 -41.182  51.166  1.00145.40           O  
ANISOU 4834  O   TRP B 376    25950  15426  13871   1071   5052  -1760       O  
ATOM   4835  CB  TRP B 376      38.671 -38.997  53.468  1.00142.48           C  
ANISOU 4835  CB  TRP B 376    24909  15110  14118    974   4927  -1252       C  
ATOM   4836  CG  TRP B 376      37.898 -40.183  53.911  1.00147.82           C  
ANISOU 4836  CG  TRP B 376    25522  15819  14822    989   4559  -1430       C  
ATOM   4837  CD1 TRP B 376      38.278 -41.104  54.839  1.00148.88           C  
ANISOU 4837  CD1 TRP B 376    25275  15931  15363    992   4536  -1555       C  
ATOM   4838  CD2 TRP B 376      36.593 -40.573  53.467  1.00150.92           C  
ANISOU 4838  CD2 TRP B 376    26236  16262  14845   1003   4141  -1509       C  
ATOM   4839  NE1 TRP B 376      37.296 -42.052  54.995  1.00149.90           N  
ANISOU 4839  NE1 TRP B 376    25481  16070  15406    996   4157  -1704       N  
ATOM   4840  CE2 TRP B 376      36.251 -41.748  54.163  1.00151.28           C  
ANISOU 4840  CE2 TRP B 376    26072  16293  15114    994   3906  -1689       C  
ATOM   4841  CE3 TRP B 376      35.685 -40.045  52.544  1.00152.92           C  
ANISOU 4841  CE3 TRP B 376    26925  16566  14614   1025   3923  -1451       C  
ATOM   4842  CZ2 TRP B 376      35.039 -42.405  53.967  1.00151.68           C  
ANISOU 4842  CZ2 TRP B 376    26320  16369  14941    984   3477  -1826       C  
ATOM   4843  CZ3 TRP B 376      34.482 -40.700  52.350  1.00154.04           C  
ANISOU 4843  CZ3 TRP B 376    27249  16757  14523   1029   3468  -1590       C  
ATOM   4844  CH2 TRP B 376      34.170 -41.867  53.058  1.00153.40           C  
ANISOU 4844  CH2 TRP B 376    26939  16652  14695    997   3257  -1783       C  
ATOM   4845  N   LEU B 377      38.560 -39.193  50.161  1.00143.06           N  
ANISOU 4845  N   LEU B 377    26122  15141  13095   1067   5176  -1418       N  
ATOM   4846  CA  LEU B 377      37.981 -39.771  48.958  1.00141.80           C  
ANISOU 4846  CA  LEU B 377    26447  15006  12426   1122   5029  -1574       C  
ATOM   4847  C   LEU B 377      39.013 -39.789  47.837  1.00142.51           C  
ANISOU 4847  C   LEU B 377    26797  15022  12330   1145   5516  -1640       C  
ATOM   4848  O   LEU B 377      38.781 -40.364  46.776  1.00142.80           O  
ANISOU 4848  O   LEU B 377    27231  15070  11958   1195   5484  -1803       O  
ATOM   4849  CB  LEU B 377      36.736 -38.992  48.525  1.00141.31           C  
ANISOU 4849  CB  LEU B 377    26735  15015  11942   1153   4640  -1426       C  
ATOM   4850  CG  LEU B 377      35.369 -39.571  48.895  1.00137.88           C  
ANISOU 4850  CG  LEU B 377    26303  14672  11413   1159   4051  -1525       C  
ATOM   4851  CD1 LEU B 377      34.305 -38.494  48.787  1.00136.74           C  
ANISOU 4851  CD1 LEU B 377    26351  14597  11005   1190   3703  -1315       C  
ATOM   4852  CD2 LEU B 377      35.023 -40.753  47.999  1.00142.55           C  
ANISOU 4852  CD2 LEU B 377    27192  15279  11691   1192   3894  -1818       C  
TER    4853      LEU B 377                                                      
HETATM 4854  C1  NT5 A 401      24.617  -4.571  94.589  1.00 53.97           C  
HETATM 4855  C10 NT5 A 401      27.153   4.599  96.357  1.00 47.59           C  
HETATM 4856  C11 NT5 A 401      26.109   4.068  95.598  1.00 44.72           C  
HETATM 4857  C12 NT5 A 401      26.711  -2.267  94.965  1.00 47.20           C  
HETATM 4858  C13 NT5 A 401      25.299  -2.277  97.095  1.00 49.56           C  
HETATM 4859  C14 NT5 A 401      26.407  -1.692  97.943  1.00 48.46           C  
HETATM 4860  C15 NT5 A 401      26.283  -0.348  98.313  1.00 48.63           C  
HETATM 4861  C16 NT5 A 401      27.254   0.275  99.089  1.00 43.34           C  
HETATM 4862  C17 NT5 A 401      28.362  -0.443  99.511  1.00 40.15           C  
HETATM 4863  C18 NT5 A 401      28.494  -1.779  99.150  1.00 42.25           C  
HETATM 4864  C19 NT5 A 401      27.540  -2.452  98.369  1.00 49.49           C  
HETATM 4865  C2  NT5 A 401      24.351  -3.108  95.009  1.00 43.47           C  
HETATM 4866  C20 NT5 A 401      27.786  -3.918  98.030  1.00 54.77           C  
HETATM 4867  C21 NT5 A 401      26.946  -5.993  97.321  1.00 54.51           C  
HETATM 4868  C22 NT5 A 401      28.207  -6.565  97.398  1.00 52.38           C  
HETATM 4869  C23 NT5 A 401      29.236  -5.725  97.811  1.00 59.70           C  
HETATM 4870  C24 NT5 A 401      27.101   1.731  99.480  1.00 45.07           C  
HETATM 4871  C3  NT5 A 401      23.993  -2.231  93.789  1.00 46.92           C  
HETATM 4872  C4  NT5 A 401      25.200  -1.847  92.929  1.00 50.85           C  
HETATM 4873  C5  NT5 A 401      26.346  -1.322  93.800  1.00 49.27           C  
HETATM 4874  C6  NT5 A 401      26.098   0.120  94.290  1.00 48.89           C  
HETATM 4875  C7  NT5 A 401      27.151   1.982  95.478  1.00 40.17           C  
HETATM 4876  C8  NT5 A 401      28.228   2.450  96.234  1.00 47.14           C  
HETATM 4877  C9  NT5 A 401      28.228   3.774  96.678  1.00 46.91           C  
HETATM 4878  F1  NT5 A 401      27.120   5.883  96.769  1.00 54.76           F  
HETATM 4879  N1  NT5 A 401      26.091   2.785  95.158  1.00 42.49           N  
HETATM 4880  N2  NT5 A 401      25.482  -2.518  95.755  1.00 47.85           N  
HETATM 4881  N3  NT5 A 401      26.735  -4.692  97.633  1.00 53.62           N  
HETATM 4882  N4  NT5 A 401      29.054  -4.412  98.128  1.00 60.47           N  
HETATM 4883  O1  NT5 A 401      27.174   0.666  95.049  1.00 41.56           O  
HETATM 4884  O2  NT5 A 401      24.236  -2.536  97.671  1.00 51.30           O  
HETATM 4885  H12 NT5 A 401      23.785  -4.983  94.306  1.00 65.94           H  
HETATM 4886  H11 NT5 A 401      24.981  -5.062  95.342  1.00 65.94           H  
HETATM 4887  H13 NT5 A 401      25.251  -4.587  93.855  1.00 65.94           H  
HETATM 4888 H111 NT5 A 401      25.392   4.620  95.384  1.00 54.84           H  
HETATM 4889 H122 NT5 A 401      27.380  -1.847  95.528  1.00 57.82           H  
HETATM 4890 H121 NT5 A 401      27.047  -3.106  94.611  1.00 57.82           H  
HETATM 4891 H151 NT5 A 401      25.539   0.136  98.035  1.00 59.54           H  
HETATM 4892 H171 NT5 A 401      29.014  -0.032 100.032  1.00 49.36           H  
HETATM 4893 H181 NT5 A 401      29.245  -2.246  99.438  1.00 51.87           H  
HETATM 4894  H21 NT5 A 401      23.582  -3.053  95.598  1.00 53.34           H  
HETATM 4895 H211 NT5 A 401      26.227  -6.517  97.049  1.00 66.59           H  
HETATM 4896 H221 NT5 A 401      28.357  -7.458  97.186  1.00 64.03           H  
HETATM 4897 H231 NT5 A 401      30.094  -6.078  97.873  1.00 72.82           H  
HETATM 4898 H241 NT5 A 401      26.175   2.000  99.371  1.00 55.26           H  
HETATM 4899 H243 NT5 A 401      27.665   2.280  98.912  1.00 55.26           H  
HETATM 4900 H242 NT5 A 401      27.364   1.847 100.406  1.00 55.26           H  
HETATM 4901  H32 NT5 A 401      23.362  -2.717  93.236  1.00 57.48           H  
HETATM 4902  H31 NT5 A 401      23.571  -1.418  94.108  1.00 57.48           H  
HETATM 4903  H42 NT5 A 401      24.936  -1.157  92.300  1.00 62.20           H  
HETATM 4904  H41 NT5 A 401      25.503  -2.627  92.439  1.00 62.20           H  
HETATM 4905  H51 NT5 A 401      27.118  -1.327  93.213  1.00 60.31           H  
HETATM 4906  H61 NT5 A 401      25.298   0.126  94.839  1.00 59.85           H  
HETATM 4907  H62 NT5 A 401      25.945   0.686  93.518  1.00 59.85           H  
HETATM 4908  H81 NT5 A 401      28.938   1.885  96.440  1.00 57.75           H  
HETATM 4909  H91 NT5 A 401      28.938   4.101  97.182  1.00 57.48           H  
HETATM 4910  O1  PG4 A 402      20.975   3.619 103.331  1.00101.13           O  
HETATM 4911  C1  PG4 A 402      20.045   2.659 102.869  1.00101.07           C  
HETATM 4912  C2  PG4 A 402      20.117   2.466 101.387  1.00102.92           C  
HETATM 4913  O2  PG4 A 402      19.096   1.567 100.969  1.00108.31           O  
HETATM 4914  C3  PG4 A 402      19.043   1.414  99.555  1.00110.92           C  
HETATM 4915  C4  PG4 A 402      20.259   0.687  99.073  1.00110.58           C  
HETATM 4916  O3  PG4 A 402      20.924   1.451  98.073  1.00108.51           O  
HETATM 4917  C5  PG4 A 402      22.033   2.183  98.584  1.00 97.50           C  
HETATM 4918  C6  PG4 A 402      22.783   2.817  97.454  1.00 82.07           C  
HETATM 4919  O4  PG4 A 402      23.103   1.828  96.483  1.00 77.23           O  
HETATM 4920  C7  PG4 A 402      22.220   1.838  95.366  1.00 63.58           C  
HETATM 4921  C8  PG4 A 402      21.753   0.447  95.071  1.00 62.88           C  
HETATM 4922  O5  PG4 A 402      21.339   0.295  93.724  1.00 62.39           O  
HETATM 4923  S   SO4 A 403      55.041 -22.356  97.106  1.00108.09           S  
HETATM 4924  O1  SO4 A 403      54.568 -23.378  96.178  1.00112.04           O  
HETATM 4925  O2  SO4 A 403      54.933 -21.037  96.489  1.00106.87           O  
HETATM 4926  O3  SO4 A 403      54.225 -22.384  98.316  1.00103.97           O  
