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***  5op6_unbound  ***

elNémo ID: 210514005334113399

Job options:

ID        	=	 210514005334113399
JOBID     	=	 5op6_unbound
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 5op6_unbound

HEADER    OXIDOREDUCTASE                          09-AUG-17   5OP6              
TITLE     FACTOR INHIBITING HIF (FIH) IN COMPLEX WITH ZINC AND GSK128863        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1-ALPHA INHIBITOR;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FACTOR INHIBITING HIF-1,FIH-1,HYPOXIA-INDUCIBLE FACTOR      
COMPND   5 ASPARAGINE HYDROXYLASE;                                              
COMPND   6 EC: 1.14.11.30,1.14.11.-;                                            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HIF1AN, FIH1;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ON-HEME, DIOXYGENASE, OXYGENASE, DNA-BINDING, METAL-BINDING,          
KEYWDS   2 TRANSCRIPTION, HELIX-LOOP-HELIX-BETA, DSBH, FACIAL TRIAD,            
KEYWDS   3 ASPARAGINYL/ASPARTYL HYDROXYLASE, EPIGENETIC REGULATION, SIGNALING,  
KEYWDS   4 ARD, BETA-HYDROXYLATION, ACTIVATOR-INHIBITOR, OXIDOREDUCTASE-PEPTIDE 
KEYWDS   5 COMPLEX, OXIDOREDUCTASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.M.LEISSING,C.J.SCHOFIELD,I.J.CLIFTON,C.C.THINNES,X.LU               
REVDAT   2   21-FEB-18 5OP6    1       JRNL                                     
REVDAT   1   18-OCT-17 5OP6    0                                                
JRNL        AUTH   T.L.YEH,T.M.LEISSING,M.I.ABBOUD,C.C.THINNES,O.ATASOYLU,      
JRNL        AUTH 2 J.P.HOLT-MARTYN,D.ZHANG,A.TUMBER,K.LIPPL,C.T.LOHANS,         
JRNL        AUTH 3 I.K.H.LEUNG,H.MORCRETTE,I.J.CLIFTON,T.D.W.CLARIDGE,          
JRNL        AUTH 4 A.KAWAMURA,E.FLASHMAN,X.LU,P.J.RATCLIFFE,R.CHOWDHURY,        
JRNL        AUTH 5 C.W.PUGH,C.J.SCHOFIELD                                       
JRNL        TITL   MOLECULAR AND CELLULAR MECHANISMS OF HIF PROLYL HYDROXYLASE  
JRNL        TITL 2 INHIBITORS IN CLINICAL TRIALS.                               
JRNL        REF    CHEM SCI                      V.   8  7651 2017              
JRNL        REFN                   ISSN 2041-6520                               
JRNL        PMID   29435217                                                     
JRNL        DOI    10.1039/C7SC02103H                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.31                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 21064                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1051                            
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 30.3074 -  4.8942    1.00     2703   118  0.2046 0.2131        
REMARK   3     2  4.8942 -  3.8873    1.00     2548   129  0.1600 0.1789        
REMARK   3     3  3.8873 -  3.3966    1.00     2475   155  0.1881 0.2207        
REMARK   3     4  3.3966 -  3.0864    1.00     2474   138  0.2218 0.2746        
REMARK   3     5  3.0864 -  2.8654    1.00     2459   126  0.2254 0.2544        
REMARK   3     6  2.8654 -  2.6965    1.00     2452   129  0.2447 0.2682        
REMARK   3     7  2.6965 -  2.5616    1.00     2470   135  0.2720 0.2925        
REMARK   3     8  2.5616 -  2.4501    1.00     2432   121  0.2970 0.3087        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.650           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.005           2747                                  
REMARK   3   ANGLE     :  0.569           3744                                  
REMARK   3   CHIRALITY :  0.043            385                                  
REMARK   3   PLANARITY :  0.003            492                                  
REMARK   3   DIHEDRAL  : 11.335           1597                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 15 THROUGH 49 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6428  32.4798 -22.1098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4853 T22:   0.7840                                     
REMARK   3      T33:   0.7352 T12:   0.0106                                     
REMARK   3      T13:  -0.0639 T23:   0.2513                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5481 L22:   0.8565                                     
REMARK   3      L33:   0.5255 L12:  -0.5479                                     
REMARK   3      L13:  -0.0979 L23:  -0.3307                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2708 S12:   0.6476 S13:   0.7613                       
REMARK   3      S21:  -0.1511 S22:  -0.1619 S23:   0.2124                       
REMARK   3      S31:  -0.3803 S32:   0.4149 S33:  -0.0007                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 50 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -23.1726  20.3848 -22.5961              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3965 T22:   0.7613                                     
REMARK   3      T33:   0.4507 T12:   0.0697                                     
REMARK   3      T13:  -0.0327 T23:   0.1444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2786 L22:   1.2901                                     
REMARK   3      L33:   1.6622 L12:   0.6393                                     
REMARK   3      L13:   0.7315 L23:  -0.7372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0385 S12:   0.5404 S13:   0.1209                       
REMARK   3      S21:  -0.3878 S22:   0.2210 S23:   0.2453                       
REMARK   3      S31:   0.0693 S32:  -0.1341 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 78 THROUGH 95 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -32.5507  29.8186  -1.4789              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6177 T22:   1.1074                                     
REMARK   3      T33:   0.7035 T12:   0.1283                                     
REMARK   3      T13:   0.0853 T23:  -0.1126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5336 L22:   0.2460                                     
REMARK   3      L33:   0.1758 L12:  -0.1749                                     
REMARK   3      L13:  -0.0201 L23:   0.2323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0479 S12:  -1.1299 S13:   0.2040                       
REMARK   3      S21:   0.5546 S22:  -0.3562 S23:   0.3531                       
REMARK   3      S31:   0.0339 S32:  -1.1248 S33:   0.0026                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 96 THROUGH 124 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -14.5190  23.3016   7.1377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7109 T22:   1.1989                                     
REMARK   3      T33:   0.6792 T12:  -0.0855                                     
REMARK   3      T13:   0.0191 T23:   0.1402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1281 L22:   0.4931                                     
REMARK   3      L33:   0.0360 L12:  -0.1872                                     
REMARK   3      L13:   0.0505 L23:   0.0131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3302 S12:  -0.5832 S13:   0.1178                       
REMARK   3      S21:   1.4055 S22:  -0.1822 S23:  -0.4990                       
REMARK   3      S31:  -0.6284 S32:  -0.3982 S33:  -0.0022                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 155 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.1755  32.7124   0.6752              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7000 T22:   1.3986                                     
REMARK   3      T33:   0.7012 T12:   0.2277                                     
REMARK   3      T13:   0.1547 T23:  -0.0875                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4131 L22:   1.0441                                     
REMARK   3      L33:   0.5245 L12:  -0.6005                                     
REMARK   3      L13:   0.4026 L23:  -0.7023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1390 S12:  -1.3026 S13:   0.5236                       
REMARK   3      S21:   0.8397 S22:  -0.1712 S23:  -0.2475                       
REMARK   3      S31:  -0.6491 S32:  -1.3345 S33:   0.0018                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 297 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.1033  21.2443 -11.0409              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3204 T22:   0.6085                                     
REMARK   3      T33:   0.4740 T12:   0.0246                                     
REMARK   3      T13:   0.0161 T23:   0.1307                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3487 L22:   0.5129                                     
REMARK   3      L33:   2.9983 L12:  -0.6465                                     
REMARK   3      L13:   2.0962 L23:  -0.4345                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0909 S12:  -0.1194 S13:   0.1852                       
REMARK   3      S21:   0.1332 S22:   0.0031 S23:   0.0920                       
REMARK   3      S31:  -0.0053 S32:  -0.1798 S33:   0.0061                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 349 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6330   3.5458  -2.6630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5873 T22:   0.5817                                     
REMARK   3      T33:   0.5451 T12:  -0.0201                                     
REMARK   3      T13:  -0.1082 T23:   0.0463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4991 L22:   1.9780                                     
REMARK   3      L33:   0.3490 L12:  -0.9249                                     
REMARK   3      L13:   0.2395 L23:  -0.6339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0947 S12:  -0.0933 S13:  -0.2058                       
REMARK   3      S21:  -0.0752 S22:  -0.0902 S23:   0.3684                       
REMARK   3      S31:   0.3170 S32:  -0.3373 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5OP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006154.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21126                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.50                              
REMARK 200  R MERGE                    (I) : 0.13800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.25000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1H2K                                                 
REMARK 200                                                                      
REMARK 200 REMARK: TETRAGONAL BIPYRAMID                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 1.1M AMMONIUM          
REMARK 280  SULFATE, 2.5% PEG 400, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 300K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.53500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.10500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.10500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.76750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.10500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.10500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      110.30250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.10500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.10500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       36.76750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.10500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.10500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      110.30250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       73.53500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 590 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
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 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     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     ARG A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  15    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  17    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  19    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  23    CD1  CD2                                            
REMARK 470     GLU A  29    CD   OE1  OE2                                       
REMARK 470     ARG A  40    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A  58    CG   OD1  ND2                                       
REMARK 470     ASN A  87    CG   OD1  ND2                                       
REMARK 470     SER A  94    OG                                                  
REMARK 470     LYS A  99    CG   CD   CE   NZ                                   
REMARK 470     GLU A 105    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 106    CD   CE   NZ                                        
REMARK 470     ASN A 110    CG   OD1  ND2                                       
REMARK 470     ASN A 113    CG   OD1  ND2                                       
REMARK 470     PHE A 114    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 124    CD   CE   NZ                                        
REMARK 470     LYS A 131    CD   CE   NZ                                        
REMARK 470     LEU A 132    CG   CD1  CD2                                       
REMARK 470     GLN A 133    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 136    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 137    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 141    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 144    CD1  CD2                                            
REMARK 470     ASP A 152    CG   OD1  OD2                                       
REMARK 470     ARG A 156    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 157    CE   NZ                                             
REMARK 470     LYS A 172    CD   CE   NZ                                        
REMARK 470     GLN A 181    CD   OE1  NE2                                       
REMARK 470     GLU A 250    CD   OE1  OE2                                       
REMARK 470     LYS A 298    CD   CE   NZ                                        
REMARK 470     LYS A 304    CG   CD   CE   NZ                                   
REMARK 470     ARG A 305    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 306    CD1                                                 
REMARK 470     GLU A 307    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 345    CE   NZ                                             
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    ASP A  66       46.68   -146.13                                   
REMARK 500    ASP A 104      109.34    -56.76                                   
REMARK 500    ARG A 138       -9.54     82.14                                   
REMARK 500    LEU A 182      106.26    -57.05                                   
REMARK 500    ILE A 210      -60.20   -123.25                                   
REMARK 500    ARG A 238       -5.92     82.96                                   
REMARK 500    ASN A 246       76.24   -153.98                                   
REMARK 500    ASN A 332      115.80   -166.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 199   NE2                                                    
REMARK 620 2 ASP A 201   OD2 123.6                                              
REMARK 620 3 HIS A 279   NE2  84.2  90.7                                        
REMARK 620 4 A0W A 404   O19 102.2 131.8 109.4                                  
REMARK 620 5 A0W A 404   O11  69.6 100.6 153.6  80.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue A0W A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405                 
DBREF  5OP6 A    1   349  UNP    Q9NWT6   HIF1N_HUMAN      1    349             
SEQADV 5OP6 SER A   -1  UNP  Q9NWT6              EXPRESSION TAG                 
SEQADV 5OP6 HIS A    0  UNP  Q9NWT6              EXPRESSION TAG                 
SEQRES   1 A  351  SER HIS MET ALA ALA THR ALA ALA GLU ALA VAL ALA SER          
SEQRES   2 A  351  GLY SER GLY GLU PRO ARG GLU GLU ALA GLY ALA LEU GLY          
SEQRES   3 A  351  PRO ALA TRP ASP GLU SER GLN LEU ARG SER TYR SER PHE          
SEQRES   4 A  351  PRO THR ARG PRO ILE PRO ARG LEU SER GLN SER ASP PRO          
SEQRES   5 A  351  ARG ALA GLU GLU LEU ILE GLU ASN GLU GLU PRO VAL VAL          
SEQRES   6 A  351  LEU THR ASP THR ASN LEU VAL TYR PRO ALA LEU LYS TRP          
SEQRES   7 A  351  ASP LEU GLU TYR LEU GLN GLU ASN ILE GLY ASN GLY ASP          
SEQRES   8 A  351  PHE SER VAL TYR SER ALA SER THR HIS LYS PHE LEU TYR          
SEQRES   9 A  351  TYR ASP GLU LYS LYS MET ALA ASN PHE GLN ASN PHE LYS          
SEQRES  10 A  351  PRO ARG SER ASN ARG GLU GLU MET LYS PHE HIS GLU PHE          
SEQRES  11 A  351  VAL GLU LYS LEU GLN ASP ILE GLN GLN ARG GLY GLY GLU          
SEQRES  12 A  351  GLU ARG LEU TYR LEU GLN GLN THR LEU ASN ASP THR VAL          
SEQRES  13 A  351  GLY ARG LYS ILE VAL MET ASP PHE LEU GLY PHE ASN TRP          
SEQRES  14 A  351  ASN TRP ILE ASN LYS GLN GLN GLY LYS ARG GLY TRP GLY          
SEQRES  15 A  351  GLN LEU THR SER ASN LEU LEU LEU ILE GLY MET GLU GLY          
SEQRES  16 A  351  ASN VAL THR PRO ALA HIS TYR ASP GLU GLN GLN ASN PHE          
SEQRES  17 A  351  PHE ALA GLN ILE LYS GLY TYR LYS ARG CYS ILE LEU PHE          
SEQRES  18 A  351  PRO PRO ASP GLN PHE GLU CYS LEU TYR PRO TYR PRO VAL          
SEQRES  19 A  351  HIS HIS PRO CYS ASP ARG GLN SER GLN VAL ASP PHE ASP          
SEQRES  20 A  351  ASN PRO ASP TYR GLU ARG PHE PRO ASN PHE GLN ASN VAL          
SEQRES  21 A  351  VAL GLY TYR GLU THR VAL VAL GLY PRO GLY ASP VAL LEU          
SEQRES  22 A  351  TYR ILE PRO MET TYR TRP TRP HIS HIS ILE GLU SER LEU          
SEQRES  23 A  351  LEU ASN GLY GLY ILE THR ILE THR VAL ASN PHE TRP TYR          
SEQRES  24 A  351  LYS GLY ALA PRO THR PRO LYS ARG ILE GLU TYR PRO LEU          
SEQRES  25 A  351  LYS ALA HIS GLN LYS VAL ALA ILE MET ARG ASN ILE GLU          
SEQRES  26 A  351  LYS MET LEU GLY GLU ALA LEU GLY ASN PRO GLN GLU VAL          
SEQRES  27 A  351  GLY PRO LEU LEU ASN THR MET ILE LYS GLY ARG TYR ASN          
HET     ZN  A 401       1                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    A0W  A 404      54                                                       
HET    GOL  A 405      14                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     A0W 2-[[1,3-DICYCLOHEXYL-4-OXIDANYL-2,6-BIS(OXIDANYLIDENE)           
HETNAM   2 A0W  PYRIMIDIN-5-YL]CARBONYLAMINO]ETHANOIC ACID                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  A0W    C19 H27 N3 O6                                                
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *46(H2 O)                                                     
HELIX    1 AA1 GLU A   19  LEU A   23  5                                   5    
HELIX    2 AA2 ASP A   28  LEU A   32  5                                   5    
HELIX    3 AA3 ASP A   49  ASN A   58  1                                  10    
HELIX    4 AA4 VAL A   70  TRP A   76  5                                   7    
HELIX    5 AA5 ASP A   77  ILE A   85  1                                   9    
HELIX    6 AA6 ASP A  104  ALA A  109  5                                   6    
HELIX    7 AA7 LYS A  124  GLN A  137  1                                  14    
HELIX    8 AA8 ARG A  138  GLY A  140  5                                   3    
HELIX    9 AA9 GLY A  155  GLY A  164  1                                  10    
HELIX   10 AB1 ASN A  166  ARG A  177  1                                  12    
HELIX   11 AB2 PRO A  220  ASP A  222  5                                   3    
HELIX   12 AB3 GLN A  223  TYR A  228  1                                   6    
HELIX   13 AB4 PHE A  252  VAL A  258  5                                   7    
HELIX   14 AB5 LYS A  311  LEU A  330  1                                  20    
HELIX   15 AB6 ASN A  332  GLN A  334  5                                   3    
HELIX   16 AB7 GLU A  335  LYS A  345  1                                  11    
SHEET    1 AA1 5 THR A  39  PRO A  41  0                                        
SHEET    2 AA1 5 GLY A 260  VAL A 265  1  O  GLU A 262   N  ARG A  40           
SHEET    3 AA1 5 LYS A 214  PHE A 219 -1  N  LEU A 218   O  TYR A 261           
SHEET    4 AA1 5 TRP A 278  SER A 283 -1  O  GLU A 282   N  ARG A 215           
SHEET    5 AA1 5 VAL A 195  TYR A 200 -1  N  THR A 196   O  ILE A 281           
SHEET    1 AA2 9 ARG A  44  LEU A  45  0                                        
SHEET    2 AA2 9 VAL A  62  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3 AA2 9 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4 AA2 9 GLN A 204  LYS A 211 -1  N  PHE A 207   O  LEU A 271           
SHEET    5 AA2 9 THR A 290  TYR A 297 -1  O  TYR A 297   N  GLN A 204           
SHEET    6 AA2 9 LEU A 182  GLY A 190 -1  N  LEU A 188   O  THR A 292           
SHEET    7 AA2 9 ARG A 143  THR A 149 -1  N  GLN A 148   O  LEU A 187           
SHEET    8 AA2 9 PHE A  90  ALA A  95 -1  N  SER A  91   O  GLN A 147           
SHEET    9 AA2 9 ARG A 120  MET A 123 -1  O  MET A 123   N  PHE A  90           
LINK         NE2 HIS A 199                ZN    ZN A 401     1555   1555  2.05  
LINK         OD2 ASP A 201                ZN    ZN A 401     1555   1555  1.99  
LINK         NE2 HIS A 279                ZN    ZN A 401     1555   1555  2.07  
LINK        ZN    ZN A 401                 O19 A0W A 404     1555   1555  2.04  
LINK        ZN    ZN A 401                 O11 A0W A 404     1555   1555  2.21  
CISPEP   1 TYR A  308    PRO A  309          0        -4.58                     
SITE     1 AC1  4 HIS A 199  ASP A 201  HIS A 279  A0W A 404                    
SITE     1 AC2  3 ALA A 312  HOH A 514  HOH A 537                               
SITE     1 AC3  4 ARG A 138  GLY A 140  GLU A 141  GLU A 142                    
SITE     1 AC4 17 TYR A  93  PHE A 100  LEU A 101  TYR A 102                    
SITE     2 AC4 17 TYR A 145  GLN A 147  LEU A 188  THR A 196                    
SITE     3 AC4 17 HIS A 199  ASP A 201  PHE A 207  LYS A 214                    
SITE     4 AC4 17 ARG A 238  HIS A 279  ILE A 281   ZN A 401                    
SITE     5 AC4 17 GOL A 405                                                     
SITE     1 AC5  3 ASP A 201  TRP A 296  A0W A 404                               
CRYST1   86.210   86.210  147.070  90.00  90.00  90.00 P 41 21 2     8          
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      0.011600  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011600  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006799        0.00000                         
ATOM      1  N   GLU A  15     -10.025  34.879 -25.059  1.00106.40           N  
ANISOU    1  N   GLU A  15    11421  15136  13870   -351   -914   3591       N  
ATOM      2  CA  GLU A  15     -10.875  35.174 -26.206  1.00108.02           C  
ANISOU    2  CA  GLU A  15    11613  15354  14073   -320  -1006   3692       C  
ATOM      3  C   GLU A  15     -12.334  35.345 -25.776  1.00109.04           C  
ANISOU    3  C   GLU A  15    11804  15231  14397   -234  -1063   3486       C  
ATOM      4  O   GLU A  15     -13.148  34.442 -25.973  1.00108.13           O  
ANISOU    4  O   GLU A  15    11708  15170  14208   -115   -992   3315       O  
ATOM      5  CB  GLU A  15     -10.763  34.061 -27.252  1.00106.91           C  
ANISOU    5  CB  GLU A  15    11444  15522  13653   -243   -899   3719       C  
ATOM      6  HA  GLU A  15     -10.581  36.003 -26.615  1.00129.62           H  
ATOM      7  N   PRO A  16     -12.667  36.498 -25.191  1.00109.16           N  
ANISOU    7  N   PRO A  16    11847  14966  14662   -292  -1191   3503       N  
ATOM      8  CA  PRO A  16     -14.037  36.696 -24.693  1.00107.64           C  
ANISOU    8  CA  PRO A  16    11713  14520  14666   -206  -1240   3309       C  
ATOM      9  C   PRO A  16     -15.059  36.645 -25.821  1.00104.08           C  
ANISOU    9  C   PRO A  16    11244  14114  14188   -141  -1302   3350       C  
ATOM     10  O   PRO A  16     -14.859  37.217 -26.895  1.00106.93           O  
ANISOU   10  O   PRO A  16    11561  14567  14500   -199  -1395   3589       O  
ATOM     11  CB  PRO A  16     -13.982  38.081 -24.036  1.00109.42           C  
ANISOU   11  CB  PRO A  16    11967  14464  15143   -302  -1379   3384       C  
ATOM     12  CG  PRO A  16     -12.800  38.761 -24.653  1.00110.53           C  
ANISOU   12  CG  PRO A  16    12048  14727  15223   -444  -1443   3677       C  
ATOM     13  CD  PRO A  16     -11.814  37.676 -24.953  1.00109.87           C  
ANISOU   13  CD  PRO A  16    11917  14954  14873   -438  -1297   3701       C  
ATOM     14  HA  PRO A  16     -14.256  36.028 -24.025  1.00129.17           H  
ATOM     15  HB2 PRO A  16     -14.798  38.568 -24.232  1.00131.30           H  
ATOM     16  HB3 PRO A  16     -13.861  37.984 -23.079  1.00131.30           H  
ATOM     17  HG2 PRO A  16     -13.073  39.209 -25.469  1.00132.64           H  
ATOM     18  HG3 PRO A  16     -12.426  39.397 -24.023  1.00132.64           H  
ATOM     19  HD2 PRO A  16     -11.306  37.893 -25.750  1.00131.84           H  
ATOM     20  HD3 PRO A  16     -11.234  37.526 -24.190  1.00131.84           H  
ATOM     21  N   ARG A  17     -16.166  35.952 -25.565  1.00 98.04           N  
ANISOU   21  N   ARG A  17    10512  13281  13459    -15  -1250   3117       N  
ATOM     22  CA  ARG A  17     -17.202  35.784 -26.573  1.00 98.49           C  
ANISOU   22  CA  ARG A  17    10551  13382  13490     58  -1305   3124       C  
ATOM     23  C   ARG A  17     -18.090  37.022 -26.654  1.00 93.42           C  
ANISOU   23  C   ARG A  17     9923  12484  13089     38  -1474   3195       C  
ATOM     24  O   ARG A  17     -18.265  37.756 -25.677  1.00 95.58           O  
ANISOU   24  O   ARG A  17    10240  12501  13576     12  -1519   3136       O  
ATOM     25  CB  ARG A  17     -18.055  34.552 -26.264  1.00 98.79           C  
ANISOU   25  CB  ARG A  17    10610  13440  13485    197  -1186   2847       C  
ATOM     26  H   ARG A  17     -16.339  35.571 -24.814  1.00117.65           H  
ATOM     27  HA  ARG A  17     -16.785  35.654 -27.439  1.00118.19           H  
ATOM     28  N   GLU A  18     -18.654  37.245 -27.840  1.00 83.88           N  
ANISOU   28  N   GLU A  18     8682  11349  11840     57  -1567   3323       N  
ATOM     29  CA  GLU A  18     -19.531  38.380 -28.099  1.00 78.06           C  
ANISOU   29  CA  GLU A  18     7950  10399  11309     46  -1728   3410       C  
ATOM     30  C   GLU A  18     -20.980  37.924 -27.968  0.50 75.41           C  
ANISOU   30  C   GLU A  18     7632   9946  11074    175  -1728   3193       C  
ATOM     31  O   GLU A  18     -21.422  37.031 -28.699  0.50 68.11           O  
ANISOU   31  O   GLU A  18     6681   9194  10003    254  -1689   3131       O  
ATOM     32  CB  GLU A  18     -19.272  38.958 -29.491  0.50 87.27           C  
ANISOU   32  CB  GLU A  18     9069  11714  12375     -8  -1835   3695       C  
ATOM     33  CG  GLU A  18     -20.073  40.211 -29.811  0.50 97.07           C  
ANISOU   33  CG  GLU A  18    10315  12744  13824    -27  -2005   3816       C  
ATOM     34  CD  GLU A  18     -19.654  41.403 -28.973  0.50103.04           C  
ANISOU   34  CD  GLU A  18    11101  13258  14792   -131  -2075   3895       C  
ATOM     35  OE1 GLU A  18     -18.590  41.329 -28.324  0.50103.73           O  
ANISOU   35  OE1 GLU A  18    11195  13375  14843   -205  -2007   3904       O  
ATOM     36  OE2 GLU A  18     -20.388  42.413 -28.965  0.50105.28           O  
ANISOU   36  OE2 GLU A  18    11403  13319  15278   -137  -2200   3949       O  
ATOM     37  H   GLU A  18     -18.540  36.738 -28.525  1.00100.66           H  
ATOM     38  HA  GLU A  18     -19.366  39.074 -27.442  1.00 93.67           H  
ATOM     39  HB2 GLU A  18     -18.331  39.183 -29.563  0.50104.72           H  
ATOM     40  HB3 GLU A  18     -19.499  38.286 -30.153  0.50104.72           H  
ATOM     41  HG2 GLU A  18     -19.943  40.440 -30.745  0.50116.49           H  
ATOM     42  HG3 GLU A  18     -21.012  40.039 -29.639  0.50116.49           H  
ATOM     43  N   GLU A  19     -21.712  38.538 -27.043  1.00 87.67           N  
ANISOU   43  N   GLU A  19     9229  11205  12878    197  -1772   3079       N  
ATOM     44  CA  GLU A  19     -23.104  38.173 -26.824  1.00 91.62           C  
ANISOU   44  CA  GLU A  19     9740  11570  13501    318  -1770   2878       C  
ATOM     45  C   GLU A  19     -23.968  38.618 -28.000  1.00 91.16           C  
ANISOU   45  C   GLU A  19     9643  11528  13465    344  -1906   3003       C  
ATOM     46  O   GLU A  19     -23.712  39.643 -28.639  1.00 95.73           O  
ANISOU   46  O   GLU A  19    10208  12092  14073    266  -2031   3237       O  
ATOM     47  CB  GLU A  19     -23.620  38.799 -25.528  1.00 90.99           C  
ANISOU   47  CB  GLU A  19     9721  11166  13685    338  -1782   2744       C  
ATOM     48  H   GLU A  19     -21.426  39.168 -26.532  1.00105.21           H  
ATOM     49  HA  GLU A  19     -23.172  37.209 -26.745  1.00109.94           H  
ATOM     50  N   ALA A  20     -25.005  37.831 -28.280  1.00 82.51           N  
ANISOU   50  N   ALA A  20     8528  10463  12359    455  -1882   2845       N  
ATOM     51  CA  ALA A  20     -25.890  38.116 -29.398  1.00 81.88           C  
ANISOU   51  CA  ALA A  20     8409  10413  12288    493  -2009   2939       C  
ATOM     52  C   ALA A  20     -26.596  39.457 -29.194  1.00 81.95           C  
ANISOU   52  C   ALA A  20     8434  10146  12556    476  -2151   3024       C  
ATOM     53  O   ALA A  20     -26.590  40.042 -28.109  1.00 85.61           O  
ANISOU   53  O   ALA A  20     8945  10375  13206    456  -2142   2965       O  
ATOM     54  CB  ALA A  20     -26.916  36.997 -29.567  1.00 78.87           C  
ANISOU   54  CB  ALA A  20     8003  10085  11877    617  -1955   2723       C  
ATOM     55  H   ALA A  20     -25.215  37.125 -27.836  1.00 99.01           H  
ATOM     56  HA  ALA A  20     -25.366  38.171 -30.212  1.00 98.26           H  
ATOM     57  HB1 ALA A  20     -27.494  37.209 -30.317  1.00 94.64           H  
ATOM     58  HB2 ALA A  20     -26.449  36.163 -29.734  1.00 94.64           H  
ATOM     59  HB3 ALA A  20     -27.441  36.925 -28.754  1.00 94.64           H  
ATOM     60  N   GLY A  21     -27.217  39.939 -30.267  1.00 78.31           N  
ANISOU   60  N   GLY A  21     7938   9715  12101    491  -2284   3164       N  
ATOM     61  CA  GLY A  21     -27.863  41.235 -30.228  1.00 80.08           C  
ANISOU   61  CA  GLY A  21     8175   9699  12554    476  -2424   3272       C  
ATOM     62  C   GLY A  21     -26.913  42.395 -30.051  1.00 86.88           C  
ANISOU   62  C   GLY A  21     9064  10477  13468    351  -2482   3484       C  
ATOM     63  O   GLY A  21     -27.345  43.484 -29.664  1.00 86.87           O  
ANISOU   63  O   GLY A  21     9093  10227  13687    332  -2574   3538       O  
ATOM     64  H   GLY A  21     -27.276  39.535 -31.024  1.00 93.97           H  
ATOM     65  HA2 GLY A  21     -28.354  41.370 -31.054  1.00 96.10           H  
ATOM     66  HA3 GLY A  21     -28.497  41.251 -29.494  1.00 96.10           H  
ATOM     67  N   ALA A  22     -25.624  42.193 -30.325  1.00 92.84           N  
ANISOU   67  N   ALA A  22     9810  11432  14033    265  -2430   3607       N  
ATOM     68  CA  ALA A  22     -24.612  43.238 -30.175  1.00 92.65           C  
ANISOU   68  CA  ALA A  22     9803  11346  14054    136  -2480   3816       C  
ATOM     69  C   ALA A  22     -24.558  43.767 -28.743  1.00 93.02           C  
ANISOU   69  C   ALA A  22     9914  11111  14318    107  -2460   3698       C  
ATOM     70  O   ALA A  22     -24.215  44.928 -28.511  1.00 90.49           O  
ANISOU   70  O   ALA A  22     9619  10626  14137     19  -2548   3845       O  
ATOM     71  CB  ALA A  22     -24.854  44.385 -31.159  1.00 91.21           C  
ANISOU   71  CB  ALA A  22     9599  11126  13931     96  -2640   4074       C  
ATOM     72  H   ALA A  22     -25.306  41.445 -30.605  1.00111.41           H  
ATOM     73  HA  ALA A  22     -23.744  42.857 -30.378  1.00111.18           H  
ATOM     74  HB1 ALA A  22     -24.168  45.059 -31.033  1.00109.45           H  
ATOM     75  HB2 ALA A  22     -24.815  44.038 -32.064  1.00109.45           H  
ATOM     76  HB3 ALA A  22     -25.729  44.768 -30.989  1.00109.45           H  
ATOM     77  N   LEU A  23     -24.883  42.912 -27.771  1.00 99.37           N  
ANISOU   77  N   LEU A  23    10747  11858  15150    184  -2343   3432       N  
ATOM     78  CA  LEU A  23     -24.915  43.313 -26.368  1.00101.16           C  
ANISOU   78  CA  LEU A  23    11043  11819  15572    180  -2314   3295       C  
ATOM     79  C   LEU A  23     -23.534  43.618 -25.799  1.00100.58           C  
ANISOU   79  C   LEU A  23    10996  11762  15459     60  -2282   3374       C  
ATOM     80  O   LEU A  23     -23.444  43.984 -24.621  1.00101.03           O  
ANISOU   80  O   LEU A  23    11118  11603  15667     50  -2266   3267       O  
ATOM     81  CB  LEU A  23     -25.587  42.219 -25.534  1.00 97.90           C  
ANISOU   81  CB  LEU A  23    10652  11367  15178    303  -2182   2995       C  
ATOM     82  CG  LEU A  23     -27.117  42.194 -25.580  1.00 95.69           C  
ANISOU   82  CG  LEU A  23    10366  10938  15053    423  -2221   2874       C  
ATOM     83  H   LEU A  23     -25.090  42.088 -27.902  1.00119.24           H  
ATOM     84  HA  LEU A  23     -25.451  44.117 -26.287  1.00121.39           H  
ATOM     85  HB2 LEU A  23     -25.274  41.357 -25.850  1.00117.48           H  
ATOM     86  HB3 LEU A  23     -25.327  42.338 -24.607  1.00117.48           H  
ATOM     87  HG  LEU A  23     -27.417  42.639 -26.388  1.00114.82           H  
ATOM     88 HD11 LEU A  23     -31.120  40.567 -24.704  1.00100.00           H  
ATOM     89 HD12 LEU A  23     -27.921  38.172 -25.524  1.00100.00           H  
ATOM     90 HD13 LEU A  23     -27.089  39.292 -22.340  1.00100.00           H  
ATOM     91 HD21 LEU A  23     -29.903  42.628 -24.801  1.00100.00           H  
ATOM     92 HD22 LEU A  23     -26.224  43.562 -21.309  1.00100.00           H  
ATOM     93 HD23 LEU A  23     -26.255  46.128 -23.552  1.00100.00           H  
ATOM     94  N   GLY A  24     -22.470  43.480 -26.586  1.00 99.96           N  
ANISOU   94  N   GLY A  24    10869  11929  15184    -26  -2275   3558       N  
ATOM     95  CA  GLY A  24     -21.138  43.792 -26.127  1.00100.15           C  
ANISOU   95  CA  GLY A  24    10903  11979  15172   -146  -2253   3655       C  
ATOM     96  C   GLY A  24     -20.445  42.582 -25.538  1.00 97.27           C  
ANISOU   96  C   GLY A  24    10539  11778  14643   -123  -2089   3490       C  
ATOM     97  O   GLY A  24     -21.027  41.497 -25.427  1.00 96.73           O  
ANISOU   97  O   GLY A  24    10469  11787  14497    -11  -1986   3290       O  
ATOM     98  H   GLY A  24     -22.502  43.204 -27.399  1.00119.96           H  
ATOM     99  HA2 GLY A  24     -20.608  44.121 -26.869  1.00120.19           H  
ATOM    100  HA3 GLY A  24     -21.182  44.484 -25.448  1.00120.19           H  
ATOM    101  N   PRO A  25     -19.182  42.742 -25.149  1.00 84.32           N  
ANISOU  101  N   PRO A  25     8898  10193  12949   -229  -2061   3573       N  
ATOM    102  CA  PRO A  25     -18.453  41.618 -24.549  1.00 80.78           C  
ANISOU  102  CA  PRO A  25     8450   9901  12342   -208  -1902   3425       C  
ATOM    103  C   PRO A  25     -19.079  41.203 -23.227  1.00 81.94           C  
ANISOU  103  C   PRO A  25     8669   9853  12613   -111  -1823   3133       C  
ATOM    104  O   PRO A  25     -19.336  42.033 -22.352  1.00 81.95           O  
ANISOU  104  O   PRO A  25     8732   9581  12825   -126  -1888   3084       O  
ATOM    105  CB  PRO A  25     -17.036  42.172 -24.355  1.00 78.84           C  
ANISOU  105  CB  PRO A  25     8189   9700  12068   -354  -1924   3599       C  
ATOM    106  CG  PRO A  25     -16.961  43.392 -25.211  1.00 80.85           C  
ANISOU  106  CG  PRO A  25     8413   9901  12405   -449  -2079   3875       C  
ATOM    107  CD  PRO A  25     -18.344  43.946 -25.257  1.00 81.58           C  
ANISOU  107  CD  PRO A  25     8543   9770  12683   -374  -2172   3813       C  
ATOM    108  HA  PRO A  25     -18.429  40.861 -25.155  1.00 96.94           H  
ATOM    109  HB2 PRO A  25     -16.901  42.401 -23.422  1.00 94.61           H  
ATOM    110  HB3 PRO A  25     -16.386  41.513 -24.643  1.00 94.61           H  
ATOM    111  HG2 PRO A  25     -16.351  44.032 -24.811  1.00 97.02           H  
ATOM    112  HG3 PRO A  25     -16.662  43.147 -26.100  1.00 97.02           H  
ATOM    113  HD2 PRO A  25     -18.499  44.537 -24.503  1.00 97.89           H  
ATOM    114  HD3 PRO A  25     -18.502  44.395 -26.102  1.00 97.89           H  
ATOM    115  N   ALA A  26     -19.325  39.899 -23.085  1.00 89.55           N  
ANISOU  115  N   ALA A  26     9627  10956  13442     -7  -1679   2939       N  
ATOM    116  CA  ALA A  26     -19.899  39.390 -21.845  1.00 86.98           C  
ANISOU  116  CA  ALA A  26     9365  10465  13218     96  -1583   2661       C  
ATOM    117  C   ALA A  26     -18.958  39.598 -20.666  1.00 83.43           C  
ANISOU  117  C   ALA A  26     8967   9926  12808     39  -1543   2609       C  
ATOM    118  O   ALA A  26     -19.415  39.817 -19.538  1.00 82.91           O  
ANISOU  118  O   ALA A  26     8974   9620  12907     95  -1530   2441       O  
ATOM    119  CB  ALA A  26     -20.238  37.908 -21.996  1.00 86.12           C  
ANISOU  119  CB  ALA A  26     9233  10546  12944    211  -1429   2481       C  
ATOM    120  H   ALA A  26     -19.169  39.300 -23.682  1.00107.46           H  
ATOM    121  HA  ALA A  26     -20.722  39.868 -21.660  1.00104.38           H  
ATOM    122  HB1 ALA A  26     -20.618  37.586 -21.164  1.00103.35           H  
ATOM    123  HB2 ALA A  26     -20.879  37.803 -22.716  1.00103.35           H  
ATOM    124  HB3 ALA A  26     -19.426  37.418 -22.201  1.00103.35           H  
ATOM    125  N   TRP A  27     -17.650  39.531 -20.903  1.00 75.83           N  
ANISOU  125  N   TRP A  27     7966   9153  11694    -66  -1524   2752       N  
ATOM    126  CA  TRP A  27     -16.657  39.721 -19.855  1.00 71.59           C  
ANISOU  126  CA  TRP A  27     7467   8555  11180   -130  -1495   2718       C  
ATOM    127  C   TRP A  27     -15.326  40.047 -20.513  1.00 71.79           C  
ANISOU  127  C   TRP A  27     7425   8773  11078   -276  -1536   2972       C  
ATOM    128  O   TRP A  27     -15.130  39.806 -21.707  1.00 72.31           O  
ANISOU  128  O   TRP A  27     7420   9061  10992   -301  -1539   3134       O  
ATOM    129  CB  TRP A  27     -16.532  38.475 -18.972  1.00 71.48           C  
ANISOU  129  CB  TRP A  27     7483   8616  11062    -29  -1314   2471       C  
ATOM    130  CG  TRP A  27     -16.275  37.225 -19.760  1.00 68.74           C  
ANISOU  130  CG  TRP A  27     7072   8585  10462     14  -1187   2466       C  
ATOM    131  CD1 TRP A  27     -17.205  36.330 -20.203  1.00 66.83           C  
ANISOU  131  CD1 TRP A  27     6815   8420  10155    132  -1111   2341       C  
ATOM    132  CD2 TRP A  27     -15.004  36.740 -20.210  1.00 65.56           C  
ANISOU  132  CD2 TRP A  27     6611   8459   9839    -61  -1123   2595       C  
ATOM    133  NE1 TRP A  27     -16.592  35.315 -20.898  1.00 66.45           N  
ANISOU  133  NE1 TRP A  27     6713   8678   9856    138  -1005   2378       N  
ATOM    134  CE2 TRP A  27     -15.241  35.544 -20.916  1.00 66.79           C  
ANISOU  134  CE2 TRP A  27     6730   8852   9797     24  -1006   2536       C  
ATOM    135  CE3 TRP A  27     -13.691  37.199 -20.082  1.00 67.59           C  
ANISOU  135  CE3 TRP A  27     6844   8788  10052   -190  -1153   2756       C  
ATOM    136  CZ2 TRP A  27     -14.212  34.801 -21.491  1.00 65.49           C  
ANISOU  136  CZ2 TRP A  27     6510   8988   9386    -10   -914   2633       C  
ATOM    137  CZ3 TRP A  27     -12.672  36.461 -20.655  1.00 70.07           C  
ANISOU  137  CZ3 TRP A  27     7093   9404  10126   -225  -1060   2858       C  
ATOM    138  CH2 TRP A  27     -12.938  35.275 -21.350  1.00 67.38           C  
ANISOU  138  CH2 TRP A  27     6723   9294   9585   -132   -940   2796       C  
ATOM    139  H   TRP A  27     -17.310  39.374 -21.677  1.00 91.00           H  
ATOM    140  HA  TRP A  27     -16.916  40.470 -19.296  1.00 85.91           H  
ATOM    141  HB2 TRP A  27     -15.792  38.597 -18.356  1.00 85.78           H  
ATOM    142  HB3 TRP A  27     -17.358  38.353 -18.478  1.00 85.78           H  
ATOM    143  HD1 TRP A  27     -18.121  36.397 -20.056  1.00 80.19           H  
ATOM    144  HE1 TRP A  27     -16.990  34.645 -21.261  1.00 79.74           H  
ATOM    145  HE3 TRP A  27     -13.506  37.986 -19.622  1.00 81.11           H  
ATOM    146  HZ2 TRP A  27     -14.385  34.013 -21.954  1.00 78.59           H  
ATOM    147  HZ3 TRP A  27     -11.794  36.757 -20.576  1.00 84.09           H  
ATOM    148  HH2 TRP A  27     -12.232  34.800 -21.724  1.00 80.86           H  
ATOM    149  N   ASP A  28     -14.413  40.603 -19.719  1.00 72.48           N  
ANISOU  149  N   ASP A  28     7537   8771  11231   -370  -1569   3006       N  
ATOM    150  CA  ASP A  28     -13.058  40.876 -20.173  1.00 75.62           C  
ANISOU  150  CA  ASP A  28     7868   9342  11522   -512  -1596   3235       C  
ATOM    151  C   ASP A  28     -12.067  40.261 -19.193  1.00 73.88           C  
ANISOU  151  C   ASP A  28     7661   9195  11216   -524  -1488   3121       C  
ATOM    152  O   ASP A  28     -12.418  39.887 -18.071  1.00 74.05           O  
ANISOU  152  O   ASP A  28     7756   9080  11298   -436  -1422   2881       O  
ATOM    153  CB  ASP A  28     -12.797  42.383 -20.325  1.00 77.62           C  
ANISOU  153  CB  ASP A  28     8119   9412  11960   -648  -1779   3449       C  
ATOM    154  CG  ASP A  28     -12.831  43.120 -19.004  1.00 77.14           C  
ANISOU  154  CG  ASP A  28     8148   9049  12113   -670  -1845   3326       C  
ATOM    155  OD1 ASP A  28     -11.802  43.114 -18.298  1.00 77.70           O  
ANISOU  155  OD1 ASP A  28     8222   9138  12163   -740  -1826   3317       O  
ATOM    156  OD2 ASP A  28     -13.879  43.715 -18.676  1.00 78.88           O  
ANISOU  156  OD2 ASP A  28     8438   9014  12521   -614  -1919   3240       O  
ATOM    157  H   ASP A  28     -14.558  40.832 -18.903  1.00 86.97           H  
ATOM    158  HA  ASP A  28     -12.923  40.459 -21.038  1.00 90.75           H  
ATOM    159  HB2 ASP A  28     -11.921  42.514 -20.720  1.00 93.14           H  
ATOM    160  HB3 ASP A  28     -13.480  42.766 -20.899  1.00 93.14           H  
ATOM    161  N   GLU A  29     -10.814  40.160 -19.637  1.00 71.09           N  
ANISOU  161  N   GLU A  29     7232   9060  10717   -628  -1470   3304       N  
ATOM    162  CA  GLU A  29      -9.795  39.454 -18.872  1.00 70.37           C  
ANISOU  162  CA  GLU A  29     7137   9093  10508   -638  -1356   3218       C  
ATOM    163  C   GLU A  29      -9.479  40.116 -17.536  1.00 69.29           C  
ANISOU  163  C   GLU A  29     7070   8710  10548   -682  -1419   3118       C  
ATOM    164  O   GLU A  29      -8.851  39.476 -16.686  1.00 70.76           O  
ANISOU  164  O   GLU A  29     7273   8956  10656   -658  -1320   2986       O  
ATOM    165  CB  GLU A  29      -8.518  39.331 -19.706  1.00 70.87           C  
ANISOU  165  CB  GLU A  29     7096   9436  10394   -749  -1336   3467       C  
ATOM    166  CG  GLU A  29      -8.695  38.517 -20.980  1.00 70.84           C  
ANISOU  166  CG  GLU A  29     7032   9708  10176   -692  -1253   3553       C  
ATOM    167  H   GLU A  29     -10.531  40.493 -20.378  1.00 85.30           H  
ATOM    168  HA  GLU A  29     -10.113  38.556 -18.687  1.00 84.45           H  
ATOM    169  HB2 GLU A  29      -8.223  40.219 -19.960  1.00 85.04           H  
ATOM    170  HB3 GLU A  29      -7.834  38.899 -19.170  1.00 85.04           H  
ATOM    171  N   SER A  30      -9.898  41.365 -17.320  1.00 69.83           N  
ANISOU  171  N   SER A  30     7183   8503  10846   -741  -1581   3172       N  
ATOM    172  CA  SER A  30      -9.628  42.016 -16.043  1.00 66.88           C  
ANISOU  172  CA  SER A  30     6888   7883  10641   -778  -1650   3069       C  
ATOM    173  C   SER A  30     -10.391  41.366 -14.897  1.00 65.02           C  
ANISOU  173  C   SER A  30     6754   7510  10439   -619  -1550   2752       C  
ATOM    174  O   SER A  30     -10.006  41.536 -13.736  1.00 64.16           O  
ANISOU  174  O   SER A  30     6713   7263  10403   -621  -1559   2627       O  
ATOM    175  CB  SER A  30      -9.977  43.503 -16.121  1.00 66.23           C  
ANISOU  175  CB  SER A  30     6838   7529  10799   -868  -1845   3198       C  
ATOM    176  OG  SER A  30     -11.375  43.707 -16.024  1.00 67.69           O  
ANISOU  176  OG  SER A  30     7096   7509  11114   -755  -1870   3069       O  
ATOM    177  H   SER A  30     -10.332  41.846 -17.885  1.00 83.79           H  
ATOM    178  HA  SER A  30      -8.680  41.943 -15.849  1.00 80.26           H  
ATOM    179  HB2 SER A  30      -9.540  43.968 -15.390  1.00 79.48           H  
ATOM    180  HB3 SER A  30      -9.665  43.855 -16.970  1.00 79.48           H  
ATOM    181  HG  SER A  30     -11.767  43.310 -16.653  1.00 81.23           H  
ATOM    182  N   GLN A  31     -11.460  40.630 -15.197  1.00 66.97           N  
ANISOU  182  N   GLN A  31     7015   7791  10639   -479  -1457   2622       N  