HETATM 4927  O4  SO4 A 403      56.438 -22.619  97.440  1.00114.57           O  
HETATM 4928  S   SO4 A 404      55.888 -14.738 107.217  1.00129.89           S  
HETATM 4929  O1  SO4 A 404      56.381 -13.368 107.330  1.00131.31           O  
HETATM 4930  O2  SO4 A 404      55.361 -14.965 105.874  1.00133.44           O  
HETATM 4931  O3  SO4 A 404      54.820 -14.949 108.190  1.00122.46           O  
HETATM 4932  O4  SO4 A 404      56.984 -15.667 107.476  1.00133.64           O  
HETATM 4933  C1  SOG A 405      14.151  10.849 115.406  1.00 64.34           C  
HETATM 4934  C2  SOG A 405      14.222  12.297 114.957  1.00 60.26           C  
HETATM 4935  C3  SOG A 405      12.874  12.957 115.233  1.00 65.64           C  
HETATM 4936  C4  SOG A 405      11.714  12.150 114.655  1.00 66.75           C  
HETATM 4937  C5  SOG A 405      11.851  10.647 114.949  1.00 66.91           C  
HETATM 4938  C6  SOG A 405      10.876   9.783 114.168  1.00 71.49           C  
HETATM 4939  C1' SOG A 405      16.267  10.244 113.627  1.00 57.74           C  
HETATM 4940  C2' SOG A 405      17.426   9.315 113.331  1.00 49.79           C  
HETATM 4941  C3' SOG A 405      18.179   9.652 112.059  1.00 48.18           C  
HETATM 4942  C4' SOG A 405      19.342  10.601 112.268  1.00 44.45           C  
HETATM 4943  C5' SOG A 405      20.284  10.708 111.082  1.00 42.97           C  
HETATM 4944  C6' SOG A 405      21.434  11.675 111.275  1.00 48.27           C  
HETATM 4945  C7' SOG A 405      22.427  11.797 110.139  1.00 58.31           C  
HETATM 4946  C8' SOG A 405      23.275  10.574 109.873  1.00 64.41           C  
HETATM 4947  S1  SOG A 405      15.722   9.952 115.344  1.00 70.15           S  
HETATM 4948  O2  SOG A 405      15.235  12.990 115.678  1.00 59.88           O  
HETATM 4949  O3  SOG A 405      12.860  14.292 114.733  1.00 71.39           O  
HETATM 4950  O4  SOG A 405      10.477  12.625 115.184  1.00 76.73           O  
HETATM 4951  O5  SOG A 405      13.172  10.181 114.629  1.00 68.95           O  
HETATM 4952  O6  SOG A 405       9.661   9.572 114.887  1.00 88.05           O  
HETATM 4953  C1  SOG A 406      10.143 -15.552  95.459  1.00110.22           C  
HETATM 4954  C2  SOG A 406      10.110 -16.052  96.898  1.00112.53           C  
HETATM 4955  C3  SOG A 406       8.834 -15.564  97.577  1.00111.94           C  
HETATM 4956  C4  SOG A 406       8.678 -14.063  97.432  1.00108.27           C  
HETATM 4957  C5  SOG A 406       8.811 -13.664  95.964  1.00111.88           C  
HETATM 4958  C6  SOG A 406       8.763 -12.162  95.746  1.00119.67           C  
HETATM 4959  C1' SOG A 406      11.243 -15.559  92.898  1.00 99.58           C  
HETATM 4960  C2' SOG A 406      11.924 -16.370  91.816  1.00 87.01           C  
HETATM 4961  C3' SOG A 406      13.003 -15.602  91.086  1.00 74.24           C  
HETATM 4962  C4' SOG A 406      14.283 -15.457  91.874  1.00 67.71           C  
HETATM 4963  C5' SOG A 406      15.308 -16.545  91.630  1.00 57.65           C  
HETATM 4964  C6' SOG A 406      16.102 -16.384  90.352  1.00 49.49           C  
HETATM 4965  C7' SOG A 406      17.215 -17.388  90.163  1.00 53.90           C  
HETATM 4966  C8' SOG A 406      18.123 -17.100  88.989  1.00 57.62           C  
HETATM 4967  S1  SOG A 406      11.633 -16.103  94.596  1.00108.41           S  
HETATM 4968  O2  SOG A 406      10.127 -17.475  96.920  1.00115.41           O  
HETATM 4969  O3  SOG A 406       8.819 -15.944  98.952  1.00114.42           O  
HETATM 4970  O4  SOG A 406       7.408 -13.648  97.926  1.00102.84           O  
HETATM 4971  O5  SOG A 406      10.064 -14.134  95.441  1.00109.22           O  
HETATM 4972  O6  SOG A 406       7.473 -11.637  96.057  1.00126.66           O  
HETATM 4973  C1  SOG A 407      16.043  -2.314  80.538  1.00143.00           C  
HETATM 4974  C2  SOG A 407      15.420  -2.564  81.907  1.00139.37           C  
HETATM 4975  C3  SOG A 407      15.588  -4.030  82.299  1.00142.79           C  
HETATM 4976  C4  SOG A 407      15.084  -4.945  81.202  1.00147.46           C  
HETATM 4977  C5  SOG A 407      15.760  -4.580  79.888  1.00145.25           C  
HETATM 4978  C6  SOG A 407      15.260  -5.404  78.716  1.00140.30           C  
HETATM 4979  C1' SOG A 407      13.918  -0.780  79.615  1.00138.85           C  
HETATM 4980  S1  SOG A 407      15.699  -0.635  79.977  1.00143.53           S  
HETATM 4981  O2  SOG A 407      16.047  -1.748  82.890  1.00134.45           O  
HETATM 4982  O3  SOG A 407      14.915  -4.298  83.527  1.00142.93           O  
HETATM 4983  O4  SOG A 407      15.369  -6.304  81.518  1.00151.10           O  
HETATM 4984  O5  SOG A 407      15.493  -3.204  79.578  1.00145.77           O  
HETATM 4985  O6  SOG A 407      16.314  -6.181  78.153  1.00138.06           O  
HETATM 4986  C1  SOG A 408      16.908   5.011 119.678  1.00142.19           C  
HETATM 4987  C2  SOG A 408      16.122   3.888 119.005  1.00144.91           C  
HETATM 4988  C3  SOG A 408      15.354   4.430 117.802  1.00142.85           C  
HETATM 4989  C4  SOG A 408      14.551   5.666 118.166  1.00140.67           C  
HETATM 4990  C5  SOG A 408      15.459   6.684 118.845  1.00137.37           C  
HETATM 4991  C6  SOG A 408      14.729   7.932 119.308  1.00138.05           C  
HETATM 4992  C1' SOG A 408      19.275   3.777 120.531  1.00137.61           C  
HETATM 4993  C2' SOG A 408      20.168   3.412 121.693  1.00131.80           C  
HETATM 4994  C3' SOG A 408      21.399   2.639 121.285  1.00128.10           C  
HETATM 4995  C4' SOG A 408      22.236   2.225 122.472  1.00126.86           C  
HETATM 4996  C5' SOG A 408      23.538   1.541 122.126  1.00127.71           C  
HETATM 4997  C6' SOG A 408      24.495   1.440 123.291  1.00127.53           C  
HETATM 4998  C7' SOG A 408      25.923   1.075 122.963  1.00124.80           C  
HETATM 4999  C8' SOG A 408      26.144  -0.351 122.515  1.00124.70           C  
HETATM 5000  S1  SOG A 408      17.725   4.470 121.194  1.00142.29           S  
HETATM 5001  O2  SOG A 408      17.002   2.858 118.569  1.00148.46           O  
HETATM 5002  O3  SOG A 408      14.504   3.422 117.258  1.00142.97           O  
HETATM 5003  O4  SOG A 408      13.971   6.244 117.000  1.00143.55           O  
HETATM 5004  O5  SOG A 408      16.047   6.089 120.011  1.00138.73           O  
HETATM 5005  O6  SOG A 408      14.265   8.707 118.206  1.00139.00           O  
HETATM 5006  C5' SOG A 409      29.594   1.040 113.822  1.00 67.05           C  
HETATM 5007  C6' SOG A 409      29.283   2.228 112.947  1.00 66.45           C  
HETATM 5008  C7' SOG A 409      28.813   1.860 111.564  1.00 62.23           C  
HETATM 5009  C8' SOG A 409      28.506   3.053 110.692  1.00 52.23           C  
HETATM 5010 CL    CL A 410      19.862   7.476  96.686  1.00 68.28          CL  
HETATM 5011  CAD PGW A 411      33.854 -35.860 101.077  1.00119.20           C  
HETATM 5012  OAE PGW A 411      33.445 -36.341 102.354  1.00118.81           O  
HETATM 5013  OAF PGW A 411      35.394 -37.533 100.268  1.00118.53           O  
HETATM 5014  P   PGW A 411      37.775 -34.043 101.360  1.00131.58           P  
HETATM 5015  C01 PGW A 411      33.641 -31.771 100.332  1.00 97.81           C  
HETATM 5016  C1  PGW A 411      36.151 -30.839  98.046  1.00 81.57           C  
HETATM 5017  O01 PGW A 411      35.530 -30.700  99.229  1.00 95.12           O  
HETATM 5018  C02 PGW A 411      35.089 -31.904  99.919  1.00103.07           C  
HETATM 5019  C2  PGW A 411      37.147 -29.742  97.772  1.00 71.95           C  
HETATM 5020  O02 PGW A 411      35.898 -31.741  97.291  1.00 85.32           O  
HETATM 5021  C03 PGW A 411      35.994 -32.121 101.112  1.00116.81           C  
HETATM 5022  C3  PGW A 411      37.002 -29.110  96.421  1.00 63.37           C  
HETATM 5023  O03 PGW A 411      32.799 -31.613  99.169  1.00 93.48           O  
HETATM 5024  C04 PGW A 411      35.972 -35.243  99.838  1.00119.95           C  
HETATM 5025  C4  PGW A 411      38.021 -28.005  96.177  1.00 63.70           C  
HETATM 5026  O04 PGW A 411      31.381 -33.157  99.923  1.00 94.87           O  
HETATM 5027  C05 PGW A 411      35.299 -36.206 100.788  1.00119.02           C  
HETATM 5028  C5  PGW A 411      38.049 -27.504  94.752  1.00 67.03           C  
HETATM 5029  C06 PGW A 411      38.123 -21.547  92.719  1.00 64.99           C  
HETATM 5030  C6  PGW A 411      39.064 -26.421  94.461  1.00 58.99           C  
HETATM 5031  C07 PGW A 411      37.201 -20.413  92.395  1.00 75.17           C  
HETATM 5032  C7  PGW A 411      38.678 -25.037  94.965  1.00 53.71           C  
HETATM 5033  C08 PGW A 411      36.996 -20.156  90.915  1.00 79.33           C  
HETATM 5034  C8  PGW A 411      39.453 -23.911  94.349  1.00 56.89           C  
HETATM 5035  C09 PGW A 411      35.994 -19.067  90.619  1.00 83.51           C  
HETATM 5036  C9  PGW A 411      39.020 -22.569  94.851  1.00 59.49           C  
HETATM 5037  C10 PGW A 411      38.454 -21.600  94.178  1.00 61.06           C  
HETATM 5038  C11 PGW A 411      34.930 -19.481  89.636  1.00 87.67           C  
HETATM 5039  O11 PGW A 411      37.307 -32.631 100.753  1.00127.26           O  
HETATM 5040  C12 PGW A 411      33.510 -19.239  90.090  1.00 86.08           C  
HETATM 5041  O12 PGW A 411      37.372 -35.078 100.199  1.00124.76           O  
HETATM 5042  C13 PGW A 411      33.055 -17.803  90.133  1.00 85.96           C  
HETATM 5043  O13 PGW A 411      39.276 -34.060 101.448  1.00131.91           O  
HETATM 5044  C14 PGW A 411      31.556 -17.676  89.985  1.00 87.37           C  
HETATM 5045  O14 PGW A 411      36.945 -34.314 102.585  1.00131.94           O  
HETATM 5046  C15 PGW A 411      29.451 -23.993  97.478  1.00 61.26           C  
HETATM 5047  C16 PGW A 411      29.676 -23.417  96.103  1.00 56.22           C  
HETATM 5048  C17 PGW A 411      29.213 -24.307  94.975  1.00 48.20           C  
HETATM 5049  C18 PGW A 411      29.750 -23.908  93.625  1.00 51.79           C  
HETATM 5050  C19 PGW A 411      31.599 -32.178  99.258  1.00 91.38           C  
HETATM 5051  C20 PGW A 411      30.563 -31.413  98.486  1.00 80.50           C  
HETATM 5052  C21 PGW A 411      30.121 -30.162  99.182  1.00 60.43           C  
HETATM 5053  C22 PGW A 411      29.075 -29.389  98.396  1.00 54.63           C  
HETATM 5054  C23 PGW A 411      28.586 -28.132  99.078  1.00 65.01           C  
HETATM 5055  C24 PGW A 411      27.472 -27.423  98.342  1.00 72.84           C  
HETATM 5056  C25 PGW A 411      26.901 -26.228  99.070  1.00 80.55           C  
HETATM 5057  C26 PGW A 411      27.813 -25.027  99.109  1.00 81.03           C  
HETATM 5058  C27 PGW A 411      28.022 -24.377  97.764  1.00 71.90           C  
HETATM 5059  C28 PGW A 411      29.292 -24.775  92.480  1.00 55.11           C  
HETATM 5060  C29 PGW A 411      29.867 -25.194  90.033  1.00 47.08           C  
HETATM 5061  C30 PGW A 411      30.363 -24.882  91.425  1.00 49.95           C  
HETATM 5062  C1  NT5 B 401      25.184 -32.007  86.906  1.00 58.26           C  
HETATM 5063  C10 NT5 B 401      27.187 -40.474  82.499  1.00 61.29           C  
HETATM 5064  C11 NT5 B 401      26.740 -40.159  83.784  1.00 64.73           C  
HETATM 5065  C12 NT5 B 401      26.648 -33.814  84.847  1.00 62.92           C  
HETATM 5066  C13 NT5 B 401      24.192 -34.253  84.341  1.00 51.04           C  
HETATM 5067  C14 NT5 B 401      24.486 -34.650  82.913  1.00 58.25           C  
HETATM 5068  C15 NT5 B 401      24.427 -36.014  82.603  1.00 68.37           C  
HETATM 5069  C16 NT5 B 401      24.683 -36.472  81.316  1.00 68.46           C  
HETATM 5070  C17 NT5 B 401      24.999 -35.568  80.315  1.00 66.04           C  
HETATM 5071  C18 NT5 B 401      25.058 -34.211  80.612  1.00 67.34           C  
HETATM 5072  C19 NT5 B 401      24.807 -33.697  81.896  1.00 63.78           C  
HETATM 5073  C2  NT5 B 401      24.859 -33.478  86.567  1.00 54.36           C  
HETATM 5074  C20 NT5 B 401      24.908 -32.187  82.098  1.00 59.36           C  
HETATM 5075  C21 NT5 B 401      24.414 -30.269  83.358  1.00 57.15           C  
HETATM 5076  C22 NT5 B 401      25.105 -29.467  82.460  1.00 61.88           C  
HETATM 5077  C23 NT5 B 401      25.686 -30.116  81.377  1.00 62.29           C  
HETATM 5078  C24 NT5 B 401      24.612 -37.956  81.016  1.00 73.24           C  
HETATM 5079  C3  NT5 B 401      25.571 -34.458  87.530  1.00 57.46           C  
HETATM 5080  C4  NT5 B 401      27.067 -34.626  87.242  1.00 60.94           C  
HETATM 5081  C5  NT5 B 401      27.333 -34.864  85.749  1.00 60.98           C  
HETATM 5082  C6  NT5 B 401      26.987 -36.298  85.302  1.00 50.62           C  
HETATM 5083  C7  NT5 B 401      27.390 -37.932  83.537  1.00 51.97           C  
HETATM 5084  C8  NT5 B 401      27.856 -38.179  82.246  1.00 56.07           C  
HETATM 5085  C9  NT5 B 401      27.754 -39.467  81.722  1.00 58.58           C  
HETATM 5086  F1  NT5 B 401      27.075 -41.728  82.016  1.00 67.32           F  
HETATM 5087  N1  NT5 B 401      26.832 -38.912  84.311  1.00 61.36           N  
HETATM 5088  N2  NT5 B 401      25.205 -33.870  85.183  1.00 53.70           N  
HETATM 5089  N3  NT5 B 401      24.314 -31.610  83.185  1.00 58.15           N  
HETATM 5090  N4  NT5 B 401      25.604 -31.461  81.177  1.00 56.68           N  
HETATM 5091  O1  NT5 B 401      27.510 -36.645  84.025  1.00 51.44           O  
HETATM 5092  O2  NT5 B 401      23.009 -34.272  84.692  1.00 54.25           O  
HETATM 5093  H12 NT5 B 401      24.733 -31.758  87.728  1.00 71.09           H  
HETATM 5094  H11 NT5 B 401      24.881 -31.434  86.184  1.00 71.09           H  
HETATM 5095  H13 NT5 B 401      26.142 -31.906  87.020  1.00 71.09           H  
HETATM 5096 H111 NT5 B 401      26.363 -40.833  84.301  1.00 78.86           H  
HETATM 5097 H122 NT5 B 401      26.782 -34.038  83.913  1.00 76.68           H  
HETATM 5098 H121 NT5 B 401      27.001 -32.930  85.037  1.00 76.68           H  
HETATM 5099 H151 NT5 B 401      24.214 -36.625  83.271  1.00 83.23           H  
HETATM 5100 H171 NT5 B 401      25.170 -35.867  79.451  1.00 80.43           H  
HETATM 5101 H181 NT5 B 401      25.274 -33.616  79.931  1.00 81.99           H  
HETATM 5102  H21 NT5 B 401      23.904 -33.614  86.667  1.00 66.42           H  
HETATM 5103 H211 NT5 B 401      24.010 -29.877  84.098  1.00 69.76           H  
HETATM 5104 H221 NT5 B 401      25.175 -28.547  82.576  1.00 75.44           H  
HETATM 5105 H231 NT5 B 401      26.155 -29.606  80.756  1.00 75.93           H  
HETATM 5106 H241 NT5 B 401      24.401 -38.440  81.830  1.00 89.07           H  
HETATM 5107 H243 NT5 B 401      25.467 -38.257  80.672  1.00 89.07           H  
HETATM 5108 H242 NT5 B 401      23.921 -38.119  80.355  1.00 89.07           H  
HETATM 5109  H32 NT5 B 401      25.466 -34.130  88.437  1.00 70.14           H  
HETATM 5110  H31 NT5 B 401      25.143 -35.326  87.458  1.00 70.14           H  
HETATM 5111  H42 NT5 B 401      27.403 -35.383  87.747  1.00 74.31           H  
HETATM 5112  H41 NT5 B 401      27.534 -33.823  87.521  1.00 74.31           H  
HETATM 5113  H51 NT5 B 401      28.289 -34.730  85.649  1.00 74.35           H  
HETATM 5114  H61 NT5 B 401      26.022 -36.390  85.277  1.00 61.93           H  
HETATM 5115  H62 NT5 B 401      27.338 -36.920  85.959  1.00 61.93           H  
HETATM 5116  H81 NT5 B 401      28.230 -37.493  81.741  1.00 68.47           H  
HETATM 5117  H91 NT5 B 401      28.060 -39.651  80.864  1.00 71.48           H  
HETATM 5118  C3  PG4 B 402      22.723 -41.084  81.685  1.00 81.50           C  
HETATM 5119  C4  PG4 B 402      22.409 -40.635  83.079  1.00 83.31           C  
HETATM 5120  O3  PG4 B 402      23.624 -40.440  83.794  1.00 83.03           O  
HETATM 5121  C5  PG4 B 402      23.429 -40.033  85.144  1.00 83.11           C  
HETATM 5122  C6  PG4 B 402      22.960 -38.613  85.199  1.00 82.45           C  
HETATM 5123  O4  PG4 B 402      23.436 -38.015  86.400  1.00 82.56           O  
HETATM 5124  C7  PG4 B 402      22.898 -38.612  87.575  1.00 80.57           C  
HETATM 5125  C8  PG4 B 402      23.766 -38.286  88.752  1.00 78.77           C  
HETATM 5126  O5  PG4 B 402      23.989 -36.897  88.894  1.00 74.95           O  
HETATM 5127  S   SO4 B 403      39.841  -8.287  65.064  1.00 83.91           S  
HETATM 5128  O1  SO4 B 403      38.425  -8.577  64.857  1.00 81.60           O  
HETATM 5129  O2  SO4 B 403      40.441  -7.804  63.823  1.00 93.71           O  
HETATM 5130  O3  SO4 B 403      40.520  -9.508  65.489  1.00 91.88           O  
HETATM 5131  O4  SO4 B 403      39.970  -7.256  66.089  1.00 76.95           O  
HETATM 5132  S   SO4 B 404      34.965 -16.570  56.617  1.00125.00           S  
HETATM 5133  O1  SO4 B 404      35.700 -16.263  55.393  1.00127.97           O  
HETATM 5134  O2  SO4 B 404      33.640 -17.081  56.283  1.00119.91           O  
HETATM 5135  O3  SO4 B 404      35.684 -17.587  57.378  1.00122.90           O  
HETATM 5136  O4  SO4 B 404      34.834 -15.353  57.415  1.00131.16           O  
HETATM 5137  C1  SOG B 405      35.993 -51.092  84.490  1.00100.54           C  
HETATM 5138  C2  SOG B 405      35.808 -52.140  85.580  1.00 93.17           C  
HETATM 5139  C3  SOG B 405      36.302 -51.581  86.911  1.00 92.52           C  
HETATM 5140  C4  SOG B 405      37.714 -51.043  86.787  1.00 98.15           C  
HETATM 5141  C5  SOG B 405      37.823 -50.081  85.606  1.00100.62           C  
HETATM 5142  C6  SOG B 405      39.248 -49.625  85.350  1.00103.13           C  
HETATM 5143  C1' SOG B 405      36.121 -50.422  81.785  1.00111.84           C  
HETATM 5144  C2' SOG B 405      35.660 -50.560  80.352  1.00107.97           C  
HETATM 5145  C3' SOG B 405      34.517 -49.629  80.020  1.00102.61           C  
HETATM 5146  C4' SOG B 405      34.936 -48.177  80.004  1.00 98.65           C  
HETATM 5147  C5' SOG B 405      33.929 -47.232  80.618  1.00 94.92           C  
HETATM 5148  C6' SOG B 405      33.234 -46.326  79.633  1.00 92.16           C  
HETATM 5149  C7' SOG B 405      34.130 -45.278  79.024  1.00 84.89           C  