ATOM    183  CA  GLN A  31     -12.218  39.919 -14.177  1.00 65.84           C  
ANISOU  183  CA  GLN A  31     6959   7534  10522   -318  -1342   2329       C  
ATOM    184  C   GLN A  31     -11.591  38.581 -13.806  1.00 69.25           C  
ANISOU  184  C   GLN A  31     7371   8198  10741   -252  -1156   2199       C  
ATOM    185  O   GLN A  31     -12.046  37.947 -12.847  1.00 66.88           O  
ANISOU  185  O   GLN A  31     7144   7815  10453   -121  -1047   1956       O  
ATOM    186  CB  GLN A  31     -13.652  39.694 -14.660  1.00 64.18           C  
ANISOU  186  CB  GLN A  31     6763   7257  10366   -198  -1322   2248       C  
ATOM    187  CG  GLN A  31     -14.321  40.941 -15.221  1.00 69.25           C  
ANISOU  187  CG  GLN A  31     7411   7705  11195   -255  -1498   2396       C  
ATOM    188  CD  GLN A  31     -15.690  40.654 -15.793  1.00 68.35           C  
ANISOU  188  CD  GLN A  31     7295   7557  11118   -139  -1478   2329       C  
ATOM    189  OE1 GLN A  31     -15.929  40.836 -16.987  1.00 67.86           O  
ANISOU  189  OE1 GLN A  31     7165   7603  11015   -177  -1536   2498       O  
ATOM    190  NE2 GLN A  31     -16.601  40.201 -14.941  1.00 69.04           N  
ANISOU  190  NE2 GLN A  31     7455   7494  11284      7  -1395   2084       N  
ATOM    191  H   GLN A  31     -11.768  40.528 -15.993  1.00 80.36           H  
ATOM    192  HA  GLN A  31     -12.254  40.464 -13.375  1.00 79.01           H  
ATOM    193  HB2 GLN A  31     -13.644  39.023 -15.359  1.00 77.02           H  
ATOM    194  HB3 GLN A  31     -14.187  39.383 -13.913  1.00 77.02           H  
ATOM    195  HG2 GLN A  31     -14.423  41.594 -14.510  1.00 83.10           H  
ATOM    196  HG3 GLN A  31     -13.769  41.305 -15.930  1.00 83.10           H  
ATOM    197 HE21 GLN A  31     -16.397  40.086 -14.114  1.00 82.85           H  
ATOM    198 HE22 GLN A  31     -17.396  40.022 -15.217  1.00 82.85           H  
ATOM    199  N   LEU A  32     -10.568  38.142 -14.537  1.00 71.44           N  
ANISOU  199  N   LEU A  32     7555   8761  10828   -333  -1112   2359       N  
ATOM    200  CA  LEU A  32      -9.885  36.890 -14.250  1.00 69.75           C  
ANISOU  200  CA  LEU A  32     7317   8783  10402   -277   -935   2259       C  
ATOM    201  C   LEU A  32      -8.702  37.144 -13.327  1.00 70.70           C  
ANISOU  201  C   LEU A  32     7450   8888  10525   -357   -954   2262       C  
ATOM    202  O   LEU A  32      -7.982  38.136 -13.478  1.00 76.96           O  
ANISOU  202  O   LEU A  32     8211   9633  11398   -506  -1095   2452       O  
ATOM    203  CB  LEU A  32      -9.395  36.230 -15.540  1.00 66.71           C  
ANISOU  203  CB  LEU A  32     6826   8725   9794   -312   -869   2430       C  
ATOM    204  CG  LEU A  32     -10.416  36.060 -16.666  1.00 67.22           C  
ANISOU  204  CG  LEU A  32     6864   8840   9838   -257   -877   2474       C  
ATOM    205  CD1 LEU A  32      -9.779  35.361 -17.851  1.00 67.14           C  
ANISOU  205  CD1 LEU A  32     6759   9165   9585   -286   -805   2637       C  
ATOM    206  CD2 LEU A  32     -11.636  35.298 -16.186  1.00 66.20           C  
ANISOU  206  CD2 LEU A  32     6800   8612   9742    -86   -774   2207       C  
ATOM    207  H   LEU A  32     -10.249  38.562 -15.217  1.00 85.73           H  
ATOM    208  HA  LEU A  32     -10.496  36.282 -13.806  1.00 83.70           H  
ATOM    209  HB2 LEU A  32      -8.666  36.763 -15.894  1.00 80.05           H  
ATOM    210  HB3 LEU A  32      -9.064  35.345 -15.319  1.00 80.05           H  
ATOM    211  HG  LEU A  32     -10.709  36.937 -16.960  1.00 80.67           H  
ATOM    212 HD11 LEU A  32     -10.441  35.263 -18.553  1.00 80.56           H  
ATOM    213 HD12 LEU A  32      -9.034  35.895 -18.169  1.00 80.56           H  
ATOM    214 HD13 LEU A  32      -9.463  34.488 -17.569  1.00 80.56           H  
ATOM    215 HD21 LEU A  32     -12.262  35.209 -16.922  1.00 79.44           H  
ATOM    216 HD22 LEU A  32     -11.359  34.421 -15.878  1.00 79.44           H  
ATOM    217 HD23 LEU A  32     -12.049  35.790 -15.459  1.00 79.44           H  
ATOM    218  N   ARG A  33      -8.508  36.243 -12.371  1.00 64.02           N  
ANISOU  218  N   ARG A  33     6649   8080   9595   -256   -811   2053       N  
ATOM    219  CA  ARG A  33      -7.326  36.298 -11.528  1.00 63.69           C  
ANISOU  219  CA  ARG A  33     6611   8067   9520   -320   -810   2048       C  
ATOM    220  C   ARG A  33      -6.114  35.807 -12.310  1.00 64.27           C  
ANISOU  220  C   ARG A  33     6567   8467   9384   -412   -754   2240       C  
ATOM    221  O   ARG A  33      -6.228  34.992 -13.229  1.00 64.20           O  
ANISOU  221  O   ARG A  33     6500   8687   9207   -371   -648   2289       O  
ATOM    222  CB  ARG A  33      -7.532  35.456 -10.269  1.00 65.29           C  
ANISOU  222  CB  ARG A  33     6903   8214   9691   -169   -667   1762       C  
ATOM    223  CG  ARG A  33      -8.727  35.894  -9.445  1.00 64.95           C  
ANISOU  223  CG  ARG A  33     6978   7849   9849    -62   -707   1569       C  
ATOM    224  CD  ARG A  33      -8.921  35.025  -8.218  1.00 63.63           C  
ANISOU  224  CD  ARG A  33     6898   7636   9642     98   -552   1295       C  
ATOM    225  NE  ARG A  33     -10.091  35.449  -7.452  1.00 68.17           N  
ANISOU  225  NE  ARG A  33     7588   7903  10412    210   -583   1119       N  
ATOM    226  CZ  ARG A  33     -10.081  36.391  -6.512  1.00 69.10           C  
ANISOU  226  CZ  ARG A  33     7798   7757  10699    192   -703   1066       C  
ATOM    227  NH1 ARG A  33      -8.957  37.020  -6.193  1.00 68.55           N  
ANISOU  227  NH1 ARG A  33     7719   7688  10638     61   -813   1168       N  
ATOM    228  NH2 ARG A  33     -11.206  36.703  -5.883  1.00 66.86           N  
ANISOU  228  NH2 ARG A  33     7618   7205  10580    309   -714    909       N  
ATOM    229  H   ARG A  33      -9.044  35.594 -12.192  1.00 76.82           H  
ATOM    230  HA  ARG A  33      -7.166  37.216 -11.259  1.00 76.43           H  
ATOM    231  HB2 ARG A  33      -7.671  34.532 -10.529  1.00 78.35           H  
ATOM    232  HB3 ARG A  33      -6.742  35.527  -9.711  1.00 78.35           H  
ATOM    233  HG2 ARG A  33      -8.593  36.808  -9.149  1.00 77.94           H  
ATOM    234  HG3 ARG A  33      -9.528  35.833  -9.988  1.00 77.94           H  
ATOM    235  HD2 ARG A  33      -9.054  34.104  -8.494  1.00 76.35           H  
ATOM    236  HD3 ARG A  33      -8.140  35.096  -7.647  1.00 76.35           H  
ATOM    237  HE  ARG A  33     -10.840  35.063  -7.622  1.00 81.81           H  
ATOM    238 HH11 ARG A  33      -8.224  36.823  -6.598  1.00 82.26           H  
ATOM    239 HH12 ARG A  33      -8.961  37.625  -5.582  1.00 82.26           H  
ATOM    240 HH21 ARG A  33     -11.937  36.298  -6.084  1.00 80.23           H  
ATOM    241 HH22 ARG A  33     -11.203  37.308  -5.272  1.00 80.23           H  
ATOM    242  N   SER A  34      -4.945  36.326 -11.952  1.00 66.78           N  
ANISOU  242  N   SER A  34     6853   8804   9717   -539   -830   2354       N  
ATOM    243  CA  SER A  34      -3.706  35.974 -12.628  1.00 69.74           C  
ANISOU  243  CA  SER A  34     7111   9474   9912   -637   -786   2555       C  
ATOM    244  C   SER A  34      -2.977  34.894 -11.842  1.00 65.07           C  
ANISOU  244  C   SER A  34     6524   9045   9153   -565   -624   2411       C  
ATOM    245  O   SER A  34      -2.972  34.906 -10.608  1.00 66.05           O  
ANISOU  245  O   SER A  34     6731   9014   9351   -512   -620   2221       O  
ATOM    246  CB  SER A  34      -2.809  37.199 -12.786  1.00 71.68           C  
ANISOU  246  CB  SER A  34     7300   9656  10278   -829   -968   2792       C  
ATOM    247  OG  SER A  34      -2.596  37.816 -11.530  1.00 74.48           O  
ANISOU  247  OG  SER A  34     7731   9777  10790   -855  -1060   2672       O  
ATOM    248  H   SER A  34      -4.844  36.891 -11.312  1.00 80.14           H  
ATOM    249  HA  SER A  34      -3.908  35.626 -13.510  1.00 83.69           H  
ATOM    250  HB2 SER A  34      -1.955  36.922 -13.153  1.00 86.01           H  
ATOM    251  HB3 SER A  34      -3.238  37.833 -13.382  1.00 86.01           H  
ATOM    252  HG  SER A  34      -2.102  38.490 -11.620  1.00 89.37           H  
ATOM    253  N   TYR A  35      -2.363  33.961 -12.566  1.00 60.14           N  
ANISOU  253  N   TYR A  35     5814   8735   8299   -556   -490   2502       N  
ATOM    254  CA  TYR A  35      -1.663  32.846 -11.951  1.00 57.72           C  
ANISOU  254  CA  TYR A  35     5503   8615   7811   -481   -319   2381       C  
ATOM    255  C   TYR A  35      -0.366  32.592 -12.706  1.00 56.52           C  
ANISOU  255  C   TYR A  35     5226   8764   7484   -586   -283   2620       C  
ATOM    256  O   TYR A  35      -0.120  33.157 -13.775  1.00 55.76           O  
ANISOU  256  O   TYR A  35     5050   8745   7392   -696   -369   2869       O  
ATOM    257  CB  TYR A  35      -2.539  31.590 -11.923  1.00 55.78           C  
ANISOU  257  CB  TYR A  35     5310   8443   7442   -295   -129   2164       C  
ATOM    258  CG  TYR A  35      -3.786  31.755 -11.083  1.00 56.50           C  
ANISOU  258  CG  TYR A  35     5521   8243   7703   -179   -144   1920       C  
ATOM    259  CD1 TYR A  35      -3.698  31.954  -9.712  1.00 55.75           C  
ANISOU  259  CD1 TYR A  35     5512   7961   7710   -138   -158   1744       C  
ATOM    260  CD2 TYR A  35      -5.049  31.712 -11.659  1.00 56.92           C  
ANISOU  260  CD2 TYR A  35     5602   8209   7815   -106   -144   1869       C  
ATOM    261  CE1 TYR A  35      -4.831  32.107  -8.937  1.00 56.52           C  
ANISOU  261  CE1 TYR A  35     5722   7792   7961    -22   -163   1528       C  
ATOM    262  CE2 TYR A  35      -6.191  31.862 -10.890  1.00 56.23           C  
ANISOU  262  CE2 TYR A  35     5619   7857   7890      4   -152   1655       C  
ATOM    263  CZ  TYR A  35      -6.074  32.059  -9.530  1.00 56.17           C  
ANISOU  263  CZ  TYR A  35     5696   7666   7978     48   -157   1487       C  
ATOM    264  OH  TYR A  35      -7.202  32.210  -8.756  1.00 60.56           O  
ANISOU  264  OH  TYR A  35     6358   7958   8693    166   -157   1281       O  
ATOM    265  H   TYR A  35      -2.340  33.955 -13.426  1.00 72.16           H  
ATOM    266  HA  TYR A  35      -1.438  33.077 -11.036  1.00 69.26           H  
ATOM    267  HB2 TYR A  35      -2.815  31.378 -12.828  1.00 66.94           H  
ATOM    268  HB3 TYR A  35      -2.025  30.856 -11.553  1.00 66.94           H  
ATOM    269  HD1 TYR A  35      -2.861  31.987  -9.308  1.00 66.90           H  
ATOM    270  HD2 TYR A  35      -5.130  31.579 -12.576  1.00 68.30           H  
ATOM    271  HE1 TYR A  35      -4.755  32.239  -8.020  1.00 67.83           H  
ATOM    272  HE2 TYR A  35      -7.031  31.831 -11.288  1.00 67.48           H  
ATOM    273  HH  TYR A  35      -7.889  32.162  -9.237  1.00 72.67           H  
ATOM    274  N   SER A  36       0.466  31.721 -12.136  1.00 61.50           N  
ANISOU  274  N   SER A  36     5842   9568   7959   -542   -147   2547       N  
ATOM    275  CA  SER A  36       1.821  31.517 -12.632  1.00 64.60           C  
ANISOU  275  CA  SER A  36     6116  10232   8199   -642   -113   2765       C  
ATOM    276  C   SER A  36       1.908  30.508 -13.768  1.00 62.38           C  
ANISOU  276  C   SER A  36     5771  10253   7675   -585     44   2859       C  
ATOM    277  O   SER A  36       2.931  30.466 -14.459  1.00 66.36           O  
ANISOU  277  O   SER A  36     6170  10985   8060   -675     59   3089       O  
ATOM    278  CB  SER A  36       2.734  31.051 -11.492  1.00 61.48           C  
ANISOU  278  CB  SER A  36     5728   9892   7741   -621    -42   2652       C  
ATOM    279  OG  SER A  36       2.337  29.777 -11.011  1.00 57.62           O  
ANISOU  279  OG  SER A  36     5302   9487   7104   -443    159   2415       O  
ATOM    280  H   SER A  36       0.266  31.233 -11.456  1.00 73.81           H  
ATOM    281  HA  SER A  36       2.164  32.363 -12.961  1.00 77.53           H  
ATOM    282  HB2 SER A  36       3.644  30.994 -11.821  1.00 73.78           H  
ATOM    283  HB3 SER A  36       2.683  31.692 -10.766  1.00 73.78           H  
ATOM    284  HG  SER A  36       2.845  29.535 -10.387  1.00 69.14           H  
ATOM    285  N   PHE A  37       0.876  29.708 -13.985  1.00 57.68           N  
ANISOU  285  N   PHE A  37     5239   9668   7011   -440    159   2691       N  
ATOM    286  CA  PHE A  37       0.969  28.598 -14.919  1.00 58.11           C  
ANISOU  286  CA  PHE A  37     5250  10011   6819   -367    324   2738       C  
ATOM    287  C   PHE A  37       0.276  28.927 -16.233  1.00 57.55           C  
ANISOU  287  C   PHE A  37     5154   9959   6752   -388    258   2883       C  
ATOM    288  O   PHE A  37      -0.614  29.780 -16.285  1.00 57.32           O  
ANISOU  288  O   PHE A  37     5167   9696   6917   -412    118   2866       O  
ATOM    289  CB  PHE A  37       0.344  27.340 -14.308  1.00 54.06           C  
ANISOU  289  CB  PHE A  37     4817   9520   6201   -183    513   2450       C  
ATOM    290  CG  PHE A  37      -1.051  27.546 -13.802  1.00 52.07           C  
ANISOU  290  CG  PHE A  37     4668   8989   6126    -93    472   2230       C  
ATOM    291  CD1 PHE A  37      -2.137  27.405 -14.647  1.00 51.43           C  
ANISOU  291  CD1 PHE A  37     4604   8884   6052    -37    470   2212       C  
ATOM    292  CD2 PHE A  37      -1.275  27.889 -12.480  1.00 51.09           C  
ANISOU  292  CD2 PHE A  37     4624   8627   6161    -61    435   2044       C  
ATOM    293  CE1 PHE A  37      -3.422  27.599 -14.181  1.00 53.39           C  
ANISOU  293  CE1 PHE A  37     4939   8877   6471     46    435   2018       C  
ATOM    294  CE2 PHE A  37      -2.555  28.084 -12.009  1.00 49.90           C  
ANISOU  294  CE2 PHE A  37     4566   8219   6174     29    405   1850       C  
ATOM    295  CZ  PHE A  37      -3.631  27.939 -12.858  1.00 53.23           C  
ANISOU  295  CZ  PHE A  37     4997   8620   6610     81    406   1839       C  
ATOM    296  H   PHE A  37       0.109  29.785 -13.603  1.00 69.22           H  
ATOM    297  HA  PHE A  37       1.903  28.414 -15.105  1.00 69.73           H  
ATOM    298  HB2 PHE A  37       0.315  26.645 -14.984  1.00 64.87           H  
ATOM    299  HB3 PHE A  37       0.891  27.050 -13.561  1.00 64.87           H  
ATOM    300  HD1 PHE A  37      -2.000  27.176 -15.538  1.00 61.71           H  
ATOM    301  HD2 PHE A  37      -0.553  27.988 -11.902  1.00 61.31           H  
ATOM    302  HE1 PHE A  37      -4.146  27.500 -14.756  1.00 64.07           H  
ATOM    303  HE2 PHE A  37      -2.693  28.313 -11.118  1.00 59.88           H  
ATOM    304  HZ  PHE A  37      -4.496  28.070 -12.542  1.00 63.88           H  
ATOM    305  N   PRO A  38       0.665  28.271 -17.323  1.00 57.39           N  
ANISOU  305  N   PRO A  38     5071  10219   6517   -376    354   3029       N  
ATOM    306  CA  PRO A  38      -0.023  28.462 -18.601  1.00 54.88           C  
ANISOU  306  CA  PRO A  38     4738   9940   6176   -376    303   3152       C  
ATOM    307  C   PRO A  38      -1.216  27.520 -18.741  1.00 53.91           C  
ANISOU  307  C   PRO A  38     4689   9807   5988   -215    411   2926       C  
ATOM    308  O   PRO A  38      -1.394  26.576 -17.970  1.00 53.74           O  
ANISOU  308  O   PRO A  38     4721   9796   5902   -100    554   2695       O  
ATOM    309  CB  PRO A  38       1.068  28.130 -19.627  1.00 55.58           C  
ANISOU  309  CB  PRO A  38     4727  10346   6046   -429    368   3412       C  
ATOM    310  CG  PRO A  38       1.898  27.087 -18.940  1.00 56.16           C  
ANISOU  310  CG  PRO A  38     4794  10594   5952   -368    544   3309       C  
ATOM    311  CD  PRO A  38       1.849  27.401 -17.461  1.00 50.09           C  
ANISOU  311  CD  PRO A  38     4081   9594   5357   -370    504   3113       C  
ATOM    312  HA  PRO A  38      -0.310  29.382 -18.707  1.00 65.86           H  
ATOM    313  HB2 PRO A  38       0.665  27.776 -20.435  1.00 66.70           H  
ATOM    314  HB3 PRO A  38       1.594  28.922 -19.818  1.00 66.70           H  
ATOM    315  HG2 PRO A  38       1.521  26.210 -19.112  1.00 67.40           H  
ATOM    316  HG3 PRO A  38       2.810  27.134 -19.266  1.00 67.40           H  
ATOM    317  HD2 PRO A  38       1.731  26.587 -16.947  1.00 60.11           H  
ATOM    318  HD3 PRO A  38       2.650  27.877 -17.191  1.00 60.11           H  
ATOM    319  N   THR A  39      -2.041  27.803 -19.750  1.00 52.56           N  
ANISOU  319  N   THR A  39     4519   9612   5839   -209    337   2999       N  
ATOM    320  CA  THR A  39      -3.220  26.990 -20.008  1.00 53.57           C  
ANISOU  320  CA  THR A  39     4707   9726   5920    -68    417   2804       C  
ATOM    321  C   THR A  39      -3.524  26.983 -21.498  1.00 56.42           C  
ANISOU  321  C   THR A  39     5031  10234   6171    -72    380   2975       C  
ATOM    322  O   THR A  39      -3.168  27.913 -22.226  1.00 60.52           O  
ANISOU  322  O   THR A  39     5495  10767   6731   -183    251   3225       O  
ATOM    323  CB  THR A  39      -4.456  27.500 -19.249  1.00 52.76           C  
ANISOU  323  CB  THR A  39     4682   9298   6065    -24    330   2602       C  
ATOM    324  OG1 THR A  39      -4.702  28.869 -19.593  1.00 54.10           O  
ANISOU  324  OG1 THR A  39     4835   9293   6427   -136    127   2766       O  
ATOM    325  CG2 THR A  39      -4.267  27.373 -17.742  1.00 53.35           C  
ANISOU  325  CG2 THR A  39     4811   9228   6233     10    384   2400       C  
ATOM    326  H   THR A  39      -1.937  28.459 -20.296  1.00 63.07           H  
ATOM    327  HA  THR A  39      -3.047  26.078 -19.729  1.00 64.28           H  
ATOM    328  HB  THR A  39      -5.225  26.966 -19.502  1.00 63.31           H  
ATOM    329  HG1 THR A  39      -5.377  29.152 -19.181  1.00 64.92           H  
ATOM    330 HG21 THR A  39      -5.056  27.699 -17.282  1.00 64.03           H  
ATOM    331 HG22 THR A  39      -4.124  26.444 -17.503  1.00 64.03           H  
ATOM    332 HG23 THR A  39      -3.499  27.894 -17.460  1.00 64.03           H  
ATOM    333  N   ARG A  40      -4.182  25.915 -21.940  1.00 53.91           N  
ANISOU  333  N   ARG A  40     4747  10024   5712     55    496   2838       N  
ATOM    334  CA  ARG A  40      -4.760  25.842 -23.268  1.00 56.46           C  
ANISOU  334  CA  ARG A  40     5058  10447   5948     80    454   2939       C  
ATOM    335  C   ARG A  40      -6.281  25.829 -23.154  1.00 52.77           C  
ANISOU  335  C   ARG A  40     4653   9767   5631    165    404   2734       C  
ATOM    336  O   ARG A  40      -6.825  25.419 -22.125  1.00 47.57           O  
ANISOU  336  O   ARG A  40     4049   8958   5066    241    471   2485       O  
ATOM    337  CB  ARG A  40      -4.296  24.589 -24.020  1.00 53.76           C  
ANISOU  337  CB  ARG A  40     4704  10419   5305    158    620   2959       C  
ATOM    338  H   ARG A  40      -4.307  25.204 -21.473  1.00 64.69           H  
ATOM    339  HA  ARG A  40      -4.497  26.623 -23.779  1.00 67.75           H  
ATOM    340  N   PRO A  41      -7.002  26.268 -24.180  1.00 57.73           N  
ANISOU  340  N   PRO A  41     5273  10376   6287    159    290   2833       N  
ATOM    341  CA  PRO A  41      -8.456  26.393 -24.040  1.00 58.61           C  
ANISOU  341  CA  PRO A  41     5434  10265   6570    229    223   2653       C  
ATOM    342  C   PRO A  41      -9.154  25.049 -24.175  1.00 54.86           C  
ANISOU  342  C   PRO A  41     4996   9881   5967    372    364   2433       C  
ATOM    343  O   PRO A  41      -8.729  24.175 -24.935  1.00 57.58           O  
ANISOU  343  O   PRO A  41     5325  10482   6070    413    464   2480       O  
ATOM    344  CB  PRO A  41      -8.847  27.345 -25.182  1.00 59.65           C  
ANISOU  344  CB  PRO A  41     5534  10376   6756    166     49   2867       C  
ATOM    345  CG  PRO A  41      -7.581  27.586 -25.992  1.00 63.33           C  
ANISOU  345  CG  PRO A  41     5935  11077   7049     75     45   3158       C  
ATOM    346  CD  PRO A  41      -6.569  26.578 -25.550  1.00 61.68           C  
ANISOU  346  CD  PRO A  41     5719  11068   6648    103    227   3106       C  
ATOM    347  HA  PRO A  41      -8.684  26.795 -23.187  1.00 70.33           H  
ATOM    348  HB2 PRO A  41      -9.527  26.927 -25.732  1.00 71.58           H  
ATOM    349  HB3 PRO A  41      -9.175  28.178 -24.810  1.00 71.58           H  
ATOM    350  HG2 PRO A  41      -7.778  27.473 -26.935  1.00 75.99           H  
ATOM    351  HG3 PRO A  41      -7.257  28.484 -25.820  1.00 75.99           H  
ATOM    352  HD2 PRO A  41      -6.612  25.785 -26.108  1.00 74.01           H  
ATOM    353  HD3 PRO A  41      -5.680  26.966 -25.547  1.00 74.01           H  
ATOM    354  N   ILE A  42     -10.229  24.885 -23.409  1.00 49.83           N  
ANISOU  354  N   ILE A  42     4408   9025   5499    450    374   2191       N  
ATOM    355  CA  ILE A  42     -11.114  23.730 -23.550  1.00 45.73           C  
ANISOU  355  CA  ILE A  42     3921   8544   4909    583    482   1976       C  
ATOM    356  C   ILE A  42     -11.980  23.967 -24.782  1.00 48.81           C  
ANISOU  356  C   ILE A  42     4295   8950   5298    593    361   2055       C  
ATOM    357  O   ILE A  42     -12.439  25.098 -24.996  1.00 47.96           O  
ANISOU  357  O   ILE A  42     4177   8681   5366    531    191   2161       O  
ATOM    358  CB  ILE A  42     -11.975  23.523 -22.295  1.00 47.11           C  
ANISOU  358  CB  ILE A  42     4148   8471   5282    664    535   1703       C  
ATOM    359  CG1 ILE A  42     -11.080  23.267 -21.081  1.00 45.29           C  
ANISOU  359  CG1 ILE A  42     3937   8235   5035    662    656   1626       C  
ATOM    360  CG2 ILE A  42     -12.953  22.362 -22.497  1.00 43.47           C  
ANISOU  360  CG2 ILE A  42     3711   8037   4770    796    639   1489       C  
ATOM    361  CD1 ILE A  42     -11.815  23.210 -19.750  1.00 43.13           C  
ANISOU  361  CD1 ILE A  42     3721   7703   4963    739    703   1379       C  
ATOM    362  H   ILE A  42     -10.471  25.434 -22.793  1.00 59.79           H  
ATOM    363  HA  ILE A  42     -10.583  22.931 -23.695  1.00 54.87           H  
ATOM    364  HB  ILE A  42     -12.486  24.332 -22.135  1.00 56.54           H  
ATOM    365 HG12 ILE A  42     -10.628  22.417 -21.203  1.00 54.34           H  
ATOM    366 HG13 ILE A  42     -10.425  23.980 -21.024  1.00 54.34           H  
ATOM    367 HG21 ILE A  42     -13.484  22.253 -21.692  1.00 52.17           H  
ATOM    368 HG22 ILE A  42     -13.531  22.565 -23.249  1.00 52.17           H  
ATOM    369 HG23 ILE A  42     -12.450  21.553 -22.674  1.00 52.17           H  
ATOM    370 HD11 ILE A  42     -11.173  23.045 -19.042  1.00 51.75           H  
ATOM    371 HD12 ILE A  42     -12.263  24.058 -19.600  1.00 51.75           H  
ATOM    372 HD13 ILE A  42     -12.467  22.492 -19.780  1.00 51.75           H  
ATOM    373  N   PRO A  43     -12.239  22.955 -25.612  1.00 51.34           N  
ANISOU  373  N   PRO A  43     4619   9457   5430    673    436   2006       N  
ATOM    374  CA  PRO A  43     -13.027  23.199 -26.826  1.00 49.25           C  
ANISOU  374  CA  PRO A  43     4341   9219   5153    683    308   2088       C  
ATOM    375  C   PRO A  43     -14.483  23.499 -26.503  1.00 52.28           C  
ANISOU  375  C   PRO A  43     4744   9340   5781    733    220   1921       C  
ATOM    376  O   PRO A  43     -15.101  22.843 -25.660  1.00 50.19           O  
ANISOU  376  O   PRO A  43     4509   8957   5604    816    317   1676       O  
ATOM    377  CB  PRO A  43     -12.890  21.889 -27.617  1.00 48.05           C  
ANISOU  377  CB  PRO A  43     4200   9329   4729    768    432   2038       C  
ATOM    378  CG  PRO A  43     -11.813  21.106 -26.934  1.00 47.75           C  
ANISOU  378  CG  PRO A  43     4170   9429   4543    781    618   1991       C  
ATOM    379  CD  PRO A  43     -11.812  21.549 -25.516  1.00 49.86           C  
ANISOU  379  CD  PRO A  43     4451   9469   5026    758    635   1877       C  
ATOM    380  HA  PRO A  43     -12.648  23.931 -27.339  1.00 59.10           H  
ATOM    381  HB2 PRO A  43     -13.731  21.406 -27.592  1.00 57.66           H  
ATOM    382  HB3 PRO A  43     -12.639  22.088 -28.533  1.00 57.66           H  
ATOM    383  HG2 PRO A  43     -12.014  20.159 -26.994  1.00 57.30           H  
ATOM    384  HG3 PRO A  43     -10.958  21.299 -27.350  1.00 57.30           H  
ATOM    385  HD2 PRO A  43     -12.452  21.034 -24.999  1.00 59.84           H  
ATOM    386  HD3 PRO A  43     -10.920  21.490 -25.141  1.00 59.84           H  
ATOM    387  N   ARG A  44     -15.029  24.505 -27.190  1.00 49.76           N  
ANISOU  387  N   ARG A  44     4404   8929   5574    685     37   2062       N  
ATOM    388  CA  ARG A  44     -16.452  24.828 -27.133  1.00 52.12           C  
ANISOU  388  CA  ARG A  44     4710   9004   6088    733    -65   1938       C  
ATOM    389  C   ARG A  44     -17.101  24.252 -28.385  1.00 51.72           C  
ANISOU  389  C   ARG A  44     4649   9098   5903    795   -104   1939       C  
ATOM    390  O   ARG A  44     -16.892  24.761 -29.491  1.00 51.27           O  
ANISOU  390  O   ARG A  44     4570   9160   5752    750   -215   2152       O  
ATOM    391  CB  ARG A  44     -16.675  26.336 -27.039  1.00 55.43           C  
ANISOU  391  CB  ARG A  44     5117   9215   6728    645   -244   2087       C  
ATOM    392  CG  ARG A  44     -16.115  26.972 -25.775  1.00 57.86           C  
ANISOU  392  CG  ARG A  44     5444   9353   7188    584   -226   2074       C  
ATOM    393  CD  ARG A  44     -16.301  28.483 -25.785  1.00 60.77           C  
ANISOU  393  CD  ARG A  44     5803   9522   7763    493   -410   2237       C  
ATOM    394  NE  ARG A  44     -17.701  28.867 -25.957  1.00 68.89           N  
ANISOU  394  NE  ARG A  44     6838  10357   8981    545   -520   2157       N  
ATOM    395  CZ  ARG A  44     -18.576  29.011 -24.964  1.00 68.93           C  
ANISOU  395  CZ  ARG A  44     6876  10104   9209    599   -516   1967       C  
ATOM    396  NH1 ARG A  44     -18.215  28.807 -23.703  1.00 68.61           N  
ANISOU  396  NH1 ARG A  44     6873   9964   9232    613   -409   1829       N  
ATOM    397  NH2 ARG A  44     -19.825  29.362 -25.236  1.00 69.34           N  
ANISOU  397  NH2 ARG A  44     6925  10001   9422    646   -618   1918       N  
ATOM    398  H   ARG A  44     -14.582  25.025 -27.709  1.00 59.71           H  
ATOM    399  HA  ARG A  44     -16.850  24.407 -26.355  1.00 62.54           H  
ATOM    400  HB2 ARG A  44     -16.247  26.761 -27.798  1.00 66.52           H  
ATOM    401  HB3 ARG A  44     -17.629  26.511 -27.060  1.00 66.52           H  
ATOM    402  HG2 ARG A  44     -16.580  26.614 -25.002  1.00 69.44           H  
ATOM    403  HG3 ARG A  44     -15.166  26.782 -25.714  1.00 69.44           H  
ATOM    404  HD2 ARG A  44     -15.989  28.848 -24.942  1.00 72.92           H  
ATOM    405  HD3 ARG A  44     -15.792  28.861 -26.520  1.00 72.92           H  
ATOM    406  HE  ARG A  44     -17.979  29.009 -26.758  1.00 82.67           H  
ATOM    407 HH11 ARG A  44     -17.406  28.579 -23.520  1.00 82.33           H  
ATOM    408 HH12 ARG A  44     -18.789  28.904 -23.070  1.00 82.33           H  
ATOM    409 HH21 ARG A  44     -20.067  29.496 -26.051  1.00 83.21           H  
ATOM    410 HH22 ARG A  44     -20.394  29.457 -24.598  1.00 83.21           H  
ATOM    411  N   LEU A  45     -17.883  23.189 -28.213  1.00 50.18           N  
ANISOU  411  N   LEU A  45     4472   8893   5700    900    -12   1702       N  
ATOM    412  CA  LEU A  45     -18.440  22.446 -29.331  1.00 55.67           C  
ANISOU  412  CA  LEU A  45     5163   9741   6248    967    -31   1670       C  
ATOM    413  C   LEU A  45     -19.947  22.317 -29.173  1.00 64.23           C  
ANISOU  413  C   LEU A  45     6243  10624   7535   1040    -89   1475       C  
ATOM    414  O   LEU A  45     -20.526  22.656 -28.136  1.00 54.03           O  
ANISOU  414  O   LEU A  45     4957   9089   6484   1052    -84   1348       O  
ATOM    415  CB  LEU A  45     -17.806  21.052 -29.443  1.00 59.69           C  
ANISOU  415  CB  LEU A  45     5695  10485   6499   1028    154   1576       C  
ATOM    416  CG  LEU A  45     -16.293  21.008 -29.666  1.00 61.58           C  
ANISOU  416  CG  LEU A  45     5934  10954   6510    969    231   1765       C  
ATOM    417  CD1 LEU A  45     -15.802  19.571 -29.642  1.00 61.50           C  
ANISOU  417  CD1 LEU A  45     5951  11146   6269   1045    427   1637       C  
ATOM    418  CD2 LEU A  45     -15.917  21.678 -30.977  1.00 62.87           C  
ANISOU  418  CD2 LEU A  45     6075  11271   6543    913     96   2038       C  
ATOM    419  H   LEU A  45     -18.107  22.877 -27.444  1.00 60.21           H  
ATOM    420  HA  LEU A  45     -18.262  22.927 -30.154  1.00 66.81           H  
ATOM    421  HB2 LEU A  45     -17.990  20.569 -28.622  1.00 71.63           H  
ATOM    422  HB3 LEU A  45     -18.220  20.589 -30.188  1.00 71.63           H  
ATOM    423  HG  LEU A  45     -15.854  21.488 -28.947  1.00 73.90           H  
ATOM    424 HD11 LEU A  45     -14.843  19.563 -29.785  1.00 73.80           H  
ATOM    425 HD12 LEU A  45     -16.012  19.181 -28.779  1.00 73.80           H  
ATOM    426 HD13 LEU A  45     -16.246  19.074 -30.346  1.00 73.80           H  
ATOM    427 HD21 LEU A  45     -14.954  21.633 -31.088  1.00 75.45           H  
ATOM    428 HD22 LEU A  45     -16.357  21.213 -31.706  1.00 75.45           H  
ATOM    429 HD23 LEU A  45     -16.205  22.603 -30.952  1.00 75.45           H  
ATOM    430  N   SER A  46     -20.577  21.818 -30.230  1.00 60.88           N  
ANISOU  430  N   SER A  46     5811  10309   7011   1093   -146   1455       N  
ATOM    431  CA  SER A  46     -22.003  21.545 -30.232  1.00 57.93           C  
ANISOU  431  CA  SER A  46     5425   9781   6805   1167   -200   1270       C  
ATOM    432  C   SER A  46     -22.267  20.096 -29.847  1.00 56.18           C  
ANISOU  432  C   SER A  46     5221   9608   6516   1261    -29   1018       C  
ATOM    433  O   SER A  46     -21.485  19.194 -30.160  1.00 56.05           O  
ANISOU  433  O   SER A  46     5229   9816   6253   1281     92   1014       O  
ATOM    434  CB  SER A  46     -22.604  21.828 -31.608  1.00 59.47           C  
ANISOU  434  CB  SER A  46     5598  10057   6940   1173   -373   1383       C  
ATOM    435  OG  SER A  46     -23.908  21.284 -31.710  1.00 58.13           O  
ANISOU  435  OG  SER A  46     5412   9787   6886   1254   -406   1186       O  
ATOM    436  H   SER A  46     -20.188  21.626 -30.973  1.00 73.06           H  
ATOM    437  HA  SER A  46     -22.441  22.118 -29.583  1.00 69.51           H  
ATOM    438  HB2 SER A  46     -22.651  22.788 -31.741  1.00 71.36           H  
ATOM    439  HB3 SER A  46     -22.040  21.426 -32.287  1.00 71.36           H  
ATOM    440  HG  SER A  46     -24.407  21.623 -31.126  1.00 69.75           H  
ATOM    441  N   GLN A  47     -23.392  19.882 -29.162  1.00 62.83           N  
ANISOU  441  N   GLN A  47     6052  10236   7586   1322    -15    810       N  
ATOM    442  CA  GLN A  47     -23.798  18.528 -28.800  1.00 65.47           C  
ANISOU  442  CA  GLN A  47     6397  10589   7891   1414    141    564       C  
ATOM    443  C   GLN A  47     -23.826  17.609 -30.015  1.00 65.44           C  
ANISOU  443  C   GLN A  47     6398  10819   7648   1454    133    554       C  
ATOM    444  O   GLN A  47     -23.545  16.411 -29.893  1.00 67.45           O  
ANISOU  444  O   GLN A  47     6677  11194   7757   1510    291    417       O  
ATOM    445  CB  GLN A  47     -25.167  18.574 -28.108  1.00 67.73           C  
ANISOU  445  CB  GLN A  47     6656  10603   8476   1472    119    374       C  
ATOM    446  CG  GLN A  47     -26.016  17.315 -28.234  1.00 69.07           C  
ANISOU  446  CG  GLN A  47     6814  10783   8646   1567    197    145       C  
ATOM    447  CD  GLN A  47     -26.852  17.291 -29.498  1.00 70.46           C  
ANISOU  447  CD  GLN A  47     6956  11018   8796   1580     28    173       C  
ATOM    448  OE1 GLN A  47     -27.099  18.329 -30.113  1.00 70.48           O  
ANISOU  448  OE1 GLN A  47     6937  10986   8856   1531   -155    337       O  
ATOM    449  NE2 GLN A  47     -27.297  16.101 -29.893  1.00 74.57           N  
ANISOU  449  NE2 GLN A  47     7475  11626   9233   1648     88     10       N  
ATOM    450  H   GLN A  47     -23.931  20.498 -28.898  1.00 75.40           H  
ATOM    451  HA  GLN A  47     -23.157  18.167 -28.168  1.00 78.57           H  
ATOM    452  HB2 GLN A  47     -25.026  18.736 -27.162  1.00 81.28           H  
ATOM    453  HB3 GLN A  47     -25.677  19.307 -28.488  1.00 81.28           H  
ATOM    454  HG2 GLN A  47     -25.433  16.541 -28.245  1.00 82.88           H  
ATOM    455  HG3 GLN A  47     -26.619  17.265 -27.475  1.00 82.88           H  
ATOM    456 HE21 GLN A  47     -27.106  15.398 -29.436  1.00 89.49           H  
ATOM    457 HE22 GLN A  47     -27.775  16.035 -30.605  1.00 89.49           H  
ATOM    458  N   SER A  48     -24.148  18.148 -31.192  1.00 61.34           N  
ANISOU  458  N   SER A  48     5859  10367   7079   1430    -49    699       N  
ATOM    459  CA  SER A  48     -24.200  17.352 -32.411  1.00 61.71           C  
ANISOU  459  CA  SER A  48     5919  10634   6894   1471    -78    699       C  
ATOM    460  C   SER A  48     -22.825  17.078 -33.007  1.00 63.41           C  
ANISOU  460  C   SER A  48     6174  11130   6791   1444     -7    863       C  
ATOM    461  O   SER A  48     -22.719  16.250 -33.917  1.00 63.79           O  
ANISOU  461  O   SER A  48     6247  11377   6612   1491      7    846       O  
ATOM    462  CB  SER A  48     -25.065  18.058 -33.456  1.00 65.99           C  
ANISOU  462  CB  SER A  48     6429  11146   7497   1464   -305    798       C  
ATOM    463  OG  SER A  48     -24.466  19.277 -33.864  1.00 67.50           O  
ANISOU  463  OG  SER A  48     6617  11368   7663   1384   -422   1063       O  
ATOM    464  H   SER A  48     -24.340  18.978 -31.308  1.00 73.60           H  
ATOM    465  HA  SER A  48     -24.613  16.498 -32.210  1.00 74.05           H  
ATOM    466  HB2 SER A  48     -25.162  17.480 -34.229  1.00 79.18           H  
ATOM    467  HB3 SER A  48     -25.935  18.247 -33.072  1.00 79.18           H  
ATOM    468  HG  SER A  48     -24.376  19.787 -33.203  1.00 81.00           H  
ATOM    469  N   ASP A  49     -21.782  17.742 -32.525  1.00 65.97           N  
ANISOU  469  N   ASP A  49     6503  11471   7092   1373     36   1020       N  
ATOM    470  CA  ASP A  49     -20.452  17.582 -33.099  1.00 64.48           C  
ANISOU  470  CA  ASP A  49     6342  11545   6614   1342     99   1201       C  
ATOM    471  C   ASP A  49     -19.830  16.281 -32.607  1.00 65.15           C  
ANISOU  471  C   ASP A  49     6463  11758   6534   1397    322   1051       C  
ATOM    472  O   ASP A  49     -19.658  16.111 -31.396  1.00 64.48           O  
ANISOU  472  O   ASP A  49     6380  11553   6568   1398    449    933       O  
ATOM    473  CB  ASP A  49     -19.568  18.759 -32.715  1.00 64.78           C  
ANISOU  473  CB  ASP A  49     6363  11545   6706   1242     64   1420       C  
ATOM    474  CG  ASP A  49     -18.266  18.787 -33.488  1.00 64.53           C  
ANISOU  474  CG  ASP A  49     6344  11781   6392   1203     94   1652       C  
ATOM    475  OD1 ASP A  49     -17.814  17.713 -33.935  1.00 66.46           O  
ANISOU  475  OD1 ASP A  49     6622  12240   6391   1260    209   1607       O  
ATOM    476  OD2 ASP A  49     -17.694  19.885 -33.650  1.00 66.31           O  
ANISOU  476  OD2 ASP A  49     6547  12002   6646   1117      4   1883       O  
ATOM    477  H   ASP A  49     -21.818  18.292 -31.864  1.00 79.16           H  
ATOM    478  HA  ASP A  49     -20.518  17.548 -34.066  1.00 77.38           H  
ATOM    479  HB2 ASP A  49     -20.043  19.584 -32.897  1.00 77.74           H  
ATOM    480  HB3 ASP A  49     -19.355  18.699 -31.770  1.00 77.74           H  
ATOM    481  N   PRO A  50     -19.473  15.347 -33.495  1.00 73.78           N  
ANISOU  481  N   PRO A  50     8810  12613   6609    206   -419    635       N  
ATOM    482  CA  PRO A  50     -18.854  14.099 -33.016  1.00 72.02           C  
ANISOU  482  CA  PRO A  50     8654  12299   6410    303   -361    405       C  
ATOM    483  C   PRO A  50     -17.588  14.327 -32.212  1.00 67.27           C  
ANISOU  483  C   PRO A  50     7971  11669   5917    428   -194    345       C  
ATOM    484  O   PRO A  50     -17.277  13.521 -31.326  1.00 63.99           O  
ANISOU  484  O   PRO A  50     7559  11124   5629    517   -169    220       O  
ATOM    485  CB  PRO A  50     -18.567  13.325 -34.311  1.00 72.78           C  
ANISOU  485  CB  PRO A  50     8905  12509   6239    259   -359    249       C  
ATOM    486  CG  PRO A  50     -19.484  13.909 -35.323  1.00 74.22           C  
ANISOU  486  CG  PRO A  50     9117  12802   6280    108   -480    407       C  
ATOM    487  CD  PRO A  50     -19.634  15.352 -34.959  1.00 73.86           C  
ANISOU  487  CD  PRO A  50     8920  12784   6360     91   -466    642       C  
ATOM    488  HA  PRO A  50     -19.486  13.597 -32.478  1.00 86.42           H  
ATOM    489  HB2 PRO A  50     -17.642  13.455 -34.571  1.00 87.34           H  
ATOM    490  HB3 PRO A  50     -18.758  12.383 -34.178  1.00 87.34           H  
ATOM    491  HG2 PRO A  50     -19.092  13.820 -36.206  1.00 89.06           H  
ATOM    492  HG3 PRO A  50     -20.341  13.458 -35.283  1.00 89.06           H  
ATOM    493  HD2 PRO A  50     -18.935  15.881 -35.375  1.00 88.64           H  
ATOM    494  HD3 PRO A  50     -20.516  15.673 -35.202  1.00 88.64           H  
ATOM    495  N   ARG A  51     -16.843  15.397 -32.499  1.00 71.31           N  
ANISOU  495  N   ARG A  51     8411  12300   6383    428    -90    442       N  
ATOM    496  CA  ARG A  51     -15.637  15.688 -31.731  1.00 73.84           C  
ANISOU  496  CA  ARG A  51     8646  12601   6809    531     59    411       C  
ATOM    497  C   ARG A  51     -15.948  15.799 -30.245  1.00 68.94           C  
ANISOU  497  C   ARG A  51     7946  11796   6451    586     33    463       C  
ATOM    498  O   ARG A  51     -15.185  15.310 -29.404  1.00 68.52           O  
ANISOU  498  O   ARG A  51     7867  11658   6507    680    110    359       O  
ATOM    499  CB  ARG A  51     -14.988  16.972 -32.243  1.00 73.30           C  
ANISOU  499  CB  ARG A  51     8507  12683   6660    490    140    556       C  
ATOM    500  CG  ARG A  51     -14.431  16.850 -33.648  1.00 79.18           C  
ANISOU  500  CG  ARG A  51     9319  13634   7131    442    200    491       C  
ATOM    501  CD  ARG A  51     -13.803  18.153 -34.114  1.00 80.71           C  
ANISOU  501  CD  ARG A  51     9434  13982   7250    383    268    657       C  
ATOM    502  NE  ARG A  51     -14.795  19.211 -34.295  1.00 81.13           N  
ANISOU  502  NE  ARG A  51     9461  14029   7336    275    141    882       N  
ATOM    503  CZ  ARG A  51     -14.507  20.453 -34.676  1.00 78.58           C  
ANISOU  503  CZ  ARG A  51     9078  13810   6970    202    153   1064       C  
ATOM    504  NH1 ARG A  51     -13.251  20.804 -34.920  1.00 78.98           N  
ANISOU  504  NH1 ARG A  51     9083  13993   6932    215    288   1057       N  
ATOM    505  NH2 ARG A  51     -15.476  21.346 -34.815  1.00 77.70           N  
ANISOU  505  NH2 ARG A  51     8946  13669   6907    116     23   1263       N  
ATOM    506  H   ARG A  51     -17.013  15.962 -33.126  1.00 85.57           H  
ATOM    507  HA  ARG A  51     -15.003  14.963 -31.851  1.00 88.61           H  
ATOM    508  HB2 ARG A  51     -15.653  17.679 -32.246  1.00 87.96           H  
ATOM    509  HB3 ARG A  51     -14.257  17.210 -31.652  1.00 87.96           H  
ATOM    510  HG2 ARG A  51     -13.748  16.161 -33.663  1.00 95.02           H  
ATOM    511  HG3 ARG A  51     -15.150  16.624 -34.259  1.00 95.02           H  
ATOM    512  HD2 ARG A  51     -13.161  18.451 -33.451  1.00 96.85           H  
ATOM    513  HD3 ARG A  51     -13.360  18.006 -34.965  1.00 96.85           H  
ATOM    514  HE  ARG A  51     -15.620  19.018 -34.144  1.00 97.36           H  
ATOM    515 HH11 ARG A  51     -12.619  20.228 -34.832  1.00 94.77           H  
ATOM    516 HH12 ARG A  51     -13.069  21.608 -35.166  1.00 94.77           H  
ATOM    517 HH21 ARG A  51     -16.292  21.124 -34.658  1.00 93.24           H  
ATOM    518 HH22 ARG A  51     -15.289  22.149 -35.061  1.00 93.24           H  
ATOM    519  N   ALA A  52     -17.066  16.443 -29.900  1.00 63.13           N  
ANISOU  519  N   ALA A  52     7168  11001   5819    530    -74    627       N  
ATOM    520  CA  ALA A  52     -17.479  16.505 -28.504  1.00 58.86           C  
ANISOU  520  CA  ALA A  52     6559  10295   5512    578    -99    670       C  
ATOM    521  C   ALA A  52     -17.863  15.130 -27.981  1.00 59.07           C  
ANISOU  521  C   ALA A  52     6642  10203   5597    606   -161    523       C  
ATOM    522  O   ALA A  52     -17.717  14.856 -26.785  1.00 56.94           O  
ANISOU  522  O   ALA A  52     6332   9806   5497    665   -141    492       O  
ATOM    523  CB  ALA A  52     -18.649  17.474 -28.346  1.00 53.64           C  
ANISOU  523  CB  ALA A  52     5836   9608   4936    521   -194    873       C  
ATOM    524  H   ALA A  52     -17.592  16.845 -30.448  1.00 75.76           H  
ATOM    525  HA  ALA A  52     -16.740  16.835 -27.969  1.00 70.64           H  
ATOM    526  HB1 ALA A  52     -18.911  17.503 -27.412  1.00 64.37           H  
ATOM    527  HB2 ALA A  52     -18.370  18.356 -28.639  1.00 64.37           H  
ATOM    528  HB3 ALA A  52     -19.391  17.164 -28.888  1.00 64.37           H  
ATOM    529  N   GLU A  53     -18.348  14.256 -28.863  1.00 66.03           N  
ANISOU  529  N   GLU A  53     7628  11123   6337    554   -246    436       N  
ATOM    530  CA  GLU A  53     -18.770  12.924 -28.448  1.00 68.38           C  
ANISOU  530  CA  GLU A  53     7997  11303   6682    565   -331    304       C  
ATOM    531  C   GLU A  53     -17.572  12.053 -28.092  1.00 73.34           C  
ANISOU  531  C   GLU A  53     8663  11877   7327    669   -232    108       C  
ATOM    532  O   GLU A  53     -17.629  11.269 -27.137  1.00 67.65           O  
ANISOU  532  O   GLU A  53     7944  11014   6745    709   -267     36       O  
ATOM    533  CB  GLU A  53     -19.592  12.278 -29.562  1.00 70.87           C  
ANISOU  533  CB  GLU A  53     8430  11672   6825    469   -460    270       C  
ATOM    534  CG  GLU A  53     -20.494  11.150 -29.113  1.00 73.43           C  
ANISOU  534  CG  GLU A  53     8813  11869   7217    434   -605    214       C  
ATOM    535  CD  GLU A  53     -21.705  11.645 -28.340  1.00 73.60           C  
ANISOU  535  CD  GLU A  53     8728  11836   7400    381   -703    402       C  
ATOM    536  OE1 GLU A  53     -21.656  12.776 -27.811  1.00 73.36           O  
ANISOU  536  OE1 GLU A  53     8575  11820   7477    412   -633    539       O  
ATOM    537  OE2 GLU A  53     -22.711  10.909 -28.271  1.00 73.77           O  
ANISOU  537  OE2 GLU A  53     8788  11803   7438    308   -852    414       O  
ATOM    538  H   GLU A  53     -18.442  14.411 -29.704  1.00 79.24           H  
ATOM    539  HA  GLU A  53     -19.333  12.999 -27.661  1.00 82.06           H  
ATOM    540  HB2 GLU A  53     -20.152  12.958 -29.967  1.00 85.04           H  
ATOM    541  HB3 GLU A  53     -18.983  11.919 -30.227  1.00 85.04           H  
ATOM    542  HG2 GLU A  53     -20.812  10.669 -29.893  1.00 88.11           H  
ATOM    543  HG3 GLU A  53     -19.992  10.554 -28.536  1.00 88.11           H  
ATOM    544  N   GLU A  54     -16.480  12.172 -28.850  1.00 80.98           N  
ANISOU  544  N   GLU A  54     9652  12960   8156    713   -110     27       N  
ATOM    545  CA  GLU A  54     -15.275  11.411 -28.546  1.00 84.70           C  
ANISOU  545  CA  GLU A  54    10139  13393   8651    827     -4   -150       C  
ATOM    546  C   GLU A  54     -14.518  11.992 -27.360  1.00 81.75           C  
ANISOU  546  C   GLU A  54     9640  12958   8464    894     90    -86       C  
ATOM    547  O   GLU A  54     -13.860  11.245 -26.627  1.00 85.08           O  
ANISOU  547  O   GLU A  54    10056  13279   8993    978    126   -200       O  
ATOM    548  CB  GLU A  54     -14.361  11.353 -29.772  1.00 84.92           C  
ANISOU  548  CB  GLU A  54    10219  13586   8461    856    107   -255       C  
ATOM    549  CG  GLU A  54     -13.899  12.712 -30.275  1.00 85.46           C  
ANISOU  549  CG  GLU A  54    10199  13824   8447    818    203   -104       C  
ATOM    550  CD  GLU A  54     -12.882  12.610 -31.398  1.00 89.26           C  
ANISOU  550  CD  GLU A  54    10715  14485   8713    851    332   -212       C  
ATOM    551  OE1 GLU A  54     -12.209  11.562 -31.502  1.00 90.12           O  
ANISOU  551  OE1 GLU A  54    10883  14572   8788    949    393   -414       O  
ATOM    552  OE2 GLU A  54     -12.757  13.580 -32.177  1.00 90.97           O  
ANISOU  552  OE2 GLU A  54    10901  14870   8796    779    372    -92       O  
ATOM    553  H   GLU A  54     -16.414  12.684 -29.538  1.00 97.17           H  
ATOM    554  HA  GLU A  54     -15.528  10.502 -28.321  1.00101.64           H  
ATOM    555  HB2 GLU A  54     -13.571  10.838 -29.547  1.00101.90           H  
ATOM    556  HB3 GLU A  54     -14.839  10.918 -30.496  1.00101.90           H  
ATOM    557  HG2 GLU A  54     -14.667  13.203 -30.610  1.00102.55           H  
ATOM    558  HG3 GLU A  54     -13.489  13.198 -29.542  1.00102.55           H  
ATOM    559  N   LEU A  55     -14.586  13.310 -27.157  1.00 62.96           N  
ANISOU  559  N   LEU A  55     7165  10631   6125    855    123     97       N  
ATOM    560  CA  LEU A  55     -13.970  13.900 -25.974  1.00 55.95           C  
ANISOU  560  CA  LEU A  55     6175   9671   5414    902    194    167       C  
ATOM    561  C   LEU A  55     -14.593  13.344 -24.701  1.00 56.17           C  
ANISOU  561  C   LEU A  55     6195   9518   5632    911    112    158       C  
ATOM    562  O   LEU A  55     -13.882  13.013 -23.746  1.00 55.87           O  
ANISOU  562  O   LEU A  55     6121   9388   5721    971    159    106       O  
ATOM    563  CB  LEU A  55     -14.099  15.422 -26.016  1.00 60.02           C  
ANISOU  563  CB  LEU A  55     6616  10255   5936    848    217    367       C  
ATOM    564  CG  LEU A  55     -13.148  16.154 -26.964  1.00 65.24           C  
ANISOU  564  CG  LEU A  55     7253  11091   6445    838    322    405       C  
ATOM    565  CD1 LEU A  55     -13.540  17.614 -27.075  1.00 66.93           C  
ANISOU  565  CD1 LEU A  55     7415  11350   6666    766    300    615       C  
ATOM    566  CD2 LEU A  55     -11.708  16.032 -26.494  1.00 65.13           C  
ANISOU  566  CD2 LEU A  55     7182  11087   6478    918    451    339       C  
ATOM    567  H   LEU A  55     -14.975  13.872 -27.680  1.00 75.55           H  
ATOM    568  HA  LEU A  55     -13.025  13.680 -25.967  1.00 67.14           H  
ATOM    569  HB2 LEU A  55     -15.004  15.643 -26.288  1.00 72.03           H  
ATOM    570  HB3 LEU A  55     -13.938  15.766 -25.124  1.00 72.03           H  
ATOM    571  HG  LEU A  55     -13.212  15.757 -27.847  1.00 78.29           H  
ATOM    572 HD11 LEU A  55     -12.926  18.061 -27.679  1.00 80.32           H  
ATOM    573 HD12 LEU A  55     -14.445  17.673 -27.419  1.00 80.32           H  
ATOM    574 HD13 LEU A  55     -13.493  18.021 -26.195  1.00 80.32           H  
ATOM    575 HD21 LEU A  55     -11.132  16.506 -27.115  1.00 78.15           H  
ATOM    576 HD22 LEU A  55     -11.631  16.421 -25.609  1.00 78.15           H  
ATOM    577 HD23 LEU A  55     -11.464  15.094 -26.466  1.00 78.15           H  
ATOM    578  N   ILE A  56     -15.922  13.229 -24.670  1.00 56.11           N  
ANISOU  578  N   ILE A  56     6212   9465   5642    844    -14    218       N  
ATOM    579  CA  ILE A  56     -16.587  12.629 -23.520  1.00 55.90           C  
ANISOU  579  CA  ILE A  56     6176   9287   5777    839    -97    212       C  
ATOM    580  C   ILE A  56     -16.240  11.150 -23.422  1.00 56.08           C  
ANISOU  580  C   ILE A  56     6279   9225   5803    880   -134     27       C  
ATOM    581  O   ILE A  56     -16.026  10.620 -22.325  1.00 57.24           O  
ANISOU  581  O   ILE A  56     6406   9247   6097    910   -145    -13       O  
ATOM    582  CB  ILE A  56     -18.109  12.850 -23.610  1.00 58.80           C  
ANISOU  582  CB  ILE A  56     6538   9651   6153    755   -222    331       C  
ATOM    583  CG1 ILE A  56     -18.427  14.348 -23.610  1.00 62.12           C  
ANISOU  583  CG1 ILE A  56     6874  10131   6597    734   -187    515       C  
ATOM    584  CG2 ILE A  56     -18.817  12.164 -22.449  1.00 59.51           C  
ANISOU  584  CG2 ILE A  56     6612   9605   6395    741   -307    328       C  
ATOM    585  CD1 ILE A  56     -19.864  14.677 -23.930  1.00 63.69           C  
ANISOU  585  CD1 ILE A  56     7055  10356   6790    662   -301    645       C  
ATOM    586  H   ILE A  56     -16.453  13.489 -25.295  1.00 67.33           H  
ATOM    587  HA  ILE A  56     -16.271  13.064 -22.712  1.00 67.08           H  
ATOM    588  HB  ILE A  56     -18.429  12.465 -24.441  1.00 70.56           H  
ATOM    589 HG12 ILE A  56     -18.231  14.707 -22.731  1.00 74.54           H  
ATOM    590 HG13 ILE A  56     -17.870  14.784 -24.273  1.00 74.54           H  
ATOM    591 HG21 ILE A  56     -19.772  12.317 -22.528  1.00 71.42           H  
ATOM    592 HG22 ILE A  56     -18.630  11.213 -22.483  1.00 71.42           H  
ATOM    593 HG23 ILE A  56     -18.490  12.537 -21.616  1.00 71.42           H  
ATOM    594 HD11 ILE A  56     -19.979  15.640 -23.909  1.00 76.43           H  
ATOM    595 HD12 ILE A  56     -20.076  14.338 -24.814  1.00 76.43           H  
ATOM    596 HD13 ILE A  56     -20.438  14.260 -23.269  1.00 76.43           H  
ATOM    597  N   GLU A  57     -16.181  10.460 -24.562  1.00 67.77           N  
ANISOU  597  N   GLU A  57     7861  10768   7123    878   -159    -91       N  
ATOM    598  CA  GLU A  57     -15.831   9.042 -24.557  1.00 71.64           C  
ANISOU  598  CA  GLU A  57     8445  11164   7610    927   -198   -281       C  
ATOM    599  C   GLU A  57     -14.396   8.829 -24.087  1.00 71.26           C  
ANISOU  599  C   GLU A  57     8356  11087   7632   1042    -72   -378       C  
ATOM    600  O   GLU A  57     -14.122   7.903 -23.315  1.00 75.38           O  
ANISOU  600  O   GLU A  57     8896  11471   8274   1087   -109   -471       O  
ATOM    601  CB  GLU A  57     -16.034   8.448 -25.951  1.00 73.57           C  
ANISOU  601  CB  GLU A  57     8821  11487   7646    904   -241   -392       C  
ATOM    602  CG  GLU A  57     -15.719   6.960 -26.054  1.00 76.46           C  
ANISOU  602  CG  GLU A  57     9311  11743   7996    961   -293   -603       C  
ATOM    603  CD  GLU A  57     -16.589   6.108 -25.149  1.00 79.79           C  
ANISOU  603  CD  GLU A  57     9765  11993   8558    909   -455   -599       C  
ATOM    604  OE1 GLU A  57     -17.696   6.558 -24.785  1.00 79.38           O  
ANISOU  604  OE1 GLU A  57     9665  11940   8558    808   -547   -442       O  
ATOM    605  OE2 GLU A  57     -16.164   4.987 -24.799  1.00 83.54           O  
ANISOU  605  OE2 GLU A  57    10309  12337   9094    968   -493   -748       O  
ATOM    606  H   GLU A  57     -16.337  10.786 -25.343  1.00 81.33           H  
ATOM    607  HA  GLU A  57     -16.419   8.575 -23.943  1.00 85.96           H  
ATOM    608  HB2 GLU A  57     -16.961   8.572 -26.209  1.00 88.29           H  
ATOM    609  HB3 GLU A  57     -15.456   8.916 -26.575  1.00 88.29           H  
ATOM    610  HG2 GLU A  57     -15.863   6.670 -26.969  1.00 91.75           H  
ATOM    611  HG3 GLU A  57     -14.793   6.816 -25.803  1.00 91.75           H  
ATOM    612  N   ASN A  58     -13.468   9.669 -24.544  1.00 62.85           N  
ANISOU  612  N   ASN A  58     7230  10154   6498   1083     70   -347       N  
ATOM    613  CA  ASN A  58     -12.080   9.598 -24.106  1.00 57.14           C  
ANISOU  613  CA  ASN A  58     6441   9424   5844   1185    195   -409       C  
ATOM    614  C   ASN A  58     -11.851  10.291 -22.768  1.00 59.44           C  
ANISOU  614  C   ASN A  58     6622   9638   6322   1176    219   -279       C  
ATOM    615  O   ASN A  58     -10.697  10.504 -22.386  1.00 59.15           O  
ANISOU  615  O   ASN A  58     6512   9616   6344   1239    323   -283       O  
ATOM    616  CB  ASN A  58     -11.165  10.210 -25.171  1.00 62.92           C  
ANISOU  616  CB  ASN A  58     7146  10348   6413   1221    336   -418       C  
ATOM    617  H   ASN A  58     -13.622  10.294 -25.114  1.00 75.42           H  
ATOM    618  HA  ASN A  58     -11.833   8.666 -24.003  1.00 68.56           H  
ATOM    619  N   GLU A  59     -12.920  10.644 -22.058  1.00 62.93           N  
ANISOU  619  N   GLU A  59     7051  10004   6854   1098    127   -163       N  
ATOM    620  CA  GLU A  59     -12.837  11.272 -20.742  1.00 64.43           C  
ANISOU  620  CA  GLU A  59     7157  10112   7211   1082    142    -49       C  
ATOM    621  C   GLU A  59     -11.904  12.482 -20.768  1.00 61.59           C  
ANISOU  621  C   GLU A  59     6715   9846   6839   1097    267     50       C  
ATOM    622  O   GLU A  59     -10.935  12.580 -20.014  1.00 59.64           O  
ANISOU  622  O   GLU A  59     6412   9560   6691   1134    331     55       O  
ATOM    623  CB  GLU A  59     -12.398  10.259 -19.682  1.00 63.33           C  
ANISOU  623  CB  GLU A  59     7019   9823   7220   1122    109   -138       C  
ATOM    624  CG  GLU A  59     -13.400   9.137 -19.469  1.00 60.53           C  
ANISOU  624  CG  GLU A  59     6742   9358   6898   1084    -38   -205       C  
ATOM    625  CD  GLU A  59     -13.175   8.386 -18.174  1.00 57.26           C  
ANISOU  625  CD  GLU A  59     6315   8787   6656   1089    -91   -235       C  
ATOM    626  OE1 GLU A  59     -12.593   7.282 -18.223  1.00 62.29           O  
ANISOU  626  OE1 GLU A  59     6999   9349   7318   1149   -117   -373       O  
ATOM    627  OE2 GLU A  59     -13.573   8.901 -17.108  1.00 55.31           O  
ANISOU  627  OE2 GLU A  59     6013   8487   6515   1033   -107   -122       O  
ATOM    628  H   GLU A  59     -13.728  10.526 -22.327  1.00 75.51           H  
ATOM    629  HA  GLU A  59     -13.720  11.589 -20.495  1.00 77.32           H  
ATOM    630  HB2 GLU A  59     -11.558   9.860 -19.957  1.00 75.99           H  
ATOM    631  HB3 GLU A  59     -12.283  10.720 -18.836  1.00 75.99           H  
ATOM    632  HG2 GLU A  59     -14.295   9.512 -19.445  1.00 72.64           H  
ATOM    633  HG3 GLU A  59     -13.325   8.503 -20.199  1.00 72.64           H  
ATOM    634  N   GLU A  60     -12.223  13.411 -21.661  1.00 63.78           N  
ANISOU  634  N   GLU A  60     6989  10250   6994   1056    289    140       N  
ATOM    635  CA  GLU A  60     -11.543  14.691 -21.748  1.00 58.07           C  
ANISOU  635  CA  GLU A  60     6198   9616   6250   1043    382    264       C  
ATOM    636  C   GLU A  60     -12.563  15.812 -21.639  1.00 52.69           C  
ANISOU  636  C   GLU A  60     5503   8930   5585    973    331    427       C  
ATOM    637  O   GLU A  60     -13.706  15.661 -22.080  1.00 49.06           O  
ANISOU  637  O   GLU A  60     5084   8476   5081    933    244    441       O  
ATOM    638  CB  GLU A  60     -10.771  14.828 -23.066  1.00 63.24           C  
ANISOU  638  CB  GLU A  60     6855  10449   6726   1063    467    227       C  
ATOM    639  CG  GLU A  60      -9.614  13.866 -23.202  1.00 63.80           C  
ANISOU  639  CG  GLU A  60     6918  10540   6781   1155    545     72       C  
ATOM    640  CD  GLU A  60      -8.826  14.099 -24.470  1.00 67.98           C  
ANISOU  640  CD  GLU A  60     7436  11268   7125   1175    649     43       C  
ATOM    641  OE1 GLU A  60      -8.819  13.204 -25.341  1.00 71.02           O  
ANISOU  641  OE1 GLU A  60     7890  11706   7386   1218    657   -107       O  
ATOM    642  OE2 GLU A  60      -8.226  15.188 -24.599  1.00 67.22           O  
ANISOU  642  OE2 GLU A  60     7266  11276   6998   1141    721    173       O  
ATOM    643  H   GLU A  60     -12.850  13.318 -22.242  1.00 76.54           H  
ATOM    644  HA  GLU A  60     -10.914  14.774 -21.014  1.00 69.68           H  
ATOM    645  HB2 GLU A  60     -11.381  14.664 -23.803  1.00 75.89           H  
ATOM    646  HB3 GLU A  60     -10.417  15.729 -23.128  1.00 75.89           H  
ATOM    647  HG2 GLU A  60      -9.014  13.981 -22.448  1.00 76.55           H  
ATOM    648  HG3 GLU A  60      -9.955  12.958 -23.222  1.00 76.55           H  
ATOM    649  N   PRO A  61     -12.179  16.950 -21.065  1.00 48.58           N  
ANISOU  649  N   PRO A  61     4929   8398   5131    956    379    554       N  
ATOM    650  CA  PRO A  61     -13.149  18.030 -20.872  1.00 42.36           C  
ANISOU  650  CA  PRO A  61     4132   7583   4379    907    331    702       C  
ATOM    651  C   PRO A  61     -13.626  18.613 -22.191  1.00 43.86           C  
ANISOU  651  C   PRO A  61     4337   7905   4422    864    307    773       C  
ATOM    652  O   PRO A  61     -12.903  18.645 -23.189  1.00 43.99           O  
ANISOU  652  O   PRO A  61     4359   8057   4300    859    359    750       O  
ATOM    653  CB  PRO A  61     -12.370  19.067 -20.057  1.00 43.88           C  
ANISOU  653  CB  PRO A  61     4283   7732   4657    902    394    802       C  
ATOM    654  CG  PRO A  61     -10.951  18.816 -20.393  1.00 46.62           C  
ANISOU  654  CG  PRO A  61     4603   8162   4947    927    480    747       C  
ATOM    655  CD  PRO A  61     -10.836  17.332 -20.598  1.00 45.34           C  
ANISOU  655  CD  PRO A  61     4466   7997   4765    979    472    575       C  
ATOM    656  HA  PRO A  61     -13.911  17.717 -20.358  1.00 50.83           H  
ATOM    657  HB2 PRO A  61     -12.634  19.961 -20.324  1.00 52.65           H  
ATOM    658  HB3 PRO A  61     -12.529  18.928 -19.110  1.00 52.65           H  
ATOM    659  HG2 PRO A  61     -10.720  19.291 -21.207  1.00 55.94           H  
ATOM    660  HG3 PRO A  61     -10.386  19.103 -19.658  1.00 55.94           H  
ATOM    661  HD2 PRO A  61     -10.172  17.135 -21.277  1.00 54.41           H  
ATOM    662  HD3 PRO A  61     -10.631  16.890 -19.760  1.00 54.41           H  
ATOM    663  N   VAL A  62     -14.873  19.080 -22.179  1.00 48.00           N  
ANISOU  663  N   VAL A  62     4864   8396   4977    831    226    867       N  
ATOM    664  CA  VAL A  62     -15.463  19.747 -23.331  1.00 44.77           C  
ANISOU  664  CA  VAL A  62     4463   8096   4451    779    181    966       C  
ATOM    665  C   VAL A  62     -16.577  20.637 -22.812  1.00 41.73           C  
ANISOU  665  C   VAL A  62     4048   7631   4177    767    118   1107       C  
ATOM    666  O   VAL A  62     -17.230  20.320 -21.815  1.00 42.00           O  
ANISOU  666  O   VAL A  62     4068   7552   4340    793     90   1090       O  
ATOM    667  CB  VAL A  62     -15.977  18.723 -24.375  1.00 46.65           C  
ANISOU  667  CB  VAL A  62     4757   8414   4553    754    119    871       C  
ATOM    668  CG1 VAL A  62     -17.031  17.815 -23.764  1.00 44.70           C  
ANISOU  668  CG1 VAL A  62     4527   8062   4397    758     29    818       C  
ATOM    669  CG2 VAL A  62     -16.519  19.433 -25.610  1.00 44.83           C  
ANISOU  669  CG2 VAL A  62     4538   8307   4188    684     67    984       C  
ATOM    670  H   VAL A  62     -15.403  19.022 -21.504  1.00 57.60           H  
ATOM    671  HA  VAL A  62     -14.795  20.308 -23.755  1.00 53.72           H  
ATOM    672  HB  VAL A  62     -15.235  18.166 -24.657  1.00 55.98           H  
ATOM    673 HG11 VAL A  62     -17.335  17.186 -24.437  1.00 53.65           H  
ATOM    674 HG12 VAL A  62     -16.639  17.337 -23.016  1.00 53.65           H  
ATOM    675 HG13 VAL A  62     -17.775  18.357 -23.457  1.00 53.65           H  
ATOM    676 HG21 VAL A  62     -16.833  18.769 -26.243  1.00 53.79           H  
ATOM    677 HG22 VAL A  62     -17.252  20.011 -25.345  1.00 53.79           H  
ATOM    678 HG23 VAL A  62     -15.809  19.961 -26.007  1.00 53.79           H  
ATOM    679  N   VAL A  63     -16.771  21.773 -23.473  1.00 41.97           N  
ANISOU  679  N   VAL A  63     4065   7722   4159    730     99   1248       N  
ATOM    680  CA  VAL A  63     -17.881  22.673 -23.183  1.00 48.67           C  
ANISOU  680  CA  VAL A  63     4883   8504   5105    730     34   1388       C  
ATOM    681  C   VAL A  63     -18.920  22.520 -24.283  1.00 44.90           C  
ANISOU  681  C   VAL A  63     4410   8116   4536    678    -67   1442       C  
ATOM    682  O   VAL A  63     -18.652  22.835 -25.448  1.00 44.05           O  
ANISOU  682  O   VAL A  63     4323   8132   4284    621    -83   1489       O  
ATOM    683  CB  VAL A  63     -17.407  24.129 -23.073  1.00 48.32           C  
ANISOU  683  CB  VAL A  63     4827   8438   5096    725     65   1525       C  
ATOM    684  CG1 VAL A  63     -18.597  25.079 -22.968  1.00 44.24           C  
ANISOU  684  CG1 VAL A  63     4280   7857   4672    736     -9   1670       C  
ATOM    685  CG2 VAL A  63     -16.499  24.291 -21.874  1.00 45.66           C  
ANISOU  685  CG2 VAL A  63     4491   7996   4860    764    148   1484       C  
ATOM    686  H   VAL A  63     -16.261  22.051 -24.108  1.00 50.36           H  
ATOM    687  HA  VAL A  63     -18.288  22.420 -22.340  1.00 58.40           H  
ATOM    688  HB  VAL A  63     -16.903  24.362 -23.868  1.00 57.99           H  
ATOM    689 HG11 VAL A  63     -18.269  25.989 -22.900  1.00 53.09           H  
ATOM    690 HG12 VAL A  63     -19.147  24.983 -23.761  1.00 53.09           H  
ATOM    691 HG13 VAL A  63     -19.112  24.852 -22.178  1.00 53.09           H  
ATOM    692 HG21 VAL A  63     -16.210  25.215 -21.819  1.00 54.79           H  
ATOM    693 HG22 VAL A  63     -16.989  24.050 -21.072  1.00 54.79           H  
ATOM    694 HG23 VAL A  63     -15.730  23.709 -21.979  1.00 54.79           H  
ATOM    695  N   LEU A  64     -20.101  22.034 -23.916  1.00 47.39           N  
ANISOU  695  N   LEU A  64     4701   8376   4927    688   -140   1444       N  
ATOM    696  CA  LEU A  64     -21.217  21.916 -24.843  1.00 48.58           C  
ANISOU  696  CA  LEU A  64     4845   8600   5013    632   -254   1518       C  
ATOM    697  C   LEU A  64     -22.066  23.176 -24.760  1.00 46.45           C  
ANISOU  697  C   LEU A  64     4511   8294   4843    645   -301   1703       C  
ATOM    698  O   LEU A  64     -22.492  23.573 -23.671  1.00 49.45           O  
ANISOU  698  O   LEU A  64     4843   8562   5385    712   -278   1737       O  
ATOM    699  CB  LEU A  64     -22.055  20.682 -24.516  1.00 48.97           C  
ANISOU  699  CB  LEU A  64     4895   8618   5093    625   -320   1435       C  
ATOM    700  CG  LEU A  64     -21.264  19.374 -24.543  1.00 49.57           C  
ANISOU  700  CG  LEU A  64     5043   8702   5088    623   -286   1244       C  
ATOM    701  CD1 LEU A  64     -22.024  18.270 -23.846  1.00 51.81           C  
ANISOU  701  CD1 LEU A  64     5324   8911   5449    623   -349   1174       C  
ATOM    702  CD2 LEU A  64     -20.968  18.981 -25.973  1.00 52.15           C  
ANISOU  702  CD2 LEU A  64     5444   9161   5209    558   -316   1198       C  
ATOM    703  H   LEU A  64     -20.282  21.762 -23.120  1.00 56.86           H  
ATOM    704  HA  LEU A  64     -20.879  21.829 -25.748  1.00 58.29           H  
ATOM    705  HB2 LEU A  64     -22.428  20.784 -23.627  1.00 58.76           H  
ATOM    706  HB3 LEU A  64     -22.770  20.608 -25.167  1.00 58.76           H  
ATOM    707  HG  LEU A  64     -20.420  19.501 -24.081  1.00 59.48           H  
ATOM    708 HD11 LEU A  64     -21.499  17.456 -23.879  1.00 62.17           H  
ATOM    709 HD12 LEU A  64     -22.179  18.528 -22.923  1.00 62.17           H  
ATOM    710 HD13 LEU A  64     -22.871  18.136 -24.299  1.00 62.17           H  
ATOM    711 HD21 LEU A  64     -20.467  18.151 -25.975  1.00 62.58           H  
ATOM    712 HD22 LEU A  64     -21.806  18.863 -26.447  1.00 62.58           H  
ATOM    713 HD23 LEU A  64     -20.447  19.684 -26.392  1.00 62.58           H  
ATOM    714  N   THR A  65     -22.306  23.803 -25.909  1.00 48.20           N  
ANISOU  714  N   THR A  65     4736   8610   4967    582   -368   1822       N  
ATOM    715  CA  THR A  65     -22.946  25.110 -25.954  1.00 49.45           C  
ANISOU  715  CA  THR A  65     4839   8731   5217    597   -417   2007       C  
ATOM    716  C   THR A  65     -24.444  25.062 -26.224  1.00 50.61           C  
ANISOU  716  C   THR A  65     4921   8887   5420    583   -537   2116       C  
ATOM    717  O   THR A  65     -25.100  26.106 -26.123  1.00 55.00           O  
ANISOU  717  O   THR A  65     5417   9394   6087    619   -579   2269       O  
ATOM    718  CB  THR A  65     -22.291  25.979 -27.034  1.00 54.05           C  
ANISOU  718  CB  THR A  65     5455   9407   5673    527   -430   2105       C  
ATOM    719  OG1 THR A  65     -22.331  25.286 -28.290  1.00 54.52           O  
ANISOU  719  OG1 THR A  65     5559   9617   5540    428   -489   2077       O  
ATOM    720  CG2 THR A  65     -20.850  26.300 -26.668  1.00 51.99           C  
ANISOU  720  CG2 THR A  65     5234   9133   5388    545   -314   2042       C  
ATOM    721  H   THR A  65     -22.105  23.487 -26.684  1.00 57.84           H  
ATOM    722  HA  THR A  65     -22.813  25.550 -25.100  1.00 59.34           H  
ATOM    723  HB  THR A  65     -22.779  26.814 -27.113  1.00 64.86           H  
ATOM    724  HG1 THR A  65     -21.974  25.756 -28.888  1.00 65.43           H  
ATOM    725 HG21 THR A  65     -20.448  26.850 -27.359  1.00 62.39           H  
ATOM    726 HG22 THR A  65     -20.822  26.781 -25.826  1.00 62.39           H  
ATOM    727 HG23 THR A  65     -20.340  25.480 -26.581  1.00 62.39           H  
ATOM    728  N   ASP A  66     -25.005  23.905 -26.565  1.00 50.50           N  
ANISOU  728  N   ASP A  66     4918   8932   5338    532   -601   2050       N  
ATOM    729  CA  ASP A  66     -26.389  23.855 -27.027  1.00 53.01           C  
ANISOU  729  CA  ASP A  66     5173   9287   5682    490   -735   2177       C  
ATOM    730  C   ASP A  66     -27.073  22.562 -26.584  1.00 55.74           C  
ANISOU  730  C   ASP A  66     5506   9623   6050    478   -776   2087       C  
ATOM    731  O   ASP A  66     -27.759  21.896 -27.363  1.00 54.99           O  
ANISOU  731  O   ASP A  66     5424   9606   5864    386   -893   2112       O  
ATOM    732  CB  ASP A  66     -26.438  24.012 -28.546  1.00 54.72           C  
ANISOU  732  CB  ASP A  66     5435   9636   5722    372   -833   2261       C  
ATOM    733  CG  ASP A  66     -25.684  22.914 -29.266  1.00 56.59           C  
ANISOU  733  CG  ASP A  66     5785   9966   5750    294   -818   2098       C  
ATOM    734  OD1 ASP A  66     -24.966  22.145 -28.591  1.00 51.91           O  
ANISOU  734  OD1 ASP A  66     5234   9326   5162    343   -723   1925       O  
ATOM    735  OD2 ASP A  66     -25.802  22.825 -30.507  1.00 59.69           O  
ANISOU  735  OD2 ASP A  66     6229  10477   5973    185   -900   2143       O  
ATOM    736  H   ASP A  66     -24.610  23.142 -26.538  1.00 60.60           H  
ATOM    737  HA  ASP A  66     -26.876  24.597 -26.636  1.00 63.62           H  
ATOM    738  HB2 ASP A  66     -27.363  23.982 -28.838  1.00 65.67           H  
ATOM    739  HB3 ASP A  66     -26.039  24.861 -28.791  1.00 65.67           H  
ATOM    740  N   THR A  67     -26.915  22.197 -25.311  1.00 54.81           N  
ANISOU  740  N   THR A  67     5365   9407   6051    557   -692   1991       N  
ATOM    741  CA  THR A  67     -27.586  21.016 -24.786  1.00 52.83           C  
ANISOU  741  CA  THR A  67     5097   9142   5836    539   -739   1922       C  
ATOM    742  C   THR A  67     -29.011  21.297 -24.340  1.00 52.19           C  
ANISOU  742  C   THR A  67     4883   9048   5897    563   -807   2068       C  
ATOM    743  O   THR A  67     -29.825  20.367 -24.300  1.00 55.68           O  
ANISOU  743  O   THR A  67     5297   9519   6338    507   -895   2068       O  
ATOM    744  CB  THR A  67     -26.814  20.430 -23.596  1.00 52.16           C  
ANISOU  744  CB  THR A  67     5042   8966   5812    599   -629   1762       C  
ATOM    745  OG1 THR A  67     -26.703  21.413 -22.558  1.00 49.27           O  
ANISOU  745  OG1 THR A  67     4616   8510   5595    699   -532   1808       O  
ATOM    746  CG2 THR A  67     -25.427  19.974 -24.022  1.00 50.38           C  
ANISOU  746  CG2 THR A  67     4932   8759   5452    581   -565   1611       C  
ATOM    747  H   THR A  67     -26.429  22.616 -24.738  1.00 65.77           H  
ATOM    748  HA  THR A  67     -27.620  20.340 -25.481  1.00 63.40           H  
ATOM    749  HB  THR A  67     -27.293  19.659 -23.254  1.00 62.60           H  
ATOM    750  HG1 THR A  67     -26.294  22.088 -22.844  1.00 59.13           H  
ATOM    751 HG21 THR A  67     -24.951  19.607 -23.261  1.00 60.46           H  
ATOM    752 HG22 THR A  67     -25.499  19.293 -24.708  1.00 60.46           H  
ATOM    753 HG23 THR A  67     -24.926  20.726 -24.375  1.00 60.46           H  
ATOM    754  N   ASN A  68     -29.332  22.547 -24.008  1.00 54.15           N  
ANISOU  754  N   ASN A  68     5048   9255   6271    646   -770   2195       N  
ATOM    755  CA  ASN A  68     -30.622  22.880 -23.409  1.00 53.40           C  
ANISOU  755  CA  ASN A  68     4811   9143   6336    703   -803   2324       C  
ATOM    756  C   ASN A  68     -30.845  22.086 -22.129  1.00 51.34           C  
ANISOU  756  C   ASN A  68     4513   8832   6162    740   -745   2228       C  
ATOM    757  O   ASN A  68     -31.985  21.830 -21.733  1.00 56.30           O  
ANISOU  757  O   ASN A  68     5026   9486   6879    746   -794   2309       O  
ATOM    758  CB  ASN A  68     -31.774  22.637 -24.389  1.00 53.85           C  
ANISOU  758  CB  ASN A  68     4804   9303   6355    612   -965   2468       C  
ATOM    759  CG  ASN A  68     -31.721  23.557 -25.593  1.00 56.57           C  
ANISOU  759  CG  ASN A  68     5166   9697   6633    573  -1035   2599       C  
ATOM    760  OD1 ASN A  68     -31.647  24.778 -25.453  1.00 56.04           O  
ANISOU  760  OD1 ASN A  68     5058   9575   6659    658   -991   2689       O  
ATOM    761  ND2 ASN A  68     -31.756  22.973 -26.787  1.00 56.39           N  
ANISOU  761  ND2 ASN A  68     5212   9774   6441    437  -1150   2609       N  
ATOM    762  H   ASN A  68     -28.815  23.225 -24.121  1.00 64.98           H  
ATOM    763  HA  ASN A  68     -30.625  23.822 -23.178  1.00 64.08           H  
ATOM    764  HB2 ASN A  68     -31.730  21.722 -24.708  1.00 64.63           H  
ATOM    765  HB3 ASN A  68     -32.616  22.789 -23.932  1.00 64.63           H  
ATOM    766 HD21 ASN A  68     -31.729  23.451 -27.501  1.00 67.67           H  
ATOM    767 HD22 ASN A  68     -31.806  22.116 -26.846  1.00 67.67           H  
ATOM    768  N   LEU A  69     -29.752  21.692 -21.473  1.00 46.70           N  
ANISOU  768  N   LEU A  69     4015   8179   5549    759   -644   2064       N  
ATOM    769  CA  LEU A  69     -29.854  20.789 -20.332  1.00 51.58           C  
ANISOU  769  CA  LEU A  69     4617   8755   6225    768   -605   1966       C  
ATOM    770  C   LEU A  69     -30.665  21.414 -19.204  1.00 52.24           C  
ANISOU  770  C   LEU A  69     4577   8796   6476    865   -541   2042       C  
ATOM    771  O   LEU A  69     -31.577  20.782 -18.659  1.00 57.12           O  
ANISOU  771  O   LEU A  69     5108   9446   7151    847   -577   2070       O  
ATOM    772  CB  LEU A  69     -28.457  20.403 -19.843  1.00 47.47           C  
ANISOU  772  CB  LEU A  69     4211   8166   5659    776   -509   1793       C  
ATOM    773  CG  LEU A  69     -28.408  19.421 -18.668  1.00 48.50           C  
ANISOU  773  CG  LEU A  69     4341   8243   5842    771   -477   1686       C  
ATOM    774  CD1 LEU A  69     -29.135  18.128 -18.997  1.00 50.39           C  
ANISOU  774  CD1 LEU A  69     4574   8541   6031    671   -606   1674       C  
ATOM    775  CD2 LEU A  69     -26.971  19.127 -18.276  1.00 49.09           C  
ANISOU  775  CD2 LEU A  69     4523   8250   5879    781   -391   1534       C  
ATOM    776  H   LEU A  69     -28.949  21.931 -21.668  1.00 56.04           H  
ATOM    777  HA  LEU A  69     -30.307  19.979 -20.612  1.00 61.89           H  
ATOM    778  HB2 LEU A  69     -27.977  19.995 -20.581  1.00 56.96           H  
ATOM    779  HB3 LEU A  69     -27.997  21.210 -19.565  1.00 56.96           H  
ATOM    780  HG  LEU A  69     -28.849  19.824 -17.903  1.00 58.19           H  
ATOM    781 HD11 LEU A  69     -29.083  17.534 -18.233  1.00 60.47           H  
ATOM    782 HD12 LEU A  69     -30.063  18.330 -19.198  1.00 60.47           H  
ATOM    783 HD13 LEU A  69     -28.712  17.716 -19.767  1.00 60.47           H  
ATOM    784 HD21 LEU A  69     -26.969  18.504 -17.531  1.00 58.91           H  
ATOM    785 HD22 LEU A  69     -26.511  18.737 -19.035  1.00 58.91           H  
ATOM    786 HD23 LEU A  69     -26.539  19.955 -18.016  1.00 58.91           H  
ATOM    787  N   VAL A  70     -30.347  22.654 -18.837  1.00 49.32           N  
ANISOU  787  N   VAL A  70     4202   8356   6183    968   -447   2077       N  
ATOM    788  CA  VAL A  70     -31.065  23.342 -17.770  1.00 49.43           C  
ANISOU  788  CA  VAL A  70     4112   8320   6349   1079   -370   2135       C  
ATOM    789  C   VAL A  70     -31.764  24.561 -18.355  1.00 51.51           C  
ANISOU  789  C   VAL A  70     4297   8589   6685   1151   -402   2299       C  
ATOM    790  O   VAL A  70     -31.850  25.613 -17.712  1.00 53.47           O  
ANISOU  790  O   VAL A  70     4518   8754   7043   1271   -316   2331       O  
ATOM    791  CB  VAL A  70     -30.120  23.734 -16.619  1.00 48.96           C  
ANISOU  791  CB  VAL A  70     4126   8143   6331   1148   -228   2020       C  
ATOM    792  CG1 VAL A  70     -29.530  22.486 -15.976  1.00 49.48           C  
ANISOU  792  CG1 VAL A  70     4253   8203   6346   1077   -208   1875       C  
ATOM    793  CG2 VAL A  70     -29.015  24.655 -17.111  1.00 47.16           C  
ANISOU  793  CG2 VAL A  70     4005   7855   6060   1166   -193   2009       C  
ATOM    794  H   VAL A  70     -29.716  23.118 -19.192  1.00 59.19           H  
ATOM    795  HA  VAL A  70     -31.745  22.750 -17.412  1.00 59.32           H  
ATOM    796  HB  VAL A  70     -30.627  24.209 -15.942  1.00 58.75           H  
ATOM    797 HG11 VAL A  70     -28.939  22.752 -15.255  1.00 59.38           H  
ATOM    798 HG12 VAL A  70     -30.252  21.940 -15.628  1.00 59.38           H  
ATOM    799 HG13 VAL A  70     -29.034  21.991 -16.646  1.00 59.38           H  
ATOM    800 HG21 VAL A  70     -28.439  24.883 -16.365  1.00 56.60           H  
ATOM    801 HG22 VAL A  70     -28.504  24.197 -17.796  1.00 56.60           H  
ATOM    802 HG23 VAL A  70     -29.415  25.459 -17.478  1.00 56.60           H  
ATOM    803  N   TYR A  71     -32.274  24.419 -19.577  1.00 55.20           N  
ANISOU  803  N   TYR A  71     4733   9148   7090   1075   -534   2404       N  
ATOM    804  CA  TYR A  71     -32.920  25.532 -20.271  1.00 59.73           C  
ANISOU  804  CA  TYR A  71     5233   9732   7729   1126   -592   2577       C  
ATOM    805  C   TYR A  71     -33.981  26.235 -19.432  1.00 62.73           C  
ANISOU  805  C   TYR A  71     5464  10078   8291   1265   -540   2672       C  
ATOM    806  O   TYR A  71     -33.976  27.475 -19.390  1.00 63.73           O  
ANISOU  806  O   TYR A  71     5582  10124   8509   1373   -502   2741       O  
ATOM    807  CB  TYR A  71     -33.509  25.012 -21.590  1.00 65.38           C  
ANISOU  807  CB  TYR A  71     5922  10570   8348    999   -758   2682       C  
ATOM    808  CG  TYR A  71     -34.366  26.016 -22.325  1.00 68.42           C  
ANISOU  808  CG  TYR A  71     6207  10981   8811   1035   -846   2886       C  
ATOM    809  CD1 TYR A  71     -33.795  27.115 -22.952  1.00 70.66           C  
ANISOU  809  CD1 TYR A  71     6552  11215   9082   1057   -852   2945       C  
ATOM    810  CD2 TYR A  71     -35.744  25.859 -22.402  1.00 71.74           C  
ANISOU  810  CD2 TYR A  71     6463  11476   9320   1038   -932   3034       C  
ATOM    811  CE1 TYR A  71     -34.573  28.035 -23.628  1.00 72.87           C  
ANISOU  811  CE1 TYR A  71     6741  11507   9440   1087   -947   3141       C  
ATOM    812  CE2 TYR A  71     -36.529  26.773 -23.076  1.00 73.83           C  
ANISOU  812  CE2 TYR A  71     6624  11759   9667   1073  -1021   3232       C  
ATOM    813  CZ  TYR A  71     -35.938  27.857 -23.686  1.00 76.33           C  
ANISOU  813  CZ  TYR A  71     7013  12014   9975   1099  -1031   3282       C  
ATOM    814  OH  TYR A  71     -36.726  28.763 -24.356  1.00 87.07           O  
ANISOU  814  OH  TYR A  71     8303  13358  11422   1113  -1113   3451       O  
ATOM    815  H   TYR A  71     -32.258  23.686 -20.027  1.00 66.23           H  
ATOM    816  HA  TYR A  71     -32.243  26.190 -20.493  1.00 71.68           H  
ATOM    817  HB2 TYR A  71     -32.780  24.760 -22.178  1.00 78.45           H  
ATOM    818  HB3 TYR A  71     -34.060  24.236 -21.401  1.00 78.45           H  
ATOM    819  HD1 TYR A  71     -32.874  27.236 -22.913  1.00 84.80           H  
ATOM    820  HD2 TYR A  71     -36.145  25.128 -21.990  1.00 86.09           H  
ATOM    821  HE1 TYR A  71     -34.178  28.768 -24.042  1.00 87.45           H  
ATOM    822  HE2 TYR A  71     -37.451  26.658 -23.118  1.00 88.59           H  
ATOM    823  HH  TYR A  71     -37.532  28.531 -24.310  1.00104.49           H  
ATOM    824  N   PRO A  72     -34.897  25.539 -18.753  1.00 61.45           N  
ANISOU  824  N   PRO A  72     5184   9974   8190   1272   -534   2683       N  
ATOM    825  CA  PRO A  72     -35.886  26.255 -17.931  1.00 59.96           C  
ANISOU  825  CA  PRO A  72     4844   9765   8173   1421   -463   2768       C  
ATOM    826  C   PRO A  72     -35.275  26.999 -16.759  1.00 57.50           C  
ANISOU  826  C   PRO A  72     4596   9319   7932   1553   -295   2659       C  
ATOM    827  O   PRO A  72     -35.898  27.938 -16.250  1.00 58.55           O  
ANISOU  827  O   PRO A  72     4641   9403   8203   1703   -227   2723       O  
ATOM    828  CB  PRO A  72     -36.827  25.138 -17.451  1.00 60.65           C  
ANISOU  828  CB  PRO A  72     4806   9965   8274   1365   -492   2787       C  
ATOM    829  CG  PRO A  72     -36.529  23.957 -18.309  1.00 59.00           C  
ANISOU  829  CG  PRO A  72     4676   9831   7910   1181   -624   2754       C  
ATOM    830  CD  PRO A  72     -35.099  24.082 -18.700  1.00 58.52           C  
ANISOU  830  CD  PRO A  72     4809   9690   7735   1146   -595   2624       C  
ATOM    831  HA  PRO A  72     -36.387  26.879 -18.479  1.00 71.95           H  
ATOM    832  HB2 PRO A  72     -36.643  24.938 -16.520  1.00 72.78           H  
ATOM    833  HB3 PRO A  72     -37.748  25.419 -17.565  1.00 72.78           H  
ATOM    834  HG2 PRO A  72     -36.673  23.143 -17.801  1.00 70.80           H  
ATOM    835  HG3 PRO A  72     -37.099  23.975 -19.093  1.00 70.80           H  
ATOM    836  HD2 PRO A  72     -34.527  23.684 -18.025  1.00 70.22           H  
ATOM    837  HD3 PRO A  72     -34.951  23.687 -19.573  1.00 70.22           H  
ATOM    838  N   ALA A  73     -34.082  26.608 -16.307  1.00 56.18           N  
ANISOU  838  N   ALA A  73     4581   9090   7677   1503   -228   2496       N  
ATOM    839  CA  ALA A  73     -33.443  27.256 -15.169  1.00 52.34           C  
ANISOU  839  CA  ALA A  73     4171   8474   7242   1605    -79   2390       C  
ATOM    840  C   ALA A  73     -32.734  28.550 -15.540  1.00 54.62           C  
ANISOU  840  C   ALA A  73     4560   8643   7549   1670    -63   2414       C  
ATOM    841  O   ALA A  73     -32.293  29.274 -14.641  1.00 58.21           O  
ANISOU  841  O   ALA A  73     5085   8975   8058   1763     49   2346       O  
ATOM    842  CB  ALA A  73     -32.443  26.297 -14.519  1.00 50.35           C  
ANISOU  842  CB  ALA A  73     4033   8203   6894   1514    -28   2223       C  
ATOM    843  H   ALA A  73     -33.622  25.966 -16.648  1.00 67.42           H  
ATOM    844  HA  ALA A  73     -34.122  27.468 -14.510  1.00 62.81           H  
ATOM    845  HB1 ALA A  73     -32.026  26.741 -13.764  1.00 60.42           H  
ATOM    846  HB2 ALA A  73     -32.915  25.505 -14.219  1.00 60.42           H  
ATOM    847  HB3 ALA A  73     -31.769  26.053 -15.173  1.00 60.42           H  
ATOM    848  N   LEU A  74     -32.615  28.865 -16.830  1.00 49.59           N  
ANISOU  848  N   LEU A  74     3941   8038   6863   1614   -177   2512       N  
ATOM    849  CA  LEU A  74     -31.887  30.059 -17.236  1.00 53.57           C  
ANISOU  849  CA  LEU A  74     4546   8435   7374   1652   -179   2546       C  
ATOM    850  C   LEU A  74     -32.598  31.344 -16.840  1.00 56.09           C  
ANISOU  850  C   LEU A  74     4804   8650   7857   1821   -143   2637       C  
ATOM    851  O   LEU A  74     -31.987  32.415 -16.913  1.00 58.08           O  
ANISOU  851  O   LEU A  74     5154   8778   8134   1868   -132   2653       O  
ATOM    852  CB  LEU A  74     -31.648  30.030 -18.747  1.00 54.26           C  
ANISOU  852  CB  LEU A  74     4660   8603   7355   1535   -317   2640       C  
ATOM    853  CG  LEU A  74     -30.785  28.862 -19.239  1.00 55.28           C  
ANISOU  853  CG  LEU A  74     4875   8820   7309   1381   -345   2534       C  
ATOM    854  CD1 LEU A  74     -30.650  28.898 -20.749  1.00 56.50           C  
ANISOU  854  CD1 LEU A  74     5053   9065   7350   1271   -474   2630       C  
ATOM    855  CD2 LEU A  74     -29.407  28.867 -18.589  1.00 45.67           C  
ANISOU  855  CD2 LEU A  74     3797   7519   6037   1370   -241   2386       C  
ATOM    856  H   LEU A  74     -32.943  28.408 -17.480  1.00 59.51           H  
ATOM    857  HA  LEU A  74     -31.020  30.057 -16.801  1.00 64.29           H  
ATOM    858  HB2 LEU A  74     -32.506  29.970 -19.195  1.00 65.12           H  
ATOM    859  HB3 LEU A  74     -31.202  30.852 -19.005  1.00 65.12           H  
ATOM    860  HG  LEU A  74     -31.222  28.029 -19.000  1.00 66.34           H  
ATOM    861 HD11 LEU A  74     -30.101  28.151 -21.034  1.00 67.80           H  
ATOM    862 HD12 LEU A  74     -31.532  28.832 -21.146  1.00 67.80           H  
ATOM    863 HD13 LEU A  74     -30.232  29.734 -21.008  1.00 67.80           H  
ATOM    864 HD21 LEU A  74     -28.897  28.114 -18.927  1.00 54.81           H  
ATOM    865 HD22 LEU A  74     -28.957  29.697 -18.809  1.00 54.81           H  
ATOM    866 HD23 LEU A  74     -29.511  28.791 -17.628  1.00 54.81           H  
ATOM    867  N   LYS A  75     -33.857  31.267 -16.421  1.00 64.42           N  
ANISOU  867  N   LYS A  75     5699   9751   9026   1914   -125   2699       N  
ATOM    868  CA  LYS A  75     -34.574  32.426 -15.908  1.00 62.37           C  
ANISOU  868  CA  LYS A  75     5373   9390   8934   2102    -68   2765       C  
ATOM    869  C   LYS A  75     -34.406  32.596 -14.404  1.00 62.08           C  
ANISOU  869  C   LYS A  75     5382   9257   8948   2211    103   2622       C  
ATOM    870  O   LYS A  75     -34.948  33.549 -13.837  1.00 64.83           O  
ANISOU  870  O   LYS A  75     5693   9508   9430   2383    174   2645       O  
ATOM    871  CB  LYS A  75     -36.065  32.319 -16.257  1.00 61.07           C  
ANISOU  871  CB  LYS A  75     5032   9315   8856   2125   -125   2881       C  
ATOM    872  CG  LYS A  75     -36.746  31.053 -15.753  1.00 60.85           C  
ANISOU  872  CG  LYS A  75     4904   9423   8794   2056    -96   2832       C  
ATOM    873  CD  LYS A  75     -38.201  30.975 -16.209  1.00 58.11           C  
ANISOU  873  CD  LYS A  75     4408   9156   8514   2040   -164   2949       C  
ATOM    874  CE  LYS A  75     -38.712  29.539 -16.221  1.00 55.64           C  
ANISOU  874  CE  LYS A  75     4015   9004   8123   1901   -211   2947       C  
ATOM    875  NZ  LYS A  75     -38.629  28.893 -14.886  1.00 54.72           N  
ANISOU  875  NZ  LYS A  75     3891   8903   7996   1924    -80   2816       N  
ATOM    876  H   LYS A  75     -34.323  30.545 -16.425  1.00 77.30           H  
ATOM    877  HA  LYS A  75     -34.226  33.223 -16.337  1.00 74.84           H  
ATOM    878  HB2 LYS A  75     -36.529  33.077 -15.868  1.00 73.28           H  
ATOM    879  HB3 LYS A  75     -36.159  32.339 -17.222  1.00 73.28           H  
ATOM    880  HG2 LYS A  75     -36.277  30.278 -16.101  1.00 73.02           H  
ATOM    881  HG3 LYS A  75     -36.731  31.046 -14.783  1.00 73.02           H  
ATOM    882  HD2 LYS A  75     -38.754  31.489 -15.600  1.00 69.73           H  
ATOM    883  HD3 LYS A  75     -38.273  31.330 -17.109  1.00 69.73           H  
ATOM    884  HE2 LYS A  75     -39.641  29.536 -16.499  1.00 66.77           H  
ATOM    885  HE3 LYS A  75     -38.177  29.018 -16.840  1.00 66.77           H  
ATOM    886  HZ1 LYS A  75     -38.935  28.058 -14.933  1.00 65.66           H  
ATOM    887  HZ2 LYS A  75     -37.784  28.876 -14.609  1.00 65.66           H  
ATOM    888  HZ3 LYS A  75     -39.118  29.347 -14.298  1.00 65.66           H  
ATOM    889  N   TRP A  76     -33.659  31.714 -13.750  1.00 65.79           N  
ANISOU  889  N   TRP A  76     5937   9746   9313   2116    167   2475       N  
ATOM    890  CA  TRP A  76     -33.514  31.779 -12.304  1.00 67.30           C  
ANISOU  890  CA  TRP A  76     6173   9861   9535   2195    322   2343       C  
ATOM    891  C   TRP A  76     -32.728  33.013 -11.874  1.00 73.48           C  
ANISOU  891  C   TRP A  76     7120  10449  10352   2281    385   2290       C  
ATOM    892  O   TRP A  76     -31.805  33.469 -12.558  1.00 72.12           O  
ANISOU  892  O   TRP A  76     7070  10207  10126   2216    316   2309       O  
ATOM    893  CB  TRP A  76     -32.810  30.529 -11.784  1.00 63.80           C  
ANISOU  893  CB  TRP A  76     5793   9478   8970   2053    352   2211       C  
ATOM    894  CG  TRP A  76     -33.636  29.292 -11.859  1.00 63.35           C  
ANISOU  894  CG  TRP A  76     5590   9591   8890   1978    309   2241       C  
ATOM    895  CD1 TRP A  76     -34.913  29.181 -12.325  1.00 64.39           C  
ANISOU  895  CD1 TRP A  76     5537   9835   9092   2015    249   2376       C  
ATOM    896  CD2 TRP A  76     -33.243  27.979 -11.449  1.00 58.32           C  
ANISOU  896  CD2 TRP A  76     4979   9025   8156   1843    309   2143       C  
ATOM    897  NE1 TRP A  76     -35.339  27.878 -12.231  1.00 64.21           N  
ANISOU  897  NE1 TRP A  76     5430   9951   9014   1903    208   2369       N  
ATOM    898  CE2 TRP A  76     -34.331  27.120 -11.696  1.00 56.29           C  
ANISOU  898  CE2 TRP A  76     4557   8919   7910   1799    242   2224       C  
ATOM    899  CE3 TRP A  76     -32.074  27.447 -10.898  1.00 58.14           C  
ANISOU  899  CE3 TRP A  76     5099   8948   8044   1754    349   2003       C  
ATOM    900  CZ2 TRP A  76     -34.285  25.759 -11.411  1.00 56.71           C  
ANISOU  900  CZ2 TRP A  76     4599   9060   7886   1666    210   2165       C  
ATOM    901  CZ3 TRP A  76     -32.029  26.096 -10.616  1.00 55.77           C  
ANISOU  901  CZ3 TRP A  76     4780   8734   7676   1633    321   1943       C  
ATOM    902  CH2 TRP A  76     -33.127  25.266 -10.872  1.00 59.66           C  
ANISOU  902  CH2 TRP A  76     5121   9368   8180   1589    250   2022       C  
ATOM    903  H   TRP A  76     -33.227  31.069 -14.120  1.00 78.94           H  
ATOM    904  HA  TRP A  76     -34.393  31.823 -11.898  1.00 80.75           H  
ATOM    905  HB2 TRP A  76     -32.008  30.381 -12.309  1.00 76.56           H  
ATOM    906  HB3 TRP A  76     -32.572  30.669 -10.854  1.00 76.56           H  
ATOM    907  HD1 TRP A  76     -35.422  29.885 -12.657  1.00 77.27           H  
ATOM    908  HE1 TRP A  76     -36.112  27.586 -12.469  1.00 77.05           H  
ATOM    909  HE3 TRP A  76     -31.340  27.992 -10.725  1.00 69.77           H  
ATOM    910  HZ2 TRP A  76     -35.013  25.205 -11.581  1.00 68.05           H  
ATOM    911  HZ3 TRP A  76     -31.256  25.732 -10.249  1.00 66.92           H  
ATOM    912  HH2 TRP A  76     -33.068  24.360 -10.672  1.00 71.59           H  
ATOM    913  N   ASP A  77     -33.109  33.544 -10.717  1.00 74.69           N  
ANISOU  913  N   ASP A  77     7275  10516  10588   2423    516   2225       N  
ATOM    914  CA  ASP A  77     -32.346  34.570 -10.019  1.00 74.98           C  
ANISOU  914  CA  ASP A  77     7491  10356  10642   2495    592   2141       C  
ATOM    915  C   ASP A  77     -32.722  34.488  -8.544  1.00 73.99           C  
ANISOU  915  C   ASP A  77     7362  10205  10545   2588    755   2021       C  
ATOM    916  O   ASP A  77     -33.532  33.649  -8.139  1.00 75.79           O  
ANISOU  916  O   ASP A  77     7442  10577  10777   2589    803   2015       O  
ATOM    917  CB  ASP A  77     -32.598  35.962 -10.613  1.00 73.91           C  
ANISOU  917  CB  ASP A  77     7378  10087  10618   2623    536   2249       C  
ATOM    918  CG  ASP A  77     -34.075  36.323 -10.679  1.00 76.89           C  
ANISOU  918  CG  ASP A  77     7562  10508  11145   2796    550   2350       C  
ATOM    919  OD1 ASP A  77     -34.852  35.867  -9.813  1.00 75.32           O  
ANISOU  919  OD1 ASP A  77     7251  10387  10981   2870    663   2298       O  
ATOM    920  OD2 ASP A  77     -34.457  37.074 -11.602  1.00 77.71           O  
ANISOU  920  OD2 ASP A  77     7620  10573  11334   2854    446   2490       O  
ATOM    921  H   ASP A  77     -33.829  33.318 -10.304  1.00 89.63           H  
ATOM    922  HA  ASP A  77     -31.400  34.374 -10.101  1.00 89.98           H  
ATOM    923  HB2 ASP A  77     -32.152  36.625 -10.063  1.00 88.69           H  
ATOM    924  HB3 ASP A  77     -32.244  35.988 -11.516  1.00 88.69           H  
ATOM    925  N   LEU A  78     -32.117  35.360  -7.735  1.00 74.40           N  
ANISOU  925  N   LEU A  78     7444  10949   9877   2835    198  -1888       N  
ATOM    926  CA  LEU A  78     -32.392  35.341  -6.301  1.00 75.57           C  
ANISOU  926  CA  LEU A  78     7535  11433   9745   2721    307  -1981       C  
ATOM    927  C   LEU A  78     -33.875  35.548  -6.021  1.00 79.36           C  
ANISOU  927  C   LEU A  78     7754  12292  10107   2741    447  -2209       C  
ATOM    928  O   LEU A  78     -34.441  34.908  -5.127  1.00 79.12           O  
ANISOU  928  O   LEU A  78     7639  12581   9844   2546    580  -2194       O  
ATOM    929  CB  LEU A  78     -31.560  36.409  -5.594  1.00 79.66           C  