HETATM 5150  C8' SOG B 405      33.928 -45.099  77.539  1.00 80.72           C  
HETATM 5151  S1  SOG B 405      35.426 -51.701  82.886  1.00112.20           S  
HETATM 5152  O2  SOG B 405      34.436 -52.496  85.706  1.00 90.91           O  
HETATM 5153  O3  SOG B 405      36.234 -52.578  87.929  1.00 86.88           O  
HETATM 5154  O4  SOG B 405      38.090 -50.362  87.981  1.00 97.62           O  
HETATM 5155  O5  SOG B 405      37.361 -50.722  84.405  1.00 99.56           O  
HETATM 5156  O6  SOG B 405      39.777 -48.933  86.480  1.00106.89           O  
HETATM 5157  C1  SOG B 406      12.253 -24.733  99.265  1.00104.16           C  
HETATM 5158  C2  SOG B 406      11.041 -25.270 100.018  1.00109.02           C  
HETATM 5159  C3  SOG B 406      11.201 -25.038 101.518  1.00108.22           C  
HETATM 5160  C4  SOG B 406      12.545 -25.536 102.008  1.00104.21           C  
HETATM 5161  C5  SOG B 406      13.649 -24.910 101.171  1.00 98.13           C  
HETATM 5162  C6  SOG B 406      15.034 -25.383 101.574  1.00 98.14           C  
HETATM 5163  C1' SOG B 406      13.820 -24.759  96.971  1.00 91.31           C  
HETATM 5164  C2' SOG B 406      14.136 -23.306  97.230  1.00 78.36           C  
HETATM 5165  C3' SOG B 406      15.542 -23.097  97.739  1.00 69.16           C  
HETATM 5166  C4' SOG B 406      16.506 -22.569  96.705  1.00 55.82           C  
HETATM 5167  C5' SOG B 406      17.891 -22.310  97.253  1.00 41.25           C  
HETATM 5168  C6' SOG B 406      18.800 -21.526  96.338  1.00 46.71           C  
HETATM 5169  C7' SOG B 406      20.162 -21.234  96.919  1.00 54.89           C  
HETATM 5170  C8' SOG B 406      21.015 -20.345  96.044  1.00 54.91           C  
HETATM 5171  S1  SOG B 406      12.128 -25.162  97.515  1.00101.39           S  
HETATM 5172  O2  SOG B 406       9.859 -24.617  99.568  1.00110.24           O  
HETATM 5173  O3  SOG B 406      10.140 -25.668 102.233  1.00111.09           O  
HETATM 5174  O4  SOG B 406      12.738 -25.192 103.377  1.00104.11           O  
HETATM 5175  O5  SOG B 406      13.457 -25.269  99.794  1.00 99.02           O  
HETATM 5176  O6  SOG B 406      15.304 -25.066 102.939  1.00105.71           O  
HETATM 5177  C1  SOG B 407      27.392 -32.988 103.554  1.00140.10           C  
HETATM 5178  C2  SOG B 407      27.019 -33.285 102.111  1.00129.45           C  
HETATM 5179  C3  SOG B 407      27.694 -34.584 101.686  1.00124.54           C  
HETATM 5180  C4  SOG B 407      29.190 -34.506 101.909  1.00127.13           C  
HETATM 5181  C5  SOG B 407      29.497 -34.081 103.341  1.00135.56           C  
HETATM 5182  C6  SOG B 407      30.978 -33.828 103.561  1.00137.44           C  
HETATM 5183  C1' SOG B 407      26.495 -31.819 105.913  1.00138.51           C  
HETATM 5184  C2' SOG B 407      25.988 -30.672 106.755  1.00132.94           C  
HETATM 5185  C3' SOG B 407      24.519 -30.378 106.564  1.00131.16           C  
HETATM 5186  C4' SOG B 407      24.027 -29.294 107.494  1.00131.32           C  
HETATM 5187  C5' SOG B 407      22.565 -28.952 107.353  1.00127.93           C  
HETATM 5188  C6' SOG B 407      22.099 -27.838 108.258  1.00125.72           C  
HETATM 5189  C7' SOG B 407      22.294 -28.118 109.726  1.00127.10           C  
HETATM 5190  C8' SOG B 407      21.949 -26.958 110.629  1.00127.37           C  
HETATM 5191  S1  SOG B 407      26.600 -31.468 104.126  1.00145.25           S  
HETATM 5192  O2  SOG B 407      25.609 -33.432 101.986  1.00126.66           O  
HETATM 5193  O3  SOG B 407      27.403 -34.876 100.321  1.00123.86           O  
HETATM 5194  O4  SOG B 407      29.796 -35.774 101.667  1.00124.52           O  
HETATM 5195  O5  SOG B 407      28.804 -32.860 103.657  1.00139.85           O  
HETATM 5196  O6  SOG B 407      31.298 -33.760 104.948  1.00136.75           O  
HETATM 5197  C1' SOG B 408      19.382 -17.161  77.019  1.00 95.32           C  
HETATM 5198  C2' SOG B 408      20.678 -16.921  76.284  1.00 94.70           C  
HETATM 5199  C3' SOG B 408      20.507 -16.919  74.784  1.00 89.17           C  
HETATM 5200  C4' SOG B 408      21.813 -16.802  74.037  1.00 86.51           C  
HETATM 5201  C5' SOG B 408      21.683 -16.912  72.538  1.00 86.65           C  
HETATM 5202  S1  SOG B 408      19.630 -17.349  78.816  1.00 95.26           S  
HETATM 5203  CAD PGW B 409      24.908  -0.924  72.128  1.00133.98           C  
HETATM 5204  OAE PGW B 409      24.540   0.233  71.383  1.00137.29           O  
HETATM 5205  OAF PGW B 409      22.580  -1.494  72.381  1.00134.88           O  
HETATM 5206  P   PGW B 409      22.209  -0.455  76.491  1.00126.48           P  
HETATM 5207  C01 PGW B 409      20.529  -4.523  78.965  1.00 95.09           C  
HETATM 5208  C1  PGW B 409      24.138  -4.100  78.743  1.00 74.90           C  
HETATM 5209  O01 PGW B 409      22.901  -4.599  78.589  1.00 84.49           O  
HETATM 5210  C02 PGW B 409      21.773  -3.692  78.746  1.00 95.97           C  
HETATM 5211  C2  PGW B 409      25.253  -5.005  78.279  1.00 65.72           C  
HETATM 5212  O02 PGW B 409      24.319  -3.021  79.244  1.00 82.86           O  
HETATM 5213  C03 PGW B 409      21.683  -2.840  77.498  1.00110.61           C  
HETATM 5214  C3  PGW B 409      26.166  -5.413  79.396  1.00 58.36           C  
HETATM 5215  O03 PGW B 409      20.598  -5.215  80.232  1.00 96.74           O  
HETATM 5216  C04 PGW B 409      23.607  -0.400  74.244  1.00131.38           C  
HETATM 5217  C4  PGW B 409      27.603  -5.675  78.959  1.00 54.39           C  
HETATM 5218  O04 PGW B 409      20.875  -3.359  81.445  1.00 93.83           O  
HETATM 5219  C05 PGW B 409      23.814  -1.349  73.085  1.00132.87           C  
HETATM 5220  C5  PGW B 409      27.883  -7.076  78.465  1.00 49.54           C  
HETATM 5221  C06 PGW B 409      32.014 -12.505  79.760  1.00 62.63           C  
HETATM 5222  C6  PGW B 409      29.272  -7.594  78.795  1.00 50.16           C  
HETATM 5223  C07 PGW B 409      31.195 -13.440  80.603  1.00 63.22           C  
HETATM 5224  C7  PGW B 409      29.567  -8.975  78.220  1.00 52.73           C  
HETATM 5225  C08 PGW B 409      31.952 -13.984  81.804  1.00 69.67           C  
HETATM 5226  C8  PGW B 409      30.847  -9.625  78.670  1.00 55.58           C  
HETATM 5227  C09 PGW B 409      31.126 -14.783  82.784  1.00 80.42           C  
HETATM 5228  C9  PGW B 409      31.062 -10.945  77.989  1.00 63.49           C  
HETATM 5229  C10 PGW B 409      31.392 -12.134  78.449  1.00 62.33           C  
HETATM 5230  C11 PGW B 409      31.901 -15.259  83.992  1.00 80.21           C  
HETATM 5231  O11 PGW B 409      22.222  -1.505  77.708  1.00121.84           O  
HETATM 5232  C12 PGW B 409      31.066 -15.964  85.033  1.00 79.69           C  
HETATM 5233  O12 PGW B 409      23.120  -1.170  75.379  1.00129.47           O  
HETATM 5234  C13 PGW B 409      31.837 -16.451  86.235  1.00 90.03           C  
HETATM 5235  O13 PGW B 409      20.818  -0.358  75.924  1.00129.25           O  
HETATM 5236  C14 PGW B 409      32.510 -15.350  87.019  1.00 94.86           C  
HETATM 5237  O14 PGW B 409      22.909   0.795  76.947  1.00125.19           O  
HETATM 5238  C15 PGW B 409      22.408 -12.888  83.438  1.00 56.83           C  
HETATM 5239  C16 PGW B 409      22.715 -12.214  84.755  1.00 50.47           C  
HETATM 5240  C17 PGW B 409      24.192 -12.006  85.002  1.00 48.96           C  
HETATM 5241  C18 PGW B 409      24.526 -11.312  86.300  1.00 48.69           C  
HETATM 5242  C19 PGW B 409      20.458  -4.482  81.334  1.00 92.25           C  
HETATM 5243  C20 PGW B 409      19.667  -5.227  82.374  1.00 81.17           C  
HETATM 5244  C21 PGW B 409      20.243  -6.568  82.693  1.00 65.23           C  
HETATM 5245  C22 PGW B 409      19.196  -7.581  83.121  1.00 58.30           C  
HETATM 5246  C23 PGW B 409      19.762  -8.959  83.349  1.00 59.34           C  
HETATM 5247  C24 PGW B 409      18.749 -10.017  83.708  1.00 67.36           C  
HETATM 5248  C25 PGW B 409      19.367 -11.361  84.009  1.00 76.69           C  
HETATM 5249  C26 PGW B 409      20.098 -11.977  82.840  1.00 72.70           C  
HETATM 5250  C27 PGW B 409      20.944 -13.183  83.181  1.00 64.91           C  
HETATM 5251  C28 PGW B 409      26.007 -11.184  86.572  1.00 48.10           C  
HETATM 5252  C29 PGW B 409      27.775 -10.594  88.282  1.00 40.85           C  
HETATM 5253  C30 PGW B 409      26.332 -10.464  87.855  1.00 44.61           C  
HETATM 5254  O   HOH A 501      22.669  -1.329  99.026  1.00 51.52           O  
HETATM 5255  O   HOH A 502      24.409  11.652  97.708  1.00 57.97           O  
HETATM 5256  O   HOH A 503      14.937  -0.166  92.163  1.00 51.50           O  
HETATM 5257  O   HOH A 504      12.592  -6.842  92.777  1.00 57.33           O  
HETATM 5258  O   HOH A 505      41.958 -16.770  98.955  1.00 44.77           O  
HETATM 5259  O   HOH A 506      21.779   5.959 108.033  1.00 39.13           O  
HETATM 5260  O   HOH A 507      16.409  12.334 104.012  1.00 46.62           O  
HETATM 5261  O   HOH A 508      50.054 -27.335  89.651  1.00 82.90           O  