ANISOU  929  CB  LEU A  78     8156  11869  10240   2877    229  -2119       C  
ATOM    930  CG  LEU A  78     -30.049  36.201  -5.672  1.00 81.05           C  
ANISOU  930  CG  LEU A  78     8594  11700  10500   2842     99  -1901       C  
ATOM    931  CD1 LEU A  78     -29.309  37.430  -5.165  1.00 81.67           C  
ANISOU  931  CD1 LEU A  78     8753  11673  10605   3044     11  -2077       C  
ATOM    932  CD2 LEU A  78     -29.629  34.967  -4.885  1.00 81.01           C  
ANISOU  932  CD2 LEU A  78     8691  11793  10294   2543    156  -1654       C  
ATOM    933  H   LEU A  78     -31.555  35.960  -7.986  1.00 89.28           H  
ATOM    934  HA  LEU A  78     -32.138  34.477  -5.943  1.00 90.68           H  
ATOM    935  HB2 LEU A  78     -31.758  37.271  -5.994  1.00 95.59           H  
ATOM    936  HB3 LEU A  78     -31.806  36.422  -4.656  1.00 95.59           H  
ATOM    937  HG  LEU A  78     -29.798  36.063  -6.598  1.00 97.25           H  
ATOM    938 HD11 LEU A  78     -28.354  37.271  -5.226  1.00 98.00           H  
ATOM    939 HD12 LEU A  78     -29.553  38.193  -5.713  1.00 98.00           H  
ATOM    940 HD13 LEU A  78     -29.560  37.591  -4.242  1.00 98.00           H  
ATOM    941 HD21 LEU A  78     -28.667  34.862  -4.953  1.00 97.21           H  
ATOM    942 HD22 LEU A  78     -29.884  35.083  -3.956  1.00 97.21           H  
ATOM    943 HD23 LEU A  78     -30.074  34.190  -5.256  1.00 97.21           H  
ATOM    944  N   GLU A  79     -34.525  36.433  -6.778  1.00 87.65           N  
ANISOU  944  N   GLU A  79     8673  13315  11316   2975    421  -2421       N  
ATOM    945  CA  GLU A  79     -35.941  36.706  -6.551  1.00 92.04           C  
ANISOU  945  CA  GLU A  79     8976  14223  11772   3013    548  -2656       C  
ATOM    946  C   GLU A  79     -36.796  35.495  -6.910  1.00 87.71           C  
ANISOU  946  C   GLU A  79     8316  13834  11177   2802    655  -2518       C  
ATOM    947  O   GLU A  79     -37.570  34.998  -6.084  1.00 94.28           O  
ANISOU  947  O   GLU A  79     9021  15012  11790   2638    798  -2555       O  
ATOM    948  CB  GLU A  79     -36.370  37.934  -7.358  1.00 91.26           C  
ANISOU  948  CB  GLU A  79     8970  13865  11841   3089    436  -2710       C  
ATOM    949  CG  GLU A  79     -37.804  38.368  -7.101  1.00 95.14           C  
ANISOU  949  CG  GLU A  79     9285  14633  12231   3076    525  -2898       C  
ATOM    950  CD  GLU A  79     -38.173  39.635  -7.849  1.00 95.77           C  
ANISOU  950  CD  GLU A  79     9461  14473  12455   3149    418  -2938       C  
ATOM    951  OE1 GLU A  79     -37.382  40.068  -8.714  1.00 94.89           O  
ANISOU  951  OE1 GLU A  79     9546  13985  12521   3175    295  -2790       O  
ATOM    952  OE2 GLU A  79     -39.254  40.198  -7.569  1.00 98.21           O  
ANISOU  952  OE2 GLU A  79     9647  14980  12687   3163    464  -3105       O  
ATOM    953  H   GLU A  79     -34.173  36.883  -7.420  1.00105.18           H  
ATOM    954  HA  GLU A  79     -36.078  36.902  -5.611  1.00110.44           H  
ATOM    955  HB2 GLU A  79     -35.790  38.676  -7.128  1.00109.52           H  
ATOM    956  HB3 GLU A  79     -36.286  37.732  -8.303  1.00109.52           H  
ATOM    957  HG2 GLU A  79     -38.404  37.663  -7.391  1.00114.16           H  
ATOM    958  HG3 GLU A  79     -37.919  38.535  -6.153  1.00114.16           H  
ATOM    959  N   TYR A  80     -36.667  35.003  -8.145  1.00 74.51           N  
ANISOU  959  N   TYR A  80     6687  11911   9710   2803    590  -2358       N  
ATOM    960  CA  TYR A  80     -37.473  33.866  -8.577  1.00 69.20           C  
ANISOU  960  CA  TYR A  80     5906  11371   9018   2613    684  -2230       C  
ATOM    961  C   TYR A  80     -37.278  32.667  -7.657  1.00 70.33           C  
ANISOU  961  C   TYR A  80     6109  11675   8940   2299    779  -2018       C  
ATOM    962  O   TYR A  80     -38.249  32.000  -7.281  1.00 73.89           O  
ANISOU  962  O   TYR A  80     6404  12430   9242   2136    922  -2030       O  
ATOM    963  CB  TYR A  80     -37.123  33.499 -10.019  1.00 67.18           C  
ANISOU  963  CB  TYR A  80     5727  10776   9021   2658    579  -2061       C  
ATOM    964  CG  TYR A  80     -37.853  32.281 -10.537  1.00 70.45           C  
ANISOU  964  CG  TYR A  80     6044  11291   9434   2460    663  -1913       C  
ATOM    965  CD1 TYR A  80     -37.326  31.008 -10.369  1.00 69.38           C  
ANISOU  965  CD1 TYR A  80     6028  11101   9233   2191    684  -1619       C  
ATOM    966  CD2 TYR A  80     -39.068  32.405 -11.196  1.00 69.38           C  
ANISOU  966  CD2 TYR A  80     5694  11303   9366   2543    722  -2068       C  
ATOM    967  CE1 TYR A  80     -37.989  29.893 -10.840  1.00 69.22           C  
ANISOU  967  CE1 TYR A  80     5915  11167   9217   2009    761  -1485       C  
ATOM    968  CE2 TYR A  80     -39.738  31.296 -11.671  1.00 68.61           C  
ANISOU  968  CE2 TYR A  80     5501  11297   9272   2363    800  -1939       C  
ATOM    969  CZ  TYR A  80     -39.195  30.043 -11.491  1.00 70.46           C  
ANISOU  969  CZ  TYR A  80     5856  11471   9443   2095    820  -1647       C  
ATOM    970  OH  TYR A  80     -39.861  28.936 -11.964  1.00 71.27           O  
ANISOU  970  OH  TYR A  80     5862  11660   9556   1915    897  -1521       O  
ATOM    971  H   TYR A  80     -36.127  35.307  -8.741  1.00 89.41           H  
ATOM    972  HA  TYR A  80     -38.410  34.115  -8.550  1.00 83.05           H  
ATOM    973  HB2 TYR A  80     -37.348  34.246 -10.595  1.00 80.61           H  
ATOM    974  HB3 TYR A  80     -36.171  33.319 -10.073  1.00 80.61           H  
ATOM    975  HD1 TYR A  80     -36.513  30.904  -9.930  1.00 83.26           H  
ATOM    976  HD2 TYR A  80     -39.437  33.250 -11.319  1.00 83.26           H  
ATOM    977  HE1 TYR A  80     -37.624  29.046 -10.720  1.00 83.06           H  
ATOM    978  HE2 TYR A  80     -40.552  31.394 -12.111  1.00 82.33           H  
ATOM    979  HH  TYR A  80     -39.423  28.241 -11.789  1.00 85.52           H  
ATOM    980  N   LEU A  81     -36.031  32.376  -7.284  1.00 76.79           N  
ANISOU  980  N   LEU A  81     7150  12292   9734   2212    703  -1822       N  
ATOM    981  CA  LEU A  81     -35.761  31.222  -6.432  1.00 78.64           C  
ANISOU  981  CA  LEU A  81     7459  12657   9765   1916    784  -1603       C  
ATOM    982  C   LEU A  81     -36.374  31.404  -5.049  1.00 82.87           C  
ANISOU  982  C   LEU A  81     7878  13589  10020   1844    920  -1763       C  
ATOM    983  O   LEU A  81     -37.071  30.516  -4.547  1.00 85.47           O  
ANISOU  983  O   LEU A  81     8108  14190  10177   1626   1059  -1697       O  
ATOM    984  CB  LEU A  81     -34.253  30.990  -6.329  1.00 74.51           C  
ANISOU  984  CB  LEU A  81     7204  11824   9283   1865    661  -1379       C  
ATOM    985  CG  LEU A  81     -33.595  30.398  -7.577  1.00 73.45           C  
ANISOU  985  CG  LEU A  81     7202  11320   9385   1846    549  -1143       C  
ATOM    986  CD1 LEU A  81     -32.077  30.455  -7.469  1.00 71.26           C  
ANISOU  986  CD1 LEU A  81     7185  10727   9166   1850    414   -976       C  
ATOM    987  CD2 LEU A  81     -34.053  28.965  -7.806  1.00 72.53           C  
ANISOU  987  CD2 LEU A  81     7042  11294   9221   1580    639   -922       C  
ATOM    988  H   LEU A  81     -35.333  32.826  -7.508  1.00 92.15           H  
ATOM    989  HA  LEU A  81     -36.159  30.434  -6.834  1.00 94.37           H  
ATOM    990  HB2 LEU A  81     -33.823  31.840  -6.148  1.00 89.41           H  
ATOM    991  HB3 LEU A  81     -34.086  30.379  -5.594  1.00 89.41           H  
ATOM    992  HG  LEU A  81     -33.858  30.922  -8.350  1.00 88.14           H  
ATOM    993 HD11 LEU A  81     -31.689  30.074  -8.272  1.00 85.52           H  
ATOM    994 HD12 LEU A  81     -31.801  31.380  -7.374  1.00 85.52           H  
ATOM    995 HD13 LEU A  81     -31.797  29.945  -6.692  1.00 85.52           H  
ATOM    996 HD21 LEU A  81     -33.620  28.618  -8.602  1.00 87.03           H  
ATOM    997 HD22 LEU A  81     -33.808  28.428  -7.036  1.00 87.03           H  
ATOM    998 HD23 LEU A  81     -35.016  28.956  -7.923  1.00 87.03           H  
ATOM    999  N   GLN A  82     -36.117  32.548  -4.413  1.00 84.84           N  
ANISOU  999  N   GLN A  82     8138  13879  10219   2022    884  -1974       N  
ATOM   1000  CA  GLN A  82     -36.706  32.812  -3.105  1.00 91.28           C  
ANISOU 1000  CA  GLN A  82     8837  15075  10771   1974   1008  -2148       C  
ATOM   1001  C   GLN A  82     -38.218  32.629  -3.133  1.00 94.26           C  
ANISOU 1001  C   GLN A  82     8955  15788  11072   1935   1157  -2298       C  
ATOM   1002  O   GLN A  82     -38.805  32.096  -2.184  1.00 98.74           O  
ANISOU 1002  O   GLN A  82     9430  16685  11401   1754   1299  -2302       O  
ATOM   1003  CB  GLN A  82     -36.349  34.228  -2.652  1.00 90.28           C  
ANISOU 1003  CB  GLN A  82     8727  14923  10652   2222    937  -2397       C  
ATOM   1004  CG  GLN A  82     -36.778  34.551  -1.229  1.00 92.52           C  
ANISOU 1004  CG  GLN A  82     8917  15579  10659   2179   1050  -2571       C  
ATOM   1005  CD  GLN A  82     -36.286  35.910  -0.755  1.00 91.64           C  
ANISOU 1005  CD  GLN A  82     8842  15418  10559   2416    968  -2800       C  
ATOM   1006  OE1 GLN A  82     -35.860  36.061   0.390  1.00 90.75           O  
ANISOU 1006  OE1 GLN A  82     8788  15438  10253   2365    991  -2830       O  
ATOM   1007  NE2 GLN A  82     -36.353  36.908  -1.631  1.00 90.44           N  
ANISOU 1007  NE2 GLN A  82     8654  15077  10634   2678    874  -2967       N  
ATOM   1008  H   GLN A  82     -35.613  33.176  -4.713  1.00101.81           H  
ATOM   1009  HA  GLN A  82     -36.339  32.188  -2.460  1.00109.54           H  
ATOM   1010  HB2 GLN A  82     -35.386  34.338  -2.702  1.00108.34           H  
ATOM   1011  HB3 GLN A  82     -36.782  34.863  -3.243  1.00108.34           H  
ATOM   1012  HG2 GLN A  82     -37.747  34.552  -1.184  1.00111.03           H  
ATOM   1013  HG3 GLN A  82     -36.419  33.877  -0.630  1.00111.03           H  
ATOM   1014 HE21 GLN A  82     -36.664  36.767  -2.420  1.00108.53           H  
ATOM   1015 HE22 GLN A  82     -36.086  37.695  -1.408  1.00108.53           H  
ATOM   1016  N   GLU A  83     -38.865  33.054  -4.221  1.00 89.42           N  
ANISOU 1016  N   GLU A  83     8221  15097  10658   2102   1126  -2421       N  
ATOM   1017  CA  GLU A  83     -40.319  32.967  -4.299  1.00 88.66           C  
ANISOU 1017  CA  GLU A  83     7870  15313  10505   2088   1260  -2586       C  
ATOM   1018  C   GLU A  83     -40.788  31.522  -4.425  1.00 88.89           C  
ANISOU 1018  C   GLU A  83     7855  15453  10465   1806   1366  -2364       C  
ATOM   1019  O   GLU A  83     -41.803  31.141  -3.831  1.00 91.39           O  
ANISOU 1019  O   GLU A  83     7998  16119  10606   1679   1521  -2443       O  
ATOM   1020  CB  GLU A  83     -40.831  33.800  -5.478  1.00 84.58           C  
ANISOU 1020  CB  GLU A  83     7246  14662  10228   2348   1189  -2767       C  
ATOM   1021  CG  GLU A  83     -40.636  35.299  -5.312  0.50 81.42           C  
ANISOU 1021  CG  GLU A  83     6863  14188   9886   2618   1099  -3015       C  
ATOM   1022  CD  GLU A  83     -41.380  35.853  -4.116  0.50 82.31           C  
ANISOU 1022  CD  GLU A  83     6868  14631   9773   2596   1192  -3223       C  
ATOM   1023  OE1 GLU A  83     -42.488  35.356  -3.821  0.50 82.53           O  
ANISOU 1023  OE1 GLU A  83     6732  14956   9672   2461   1325  -3269       O  
ATOM   1024  OE2 GLU A  83     -40.851  36.781  -3.468  0.50 81.98           O  
ANISOU 1024  OE2 GLU A  83     6913  14545   9690   2707   1128  -3335       O  
ATOM   1025  H   GLU A  83     -38.489  33.391  -4.916  1.00107.31           H  
ATOM   1026  HA  GLU A  83     -40.701  33.335  -3.486  1.00106.40           H  
ATOM   1027  HB2 GLU A  83     -40.358  33.527  -6.280  1.00101.49           H  
ATOM   1028  HB3 GLU A  83     -41.781  33.636  -5.586  1.00101.49           H  
ATOM   1029  HG2 GLU A  83     -39.691  35.483  -5.190  0.50 97.71           H  
ATOM   1030  HG3 GLU A  83     -40.963  35.750  -6.106  0.50 97.71           H  
ATOM   1031  N   ASN A  84     -40.062  30.701  -5.187  1.00 84.30           N  
ANISOU 1031  N   ASN A  84     7427  14580  10023   1704   1288  -2088       N  
ATOM   1032  CA  ASN A  84     -40.533  29.374  -5.557  1.00 85.94           C  
ANISOU 1032  CA  ASN A  84     7585  14847  10221   1466   1372  -1885       C  
ATOM   1033  C   ASN A  84     -39.672  28.231  -5.036  0.80 81.41           C  
ANISOU 1033  C   ASN A  84     7193  14201   9537   1199   1382  -1572       C  
ATOM   1034  O   ASN A  84     -40.030  27.068  -5.252  0.80 68.34           O  
ANISOU 1034  O   ASN A  84     5502  12603   7860    981   1458  -1390       O  
ATOM   1035  CB  ASN A  84     -40.632  29.265  -7.085  0.80 89.18           C  
ANISOU 1035  CB  ASN A  84     7982  14993  10911   1568   1283  -1830       C  
ATOM   1036  CG  ASN A  84     -41.776  30.081  -7.654  0.80 96.37           C  
ANISOU 1036  CG  ASN A  84     8669  16036  11912   1778   1310  -2116       C  
ATOM   1037  OD1 ASN A  84     -42.928  29.648  -7.632  0.80 98.73           O  
ANISOU 1037  OD1 ASN A  84     8769  16604  12139   1687   1439  -2189       O  
ATOM   1038  ND2 ASN A  84     -41.465  31.264  -8.172  0.80 97.37           N  
ANISOU 1038  ND2 ASN A  84     8826  15971  12200   2060   1189  -2278       N  
ATOM   1039  H   ASN A  84     -39.286  30.896  -5.502  1.00101.16           H  
ATOM   1040  HA  ASN A  84     -41.425  29.254  -5.197  1.00103.13           H  
ATOM   1041  HB2 ASN A  84     -39.807  29.587  -7.480  0.80107.02           H  
ATOM   1042  HB3 ASN A  84     -40.775  28.336  -7.327  0.80107.02           H  
ATOM   1043 HD21 ASN A  84     -42.081  31.762  -8.507  0.80116.85           H  
ATOM   1044 HD22 ASN A  84     -40.648  31.532  -8.173  0.80116.85           H  
ATOM   1045  N   ILE A  85     -38.556  28.509  -4.359  1.00 94.18           N  
ANISOU 1045  N   ILE A  85     9001  15696  11085   1206   1307  -1503       N  
ATOM   1046  CA  ILE A  85     -37.719  27.415  -3.877  1.00 96.12           C  
ANISOU 1046  CA  ILE A  85     9426  15868  11228    955   1312  -1202       C  
ATOM   1047  C   ILE A  85     -38.312  26.747  -2.643  1.00 93.78           C  
ANISOU 1047  C   ILE A  85     9042  15951  10638    724   1485  -1181       C  
ATOM   1048  O   ILE A  85     -38.006  25.579  -2.375  1.00 96.22           O  
ANISOU 1048  O   ILE A  85     9438  16260  10861    473   1531   -922       O  
ATOM   1049  CB  ILE A  85     -36.287  27.900  -3.586  1.00 95.05           C  
ANISOU 1049  CB  ILE A  85     9530  15465  11122   1037   1170  -1127       C  
ATOM   1050  CG1 ILE A  85     -35.320  26.717  -3.486  1.00 92.39           C  
ANISOU 1050  CG1 ILE A  85     9396  14953  10757    800   1138   -783       C  
ATOM   1051  CG2 ILE A  85     -36.233  28.737  -2.307  1.00 98.68           C  
ANISOU 1051  CG2 ILE A  85     9974  16147  11373   1108   1208  -1323       C  
ATOM   1052  CD1 ILE A  85     -35.053  26.022  -4.805  1.00 88.51           C  
ANISOU 1052  CD1 ILE A  85     8967  14158  10502    763   1058   -579       C  
ATOM   1053  H   ILE A  85     -38.270  29.298  -4.172  1.00113.01           H  
ATOM   1054  HA  ILE A  85     -37.662  26.742  -4.573  1.00115.35           H  
ATOM   1055  HB  ILE A  85     -36.003  28.460  -4.325  1.00114.06           H  
ATOM   1056 HG12 ILE A  85     -34.471  27.037  -3.143  1.00110.87           H  
ATOM   1057 HG13 ILE A  85     -35.693  26.061  -2.876  1.00110.87           H  
ATOM   1058 HG21 ILE A  85     -35.319  29.025  -2.157  1.00118.42           H  
ATOM   1059 HG22 ILE A  85     -36.810  29.510  -2.412  1.00118.42           H  
ATOM   1060 HG23 ILE A  85     -36.536  28.195  -1.562  1.00118.42           H  
ATOM   1061 HD11 ILE A  85     -34.435  25.289  -4.656  1.00106.21           H  
ATOM   1062 HD12 ILE A  85     -35.890  25.683  -5.158  1.00106.21           H  
ATOM   1063 HD13 ILE A  85     -34.666  26.660  -5.425  1.00106.21           H  
ATOM   1064  N   GLY A  86     -39.148  27.452  -1.886  1.00 86.73           N  
ANISOU 1064  N   GLY A  86     7982  15382   9592    802   1583  -1445       N  
ATOM   1065  CA  GLY A  86     -39.813  26.867  -0.740  1.00 86.74           C  
ANISOU 1065  CA  GLY A  86     7880  15762   9313    594   1757  -1445       C  
ATOM   1066  C   GLY A  86     -39.049  27.064   0.552  1.00 90.09           C  
ANISOU 1066  C   GLY A  86     8436  16273   9521    544   1759  -1424       C  
ATOM   1067  O   GLY A  86     -37.964  27.650   0.606  1.00 86.00           O  
ANISOU 1067  O   GLY A  86     8093  15518   9065    667   1624  -1409       O  
ATOM   1068  H   GLY A  86     -39.345  28.278  -2.021  1.00104.08           H  
ATOM   1069  HA2 GLY A  86     -40.691  27.266  -0.640  1.00104.08           H  
ATOM   1070  HA3 GLY A  86     -39.925  25.914  -0.886  1.00104.08           H  
ATOM   1071  N   ASN A  87     -39.646  26.555   1.628  0.80 98.19           N  
ANISOU 1071  N   ASN A  87     9372  17653  10284    359   1919  -1425       N  
ATOM   1072  CA  ASN A  87     -39.062  26.645   2.962  0.80100.72           C  
ANISOU 1072  CA  ASN A  87     9795  18114  10362    288   1946  -1407       C  
ATOM   1073  C   ASN A  87     -38.274  25.370   3.237  0.80 98.70           C  
ANISOU 1073  C   ASN A  87     9720  17752  10028     24   1951  -1057       C  
ATOM   1074  O   ASN A  87     -38.857  24.297   3.423  0.80101.96           O  
ANISOU 1074  O   ASN A  87    10064  18340  10335   -210   2081   -913       O  
ATOM   1075  CB  ASN A  87     -40.148  26.857   4.013  0.80101.56           C  
ANISOU 1075  CB  ASN A  87     9700  18672  10216    245   2118  -1612       C  
ATOM   1076  H   ASN A  87     -40.402  26.146   1.609  0.80117.83           H  
ATOM   1077  HA  ASN A  87     -38.451  27.397   2.996  0.80120.87           H  
ATOM   1078  N   GLY A  88     -36.951  25.488   3.261  1.00 94.67           N  
ANISOU 1078  N   GLY A  88     9441  16955   9573     61   1809   -922       N  
ATOM   1079  CA  GLY A  88     -36.092  24.349   3.523  1.00 90.25           C  
ANISOU 1079  CA  GLY A  88     9072  16271   8949   -172   1796   -593       C  
ATOM   1080  C   GLY A  88     -34.716  24.824   3.928  1.00 86.32           C  
ANISOU 1080  C   GLY A  88     8801  15551   8447    -89   1655   -539       C  
ATOM   1081  O   GLY A  88     -34.370  25.997   3.781  1.00 81.19           O  
ANISOU 1081  O   GLY A  88     8172  14783   7895    157   1551   -736       O  
ATOM   1082  H   GLY A  88     -36.527  26.225   3.127  1.00113.60           H  
ATOM   1083  HA2 GLY A  88     -36.464  23.812   4.240  1.00108.30           H  
ATOM   1084  HA3 GLY A  88     -36.015  23.802   2.726  1.00108.30           H  
ATOM   1085  N   ASP A  89     -33.929  23.886   4.447  1.00 95.63           N  
ANISOU 1085  N   ASP A  89    10151  16672   9512   -297   1654   -267       N  
ATOM   1086  CA  ASP A  89     -32.586  24.187   4.922  1.00 97.75           C  
ANISOU 1086  CA  ASP A  89    10645  16743   9754   -251   1529   -189       C  
ATOM   1087  C   ASP A  89     -31.595  24.102   3.768  1.00 91.11           C  
ANISOU 1087  C   ASP A  89     9976  15449   9193   -181   1354    -29       C  
ATOM   1088  O   ASP A  89     -31.549  23.096   3.052  1.00 91.42           O  
ANISOU 1088  O   ASP A  89    10055  15342   9339   -331   1352    201       O  
ATOM   1089  CB  ASP A  89     -32.181  23.225   6.040  1.00 98.90           C  
ANISOU 1089  CB  ASP A  89    10898  17039   9640   -503   1606     29       C  
ATOM   1090  CG  ASP A  89     -32.907  23.506   7.343  1.00103.39           C  
ANISOU 1090  CG  ASP A  89    11334  18036   9913   -539   1754   -145       C  
ATOM   1091  OD1 ASP A  89     -33.028  24.693   7.716  1.00104.76           O  
ANISOU 1091  OD1 ASP A  89    11442  18306  10055   -331   1731   -419       O  
ATOM   1092  OD2 ASP A  89     -33.357  22.540   7.993  1.00105.90           O  
ANISOU 1092  OD2 ASP A  89    11612  18594  10031   -775   1896     -6       O  
ATOM   1093  H   ASP A  89     -34.154  23.061   4.535  1.00114.76           H  
ATOM   1094  HA  ASP A  89     -32.566  25.090   5.275  1.00117.30           H  
ATOM   1095  HB2 ASP A  89     -32.392  22.318   5.769  1.00118.68           H  
ATOM   1096  HB3 ASP A  89     -31.229  23.311   6.202  1.00118.68           H  
ATOM   1097  N   PHE A  90     -30.811  25.164   3.590  1.00 83.79           N  
ANISOU 1097  N   PHE A  90     9146  14303   8386     48   1210   -155       N  
ATOM   1098  CA  PHE A  90     -29.768  25.228   2.576  1.00 78.64           C  
ANISOU 1098  CA  PHE A  90     8668  13215   7994    137   1036    -23       C  
ATOM   1099  C   PHE A  90     -28.417  25.384   3.258  1.00 78.24           C  
ANISOU 1099  C   PHE A  90     8844  13008   7876    140    931     72       C  
ATOM   1100  O   PHE A  90     -28.249  26.253   4.121  1.00 79.06           O  
ANISOU 1100  O   PHE A  90     8946  13242   7853    257    927   -116       O  
ATOM   1101  CB  PHE A  90     -30.006  26.393   1.608  1.00 78.98           C  
ANISOU 1101  CB  PHE A  90     8631  13100   8279    424    947   -256       C  
ATOM   1102  CG  PHE A  90     -31.190  26.198   0.709  1.00 83.20           C  
ANISOU 1102  CG  PHE A  90     8968  13715   8929    434   1020   -322       C  
ATOM   1103  CD1 PHE A  90     -31.058  25.524  -0.493  1.00 81.43           C  
ANISOU 1103  CD1 PHE A  90     8787  13231   8921    384    962   -136       C  
ATOM   1104  CD2 PHE A  90     -32.436  26.689   1.064  1.00 85.26           C  
ANISOU 1104  CD2 PHE A  90     8998  14313   9084    494   1145   -573       C  
ATOM   1105  CE1 PHE A  90     -32.144  25.342  -1.321  1.00 83.07           C  
ANISOU 1105  CE1 PHE A  90     8811  13516   9236    397   1027   -200       C  
ATOM   1106  CE2 PHE A  90     -33.526  26.509   0.237  1.00 84.80           C  
ANISOU 1106  CE2 PHE A  90     8756  14330   9133    506   1211   -638       C  
ATOM   1107  CZ  PHE A  90     -33.380  25.834  -0.955  1.00 84.25           C  
ANISOU 1107  CZ  PHE A  90     8731  14001   9278    457   1152   -452       C  
ATOM   1108  H   PHE A  90     -30.870  25.881   4.062  1.00100.55           H  
ATOM   1109  HA  PHE A  90     -29.761  24.403   2.067  1.00 94.36           H  
ATOM   1110  HB2 PHE A  90     -30.154  27.202   2.122  1.00 94.78           H  
ATOM   1111  HB3 PHE A  90     -29.222  26.498   1.047  1.00 94.78           H  
ATOM   1112  HD1 PHE A  90     -30.227  25.189  -0.743  1.00 97.71           H  
ATOM   1113  HD2 PHE A  90     -32.539  27.144   1.869  1.00102.31           H  
ATOM   1114  HE1 PHE A  90     -32.044  24.887  -2.126  1.00 99.68           H  
ATOM   1115  HE2 PHE A  90     -34.358  26.842   0.485  1.00101.76           H  
ATOM   1116  HZ  PHE A  90     -34.113  25.713  -1.514  1.00101.10           H  
ATOM   1117  N   SER A  91     -27.458  24.546   2.870  1.00 80.06           N  
ANISOU 1117  N   SER A  91     9266  12961   8191     13    846    358       N  
ATOM   1118  CA  SER A  91     -26.113  24.624   3.426  1.00 80.98           C  
ANISOU 1118  CA  SER A  91     9608  12897   8262     10    736    468       C  
ATOM   1119  C   SER A  91     -25.383  25.823   2.831  1.00 77.44           C  
ANISOU 1119  C   SER A  91     9238  12154   8033    285    573    317       C  
ATOM   1120  O   SER A  91     -25.241  25.928   1.608  1.00 73.91           O  
ANISOU 1120  O   SER A  91     8810  11426   7848    382    483    351       O  
ATOM   1121  CB  SER A  91     -25.348  23.333   3.142  1.00 79.42           C  
ANISOU 1121  CB  SER A  91     9585  12492   8099   -212    696    821       C  
ATOM   1122  OG  SER A  91     -26.121  22.194   3.477  1.00 81.12           O  
ANISOU 1122  OG  SER A  91     9712  12953   8156   -461    848    965       O  
ATOM   1123  H   SER A  91     -27.563  23.924   2.285  1.00 96.07           H  
ATOM   1124  HA  SER A  91     -26.167  24.743   4.387  1.00 97.17           H  
ATOM   1125  HB2 SER A  91     -25.130  23.299   2.198  1.00 95.30           H  
ATOM   1126  HB3 SER A  91     -24.534  23.327   3.670  1.00 95.30           H  
ATOM   1127  HG  SER A  91     -26.830  22.185   3.027  1.00 97.34           H  
ATOM   1128  N   VAL A  92     -24.923  26.728   3.693  1.00 74.82           N  
ANISOU 1128  N   VAL A  92     8948  11884   7595    412    537    149       N  
ATOM   1129  CA  VAL A  92     -24.237  27.946   3.278  1.00 72.43           C  
ANISOU 1129  CA  VAL A  92     8714  11327   7480    678    391    -16       C  
ATOM   1130  C   VAL A  92     -22.859  27.959   3.922  1.00 73.28           C  
ANISOU 1130  C   VAL A  92     9047  11268   7529    657    286     96       C  
ATOM   1131  O   VAL A  92     -22.733  27.753   5.135  1.00 75.70           O  
ANISOU 1131  O   VAL A  92     9380  11802   7579    550    349    105       O  
ATOM   1132  CB  VAL A  92     -25.035  29.204   3.666  1.00 76.89           C  
ANISOU 1132  CB  VAL A  92     9097  12123   7995    888    440   -371       C  
ATOM   1133  CG1 VAL A  92     -24.362  30.455   3.123  1.00 75.20           C  
ANISOU 1133  CG1 VAL A  92     8947  11624   8002   1167    289   -538       C  
ATOM   1134  CG2 VAL A  92     -26.468  29.105   3.154  1.00 78.48           C  
ANISOU 1134  CG2 VAL A  92     9065  12533   8221    886    560   -480       C  
ATOM   1135  H   VAL A  92     -24.999  26.654   4.547  1.00 89.78           H  
ATOM   1136  HA  VAL A  92     -24.125  27.940   2.315  1.00 86.92           H  
ATOM   1137  HB  VAL A  92     -25.066  29.275   4.633  1.00 92.27           H  
ATOM   1138 HG11 VAL A  92     -24.883  31.231   3.380  1.00 90.24           H  
ATOM   1139 HG12 VAL A  92     -23.468  30.518   3.494  1.00 90.24           H  
ATOM   1140 HG13 VAL A  92     -24.315  30.393   2.156  1.00 90.24           H  
ATOM   1141 HG21 VAL A  92     -26.950  29.907   3.410  1.00 94.18           H  
ATOM   1142 HG22 VAL A  92     -26.452  29.022   2.188  1.00 94.18           H  
ATOM   1143 HG23 VAL A  92     -26.890  28.326   3.548  1.00 94.18           H  
ATOM   1144  N   TYR A  93     -21.832  28.204   3.114  1.00 70.53           N  
ANISOU 1144  N   TYR A  93     8858  10524   7416    761    127    178       N  
ATOM   1145  CA  TYR A  93     -20.450  28.208   3.573  1.00 71.16           C  
ANISOU 1145  CA  TYR A  93     9161  10398   7477    750     11    294       C  
ATOM   1146  C   TYR A  93     -19.917  29.633   3.564  1.00 70.42           C  
ANISOU 1146  C   TYR A  93     9097  10159   7503   1026    -99     51       C  
ATOM   1147  O   TYR A  93     -20.076  30.355   2.573  1.00 66.68           O  
ANISOU 1147  O   TYR A  93     8571   9497   7266   1217   -163    -70       O  
ATOM   1148  CB  TYR A  93     -19.580  27.309   2.690  1.00 66.98           C  
ANISOU 1148  CB  TYR A  93     8810   9515   7124    639    -89    596       C  
ATOM   1149  CG  TYR A  93     -19.989  25.851   2.712  1.00 64.51           C  
ANISOU 1149  CG  TYR A  93     8487   9321   6702    357     11    855       C  
ATOM   1150  CD1 TYR A  93     -21.043  25.393   1.930  1.00 65.89           C  
ANISOU 1150  CD1 TYR A  93     8507   9572   6955    304     94    873       C  
ATOM   1151  CD2 TYR A  93     -19.322  24.933   3.512  1.00 64.63           C  
ANISOU 1151  CD2 TYR A  93     8647   9371   6538    146     22   1079       C  
ATOM   1152  CE1 TYR A  93     -21.422  24.062   1.947  1.00 66.52           C  
ANISOU 1152  CE1 TYR A  93     8574   9757   6943     46    187   1106       C  
ATOM   1153  CE2 TYR A  93     -19.692  23.601   3.535  1.00 66.39           C  
ANISOU 1153  CE2 TYR A  93     8861   9697   6666   -112    114   1317       C  
ATOM   1154  CZ  TYR A  93     -20.742  23.170   2.751  1.00 67.93           C  
ANISOU 1154  CZ  TYR A  93     8899   9964   6947   -162    198   1329       C  
ATOM   1155  OH  TYR A  93     -21.115  21.845   2.771  1.00 67.21           O  
ANISOU 1155  OH  TYR A  93     8796   9973   6769   -420    292   1564       O  
ATOM   1156  H   TYR A  93     -21.914  28.374   2.275  1.00 84.64           H  
ATOM   1157  HA  TYR A  93     -20.411  27.872   4.482  1.00 85.39           H  
ATOM   1158  HB2 TYR A  93     -19.639  27.620   1.773  1.00 80.37           H  
ATOM   1159  HB3 TYR A  93     -18.661  27.363   2.997  1.00 80.37           H  
ATOM   1160  HD1 TYR A  93     -21.503  25.992   1.387  1.00 79.06           H  
ATOM   1161  HD2 TYR A  93     -18.613  25.220   4.042  1.00 77.56           H  
ATOM   1162  HE1 TYR A  93     -22.129  23.771   1.418  1.00 79.82           H  
ATOM   1163  HE2 TYR A  93     -19.236  22.998   4.077  1.00 79.66           H  
ATOM   1164  HH  TYR A  93     -20.621  21.416   3.299  1.00 80.65           H  
ATOM   1165  N   SER A  94     -19.292  30.034   4.666  1.00 73.44           N  
ANISOU 1165  N   SER A  94     9559  10626   7720   1046   -121    -20       N  
ATOM   1166  CA  SER A  94     -18.732  31.368   4.803  1.00 72.34           C  
ANISOU 1166  CA  SER A  94     9452  10363   7672   1296   -223   -251       C  
ATOM   1167  C   SER A  94     -17.218  31.324   4.640  1.00 71.57           C  
ANISOU 1167  C   SER A  94     9597   9903   7695   1311   -381    -95       C  
ATOM   1168  O   SER A  94     -16.569  30.298   4.860  1.00 68.47           O  
ANISOU 1168  O   SER A  94     9350   9440   7225   1113   -397    167       O  
ATOM   1169  CB  SER A  94     -19.094  31.973   6.162  1.00 74.79           C  
ANISOU 1169  CB  SER A  94     9671  11026   7721   1334   -141   -474       C  
ATOM   1170  H   SER A  94     -19.179  29.539   5.360  1.00 88.13           H  
ATOM   1171  HA  SER A  94     -19.095  31.940   4.109  1.00 86.81           H  
ATOM   1172  N   ALA A  95     -16.660  32.465   4.244  1.00 72.68           N  
ANISOU 1172  N   ALA A  95     9778   9809   8028   1551   -499   -263       N  
ATOM   1173  CA  ALA A  95     -15.223  32.593   4.064  1.00 69.44           C  
ANISOU 1173  CA  ALA A  95     9588   9045   7752   1597   -654   -152       C  
ATOM   1174  C   ALA A  95     -14.844  34.058   4.216  1.00 68.26           C  
ANISOU 1174  C   ALA A  95     9432   8804   7702   1865   -737   -430       C  
ATOM   1175  O   ALA A  95     -15.523  34.938   3.681  1.00 68.73           O  
ANISOU 1175  O   ALA A  95     9351   8872   7892   2053   -726   -644       O  
ATOM   1176  CB  ALA A  95     -14.781  32.066   2.694  1.00 67.71           C  
ANISOU 1176  CB  ALA A  95     9469   8458   7800   1575   -744     63       C  
ATOM   1177  H   ALA A  95     -17.099  33.184   4.071  1.00 87.22           H  
ATOM   1178  HA  ALA A  95     -14.765  32.084   4.751  1.00 83.33           H  
ATOM   1179  HB1 ALA A  95     -13.820  32.168   2.612  1.00 81.25           H  
ATOM   1180  HB2 ALA A  95     -15.022  31.129   2.624  1.00 81.25           H  
ATOM   1181  HB3 ALA A  95     -15.229  32.576   2.001  1.00 81.25           H  
ATOM   1182  N   SER A  96     -13.763  34.308   4.956  1.00 95.41           N  
ANISOU 1182  N   SER A  96    11441  14409  10400   -231  -1425    430       N  
ATOM   1183  CA  SER A  96     -13.280  35.668   5.161  1.00 97.36           C  
ANISOU 1183  CA  SER A  96    11911  14452  10631   -186  -1765    347       C  
ATOM   1184  C   SER A  96     -12.615  36.263   3.926  1.00 95.06           C  
ANISOU 1184  C   SER A  96    11371  14035  10714   -249  -1895    403       C  
ATOM   1185  O   SER A  96     -12.391  37.478   3.896  1.00 97.76           O  
ANISOU 1185  O   SER A  96    11859  14230  11055   -191  -2127    310       O  
ATOM   1186  CB  SER A  96     -12.297  35.697   6.331  1.00 99.26           C  
ANISOU 1186  CB  SER A  96    12436  14503  10773   -262  -2121    435       C  
ATOM   1187  OG  SER A  96     -11.300  34.700   6.186  1.00 99.92           O  
ANISOU 1187  OG  SER A  96    12334  14526  11105   -446  -2200    663       O  
ATOM   1188  H   SER A  96     -13.293  33.705   5.349  1.00114.49           H  
ATOM   1189  HA  SER A  96     -14.033  36.234   5.392  1.00116.84           H  
ATOM   1190  HB2 SER A  96     -11.869  36.567   6.362  1.00119.11           H  
ATOM   1191  HB3 SER A  96     -12.783  35.538   7.155  1.00119.11           H  
ATOM   1192  HG  SER A  96     -10.768  34.728   6.836  1.00119.90           H  
ATOM   1193  N   THR A  97     -12.290  35.454   2.921  1.00 91.37           N  
ANISOU 1193  N   THR A  97    10538  13617  10562   -365  -1754    551       N  
ATOM   1194  CA  THR A  97     -11.647  35.938   1.705  1.00 89.61           C  
ANISOU 1194  CA  THR A  97    10061  13280  10706   -430  -1859    617       C  
ATOM   1195  C   THR A  97     -12.275  35.222   0.515  1.00 86.84           C  
ANISOU 1195  C   THR A  97     9333  13123  10538   -434  -1489    640       C  
ATOM   1196  O   THR A  97     -13.244  34.469   0.655  1.00 87.64           O  
ANISOU 1196  O   THR A  97     9389  13440  10469   -375  -1164    588       O  
ATOM   1197  CB  THR A  97     -10.131  35.712   1.761  1.00 89.73           C  
ANISOU 1197  CB  THR A  97    10029  13076  10988   -613  -2190    828       C  
ATOM   1198  OG1 THR A  97      -9.863  34.307   1.860  1.00 89.78           O  
ANISOU 1198  OG1 THR A  97     9873  13168  11073   -736  -2057    998       O  
ATOM   1199  CG2 THR A  97      -9.524  36.432   2.957  1.00 93.12           C  
ANISOU 1199  CG2 THR A  97    10839  13311  11233   -604  -2563    799       C  
ATOM   1200  H   THR A  97     -12.435  34.606   2.921  1.00109.65           H  
ATOM   1201  HA  THR A  97     -11.812  36.889   1.611  1.00107.53           H  
ATOM   1202  HB  THR A  97      -9.723  36.062   0.953  1.00107.68           H  
ATOM   1203  HG1 THR A  97      -9.035  34.174   1.891  1.00107.74           H  
ATOM   1204 HG21 THR A  97      -8.566  36.283   2.983  1.00111.75           H  
ATOM   1205 HG22 THR A  97      -9.693  37.385   2.891  1.00111.75           H  
ATOM   1206 HG23 THR A  97      -9.917  36.099   3.779  1.00111.75           H  
ATOM   1207  N   HIS A  98     -11.714  35.460  -0.672  1.00 83.61           N  
ANISOU 1207  N   HIS A  98     8653  12634  10482   -504  -1539    719       N  
ATOM   1208  CA  HIS A  98     -12.189  34.771  -1.866  1.00 80.66           C  
ANISOU 1208  CA  HIS A  98     7907  12426  10315   -519  -1212    758       C  
ATOM   1209  C   HIS A  98     -11.823  33.293  -1.841  1.00 81.41           C  
ANISOU 1209  C   HIS A  98     7808  12600  10526   -660  -1084    949       C  
ATOM   1210  O   HIS A  98     -12.582  32.458  -2.347  1.00 82.38           O  
ANISOU 1210  O   HIS A  98     7712  12927  10661   -641   -740    947       O  
ATOM   1211  CB  HIS A  98     -11.615  35.436  -3.117  1.00 77.12           C  
ANISOU 1211  CB  HIS A  98     7231  11856  10214   -559  -1318    800       C  
ATOM   1212  CG  HIS A  98     -10.120  35.518  -3.127  1.00 78.73           C  
ANISOU 1212  CG  HIS A  98     7411  11820  10684   -720  -1672    985       C  
ATOM   1213  ND1 HIS A  98      -9.431  36.619  -2.664  1.00 78.19           N  
ANISOU 1213  ND1 HIS A  98     7582  11529  10598   -715  -2037    954       N  
ATOM   1214  CD2 HIS A  98      -9.181  34.632  -3.538  1.00 77.59           C  
ANISOU 1214  CD2 HIS A  98     7032  11620  10830   -891  -1718   1203       C  
ATOM   1215  CE1 HIS A  98      -8.133  36.409  -2.792  1.00 79.90           C  
ANISOU 1215  CE1 HIS A  98     7709  11562  11087   -876  -2292   1144       C  
ATOM   1216  NE2 HIS A  98      -7.955  35.211  -3.320  1.00 78.73           N  
ANISOU 1216  NE2 HIS A  98     7275  11511  11129   -985  -2105   1299       N  
ATOM   1217  H   HIS A  98     -11.066  36.008  -0.808  1.00100.34           H  
ATOM   1218  HA  HIS A  98     -13.156  34.839  -1.906  1.00 96.79           H  
ATOM   1219  HB2 HIS A  98     -11.890  34.927  -3.896  1.00 92.54           H  
ATOM   1220  HB3 HIS A  98     -11.962  36.340  -3.177  1.00 92.54           H  
ATOM   1221  HD2 HIS A  98      -9.338  33.790  -3.901  1.00 93.11           H  
ATOM   1222  HE1 HIS A  98      -7.459  37.003  -2.552  1.00 95.88           H  
ATOM   1223  HE2 HIS A  98      -7.194  34.852  -3.498  1.00 94.48           H  
ATOM   1224  N   LYS A  99     -10.682  32.951  -1.252  1.00 79.10           N  
ANISOU 1224  N   LYS A  99     7591  12146  10317   -799  -1357   1113       N  
ATOM   1225  CA  LYS A  99     -10.219  31.566  -1.212  1.00 76.10           C  
ANISOU 1225  CA  LYS A  99     7030  11820  10064   -944  -1268   1306       C  
ATOM   1226  C   LYS A  99     -11.081  30.780  -0.234  1.00 75.62           C  
ANISOU 1226  C   LYS A  99     7124  11941   9667   -884  -1048   1249       C  
ATOM   1227  O   LYS A  99     -10.907  30.871   0.983  1.00 77.48           O  
ANISOU 1227  O   LYS A  99     7669  12110   9659   -873  -1220   1231       O  
ATOM   1228  CB  LYS A  99      -8.748  31.511  -0.816  1.00 77.95           C  
ANISOU 1228  CB  LYS A  99     7324  11819  10474  -1104  -1642   1487       C  
ATOM   1229  H   LYS A  99     -10.152  33.507  -0.865  1.00 94.92           H  
ATOM   1230  HA  LYS A  99     -10.314  31.169  -2.092  1.00 91.32           H  
ATOM   1231  N   PHE A 100     -12.028  30.011  -0.764  1.00 74.41           N  
ANISOU 1231  N   PHE A 100     6758  12017   9499   -841   -665   1218       N  
ATOM   1232  CA  PHE A 100     -12.797  29.084   0.048  1.00 71.88           C  
ANISOU 1232  CA  PHE A 100     6528  11877   8905   -804   -427   1192       C  
ATOM   1233  C   PHE A 100     -11.984  27.818   0.310  1.00 75.71           C  
ANISOU 1233  C   PHE A 100     6898  12345   9524   -975   -459   1413       C  
ATOM   1234  O   PHE A 100     -10.939  27.581  -0.300  1.00 73.27           O  
ANISOU 1234  O   PHE A 100     6389  11912   9539  -1118   -613   1583       O  
ATOM   1235  CB  PHE A 100     -14.112  28.725  -0.641  1.00 72.05           C  
ANISOU 1235  CB  PHE A 100     6353  12147   8874   -696     -5   1078       C  
ATOM   1236  CG  PHE A 100     -15.209  29.723  -0.422  1.00 72.40           C  
ANISOU 1236  CG  PHE A 100     6600  12265   8645   -502     88    836       C  
ATOM   1237  CD1 PHE A 100     -15.170  30.970  -1.022  1.00 70.26           C  
ANISOU 1237  CD1 PHE A 100     6346  11890   8458   -432    -48    731       C  
ATOM   1238  CD2 PHE A 100     -16.291  29.402   0.378  1.00 70.51           C  
ANISOU 1238  CD2 PHE A 100     6530  12197   8064   -390    317    713       C  
ATOM   1239  CE1 PHE A 100     -16.186  31.880  -0.817  1.00 68.04           C  
ANISOU 1239  CE1 PHE A 100     6251  11677   7925   -254     38    507       C  
ATOM   1240  CE2 PHE A 100     -17.308  30.307   0.585  1.00 72.11           C  
ANISOU 1240  CE2 PHE A 100     6917  12468   8015   -211    406    490       C  
ATOM   1241  CZ  PHE A 100     -17.258  31.547  -0.013  1.00 71.35           C  
ANISOU 1241  CZ  PHE A 100     6837  12268   8005   -143    266    386       C  
ATOM   1242  H   PHE A 100     -12.242  30.009  -1.597  1.00 89.30           H  
ATOM   1243  HA  PHE A 100     -13.003  29.498   0.901  1.00 86.25           H  
ATOM   1244  HB2 PHE A 100     -13.956  28.663  -1.597  1.00 86.45           H  
ATOM   1245  HB3 PHE A 100     -14.418  27.869  -0.302  1.00 86.45           H  
ATOM   1246  HD1 PHE A 100     -14.449  31.198  -1.563  1.00 84.31           H  
ATOM   1247  HD2 PHE A 100     -16.330  28.567   0.784  1.00 84.61           H  
ATOM   1248  HE1 PHE A 100     -16.150  32.717  -1.222  1.00 81.65           H  
ATOM   1249  HE2 PHE A 100     -18.029  30.081   1.127  1.00 86.54           H  
ATOM   1250  HZ  PHE A 100     -17.944  32.160   0.125  1.00 85.62           H  
ATOM   1251  N   LEU A 101     -12.473  26.997   1.235  1.00 78.94           N  
ANISOU 1251  N   LEU A 101     7437  12879   9678   -960   -311   1412       N  
ATOM   1252  CA  LEU A 101     -11.840  25.713   1.500  1.00 78.92           C  
ANISOU 1252  CA  LEU A 101     7321  12886   9777  -1112   -300   1612       C  
ATOM   1253  C   LEU A 101     -12.810  24.839   2.280  1.00 77.76           C  
ANISOU 1253  C   LEU A 101     7269  12944   9331  -1049    -15   1561       C  
ATOM   1254  O   LEU A 101     -13.564  25.327   3.126  1.00 83.39           O  
ANISOU 1254  O   LEU A 101     8271  13708   9707   -915     18   1400       O  
ATOM   1255  CB  LEU A 101     -10.526  25.871   2.275  1.00 80.17           C  
ANISOU 1255  CB  LEU A 101     7672  12809   9979  -1230   -707   1741       C  
ATOM   1256  CG  LEU A 101      -9.543  24.696   2.188  1.00 79.82           C  
ANISOU 1256  CG  LEU A 101     7434  12720  10172  -1420   -763   1982       C  
ATOM   1257  CD1 LEU A 101      -9.003  24.526   0.769  1.00 76.10           C  
ANISOU 1257  CD1 LEU A 101     6577  12219  10120  -1519   -730   2100       C  
ATOM   1258  CD2 LEU A 101      -8.393  24.872   3.173  1.00 82.81           C  
ANISOU 1258  CD2 LEU A 101     8064  12879  10523  -1514  -1157   2083       C  
ATOM   1259  H   LEU A 101     -13.166  27.160   1.719  1.00 94.73           H  
ATOM   1260  HA  LEU A 101     -11.645  25.272   0.658  1.00 94.70           H  
ATOM   1261  HB2 LEU A 101     -10.067  26.657   1.939  1.00 96.20           H  
ATOM   1262  HB3 LEU A 101     -10.739  26.000   3.213  1.00 96.20           H  
ATOM   1263  HG  LEU A 101     -10.012  23.881   2.425  1.00 95.78           H  
ATOM   1264 HD11 LEU A 101      -8.387  23.776   0.754  1.00 91.32           H  
ATOM   1265 HD12 LEU A 101      -9.745  24.357   0.167  1.00 91.32           H  
ATOM   1266 HD13 LEU A 101      -8.542  25.338   0.507  1.00 91.32           H  
ATOM   1267 HD21 LEU A 101      -7.791  24.116   3.094  1.00 99.38           H  
ATOM   1268 HD22 LEU A 101      -7.922  25.694   2.964  1.00 99.38           H  
ATOM   1269 HD23 LEU A 101      -8.753  24.916   4.073  1.00 99.38           H  
ATOM   1270  N   TYR A 102     -12.767  23.542   1.994  1.00 72.23           N  
ANISOU 1270  N   TYR A 102     6325  12360   8760  -1149    188   1701       N  
ATOM   1271  CA  TYR A 102     -13.696  22.575   2.556  1.00 72.98           C  
ANISOU 1271  CA  TYR A 102     6446  12665   8619  -1101    499   1671       C  
ATOM   1272  C   TYR A 102     -12.995  21.693   3.581  1.00 71.90           C  
ANISOU 1272  C   TYR A 102     6442  12472   8404  -1217    368   1824       C  
ATOM   1273  O   TYR A 102     -11.823  21.343   3.426  1.00 70.28           O  
ANISOU 1273  O   TYR A 102     6135  12124   8444  -1373    151   2006       O  
ATOM   1274  CB  TYR A 102     -14.303  21.705   1.451  1.00 72.05           C  
ANISOU 1274  CB  TYR A 102     5944  12742   8692  -1117    864   1705       C  
ATOM   1275  CG  TYR A 102     -15.113  20.536   1.964  1.00 74.71           C  
ANISOU 1275  CG  TYR A 102     6262  13287   8839  -1098   1180   1711       C  
ATOM   1276  CD1 TYR A 102     -16.366  20.729   2.532  1.00 75.25           C  
ANISOU 1276  CD1 TYR A 102     6511  13509   8572   -936   1403   1526       C  
ATOM   1277  CD2 TYR A 102     -14.628  19.237   1.875  1.00 73.36           C  
ANISOU 1277  CD2 TYR A 102     5984  13057   8833  -1207   1219   1854       C  
ATOM   1278  CE1 TYR A 102     -17.112  19.663   3.002  1.00 76.12           C  
ANISOU 1278  CE1 TYR A 102     6603  13807   8512   -919   1696   1532       C  
ATOM   1279  CE2 TYR A 102     -15.367  18.164   2.342  1.00 73.74           C  
ANISOU 1279  CE2 TYR A 102     6174  13104   8742  -1133   1423   1774       C  
ATOM   1280  CZ  TYR A 102     -16.610  18.383   2.904  1.00 74.81           C  
ANISOU 1280  CZ  TYR A 102     6427  13437   8560  -1000   1656   1626       C  
ATOM   1281  OH  TYR A 102     -17.354  17.322   3.371  1.00 76.33           O  
ANISOU 1281  OH  TYR A 102     6769  13576   8657   -930   1830   1542       O  
ATOM   1282  H   TYR A 102     -12.191  23.191   1.460  1.00 86.68           H  
ATOM   1283  HA  TYR A 102     -14.417  23.047   3.002  1.00 87.58           H  
ATOM   1284  HB2 TYR A 102     -14.888  22.255   0.907  1.00 86.47           H  
ATOM   1285  HB3 TYR A 102     -13.585  21.351   0.904  1.00 86.47           H  
ATOM   1286  HD1 TYR A 102     -16.709  21.591   2.600  1.00 90.30           H  
ATOM   1287  HD2 TYR A 102     -13.792  19.086   1.498  1.00 88.03           H  
ATOM   1288  HE1 TYR A 102     -17.949  19.808   3.380  1.00 91.34           H  
ATOM   1289  HE2 TYR A 102     -15.030  17.300   2.277  1.00 88.49           H  
ATOM   1290  HH  TYR A 102     -16.937  16.603   3.252  1.00 91.60           H  
ATOM   1291  N   TYR A 103     -13.732  21.334   4.632  1.00 75.40           N  
ANISOU 1291  N   TYR A 103     7114  13030   8506  -1138    505   1748       N  
ATOM   1292  CA  TYR A 103     -13.218  20.491   5.708  1.00 79.47           C  
ANISOU 1292  CA  TYR A 103     7786  13511   8896  -1228    409   1874       C  
ATOM   1293  C   TYR A 103     -14.187  19.337   5.921  1.00 77.94           C  
ANISOU 1293  C   TYR A 103     7505  13556   8551  -1196    794   1869       C  
ATOM   1294  O   TYR A 103     -15.283  19.536   6.454  1.00 80.68           O  
ANISOU 1294  O   TYR A 103     8028  14035   8592  -1050    988   1706       O  
ATOM   1295  CB  TYR A 103     -13.043  21.291   7.000  1.00 82.98           C  
ANISOU 1295  CB  TYR A 103     8669  13824   9036  -1160    136   1788       C  
ATOM   1296  CG  TYR A 103     -12.208  22.540   6.837  1.00 83.31           C  
ANISOU 1296  CG  TYR A 103     8821  13635   9196  -1169   -237   1766       C  
ATOM   1297  CD1 TYR A 103     -10.829  22.503   6.994  1.00 85.58           C  
ANISOU 1297  CD1 TYR A 103     9125  13711   9681  -1318   -584   1933       C  
ATOM   1298  CD2 TYR A 103     -12.800  23.757   6.525  1.00 84.54           C  
ANISOU 1298  CD2 TYR A 103     9065  13783   9272  -1027   -243   1577       C  
ATOM   1299  CE1 TYR A 103     -10.061  23.645   6.845  1.00 86.00           C  
ANISOU 1299  CE1 TYR A 103     9277  13549   9850  -1328   -926   1914       C  
ATOM   1300  CE2 TYR A 103     -12.042  24.905   6.373  1.00 86.36           C  
ANISOU 1300  CE2 TYR A 103     9397  13801   9614  -1035   -583   1557       C  
ATOM   1301  CZ  TYR A 103     -10.673  24.843   6.534  1.00 87.84           C  
ANISOU 1301  CZ  TYR A 103     9596  13778   9999  -1186   -923   1726       C  
ATOM   1302  OH  TYR A 103      -9.915  25.983   6.384  1.00 89.66           O  
ANISOU 1302  OH  TYR A 103     9924  13794  10348  -1194  -1261   1707       O  
ATOM   1303  H   TYR A 103     -14.550  21.572   4.746  1.00 90.48           H  
ATOM   1304  HA  TYR A 103     -12.357  20.127   5.452  1.00 95.36           H  
ATOM   1305  HB2 TYR A 103     -13.917  21.559   7.323  1.00 99.58           H  
ATOM   1306  HB3 TYR A 103     -12.608  20.728   7.659  1.00 99.58           H  
ATOM   1307  HD1 TYR A 103     -10.414  21.698   7.203  1.00102.70           H  
ATOM   1308  HD2 TYR A 103     -13.723  23.802   6.415  1.00101.45           H  
ATOM   1309  HE1 TYR A 103      -9.138  23.606   6.953  1.00103.20           H  
ATOM   1310  HE2 TYR A 103     -12.453  25.713   6.164  1.00103.63           H  
ATOM   1311  HH  TYR A 103     -10.410  26.635   6.198  1.00107.59           H  
ATOM   1312  N   ASP A 104     -13.791  18.136   5.504  1.00 71.01           N  
ANISOU 1312  N   ASP A 104     6356  12733   7889  -1333    907   2046       N  
ATOM   1313  CA  ASP A 104     -14.591  16.950   5.776  1.00 67.40           C  
ANISOU 1313  CA  ASP A 104     5819  12488   7300  -1321   1250   2065       C  
ATOM   1314  C   ASP A 104     -14.805  16.823   7.279  1.00 71.69           C  
ANISOU 1314  C   ASP A 104     6737  13033   7469  -1270   1196   2025       C  
ATOM   1315  O   ASP A 104     -13.865  16.525   8.022  1.00 70.81           O  
ANISOU 1315  O   ASP A 104     6770  12786   7348  -1375    946   2154       O  
ATOM   1316  CB  ASP A 104     -13.909  15.700   5.214  1.00 69.64           C  
ANISOU 1316  CB  ASP A 104     5786  12793   7881  -1495   1311   2284       C  
ATOM   1317  CG  ASP A 104     -14.788  14.463   5.300  1.00 69.97           C  
ANISOU 1317  CG  ASP A 104     5937  12754   7895  -1363   1544   2130       C  
ATOM   1318  OD1 ASP A 104     -15.582  14.353   6.257  1.00 70.21           O  
ANISOU 1318  OD1 ASP A 104     6107  12986   7583  -1310   1722   2092       O  
ATOM   1319  OD2 ASP A 104     -14.683  13.596   4.408  1.00 72.97           O  
ANISOU 1319  OD2 ASP A 104     6319  12821   8587  -1304   1533   2019       O  
ATOM   1320  H   ASP A 104     -13.068  17.985   5.064  1.00 85.21           H  
ATOM   1321  HA  ASP A 104     -15.457  17.042   5.350  1.00 80.87           H  
ATOM   1322  HB2 ASP A 104     -13.694  15.850   4.280  1.00 83.57           H  
ATOM   1323  HB3 ASP A 104     -13.099  15.528   5.718  1.00 83.57           H  
ATOM   1324  N   GLU A 105     -16.039  17.058   7.735  1.00 75.28           N  
ANISOU 1324  N   GLU A 105     7352  13637   7614  -1108   1428   1844       N  
ATOM   1325  CA  GLU A 105     -16.320  17.031   9.167  1.00 75.35           C  
ANISOU 1325  CA  GLU A 105     7734  13649   7247  -1042   1385   1789       C  
ATOM   1326  C   GLU A 105     -15.923  15.697   9.787  1.00 76.19           C  
ANISOU 1326  C   GLU A 105     7822  13791   7335  -1161   1432   1963       C  
ATOM   1327  O   GLU A 105     -15.409  15.655  10.911  1.00 75.60           O  
ANISOU 1327  O   GLU A 105     8037  13612   7078  -1188   1218   2009       O  
ATOM   1328  CB  GLU A 105     -17.802  17.315   9.413  1.00 76.18           C  
ANISOU 1328  CB  GLU A 105     7951  13941   7053   -854   1693   1579       C  
ATOM   1329  H   GLU A 105     -16.721  17.232   7.240  1.00 90.34           H  
ATOM   1330  HA  GLU A 105     -15.805  17.729   9.602  1.00 90.42           H  
ATOM   1331  N   LYS A 106     -16.147  14.594   9.068  1.00 75.54           N  
ANISOU 1331  N   LYS A 106     7404  13854   7443  -1234   1706   2062       N  
ATOM   1332  CA  LYS A 106     -15.836  13.277   9.613  1.00 77.78           C  
ANISOU 1332  CA  LYS A 106     7652  14186   7713  -1345   1777   2226       C  
ATOM   1333  C   LYS A 106     -14.343  13.108   9.872  1.00 78.50           C  
ANISOU 1333  C   LYS A 106     7779  14064   7982  -1512   1408   2415       C  
ATOM   1334  O   LYS A 106     -13.953  12.454  10.845  1.00 81.87           O  
ANISOU 1334  O   LYS A 106     8375  14460   8273  -1573   1326   2512       O  
ATOM   1335  CB  LYS A 106     -16.332  12.186   8.662  1.00 76.99           C  
ANISOU 1335  CB  LYS A 106     7320  13994   7937  -1302   1987   2149       C  
ATOM   1336  CG  LYS A 106     -17.827  12.235   8.385  1.00 76.75           C  
ANISOU 1336  CG  LYS A 106     7392  13887   7881  -1086   2219   1858       C  
ATOM   1337  H   LYS A 106     -16.474  14.584   8.272  1.00 90.65           H  
ATOM   1338  HA  LYS A 106     -16.299  13.169  10.458  1.00 93.33           H  
ATOM   1339  HB2 LYS A 106     -15.871  12.280   7.813  1.00 92.38           H  
ATOM   1340  HB3 LYS A 106     -16.132  11.320   9.050  1.00 92.38           H  
ATOM   1341  N   LYS A 107     -13.496  13.684   9.021  1.00 72.96           N  
ANISOU 1341  N   LYS A 107     6923  13215   7584  -1586   1183   2471       N  
ATOM   1342  CA  LYS A 107     -12.051  13.541   9.146  1.00 72.54           C  
ANISOU 1342  CA  LYS A 107     6870  12954   7738  -1750    834   2654       C  
ATOM   1343  C   LYS A 107     -11.426  14.571  10.080  1.00 78.85           C  
ANISOU 1343  C   LYS A 107     8045  13544   8369  -1720    448   2606       C  
ATOM   1344  O   LYS A 107     -10.209  14.534  10.290  1.00 77.17           O  
ANISOU 1344  O   LYS A 107     7868  13144   8308  -1849    131   2749       O  
ATOM   1345  CB  LYS A 107     -11.399  13.628   7.761  1.00 70.26           C  
ANISOU 1345  CB  LYS A 107     6223  12602   7873  -1850    779   2748       C  
ATOM   1346  CG  LYS A 107     -11.788  12.484   6.834  1.00 62.69           C  
ANISOU 1346  CG  LYS A 107     4969  11714   7136  -1846   1066   2754       C  
ATOM   1347  CD  LYS A 107     -11.307  12.706   5.405  1.00 59.68           C  
ANISOU 1347  CD  LYS A 107     4490  11042   7144  -1770    940   2635       C  
ATOM   1348  CE  LYS A 107     -11.677  11.528   4.518  1.00 60.00           C  
ANISOU 1348  CE  LYS A 107     4604  10811   7383  -1597   1075   2397       C  
ATOM   1349  NZ  LYS A 107     -11.291  11.732   3.100  1.00 78.92           N  
ANISOU 1349  NZ  LYS A 107     6991  12924  10070  -1514    997   2249       N  
ATOM   1350  H   LYS A 107     -13.739  14.170   8.354  1.00 87.55           H  
ATOM   1351  HA  LYS A 107     -11.858  12.661   9.508  1.00 87.05           H  
ATOM   1352  HB2 LYS A 107     -11.670  14.458   7.338  1.00 84.32           H  
ATOM   1353  HB3 LYS A 107     -10.435  13.611   7.866  1.00 84.32           H  
ATOM   1354  HG2 LYS A 107     -11.390  11.662   7.162  1.00 75.22           H  
ATOM   1355  HG3 LYS A 107     -12.754  12.403   6.818  1.00 75.22           H  
ATOM   1356  HD2 LYS A 107     -11.725  13.503   5.045  1.00 71.62           H  
ATOM   1357  HD3 LYS A 107     -10.341  12.799   5.401  1.00 71.62           H  
ATOM   1358  HE2 LYS A 107     -11.224  10.734   4.841  1.00 72.00           H  
ATOM   1359  HE3 LYS A 107     -12.638  11.398   4.551  1.00 72.00           H  
ATOM   1360  HZ1 LYS A 107     -11.525  11.022   2.616  1.00 94.70           H  
ATOM   1361  HZ2 LYS A 107     -11.700  12.452   2.773  1.00 94.70           H  
ATOM   1362  HZ3 LYS A 107     -10.411  11.847   3.038  1.00 94.70           H  
ATOM   1363  N   MET A 108     -12.222  15.483  10.645  1.00 91.44           N  
ANISOU 1363  N   MET A 108     9919  15164   9659  -1554    465   2407       N  
ATOM   1364  CA  MET A 108     -11.691  16.442  11.610  1.00100.08           C  
ANISOU 1364  CA  MET A 108    11391  16067  10566  -1517    107   2353       C  
ATOM   1365  C   MET A 108     -11.030  15.740  12.789  1.00100.84           C  
ANISOU 1365  C   MET A 108    11705  16087  10523  -1602    -60   2479       C  
ATOM   1366  O   MET A 108     -10.093  16.280  13.387  1.00103.48           O  
ANISOU 1366  O   MET A 108    12260  16213  10846  -1647   -432   2521       O  
ATOM   1367  CB  MET A 108     -12.812  17.355  12.109  1.00104.03           C  
ANISOU 1367  CB  MET A 108    12159  16643  10723  -1316    212   2117       C  
ATOM   1368  CG  MET A 108     -13.456  18.222  11.035  1.00102.75           C  
ANISOU 1368  CG  MET A 108    11832  16538  10672  -1217    339   1972       C  
ATOM   1369  SD  MET A 108     -12.649  19.824  10.844  1.00105.41           S  
ANISOU 1369  SD  MET A 108    12320  16620  11110  -1199    -84   1906       S  
ATOM   1370  CE  MET A 108     -13.200  20.666  12.330  1.00108.31           C  
ANISOU 1370  CE  MET A 108    13202  16953  10996  -1035   -201   1724       C  
ATOM   1371  H   MET A 108     -13.063  15.566  10.486  1.00109.73           H  
ATOM   1372  HA  MET A 108     -11.031  16.997  11.167  1.00120.09           H  
ATOM   1373  HB2 MET A 108     -13.510  16.804  12.498  1.00124.83           H  
ATOM   1374  HB3 MET A 108     -12.450  17.948  12.786  1.00124.83           H  
ATOM   1375  HG2 MET A 108     -13.405  17.758  10.184  1.00123.30           H  
ATOM   1376  HG3 MET A 108     -14.383  18.380  11.271  1.00123.30           H  
ATOM   1377  HE1 MET A 108     -12.824  21.560  12.344  1.00129.97           H  
ATOM   1378  HE2 MET A 108     -14.169  20.714  12.324  1.00129.97           H  
ATOM   1379  HE3 MET A 108     -12.898  20.167  13.105  1.00129.97           H  
ATOM   1380  N   ALA A 109     -11.504  14.542  13.139  1.00 87.95           N  
ANISOU 1380  N   ALA A 109    10014  14617   8786  -1623    207   2542       N  
ATOM   1381  CA  ALA A 109     -10.950  13.823  14.281  1.00 91.11           C  
ANISOU 1381  CA  ALA A 109    10623  14958   9036  -1697     73   2659       C  
ATOM   1382  C   ALA A 109      -9.509  13.398  14.023  1.00 96.29           C  
ANISOU 1382  C   ALA A 109    11136  15439  10010  -1891   -211   2874       C  
ATOM   1383  O   ALA A 109      -8.645  13.541  14.896  1.00 98.44           O  
ANISOU 1383  O   ALA A 109    11654  15539  10211  -1946   -532   2942       O  
ATOM   1384  CB  ALA A 109     -11.819  12.607  14.599  1.00 91.17           C  
ANISOU 1384  CB  ALA A 109    10566  15189   8885  -1678    448   2680       C  
ATOM   1385  H   ALA A 109     -12.140  14.130  12.733  1.00105.54           H  
ATOM   1386  HA  ALA A 109     -10.956  14.407  15.055  1.00109.33           H  
ATOM   1387  HB1 ALA A 109     -11.440  12.138  15.359  1.00109.40           H  
ATOM   1388  HB2 ALA A 109     -12.717  12.907  14.809  1.00109.40           H  
ATOM   1389  HB3 ALA A 109     -11.838  12.022  13.825  1.00109.40           H  
ATOM   1390  N   ASN A 110      -9.233  12.869  12.829  0.50 99.76           N  
ANISOU 1390  N   ASN A 110    11178  15920  10806  -1996    -97   2984       N  
ATOM   1391  CA  ASN A 110      -7.890  12.389  12.518  0.50102.03           C  
ANISOU 1391  CA  ASN A 110    11301  16053  11413  -2184   -340   3196       C  
ATOM   1392  C   ASN A 110      -6.844  13.461  12.799  0.50108.29           C  
ANISOU 1392  C   ASN A 110    12294  16584  12267  -2214   -789   3201       C  
ATOM   1393  O   ASN A 110      -5.825  13.198  13.447  0.50107.36           O  
ANISOU 1393  O   ASN A 110    12301  16309  12181  -2323  -1071   3332       O  
ATOM   1394  CB  ASN A 110      -7.823  11.942  11.057  0.50100.33           C  
ANISOU 1394  CB  ASN A 110    10633  15912  11575  -2266   -159   3279       C  
ATOM   1395  H   ASN A 110      -9.801  12.777  12.190  0.50119.71           H  
ATOM   1396  HA  ASN A 110      -7.691  11.621  13.076  0.50122.44           H  
ATOM   1397  N   PHE A 111      -7.084  14.678  12.322  1.00120.97           N  
ANISOU 1397  N   PHE A 111    13934  18137  13892  -2118   -863   3058       N  
ATOM   1398  CA  PHE A 111      -6.167  15.801  12.507  1.00120.07           C  
ANISOU 1398  CA  PHE A 111    14001  17777  13844  -2134  -1278   3045       C  
ATOM   1399  C   PHE A 111      -6.786  16.753  13.526  1.00124.35           C  
ANISOU 1399  C   PHE A 111    14952  18299  13995  -1968  -1358   2853       C  
ATOM   1400  O   PHE A 111      -7.674  17.544  13.193  1.00125.50           O  
ANISOU 1400  O   PHE A 111    15126  18526  14034  -1828  -1218   2676       O  
ATOM   1401  CB  PHE A 111      -5.891  16.500  11.180  1.00113.21           C  
ANISOU 1401  CB  PHE A 111    12861  16846  13307  -2156  -1323   3036       C  
ATOM   1402  CG  PHE A 111      -5.029  15.701  10.242  1.00107.10           C  
ANISOU 1402  CG  PHE A 111    11718  16037  12939  -2333  -1332   3240       C  
ATOM   1403  CD1 PHE A 111      -5.496  14.521   9.685  1.00103.68           C  
ANISOU 1403  CD1 PHE A 111    10992  15798  12604  -2379   -990   3318       C  
ATOM   1404  CD2 PHE A 111      -3.753  16.131   9.915  1.00104.15           C  
ANISOU 1404  CD2 PHE A 111    11287  15435  12849  -2451  -1682   3354       C  
ATOM   1405  CE1 PHE A 111      -4.706  13.783   8.823  1.00100.16           C  
ANISOU 1405  CE1 PHE A 111    10208  15320  12529  -2539   -996   3505       C  
ATOM   1406  CE2 PHE A 111      -2.959  15.398   9.052  1.00100.44           C  
ANISOU 1406  CE2 PHE A 111    10478  14932  12752  -2612  -1687   3543       C  
ATOM   1407  CZ  PHE A 111      -3.436  14.223   8.505  1.00 99.25           C  
ANISOU 1407  CZ  PHE A 111    10041  14977  12692  -2655  -1344   3618       C  
ATOM   1408  H   PHE A 111      -7.790  14.885  11.877  1.00145.16           H  
ATOM   1409  HA  PHE A 111      -5.326  15.476  12.863  1.00144.08           H  
ATOM   1410  HB2 PHE A 111      -6.736  16.670  10.734  1.00135.85           H  
ATOM   1411  HB3 PHE A 111      -5.438  17.339  11.357  1.00135.85           H  
ATOM   1412  HD1 PHE A 111      -6.351  14.220   9.897  1.00124.42           H  
ATOM   1413  HD2 PHE A 111      -3.427  16.922  10.280  1.00124.98           H  
ATOM   1414  HE1 PHE A 111      -5.030  12.992   8.456  1.00120.19           H  
ATOM   1415  HE2 PHE A 111      -2.104  15.696   8.839  1.00120.53           H  
ATOM   1416  HZ  PHE A 111      -2.904  13.728   7.925  1.00119.10           H  
ATOM   1417  N   GLN A 112      -6.310  16.674  14.770  1.00128.81           N  
ANISOU 1417  N   GLN A 112    15838  18755  14348  -1985  -1587   2888       N  
ATOM   1418  CA  GLN A 112      -6.853  17.521  15.828  1.00132.61           C  
ANISOU 1418  CA  GLN A 112    16729  19212  14445  -1830  -1675   2714       C  
ATOM   1419  C   GLN A 112      -6.332  18.949  15.718  1.00129.92           C  
ANISOU 1419  C   GLN A 112    16535  18668  14162  -1791  -2013   2628       C  
ATOM   1420  O   GLN A 112      -7.061  19.905  16.008  1.00135.76           O  
ANISOU 1420  O   GLN A 112    17490  19428  14664  -1634  -1997   2438       O  
ATOM   1421  CB  GLN A 112      -6.503  16.933  17.196  1.00133.68           C  
ANISOU 1421  CB  GLN A 112    17160  19297  14333  -1860  -1808   2784       C  
ATOM   1422  CG  GLN A 112      -7.431  17.372  18.316  1.00135.24           C  
ANISOU 1422  CG  GLN A 112    17743  19563  14078  -1687  -1738   2607       C  
ATOM   1423  CD  GLN A 112      -8.824  16.791  18.176  1.00134.41           C  
ANISOU 1423  CD  GLN A 112    17545  19732  13794  -1582  -1271   2513       C  
ATOM   1424  OE1 GLN A 112      -9.045  15.860  17.400  1.00132.33           O  
ANISOU 1424  OE1 GLN A 112    16947  19610  13725  -1652  -1002   2603       O  
ATOM   1425  NE2 GLN A 112      -9.774  17.340  18.925  1.00136.33           N  
ANISOU 1425  NE2 GLN A 112    18081  20048  13668  -1411  -1173   2332       N  
ATOM   1426  H   GLN A 112      -5.680  16.145  15.023  1.00154.57           H  
ATOM   1427  HA  GLN A 112      -7.819  17.546  15.748  1.00159.13           H  
ATOM   1428  HB2 GLN A 112      -6.546  15.966  17.139  1.00160.41           H  
ATOM   1429  HB3 GLN A 112      -5.604  17.209  17.432  1.00160.41           H  
ATOM   1430  HG2 GLN A 112      -7.066  17.076  19.165  1.00162.28           H  
ATOM   1431  HG3 GLN A 112      -7.506  18.339  18.305  1.00162.28           H  
ATOM   1432 HE21 GLN A 112      -9.583  17.990  19.454  1.00163.59           H  
ATOM   1433 HE22 GLN A 112     -10.581  17.044  18.881  1.00163.59           H  
ATOM   1434  N   ASN A 113      -5.075  19.114  15.298  0.80116.90           N  
ANISOU 1434  N   ASN A 113    14768  16819  12830  -1931  -2321   2765       N  
ATOM   1435  CA  ASN A 113      -4.454  20.436  15.308  0.80115.68           C  
ANISOU 1435  CA  ASN A 113    14774  16448  12732  -1906  -2681   2700       C  
ATOM   1436  C   ASN A 113      -5.189  21.407  14.392  0.80115.66           C  
ANISOU 1436  C   ASN A 113    14661  16507  12779  -1790  -2546   2537       C  
ATOM   1437  O   ASN A 113      -5.298  22.600  14.701  0.80117.09           O  
ANISOU 1437  O   ASN A 113    15082  16588  12820  -1684  -2728   2394       O  
ATOM   1438  CB  ASN A 113      -2.986  20.324  14.896  0.80116.68           C  
ANISOU 1438  CB  ASN A 113    14741  16362  13228  -2088  -3000   2891       C  
ATOM   1439  H   ASN A 113      -4.568  18.484  15.006  0.80140.28           H  
ATOM   1440  HA  ASN A 113      -4.486  20.792  16.209  0.80138.82           H  
ATOM   1441  N   PHE A 114      -5.697  20.921  13.263  0.80113.32           N  
ANISOU 1441  N   PHE A 114    14005  16372  12681  -1806  -2231   2557       N  
ATOM   1442  CA  PHE A 114      -6.334  21.800  12.293  0.80111.32           C  
ANISOU 1442  CA  PHE A 114    13616  16172  12509  -1707  -2105   2416       C  
ATOM   1443  C   PHE A 114      -7.554  22.484  12.900  0.80109.27           C  
ANISOU 1443  C   PHE A 114    13631  16025  11863  -1506  -1957   2187       C  
ATOM   1444  O   PHE A 114      -8.222  21.946  13.788  0.80108.88           O  
ANISOU 1444  O   PHE A 114    13764  16099  11506  -1441  -1792   2143       O  
ATOM   1445  CB  PHE A 114      -6.745  21.009  11.050  0.80110.64           C  
ANISOU 1445  CB  PHE A 114    13102  16261  12677  -1755  -1762   2478       C  
ATOM   1446  H   PHE A 114      -5.685  20.091  13.038  0.80135.99           H  
ATOM   1447  HA  PHE A 114      -5.705  22.486  12.022  0.80133.59           H  
ATOM   1448  N   LYS A 115      -7.838  23.691  12.410  0.80106.89           N  
ANISOU 1448  N   LYS A 115    13360  15676  11579  -1407  -2018   2042       N  
ATOM   1449  CA  LYS A 115      -9.004  24.454  12.819  0.80102.93           C  
ANISOU 1449  CA  LYS A 115    13088  15277  10745  -1213  -1877   1816       C  
ATOM   1450  C   LYS A 115      -9.579  25.138  11.585  0.80 97.68           C  
ANISOU 1450  C   LYS A 115    12191  14680  10244  -1142  -1716   1707       C  
ATOM   1451  O   LYS A 115      -8.818  25.704  10.785  0.80 92.09           O  
ANISOU 1451  O   LYS A 115    11329  13826   9834  -1210  -1915   1759       O  
ATOM   1452  CB  LYS A 115      -8.655  25.503  13.884  0.80104.66           C  
ANISOU 1452  CB  LYS A 115    13725  15313  10728  -1142  -2227   1722       C  
ATOM   1453  H   LYS A 115      -7.354  24.094  11.824  0.80128.27           H  
ATOM   1454  HA  LYS A 115      -9.675  23.854  13.182  0.80123.52           H  
ATOM   1455  N   PRO A 116     -10.912  25.108  11.393  0.80101.02           N  
ANISOU 1455  N   PRO A 116    12580  15319  10483  -1003  -1358   1557       N  
ATOM   1456  CA  PRO A 116     -11.479  25.758  10.208  0.80 99.24           C  
ANISOU 1456  CA  PRO A 116    12134  15160  10413   -932  -1202   1450       C  
ATOM   1457  C   PRO A 116     -11.815  27.229  10.434  0.80 99.88           C  
ANISOU 1457  C   PRO A 116    12473  15156  10322   -786  -1360   1254       C  
ATOM   1458  O   PRO A 116     -11.952  27.639  11.587  0.80101.06           O  
ANISOU 1458  O   PRO A 116    12985  15255  10159   -706  -1495   1168       O  
ATOM   1459  CB  PRO A 116     -12.749  24.947   9.945  0.80 98.25           C  
ANISOU 1459  CB  PRO A 116    11852  15310  10170   -857   -740   1387       C  
ATOM   1460  CG  PRO A 116     -13.139  24.374  11.297  0.80100.83           C  
ANISOU 1460  CG  PRO A 116    12467  15706  10138   -813   -679   1370       C  
ATOM   1461  CD  PRO A 116     -11.970  24.539  12.246  0.80103.57           C  
ANISOU 1461  CD  PRO A 116    13074  15830  10449   -900  -1084   1470       C  
ATOM   1462  HA  PRO A 116     -10.878  25.673   9.452  0.80119.09           H  
ATOM   1463  HB2 PRO A 116     -13.445  25.530   9.606  0.80117.90           H  
ATOM   1464  HB3 PRO A 116     -12.558  24.236   9.314  0.80117.90           H  
ATOM   1465  HG2 PRO A 116     -13.911  24.856  11.634  0.80121.00           H  
ATOM   1466  HG3 PRO A 116     -13.352  23.434  11.193  0.80121.00           H  
ATOM   1467  HD2 PRO A 116     -12.198  25.157  12.959  0.80124.29           H  
ATOM   1468  HD3 PRO A 116     -11.695  23.678  12.596  0.80124.29           H  
ATOM   1469  N   ASN A 119     -17.608  27.755   9.741  1.00101.01           N  
ANISOU 1469  N   ASN A 119    12577  16158   9646   -132     69    518       N  
ATOM   1470  CA  ASN A 119     -17.369  27.571   8.314  1.00 98.78           C  
ANISOU 1470  CA  ASN A 119    11893  15895   9744   -212    159    596       C  
ATOM   1471  C   ASN A 119     -18.689  27.430   7.561  1.00 99.25           C  
ANISOU 1471  C   ASN A 119    11750  16184   9775    -97    568    465       C  
ATOM   1472  O   ASN A 119     -18.976  28.196   6.641  1.00 98.75           O  
ANISOU 1472  O   ASN A 119    11555  16122   9844    -36    601    369       O  
ATOM   1473  CB  ASN A 119     -16.493  26.339   8.072  1.00 96.08           C  
ANISOU 1473  CB  ASN A 119    11315  15535   9655   -401    147    833       C  
ATOM   1474  CG  ASN A 119     -16.054  26.210   6.625  1.00 92.18           C  
ANISOU 1474  CG  ASN A 119    10425  15027   9574   -497    183    930       C  
ATOM   1475  OD1 ASN A 119     -15.922  27.206   5.913  1.00 90.73           O  
ANISOU 1475  OD1 ASN A 119    10188  14755   9530   -460     65    860       O  
ATOM   1476  ND2 ASN A 119     -15.829  24.978   6.182  1.00 89.39           N  
ANISOU 1476  ND2 ASN A 119     9791  14759   9416   -619    348   1092       N  
ATOM   1477  HA  ASN A 119     -16.903  28.347   7.966  1.00118.53           H  
ATOM   1478  HB2 ASN A 119     -15.697  26.404   8.623  1.00115.29           H  
ATOM   1479  HB3 ASN A 119     -16.995  25.543   8.306  1.00115.29           H  
ATOM   1480 HD21 ASN A 119     -15.578  24.852   5.369  1.00107.27           H  
ATOM   1481 HD22 ASN A 119     -15.933  24.306   6.708  1.00107.27           H  
ATOM   1482  N   ARG A 120     -19.486  26.446   7.962  1.00 99.33           N  
ANISOU 1482  N   ARG A 120    11740  16387   9614    -68    878    461       N  
ATOM   1483  CA  ARG A 120     -20.780  26.173   7.354  1.00 98.78           C  
ANISOU 1483  CA  ARG A 120    11484  16547   9500     39   1285    343       C  
ATOM   1484  C   ARG A 120     -21.906  26.642   8.269  1.00100.65           C  
ANISOU 1484  C   ARG A 120    12029  16885   9330    220   1421    141       C  
ATOM   1485  O   ARG A 120     -21.750  26.739   9.489  1.00109.35           O  
ANISOU 1485  O   ARG A 120    13462  17923  10165    244   1273    128       O  
ATOM   1486  CB  ARG A 120     -20.928  24.677   7.057  1.00 96.52           C  
ANISOU 1486  CB  ARG A 120    10921  16418   9334    -57   1567    483       C  
ATOM   1487  CG  ARG A 120     -22.276  24.282   6.472  1.00 92.23           C  
ANISOU 1487  CG  ARG A 120    10179  16118   8744     48   2000    369       C  
ATOM   1488  CD  ARG A 120     -22.282  22.831   6.019  1.00 88.14           C  
ANISOU 1488  CD  ARG A 120     9348  15735   8405    -64   2249    525       C  
ATOM   1489  NE  ARG A 120     -22.011  21.907   7.118  1.00 87.06           N  
ANISOU 1489  NE  ARG A 120     9369  15608   8102   -132   2236    635       N  
ATOM   1490  CZ  ARG A 120     -22.935  21.409   7.937  1.00 88.28           C  
ANISOU 1490  CZ  ARG A 120     9670  15915   7957    -45   2475    562       C  
ATOM   1491  NH1 ARG A 120     -24.213  21.738   7.799  1.00 87.84           N  
ANISOU 1491  NH1 ARG A 120     9665  15900   7811    112   2695    366       N  
ATOM   1492  NH2 ARG A 120     -22.578  20.576   8.906  1.00 87.51           N  
ANISOU 1492  NH2 ARG A 120     9711  15809   7728   -117   2439    677       N  
ATOM   1493  H   ARG A 120     -19.292  25.907   8.604  1.00119.20           H  
ATOM   1494  HA  ARG A 120     -20.847  26.657   6.516  1.00118.53           H  
ATOM   1495  HB2 ARG A 120     -20.244  24.417   6.421  1.00115.82           H  
ATOM   1496  HB3 ARG A 120     -20.810  24.184   7.884  1.00115.82           H  
ATOM   1497  HG2 ARG A 120     -22.963  24.393   7.148  1.00110.67           H  
ATOM   1498  HG3 ARG A 120     -22.468  24.842   5.704  1.00110.67           H  
ATOM   1499  HD2 ARG A 120     -23.153  22.616   5.652  1.00105.77           H  
ATOM   1500  HD3 ARG A 120     -21.596  22.707   5.344  1.00105.77           H  
ATOM   1501  HE  ARG A 120     -21.195  21.667   7.246  1.00104.47           H  
ATOM   1502 HH11 ARG A 120     -24.453  22.278   7.174  1.00105.41           H  
ATOM   1503 HH12 ARG A 120     -24.802  21.411   8.334  1.00105.41           H  
ATOM   1504 HH21 ARG A 120     -21.752  20.358   9.003  1.00105.01           H  
ATOM   1505 HH22 ARG A 120     -23.173  20.253   9.437  1.00105.01           H  
ATOM   1506  N   GLU A 121     -23.053  26.938   7.659  1.00 91.19           N  
ANISOU 1506  N   GLU A 121    10717  15844   8087    351   1706    -19       N  
ATOM   1507  CA  GLU A 121     -24.218  27.399   8.404  1.00 88.89           C  
ANISOU 1507  CA  GLU A 121    10686  15663   7427    532   1869   -222       C  
ATOM   1508  C   GLU A 121     -25.479  27.047   7.631  1.00 87.37           C  
ANISOU 1508  C   GLU A 121    10247  15701   7249    625   2289   -327       C  
ATOM   1509  O   GLU A 121     -25.561  27.299   6.425  1.00 83.04           O  
ANISOU 1509  O   GLU A 121     9422  15174   6955    621   2360   -344       O  
ATOM   1510  CB  GLU A 121     -24.152  28.911   8.650  1.00 91.13           C  
ANISOU 1510  CB  GLU A 121    11238  15802   7585    639   1607   -375       C  
ATOM   1511  H   GLU A 121     -23.180  26.880   6.811  1.00109.43           H  
ATOM   1512  HA  GLU A 121     -24.249  26.950   9.263  1.00106.67           H  
ATOM   1513  N   GLU A 122     -26.452  26.468   8.327  1.00 97.20           N  
ANISOU 1513  N   GLU A 122    11594  17115   8223    710   2565   -396       N  
ATOM   1514  CA  GLU A 122     -27.736  26.129   7.733  1.00 97.19           C  
ANISOU 1514  CA  GLU A 122    11499  16919   8510    740   2786   -475       C  
ATOM   1515  C   GLU A 122     -28.714  27.283   7.906  1.00 96.93           C  
ANISOU 1515  C   GLU A 122    11683  16812   8334    895   2798   -687       C  
ATOM   1516  O   GLU A 122     -28.670  28.017   8.897  1.00 99.33           O  
ANISOU 1516  O   GLU A 122    12284  17213   8242   1001   2701   -790       O  
ATOM   1517  CB  GLU A 122     -28.310  24.864   8.374  1.00 98.39           C  
ANISOU 1517  CB  GLU A 122    11721  16950   8711    685   2939   -410       C  
ATOM   1518  CG  GLU A 122     -27.397  23.655   8.278  1.00 97.45           C  
ANISOU 1518  CG  GLU A 122    11410  16873   8742    531   2925   -201       C  
ATOM   1519  CD  GLU A 122     -27.186  23.197   6.848  1.00 96.90           C  
ANISOU 1519  CD  GLU A 122    11017  16643   9158    430   2926   -115       C  
ATOM   1520  OE1 GLU A 122     -28.089  23.418   6.014  1.00 96.49           O  
ANISOU 1520  OE1 GLU A 122    10930  16371   9363    470   2994   -212       O  
ATOM   1521  OE2 GLU A 122     -26.115  22.621   6.558  1.00 96.41           O  
ANISOU 1521  OE2 GLU A 122    10762  16649   9222    302   2843     55       O  
ATOM   1522  H   GLU A 122     -26.390  26.260   9.159  1.00116.64           H  
ATOM   1523  HA  GLU A 122     -27.619  25.965   6.784  1.00116.63           H  
ATOM   1524  HB2 GLU A 122     -28.474  25.038   9.314  1.00118.07           H  
ATOM   1525  HB3 GLU A 122     -29.144  24.642   7.931  1.00118.07           H  
ATOM   1526  HG2 GLU A 122     -26.532  23.881   8.652  1.00116.94           H  
ATOM   1527  HG3 GLU A 122     -27.792  22.920   8.773  1.00116.94           H  
ATOM   1528  N   MET A 123     -29.606  27.435   6.932  1.00 93.36           N  
ANISOU 1528  N   MET A 123    11107  16153   8212    901   2895   -745       N  
ATOM   1529  CA  MET A 123     -30.558  28.536   6.956  1.00 91.86           C  
ANISOU 1529  CA  MET A 123    11087  15876   7938   1023   2910   -925       C  
ATOM   1530  C   MET A 123     -31.550  28.360   5.817  1.00 89.17           C  
ANISOU 1530  C   MET A 123    10599  15274   8007    982   3029   -929       C  
ATOM   1531  O   MET A 123     -31.305  27.615   4.864  1.00 87.96           O  
ANISOU 1531  O   MET A 123    10217  15012   8193    879   3047   -810       O  
ATOM   1532  CB  MET A 123     -29.848  29.888   6.837  1.00 91.85           C  
ANISOU 1532  CB  MET A 123    11135  16037   7728   1121   2718  -1025       C  
ATOM   1533  CG  MET A 123     -28.992  30.016   5.586  1.00 90.10           C  
ANISOU 1533  CG  MET A 123    10597  15867   7772   1055   2635   -947       C  
ATOM   1534  SD  MET A 123     -28.078  31.568   5.490  1.00 92.10           S  
ANISOU 1534  SD  MET A 123    10922  16318   7755   1171   2393  -1076       S  
ATOM   1535  CE  MET A 123     -26.951  31.388   6.870  1.00 92.10           C  
ANISOU 1535  CE  MET A 123    11244  16164   7587   1075   2057   -945       C  
ATOM   1536  H   MET A 123     -29.680  26.916   6.250  1.00112.03           H  
ATOM   1537  HA  MET A 123     -31.038  28.522   7.799  1.00110.23           H  
ATOM   1538  HB2 MET A 123     -30.515  30.592   6.815  1.00110.22           H  
ATOM   1539  HB3 MET A 123     -29.269  30.006   7.607  1.00110.22           H  
ATOM   1540  HG2 MET A 123     -28.348  29.291   5.572  1.00108.12           H  
ATOM   1541  HG3 MET A 123     -29.566  29.962   4.807  1.00108.12           H  
ATOM   1542  HE1 MET A 123     -26.391  32.179   6.925  1.00110.52           H  
ATOM   1543  HE2 MET A 123     -27.466  31.289   7.686  1.00110.52           H  
ATOM   1544  HE3 MET A 123     -26.401  30.602   6.728  1.00110.52           H  
ATOM   1545  N   LYS A 124     -32.676  29.059   5.933  1.00 85.95           N  
ANISOU 1545  N   LYS A 124    10354  14745   7559   1058   3095  -1062       N  
ATOM   1546  CA  LYS A 124     -33.648  29.117   4.857  1.00 82.03           C  
ANISOU 1546  CA  LYS A 124     9767  14001   7401   1030   3181  -1072       C  
ATOM   1547  C   LYS A 124     -33.137  30.024   3.741  1.00 79.94           C  
ANISOU 1547  C   LYS A 124     9339  13756   7277   1054   3053  -1091       C  
ATOM   1548  O   LYS A 124     -32.222  30.830   3.929  1.00 80.96           O  
ANISOU 1548  O   LYS A 124     9465  14096   7200   1118   2907  -1141       O  
ATOM   1549  CB  LYS A 124     -34.996  29.615   5.378  1.00 80.85           C  
ANISOU 1549  CB  LYS A 124     9841  13730   7150   1089   3292  -1197       C  
ATOM   1550  CG  LYS A 124     -35.633  28.695   6.408  1.00 79.94           C  
ANISOU 1550  CG  LYS A 124     9880  13563   6932   1053   3438  -1183       C  
ATOM   1551  H   LYS A 124     -32.898  29.509   6.632  1.00103.14           H  
ATOM   1552  HA  LYS A 124     -33.773  28.227   4.491  1.00 98.44           H  
ATOM   1553  HB2 LYS A 124     -34.869  30.483   5.793  1.00 97.03           H  
ATOM   1554  HB3 LYS A 124     -35.610  29.694   4.631  1.00 97.03           H  
ATOM   1555  N   PHE A 125     -33.747  29.884   2.561  1.00 94.50           N  
ANISOU 1555  N   PHE A 125     8890  18796   8218   2094   2226   -697       N  
ATOM   1556  CA  PHE A 125     -33.242  30.588   1.387  1.00 88.82           C  
ANISOU 1556  CA  PHE A 125     8223  17721   7803   2221   2210   -759       C  
ATOM   1557  C   PHE A 125     -33.293  32.098   1.581  1.00 89.13           C  
ANISOU 1557  C   PHE A 125     8353  17734   7779   2597   2173  -1115       C  
ATOM   1558  O   PHE A 125     -32.337  32.805   1.244  1.00 83.72           O  
ANISOU 1558  O   PHE A 125     7751  16811   7249   2747   2122  -1244       O  
ATOM   1559  CB  PHE A 125     -34.032  30.182   0.145  1.00 89.15           C  
ANISOU 1559  CB  PHE A 125     8214  17560   8099   2121   2239   -596       C  
ATOM   1560  CG  PHE A 125     -33.303  30.444  -1.145  1.00 88.01           C  
ANISOU 1560  CG  PHE A 125     8119  17003   8317   2135   2223   -541       C  
ATOM   1561  CD1 PHE A 125     -33.309  31.705  -1.718  1.00 86.68           C  
ANISOU 1561  CD1 PHE A 125     8017  16629   8290   2419   2201   -767       C  
ATOM   1562  CD2 PHE A 125     -32.610  29.428  -1.782  1.00 85.59           C  
ANISOU 1562  CD2 PHE A 125     7807  16486   8226   1864   2219   -257       C  
ATOM   1563  CE1 PHE A 125     -32.638  31.947  -2.903  1.00 83.52           C  
ANISOU 1563  CE1 PHE A 125     7663  15825   8245   2438   2180   -708       C  
ATOM   1564  CE2 PHE A 125     -31.937  29.664  -2.967  1.00 80.78           C  
ANISOU 1564  CE2 PHE A 125     7244  15485   7962   1885   2205   -192       C  
ATOM   1565  CZ  PHE A 125     -31.951  30.925  -3.528  1.00 80.61           C  
ANISOU 1565  CZ  PHE A 125     7276  15266   8084   2176   2189   -416       C  
ATOM   1566  H   PHE A 125     -34.440  29.396   2.418  1.00113.40           H  
ATOM   1567  HA  PHE A 125     -32.315  30.337   1.246  1.00106.58           H  
ATOM   1568  HB2 PHE A 125     -34.223  29.233   0.191  1.00106.98           H  
ATOM   1569  HB3 PHE A 125     -34.862  30.684   0.124  1.00106.98           H  
ATOM   1570  HD1 PHE A 125     -33.770  32.397  -1.302  1.00104.02           H  
ATOM   1571  HD2 PHE A 125     -32.597  28.576  -1.409  1.00102.71           H  
ATOM   1572  HE1 PHE A 125     -32.649  32.797  -3.279  1.00100.22           H  
ATOM   1573  HE2 PHE A 125     -31.475  28.973  -3.386  1.00 96.93           H  
ATOM   1574  HZ  PHE A 125     -31.499  31.086  -4.325  1.00 96.73           H  
ATOM   1575  N   HIS A 126     -34.400  32.614   2.121  1.00 97.27           N  
ANISOU 1575  N   HIS A 126     9374  18982   8603   2761   2185  -1276       N  
ATOM   1576  CA  HIS A 126     -34.519  34.058   2.290  1.00 98.43           C  
ANISOU 1576  CA  HIS A 126     9628  19069   8702   3111   2129  -1609       C  
ATOM   1577  C   HIS A 126     -33.440  34.599   3.218  1.00101.07           C  
ANISOU 1577  C   HIS A 126    10093  19438   8872   3260   2046  -1823       C  
ATOM   1578  O   HIS A 126     -32.985  35.735   3.045  1.00100.49           O  
ANISOU 1578  O   HIS A 126    10147  19142   8892   3525   1957  -2079       O  
ATOM   1579  CB  HIS A 126     -35.913  34.418   2.812  1.00100.02           C  
ANISOU 1579  CB  HIS A 126     9787  19527   8689   3237   2164  -1708       C  
ATOM   1580  CG  HIS A 126     -36.143  34.044   4.243  1.00106.40           C  
ANISOU 1580  CG  HIS A 126    10577  20714   9136   3213   2177  -1729       C  
ATOM   1581  ND1 HIS A 126     -35.838  34.887   5.289  1.00110.01           N  
ANISOU 1581  ND1 HIS A 126    11159  21288   9350   3446   2112  -1998       N  
ATOM   1582  CD2 HIS A 126     -36.654  32.921   4.801  1.00108.42           C  
ANISOU 1582  CD2 HIS A 126    10716  21235   9243   2988   2238  -1516       C  
ATOM   1583  CE1 HIS A 126     -36.148  34.299   6.431  1.00111.62           C  
ANISOU 1583  CE1 HIS A 126    11323  21822   9264   3364   2143  -1942       C  
ATOM   1584  NE2 HIS A 126     -36.645  33.105   6.163  1.00110.01           N  
ANISOU 1584  NE2 HIS A 126    10965  21714   9118   3086   2221  -1649       N  
ATOM   1585  H   HIS A 126     -35.078  32.160   2.392  1.00116.73           H  
ATOM   1586  HA  HIS A 126     -34.407  34.484   1.425  1.00118.12           H  
ATOM   1587  HB2 HIS A 126     -36.037  35.377   2.733  1.00120.02           H  
ATOM   1588  HB3 HIS A 126     -36.576  33.957   2.275  1.00120.02           H  
ATOM   1589  HD1 HIS A 126     -35.498  35.673   5.211  1.00132.01           H  
ATOM   1590  HD2 HIS A 126     -36.954  32.166   4.348  1.00130.10           H  
ATOM   1591  HE1 HIS A 126     -36.035  34.664   7.279  1.00133.94           H  
ATOM   1592  N   GLU A 127     -33.007  33.800   4.197  1.00104.82           N  
ANISOU 1592  N   GLU A 127    10556  20161   9110   3089   2055  -1726       N  
ATOM   1593  CA  GLU A 127     -31.919  34.224   5.072  1.00106.80           C  
ANISOU 1593  CA  GLU A 127    10957  20437   9185   3205   1962  -1924       C  
ATOM   1594  C   GLU A 127     -30.622  34.383   4.291  1.00101.19           C  
ANISOU 1594  C   GLU A 127    10377  19167   8906   3104   1802  -1842       C  
ATOM   1595  O   GLU A 127     -29.858  35.327   4.525  1.00103.84           O  
ANISOU 1595  O   GLU A 127    10932  19151   9373   3241   1590  -2034       O  
ATOM   1596  CB  GLU A 127     -31.740  33.218   6.209  1.00107.05           C  
ANISOU 1596  CB  GLU A 127    10967  20790   8918   2968   1982  -1773       C  
ATOM   1597  CG  GLU A 127     -32.976  33.047   7.084  1.00109.41           C  
ANISOU 1597  CG  GLU A 127    11203  21416   8951   2984   2029  -1776       C  
ATOM   1598  CD  GLU A 127     -32.827  31.939   8.113  1.00110.75           C  
ANISOU 1598  CD  GLU A 127    11334  21858   8886   2723   2049  -1586       C  
ATOM   1599  OE1 GLU A 127     -32.812  30.756   7.715  1.00108.74           O  
ANISOU 1599  OE1 GLU A 127    10955  21594   8767   2405   2104  -1269       O  
ATOM   1600  OE2 GLU A 127     -32.722  32.253   9.318  1.00114.36           O  
ANISOU 1600  OE2 GLU A 127    11903  22512   9037   2837   1994  -1753       O  
ATOM   1601  H   GLU A 127     -33.324  33.020   4.372  1.00125.79           H  
ATOM   1602  HA  GLU A 127     -32.143  35.084   5.463  1.00128.16           H  
ATOM   1603  HB2 GLU A 127     -31.524  32.352   5.828  1.00128.46           H  
ATOM   1604  HB3 GLU A 127     -31.013  33.516   6.778  1.00128.46           H  
ATOM   1605  HG2 GLU A 127     -33.143  33.876   7.559  1.00131.29           H  
ATOM   1606  HG3 GLU A 127     -33.734  32.830   6.519  1.00131.29           H  
ATOM   1607  N   PHE A 128     -30.355  33.466   3.359  1.00 92.24           N  
ANISOU 1607  N   PHE A 128     9131  17875   8040   2835   1866  -1527       N  
ATOM   1608  CA  PHE A 128     -29.168  33.581   2.519  1.00 89.14           C  
ANISOU 1608  CA  PHE A 128     8868  16884   8117   2714   1703  -1398       C  
ATOM   1609  C   PHE A 128     -29.227  34.835   1.656  1.00 89.19           C  
ANISOU 1609  C   PHE A 128     8946  16558   8384   3014   1645  -1615       C  
ATOM   1610  O   PHE A 128     -28.223  35.540   1.501  1.00 89.75           O  
ANISOU 1610  O   PHE A 128     9207  16153   8740   3060   1438  -1684       O  
ATOM   1611  CB  PHE A 128     -29.025  32.329   1.652  1.00 84.91           C  
ANISOU 1611  CB  PHE A 128     8189  16291   7783   2396   1811  -1021       C  
ATOM   1612  CG  PHE A 128     -27.987  32.450   0.573  1.00 81.78           C  
ANISOU 1612  CG  PHE A 128     7893  15300   7879   2308   1690   -873       C  
ATOM   1613  CD1 PHE A 128     -26.638  32.473   0.886  1.00 81.24           C  
ANISOU 1613  CD1 PHE A 128     8012  14835   8019   2159   1478   -795       C  
ATOM   1614  CD2 PHE A 128     -28.362  32.527  -0.759  1.00 79.81           C  
ANISOU 1614  CD2 PHE A 128     7549  14891   7885   2376   1791   -802       C  
ATOM   1615  CE1 PHE A 128     -25.683  32.579  -0.109  1.00 78.38           C  
ANISOU 1615  CE1 PHE A 128     7734  13933   8115   2085   1376   -641       C  
ATOM   1616  CE2 PHE A 128     -27.412  32.633  -1.757  1.00 75.10           C  
ANISOU 1616  CE2 PHE A 128     7047  13754   7735   2309   1691   -656       C  
ATOM   1617  CZ  PHE A 128     -26.071  32.659  -1.431  1.00 74.73           C  
ANISOU 1617  CZ  PHE A 128     7179  13320   7894   2165   1488   -571       C  
ATOM   1618  H   PHE A 128     -30.842  32.775   3.197  1.00110.69           H  
ATOM   1619  HA  PHE A 128     -28.384  33.644   3.087  1.00106.97           H  
ATOM   1620  HB2 PHE A 128     -28.777  31.583   2.220  1.00101.89           H  
ATOM   1621  HB3 PHE A 128     -29.877  32.147   1.225  1.00101.89           H  
ATOM   1622  HD1 PHE A 128     -26.372  32.420   1.775  1.00 97.48           H  
ATOM   1623  HD2 PHE A 128     -29.264  32.510  -0.984  1.00 95.77           H  
ATOM   1624  HE1 PHE A 128     -24.780  32.596   0.112  1.00 94.06           H  
ATOM   1625  HE2 PHE A 128     -27.676  32.687  -2.647  1.00 90.12           H  
ATOM   1626  HZ  PHE A 128     -25.430  32.730  -2.101  1.00 89.67           H  
ATOM   1627  N   VAL A 129     -30.400  35.135   1.090  1.00 90.01           N  
ANISOU 1627  N   VAL A 129     8895  16907   8398   3221   1824  -1721       N  
ATOM   1628  CA  VAL A 129     -30.555  36.344   0.285  1.00 91.04           C  
ANISOU 1628  CA  VAL A 129     9084  16758   8751   3523   1783  -1940       C  
ATOM   1629  C   VAL A 129     -30.375  37.584   1.147  1.00 93.79           C  
ANISOU 1629  C   VAL A 129     9625  17045   8965   3803   1618  -2292       C  
ATOM   1630  O   VAL A 129     -29.849  38.604   0.684  1.00 89.44           O  
ANISOU 1630  O   VAL A 129     9219  16072   8692   3977   1468  -2444       O  
ATOM   1631  CB  VAL A 129     -31.927  36.345  -0.422  1.00 95.04           C  
ANISOU 1631  CB  VAL A 129     9470  17392   9249   3544   1915  -1897       C  
ATOM   1632  CG1 VAL A 129     -32.088  37.590  -1.287  1.00 96.83           C  
ANISOU 1632  CG1 VAL A 129     9801  17246   9745   3774   1835  -2072       C  
ATOM   1633  CG2 VAL A 129     -32.098  35.089  -1.267  1.00 92.38           C  
ANISOU 1633  CG2 VAL A 129     9004  17020   9076   3222   2016  -1533       C  
ATOM   1634  H   VAL A 129     -31.112  34.658   1.157  1.00108.02           H  
ATOM   1635  HA  VAL A 129     -29.868  36.355  -0.400  1.00109.25           H  
ATOM   1636  HB  VAL A 129     -32.628  36.352   0.249  1.00114.05           H  
ATOM   1637 HG11 VAL A 129     -32.956  37.565  -1.718  1.00116.20           H  
ATOM   1638 HG12 VAL A 129     -32.021  38.377  -0.723  1.00116.20           H  
ATOM   1639 HG13 VAL A 129     -31.386  37.602  -1.957  1.00116.20           H  
ATOM   1640 HG21 VAL A 129     -32.966  35.115  -1.699  1.00110.86           H  
ATOM   1641 HG22 VAL A 129     -31.396  35.062  -1.936  1.00110.86           H  
ATOM   1642 HG23 VAL A 129     -32.037  34.311  -0.692  1.00110.86           H  
ATOM   1643  N   GLU A 130     -30.812  37.525   2.407  1.00102.15           N  
ANISOU 1643  N   GLU A 130    10694  18521   9598   3857   1642  -2425       N  
ATOM   1644  CA  GLU A 130     -30.617  38.651   3.314  1.00110.51           C  
ANISOU 1644  CA  GLU A 130    11957  19532  10500   4119   1473  -2759       C  
ATOM   1645  C   GLU A 130     -29.141  38.861   3.629  1.00109.02           C  
ANISOU 1645  C   GLU A 130    12006  18856  10562   3985   1190  -2727       C  
ATOM   1646  O   GLU A 130     -28.656  39.999   3.623  1.00111.54           O  
ANISOU 1646  O   GLU A 130    12509  18831  11039   4194    998  -2953       O  
ATOM   1647  CB  GLU A 130     -31.412  38.426   4.599  1.00115.66           C  
ANISOU 1647  CB  GLU A 130    12566  20756  10623   4196   1574  -2878       C  
ATOM   1648  CG  GLU A 130     -32.924  38.491   4.414  1.00118.13           C  
ANISOU 1648  CG  GLU A 130    12745  21296  10845   4221   1702  -2829       C  
ATOM   1649  CD  GLU A 130     -33.685  37.827   5.547  1.00120.08           C  
ANISOU 1649  CD  GLU A 130    12917  21994  10713   4116   1782  -2751       C  
ATOM   1650  OE1 GLU A 130     -33.135  37.742   6.667  1.00121.19           O  
ANISOU 1650  OE1 GLU A 130    13163  22300  10585   4138   1720  -2853       O  
ATOM   1651  OE2 GLU A 130     -34.832  37.388   5.316  1.00119.71           O  
ANISOU 1651  OE2 GLU A 130    12718  22118  10649   4012   1897  -2586       O  
ATOM   1652  H   GLU A 130     -31.220  36.852   2.755  1.00122.58           H  
ATOM   1653  HA  GLU A 130     -30.951  39.458   2.892  1.00132.61           H  
ATOM   1654  HB2 GLU A 130     -31.195  37.549   4.951  1.00138.79           H  
ATOM   1655  HB3 GLU A 130     -31.164  39.108   5.243  1.00138.79           H  
ATOM   1656  HG2 GLU A 130     -33.198  39.421   4.373  1.00141.76           H  
ATOM   1657  HG3 GLU A 130     -33.161  38.039   3.589  1.00141.76           H  
ATOM   1658  N   LYS A 131     -28.411  37.779   3.909  1.00100.92           N  
ANISOU 1658  N   LYS A 131    10975  17792   9580   3637   1156  -2444       N  
ATOM   1659  CA  LYS A 131     -26.981  37.899   4.174  1.00 93.01           C  