HETATM 5262  O   HOH A 509      17.383   3.350 114.982  1.00 83.60           O  
HETATM 5263  O   HOH A 510      13.577   3.539 114.620  1.00 82.14           O  
HETATM 5264  O   HOH A 511      13.918  -4.404  92.711  1.00 66.56           O  
HETATM 5265  O   HOH A 512      20.152  -2.835  96.084  1.00 67.10           O  
HETATM 5266  O   HOH A 513      28.088  -9.692  96.739  1.00 55.78           O  
HETATM 5267  O   HOH A 514      18.406   5.302 111.767  1.00 61.97           O  
HETATM 5268  O   HOH A 515      61.836  -9.625  92.860  1.00 61.63           O  
HETATM 5269  O   HOH A 516      20.601   8.820  84.645  1.00 72.94           O  
HETATM 5270  O   HOH A 517      22.396  -9.145  95.475  1.00 48.80           O  
HETATM 5271  O   HOH A 518      49.293 -22.799  89.829  1.00 93.60           O  
HETATM 5272  O   HOH A 519      24.394   2.685 111.731  1.00 76.25           O  
HETATM 5273  O   HOH A 520      19.968   1.434 115.426  1.00 76.08           O  
HETATM 5274  O   HOH B 501      24.118 -43.893  94.772  1.00 59.12           O  
HETATM 5275  O   HOH B 502      19.154 -34.412  95.574  1.00 63.48           O  
HETATM 5276  O   HOH B 503      19.802 -30.647  77.501  1.00 50.74           O  
HETATM 5277  O   HOH B 504      23.765 -54.422  91.882  1.00 68.10           O  
HETATM 5278  O   HOH B 505      38.802 -16.063  63.090  1.00 82.70           O  
HETATM 5279  O   HOH B 506      21.026 -34.060  89.319  1.00 58.42           O  
HETATM 5280  O   HOH B 507      29.071 -32.214  74.776  1.00 52.35           O  
HETATM 5281  O   HOH B 508      34.734 -10.784  65.127  1.00 94.81           O  
HETATM 5282  O   HOH B 509      34.511 -26.417  68.452  1.00 67.34           O  
HETATM 5283  O   HOH B 510      23.146 -44.880  87.247  1.00 61.27           O  
HETATM 5284  O   HOH B 511      34.404  -3.196  63.104  1.00 63.66           O  
HETATM 5285  O   HOH B 512      40.097  -8.218  72.647  1.00 52.24           O  
HETATM 5286  O   HOH B 513      39.050   8.503  56.183  1.00 67.70           O  
HETATM 5287  O   HOH B 514      21.992 -28.081  88.473  1.00 60.08           O  
HETATM 5288  O   HOH B 515      17.444 -32.313  97.081  1.00 66.73           O  
HETATM 5289  O   HOH B 516      13.071 -31.397 100.115  1.00 65.15           O  
HETATM 5290  O   HOH B 517      18.817   0.317  78.334  1.00 86.45           O  
HETATM 5291  O   HOH B 518      42.061 -30.243  56.555  1.00 68.90           O  
HETATM 5292  O   HOH B 519      28.834 -50.436  89.873  1.00 60.26           O  
HETATM 5293  O   HOH B 520      33.675 -51.601  92.192  1.00 73.56           O  
HETATM 5294  O   HOH B 521      37.601 -12.529  63.966  1.00 80.05           O  
HETATM 5295  O   HOH B 522      39.485  -8.046  60.342  1.00 74.63           O  
HETATM 5296  O   HOH B 523      44.881  -9.423  66.924  1.00 67.76           O  
HETATM 5297  O   HOH B 524      15.769 -38.895  87.062  1.00 69.58           O  
HETATM 5298  O   HOH B 525      40.610  -8.673  75.676  1.00 73.00           O  
HETATM 5299  O   HOH B 526      29.728 -30.845  57.416  1.00 61.84           O  
HETATM 5300  O   HOH B 527      39.944 -13.560  77.792  1.00 82.38           O  
HETATM 5301  O   HOH B 528      32.288 -31.118  59.406  1.00 65.54           O  
HETATM 5302  O   HOH B 529      29.660 -31.059  52.218  1.00 78.04           O  
HETATM 5303  O   HOH B 530      23.184 -21.607  57.187  1.00 74.27           O  
CONECT  763 1328                                                                
CONECT 1328  763                                                                
CONECT 3047 3675                                                                
CONECT 3675 3047                                                                
CONECT 4854 4865 4885 4886 4887                                                 
CONECT 4855 4856 4877 4878                                                      
CONECT 4856 4855 4879 4888                                                      
CONECT 4857 4873 4880 4889 4890                                                 
CONECT 4858 4859 4880 4884                                                      
CONECT 4859 4858 4860 4864                                                      
CONECT 4860 4859 4861 4891                                                      
CONECT 4861 4860 4862 4870                                                      
CONECT 4862 4861 4863 4892                                                      
CONECT 4863 4862 4864 4893                                                      
CONECT 4864 4859 4863 4866                                                      
CONECT 4865 4854 4871 4880 4894                                                 
CONECT 4866 4864 4881 4882                                                      
CONECT 4867 4868 4881 4895                                                      
CONECT 4868 4867 4869 4896                                                      
CONECT 4869 4868 4882 4897                                                      
CONECT 4870 4861 4898 4899 4900                                                 
CONECT 4871 4865 4872 4901 4902                                                 
CONECT 4872 4871 4873 4903 4904                                                 
CONECT 4873 4857 4872 4874 4905                                                 
CONECT 4874 4873 4883 4906 4907                                                 
CONECT 4875 4876 4879 4883                                                      
CONECT 4876 4875 4877 4908                                                      
CONECT 4877 4855 4876 4909                                                      
CONECT 4878 4855                                                                
CONECT 4879 4856 4875                                                           
CONECT 4880 4857 4858 4865                                                      
CONECT 4881 4866 4867                                                           
CONECT 4882 4866 4869                                                           
CONECT 4883 4874 4875                                                           
CONECT 4884 4858                                                                
CONECT 4885 4854                                                                
CONECT 4886 4854                                                                
CONECT 4887 4854                                                                
CONECT 4888 4856                                                                
CONECT 4889 4857                                                                
CONECT 4890 4857                                                                
CONECT 4891 4860                                                                
CONECT 4892 4862                                                                
CONECT 4893 4863                                                                
CONECT 4894 4865                                                                
CONECT 4895 4867                                                                
CONECT 4896 4868                                                                
CONECT 4897 4869                                                                
CONECT 4898 4870                                                                
CONECT 4899 4870                                                                
CONECT 4900 4870                                                                
CONECT 4901 4871                                                                
CONECT 4902 4871                                                                
CONECT 4903 4872                                                                
CONECT 4904 4872                                                                
CONECT 4905 4873                                                                
CONECT 4906 4874                                                                
CONECT 4907 4874                                                                
CONECT 4908 4876                                                                
CONECT 4909 4877                                                                
CONECT 4910 4911                                                                
CONECT 4911 4910 4912                                                           
CONECT 4912 4911 4913                                                           
CONECT 4913 4912 4914                                                           
CONECT 4914 4913 4915                                                           
CONECT 4915 4914 4916                                                           
CONECT 4916 4915 4917                                                           
CONECT 4917 4916 4918                                                           
CONECT 4918 4917 4919                                                           