ANISOU 1659  CA  LYS A 131    10182  16321   8835   3485    890  -2381       C  
ATOM   1660  C   LYS A 131     -26.239  38.392   2.938  1.00 93.59           C  
ANISOU 1660  C   LYS A 131    10310  15818   9430   3493    786  -2306       C  
ATOM   1661  O   LYS A 131     -25.393  39.288   3.024  1.00 88.93           O  
ANISOU 1661  O   LYS A 131     9918  14811   9061   3595    549  -2441       O  
ATOM   1662  CB  LYS A 131     -26.423  36.554   4.640  1.00 87.16           C  
ANISOU 1662  CB  LYS A 131     9399  15679   8038   3101    903  -2068       C  
ATOM   1663  CG  LYS A 131     -27.041  36.044   5.933  1.00 88.09           C  
ANISOU 1663  CG  LYS A 131     9477  16347   7648   3078    990  -2125       C  
ATOM   1664  H   LYS A 131     -28.717  36.977   3.950  1.00121.11           H  
ATOM   1665  HA  LYS A 131     -26.844  38.544   4.885  1.00111.61           H  
ATOM   1666  HB2 LYS A 131     -26.589  35.891   3.952  1.00104.59           H  
ATOM   1667  HB3 LYS A 131     -25.468  36.646   4.784  1.00104.59           H  
ATOM   1668  N   LEU A 132     -26.547  37.815   1.773  1.00102.62           N  
ANISOU 1668  N   LEU A 132    11283  16928  10780   3391    956  -2087       N  
ATOM   1669  CA  LEU A 132     -25.911  38.253   0.533  1.00106.70           C  
ANISOU 1669  CA  LEU A 132    11841  16917  11785   3413    883  -2002       C  
ATOM   1670  C   LEU A 132     -26.251  39.706   0.242  1.00106.96           C  
ANISOU 1670  C   LEU A 132    11956  16793  11890   3791    815  -2334       C  
ATOM   1671  O   LEU A 132     -25.423  40.452  -0.298  1.00111.81           O  
ANISOU 1671  O   LEU A 132    12701  16903  12878   3861    642  -2363       O  
ATOM   1672  CB  LEU A 132     -26.339  37.364  -0.637  1.00 30.00           C  
ATOM   1673  H   LEU A 132     -27.114  37.176   1.677  1.00123.14           H  
ATOM   1674  HA  LEU A 132     -24.948  38.188   0.635  1.00128.04           H  
ATOM   1675  N   GLN A 133     -27.468  40.135   0.584  1.00 99.50           N  
ANISOU 1675  N   GLN A 133    10934  16274  10598   4042    950  -2581       N  
ATOM   1676  CA  GLN A 133     -27.836  41.538   0.434  1.00103.27           C  
ANISOU 1676  CA  GLN A 133    11499  16638  11099   4415    883  -2919       C  
ATOM   1677  C   GLN A 133     -27.226  42.389   1.541  1.00110.33           C  
ANISOU 1677  C   GLN A 133    12632  17401  11889   4544    630  -3170       C  
ATOM   1678  O   GLN A 133     -26.831  43.535   1.301  1.00109.62           O  
ANISOU 1678  O   GLN A 133    12689  16945  12016   4758    456  -3368       O  
ATOM   1679  CB  GLN A 133     -29.358  41.682   0.427  1.00105.78           C  
ANISOU 1679  CB  GLN A 133    11649  17466  11078   4642   1120  -3087       C  
ATOM   1680  H   GLN A 133     -28.091  39.635   0.903  1.00119.40           H  
ATOM   1681  HA  GLN A 133     -27.499  41.864  -0.415  1.00123.92           H  
ATOM   1682  N   ASP A 134     -27.142  41.843   2.757  1.00118.88           N  
ANISOU 1682  N   ASP A 134    13758  18772  12639   4419    599  -3162       N  
ATOM   1683  CA  ASP A 134     -26.503  42.561   3.856  1.00123.22           C  
ANISOU 1683  CA  ASP A 134    14548  19190  13081   4519    342  -3383       C  
ATOM   1684  C   ASP A 134     -25.038  42.840   3.543  1.00124.84           C  
ANISOU 1684  C   ASP A 134    14922  18769  13742   4381     71  -3272       C  
ATOM   1685  O   ASP A 134     -24.553  43.962   3.724  1.00125.41           O  
ANISOU 1685  O   ASP A 134    15186  18518  13948   4578   -157  -3498       O  
ATOM   1686  CB  ASP A 134     -26.632  41.757   5.150  1.00123.70           C  
ANISOU 1686  CB  ASP A 134    14612  19670  12717   4370    372  -3344       C  
ATOM   1687  CG  ASP A 134     -25.804  42.336   6.283  1.00126.72           C  
ANISOU 1687  CG  ASP A 134    15258  19875  13014   4418     85  -3522       C  
ATOM   1688  OD1 ASP A 134     -25.670  43.576   6.351  1.00128.67           O  
ANISOU 1688  OD1 ASP A 134    15673  19881  13335   4695    -90  -3806       O  
ATOM   1689  OD2 ASP A 134     -25.285  41.549   7.103  1.00128.25           O  
ANISOU 1689  OD2 ASP A 134    15494  20164  13069   4178     26  -3379       O  
ATOM   1690  H   ASP A 134     -27.445  41.066   2.968  1.00142.66           H  
ATOM   1691  HA  ASP A 134     -26.951  43.412   3.983  1.00147.87           H  
ATOM   1692  HB2 ASP A 134     -27.561  41.752   5.429  1.00148.43           H  
ATOM   1693  HB3 ASP A 134     -26.328  40.849   4.990  1.00148.43           H  
ATOM   1694  N   ILE A 135     -24.315  41.820   3.075  1.00127.22           N  
ANISOU 1694  N   ILE A 135    15154  18891  14292   4042     91  -2916       N  
ATOM   1695  CA  ILE A 135     -22.911  42.000   2.723  1.00126.14           C  
ANISOU 1695  CA  ILE A 135    15157  18162  14608   3895   -148  -2768       C  
ATOM   1696  C   ILE A 135     -22.781  42.874   1.482  1.00128.08           C  
ANISOU 1696  C   ILE A 135    15405  17992  15267   4074   -177  -2811       C  
ATOM   1697  O   ILE A 135     -21.770  43.567   1.306  1.00124.40           O  
ANISOU 1697  O   ILE A 135    15093  17023  15148   4097   -417  -2827       O  
ATOM   1698  CB  ILE A 135     -22.233  40.631   2.527  1.00121.55           C  
ANISOU 1698  CB  ILE A 135    14491  17526  14165   3493    -95  -2365       C  
ATOM   1699  CG1 ILE A 135     -22.376  39.772   3.789  1.00122.93           C  
ANISOU 1699  CG1 ILE A 135    14662  18123  13922   3319    -66  -2326       C  
ATOM   1700  CG2 ILE A 135     -20.753  40.808   2.197  1.00119.22           C  
ANISOU 1700  CG2 ILE A 135    14337  16622  14341   3342   -340  -2197       C  
ATOM   1701  CD1 ILE A 135     -22.091  38.302   3.565  1.00120.53           C  
ANISOU 1701  CD1 ILE A 135    14223  17911  13662   2945     63  -1940       C  
ATOM   1702  H   ILE A 135     -24.613  41.023   2.953  1.00152.66           H  
ATOM   1703  HA  ILE A 135     -22.461  42.453   3.453  1.00151.37           H  
ATOM   1704  HB  ILE A 135     -22.664  40.173   1.789  1.00145.85           H  
ATOM   1705 HG12 ILE A 135     -21.753  40.095   4.459  1.00147.51           H  
ATOM   1706 HG13 ILE A 135     -23.284  39.851   4.119  1.00147.51           H  
ATOM   1707 HG21 ILE A 135     -20.349  39.934   2.079  1.00143.07           H  
ATOM   1708 HG22 ILE A 135     -20.672  41.324   1.379  1.00143.07           H  
ATOM   1709 HG23 ILE A 135     -20.320  41.277   2.928  1.00143.07           H  
ATOM   1710 HD11 ILE A 135     -22.202  37.828   4.404  1.00144.64           H  
ATOM   1711 HD12 ILE A 135     -22.713  37.957   2.905  1.00144.64           H  
ATOM   1712 HD13 ILE A 135     -21.181  38.202   3.245  1.00144.64           H  
ATOM   1713  N   GLN A 136     -23.785  42.854   0.600  1.00135.55           N  
ANISOU 1713  N   GLN A 136    16178  19132  16191   4200     61  -2821       N  
ATOM   1714  CA  GLN A 136     -23.793  43.764  -0.542  1.00136.41           C  
ANISOU 1714  CA  GLN A 136    16291  18888  16651   4410     45  -2898       C  
ATOM   1715  C   GLN A 136     -23.587  45.201  -0.080  1.00135.55           C  
ANISOU 1715  C   GLN A 136    16379  18558  16564   4707   -187  -3245       C  
ATOM   1716  O   GLN A 136     -22.685  45.900  -0.555  1.00134.92           O  
ANISOU 1716  O   GLN A 136    16418  17959  16886   4747   -384  -3238       O  
ATOM   1717  CB  GLN A 136     -25.108  43.626  -1.312  1.00133.04           C  
ANISOU 1717  CB  GLN A 136    15660  18800  16090   4549    333  -2930       C  
ATOM   1718  H   GLN A 136     -24.463  42.328   0.641  1.00162.65           H  
ATOM   1719  HA  GLN A 136     -23.066  43.532  -1.140  1.00163.69           H  
ATOM   1720  N   GLN A 137     -24.420  45.657   0.850  1.00117.52           N  
ANISOU 1720  N   GLN A 137    14134  16665  13853   4924   -166  -3547       N  
ATOM   1721  CA  GLN A 137     -24.146  46.901   1.548  1.00117.84           C  
ANISOU 1721  CA  GLN A 137    14394  16527  13852   5176   -417  -3875       C  
ATOM   1722  C   GLN A 137     -22.969  46.703   2.496  1.00128.66           C  
ANISOU 1722  C   GLN A 137    15946  17677  15260   4976   -682  -3805       C  
ATOM   1723  O   GLN A 137     -22.690  45.590   2.949  1.00127.37           O  
ANISOU 1723  O   GLN A 137    15732  17685  14977   4687   -631  -3576       O  
ATOM   1724  CB  GLN A 137     -25.378  47.364   2.325  1.00122.70           C  
ANISOU 1724  CB  GLN A 137    15006  17647  13969   5463   -309  -4203       C  
ATOM   1725  H   GLN A 137     -25.147  45.266   1.091  1.00141.02           H  
ATOM   1726  HA  GLN A 137     -23.911  47.588   0.905  1.00141.40           H  
ATOM   1727  N   ARG A 138     -22.268  47.796   2.785  1.00142.95           N  
ANISOU 1727  N   ARG A 138    17971  19098  17246   5129   -974  -4002       N  
ATOM   1728  CA  ARG A 138     -21.091  47.852   3.643  1.00143.44           C  
ANISOU 1728  CA  ARG A 138    18233  18873  17393   4983  -1277  -3975       C  
ATOM   1729  C   ARG A 138     -19.824  47.450   2.895  0.50101.94           C  
ANISOU 1729  C   ARG A 138    12971  13102  12660   4705  -1391  -3634       C  
ATOM   1730  O   ARG A 138     -18.732  47.619   3.437  0.50 91.70           O  
ANISOU 1730  O   ARG A 138    11841  11473  11530   4591  -1670  -3595       O  
ATOM   1731  CB  ARG A 138     -21.210  46.971   4.903  1.00106.81           C  
ANISOU 1731  CB  ARG A 138    13614  14651  12317   4815  -1249  -3944       C  
ATOM   1732  CG  ARG A 138     -22.474  47.195   5.713  0.50 98.60           C  
ANISOU 1732  CG  ARG A 138    12564  14173  10726   5066  -1107  -4238       C  
ATOM   1733  CD  ARG A 138     -22.539  46.287   6.931  0.50 99.48           C  
ANISOU 1733  CD  ARG A 138    12692  14683  10423   4892  -1075  -4181       C  
ATOM   1734  NE  ARG A 138     -22.767  44.887   6.575  0.50 96.93           N  
ANISOU 1734  NE  ARG A 138    12143  14626  10062   4590   -819  -3843       N  
ATOM   1735  CZ  ARG A 138     -21.812  43.973   6.404  0.50 94.55           C  
ANISOU 1735  CZ  ARG A 138    11814  14104  10005   4237   -870  -3510       C  
ATOM   1736  NH1 ARG A 138     -20.531  44.287   6.552  0.50 94.31           N  
ANISOU 1736  NH1 ARG A 138    11960  13581  10291   4127  -1165  -3454       N  
ATOM   1737  NH2 ARG A 138     -22.143  42.731   6.082  0.50 92.43           N  
ANISOU 1737  NH2 ARG A 138    11340  14110   9669   3991   -626  -3226       N  
ATOM   1738  H   ARG A 138     -22.474  48.570   2.471  0.50171.54           H  
ATOM   1739  HA  ARG A 138     -20.974  48.768   3.940  0.50172.12           H  
ATOM   1740  HB2 ARG A 138     -21.195  46.040   4.633  0.50128.17           H  
ATOM   1741  HB3 ARG A 138     -20.454  47.155   5.482  0.50128.17           H  
ATOM   1742  HG2 ARG A 138     -22.497  48.115   6.020  0.50118.32           H  
ATOM   1743  HG3 ARG A 138     -23.246  47.010   5.156  0.50118.32           H  
ATOM   1744  HD2 ARG A 138     -21.699  46.342   7.413  0.50119.38           H  
ATOM   1745  HD3 ARG A 138     -23.269  46.574   7.502  0.50119.38           H  
ATOM   1746  HE  ARG A 138     -23.581  44.633   6.467  0.50116.32           H  
ATOM   1747 HH11 ARG A 138     -20.306  45.090   6.761  0.50113.17           H  
ATOM   1748 HH12 ARG A 138     -19.926  43.686   6.438  0.50113.17           H  
ATOM   1749 HH21 ARG A 138     -22.971  42.518   5.984  0.50110.91           H  
ATOM   1750 HH22 ARG A 138     -21.531  42.138   5.970  0.50110.91           H  
ATOM   1751  N   GLY A 139     -19.921  46.927   1.677  0.50 92.64           N  
ANISOU 1751  N   GLY A 139    11613  11841  11747   4599  -1191  -3381       N  
ATOM   1752  CA  GLY A 139     -18.729  46.436   0.997  0.50102.99           C  
ANISOU 1752  CA  GLY A 139    12913  12693  13526   4329  -1276  -3031       C  
ATOM   1753  C   GLY A 139     -17.958  45.430   1.821  0.50113.27           C  
ANISOU 1753  C   GLY A 139    14254  14036  14746   3999  -1360  -2809       C  
ATOM   1754  O   GLY A 139     -16.722  45.400   1.776  0.50106.65           O  
ANISOU 1754  O   GLY A 139    13509  12754  14259   3825  -1571  -2625       O  
ATOM   1755  H   GLY A 139     -20.651  46.846   1.229  0.50111.17           H  
ATOM   1756  HA2 GLY A 139     -18.984  46.016   0.161  0.50123.59           H  
ATOM   1757  HA3 GLY A 139     -18.142  47.182   0.798  0.50123.59           H  
ATOM   1758  N   GLY A 140     -18.668  44.601   2.581  1.00132.36           N  
ANISOU 1758  N   GLY A 140    16599  16982  16710   3910  -1197  -2817       N  
ATOM   1759  CA  GLY A 140     -17.996  43.668   3.468  1.00133.97           C  
ANISOU 1759  CA  GLY A 140    16848  17260  16793   3609  -1278  -2632       C  
ATOM   1760  C   GLY A 140     -17.098  42.716   2.698  1.00123.32           C  
ANISOU 1760  C   GLY A 140    15413  15622  15822   3282  -1242  -2210       C  
ATOM   1761  O   GLY A 140     -17.456  42.220   1.627  1.00120.56           O  
ANISOU 1761  O   GLY A 140    14895  15295  15617   3230  -1018  -2020       O  
ATOM   1762  H   GLY A 140     -19.527  44.560   2.599  1.00158.83           H  
ATOM   1763  HA2 GLY A 140     -17.454  44.157   4.106  1.00160.76           H  
ATOM   1764  HA3 GLY A 140     -18.654  43.148   3.955  1.00160.76           H  
ATOM   1765  N   GLU A 141     -15.913  42.461   3.257  1.00114.81           N  
ANISOU 1765  N   GLU A 141    14457  14263  14901   3063  -1469  -2060       N  
ATOM   1766  CA  GLU A 141     -14.966  41.539   2.642  1.00109.04           C  
ANISOU 1766  CA  GLU A 141    13661  13249  14519   2744  -1453  -1651       C  
ATOM   1767  C   GLU A 141     -15.426  40.089   2.714  1.00107.60           C  
ANISOU 1767  C   GLU A 141    13316  13488  14081   2489  -1197  -1413       C  
ATOM   1768  O   GLU A 141     -14.845  39.240   2.029  1.00103.78           O  
ANISOU 1768  O   GLU A 141    12748  12822  13862   2243  -1124  -1065       O  
ATOM   1769  CB  GLU A 141     -13.597  41.677   3.312  1.00111.19           C  
ANISOU 1769  CB  GLU A 141    14110  13129  15010   2583  -1776  -1565       C  
ATOM   1770  H   GLU A 141     -15.637  42.811   3.993  1.00137.77           H  
ATOM   1771  HA  GLU A 141     -14.865  41.773   1.707  1.00130.84           H  
ATOM   1772  N   GLU A 142     -16.445  39.788   3.515  1.00109.66           N  
ANISOU 1772  N   GLU A 142    13528  14298  13839   2546  -1060  -1584       N  
ATOM   1773  CA  GLU A 142     -16.922  38.419   3.646  1.00105.53           C  
ANISOU 1773  CA  GLU A 142    12845  14193  13058   2306   -824  -1363       C  
ATOM   1774  C   GLU A 142     -17.579  37.950   2.353  1.00104.16           C  
ANISOU 1774  C   GLU A 142    12472  14092  13012   2302   -551  -1195       C  
ATOM   1775  O   GLU A 142     -18.140  38.741   1.589  1.00100.91           O  
ANISOU 1775  O   GLU A 142    12025  13611  12706   2556   -487  -1351       O  
ATOM   1776  CB  GLU A 142     -17.916  38.311   4.804  1.00106.74           C  
ANISOU 1776  CB  GLU A 142    12990  14923  12645   2404   -740  -1600       C  
ATOM   1777  CG  GLU A 142     -18.391  36.891   5.093  1.00104.34           C  
ANISOU 1777  CG  GLU A 142    12525  15069  12050   2147   -516  -1375       C  
ATOM   1778  CD  GLU A 142     -19.416  36.833   6.208  1.00108.03           C  
ANISOU 1778  CD  GLU A 142    12973  16112  11960   2268   -420  -1605       C  
ATOM   1779  OE1 GLU A 142     -19.883  37.906   6.646  1.00110.48           O  
ANISOU 1779  OE1 GLU A 142    13384  16494  12100   2577   -496  -1948       O  
ATOM   1780  OE2 GLU A 142     -19.756  35.713   6.646  1.00107.53           O  
ANISOU 1780  OE2 GLU A 142    12796  16430  11631   2059   -266  -1438       O  
ATOM   1781  H   GLU A 142     -16.875  40.359   3.992  1.00131.59           H  
ATOM   1782  HA  GLU A 142     -16.171  37.835   3.835  1.00126.63           H  
ATOM   1783  HB2 GLU A 142     -17.494  38.651   5.608  1.00128.09           H  
ATOM   1784  HB3 GLU A 142     -18.697  38.846   4.593  1.00128.09           H  
ATOM   1785  HG2 GLU A 142     -18.797  36.524   4.293  1.00125.20           H  
ATOM   1786  HG3 GLU A 142     -17.630  36.351   5.357  1.00125.20           H  
ATOM   1787  N   ARG A 143     -17.504  36.642   2.114  1.00112.42           N  
ANISOU 1787  N   ARG A 143    13392  15276  14045   2009   -396   -874       N  
ATOM   1788  CA  ARG A 143     -18.127  36.021   0.956  1.00114.45           C  
ANISOU 1788  CA  ARG A 143    13462  15631  14390   1969   -138   -687       C  
ATOM   1789  C   ARG A 143     -18.822  34.740   1.393  1.00113.00           C  
ANISOU 1789  C   ARG A 143    13131  15965  13840   1762     70   -543       C  
ATOM   1790  O   ARG A 143     -18.393  34.075   2.340  1.00117.25           O  
ANISOU 1790  O   ARG A 143    13711  16635  14203   1548      3   -450       O  
ATOM   1791  CB  ARG A 143     -17.100  35.718  -0.145  1.00105.60           C  
ANISOU 1791  CB  ARG A 143    12346  14002  13775   1808   -175   -365       C  
ATOM   1792  CG  ARG A 143     -16.508  36.958  -0.801  1.00103.95           C  
ANISOU 1792  CG  ARG A 143    12249  13279  13970   2023   -343   -474       C  
ATOM   1793  CD  ARG A 143     -15.416  36.583  -1.784  1.00102.50           C  
ANISOU 1793  CD  ARG A 143    12072  12602  14273   1849   -380   -126       C  
ATOM   1794  NE  ARG A 143     -14.831  37.743  -2.457  1.00102.18           N  
ANISOU 1794  NE  ARG A 143    12124  12059  14639   2050   -533   -203       N  
ATOM   1795  CZ  ARG A 143     -13.803  38.452  -1.993  1.00102.89           C  
ANISOU 1795  CZ  ARG A 143    12373  11770  14951   2062   -811   -252       C  
ATOM   1796  NH1 ARG A 143     -13.228  38.140  -0.838  1.00104.64           N  
ANISOU 1796  NH1 ARG A 143    12688  12048  15023   1888   -973   -242       N  
ATOM   1797  NH2 ARG A 143     -13.348  39.486  -2.687  1.00101.77           N  
ANISOU 1797  NH2 ARG A 143    12296  11184  15187   2250   -932   -309       N  
ATOM   1798  H   ARG A 143     -17.088  36.086   2.621  1.00134.90           H  
ATOM   1799  HA  ARG A 143     -18.796  36.622   0.591  1.00137.34           H  
ATOM   1800  HB2 ARG A 143     -16.370  35.211   0.242  1.00126.72           H  
ATOM   1801  HB3 ARG A 143     -17.532  35.194  -0.838  1.00126.72           H  
ATOM   1802  HG2 ARG A 143     -17.205  37.431  -1.284  1.00124.74           H  
ATOM   1803  HG3 ARG A 143     -16.123  37.531  -0.119  1.00124.74           H  
ATOM   1804  HD2 ARG A 143     -14.706  36.125  -1.307  1.00123.01           H  
ATOM   1805  HD3 ARG A 143     -15.789  36.000  -2.463  1.00123.01           H  
ATOM   1806  HE  ARG A 143     -15.175  37.984  -3.206  1.00122.61           H  
ATOM   1807 HH11 ARG A 143     -13.515  37.471  -0.381  1.00125.57           H  
ATOM   1808 HH12 ARG A 143     -12.566  38.606  -0.548  1.00125.57           H  
ATOM   1809 HH21 ARG A 143     -13.716  39.696  -3.435  1.00122.12           H  
ATOM   1810 HH22 ARG A 143     -12.687  39.947  -2.388  1.00122.12           H  
ATOM   1811  N   LEU A 144     -19.904  34.405   0.695  1.00100.77           N  
ANISOU 1811  N   LEU A 144    11406  14703  12178   1827    317   -523       N  
ATOM   1812  CA  LEU A 144     -20.701  33.226   0.999  1.00 96.21           C  
ANISOU 1812  CA  LEU A 144    10664  14629  11261   1652    529   -388       C  
ATOM   1813  C   LEU A 144     -20.836  32.372  -0.254  1.00 72.91           C  
ANISOU 1813  C   LEU A 144     7569  11604   8531   1503    707    -87       C  
ATOM   1814  O   LEU A 144     -20.519  32.801  -1.366  1.00 64.38           O  
ANISOU 1814  O   LEU A 144     6507  10138   7818   1591    695    -29       O  
ATOM   1815  CB  LEU A 144     -22.086  33.611   1.534  1.00103.85           C  
ANISOU 1815  CB  LEU A 144    11544  16118  11797   1891    668   -679       C  
ATOM   1816  CG  LEU A 144     -22.089  34.521   2.765  1.00 82.90           C  
ANISOU 1816  CG  LEU A 144     9042  13572   8886   2085    505  -1008       C  
ATOM   1817  H   LEU A 144     -20.201  34.856   0.026  1.00120.92           H  
ATOM   1818  HA  LEU A 144     -20.248  32.701   1.678  1.00115.45           H  
ATOM   1819  HB2 LEU A 144     -22.570  34.072   0.831  1.00124.62           H  
ATOM   1820  HB3 LEU A 144     -22.559  32.798   1.773  1.00124.62           H  
ATOM   1821  N   TYR A 145     -21.325  31.145  -0.063  1.00 65.11           N  
ANISOU 1821  N   TYR A 145     6439  10990   7309   1279    872    108       N  
ATOM   1822  CA  TYR A 145     -21.428  30.194  -1.169  1.00 63.34           C  
ANISOU 1822  CA  TYR A 145     6088  10711   7266   1107   1030    415       C  
ATOM   1823  C   TYR A 145     -22.481  29.153  -0.785  1.00 71.64           C  
ANISOU 1823  C   TYR A 145     6956  12331   7933    976   1234    494       C  
ATOM   1824  O   TYR A 145     -22.213  28.281   0.046  1.00 93.06           O  
ANISOU 1824  O   TYR A 145     9661  15240  10458    732   1222    634       O  
ATOM   1825  CB  TYR A 145     -20.078  29.549  -1.456  1.00 64.98           C  
ANISOU 1825  CB  TYR A 145     6384  10500   7803    833    918    734       C  
ATOM   1826  CG  TYR A 145     -19.885  29.060  -2.879  1.00 62.02           C  
ANISOU 1826  CG  TYR A 145     5954   9844   7768    757   1018   1004       C  
ATOM   1827  CD1 TYR A 145     -20.970  28.805  -3.709  1.00 61.54           C  
ANISOU 1827  CD1 TYR A 145     5740  10006   7638    842   1221   1016       C  
ATOM   1828  CD2 TYR A 145     -18.609  28.855  -3.391  1.00 60.57           C  
ANISOU 1828  CD2 TYR A 145     5874   9166   7974    608    904   1253       C  
ATOM   1829  CE1 TYR A 145     -20.789  28.361  -5.007  1.00 54.67           C  
ANISOU 1829  CE1 TYR A 145     4835   8869   7068    783   1304   1258       C  
ATOM   1830  CE2 TYR A 145     -18.418  28.410  -4.686  1.00 57.79           C  
ANISOU 1830  CE2 TYR A 145     5484   8552   7921    554    997   1503       C  
ATOM   1831  CZ  TYR A 145     -19.510  28.164  -5.490  1.00 55.25           C  
ANISOU 1831  CZ  TYR A 145     5022   8455   7514    645   1194   1500       C  
ATOM   1832  OH  TYR A 145     -19.315  27.723  -6.779  1.00 54.54           O  
ANISOU 1832  OH  TYR A 145     4911   8098   7714    601   1280   1745       O  
ATOM   1833  H   TYR A 145     -21.601  30.841   0.692  1.00 78.13           H  
ATOM   1834  HA  TYR A 145     -21.726  30.655  -1.968  1.00 76.00           H  
ATOM   1835  HB2 TYR A 145     -19.382  30.198  -1.273  1.00 77.97           H  
ATOM   1836  HB3 TYR A 145     -19.972  28.785  -0.868  1.00 77.97           H  
ATOM   1837  HD1 TYR A 145     -21.833  28.936  -3.387  1.00 73.85           H  
ATOM   1838  HD2 TYR A 145     -17.869  29.019  -2.852  1.00 72.69           H  
ATOM   1839  HE1 TYR A 145     -21.524  28.194  -5.551  1.00 65.60           H  
ATOM   1840  HE2 TYR A 145     -17.558  28.278  -5.013  1.00 69.35           H  
ATOM   1841  HH  TYR A 145     -18.493  27.648  -6.936  1.00 65.45           H  
ATOM   1842  N   LEU A 146     -23.665  29.258  -1.387  1.00 74.67           N  
ANISOU 1842  N   LEU A 146     7192  12971   8209   1138   1414    409       N  
ATOM   1843  CA  LEU A 146     -24.726  28.289  -1.148  1.00 74.35           C  
ANISOU 1843  CA  LEU A 146     6957  13457   7836   1022   1612    500       C  
ATOM   1844  C   LEU A 146     -24.476  27.036  -1.976  1.00 76.40           C  
ANISOU 1844  C   LEU A 146     7134  13619   8274    735   1699    875       C  
ATOM   1845  O   LEU A 146     -24.227  27.117  -3.183  1.00 72.35           O  
ANISOU 1845  O   LEU A 146     6634  12761   8093    766   1714    989       O  
ATOM   1846  CB  LEU A 146     -26.091  28.887  -1.493  1.00 68.75           C  
ANISOU 1846  CB  LEU A 146     6115  13052   6957   1306   1765    275       C  
ATOM   1847  CG  LEU A 146     -27.322  28.031  -1.167  1.00 66.72           C  
ANISOU 1847  CG  LEU A 146     5640  13378   6332   1229   1970    334       C  
ATOM   1848  CD1 LEU A 146     -28.530  28.923  -0.905  1.00 68.11           C  
ANISOU 1848  CD1 LEU A 146     5735  13899   6245   1556   2064     16       C  
ATOM   1849  CD2 LEU A 146     -27.653  27.041  -2.281  1.00 64.25           C  
ANISOU 1849  CD2 LEU A 146     5184  13057   6170   1056   2109    624       C  
ATOM   1850  H   LEU A 146     -23.876  29.883  -1.938  1.00 89.61           H  
ATOM   1851  HA  LEU A 146     -24.729  28.040  -0.210  1.00 89.22           H  
ATOM   1852  HB2 LEU A 146     -26.186  29.722  -1.009  1.00 82.50           H  
ATOM   1853  HB3 LEU A 146     -26.110  29.065  -2.446  1.00 82.50           H  
ATOM   1854  HG  LEU A 146     -27.147  27.523  -0.360  1.00 80.06           H  
ATOM   1855 HD11 LEU A 146     -29.296  28.364  -0.702  1.00 81.73           H  
ATOM   1856 HD12 LEU A 146     -28.335  29.504  -0.154  1.00 81.73           H  
ATOM   1857 HD13 LEU A 146     -28.707  29.453  -1.698  1.00 81.73           H  
ATOM   1858 HD21 LEU A 146     -28.436  26.529  -2.025  1.00 77.10           H  
ATOM   1859 HD22 LEU A 146     -27.832  27.533  -3.097  1.00 77.10           H  
ATOM   1860 HD23 LEU A 146     -26.897  26.448  -2.411  1.00 77.10           H  
ATOM   1861  N   GLN A 147     -24.550  25.877  -1.327  1.00 77.20           N  
ANISOU 1861  N   GLN A 147     7156  14027   8149    463   1757   1067       N  
ATOM   1862  CA  GLN A 147     -24.397  24.593  -2.003  1.00 72.56           C  
ANISOU 1862  CA  GLN A 147     6486  13403   7682    178   1843   1424       C  
ATOM   1863  C   GLN A 147     -25.340  23.605  -1.336  1.00 73.78           C  
ANISOU 1863  C   GLN A 147     6564  13957   7512     27   1901   1453       C  
ATOM   1864  O   GLN A 147     -25.113  23.204  -0.191  1.00 77.92           O  
ANISOU 1864  O   GLN A 147     7091  14716   7798   -112   1868   1472       O  
ATOM   1865  CB  GLN A 147     -22.954  24.096  -1.942  1.00 69.04           C  
ANISOU 1865  CB  GLN A 147     6185  12561   7486    -72   1697   1663       C  
ATOM   1866  CG  GLN A 147     -21.961  25.015  -2.634  1.00 68.36           C  
ANISOU 1866  CG  GLN A 147     6268  11894   7813     64   1550   1624       C  
ATOM   1867  CD  GLN A 147     -20.610  24.362  -2.848  1.00 67.98           C  
ANISOU 1867  CD  GLN A 147     6330  11444   8055   -196   1443   1927       C  
ATOM   1868  OE1 GLN A 147     -20.430  23.176  -2.569  1.00 68.22           O  
ANISOU 1868  OE1 GLN A 147     6313  11621   7988   -483   1485   2175       O  
ATOM   1869  NE2 GLN A 147     -19.651  25.133  -3.351  1.00 63.52           N  
ANISOU 1869  NE2 GLN A 147     5910  10369   7854    -95   1304   1916       N  
ATOM   1870  H   GLN A 147     -24.691  25.808  -0.481  1.00 92.64           H  
ATOM   1871  HA  GLN A 147     -24.653  24.684  -2.934  1.00 87.08           H  
ATOM   1872  HB2 GLN A 147     -22.689  24.018  -1.013  1.00 82.85           H  
ATOM   1873  HB3 GLN A 147     -22.904  23.228  -2.373  1.00 82.85           H  
ATOM   1874  HG2 GLN A 147     -22.313  25.266  -3.502  1.00 82.04           H  
ATOM   1875  HG3 GLN A 147     -21.829  25.806  -2.088  1.00 82.04           H  
ATOM   1876 HE21 GLN A 147     -19.815  25.957  -3.537  1.00 76.22           H  
ATOM   1877 HE22 GLN A 147     -18.867  24.809  -3.491  1.00 76.22           H  
ATOM   1878  N   GLN A 148     -26.395  23.218  -2.046  1.00 70.23           N  
ANISOU 1878  N   GLN A 148     6132  13438   7115     60   1908   1420       N  
ATOM   1879  CA  GLN A 148     -27.398  22.320  -1.496  1.00 73.17           C  
ANISOU 1879  CA  GLN A 148     6497  14021   7281    -45   1882   1410       C  
ATOM   1880  C   GLN A 148     -27.874  21.369  -2.581  1.00 73.07           C  
ANISOU 1880  C   GLN A 148     6569  13703   7492   -150   1828   1526       C  
ATOM   1881  O   GLN A 148     -28.125  21.790  -3.714  1.00 66.97           O  
ANISOU 1881  O   GLN A 148     5815  12720   6910    -30   1858   1495       O  
ATOM   1882  CB  GLN A 148     -28.583  23.106  -0.922  1.00 78.69           C  
ANISOU 1882  CB  GLN A 148     7083  15125   7690    193   1967   1159       C  
ATOM   1883  CG  GLN A 148     -29.684  22.239  -0.340  1.00 83.51           C  
ANISOU 1883  CG  GLN A 148     7656  15963   8111    102   1947   1170       C  
ATOM   1884  CD  GLN A 148     -29.184  21.324   0.755  1.00 87.85           C  
ANISOU 1884  CD  GLN A 148     8228  16631   8521   -123   1879   1289       C  
ATOM   1885  OE1 GLN A 148     -28.275  21.676   1.506  1.00 90.58           O  
ANISOU 1885  OE1 GLN A 148     8586  17073   8758   -148   1874   1275       O  
ATOM   1886  NE2 GLN A 148     -29.771  20.137   0.847  1.00 88.26           N  
ANISOU 1886  NE2 GLN A 148     8286  16672   8577   -281   1821   1401       N  
ATOM   1887  H   GLN A 148     -26.552  23.465  -2.855  1.00 84.28           H  
ATOM   1888  HA  GLN A 148     -27.004  21.796  -0.781  1.00 87.80           H  
ATOM   1889  HB2 GLN A 148     -28.258  23.685  -0.215  1.00 94.43           H  
ATOM   1890  HB3 GLN A 148     -28.972  23.642  -1.631  1.00 94.43           H  
ATOM   1891  HG2 GLN A 148     -30.372  22.810   0.036  1.00100.21           H  
ATOM   1892  HG3 GLN A 148     -30.058  21.687  -1.045  1.00100.21           H  
ATOM   1893 HE21 GLN A 148     -30.399  19.925   0.299  1.00105.92           H  
ATOM   1894 HE22 GLN A 148     -29.523  19.580   1.453  1.00105.92           H  
ATOM   1895  N   THR A 149     -27.994  20.093  -2.230  1.00 83.76           N  
ANISOU 1895  N   THR A 149     7978  15032   8814   -354   1743   1640       N  
ATOM   1896  CA  THR A 149     -28.541  19.111  -3.154  1.00 87.37           C  
ANISOU 1896  CA  THR A 149     8514  15250   9433   -428   1685   1711       C  
ATOM   1897  C   THR A 149     -30.049  19.291  -3.271  1.00 88.28           C  
ANISOU 1897  C   THR A 149     8523  15610   9410   -302   1748   1599       C  
ATOM   1898  O   THR A 149     -30.742  19.525  -2.276  1.00 93.19           O  
ANISOU 1898  O   THR A 149     9028  16611   9768   -246   1792   1510       O  
ATOM   1899  CB  THR A 149     -28.215  17.693  -2.680  1.00 87.00           C  
ANISOU 1899  CB  THR A 149     8551  15115   9390   -644   1572   1834       C  
ATOM   1900  OG1 THR A 149     -26.805  17.574  -2.462  1.00 86.55           O  
ANISOU 1900  OG1 THR A 149     8595  14840   9449   -756   1508   1926       O  
ATOM   1901  CG2 THR A 149     -28.650  16.658  -3.714  1.00 85.34           C  
ANISOU 1901  CG2 THR A 149     8439  14633   9355   -696   1504   1885       C  
ATOM   1902  H   THR A 149     -27.766  19.772  -1.465  1.00100.51           H  
ATOM   1903  HA  THR A 149     -28.148  19.240  -4.031  1.00104.84           H  
ATOM   1904  HB  THR A 149     -28.686  17.515  -1.851  1.00104.40           H  
ATOM   1905  HG1 THR A 149     -26.619  16.797  -2.201  1.00103.85           H  
ATOM   1906 HG21 THR A 149     -28.437  15.766  -3.399  1.00102.41           H  
ATOM   1907 HG22 THR A 149     -29.606  16.720  -3.862  1.00102.41           H  
ATOM   1908 HG23 THR A 149     -28.190  16.815  -4.553  1.00102.41           H  
ATOM   1909  N   LEU A 150     -30.556  19.190  -4.496  1.00 83.96           N  
ANISOU 1909  N   LEU A 150     8020  14841   9039   -253   1746   1602       N  
ATOM   1910  CA  LEU A 150     -31.987  19.321  -4.726  1.00 87.50           C  
ANISOU 1910  CA  LEU A 150     8376  15482   9387   -145   1794   1515       C  
ATOM   1911  C   LEU A 150     -32.732  18.142  -4.116  1.00 90.88           C  
ANISOU 1911  C   LEU A 150     8769  16082   9681   -279   1739   1584       C  
ATOM   1912  O   LEU A 150     -32.312  16.988  -4.242  1.00 89.15           O  
ANISOU 1912  O   LEU A 150     8645  15667   9562   -445   1644   1705       O  
ATOM   1913  CB  LEU A 150     -32.278  19.408  -6.223  1.00 88.18           C  
ANISOU 1913  CB  LEU A 150     8532  15271   9702    -84   1792   1515       C  
ATOM   1914  CG  LEU A 150     -31.546  20.518  -6.980  1.00 87.42           C  
ANISOU 1914  CG  LEU A 150     8475  14959   9782     54   1838   1458       C  
ATOM   1915  CD1 LEU A 150     -31.937  20.506  -8.451  1.00 84.39           C  
ANISOU 1915  CD1 LEU A 150     8161  14300   9605    105   1826   1458       C  
ATOM   1916  CD2 LEU A 150     -31.824  21.881  -6.364  1.00 89.39           C  
ANISOU 1916  CD2 LEU A 150     8601  15489   9873    271   1939   1280       C  
ATOM   1917  H   LEU A 150     -30.093  19.045  -5.207  1.00100.75           H  
ATOM   1918  HA  LEU A 150     -32.306  20.135  -4.305  1.00104.99           H  
ATOM   1919  HB2 LEU A 150     -32.029  18.565  -6.632  1.00105.82           H  
ATOM   1920  HB3 LEU A 150     -33.230  19.556  -6.341  1.00105.82           H  
ATOM   1921  HG  LEU A 150     -30.591  20.356  -6.926  1.00104.91           H  
ATOM   1922 HD11 LEU A 150     -31.462  21.216  -8.910  1.00101.27           H  
ATOM   1923 HD12 LEU A 150     -31.699  19.647  -8.834  1.00101.27           H  
ATOM   1924 HD13 LEU A 150     -32.894  20.647  -8.524  1.00101.27           H  
ATOM   1925 HD21 LEU A 150     -31.346  22.558  -6.868  1.00107.26           H  
ATOM   1926 HD22 LEU A 150     -32.777  22.054  -6.398  1.00107.26           H  
ATOM   1927 HD23 LEU A 150     -31.521  21.878  -5.442  1.00107.26           H  
ATOM   1928  N   ASN A 151     -33.847  18.438  -3.452  1.00 96.64           N  
ANISOU 1928  N   ASN A 151     9359  17173  10186   -189   1797   1497       N  
ATOM   1929  CA  ASN A 151     -34.624  17.428  -2.749  1.00 97.44           C  
ANISOU 1929  CA  ASN A 151     9394  17488  10140   -296   1757   1560       C  
ATOM   1930  C   ASN A 151     -36.106  17.710  -2.982  1.00 95.91           C  
ANISOU 1930  C   ASN A 151     9086  17504   9853   -172   1814   1488       C  
ATOM   1931  O   ASN A 151     -36.480  18.515  -3.841  1.00 98.33           O  
ANISOU 1931  O   ASN A 151     9390  17726  10245    -27   1866   1403       O  
ATOM   1932  CB  ASN A 151     -34.254  17.413  -1.260  1.00 98.41           C  
ANISOU 1932  CB  ASN A 151     9456  17899  10035   -345   1761   1548       C  
ATOM   1933  CG  ASN A 151     -34.508  18.746  -0.583  1.00101.38           C  
ANISOU 1933  CG  ASN A 151     9732  18584  10202   -146   1864   1372       C  
ATOM   1934  OD1 ASN A 151     -35.645  19.078  -0.249  1.00104.86           O  
ANISOU 1934  OD1 ASN A 151    10060  19305  10478    -25   1921   1282       O  
ATOM   1935  ND2 ASN A 151     -33.445  19.515  -0.372  1.00101.09           N  
ANISOU 1935  ND2 ASN A 151     9741  18498  10172    -98   1885   1316       N  
ATOM   1936  H   ASN A 151     -34.177  19.230  -3.396  1.00115.97           H  
ATOM   1937  HA  ASN A 151     -34.421  16.554  -3.119  1.00116.93           H  
ATOM   1938  HB2 ASN A 151     -34.787  16.741  -0.807  1.00118.09           H  
ATOM   1939  HB3 ASN A 151     -33.311  17.206  -1.170  1.00118.09           H  
ATOM   1940 HD21 ASN A 151     -33.537  20.281   0.009  1.00121.31           H  
ATOM   1941 HD22 ASN A 151     -32.665  19.247  -0.615  1.00121.31           H  
ATOM   1942  N   ASP A 152     -36.959  17.041  -2.203  0.80 80.78           N  
ANISOU 1942  N   ASP A 152     7068  15859   7764   -227   1802   1525       N  
ATOM   1943  CA  ASP A 152     -38.399  17.118  -2.410  0.80 76.13           C  
ANISOU 1943  CA  ASP A 152     6355  15488   7084   -135   1838   1496       C  
ATOM   1944  C   ASP A 152     -39.017  18.391  -1.847  0.80 81.03           C  
ANISOU 1944  C   ASP A 152     6874  16391   7524     77   1950   1317       C  
ATOM   1945  O   ASP A 152     -40.146  18.727  -2.219  0.80 82.23           O  
ANISOU 1945  O   ASP A 152     6947  16653   7643    190   1995   1263       O  
ATOM   1946  CB  ASP A 152     -39.081  15.902  -1.780  0.80 80.51           C  
ANISOU 1946  CB  ASP A 152     6784  16327   7481   -266   1761   1640       C  
ATOM   1947  H   ASP A 152     -36.724  16.535  -1.548  0.80 96.93           H  
ATOM   1948  HA  ASP A 152     -38.578  17.099  -3.363  0.80 91.36           H  
ATOM   1949  N   THR A 153     -38.313  19.108  -0.974  0.80 85.84           N  
ANISOU 1949  N   THR A 153     7480  17136   8001    144   1987   1222       N  
ATOM   1950  CA  THR A 153     -38.875  20.284  -0.319  0.80 90.13           C  
ANISOU 1950  CA  THR A 153     7929  17982   8334    367   2079   1035       C  
ATOM   1951  C   THR A 153     -38.944  21.502  -1.231  0.80 88.34           C  
ANISOU 1951  C   THR A 153     7736  17611   8218    573   2132    886       C  
ATOM   1952  O   THR A 153     -39.276  22.592  -0.754  0.80 85.13           O  
ANISOU 1952  O   THR A 153     7281  17408   7656    786   2198    701       O  
ATOM   1953  CB  THR A 153     -38.057  20.641   0.926  0.80 96.29           C  
ANISOU 1953  CB  THR A 153     8710  18953   8924    384   2093    966       C  
ATOM   1954  OG1 THR A 153     -36.758  21.099   0.533  0.80 94.65           O  
ANISOU 1954  OG1 THR A 153     8615  18493   8855    380   2076    946       O  
ATOM   1955  CG2 THR A 153     -37.914  19.440   1.843  0.80 98.66           C  
ANISOU 1955  CG2 THR A 153     8984  19375   9126    176   2036   1113       C  
ATOM   1956  H   THR A 153     -37.503  18.933  -0.745  0.80103.01           H  
ATOM   1957  HA  THR A 153     -39.778  20.078  -0.031  0.80108.16           H  
ATOM   1958  HB  THR A 153     -38.510  21.345   1.416  0.80115.55           H  
ATOM   1959  HG1 THR A 153     -36.358  20.496   0.105  0.80113.58           H  
ATOM   1960 HG21 THR A 153     -37.395  19.681   2.626  0.80118.39           H  
ATOM   1961 HG22 THR A 153     -38.789  19.134   2.127  0.80118.39           H  
ATOM   1962 HG23 THR A 153     -37.464  18.718   1.376  0.80118.39           H  
ATOM   1963  N   VAL A 154     -38.642  21.350  -2.515  1.00 90.57           N  
ANISOU 1963  N   VAL A 154     8109  17541   8762    525   2101    951       N  
ATOM   1964  CA  VAL A 154     -38.638  22.479  -3.438  1.00 86.65           C  
ANISOU 1964  CA  VAL A 154     7652  16873   8398    714   2145    816       C  
ATOM   1965  C   VAL A 154     -40.059  22.768  -3.902  1.00 87.84           C  
ANISOU 1965  C   VAL A 154     7724  17128   8522    834   2184    753       C  
ATOM   1966  O   VAL A 154     -40.901  21.869  -4.007  1.00 85.55           O  
ANISOU 1966  O   VAL A 154     7379  16909   8215    724   2159    868       O  
ATOM   1967  CB  VAL A 154     -37.699  22.205  -4.629  1.00 82.44           C  
ANISOU 1967  CB  VAL A 154     7251  15912   8161    618   2098    916       C  
ATOM   1968  CG1 VAL A 154     -36.261  22.084  -4.152  1.00 81.23           C  
ANISOU 1968  CG1 VAL A 154     7170  15658   8037    522   2067    970       C  
ATOM   1969  CG2 VAL A 154     -38.122  20.951  -5.382  1.00 79.05           C  
ANISOU 1969  CG2 VAL A 154     6856  15315   7864    437   2033   1089       C  
ATOM   1970  H   VAL A 154     -38.434  20.599  -2.879  1.00108.68           H  
ATOM   1971  HA  VAL A 154     -38.310  23.265  -2.973  1.00103.98           H  
ATOM   1972  HB  VAL A 154     -37.746  22.953  -5.245  1.00 98.93           H  
ATOM   1973 HG11 VAL A 154     -35.689  21.912  -4.916  1.00 97.48           H  
ATOM   1974 HG12 VAL A 154     -36.001  22.914  -3.723  1.00 97.48           H  
ATOM   1975 HG13 VAL A 154     -36.199  21.351  -3.520  1.00 97.48           H  
ATOM   1976 HG21 VAL A 154     -37.512  20.807  -6.123  1.00 94.86           H  
ATOM   1977 HG22 VAL A 154     -38.091  20.194  -4.777  1.00 94.86           H  
ATOM   1978 HG23 VAL A 154     -39.025  21.073  -5.715  1.00 94.86           H  
ATOM   1979  N   GLY A 155     -40.324  24.038  -4.194  1.00 89.46           N  
ANISOU 1979  N   GLY A 155     7927  17333   8731   1064   2240    567       N  
ATOM   1980  CA  GLY A 155     -41.655  24.477  -4.554  1.00 90.35           C  
ANISOU 1980  CA  GLY A 155     7967  17556   8807   1199   2280    487       C  
ATOM   1981  C   GLY A 155     -42.116  23.933  -5.895  1.00 88.36           C  
ANISOU 1981  C   GLY A 155     7749  17050   8774   1111   2251    597       C  
ATOM   1982  O   GLY A 155     -41.387  23.271  -6.634  1.00 87.73           O  
ANISOU 1982  O   GLY A 155     7764  16681   8888    964   2198    723       O  
ATOM   1983  H   GLY A 155     -39.738  24.667  -4.188  1.00107.35           H  
ATOM   1984  HA2 GLY A 155     -42.284  24.189  -3.874  1.00108.42           H  
ATOM   1985  HA3 GLY A 155     -41.673  25.446  -4.596  1.00108.42           H  
ATOM   1986  N   ARG A 156     -43.375  24.243  -6.213  1.00 85.37           N  
ANISOU 1986  N   ARG A 156     6112  17881   8445   1219    910   2005       N  
ATOM   1987  CA  ARG A 156     -44.001  23.690  -7.410  1.00 83.37           C  
ANISOU 1987  CA  ARG A 156     5845  17514   8320   1025    862   2173       C  
ATOM   1988  C   ARG A 156     -43.276  24.141  -8.673  1.00 78.63           C  
ANISOU 1988  C   ARG A 156     5415  16446   8014   1083    852   2050       C  
ATOM   1989  O   ARG A 156     -42.908  23.318  -9.518  1.00 76.05           O  
ANISOU 1989  O   ARG A 156     5165  15857   7872    833    797   2200       O  
ATOM   1990  CB  ARG A 156     -45.476  24.094  -7.462  1.00 81.83           C  
ANISOU 1990  CB  ARG A 156     5473  17690   7927   1155    868   2175       C  
ATOM   1991  H   ARG A 156     -43.882  24.767  -5.757  1.00102.45           H  
ATOM   1992  HA  ARG A 156     -43.957  22.721  -7.370  1.00100.05           H  
ATOM   1993  N   LYS A 157     -43.062  25.451  -8.818  1.00 78.30           N  
ANISOU 1993  N   LYS A 157     5433  16297   8019   1418    885   1780       N  
ATOM   1994  CA  LYS A 157     -42.459  25.964 -10.044  1.00 78.80           C  
ANISOU 1994  CA  LYS A 157     5640  15949   8351   1487    862   1686       C  
ATOM   1995  C   LYS A 157     -41.054  25.412 -10.257  1.00 75.88           C  
ANISOU 1995  C   LYS A 157     5421  15232   8177   1313    844   1737       C  
ATOM   1996  O   LYS A 157     -40.632  25.223 -11.404  1.00 72.85           O  
ANISOU 1996  O   LYS A 157     5131  14549   8000   1219    804   1786       O  
ATOM   1997  CB  LYS A 157     -42.430  27.494 -10.018  1.00 79.28           C  
ANISOU 1997  CB  LYS A 157     5742  15949   8431   1884    871   1396       C  
ATOM   1998  CG  LYS A 157     -43.775  28.147 -10.290  1.00 81.57           C  
ANISOU 1998  CG  LYS A 157     5917  16474   8601   2077    865   1331       C  
ATOM   1999  CD  LYS A 157     -43.637  29.654 -10.445  1.00 83.58           C  
ANISOU 1999  CD  LYS A 157     6250  16569   8938   2465    834   1046       C  
ATOM   2000  H   LYS A 157     -43.253  26.051  -8.233  1.00 93.96           H  
ATOM   2001  HA  LYS A 157     -43.003  25.690 -10.799  1.00 94.56           H  
ATOM   2002  HB2 LYS A 157     -42.132  27.785  -9.143  1.00 95.13           H  
ATOM   2003  HB3 LYS A 157     -41.809  27.805 -10.696  1.00 95.13           H  
ATOM   2004  HG2 LYS A 157     -44.145  27.789 -11.111  1.00 97.88           H  
ATOM   2005  HG3 LYS A 157     -44.372  27.971  -9.546  1.00 97.88           H  
ATOM   2006  N   ILE A 158     -40.320  25.141  -9.176  1.00 76.15           N  
ANISOU 2006  N   ILE A 158     5477  15320   8138   1275    870   1728       N  
ATOM   2007  CA  ILE A 158     -38.953  24.646  -9.313  1.00 77.51           C  
ANISOU 2007  CA  ILE A 158     5789  15179   8483   1125    854   1768       C  
ATOM   2008  C   ILE A 158     -38.959  23.197  -9.783  1.00 76.25           C  
ANISOU 2008  C   ILE A 158     5635  14949   8388    756    792   2033       C  
ATOM   2009  O   ILE A 158     -38.070  22.770 -10.529  1.00 72.22           O  
ANISOU 2009  O   ILE A 158     5243  14126   8072    628    748   2078       O  
ATOM   2010  CB  ILE A 158     -38.188  24.807  -7.986  1.00 73.99           C  
ANISOU 2010  CB  ILE A 158     5361  14824   7929   1204    895   1672       C  
ATOM   2011  CG1 ILE A 158     -38.181  26.272  -7.536  1.00 75.88           C  
ANISOU 2011  CG1 ILE A 158     5606  15108   8117   1593    921   1376       C  
ATOM   2012  CG2 ILE A 158     -36.771  24.298  -8.121  1.00 73.02           C  
ANISOU 2012  CG2 ILE A 158     5377  14391   7976   1052    878   1715       C  
ATOM   2013  CD1 ILE A 158     -37.577  27.251  -8.535  1.00 72.82           C  
ANISOU 2013  CD1 ILE A 158     5342  14354   7972   1781    886   1222       C  
ATOM   2014  H   ILE A 158     -40.587  25.235  -8.364  1.00 91.38           H  
ATOM   2015  HA  ILE A 158     -38.495  25.174  -9.986  1.00 93.02           H  
ATOM   2016  HB  ILE A 158     -38.639  24.281  -7.307  1.00 88.79           H  
ATOM   2017 HG12 ILE A 158     -39.097  26.549  -7.372  1.00 91.06           H  
ATOM   2018 HG13 ILE A 158     -37.670  26.340  -6.714  1.00 91.06           H  
ATOM   2019 HG21 ILE A 158     -36.313  24.411  -7.273  1.00 87.62           H  
ATOM   2020 HG22 ILE A 158     -36.795  23.358  -8.362  1.00 87.62           H  
ATOM   2021 HG23 ILE A 158     -36.318  24.805  -8.812  1.00 87.62           H  
ATOM   2022 HD11 ILE A 158     -37.618  28.146  -8.163  1.00 87.38           H  
ATOM   2023 HD12 ILE A 158     -36.655  27.003  -8.701  1.00 87.38           H  
ATOM   2024 HD13 ILE A 158     -38.085  27.212  -9.361  1.00 87.38           H  
ATOM   2025  N   VAL A 159     -39.945  22.412  -9.343  1.00 76.06           N  
ANISOU 2025  N   VAL A 159     5480  15218   8201    585    768   2215       N  
ATOM   2026  CA  VAL A 159     -40.080  21.046  -9.839  1.00 76.91           C  
ANISOU 2026  CA  VAL A 159     5590  15245   8388    240    671   2468       C  
ATOM   2027  C   VAL A 159     -40.408  21.055 -11.325  1.00 78.88           C  
ANISOU 2027  C   VAL A 159     5873  15295   8804    214    618   2475       C  
ATOM   2028  O   VAL A 159     -39.896  20.233 -12.094  1.00 75.27           O  
ANISOU 2028  O   VAL A 159     5499  14585   8515     12    530   2576       O  
ATOM   2029  CB  VAL A 159     -41.145  20.283  -9.029  1.00 83.18           C  
ANISOU 2029  CB  VAL A 159     6221  16414   8969     70    638   2678       C  
ATOM   2030  CG1 VAL A 159     -41.345  18.877  -9.588  1.00 82.90           C  
ANISOU 2030  CG1 VAL A 159     6191  16266   9039   -290    502   2943       C  
ATOM   2031  CG2 VAL A 159     -40.749  20.206  -7.565  1.00 82.66           C  
ANISOU 2031  CG2 VAL A 159     6122  16556   8730     87    679   2687       C  
ATOM   2032  H   VAL A 159     -40.539  22.644  -8.765  1.00 91.27           H  
ATOM   2033  HA  VAL A 159     -39.234  20.586  -9.724  1.00 92.29           H  
ATOM   2034  HB  VAL A 159     -41.990  20.756  -9.090  1.00 99.82           H  
ATOM   2035 HG11 VAL A 159     -42.019  18.421  -9.061  1.00 99.48           H  
ATOM   2036 HG12 VAL A 159     -41.635  18.944 -10.512  1.00 99.48           H  
ATOM   2037 HG13 VAL A 159     -40.504  18.396  -9.539  1.00 99.48           H  
ATOM   2038 HG21 VAL A 159     -41.435  19.722  -7.078  1.00 99.19           H  
ATOM   2039 HG22 VAL A 159     -39.901  19.742  -7.492  1.00 99.19           H  
ATOM   2040 HG23 VAL A 159     -40.666  21.106  -7.213  1.00 99.19           H  
ATOM   2041  N   MET A 160     -41.277  21.973 -11.753  1.00 84.42           N  
ANISOU 2041  N   MET A 160     6505  16116   9453    428    660   2363       N  
ATOM   2042  CA  MET A 160     -41.590  22.086 -13.173  1.00 84.84           C  
ANISOU 2042  CA  MET A 160     6589  15995   9653    431    613   2359       C  
ATOM   2043  C   MET A 160     -40.345  22.419 -13.984  1.00 74.96           C  
ANISOU 2043  C   MET A 160     5502  14361   8619    496    600   2254       C  
ATOM   2044  O   MET A 160     -40.106  21.822 -15.040  1.00 73.92           O  
ANISOU 2044  O   MET A 160     5427  14026   8632    353    520   2330       O  
ATOM   2045  CB  MET A 160     -42.670  23.144 -13.385  1.00 87.50           C  
ANISOU 2045  CB  MET A 160     6829  16528   9890    683    662   2242       C  
ATOM   2046  CG  MET A 160     -44.024  22.767 -12.796  1.00 94.18           C  
ANISOU 2046  CG  MET A 160     7492  17781  10512    611    662   2368       C  
ATOM   2047  SD  MET A 160     -44.828  21.403 -13.658  1.00 98.84           S  
ANISOU 2047  SD  MET A 160     8014  18390  11151    258    544   2638       S  
ATOM   2048  CE  MET A 160     -45.214  22.177 -15.226  1.00 93.63           C  
ANISOU 2048  CE  MET A 160     7389  17558  10628    426    534   2518       C  
ATOM   2049  H   MET A 160     -41.692  22.533 -11.249  1.00101.30           H  
ATOM   2050  HA  MET A 160     -41.943  21.237 -13.482  1.00101.81           H  
ATOM   2051  HB2 MET A 160     -42.384  23.971 -12.967  1.00105.00           H  
ATOM   2052  HB3 MET A 160     -42.790  23.282 -14.338  1.00105.00           H  
ATOM   2053  HG2 MET A 160     -43.901  22.503 -11.871  1.00113.02           H  
ATOM   2054  HG3 MET A 160     -44.612  23.537 -12.844  1.00113.02           H  
ATOM   2055  HE1 MET A 160     -45.660  21.531 -15.795  1.00112.35           H  
ATOM   2056  HE2 MET A 160     -45.795  22.937 -15.068  1.00112.35           H  
ATOM   2057  HE3 MET A 160     -44.389  22.472 -15.643  1.00112.35           H  
ATOM   2058  N   ASP A 161     -39.537  23.368 -13.507  1.00 64.03           N  
ANISOU 2058  N   ASP A 161     4188  12887   7254    716    665   2081       N  
ATOM   2059  CA  ASP A 161     -38.274  23.660 -14.177  1.00 67.63           C  
ANISOU 2059  CA  ASP A 161     4791  13000   7904    764    647   2010       C  
ATOM   2060  C   ASP A 161     -37.375  22.434 -14.181  1.00 61.07           C  
ANISOU 2060  C   ASP A 161     4033  12017   7155    496    587   2143       C  
ATOM   2061  O   ASP A 161     -36.793  22.075 -15.211  1.00 58.45           O  
ANISOU 2061  O   ASP A 161     3843  11399   6968    413    510   2156       O  
ATOM   2062  CB  ASP A 161     -37.574  24.833 -13.492  1.00 65.18           C  
ANISOU 2062  CB  ASP A 161     4532  12638   7596   1029    709   1818       C  
ATOM   2063  CG  ASP A 161     -38.439  26.070 -13.430  1.00 71.25           C  
ANISOU 2063  CG  ASP A 161     5237  13539   8294   1322    737   1664       C  
ATOM   2064  OD1 ASP A 161     -39.330  26.216 -14.294  1.00 68.12           O  
ANISOU 2064  OD1 ASP A 161     4795  13180   7910   1344    713   1696       O  
ATOM   2065  OD2 ASP A 161     -38.228  26.896 -12.519  1.00 71.86           O  
ANISOU 2065  OD2 ASP A 161     5313  13684   8306   1539    771   1501       O  
ATOM   2066  H   ASP A 161     -39.695  23.847 -12.810  1.00 76.83           H  
ATOM   2067  HA  ASP A 161     -38.452  23.909 -15.097  1.00 81.15           H  
ATOM   2068  HB2 ASP A 161     -37.346  24.579 -12.584  1.00 78.22           H  
ATOM   2069  HB3 ASP A 161     -36.769  25.054 -13.987  1.00 78.22           H  
ATOM   2070  N   PHE A 162     -37.257  21.773 -13.029  1.00 64.04           N  
ANISOU 2070  N   PHE A 162     4376  12533   7422    361    599   2220       N  
ATOM   2071  CA  PHE A 162     -36.440  20.570 -12.930  1.00 65.49           C  
ANISOU 2071  CA  PHE A 162     4653  12550   7679    104    517   2345       C  
ATOM   2072  C   PHE A 162     -36.870  19.537 -13.962  1.00 62.37           C  
ANISOU 2072  C   PHE A 162     4252  12066   7379   -118    388   2494       C  
ATOM   2073  O   PHE A 162     -36.038  18.964 -14.673  1.00 64.26           O  
ANISOU 2073  O   PHE A 162     4685  11978   7754   -208    284   2477       O  
ATOM   2074  CB  PHE A 162     -36.541  20.001 -11.514  1.00 67.86           C  
ANISOU 2074  CB  PHE A 162     4871  13090   7824    -17    541   2450       C  
ATOM   2075  CG  PHE A 162     -35.610  18.854 -11.251  1.00 68.60           C  
ANISOU 2075  CG  PHE A 162     5083  12989   7992   -257    448   2567       C  
ATOM   2076  CD1 PHE A 162     -34.293  19.083 -10.886  1.00 64.07           C  
ANISOU 2076  CD1 PHE A 162     4714  12163   7467   -184    460   2433       C  
ATOM   2077  CD2 PHE A 162     -36.054  17.546 -11.355  1.00 71.32           C  
ANISOU 2077  CD2 PHE A 162     5367  13370   8360   -555    321   2800       C  
ATOM   2078  CE1 PHE A 162     -33.435  18.029 -10.636  1.00 66.96           C  
ANISOU 2078  CE1 PHE A 162     5219  12329   7894   -381    360   2520       C  
ATOM   2079  CE2 PHE A 162     -35.201  16.486 -11.106  1.00 69.55           C  
ANISOU 2079  CE2 PHE A 162     5298  12915   8214   -757    199   2888       C  
ATOM   2080  CZ  PHE A 162     -33.890  16.728 -10.746  1.00 67.12           C  
ANISOU 2080  CZ  PHE A 162     5190  12369   7942   -659    225   2743       C  
ATOM   2081  H   PHE A 162     -37.639  22.002 -12.293  1.00 76.84           H  
ATOM   2082  HA  PHE A 162     -35.513  20.800 -13.100  1.00 78.58           H  
ATOM   2083  HB2 PHE A 162     -36.331  20.704 -10.880  1.00 81.43           H  
ATOM   2084  HB3 PHE A 162     -37.446  19.687 -11.368  1.00 81.43           H  
ATOM   2085  HD1 PHE A 162     -33.983  19.957 -10.810  1.00 76.89           H  
ATOM   2086  HD2 PHE A 162     -36.937  17.378 -11.596  1.00 85.58           H  
ATOM   2087  HE1 PHE A 162     -32.552  18.194 -10.394  1.00 80.35           H  
ATOM   2088  HE2 PHE A 162     -35.509  15.612 -11.181  1.00 83.46           H  
ATOM   2089  HZ  PHE A 162     -33.314  16.018 -10.579  1.00 80.54           H  
ATOM   2090  N   LEU A 163     -38.175  19.289 -14.061  1.00 64.86           N  
ANISOU 2090  N   LEU A 163     4421  12617   7607   -190    367   2600       N  
ATOM   2091  CA  LEU A 163     -38.671  18.352 -15.058  1.00 64.23           C  
ANISOU 2091  CA  LEU A 163     4322  12463   7621   -394    226   2731       C  
ATOM   2092  C   LEU A 163     -38.407  18.841 -16.475  1.00 58.44           C  
ANISOU 2092  C   LEU A 163     3649  11529   7026   -262    203   2620       C  
ATOM   2093  O   LEU A 163     -38.269  18.017 -17.385  1.00 60.03           O  
ANISOU 2093  O   LEU A 163     3938  11533   7337   -404     58   2661       O  
ATOM   2094  CB  LEU A 163     -40.166  18.112 -14.843  1.00 68.14           C  
ANISOU 2094  CB  LEU A 163     4666  13249   7976   -478    211   2854       C  
ATOM   2095  CG  LEU A 163     -40.514  17.359 -13.557  1.00 68.56           C  
ANISOU 2095  CG  LEU A 163     4645  13519   7887   -667    190   3030       C  
ATOM   2096  CD1 LEU A 163     -42.006  17.425 -13.287  1.00 71.00           C  
ANISOU 2096  CD1 LEU A 163     4783  14175   8018   -679    206   3127       C  
ATOM   2097  CD2 LEU A 163     -40.053  15.913 -13.639  1.00 66.13           C  
ANISOU 2097  CD2 LEU A 163     4400  13021   7706   -992      9   3218       C  
ATOM   2098  H   LEU A 163     -38.784  19.645 -13.568  1.00 77.83           H  
ATOM   2099  HA  LEU A 163     -38.214  17.504 -14.946  1.00 77.08           H  
ATOM   2100  HB2 LEU A 163     -40.617  18.970 -14.812  1.00 81.77           H  
ATOM   2101  HB3 LEU A 163     -40.507  17.592 -15.588  1.00 81.77           H  
ATOM   2102  HG  LEU A 163     -40.055  17.778 -12.812  1.00 82.27           H  
ATOM   2103 HD11 LEU A 163     -42.200  16.942 -12.469  1.00 85.20           H  
ATOM   2104 HD12 LEU A 163     -42.269  18.354 -13.194  1.00 85.20           H  
ATOM   2105 HD13 LEU A 163     -42.479  17.020 -14.031  1.00 85.20           H  
ATOM   2106 HD21 LEU A 163     -40.285  15.461 -12.813  1.00 79.36           H  
ATOM   2107 HD22 LEU A 163     -40.495  15.484 -14.388  1.00 79.36           H  
ATOM   2108 HD23 LEU A 163     -39.092  15.896 -13.768  1.00 79.36           H  
ATOM   2109  N   GLY A 164     -38.309  20.153 -16.677  1.00 58.26           N  
ANISOU 2109  N   GLY A 164     3650  11496   6990     17    316   2456       N  
ATOM   2110  CA  GLY A 164     -38.021  20.702 -17.983  1.00 59.02           C  
ANISOU 2110  CA  GLY A 164     3853  11376   7198    151    290   2353       C  
ATOM   2111  C   GLY A 164     -36.586  20.578 -18.438  1.00 55.55           C  
ANISOU 2111  C   GLY A 164     3664  10572   6871    156    240   2263       C  
ATOM   2112  O   GLY A 164     -36.255  21.032 -19.537  1.00 58.82           O  
ANISOU 2112  O   GLY A 164     4164  10824   7360    264    218   2193       O  
ATOM   2113  H   GLY A 164     -38.407  20.746 -16.062  1.00 69.91           H  
ATOM   2114  HA2 GLY A 164     -38.580  20.258 -18.640  1.00 70.83           H  
ATOM   2115  HA3 GLY A 164     -38.252  21.645 -17.984  1.00 70.83           H  
ATOM   2116  N   PHE A 165     -35.712  19.988 -17.628  1.00 50.81           N  
ANISOU 2116  N   PHE A 165     3170   9863   6272     48    221   2271       N  
ATOM   2117  CA  PHE A 165     -34.344  19.758 -18.061  1.00 50.61           C  
ANISOU 2117  CA  PHE A 165     3365   9524   6340     48    164   2191       C  
ATOM   2118  C   PHE A 165     -34.322  18.745 -19.202  1.00 50.20           C  
ANISOU 2118  C   PHE A 165     3373   9339   6363    -75      7   2227       C  
ATOM   2119  O   PHE A 165     -35.267  17.978 -19.407  1.00 48.80           O  
ANISOU 2119  O   PHE A 165     3088   9275   6179   -222    -83   2334       O  
ATOM   2120  CB  PHE A 165     -33.482  19.261 -16.898  1.00 53.39           C  
ANISOU 2120  CB  PHE A 165     3804   9811   6669    -43    165   2198       C  
ATOM   2121  CG  PHE A 165     -33.257  20.284 -15.812  1.00 54.01           C  
ANISOU 2121  CG  PHE A 165     3860   9986   6677    106    302   2119       C  
ATOM   2122  CD1 PHE A 165     -33.771  21.569 -15.913  1.00 52.90           C  
ANISOU 2122  CD1 PHE A 165     3641   9947   6511    320    395   2033       C  
ATOM   2123  CD2 PHE A 165     -32.519  19.953 -14.687  1.00 49.41           C  
ANISOU 2123  CD2 PHE A 165     3340   9380   6054     44    316   2118       C  
ATOM   2124  CE1 PHE A 165     -33.558  22.497 -14.912  1.00 48.63           C  
ANISOU 2124  CE1 PHE A 165     3093   9475   5912    477    486   1930       C  
ATOM   2125  CE2 PHE A 165     -32.302  20.877 -13.685  1.00 49.03           C  
ANISOU 2125  CE2 PHE A 165     3272   9423   5933    193    424   2023       C  
ATOM   2126  CZ  PHE A 165     -32.823  22.151 -13.799  1.00 53.28           C  
ANISOU 2126  CZ  PHE A 165     3739  10052   6451    414    502   1919       C  
ATOM   2127  H   PHE A 165     -35.886  19.715 -16.831  1.00 60.97           H  
ATOM   2128  HA  PHE A 165     -33.967  20.590 -18.386  1.00 60.73           H  
ATOM   2129  HB2 PHE A 165     -33.916  18.493 -16.495  1.00 64.06           H  
ATOM   2130  HB3 PHE A 165     -32.613  19.001 -17.244  1.00 64.06           H  
ATOM   2131  HD1 PHE A 165     -34.269  21.807 -16.662  1.00 63.48           H  
ATOM   2132  HD2 PHE A 165     -32.166  19.097 -14.605  1.00 59.29           H  
ATOM   2133  HE1 PHE A 165     -33.909  23.355 -14.990  1.00 58.36           H  
ATOM   2134  HE2 PHE A 165     -31.806  20.642 -12.934  1.00 58.83           H  
ATOM   2135  HZ  PHE A 165     -32.678  22.775 -13.125  1.00 63.93           H  
ATOM   2136  N   ASN A 166     -33.223  18.752 -19.958  1.00 50.99           N  
ANISOU 2136  N   ASN A 166     3637   9209   6527     -7    -37   2132       N  
ATOM   2137  CA  ASN A 166     -33.083  17.860 -21.109  1.00 49.29           C  
ANISOU 2137  CA  ASN A 166     3488   8874   6365    -68   -196   2120       C  
ATOM   2138  C   ASN A 166     -32.594  16.496 -20.624  1.00 51.07           C  
ANISOU 2138  C   ASN A 166     3813   8967   6623   -249   -345   2153       C  
ATOM   2139  O   ASN A 166     -31.446  16.090 -20.819  1.00 52.77           O  
ANISOU 2139  O   ASN A 166     4183   8996   6869   -222   -413   2069       O  
ATOM   2140  CB  ASN A 166     -32.144  18.453 -22.148  1.00 47.94           C  
ANISOU 2140  CB  ASN A 166     3420   8577   6218    100   -181   2012       C  
ATOM   2141  CG  ASN A 166     -32.180  17.695 -23.459  1.00 50.00           C  
ANISOU 2141  CG  ASN A 166     3712   8787   6500     91   -335   1977       C  
ATOM   2142  OD1 ASN A 166     -32.722  16.591 -23.538  1.00 46.14           O  
ANISOU 2142  OD1 ASN A 166     3210   8287   6033    -54   -486   2014       O  
ATOM   2143  ND2 ASN A 166     -31.597  18.282 -24.497  1.00 44.43           N  
ANISOU 2143  ND2 ASN A 166     3041   8057   5785    245   -314   1911       N  
ATOM   2144  H   ASN A 166     -32.545  19.264 -19.826  1.00 61.18           H  
ATOM   2145  HA  ASN A 166     -33.952  17.738 -21.524  1.00 59.14           H  
ATOM   2146  HB2 ASN A 166     -32.404  19.371 -22.324  1.00 57.53           H  
ATOM   2147  HB3 ASN A 166     -31.236  18.423 -21.808  1.00 57.53           H  
ATOM   2148 HD21 ASN A 166     -31.590  17.893 -25.264  1.00 53.32           H  
ATOM   2149 HD22 ASN A 166     -31.227  19.053 -24.403  1.00 53.32           H  
ATOM   2150  N   TRP A 167     -33.508  15.779 -19.971  1.00 55.41           N  
ANISOU 2150  N   TRP A 167     4260   9632   7162   -439   -408   2290       N  
ATOM   2151  CA  TRP A 167     -33.185  14.449 -19.476  1.00 54.57           C  
ANISOU 2151  CA  TRP A 167     4241   9389   7103   -639   -582   2359       C  
ATOM   2152  C   TRP A 167     -32.959  13.470 -20.620  1.00 56.10           C  
ANISOU 2152  C   TRP A 167     4549   9382   7384   -673   -812   2293       C  
ATOM   2153  O   TRP A 167     -32.204  12.504 -20.467  1.00 56.27           O  
ANISOU 2153  O   TRP A 167     4719   9199   7463   -746   -975   2267       O  
ATOM   2154  CB  TRP A 167     -34.298  13.961 -18.552  1.00 53.30           C  
ANISOU 2154  CB  TRP A 167     3913   9431   6907   -857   -605   2565       C  
ATOM   2155  CG  TRP A 167     -34.487  14.855 -17.364  1.00 54.16           C  
ANISOU 2155  CG  TRP A 167     3903   9775   6902   -797   -392   2607       C  
ATOM   2156  CD1 TRP A 167     -35.487  15.764 -17.169  1.00 58.36           C  
ANISOU 2156  CD1 TRP A 167     4237  10598   7341   -711   -242   2639       C  
ATOM   2157  CD2 TRP A 167     -33.640  14.938 -16.211  1.00 53.51           C  
ANISOU 2157  CD2 TRP A 167     3889   9666   6776   -789   -318   2599       C  
ATOM   2158  NE1 TRP A 167     -35.318  16.402 -15.963  1.00 58.74           N  
ANISOU 2158  NE1 TRP A 167     4229  10805   7286   -638    -86   2636       N  
ATOM   2159  CE2 TRP A 167     -34.191  15.913 -15.356  1.00 54.22           C  
ANISOU 2159  CE2 TRP A 167     3817  10043   6742   -693   -127   2616       C  
ATOM   2160  CE3 TRP A 167     -32.470  14.280 -15.818  1.00 52.53           C  
ANISOU 2160  CE3 TRP A 167     3946   9314   6699   -841   -402   2569       C  
ATOM   2161  CZ2 TRP A 167     -33.613  16.245 -14.131  1.00 59.12           C  
ANISOU 2161  CZ2 TRP A 167     4451  10731   7282   -650    -22   2598       C  
ATOM   2162  CZ3 TRP A 167     -31.897  14.611 -14.602  1.00 51.62           C  
ANISOU 2162  CZ3 TRP A 167     3841   9262   6508   -813   -289   2570       C  
ATOM   2163  CH2 TRP A 167     -32.468  15.585 -13.774  1.00 56.40           C  
ANISOU 2163  CH2 TRP A 167     4284  10157   6988   -721   -101   2582       C  
ATOM   2164  H   TRP A 167     -34.311  16.039 -19.806  1.00 66.49           H  
ATOM   2165  HA  TRP A 167     -32.366  14.496 -18.959  1.00 65.48           H  
ATOM   2166  HB2 TRP A 167     -35.133  13.937 -19.045  1.00 63.96           H  
ATOM   2167  HB3 TRP A 167     -34.076  13.074 -18.229  1.00 63.96           H  
ATOM   2168  HD1 TRP A 167     -36.183  15.926 -17.764  1.00 70.04           H  
ATOM   2169  HE1 TRP A 167     -35.835  17.009 -15.642  1.00 70.49           H  
ATOM   2170  HE3 TRP A 167     -32.084  13.632 -16.363  1.00 63.03           H  
ATOM   2171  HZ2 TRP A 167     -33.990  16.891 -13.579  1.00 70.95           H  
ATOM   2172  HZ3 TRP A 167     -31.119  14.179 -14.331  1.00 61.94           H  
ATOM   2173  HH2 TRP A 167     -32.062  15.786 -12.962  1.00 67.68           H  
ATOM   2174  N   ASN A 168     -33.587  13.708 -21.773  1.00 60.85           N  
ANISOU 2174  N   ASN A 168     5087  10043   7991   -601   -841   2250       N  
ATOM   2175  CA  ASN A 168     -33.369  12.842 -22.926  1.00 65.32           C  
ANISOU 2175  CA  ASN A 168     5756  10442   8619   -592  -1066   2151       C  
ATOM   2176  C   ASN A 168     -31.890  12.782 -23.284  1.00 65.01           C  
ANISOU 2176  C   ASN A 168     5898  10223   8578   -429  -1089   1981       C  
ATOM   2177  O   ASN A 168     -31.331  11.699 -23.491  1.00 66.94           O  
ANISOU 2177  O   ASN A 168     6281  10275   8879   -466  -1307   1910       O  
ATOM   2178  CB  ASN A 168     -34.192  13.338 -24.117  1.00 68.82           C  
ANISOU 2178  CB  ASN A 168     6089  11019   9039   -496  -1053   2117       C  
ATOM   2179  CG  ASN A 168     -34.022  12.465 -25.350  1.00 71.33           C  
ANISOU 2179  CG  ASN A 168     6502  11200   9402   -463  -1295   1992       C  
ATOM   2180  OD1 ASN A 168     -34.005  11.237 -25.258  1.00 75.56           O  
ANISOU 2180  OD1 ASN A 168     7125  11566  10018   -610  -1541   1995       O  
ATOM   2181  ND2 ASN A 168     -33.887  13.100 -26.511  1.00 68.90           N  
ANISOU 2181  ND2 ASN A 168     6175  10964   9039   -261  -1242   1881       N  
ATOM   2182  H   ASN A 168     -34.137  14.356 -21.910  1.00 73.02           H  
ATOM   2183  HA  ASN A 168     -33.663  11.944 -22.708  1.00 78.38           H  
ATOM   2184  HB2 ASN A 168     -35.131  13.336 -23.875  1.00 82.58           H  
ATOM   2185  HB3 ASN A 168     -33.909  14.237 -24.344  1.00 82.58           H  
ATOM   2186 HD21 ASN A 168     -33.788  12.650 -27.237  1.00 82.68           H  
ATOM   2187 HD22 ASN A 168     -33.899  13.959 -26.535  1.00 82.68           H  
ATOM   2188  N   TRP A 169     -31.233  13.942 -23.344  1.00 59.15           N  
ANISOU 2188  N   TRP A 169     5154   9546   7774   -247   -881   1919       N  
ATOM   2189  CA  TRP A 169     -29.845  13.984 -23.791  1.00 54.23           C  
ANISOU 2189  CA  TRP A 169     4665   8809   7130    -88   -890   1776       C  
ATOM   2190  C   TRP A 169     -28.905  13.405 -22.741  1.00 57.17           C  
ANISOU 2190  C   TRP A 169     5162   9036   7525   -155   -928   1771       C  
ATOM   2191  O   TRP A 169     -28.051  12.567 -23.055  1.00 56.69           O  
ANISOU 2191  O   TRP A 169     5232   8828   7481   -113  -1089   1665       O  
ATOM   2192  CB  TRP A 169     -29.442  15.420 -24.129  1.00 52.51           C  
ANISOU 2192  CB  TRP A 169     4396   8701   6852     90   -675   1752       C  
ATOM   2193  CG  TRP A 169     -27.981  15.550 -24.405  1.00 55.38           C  
ANISOU 2193  CG  TRP A 169     4867   8994   7182    224   -661   1648       C  
ATOM   2194  CD1 TRP A 169     -27.353  15.363 -25.600  1.00 54.66           C  
ANISOU 2194  CD1 TRP A 169     4807   8920   7041    366   -742   1541       C  
ATOM   2195  CD2 TRP A 169     -26.955  15.882 -23.460  1.00 55.33           C  
ANISOU 2195  CD2 TRP A 169     4930   8922   7170    232   -565   1643       C  
ATOM   2196  NE1 TRP A 169     -26.002  15.561 -25.461  1.00 54.61           N  
ANISOU 2196  NE1 TRP A 169     4874   8881   6995    458   -696   1483       N  
ATOM   2197  CE2 TRP A 169     -25.731  15.880 -24.156  1.00 55.45           C  
ANISOU 2197  CE2 TRP A 169     5011   8921   7137    371   -591   1544       C  
ATOM   2198  CE3 TRP A 169     -26.954  16.181 -22.094  1.00 53.58           C  
ANISOU 2198  CE3 TRP A 169     4710   8681   6966    144   -463   1710       C  
ATOM   2199  CZ2 TRP A 169     -24.517  16.166 -23.534  1.00 55.73           C  
ANISOU 2199  CZ2 TRP A 169     5113   8907   7155    407   -522   1520       C  
ATOM   2200  CZ3 TRP A 169     -25.749  16.466 -21.478  1.00 58.45           C  
ANISOU 2200  CZ3 TRP A 169     5407   9232   7569    187   -399   1671       C  
ATOM   2201  CH2 TRP A 169     -24.546  16.457 -22.198  1.00 57.66           C  
ANISOU 2201  CH2 TRP A 169     5371   9101   7434    309   -429   1581       C  
ATOM   2202  H   TRP A 169     -31.565  14.707 -23.134  1.00 70.98           H  
ATOM   2203  HA  TRP A 169     -29.758  13.452 -24.597  1.00 65.07           H  
ATOM   2204  HB2 TRP A 169     -29.925  15.706 -24.921  1.00 63.01           H  
ATOM   2205  HB3 TRP A 169     -29.660  15.995 -23.380  1.00 63.01           H  
ATOM   2206  HD1 TRP A 169     -27.779  15.134 -26.395  1.00 65.59           H  
ATOM   2207  HE1 TRP A 169     -25.419  15.495 -26.091  1.00 65.53           H  
ATOM   2208  HE3 TRP A 169     -27.748  16.188 -21.609  1.00 64.29           H  
ATOM   2209  HZ2 TRP A 169     -23.718  16.163 -24.010  1.00 66.87           H  
ATOM   2210  HZ3 TRP A 169     -25.736  16.666 -20.569  1.00 70.14           H  
ATOM   2211  HH2 TRP A 169     -23.751  16.653 -21.757  1.00 69.19           H  
ATOM   2212  N   ILE A 170     -29.034  13.848 -21.489  1.00 54.28           N  
ANISOU 2212  N   ILE A 170     4752   8724   7148   -239   -787   1874       N  
ATOM   2213  CA  ILE A 170     -28.078  13.430 -20.469  1.00 53.39           C  
ANISOU 2213  CA  ILE A 170     4749   8495   7042   -285   -802   1872       C  
ATOM   2214  C   ILE A 170     -28.252  11.950 -20.147  1.00 54.09           C  
ANISOU 2214  C   ILE A 170     4915   8436   7202   -465  -1047   1927       C  
ATOM   2215  O   ILE A 170     -27.272  11.236 -19.907  1.00 55.83           O  
ANISOU 2215  O   ILE A 170     5277   8488   7448   -455  -1166   1864       O  
ATOM   2216  CB  ILE A 170     -28.210  14.314 -19.213  1.00 54.93           C  
ANISOU 2216  CB  ILE A 170     4867   8813   7192   -313   -595   1956       C  
ATOM   2217  CG1 ILE A 170     -26.930  14.238 -18.379  1.00 55.69           C  
ANISOU 2217  CG1 ILE A 170     5081   8803   7275   -288   -568   1909       C  
ATOM   2218  CG2 ILE A 170     -29.419  13.910 -18.380  1.00 56.43           C  
ANISOU 2218  CG2 ILE A 170     4937   9127   7378   -507   -614   2125       C  
ATOM   2219  CD1 ILE A 170     -26.836  15.299 -17.304  1.00 56.20           C  
ANISOU 2219  CD1 ILE A 170     5086   8981   7284   -253   -365   1935       C  
ATOM   2220  H   ILE A 170     -29.651  14.378 -21.211  1.00 65.14           H  
ATOM   2221  HA  ILE A 170     -27.181  13.550 -20.818  1.00 64.07           H  
ATOM   2222  HB  ILE A 170     -28.332  15.233 -19.500  1.00 65.92           H  
ATOM   2223 HG12 ILE A 170     -26.891  13.372 -17.944  1.00 66.83           H  
ATOM   2224 HG13 ILE A 170     -26.167  14.345 -18.968  1.00 66.83           H  
ATOM   2225 HG21 ILE A 170     -29.472  14.485 -17.601  1.00 67.72           H  
ATOM   2226 HG22 ILE A 170     -30.220  14.008 -18.919  1.00 67.72           H  
ATOM   2227 HG23 ILE A 170     -29.317  12.986 -18.104  1.00 67.72           H  
ATOM   2228 HD11 ILE A 170     -26.003  15.186 -16.821  1.00 67.44           H  
ATOM   2229 HD12 ILE A 170     -26.861  16.174 -17.722  1.00 67.44           H  
ATOM   2230 HD13 ILE A 170     -27.587  15.200 -16.697  1.00 67.44           H  
ATOM   2231  N   ASN A 171     -29.494  11.462 -20.144  1.00 61.51           N  
ANISOU 2231  N   ASN A 171     5760   9431   8182   -636  -1144   2055       N  
ATOM   2232  CA  ASN A 171     -29.716  10.038 -19.920  1.00 66.02           C  
ANISOU 2232  CA  ASN A 171     6406   9831   8846   -833  -1421   2132       C  
ATOM   2233  C   ASN A 171     -29.100   9.211 -21.040  1.00 64.77           C  
ANISOU 2233  C   ASN A 171     6404   9459   8748   -724  -1666   1949       C  
ATOM   2234  O   ASN A 171     -28.550   8.131 -20.795  1.00 68.38           O  
ANISOU 2234  O   ASN A 171     7009   9694   9279   -784  -1895   1925       O  
ATOM   2235  CB  ASN A 171     -31.212   9.748 -19.792  1.00 66.99           C  
ANISOU 2235  CB  ASN A 171     6371  10085   8999  -1051  -1484   2324       C  
ATOM   2236  CG  ASN A 171     -31.810  10.330 -18.525  1.00 66.88           C  
ANISOU 2236  CG  ASN A 171     6194  10312   8906  -1166  -1282   2513       C  
ATOM   2237  OD1 ASN A 171     -31.104  10.558 -17.543  1.00 71.54           O  
ANISOU 2237  OD1 ASN A 171     6824  10909   9450  -1148  -1172   2528       O  
ATOM   2238  ND2 ASN A 171     -33.115  10.568 -18.538  1.00 71.63           N  
ANISOU 2238  ND2 ASN A 171     6599  11138   9477  -1271  -1236   2651       N  
ATOM   2239  H   ASN A 171     -30.208  11.924 -20.267  1.00 73.82           H  
ATOM   2240  HA  ASN A 171     -29.289   9.779 -19.088  1.00 79.22           H  
ATOM   2241  HB2 ASN A 171     -31.676  10.137 -20.549  1.00 80.39           H  
ATOM   2242  HB3 ASN A 171     -31.349   8.788 -19.775  1.00 80.39           H  
ATOM   2243 HD21 ASN A 171     -33.499  10.897 -17.843  1.00 85.95           H  
ATOM   2244 HD22 ASN A 171     -33.577  10.392 -19.242  1.00 85.95           H  
ATOM   2245  N   LYS A 172     -29.178   9.703 -22.278  1.00 63.42           N  
ANISOU 2245  N   LYS A 172     6200   9361   8536   -547  -1633   1814       N  
ATOM   2246  CA  LYS A 172     -28.509   9.025 -23.381  1.00 64.51           C  
ANISOU 2246  CA  LYS A 172     6468   9354   8689   -389  -1846   1607       C  
ATOM   2247  C   LYS A 172     -26.999   9.037 -23.193  1.00 67.05           C  
ANISOU 2247  C   LYS A 172     6918   9595   8963   -220  -1813   1472       C  
ATOM   2248  O   LYS A 172     -26.319   8.070 -23.553  1.00 68.66           O  
ANISOU 2248  O   LYS A 172     7266   9623   9199   -140  -2052   1328       O  
ATOM   2249  CB  LYS A 172     -28.890   9.683 -24.708  1.00 65.52           C  
ANISOU 2249  CB  LYS A 172     6504   9642   8749   -223  -1781   1509       C  
ATOM   2250  CG  LYS A 172     -28.435   8.913 -25.934  1.00 67.77           C  
ANISOU 2250  CG  LYS A 172     6891   9832   9027    -55  -2027   1291       C  
ATOM   2251  H   LYS A 172     -29.606  10.416 -22.500  1.00 76.11           H  
ATOM   2252  HA  LYS A 172     -28.802   8.101 -23.409  1.00 77.41           H  
ATOM   2253  HB2 LYS A 172     -29.856   9.763 -24.750  1.00 78.62           H  
ATOM   2254  HB3 LYS A 172     -28.486  10.565 -24.745  1.00 78.62           H  
ATOM   2255  N   GLN A 173     -26.458  10.120 -22.627  1.00 66.40           N  
ANISOU 2255  N   GLN A 173     6784   9640   8804   -156  -1537   1509       N  
ATOM   2256  CA  GLN A 173     -25.034  10.161 -22.314  1.00 63.43           C  
ANISOU 2256  CA  GLN A 173     6511   9206   8383    -26  -1498   1409       C  
ATOM   2257  C   GLN A 173     -24.686   9.163 -21.217  1.00 63.43           C  
ANISOU 2257  C   GLN A 173     6630   9014   8456   -166  -1649   1464       C  
ATOM   2258  O   GLN A 173     -23.629   8.524 -21.264  1.00 66.88           O  
ANISOU 2258  O   GLN A 173     7199   9320   8891    -59  -1785   1337       O  
ATOM   2259  CB  GLN A 173     -24.632  11.577 -21.899  1.00 60.34           C  
ANISOU 2259  CB  GLN A 173     6033   8977   7915     42  -1191   1454       C  
ATOM   2260  CG  GLN A 173     -24.547  12.567 -23.047  1.00 60.91           C  
ANISOU 2260  CG  GLN A 173     6018   9214   7911    217  -1064   1391       C  
ATOM   2261  CD  GLN A 173     -23.369  12.302 -23.961  1.00 61.94           C  
ANISOU 2261  CD  GLN A 173     6211   9356   7968    421  -1146   1224       C  
ATOM   2262  OE1 GLN A 173     -22.354  11.739 -23.543  1.00 60.98           O  
ANISOU 2262  OE1 GLN A 173     6193   9140   7837    463  -1222   1151       O  
ATOM   2263  NE2 GLN A 173     -23.495  12.711 -25.219  1.00 60.91           N  
ANISOU 2263  NE2 GLN A 173     6004   9371   7768    560  -1131   1167       N  
ATOM   2264  H   GLN A 173     -26.891  10.833 -22.418  1.00 79.68           H  
ATOM   2265  HA  GLN A 173     -24.529   9.925 -23.107  1.00 76.11           H  
ATOM   2266  HB2 GLN A 173     -25.287  11.914 -21.267  1.00 72.40           H  
ATOM   2267  HB3 GLN A 173     -23.759  11.541 -21.476  1.00 72.40           H  
ATOM   2268  HG2 GLN A 173     -25.358  12.506 -23.577  1.00 73.09           H  
ATOM   2269  HG3 GLN A 173     -24.453  13.462 -22.686  1.00 73.09           H  
ATOM   2270 HE21 GLN A 173     -24.218  13.101 -25.473  1.00 73.09           H  
ATOM   2271 HE22 GLN A 173     -22.855  12.584 -25.778  1.00 73.09           H  
ATOM   2272  N   GLN A 174     -25.563   9.015 -20.222  1.00 60.65           N  
ANISOU 2272  N   GLN A 174     6222   8664   8158   -400  -1634   1663       N  
ATOM   2273  CA  GLN A 174     -25.316   8.056 -19.150  1.00 60.86           C  
ANISOU 2273  CA  GLN A 174     6348   8524   8253   -562  -1787   1761       C  
ATOM   2274  C   GLN A 174     -25.167   6.645 -19.706  1.00 66.27           C  
ANISOU 2274  C   GLN A 174     7187   8947   9044   -572  -2156   1671       C  
ATOM   2275  O   GLN A 174     -24.233   5.918 -19.350  1.00 67.51           O  
ANISOU 2275  O   GLN A 174     7494   8923   9234   -529  -2309   1605       O  
ATOM   2276  CB  GLN A 174     -26.450   8.118 -18.127  1.00 62.51           C  
ANISOU 2276  CB  GLN A 174     6428   8843   8481   -821  -1719   2016       C  
ATOM   2277  CG  GLN A 174     -26.284   7.169 -16.947  1.00 65.68           C  
ANISOU 2277  CG  GLN A 174     6903   9111   8941  -1020  -1869   2173       C  
ATOM   2278  CD  GLN A 174     -27.444   7.239 -15.973  1.00 63.05           C  
ANISOU 2278  CD  GLN A 174     6404   8958   8592  -1277  -1796   2448       C  
ATOM   2279  OE1 GLN A 174     -28.462   7.875 -16.246  1.00 64.80           O  
ANISOU 2279  OE1 GLN A 174     6459   9388   8773  -1307  -1667   2510       O  
ATOM   2280  NE2 GLN A 174     -27.296   6.582 -14.831  1.00 66.89           N  
ANISOU 2280  NE2 GLN A 174     6921   9394   9100  -1456  -1881   2622       N  
ATOM   2281  H   GLN A 174     -26.299   9.453 -20.146  1.00 72.78           H  
ATOM   2282  HA  GLN A 174     -24.490   8.290 -18.699  1.00 73.04           H  
ATOM   2283  HB2 GLN A 174     -26.502   9.020 -17.775  1.00 75.01           H  
ATOM   2284  HB3 GLN A 174     -27.282   7.892 -18.571  1.00 75.01           H  
ATOM   2285  HG2 GLN A 174     -26.224   6.259 -17.278  1.00 78.82           H  
ATOM   2286  HG3 GLN A 174     -25.474   7.401 -16.466  1.00 78.82           H  
ATOM   2287 HE21 GLN A 174     -26.571   6.148 -14.675  1.00 80.27           H  
ATOM   2288 HE22 GLN A 174     -27.926   6.591 -14.245  1.00 80.27           H  
ATOM   2289  N   GLY A 175     -26.086   6.238 -20.584  1.00 66.02           N  
ANISOU 2289  N   GLY A 175     7126   8885   9073   -619  -2323   1659       N  
ATOM   2290  CA  GLY A 175     -26.002   4.909 -21.164  1.00 64.18           C  
ANISOU 2290  CA  GLY A 175     7050   8381   8955   -616  -2713   1549       C  
ATOM   2291  C   GLY A 175     -24.841   4.766 -22.129  1.00 69.86           C  
ANISOU 2291  C   GLY A 175     7885   9047   9609   -292  -2797   1247       C  
ATOM   2292  O   GLY A 175     -24.147   3.746 -22.131  1.00 71.55           O  
ANISOU 2292  O   GLY A 175     8272   9025   9887   -222  -3075   1125       O  
ATOM   2293  H   GLY A 175     -26.755   6.708 -20.853  1.00 79.22           H  
ATOM   2294  HA2 GLY A 175     -25.895   4.254 -20.457  1.00 77.02           H  
ATOM   2295  HA3 GLY A 175     -26.824   4.713 -21.642  1.00 77.02           H  
ATOM   2296  N   LYS A 176     -24.612   5.785 -22.961  1.00 72.35           N  
ANISOU 2296  N   LYS A 176     8100   9600   9790    -84  -2569   1130       N  
ATOM   2297  CA  LYS A 176     -23.529   5.714 -23.938  1.00 74.40           C  
ANISOU 2297  CA  LYS A 176     8426   9891   9950    231  -2629    862       C  
ATOM   2298  C   LYS A 176     -22.179   5.475 -23.274  1.00 74.92           C  
ANISOU 2298  C   LYS A 176     8603   9879   9983    338  -2631    791       C  
ATOM   2299  O   LYS A 176     -21.312   4.816 -23.859  1.00 77.13           O  
ANISOU 2299  O   LYS A 176     8991  10087  10227    564  -2828    566       O  
ATOM   2300  CB  LYS A 176     -23.484   6.995 -24.771  1.00 72.81           C  
ANISOU 2300  CB  LYS A 176     8069   9996   9601    394  -2344    823       C  
ATOM   2301  CG  LYS A 176     -24.152   6.876 -26.133  1.00 73.46           C  
ANISOU 2301  CG  LYS A 176     8099  10159   9655    499  -2466    705       C  
ATOM   2302  CD  LYS A 176     -23.880   8.101 -26.994  1.00 73.72           C  
ANISOU 2302  CD  LYS A 176     7985  10499   9525    687  -2203    669       C  
ATOM   2303  CE  LYS A 176     -24.718   9.293 -26.561  1.00 73.14           C  
ANISOU 2303  CE  LYS A 176     7762  10567   9459    529  -1913    890       C  
ATOM   2304  NZ  LYS A 176     -25.876   9.515 -27.475  1.00 76.75           N  
ANISOU 2304  NZ  LYS A 176     8112  11136   9915    514  -1933    910       N  
ATOM   2305  H   LYS A 176     -25.063   6.517 -22.979  1.00 86.82           H  
ATOM   2306  HA  LYS A 176     -23.699   4.973 -24.540  1.00 89.28           H  
ATOM   2307  HB2 LYS A 176     -23.935   7.701 -24.281  1.00 87.38           H  
ATOM   2308  HB3 LYS A 176     -22.557   7.239 -24.917  1.00 87.38           H  
ATOM   2309  HG2 LYS A 176     -23.804   6.096 -26.593  1.00 88.16           H  
ATOM   2310  HG3 LYS A 176     -25.112   6.795 -26.013  1.00 88.16           H  
ATOM   2311  HD2 LYS A 176     -22.944   8.344 -26.917  1.00 88.46           H  
ATOM   2312  HD3 LYS A 176     -24.097   7.897 -27.917  1.00 88.46           H  
ATOM   2313  HE2 LYS A 176     -25.062   9.134 -25.668  1.00 87.76           H  
ATOM   2314  HE3 LYS A 176     -24.167  10.092 -26.570  1.00 87.76           H  
ATOM   2315  HZ1 LYS A 176     -26.350  10.216 -27.200  1.00 92.10           H  
ATOM   2316  HZ2 LYS A 176     -25.585   9.668 -28.302  1.00 92.10           H  
ATOM   2317  HZ3 LYS A 176     -26.400   8.796 -27.481  1.00 92.10           H  
ATOM   2318  N   ARG A 177     -21.976   6.000 -22.066  1.00 73.09           N  
ANISOU 2318  N   ARG A 177     8340   9680   9751    198  -2420    965       N  
ATOM   2319  CA  ARG A 177     -20.716   5.842 -21.351  1.00 73.62           C  
ANISOU 2319  CA  ARG A 177     8499   9690   9783    283  -2404    916       C  
ATOM   2320  C   ARG A 177     -20.774   4.760 -20.279  1.00 75.08           C  
ANISOU 2320  C   ARG A 177     8818   9607  10102     93  -2628   1028       C  
ATOM   2321  O   ARG A 177     -19.771   4.532 -19.595  1.00 76.99           O  
ANISOU 2321  O   ARG A 177     9144   9782  10325    148  -2638   1000       O  
ATOM   2322  CB  ARG A 177     -20.299   7.172 -20.709  1.00 70.98           C  
ANISOU 2322  CB  ARG A 177     8047   9571   9351    276  -2035   1016       C  
ATOM   2323  CG  ARG A 177     -20.432   8.394 -21.611  1.00 69.02           C  
ANISOU 2323  CG  ARG A 177     7650   9578   8997    397  -1800    985       C  
ATOM   2324  CD  ARG A 177     -19.705   8.235 -22.934  1.00 70.74           C  
ANISOU 2324  CD  ARG A 177     7876   9889   9115    671  -1893    764       C  
ATOM   2325  NE  ARG A 177     -20.195   9.199 -23.912  1.00 74.06           N  
ANISOU 2325  NE  ARG A 177     8150  10531   9459    739  -1732    775       N  
ATOM   2326  CZ  ARG A 177     -20.162   9.021 -25.229  1.00 74.64           C  
ANISOU 2326  CZ  ARG A 177     8193  10715   9453    928  -1833    624       C  
ATOM   2327  NH1 ARG A 177     -19.660   7.911 -25.754  1.00 74.16           N  
ANISOU 2327  NH1 ARG A 177     8240  10563   9373   1092  -2106    420       N  
ATOM   2328  NH2 ARG A 177     -20.645   9.958 -26.029  1.00 74.32           N  
ANISOU 2328  NH2 ARG A 177     8011  10882   9344    968  -1674    671       N  
ATOM   2329  H   ARG A 177     -22.562   6.459 -21.635  1.00 87.71           H  
ATOM   2330  HA  ARG A 177     -20.027   5.591 -21.986  1.00 88.34           H  
ATOM   2331  HB2 ARG A 177     -20.853   7.324 -19.927  1.00 85.18           H  
ATOM   2332  HB3 ARG A 177     -19.369   7.107 -20.440  1.00 85.18           H  
ATOM   2333  HG2 ARG A 177     -21.371   8.544 -21.802  1.00 82.82           H  
ATOM   2334  HG3 ARG A 177     -20.060   9.165 -21.155  1.00 82.82           H  
ATOM   2335  HD2 ARG A 177     -18.757   8.389 -22.801  1.00 84.89           H  
ATOM   2336  HD3 ARG A 177     -19.858   7.342 -23.280  1.00 84.89           H  
ATOM   2337  HE  ARG A 177     -20.529   9.934 -23.616  1.00 88.88           H  
ATOM   2338 HH11 ARG A 177     -19.348   7.296 -25.241  1.00 88.99           H  
ATOM   2339 HH12 ARG A 177     -19.645   7.808 -26.608  1.00 88.99           H  
ATOM   2340 HH21 ARG A 177     -20.971  10.681 -25.696  1.00 89.18           H  
ATOM   2341 HH22 ARG A 177     -20.624   9.849 -26.881  1.00 89.18           H  
ATOM   2342  N   GLY A 178     -21.912   4.091 -20.116  1.00 70.25           N  
ANISOU 2342  N   GLY A 178     8219   8849   9624   -139  -2817   1170       N  
ATOM   2343  CA  GLY A 178     -22.028   3.070 -19.093  1.00 70.08           C  
ANISOU 2343  CA  GLY A 178     8310   8580   9736   -356  -3045   1327       C  
ATOM   2344  C   GLY A 178     -21.846   3.580 -17.684  1.00 68.11           C  
ANISOU 2344  C   GLY A 178     8001   8434   9446   -512  -2810   1539       C  
ATOM   2345  O   GLY A 178     -21.522   2.798 -16.787  1.00 69.18           O  
ANISOU 2345  O   GLY A 178     8241   8389   9653   -628  -2973   1642       O  
ATOM   2346  H   GLY A 178     -22.624   4.211 -20.583  1.00 84.30           H  
ATOM   2347  HA2 GLY A 178     -22.904   2.659 -19.154  1.00 84.09           H  
ATOM   2348  HA3 GLY A 178     -21.361   2.384 -19.253  1.00 84.09           H  
ATOM   2349  N   TRP A 179     -22.046   4.876 -17.460  1.00 70.97           N  
ANISOU 2349  N   TRP A 179     8196   9076   9692   -508  -2447   1603       N  
ATOM   2350  CA  TRP A 179     -21.899   5.443 -16.132  1.00 69.54           C  
ANISOU 2350  CA  TRP A 179     7948   9020   9454   -628  -2222   1774       C  
ATOM   2351  C   TRP A 179     -22.902   4.820 -15.165  1.00 71.98           C  
ANISOU 2351  C   TRP A 179     8217   9286   9845   -946  -2330   2059       C  
ATOM   2352  O   TRP A 179     -23.869   4.161 -15.555  1.00 74.16           O  
ANISOU 2352  O   TRP A 179     8484   9472  10224  -1101  -2535   2150       O  
ATOM   2353  CB  TRP A 179     -22.098   6.957 -16.171  1.00 63.56           C  
ANISOU 2353  CB  TRP A 179     7022   8550   8576   -558  -1856   1773       C  
ATOM   2354  CG  TRP A 179     -21.029   7.693 -16.910  1.00 57.01           C  
ANISOU 2354  CG  TRP A 179     6206   7799   7657   -288  -1723   1558       C  
ATOM   2355  CD1 TRP A 179     -19.849   7.186 -17.370  1.00 57.70           C  
ANISOU 2355  CD1 TRP A 179     6417   7780   7728    -96  -1857   1374       C  
ATOM   2356  CD2 TRP A 179     -21.040   9.077 -17.277  1.00 52.76           C  
ANISOU 2356  CD2 TRP A 179     5540   7478   7028   -183  -1442   1523       C  
ATOM   2357  NE1 TRP A 179     -19.125   8.168 -18.000  1.00 54.11           N  
ANISOU 2357  NE1 TRP A 179     5898   7496   7164    105  -1664   1246       N  
ATOM   2358  CE2 TRP A 179     -19.835   9.339 -17.957  1.00 52.39           C  
ANISOU 2358  CE2 TRP A 179     5536   7456   6913     45  -1417   1343       C  
ATOM   2359  CE3 TRP A 179     -21.954  10.120 -17.097  1.00 49.76           C  
ANISOU 2359  CE3 TRP A 179     5010   7277   6618   -253  -1225   1630       C  
ATOM   2360  CZ2 TRP A 179     -19.518  10.601 -18.457  1.00 46.32           C  
ANISOU 2360  CZ2 TRP A 179     4667   6872   6062    169  -1191   1299       C  
ATOM   2361  CZ3 TRP A 179     -21.637  11.371 -17.594  1.00 49.05           C  
ANISOU 2361  CZ3 TRP A 179     4842   7336   6459   -106  -1013   1559       C  
ATOM   2362  CH2 TRP A 179     -20.430  11.601 -18.265  1.00 45.57           C  
ANISOU 2362  CH2 TRP A 179     4448   6901   5965     86  -1002   1410       C  
ATOM   2363  H   TRP A 179     -22.267   5.446 -18.064  1.00 85.16           H  
ATOM   2364  HA  TRP A 179     -21.005   5.262 -15.802  1.00 83.45           H  
ATOM   2365  HB2 TRP A 179     -22.943   7.149 -16.606  1.00 76.27           H  
ATOM   2366  HB3 TRP A 179     -22.113   7.293 -15.261  1.00 76.27           H  
ATOM   2367  HD1 TRP A 179     -19.575   6.303 -17.270  1.00 69.25           H  
ATOM   2368  HE1 TRP A 179     -18.352   8.064 -18.363  1.00 64.93           H  
ATOM   2369  HE3 TRP A 179     -22.757   9.976 -16.652  1.00 59.71           H  
ATOM   2370  HZ2 TRP A 179     -18.717  10.757 -18.903  1.00 55.59           H  
ATOM   2371  HZ3 TRP A 179     -22.237  12.073 -17.480  1.00 58.86           H  
ATOM   2372  HH2 TRP A 179     -20.244  12.453 -18.589  1.00 54.69           H  
ATOM   2373  N   GLY A 180     -22.659   5.048 -13.880  1.00 69.49           N  
ANISOU 2373  N   GLY A 180     7865   9063   9475  -1049  -2193   2209       N  
ATOM   2374  CA  GLY A 180     -23.560   4.609 -12.840  1.00 66.61           C  
ANISOU 2374  CA  GLY A 180     7418   8750   9142  -1349  -2244   2513       C  
ATOM   2375  C   GLY A 180     -24.768   5.516 -12.731  1.00 69.90           C  
ANISOU 2375  C   GLY A 180     7608   9472   9479  -1448  -2008   2644       C  
ATOM   2376  O   GLY A 180     -25.135   6.234 -13.665  1.00 66.32           O  
ANISOU 2376  O   GLY A 180     7084   9116   8997  -1321  -1889   2515       O  
ATOM   2377  H   GLY A 180     -21.965   5.463 -13.587  1.00 83.38           H  
ATOM   2378  HA2 GLY A 180     -23.865   3.708 -13.031  1.00 79.94           H  
ATOM   2379  HA3 GLY A 180     -23.098   4.605 -11.987  1.00 79.94           H  
ATOM   2380  N   GLN A 181     -25.392   5.483 -11.558  1.00 83.83           N  
ANISOU 2380  N   GLN A 181     9245  11414  11192  -1667  -1942   2908       N  
ATOM   2381  CA  GLN A 181     -26.605   6.249 -11.322  1.00 89.02           C  
ANISOU 2381  CA  GLN A 181     9665  12401  11757  -1762  -1738   3050       C  
ATOM   2382  C   GLN A 181     -26.281   7.710 -11.036  1.00 83.80           C  
ANISOU 2382  C   GLN A 181     8911  11987  10942  -1551  -1386   2910       C  
ATOM   2383  O   GLN A 181     -25.244   8.037 -10.451  1.00 85.83           O  
ANISOU 2383  O   GLN A 181     9243  12228  11142  -1433  -1287   2817       O  
ATOM   2384  CB  GLN A 181     -27.386   5.660 -10.147  1.00 90.26           C  
ANISOU 2384  CB  GLN A 181     9694  12714  11888  -2067  -1802   3396       C  
ATOM   2385  CG  GLN A 181     -26.635   5.708  -8.824  1.00 89.95           C  
ANISOU 2385  CG  GLN A 181     9667  12760  11749  -2078  -1708   3476       C  
ATOM   2386  H   GLN A 181     -25.130   5.022 -10.881  1.00100.59           H  
ATOM   2387  HA  GLN A 181     -27.168   6.211 -12.111  1.00106.82           H  
ATOM   2388  HB2 GLN A 181     -28.211   6.159 -10.038  1.00108.31           H  
ATOM   2389  HB3 GLN A 181     -27.587   4.731 -10.340  1.00108.31           H  
ATOM   2390  N   LEU A 182     -27.183   8.595 -11.462  1.00 71.95           N  
ANISOU 2390  N   LEU A 182     7249  10707   9384  -1501  -1216   2893       N  
ATOM   2391  CA  LEU A 182     -27.104   9.998 -11.076  1.00 66.44           C  
ANISOU 2391  CA  LEU A 182     6443  10252   8550  -1326   -912   2793       C  
ATOM   2392  C   LEU A 182     -27.115  10.095  -9.558  1.00 64.32           C  
ANISOU 2392  C   LEU A 182     6080  10201   8158  -1417   -807   2944       C  
ATOM   2393  O   LEU A 182     -28.159   9.900  -8.928  1.00 67.94           O  
ANISOU 2393  O   LEU A 182     6360  10907   8548  -1591   -796   3166       O  
ATOM   2394  CB  LEU A 182     -28.267  10.798 -11.667  1.00 69.98           C  
ANISOU 2394  CB  LEU A 182     6717  10913   8959  -1285   -785   2792       C  
ATOM   2395  CG  LEU A 182     -28.371  12.271 -11.252  1.00 70.89           C  