CONECT 4919 4918 4920                                                           
CONECT 4920 4919 4921                                                           
CONECT 4921 4920 4922                                                           
CONECT 4922 4921                                                                
CONECT 4923 4924 4925 4926 4927                                                 
CONECT 4924 4923                                                                
CONECT 4925 4923                                                                
CONECT 4926 4923                                                                
CONECT 4927 4923                                                                
CONECT 4928 4929 4930 4931 4932                                                 
CONECT 4929 4928                                                                
CONECT 4930 4928                                                                
CONECT 4931 4928                                                                
CONECT 4932 4928                                                                
CONECT 4933 4934 4947 4951                                                      
CONECT 4934 4933 4935 4948                                                      
CONECT 4935 4934 4936 4949                                                      
CONECT 4936 4935 4937 4950                                                      
CONECT 4937 4936 4938 4951                                                      
CONECT 4938 4937 4952                                                           
CONECT 4939 4940 4947                                                           
CONECT 4940 4939 4941                                                           
CONECT 4941 4940 4942                                                           
CONECT 4942 4941 4943                                                           
CONECT 4943 4942 4944                                                           
CONECT 4944 4943 4945                                                           
CONECT 4945 4944 4946                                                           
CONECT 4946 4945                                                                
CONECT 4947 4933 4939                                                           
CONECT 4948 4934                                                                
CONECT 4949 4935                                                                
CONECT 4950 4936                                                                
CONECT 4951 4933 4937                                                           
CONECT 4952 4938                                                                
CONECT 4953 4954 4967 4971                                                      
CONECT 4954 4953 4955 4968                                                      
CONECT 4955 4954 4956 4969                                                      
CONECT 4956 4955 4957 4970                                                      
CONECT 4957 4956 4958 4971                                                      
CONECT 4958 4957 4972                                                           
CONECT 4959 4960 4967                                                           
CONECT 4960 4959 4961                                                           
CONECT 4961 4960 4962                                                           
CONECT 4962 4961 4963                                                           
CONECT 4963 4962 4964                                                           
CONECT 4964 4963 4965                                                           
CONECT 4965 4964 4966                                                           
CONECT 4966 4965                                                                
CONECT 4967 4953 4959                                                           
CONECT 4968 4954                                                                
CONECT 4969 4955                                                                
CONECT 4970 4956                                                                
CONECT 4971 4953 4957                                                           
CONECT 4972 4958                                                                
CONECT 4973 4974 4980 4984                                                      
CONECT 4974 4973 4975 4981                                                      
CONECT 4975 4974 4976 4982                                                      
CONECT 4976 4975 4977 4983                                                      
CONECT 4977 4976 4978 4984                                                      
CONECT 4978 4977 4985                                                           
CONECT 4979 4980                                                                
CONECT 4980 4973 4979                                                           
CONECT 4981 4974                                                                
CONECT 4982 4975                                                                
CONECT 4983 4976                                                                
CONECT 4984 4973 4977                                                           
CONECT 4985 4978                                                                
CONECT 4986 4987 5000 5004                                                      
CONECT 4987 4986 4988 5001                                                      
CONECT 4988 4987 4989 5002                                                      
CONECT 4989 4988 4990 5003                                                      
CONECT 4990 4989 4991 5004                                                      
CONECT 4991 4990 5005                                                           
CONECT 4992 4993 5000                                                           
CONECT 4993 4992 4994                                                           
CONECT 4994 4993 4995                                                           
CONECT 4995 4994 4996                                                           
CONECT 4996 4995 4997                                                           
CONECT 4997 4996 4998                                                           
CONECT 4998 4997 4999                                                           
CONECT 4999 4998                                                                
CONECT 5000 4986 4992                                                           
CONECT 5001 4987                                                                
CONECT 5002 4988                                                                
CONECT 5003 4989                                                                
CONECT 5004 4986 4990                                                           
CONECT 5005 4991                                                                
CONECT 5006 5007                                                                
CONECT 5007 5006 5008                                                           
CONECT 5008 5007 5009                                                           
CONECT 5009 5008                                                                
CONECT 5011 5012 5027                                                           
CONECT 5012 5011                                                                
CONECT 5013 5027                                                                
CONECT 5014 5039 5041 5043 5045                                                 
CONECT 5015 5018 5023                                                           
CONECT 5016 5017 5019 5020                                                      
CONECT 5017 5016 5018                                                           
CONECT 5018 5015 5017 5021                                                      
CONECT 5019 5016 5022                                                           
CONECT 5020 5016                                                                
CONECT 5021 5018 5039                                                           
CONECT 5022 5019 5025                                                           
CONECT 5023 5015 5050                                                           
CONECT 5024 5027 5041                                                           
CONECT 5025 5022 5028                                                           
CONECT 5026 5050                                                                
CONECT 5027 5011 5013 5024                                                      
CONECT 5028 5025 5030                                                           
CONECT 5029 5031 5037                                                           
CONECT 5030 5028 5032                                                           
CONECT 5031 5029 5033                                                           
CONECT 5032 5030 5034                                                           
CONECT 5033 5031 5035                                                           
CONECT 5034 5032 5036                                                           
CONECT 5035 5033 5038                                                           
CONECT 5036 5034 5037                                                           
CONECT 5037 5029 5036                                                           
CONECT 5038 5035 5040                                                           
CONECT 5039 5014 5021                                                           
CONECT 5040 5038 5042                                                           
CONECT 5041 5014 5024                                                           
CONECT 5042 5040 5044                                                           
CONECT 5043 5014                                                                
CONECT 5044 5042                                                                
CONECT 5045 5014                                                                
CONECT 5046 5047 5058                                                           
CONECT 5047 5046 5048                                                           
CONECT 5048 5047 5049                                                           
CONECT 5049 5048 5059                                                           
CONECT 5050 5023 5026 5051                                                      
CONECT 5051 5050 5052                                                           
CONECT 5052 5051 5053                                                           
CONECT 5053 5052 5054                                                           
CONECT 5054 5053 5055                                                           
CONECT 5055 5054 5056                                                           
CONECT 5056 5055 5057                                                           
CONECT 5057 5056 5058                                                           
CONECT 5058 5046 5057                                                           
CONECT 5059 5049 5061                                                           
CONECT 5060 5061                                                                
CONECT 5061 5059 5060                                                           
CONECT 5062 5073 5093 5094 5095                                                 
CONECT 5063 5064 5085 5086                                                      
CONECT 5064 5063 5087 5096                                                      
CONECT 5065 5081 5088 5097 5098                                                 
CONECT 5066 5067 5088 5092                                                      
CONECT 5067 5066 5068 5072                                                      
CONECT 5068 5067 5069 5099                                                      
CONECT 5069 5068 5070 5078                                                      
CONECT 5070 5069 5071 5100                                                      
CONECT 5071 5070 5072 5101                                                      
CONECT 5072 5067 5071 5074                                                      
CONECT 5073 5062 5079 5088 5102                                                 
CONECT 5074 5072 5089 5090                                                      
CONECT 5075 5076 5089 5103                                                      
CONECT 5076 5075 5077 5104                                                      
CONECT 5077 5076 5090 5105                                                      
CONECT 5078 5069 5106 5107 5108                                                 
CONECT 5079 5073 5080 5109 5110                                                 
CONECT 5080 5079 5081 5111 5112                                                 
CONECT 5081 5065 5080 5082 5113                                                 
CONECT 5082 5081 5091 5114 5115                                                 
CONECT 5083 5084 5087 5091                                                      
CONECT 5084 5083 5085 5116                                                      
CONECT 5085 5063 5084 5117                                                      
CONECT 5086 5063                                                                
CONECT 5087 5064 5083                                                           
CONECT 5088 5065 5066 5073                                                      
CONECT 5089 5074 5075                                                           
CONECT 5090 5074 5077                                                           
CONECT 5091 5082 5083                                                           
CONECT 5092 5066                                                                
CONECT 5093 5062                                                                
CONECT 5094 5062                                                                
CONECT 5095 5062                                                                
CONECT 5096 5064                                                                
CONECT 5097 5065                                                                
CONECT 5098 5065                                                                
CONECT 5099 5068                                                                
CONECT 5100 5070                                                                
CONECT 5101 5071                                                                
CONECT 5102 5073                                                                
CONECT 5103 5075                                                                
CONECT 5104 5076                                                                
CONECT 5105 5077                                                                
CONECT 5106 5078                                                                
CONECT 5107 5078                                                                
CONECT 5108 5078                                                                
CONECT 5109 5079                                                                
CONECT 5110 5079                                                                
CONECT 5111 5080                                                                
CONECT 5112 5080                                                                
CONECT 5113 5081                                                                
CONECT 5114 5082                                                                
CONECT 5115 5082                                                                
CONECT 5116 5084                                                                
CONECT 5117 5085                                                                
CONECT 5118 5119                                                                
CONECT 5119 5118 5120                                                           
CONECT 5120 5119 5121                                                           
CONECT 5121 5120 5122                                                           
CONECT 5122 5121 5123                                                           
CONECT 5123 5122 5124                                                           
CONECT 5124 5123 5125                                                           
CONECT 5125 5124 5126                                                           
CONECT 5126 5125                                                                
CONECT 5127 5128 5129 5130 5131                                                 
CONECT 5128 5127                                                                
CONECT 5129 5127                                                                
CONECT 5130 5127                                                                
CONECT 5131 5127                                                                
CONECT 5132 5133 5134 5135 5136                                                 
CONECT 5133 5132                                                                
CONECT 5134 5132                                                                
CONECT 5135 5132                                                                
CONECT 5136 5132                                                                
CONECT 5137 5138 5151 5155                                                      
CONECT 5138 5137 5139 5152                                                      
CONECT 5139 5138 5140 5153                                                      
CONECT 5140 5139 5141 5154                                                      
CONECT 5141 5140 5142 5155                                                      
CONECT 5142 5141 5156                                                           
CONECT 5143 5144 5151                                                           
CONECT 5144 5143 5145                                                           
CONECT 5145 5144 5146                                                           
CONECT 5146 5145 5147                                                           
CONECT 5147 5146 5148                                                           
CONECT 5148 5147 5149                                                           
CONECT 5149 5148 5150                                                           
CONECT 5150 5149                                                                
CONECT 5151 5137 5143                                                           
CONECT 5152 5138                                                                
CONECT 5153 5139                                                                
CONECT 5154 5140                                                                
CONECT 5155 5137 5141                                                           
CONECT 5156 5142                                                                
CONECT 5157 5158 5171 5175                                                      
CONECT 5158 5157 5159 5172                                                      
CONECT 5159 5158 5160 5173                                                      
CONECT 5160 5159 5161 5174                                                      
CONECT 5161 5160 5162 5175                                                      
CONECT 5162 5161 5176                                                           
CONECT 5163 5164 5171                                                           
CONECT 5164 5163 5165                                                           
CONECT 5165 5164 5166                                                           
CONECT 5166 5165 5167                                                           
CONECT 5167 5166 5168                                                           
CONECT 5168 5167 5169                                                           
CONECT 5169 5168 5170                                                           
CONECT 5170 5169                                                                
CONECT 5171 5157 5163                                                           
CONECT 5172 5158                                                                
CONECT 5173 5159                                                                
CONECT 5174 5160                                                                
CONECT 5175 5157 5161                                                           
CONECT 5176 5162                                                                
CONECT 5177 5178 5191 5195                                                      
CONECT 5178 5177 5179 5192                                                      
CONECT 5179 5178 5180 5193                                                      
CONECT 5180 5179 5181 5194                                                      
CONECT 5181 5180 5182 5195                                                      
CONECT 5182 5181 5196                                                           
CONECT 5183 5184 5191                                                           
CONECT 5184 5183 5185                                                           
CONECT 5185 5184 5186                                                           
CONECT 5186 5185 5187                                                           
CONECT 5187 5186 5188                                                           
CONECT 5188 5187 5189                                                           
CONECT 5189 5188 5190                                                           
CONECT 5190 5189                                                                
CONECT 5191 5177 5183                                                           
CONECT 5192 5178                                                                
CONECT 5193 5179                                                                
CONECT 5194 5180                                                                
CONECT 5195 5177 5181                                                           
CONECT 5196 5182                                                                
CONECT 5197 5198 5202                                                           
CONECT 5198 5197 5199                                                           
CONECT 5199 5198 5200                                                           
CONECT 5200 5199 5201                                                           
CONECT 5201 5200                                                                
CONECT 5202 5197                                                                
CONECT 5203 5204 5219                                                           
CONECT 5204 5203                                                                
CONECT 5205 5219                                                                
CONECT 5206 5231 5233 5235 5237                                                 
CONECT 5207 5210 5215                                                           
CONECT 5208 5209 5211 5212                                                      
CONECT 5209 5208 5210                                                           
CONECT 5210 5207 5209 5213                                                      
CONECT 5211 5208 5214                                                           
CONECT 5212 5208                                                                
CONECT 5213 5210 5231                                                           
CONECT 5214 5211 5217                                                           
CONECT 5215 5207 5242                                                           
CONECT 5216 5219 5233                                                           
CONECT 5217 5214 5220                                                           
CONECT 5218 5242                                                                
CONECT 5219 5203 5205 5216                                                      
CONECT 5220 5217 5222                                                           
CONECT 5221 5223 5229                                                           
CONECT 5222 5220 5224                                                           
CONECT 5223 5221 5225                                                           
CONECT 5224 5222 5226                                                           
CONECT 5225 5223 5227                                                           
CONECT 5226 5224 5228                                                           
CONECT 5227 5225 5230                                                           
CONECT 5228 5226 5229                                                           
CONECT 5229 5221 5228                                                           
CONECT 5230 5227 5232                                                           
CONECT 5231 5206 5213                                                           
CONECT 5232 5230 5234                                                           
CONECT 5233 5206 5216                                                           
CONECT 5234 5232 5236                                                           
CONECT 5235 5206                                                                
CONECT 5236 5234                                                                
CONECT 5237 5206                                                                
CONECT 5238 5239 5250                                                           
CONECT 5239 5238 5240                                                           
CONECT 5240 5239 5241                                                           
CONECT 5241 5240 5251                                                           
CONECT 5242 5215 5218 5243                                                      
CONECT 5243 5242 5244                                                           
CONECT 5244 5243 5245                                                           
CONECT 5245 5244 5246                                                           
CONECT 5246 5245 5247                                                           
CONECT 5247 5246 5248                                                           
CONECT 5248 5247 5249                                                           
CONECT 5249 5248 5250                                                           
CONECT 5250 5238 5249                                                           
CONECT 5251 5241 5253                                                           
CONECT 5252 5253                                                                
CONECT 5253 5251 5252                                                           
MASTER      407    0   20   26    4    0    0    6 5251    2  403   58          
END