ANISOU 2395  CG  LEU A 182     6713  11276   8946  -1099   -504   2694       C  
ATOM   2396  CD1 LEU A 182     -27.342  13.123 -11.976  1.00 69.50           C  
ANISOU 2396  CD1 LEU A 182     6665  10941   8802   -856   -417   2446       C  
ATOM   2397  CD2 LEU A 182     -29.771  12.797 -11.502  1.00 71.84           C  
ANISOU 2397  CD2 LEU A 182     6623  11661   9011  -1114   -416   2769       C  
ATOM   2398  H   LEU A 182     -27.847   8.406 -11.975  1.00 86.35           H  
ATOM   2399  HA  LEU A 182     -26.273  10.377 -11.402  1.00 79.73           H  
ATOM   2400  HB2 LEU A 182     -28.188  10.777 -12.634  1.00 83.97           H  
ATOM   2401  HB3 LEU A 182     -29.095  10.367 -11.405  1.00 83.97           H  
ATOM   2402  HG  LEU A 182     -28.195  12.340 -10.300  1.00 85.07           H  
ATOM   2403 HD11 LEU A 182     -27.438  14.045 -11.689  1.00 83.40           H  
ATOM   2404 HD12 LEU A 182     -26.454  12.799 -11.758  1.00 83.40           H  
ATOM   2405 HD13 LEU A 182     -27.494  13.057 -12.932  1.00 83.40           H  
ATOM   2406 HD21 LEU A 182     -29.811  13.727 -11.232  1.00 86.21           H  
ATOM   2407 HD22 LEU A 182     -29.973  12.717 -12.447  1.00 86.21           H  
ATOM   2408 HD23 LEU A 182     -30.401  12.274 -10.983  1.00 86.21           H  
ATOM   2409  N   THR A 183     -25.964  10.397  -8.960  1.00 65.33           N  
ANISOU 2409  N   THR A 183     6309  10270   8242  -1298   -731   2833       N  
ATOM   2410  CA  THR A 183     -25.876  10.384  -7.504  1.00 64.84           C  
ANISOU 2410  CA  THR A 183     6170  10409   8055  -1378   -655   2969       C  
ATOM   2411  C   THR A 183     -26.607  11.573  -6.890  1.00 66.69           C  
ANISOU 2411  C   THR A 183     6196  11017   8125  -1286   -408   2958       C  
ATOM   2412  O   THR A 183     -27.289  11.423  -5.870  1.00 70.95           O  
ANISOU 2412  O   THR A 183     6568  11852   8536  -1412   -366   3153       O  
ATOM   2413  CB  THR A 183     -24.414  10.368  -7.062  1.00 64.27           C  
ANISOU 2413  CB  THR A 183     6266  10169   7983  -1269   -656   2838       C  
ATOM   2414  OG1 THR A 183     -23.781  11.600  -7.431  1.00 67.11           O  
ANISOU 2414  OG1 THR A 183     6657  10526   8316  -1024   -478   2589       O  
ATOM   2415  CG2 THR A 183     -23.671   9.203  -7.706  1.00 66.30           C  
ANISOU 2415  CG2 THR A 183     6730  10068   8394  -1314   -914   2817       C  
ATOM   2416  H   THR A 183     -25.235  10.609  -9.364  1.00 78.39           H  
ATOM   2417  HA  THR A 183     -26.296   9.575  -7.173  1.00 77.80           H  
ATOM   2418  HB  THR A 183     -24.371  10.262  -6.099  1.00 77.12           H  
ATOM   2419  HG1 THR A 183     -22.977  11.593  -7.189  1.00 80.54           H  
ATOM   2420 HG21 THR A 183     -22.744   9.201  -7.419  1.00 79.56           H  
ATOM   2421 HG22 THR A 183     -24.083   8.364  -7.447  1.00 79.56           H  
ATOM   2422 HG23 THR A 183     -23.702   9.284  -8.672  1.00 79.56           H  
ATOM   2423  N   SER A 184     -26.486  12.756  -7.487  1.00 65.59           N  
ANISOU 2423  N   SER A 184     6058  10883   7981  -1061   -257   2737       N  
ATOM   2424  CA  SER A 184     -27.114  13.933  -6.901  1.00 66.96           C  
ANISOU 2424  CA  SER A 184     6057  11378   8008   -932    -50   2687       C  
ATOM   2425  C   SER A 184     -27.057  15.092  -7.884  1.00 65.42           C  
ANISOU 2425  C   SER A 184     5891  11098   7867   -711     49   2467       C  
ATOM   2426  O   SER A 184     -26.183  15.156  -8.752  1.00 64.33           O  
ANISOU 2426  O   SER A 184     5916  10681   7844   -631      0   2332       O  
ATOM   2427  CB  SER A 184     -26.433  14.334  -5.588  1.00 67.16           C  
ANISOU 2427  CB  SER A 184     6077  11537   7902   -859     51   2642       C  
ATOM   2428  OG  SER A 184     -25.169  14.928  -5.836  1.00 64.18           O  
ANISOU 2428  OG  SER A 184     5873  10923   7589   -691     82   2419       O  
ATOM   2429  H   SER A 184     -26.055  12.902  -8.217  1.00 78.71           H  
ATOM   2430  HA  SER A 184     -28.045  13.739  -6.713  1.00 80.36           H  
ATOM   2431  HB2 SER A 184     -26.996  14.973  -5.123  1.00 80.59           H  
ATOM   2432  HB3 SER A 184     -26.309  13.543  -5.042  1.00 80.59           H  
ATOM   2433  HG  SER A 184     -24.806  15.144  -5.110  1.00 77.01           H  
ATOM   2434  N   ASN A 185     -28.010  16.006  -7.728  1.00 65.39           N  
ANISOU 2434  N   ASN A 185     5717  11359   7768   -608    181   2441       N  
ATOM   2435  CA  ASN A 185     -27.983  17.311  -8.371  1.00 64.49           C  
ANISOU 2435  CA  ASN A 185     5616  11202   7686   -377    285   2238       C  
ATOM   2436  C   ASN A 185     -27.638  18.351  -7.317  1.00 63.41           C  
ANISOU 2436  C   ASN A 185     5449  11207   7436   -201    411   2100       C  
ATOM   2437  O   ASN A 185     -28.298  18.424  -6.276  1.00 68.43           O  
ANISOU 2437  O   ASN A 185     5923  12167   7911   -201    477   2164       O  
ATOM   2438  CB  ASN A 185     -29.330  17.649  -9.015  1.00 63.34           C  
ANISOU 2438  CB  ASN A 185     5308  11233   7525   -352    317   2283       C  
ATOM   2439  CG  ASN A 185     -29.579  16.874 -10.285  1.00 65.08           C  
ANISOU 2439  CG  ASN A 185     5582  11269   7878   -473    186   2355       C  
ATOM   2440  OD1 ASN A 185     -30.541  16.110 -10.383  1.00 69.45           O  
ANISOU 2440  OD1 ASN A 185     6018  11953   8418   -642    114   2530       O  
ATOM   2441  ND2 ASN A 185     -28.714  17.068 -11.273  1.00 63.20           N  
ANISOU 2441  ND2 ASN A 185     5510  10744   7760   -386    145   2224       N  
ATOM   2442  H   ASN A 185     -28.706  15.886  -7.237  1.00 78.47           H  
ATOM   2443  HA  ASN A 185     -27.298  17.324  -9.058  1.00 77.39           H  
ATOM   2444  HB2 ASN A 185     -30.040  17.438  -8.389  1.00 76.01           H  
ATOM   2445  HB3 ASN A 185     -29.348  18.595  -9.231  1.00 76.01           H  
ATOM   2446 HD21 ASN A 185     -28.812  16.650 -12.018  1.00 75.85           H  
ATOM   2447 HD22 ASN A 185     -28.056  17.612 -11.168  1.00 75.85           H  
ATOM   2448  N   LEU A 186     -26.611  19.149  -7.582  1.00 59.98           N  
ANISOU 2448  N   LEU A 186     5160  10551   7080    -53    432   1915       N  
ATOM   2449  CA  LEU A 186     -26.128  20.130  -6.620  1.00 61.02           C  
ANISOU 2449  CA  LEU A 186     5298  10755   7134    113    513   1759       C  
ATOM   2450  C   LEU A 186     -26.370  21.530  -7.169  1.00 62.01           C  
ANISOU 2450  C   LEU A 186     5418  10830   7313    330    564   1589       C  
ATOM   2451  O   LEU A 186     -25.927  21.851  -8.277  1.00 59.43           O  
ANISOU 2451  O   LEU A 186     5196  10253   7130    358    526   1543       O  
ATOM   2452  CB  LEU A 186     -24.646  19.909  -6.323  1.00 60.79           C  
ANISOU 2452  CB  LEU A 186     5442  10501   7157     87    469   1698       C  
ATOM   2453  CG  LEU A 186     -24.071  20.730  -5.168  1.00 63.50           C  
ANISOU 2453  CG  LEU A 186     5794  10921   7411    224    527   1550       C  
ATOM   2454  CD1 LEU A 186     -24.656  20.285  -3.832  1.00 62.30           C  
ANISOU 2454  CD1 LEU A 186     5496  11116   7060    180    571   1641       C  
ATOM   2455  CD2 LEU A 186     -22.551  20.633  -5.149  1.00 60.65           C  
ANISOU 2455  CD2 LEU A 186     5609  10303   7132    205    476   1481       C  
ATOM   2456  H   LEU A 186     -26.172  19.141  -8.321  1.00 71.98           H  
ATOM   2457  HA  LEU A 186     -26.623  20.037  -5.791  1.00 73.23           H  
ATOM   2458  HB2 LEU A 186     -24.513  18.973  -6.107  1.00 72.95           H  
ATOM   2459  HB3 LEU A 186     -24.138  20.132  -7.118  1.00 72.95           H  
ATOM   2460  HG  LEU A 186     -24.307  21.662  -5.299  1.00 76.20           H  
ATOM   2461 HD11 LEU A 186     -24.271  20.825  -3.123  1.00 74.76           H  
ATOM   2462 HD12 LEU A 186     -25.619  20.404  -3.853  1.00 74.76           H  
ATOM   2463 HD13 LEU A 186     -24.441  19.350  -3.689  1.00 74.76           H  
ATOM   2464 HD21 LEU A 186     -22.210  21.161  -4.410  1.00 72.78           H  
ATOM   2465 HD22 LEU A 186     -22.295  19.704  -5.038  1.00 72.78           H  
ATOM   2466 HD23 LEU A 186     -22.202  20.974  -5.988  1.00 72.78           H  
ATOM   2467  N   LEU A 187     -27.080  22.352  -6.398  1.00 61.29           N  
ANISOU 2467  N   LEU A 187     5199  10989   7098    491    636   1499       N  
ATOM   2468  CA  LEU A 187     -27.278  23.758  -6.729  1.00 60.02           C  
ANISOU 2468  CA  LEU A 187     5047  10765   6991    725    655   1315       C  
ATOM   2469  C   LEU A 187     -26.182  24.587  -6.073  1.00 63.41           C  
ANISOU 2469  C   LEU A 187     5603  11041   7449    851    637   1129       C  
ATOM   2470  O   LEU A 187     -26.023  24.552  -4.848  1.00 64.64           O  
ANISOU 2470  O   LEU A 187     5718  11378   7465    891    664   1074       O  
ATOM   2471  CB  LEU A 187     -28.653  24.237  -6.267  1.00 63.55           C  
ANISOU 2471  CB  LEU A 187     5288  11572   7288    871    718   1285       C  
ATOM   2472  CG  LEU A 187     -28.924  25.739  -6.406  1.00 66.12           C  
ANISOU 2472  CG  LEU A 187     5621  11848   7654   1156    713   1067       C  
ATOM   2473  CD1 LEU A 187     -28.893  26.161  -7.868  1.00 63.13           C  
ANISOU 2473  CD1 LEU A 187     5336  11178   7474   1161    664   1081       C  
ATOM   2474  CD2 LEU A 187     -30.255  26.103  -5.764  1.00 68.89           C  
ANISOU 2474  CD2 LEU A 187     5747  12619   7811   1328    775   1021       C  
ATOM   2475  H   LEU A 187     -27.463  22.113  -5.666  1.00 73.54           H  
ATOM   2476  HA  LEU A 187     -27.219  23.875  -7.690  1.00 72.02           H  
ATOM   2477  HB2 LEU A 187     -29.329  23.773  -6.785  1.00 76.27           H  
ATOM   2478  HB3 LEU A 187     -28.755  24.011  -5.329  1.00 76.27           H  
ATOM   2479  HG  LEU A 187     -28.227  26.227  -5.941  1.00 79.34           H  
ATOM   2480 HD11 LEU A 187     -29.067  27.114  -7.925  1.00 75.76           H  
ATOM   2481 HD12 LEU A 187     -28.017  25.962  -8.235  1.00 75.76           H  
ATOM   2482 HD13 LEU A 187     -29.574  25.670  -8.353  1.00 75.76           H  
ATOM   2483 HD21 LEU A 187     -30.403  27.056  -5.864  1.00 82.67           H  
ATOM   2484 HD22 LEU A 187     -30.963  25.608  -6.205  1.00 82.67           H  
ATOM   2485 HD23 LEU A 187     -30.225  25.869  -4.823  1.00 82.67           H  
ATOM   2486  N   LEU A 188     -25.433  25.332  -6.883  1.00 58.11           N  
ANISOU 2486  N   LEU A 188     5076  10052   6953    905    582   1045       N  
ATOM   2487  CA  LEU A 188     -24.382  26.214  -6.395  1.00 57.83           C  
ANISOU 2487  CA  LEU A 188     5163   9832   6978   1007    536    879       C  
ATOM   2488  C   LEU A 188     -24.728  27.654  -6.734  1.00 58.07           C  
ANISOU 2488  C   LEU A 188     5211   9751   7102   1221    490    726       C  
ATOM   2489  O   LEU A 188     -24.932  27.988  -7.905  1.00 55.68           O  
ANISOU 2489  O   LEU A 188     4933   9293   6929   1219    461    781       O  
ATOM   2490  CB  LEU A 188     -23.021  25.863  -7.001  1.00 58.97           C  
ANISOU 2490  CB  LEU A 188     5462   9690   7256    864    484    936       C  
ATOM   2491  CG  LEU A 188     -22.460  24.471  -6.707  1.00 57.49           C  
ANISOU 2491  CG  LEU A 188     5295   9543   7004    673    492   1064       C  
ATOM   2492  CD1 LEU A 188     -23.003  23.448  -7.689  1.00 60.20           C  
ANISOU 2492  CD1 LEU A 188     5603   9901   7372    534    488   1234       C  
ATOM   2493  CD2 LEU A 188     -20.943  24.481  -6.744  1.00 57.57           C  
ANISOU 2493  CD2 LEU A 188     5448   9328   7099    618    440   1031       C  
ATOM   2494  H   LEU A 188     -25.519  25.342  -7.739  1.00 69.74           H  
ATOM   2495  HA  LEU A 188     -24.318  26.133  -5.430  1.00 69.40           H  
ATOM   2496  HB2 LEU A 188     -23.092  25.943  -7.965  1.00 70.77           H  
ATOM   2497  HB3 LEU A 188     -22.372  26.506  -6.675  1.00 70.77           H  
ATOM   2498  HG  LEU A 188     -22.735  24.204  -5.816  1.00 68.98           H  
ATOM   2499 HD11 LEU A 188     -22.629  22.578  -7.477  1.00 72.24           H  
ATOM   2500 HD12 LEU A 188     -23.969  23.421  -7.614  1.00 72.24           H  
ATOM   2501 HD13 LEU A 188     -22.748  23.708  -8.588  1.00 72.24           H  
ATOM   2502 HD21 LEU A 188     -20.617  23.587  -6.554  1.00 69.08           H  
ATOM   2503 HD22 LEU A 188     -20.651  24.760  -7.626  1.00 69.08           H  
ATOM   2504 HD23 LEU A 188     -20.616  25.102  -6.074  1.00 69.08           H  
ATOM   2505  N   ILE A 189     -24.776  28.501  -5.712  1.00 60.29           N  
ANISOU 2505  N   ILE A 189     5483  10107   7316   1413    466    530       N  
ATOM   2506  CA  ILE A 189     -24.977  29.934  -5.880  1.00 59.93           C  
ANISOU 2506  CA  ILE A 189     5485   9908   7379   1639    376    350       C  
ATOM   2507  C   ILE A 189     -23.846  30.632  -5.138  1.00 63.59           C  
ANISOU 2507  C   ILE A 189     6084  10174   7904   1698    279    182       C  
ATOM   2508  O   ILE A 189     -23.685  30.442  -3.926  1.00 65.34           O  
ANISOU 2508  O   ILE A 189     6272  10584   7972   1753    302     77       O  
ATOM   2509  CB  ILE A 189     -26.349  30.396  -5.359  1.00 62.04           C  
ANISOU 2509  CB  ILE A 189     5593  10483   7494   1877    407    229       C  
ATOM   2510  CG1 ILE A 189     -27.471  29.606  -6.046  1.00 63.71           C  
ANISOU 2510  CG1 ILE A 189     5651  10921   7633   1785    503    418       C  
ATOM   2511  CG2 ILE A 189     -26.532  31.889  -5.603  1.00 63.83           C  
ANISOU 2511  CG2 ILE A 189     5894  10501   7859   2128    277     31       C  
ATOM   2512  CD1 ILE A 189     -28.868  29.875  -5.489  1.00 65.79           C  
ANISOU 2512  CD1 ILE A 189     5712  11580   7706   1997    555    335       C  
ATOM   2513  H   ILE A 189     -24.692  28.262  -4.890  1.00 72.34           H  
ATOM   2514  HA  ILE A 189     -24.914  30.161  -6.820  1.00 71.92           H  
ATOM   2515  HB  ILE A 189     -26.392  30.229  -4.404  1.00 74.44           H  
ATOM   2516 HG12 ILE A 189     -27.481  29.837  -6.988  1.00 76.45           H  
ATOM   2517 HG13 ILE A 189     -27.291  28.659  -5.944  1.00 76.45           H  
ATOM   2518 HG21 ILE A 189     -27.402  32.159  -5.269  1.00 76.60           H  
ATOM   2519 HG22 ILE A 189     -25.833  32.373  -5.137  1.00 76.60           H  
ATOM   2520 HG23 ILE A 189     -26.476  32.062  -6.556  1.00 76.60           H  
ATOM   2521 HD11 ILE A 189     -29.511  29.338  -5.978  1.00 78.95           H  
ATOM   2522 HD12 ILE A 189     -28.884  29.636  -4.549  1.00 78.95           H  
ATOM   2523 HD13 ILE A 189     -29.074  30.817  -5.595  1.00 78.95           H  
ATOM   2524  N   GLY A 190     -23.055  31.424  -5.864  1.00 63.59           N  
ANISOU 2524  N   GLY A 190     6226   9811   8125   1676    163    172       N  
ATOM   2525  CA  GLY A 190     -21.883  32.047  -5.295  1.00 61.69           C  
ANISOU 2525  CA  GLY A 190     6117   9348   7973   1685     49     48       C  
ATOM   2526  C   GLY A 190     -21.840  33.534  -5.588  1.00 65.10           C  
ANISOU 2526  C   GLY A 190     6648   9486   8600   1846   -128    -91       C  
ATOM   2527  O   GLY A 190     -22.540  34.046  -6.462  1.00 63.74           O  
ANISOU 2527  O   GLY A 190     6460   9232   8525   1915   -163    -48       O  
ATOM   2528  H   GLY A 190     -23.184  31.611  -6.694  1.00 76.31           H  
ATOM   2529  HA2 GLY A 190     -21.882  31.921  -4.334  1.00 74.02           H  
ATOM   2530  HA3 GLY A 190     -21.085  31.636  -5.663  1.00 74.02           H  
ATOM   2531  N   MET A 191     -20.993  34.220  -4.829  1.00 68.46           N  
ANISOU 2531  N   MET A 191     7180   9743   9090   1900   -260   -257       N  
ATOM   2532  CA  MET A 191     -20.779  35.647  -4.992  1.00 71.53           C  
ANISOU 2532  CA  MET A 191     7689   9794   9693   2031   -480   -393       C  
ATOM   2533  C   MET A 191     -19.610  35.899  -5.938  1.00 70.55           C  
ANISOU 2533  C   MET A 191     7674   9331   9800   1794   -575   -200       C  
ATOM   2534  O   MET A 191     -18.751  35.040  -6.151  1.00 68.79           O  
ANISOU 2534  O   MET A 191     7445   9145   9546   1568   -485    -34       O  
ATOM   2535  CB  MET A 191     -20.511  36.308  -3.638  1.00 75.31           C  
ANISOU 2535  CB  MET A 191     8225  10266  10122   2227   -607   -695       C  
ATOM   2536  CG  MET A 191     -21.695  36.239  -2.675  1.00 76.15           C  
ANISOU 2536  CG  MET A 191     8203  10749   9980   2509   -534   -909       C  
ATOM   2537  SD  MET A 191     -21.340  36.835  -1.005  1.00 79.98           S  
ANISOU 2537  SD  MET A 191     8729  11315  10344   2755   -664  -1279       S  
ATOM   2538  CE  MET A 191     -20.695  38.473  -1.335  1.00 80.80           C  
ANISOU 2538  CE  MET A 191     9055  10847  10797   2848  -1010  -1444       C  
ATOM   2539  H   MET A 191     -20.522  33.871  -4.200  1.00 82.15           H  
ATOM   2540  HA  MET A 191     -21.580  36.046  -5.367  1.00 85.83           H  
ATOM   2541  HB2 MET A 191     -19.759  35.863  -3.217  1.00 90.37           H  
ATOM   2542  HB3 MET A 191     -20.301  37.244  -3.783  1.00 90.37           H  
ATOM   2543  HG2 MET A 191     -22.417  36.779  -3.032  1.00 91.37           H  
ATOM   2544  HG3 MET A 191     -21.982  35.315  -2.602  1.00 91.37           H  
ATOM   2545  HE1 MET A 191     -20.466  38.897  -0.493  1.00 96.96           H  
ATOM   2546  HE2 MET A 191     -19.905  38.395  -1.892  1.00 96.96           H  
ATOM   2547  HE3 MET A 191     -21.374  38.993  -1.793  1.00 96.96           H  
ATOM   2548  N   GLU A 192     -19.591  37.100  -6.512  1.00 76.68           N  
ANISOU 2548  N   GLU A 192     8542   9788  10804   1854   -772   -214       N  
ATOM   2549  CA  GLU A 192     -18.512  37.475  -7.414  1.00 76.23           C  
ANISOU 2549  CA  GLU A 192     8567   9430  10968   1626   -884     -5       C  
ATOM   2550  C   GLU A 192     -17.180  37.419  -6.680  1.00 74.28           C  
ANISOU 2550  C   GLU A 192     8389   9093  10742   1495   -950    -47       C  
ATOM   2551  O   GLU A 192     -17.060  37.898  -5.548  1.00 75.88           O  
ANISOU 2551  O   GLU A 192     8651   9255  10924   1642  -1060   -300       O  
ATOM   2552  CB  GLU A 192     -18.755  38.876  -7.975  1.00 79.51           C  
ANISOU 2552  CB  GLU A 192     9075   9502  11634   1722  -1125    -21       C  
ATOM   2553  CG  GLU A 192     -18.653  39.993  -6.946  1.00 82.17           C  
ANISOU 2553  CG  GLU A 192     9533   9614  12073   1925  -1371   -319       C  
ATOM   2554  CD  GLU A 192     -19.106  41.329  -7.497  1.00 86.22           C  
ANISOU 2554  CD  GLU A 192    10142   9784  12834   2058  -1629   -349       C  
ATOM   2555  OE1 GLU A 192     -19.776  41.339  -8.552  1.00 85.47           O  
ANISOU 2555  OE1 GLU A 192     9994   9701  12780   2047  -1577   -171       O  
ATOM   2556  OE2 GLU A 192     -18.790  42.368  -6.878  1.00 90.39           O  
ANISOU 2556  OE2 GLU A 192    10803  10018  13521   2176  -1901   -551       O  
ATOM   2557  H   GLU A 192     -20.187  37.709  -6.396  1.00 92.01           H  
ATOM   2558  HA  GLU A 192     -18.479  36.850  -8.155  1.00 91.48           H  
ATOM   2559  HB2 GLU A 192     -18.098  39.051  -8.667  1.00 95.41           H  
ATOM   2560  HB3 GLU A 192     -19.647  38.907  -8.356  1.00 95.41           H  
ATOM   2561  HG2 GLU A 192     -19.213  39.776  -6.184  1.00 98.60           H  
ATOM   2562  HG3 GLU A 192     -17.729  40.082  -6.664  1.00 98.60           H  
ATOM   2563  N   GLY A 193     -16.180  36.827  -7.328  1.00 70.65           N  
ANISOU 2563  N   GLY A 193     7912   8624  10309   1234   -888    192       N  
ATOM   2564  CA  GLY A 193     -14.875  36.660  -6.732  1.00 70.22           C  
ANISOU 2564  CA  GLY A 193     7901   8520  10260   1091   -933    185       C  
ATOM   2565  C   GLY A 193     -14.672  35.353  -5.998  1.00 69.88           C  
ANISOU 2565  C   GLY A 193     7793   8784   9975   1057   -736    151       C  
ATOM   2566  O   GLY A 193     -13.524  35.007  -5.692  1.00 68.52           O  
ANISOU 2566  O   GLY A 193     7638   8606   9791    911   -743    195       O  
ATOM   2567  H   GLY A 193     -16.241  36.511  -8.125  1.00 84.78           H  
ATOM   2568  HA2 GLY A 193     -14.202  36.720  -7.427  1.00 84.26           H  
ATOM   2569  HA3 GLY A 193     -14.722  37.383  -6.103  1.00 84.26           H  
ATOM   2570  N   ASN A 194     -15.742  34.619  -5.699  1.00 69.87           N  
ANISOU 2570  N   ASN A 194     7712   9053   9784   1179   -574     90       N  
ATOM   2571  CA  ASN A 194     -15.598  33.341  -5.015  1.00 66.24           C  
ANISOU 2571  CA  ASN A 194     7189   8875   9104   1129   -406     93       C  
ATOM   2572  C   ASN A 194     -14.655  32.427  -5.786  1.00 61.14           C  
ANISOU 2572  C   ASN A 194     6525   8245   8459    897   -329    325       C  
ATOM   2573  O   ASN A 194     -14.710  32.345  -7.016  1.00 60.54           O  
ANISOU 2573  O   ASN A 194     6423   8117   8462    807   -309    508       O  
ATOM   2574  CB  ASN A 194     -16.962  32.671  -4.853  1.00 61.78           C  
ANISOU 2574  CB  ASN A 194     6520   8596   8359   1247   -255     71       C  
ATOM   2575  CG  ASN A 194     -17.732  33.204  -3.666  1.00 63.04           C  
ANISOU 2575  CG  ASN A 194     6658   8887   8407   1494   -289   -189       C  
ATOM   2576  OD1 ASN A 194     -17.439  34.285  -3.158  1.00 64.95           O  
ANISOU 2576  OD1 ASN A 194     6984   8946   8748   1618   -457   -380       O  
ATOM   2577  ND2 ASN A 194     -18.720  32.443  -3.212  1.00 63.74           N  
ANISOU 2577  ND2 ASN A 194     6625   9308   8283   1569   -144   -198       N  
ATOM   2578  H   ASN A 194     -16.553  34.837  -5.881  1.00 83.85           H  
ATOM   2579  HA  ASN A 194     -15.225  33.489  -4.132  1.00 79.49           H  
ATOM   2580  HB2 ASN A 194     -17.491  32.831  -5.651  1.00 74.14           H  
ATOM   2581  HB3 ASN A 194     -16.834  31.718  -4.725  1.00 74.14           H  
ATOM   2582 HD21 ASN A 194     -19.188  32.702  -2.538  1.00 76.48           H  
ATOM   2583 HD22 ASN A 194     -18.892  31.691  -3.591  1.00 76.48           H  
ATOM   2584  N   VAL A 195     -13.779  31.743  -5.053  1.00 56.11           N  
ANISOU 2584  N   VAL A 195     5897   7698   7724    817   -294    306       N  
ATOM   2585  CA  VAL A 195     -12.799  30.830  -5.632  1.00 54.40           C  
ANISOU 2585  CA  VAL A 195     5663   7521   7485    632   -235    488       C  
ATOM   2586  C   VAL A 195     -12.981  29.463  -4.987  1.00 51.30           C  
ANISOU 2586  C   VAL A 195     5227   7375   6888    623    -99    488       C  
ATOM   2587  O   VAL A 195     -12.922  29.336  -3.757  1.00 53.81           O  
ANISOU 2587  O   VAL A 195     5554   7793   7098    685    -95    352       O  
ATOM   2588  CB  VAL A 195     -11.359  31.335  -5.436  1.00 56.05           C  
ANISOU 2588  CB  VAL A 195     5926   7578   7795    523   -355    494       C  
ATOM   2589  CG1 VAL A 195     -10.361  30.374  -6.072  1.00 53.26           C  
ANISOU 2589  CG1 VAL A 195     5532   7311   7394    364   -291    673       C  
ATOM   2590  CG2 VAL A 195     -11.195  32.736  -6.019  1.00 58.02           C  
ANISOU 2590  CG2 VAL A 195     6220   7558   8268    508   -526    519       C  
ATOM   2591  H   VAL A 195     -13.734  31.793  -4.195  1.00 67.33           H  
ATOM   2592  HA  VAL A 195     -12.965  30.743  -6.584  1.00 65.28           H  
ATOM   2593  HB  VAL A 195     -11.167  31.382  -4.487  1.00 67.27           H  
ATOM   2594 HG11 VAL A 195      -9.464  30.715  -5.934  1.00 63.91           H  
ATOM   2595 HG12 VAL A 195     -10.452  29.503  -5.654  1.00 63.91           H  
ATOM   2596 HG13 VAL A 195     -10.549  30.307  -7.021  1.00 63.91           H  
ATOM   2597 HG21 VAL A 195     -10.280  33.029  -5.883  1.00 69.63           H  
ATOM   2598 HG22 VAL A 195     -11.395  32.708  -6.968  1.00 69.63           H  
ATOM   2599 HG23 VAL A 195     -11.807  33.339  -5.569  1.00 69.63           H  
ATOM   2600  N   THR A 196     -13.202  28.443  -5.815  1.00 46.81           N  
ANISOU 2600  N   THR A 196     4612   6905   6269    546     -6    645       N  
ATOM   2601  CA  THR A 196     -13.176  27.064  -5.358  1.00 47.32           C  
ANISOU 2601  CA  THR A 196     4653   7151   6176    498     81    687       C  
ATOM   2602  C   THR A 196     -11.796  26.502  -5.662  1.00 47.38           C  
ANISOU 2602  C   THR A 196     4688   7121   6193    381     57    769       C  
ATOM   2603  O   THR A 196     -11.458  26.337  -6.844  1.00 46.92           O  
ANISOU 2603  O   THR A 196     4613   7020   6194    319     51    891       O  
ATOM   2604  CB  THR A 196     -14.258  26.238  -6.053  1.00 47.81           C  
ANISOU 2604  CB  THR A 196     4655   7324   6185    489    162    793       C  
ATOM   2605  OG1 THR A 196     -15.542  26.825  -5.809  1.00 49.59           O  
ANISOU 2605  OG1 THR A 196     4834   7613   6395    607    185    720       O  
ATOM   2606  CG2 THR A 196     -14.261  24.813  -5.533  1.00 46.87           C  
ANISOU 2606  CG2 THR A 196     4523   7359   5927    424    213    851       C  
ATOM   2607  H   THR A 196     -13.370  28.530  -6.654  1.00 56.17           H  
ATOM   2608  HA  THR A 196     -13.324  27.031  -4.400  1.00 56.78           H  
ATOM   2609  HB  THR A 196     -14.087  26.218  -7.008  1.00 57.37           H  
ATOM   2610  HG1 THR A 196     -16.140  26.375  -6.189  1.00 59.51           H  
ATOM   2611 HG21 THR A 196     -14.951  24.298  -5.981  1.00 56.25           H  
ATOM   2612 HG22 THR A 196     -13.400  24.397  -5.698  1.00 56.25           H  
ATOM   2613 HG23 THR A 196     -14.435  24.809  -4.578  1.00 56.25           H  
ATOM   2614  N   PRO A 197     -10.963  26.208  -4.660  1.00 48.61           N  
ANISOU 2614  N   PRO A 197     4874   7317   6279    360     39    706       N  
ATOM   2615  CA  PRO A 197      -9.573  25.833  -4.946  1.00 47.35           C  
ANISOU 2615  CA  PRO A 197     4730   7129   6131    267      2    771       C  
ATOM   2616  C   PRO A 197      -9.473  24.555  -5.765  1.00 47.15           C  
ANISOU 2616  C   PRO A 197     4684   7184   6046    221     46    896       C  
ATOM   2617  O   PRO A 197     -10.418  23.770  -5.875  1.00 44.50           O  
ANISOU 2617  O   PRO A 197     4335   6922   5650    237     96    932       O  
ATOM   2618  CB  PRO A 197      -8.955  25.644  -3.554  1.00 50.69           C  
ANISOU 2618  CB  PRO A 197     5185   7613   6463    276    -17    665       C  
ATOM   2619  CG  PRO A 197      -9.850  26.364  -2.628  1.00 53.68           C  
ANISOU 2619  CG  PRO A 197     5567   8013   6816    383    -18    521       C  
ATOM   2620  CD  PRO A 197     -11.221  26.269  -3.212  1.00 50.81           C  
ANISOU 2620  CD  PRO A 197     5160   7695   6450    434     46    567       C  
ATOM   2621  HA  PRO A 197      -9.115  26.552  -5.409  1.00 56.82           H  
ATOM   2622  HB2 PRO A 197      -8.926  24.699  -3.336  1.00 60.83           H  
ATOM   2623  HB3 PRO A 197      -8.065  26.028  -3.538  1.00 60.83           H  
ATOM   2624  HG2 PRO A 197      -9.822  25.940  -1.756  1.00 64.42           H  
ATOM   2625  HG3 PRO A 197      -9.572  27.291  -2.564  1.00 64.42           H  
ATOM   2626  HD2 PRO A 197     -11.663  25.459  -2.911  1.00 60.97           H  
ATOM   2627  HD3 PRO A 197     -11.739  27.060  -2.992  1.00 60.97           H  
ATOM   2628  N   ALA A 198      -8.287  24.347  -6.334  1.00 46.38           N  
ANISOU 2628  N   ALA A 198     4577   7081   5963    166      9    959       N  
ATOM   2629  CA  ALA A 198      -8.051  23.180  -7.170  1.00 42.22           C  
ANISOU 2629  CA  ALA A 198     4034   6631   5377    157     22   1045       C  
ATOM   2630  C   ALA A 198      -8.263  21.899  -6.372  1.00 45.14           C  
ANISOU 2630  C   ALA A 198     4446   7070   5635    168     33   1023       C  
ATOM   2631  O   ALA A 198      -7.687  21.715  -5.296  1.00 41.16           O  
ANISOU 2631  O   ALA A 198     3973   6594   5074    160     18    969       O  
ATOM   2632  CB  ALA A 198      -6.638  23.221  -7.747  1.00 39.45           C  
ANISOU 2632  CB  ALA A 198     3646   6315   5029    123    -23   1096       C  
ATOM   2633  H   ALA A 198      -7.607  24.867  -6.250  1.00 55.66           H  
ATOM   2634  HA  ALA A 198      -8.680  23.184  -7.909  1.00 50.67           H  
ATOM   2635  HB1 ALA A 198      -6.500  22.437  -8.300  1.00 47.34           H  
ATOM   2636  HB2 ALA A 198      -6.539  24.025  -8.281  1.00 47.34           H  
ATOM   2637  HB3 ALA A 198      -5.999  23.228  -7.017  1.00 47.34           H  
ATOM   2638  N   HIS A 199      -9.099  21.016  -6.911  1.00 44.15           N  
ANISOU 2638  N   HIS A 199     4322   6968   5485    177     44   1076       N  
ATOM   2639  CA  HIS A 199      -9.425  19.745  -6.282  1.00 40.11           C  
ANISOU 2639  CA  HIS A 199     3850   6498   4891    162     25   1096       C  
ATOM   2640  C   HIS A 199      -9.916  18.809  -7.374  1.00 42.09           C  
ANISOU 2640  C   HIS A 199     4105   6735   5152    168    -13   1160       C  
ATOM   2641  O   HIS A 199     -10.263  19.249  -8.473  1.00 49.54           O  
ANISOU 2641  O   HIS A 199     5007   7665   6149    191      3   1180       O  
ATOM   2642  CB  HIS A 199     -10.495  19.915  -5.201  1.00 46.03           C  
ANISOU 2642  CB  HIS A 199     4588   7303   5599    148     74   1083       C  
ATOM   2643  CG  HIS A 199     -11.855  20.217  -5.752  1.00 42.88           C  
ANISOU 2643  CG  HIS A 199     4140   6917   5236    158    118   1116       C  
ATOM   2644  ND1 HIS A 199     -12.263  21.493  -6.076  1.00 43.02           N  
ANISOU 2644  ND1 HIS A 199     4121   6902   5324    206    156   1068       N  
ATOM   2645  CD2 HIS A 199     -12.893  19.403  -6.056  1.00 42.04           C  
ANISOU 2645  CD2 HIS A 199     4013   6847   5112    123    114   1199       C  
ATOM   2646  CE1 HIS A 199     -13.497  21.454  -6.545  1.00 45.15           C  
ANISOU 2646  CE1 HIS A 199     4345   7206   5605    215    188   1112       C  
ATOM   2647  NE2 HIS A 199     -13.903  20.198  -6.544  1.00 46.57           N  
ANISOU 2647  NE2 HIS A 199     4528   7435   5730    157    167   1194       N  
ATOM   2648  H   HIS A 199      -9.501  21.137  -7.662  1.00 52.98           H  
ATOM   2649  HA  HIS A 199      -8.629  19.364  -5.878  1.00 48.13           H  
ATOM   2650  HB2 HIS A 199     -10.557  19.094  -4.688  1.00 55.24           H  
ATOM   2651  HB3 HIS A 199     -10.240  20.649  -4.620  1.00 55.24           H  
ATOM   2652  HD1 HIS A 199     -11.789  22.205  -5.982  1.00 51.62           H  
ATOM   2653  HD2 HIS A 199     -12.920  18.480  -5.950  1.00 50.44           H  
ATOM   2654  HE1 HIS A 199     -13.995  22.186  -6.828  1.00 54.18           H  
ATOM   2655  N   TYR A 200      -9.953  17.515  -7.065  1.00 41.70           N  
ANISOU 2655  N   TYR A 200     4107   6682   5054    148    -82   1192       N  
ATOM   2656  CA  TYR A 200     -10.527  16.536  -7.975  1.00 49.27           C  
ANISOU 2656  CA  TYR A 200     5086   7603   6032    151   -155   1238       C  
ATOM   2657  C   TYR A 200     -11.645  15.771  -7.279  1.00 51.78           C  
ANISOU 2657  C   TYR A 200     5419   7921   6333     65   -182   1320       C  
ATOM   2658  O   TYR A 200     -11.607  15.542  -6.066  1.00 52.65           O  
ANISOU 2658  O   TYR A 200     5543   8073   6389     14   -177   1350       O  
ATOM   2659  CB  TYR A 200      -9.467  15.557  -8.509  1.00 45.28           C  
ANISOU 2659  CB  TYR A 200     4636   7067   5502    218   -271   1204       C  
ATOM   2660  CG  TYR A 200      -8.904  14.602  -7.487  1.00 38.99           C  
ANISOU 2660  CG  TYR A 200     3916   6241   4658    198   -356   1211       C  
ATOM   2661  CD1 TYR A 200      -7.817  14.960  -6.704  1.00 45.73           C  
ANISOU 2661  CD1 TYR A 200     4771   7141   5465    215   -329   1168       C  
ATOM   2662  CD2 TYR A 200      -9.445  13.335  -7.320  1.00 39.49           C  
ANISOU 2662  CD2 TYR A 200     4051   6223   4732    156   -482   1271       C  
ATOM   2663  CE1 TYR A 200      -7.291  14.090  -5.775  1.00 40.84           C  
ANISOU 2663  CE1 TYR A 200     4220   6502   4797    203   -410   1181       C  
ATOM   2664  CE2 TYR A 200      -8.927  12.456  -6.393  1.00 42.65           C  
ANISOU 2664  CE2 TYR A 200     4525   6584   5098    133   -578   1299       C  
ATOM   2665  CZ  TYR A 200      -7.848  12.838  -5.623  1.00 44.08           C  
ANISOU 2665  CZ  TYR A 200     4704   6826   5219    164   -535   1251       C  
ATOM   2666  OH  TYR A 200      -7.324  11.969  -4.697  1.00 44.52           O  
ANISOU 2666  OH  TYR A 200     4830   6850   5234    148   -633   1286       O  
ATOM   2667  H   TYR A 200      -9.650  17.181  -6.333  1.00 50.04           H  
ATOM   2668  HA  TYR A 200     -10.912  17.002  -8.734  1.00 59.13           H  
ATOM   2669  HB2 TYR A 200      -9.867  15.027  -9.216  1.00 54.34           H  
ATOM   2670  HB3 TYR A 200      -8.727  16.071  -8.868  1.00 54.34           H  
ATOM   2671  HD1 TYR A 200      -7.440  15.803  -6.805  1.00 54.88           H  
ATOM   2672  HD2 TYR A 200     -10.172  13.077  -7.839  1.00 47.39           H  
ATOM   2673  HE1 TYR A 200      -6.564  14.345  -5.254  1.00 49.01           H  
ATOM   2674  HE2 TYR A 200      -9.301  11.611  -6.289  1.00 51.19           H  
ATOM   2675  HH  TYR A 200      -6.677  12.327  -4.300  1.00 53.42           H  
ATOM   2676  N   ASP A 201     -12.648  15.395  -8.064  1.00 46.58           N  
ANISOU 2676  N   ASP A 201     4744   7239   5717     42   -214   1370       N  
ATOM   2677  CA  ASP A 201     -13.765  14.590  -7.602  1.00 46.31           C  
ANISOU 2677  CA  ASP A 201     4705   7214   5677    -65   -263   1481       C  
ATOM   2678  C   ASP A 201     -13.676  13.205  -8.227  1.00 49.79           C  
ANISOU 2678  C   ASP A 201     5231   7529   6160    -80   -446   1511       C  
ATOM   2679  O   ASP A 201     -13.019  13.003  -9.252  1.00 49.61           O  
ANISOU 2679  O   ASP A 201     5246   7442   6160     22   -513   1424       O  
ATOM   2680  CB  ASP A 201     -15.108  15.239  -7.960  1.00 39.96           C  
ANISOU 2680  CB  ASP A 201     3805   6484   4893    -90   -178   1521       C  
ATOM   2681  CG  ASP A 201     -15.267  16.629  -7.370  1.00 45.58           C  
ANISOU 2681  CG  ASP A 201     4443   7300   5574    -43    -28   1466       C  
ATOM   2682  OD1 ASP A 201     -14.977  16.810  -6.171  1.00 45.44           O  
ANISOU 2682  OD1 ASP A 201     4422   7355   5488    -55      9   1455       O  
ATOM   2683  OD2 ASP A 201     -15.686  17.543  -8.108  1.00 46.36           O  
ANISOU 2683  OD2 ASP A 201     4492   7405   5717     15     35   1427       O  
ATOM   2684  H   ASP A 201     -12.702  15.603  -8.897  1.00 55.90           H  
ATOM   2685  HA  ASP A 201     -13.717  14.495  -6.638  1.00 55.57           H  
ATOM   2686  HB2 ASP A 201     -15.176  15.313  -8.924  1.00 47.95           H  
ATOM   2687  HB3 ASP A 201     -15.827  14.685  -7.619  1.00 47.95           H  
ATOM   2688  N   GLU A 202     -14.356  12.248  -7.601  1.00 57.06           N  
ANISOU 2688  N   GLU A 202     6172   8424   7084   -206   -543   1639       N  
ATOM   2689  CA  GLU A 202     -14.271  10.852  -8.003  1.00 57.48           C  
ANISOU 2689  CA  GLU A 202     6330   8314   7197   -235   -765   1674       C  
ATOM   2690  C   GLU A 202     -15.448  10.409  -8.863  1.00 59.61           C  
ANISOU 2690  C   GLU A 202     6578   8532   7538   -302   -853   1734       C  
ATOM   2691  O   GLU A 202     -15.569   9.217  -9.160  1.00 59.99           O  
ANISOU 2691  O   GLU A 202     6716   8422   7655   -348  -1072   1773       O  
ATOM   2692  CB  GLU A 202     -14.160   9.963  -6.764  1.00 56.52           C  
ANISOU 2692  CB  GLU A 202     6260   8162   7053   -355   -867   1805       C  
ATOM   2693  CG  GLU A 202     -12.983  10.317  -5.867  1.00 53.68           C  
ANISOU 2693  CG  GLU A 202     5923   7857   6615   -290   -796   1744       C  
ATOM   2694  CD  GLU A 202     -12.721   9.269  -4.808  1.00 53.90           C  
ANISOU 2694  CD  GLU A 202     6023   7832   6627   -387   -935   1872       C  
ATOM   2695  OE1 GLU A 202     -13.249   9.414  -3.686  1.00 60.29           O  
ANISOU 2695  OE1 GLU A 202     6758   8786   7364   -507   -861   2009       O  
ATOM   2696  OE2 GLU A 202     -11.996   8.295  -5.101  1.00 52.26           O  
ANISOU 2696  OE2 GLU A 202     5938   7449   6469   -333  -1129   1836       O  
ATOM   2697  H   GLU A 202     -14.878  12.386  -6.932  1.00 68.47           H  
ATOM   2698  HA  GLU A 202     -13.464  10.729  -8.526  1.00 68.98           H  
ATOM   2699  HB2 GLU A 202     -14.971  10.052  -6.240  1.00 67.83           H  
ATOM   2700  HB3 GLU A 202     -14.050   9.041  -7.048  1.00 67.83           H  
ATOM   2701  HG2 GLU A 202     -12.184  10.400  -6.411  1.00 64.41           H  
ATOM   2702  HG3 GLU A 202     -13.169  11.157  -5.419  1.00 64.41           H  
ATOM   2703  N   GLN A 203     -16.305  11.337  -9.282  1.00 64.46           N  
ANISOU 2703  N   GLN A 203     7081   9264   8147   -302   -708   1737       N  
ATOM   2704  CA  GLN A 203     -17.471  11.015 -10.089  1.00 58.25           C  
ANISOU 2704  CA  GLN A 203     6255   8457   7421   -366   -777   1795       C  
ATOM   2705  C   GLN A 203     -17.465  11.862 -11.355  1.00 54.50           C  
ANISOU 2705  C   GLN A 203     5737   8016   6956   -226   -691   1670       C  
ATOM   2706  O   GLN A 203     -16.824  12.915 -11.422  1.00 51.10           O  
ANISOU 2706  O   GLN A 203     5273   7657   6485   -119   -544   1584       O  
ATOM   2707  CB  GLN A 203     -18.774  11.241  -9.304  1.00 58.97           C  
ANISOU 2707  CB  GLN A 203     6221   8705   7480   -523   -692   1963       C  
ATOM   2708  CG  GLN A 203     -18.878  10.413  -8.034  1.00 61.56           C  
ANISOU 2708  CG  GLN A 203     6561   9052   7778   -685   -774   2134       C  
ATOM   2709  CD  GLN A 203     -20.255  10.485  -7.398  1.00 65.59           C  
ANISOU 2709  CD  GLN A 203     6917   9767   8239   -848   -714   2326       C  
ATOM   2710  OE1 GLN A 203     -21.149  11.169  -7.897  1.00 64.07           O  
ANISOU 2710  OE1 GLN A 203     6613   9695   8037   -827   -610   2315       O  
ATOM   2711  NE2 GLN A 203     -20.434   9.769  -6.292  1.00 68.37           N  
ANISOU 2711  NE2 GLN A 203     7248  10181   8549  -1011   -784   2517       N  
ATOM   2712  H   GLN A 203     -16.228  12.175  -9.106  1.00 77.35           H  
ATOM   2713  HA  GLN A 203     -17.432  10.081 -10.348  1.00 69.90           H  
ATOM   2714  HB2 GLN A 203     -18.829  12.176  -9.053  1.00 70.77           H  
ATOM   2715  HB3 GLN A 203     -19.525  11.008  -9.872  1.00 70.77           H  
ATOM   2716  HG2 GLN A 203     -18.693   9.485  -8.246  1.00 73.88           H  
ATOM   2717  HG3 GLN A 203     -18.232  10.741  -7.389  1.00 73.88           H  
ATOM   2718 HE21 GLN A 203     -19.788   9.299  -5.975  1.00 82.05           H  
ATOM   2719 HE22 GLN A 203     -21.197   9.777  -5.894  1.00 82.05           H  
ATOM   2720  N   GLN A 204     -18.174  11.372 -12.370  1.00 52.77           N  
ANISOU 2720  N   GLN A 204     5517   7740   6794   -236   -803   1672       N  
ATOM   2721  CA  GLN A 204     -18.362  12.134 -13.597  1.00 49.08           C  
ANISOU 2721  CA  GLN A 204     4990   7332   6327   -118   -727   1584       C  
ATOM   2722  C   GLN A 204     -19.325  13.286 -13.343  1.00 47.09           C  
ANISOU 2722  C   GLN A 204     4604   7234   6054   -157   -535   1651       C  
ATOM   2723  O   GLN A 204     -20.317  13.137 -12.626  1.00 46.44           O  
ANISOU 2723  O   GLN A 204     4459   7220   5968   -290   -519   1774       O  
ATOM   2724  CB  GLN A 204     -18.904  11.234 -14.709  1.00 49.73           C  
ANISOU 2724  CB  GLN A 204     5107   7321   6468   -114   -917   1558       C  
ATOM   2725  CG  GLN A 204     -18.103   9.956 -14.957  1.00 51.80           C  
ANISOU 2725  CG  GLN A 204     5513   7406   6761    -58  -1161   1473       C  
ATOM   2726  CD  GLN A 204     -16.817  10.196 -15.732  1.00 52.25           C  
ANISOU 2726  CD  GLN A 204     5602   7495   6755    163  -1150   1298       C  
ATOM   2727  OE1 GLN A 204     -16.430  11.338 -15.980  1.00 49.38           O  
ANISOU 2727  OE1 GLN A 204     5153   7277   6331    244   -958   1269       O  
ATOM   2728  NE2 GLN A 204     -16.151   9.112 -16.120  1.00 50.59           N  
ANISOU 2728  NE2 GLN A 204     5507   7158   6556    265  -1374   1185       N  
ATOM   2729  H   GLN A 204     -18.555  10.601 -12.372  1.00 63.33           H  
ATOM   2730  HA  GLN A 204     -17.511  12.500 -13.885  1.00 58.90           H  
ATOM   2731  HB2 GLN A 204     -19.809  10.971 -14.479  1.00 59.68           H  
ATOM   2732  HB3 GLN A 204     -18.913  11.739 -15.537  1.00 59.68           H  
ATOM   2733  HG2 GLN A 204     -17.867   9.562 -14.103  1.00 62.16           H  
ATOM   2734  HG3 GLN A 204     -18.648   9.337 -15.468  1.00 62.16           H  
ATOM   2735 HE21 GLN A 204     -16.454   8.330 -15.931  1.00 60.70           H  
ATOM   2736 HE22 GLN A 204     -15.418   9.194 -16.562  1.00 60.70           H  
ATOM   2737  N   ASN A 205     -19.033  14.442 -13.938  1.00 47.82           N  
ANISOU 2737  N   ASN A 205     4646   7394   6129    -36   -401   1576       N  
ATOM   2738  CA  ASN A 205     -19.785  15.657 -13.649  1.00 49.89           C  
ANISOU 2738  CA  ASN A 205     4801   7778   6378    -34   -235   1610       C  
ATOM   2739  C   ASN A 205     -20.097  16.411 -14.930  1.00 48.88           C  
ANISOU 2739  C   ASN A 205     4615   7684   6274     62   -190   1575       C  
ATOM   2740  O   ASN A 205     -19.195  16.700 -15.722  1.00 44.83           O  
ANISOU 2740  O   ASN A 205     4127   7148   5757    163   -194   1508       O  
ATOM   2741  CB  ASN A 205     -19.009  16.575 -12.698  1.00 47.07           C  
ANISOU 2741  CB  ASN A 205     4447   7451   5986      8   -115   1569       C  
ATOM   2742  CG  ASN A 205     -19.707  17.904 -12.474  1.00 46.95           C  
ANISOU 2742  CG  ASN A 205     4337   7533   5967     53     25   1565       C  
ATOM   2743  OD1 ASN A 205     -20.892  18.059 -12.773  1.00 49.16           O  
ANISOU 2743  OD1 ASN A 205     4535   7890   6254     37     49   1613       O  
ATOM   2744  ND2 ASN A 205     -18.975  18.871 -11.940  1.00 46.94           N  
ANISOU 2744  ND2 ASN A 205     4350   7525   5961    115    102   1501       N  
ATOM   2745  H   ASN A 205     -18.402  14.547 -14.513  1.00 57.38           H  
ATOM   2746  HA  ASN A 205     -20.624  15.419 -13.225  1.00 59.87           H  
ATOM   2747  HB2 ASN A 205     -18.917  16.135 -11.839  1.00 56.48           H  
ATOM   2748  HB3 ASN A 205     -18.134  16.755 -13.076  1.00 56.48           H  
ATOM   2749 HD21 ASN A 205     -19.323  19.643 -11.792  1.00 56.33           H  
ATOM   2750 HD22 ASN A 205     -18.151  18.726 -11.741  1.00 56.33           H  
ATOM   2751  N   PHE A 206     -21.375  16.738 -15.114  1.00 47.72           N  
ANISOU 2751  N   PHE A 206     4374   7619   6138     31   -148   1633       N  
ATOM   2752  CA  PHE A 206     -21.804  17.703 -16.115  1.00 41.39           C  
ANISOU 2752  CA  PHE A 206     3501   6870   5355    122    -79   1619       C  
ATOM   2753  C   PHE A 206     -22.102  19.014 -15.402  1.00 42.31           C  
ANISOU 2753  C   PHE A 206     3557   7053   5468    166     62   1618       C  
ATOM   2754  O   PHE A 206     -23.016  19.088 -14.574  1.00 39.89           O  
ANISOU 2754  O   PHE A 206     3183   6842   5132    120    107   1659       O  
ATOM   2755  CB  PHE A 206     -23.025  17.208 -16.886  1.00 45.79           C  
ANISOU 2755  CB  PHE A 206     3995   7475   5929     81   -144   1669       C  
ATOM   2756  CG  PHE A 206     -22.688  16.265 -18.002  1.00 43.28           C  
ANISOU 2756  CG  PHE A 206     3735   7086   5623    105   -295   1624       C  
ATOM   2757  CD1 PHE A 206     -21.859  16.665 -19.034  1.00 42.38           C  
ANISOU 2757  CD1 PHE A 206     3634   6977   5490    236   -290   1553       C  
ATOM   2758  CD2 PHE A 206     -23.207  14.982 -18.024  1.00 49.51           C  
ANISOU 2758  CD2 PHE A 206     4557   7817   6437      1   -457   1654       C  
ATOM   2759  CE1 PHE A 206     -21.545  15.804 -20.063  1.00 44.36           C  
ANISOU 2759  CE1 PHE A 206     3926   7205   5724    296   -433   1484       C  
ATOM   2760  CE2 PHE A 206     -22.898  14.114 -19.054  1.00 47.76           C  
ANISOU 2760  CE2 PHE A 206     4400   7519   6228     53   -625   1576       C  
ATOM   2761  CZ  PHE A 206     -22.067  14.525 -20.075  1.00 45.60           C  
ANISOU 2761  CZ  PHE A 206     4134   7280   5912    218   -607   1477       C  
ATOM   2762  H   PHE A 206     -22.024  16.405 -14.659  1.00 57.26           H  
ATOM   2763  HA  PHE A 206     -21.084  17.855 -16.746  1.00 49.67           H  
ATOM   2764  HB2 PHE A 206     -23.616  16.744 -16.273  1.00 54.95           H  
ATOM   2765  HB3 PHE A 206     -23.483  17.972 -17.271  1.00 54.95           H  
ATOM   2766  HD1 PHE A 206     -21.505  17.525 -19.031  1.00 50.85           H  
ATOM   2767  HD2 PHE A 206     -23.767  14.701 -17.337  1.00 59.41           H  
ATOM   2768  HE1 PHE A 206     -20.985  16.085 -20.751  1.00 53.23           H  
ATOM   2769  HE2 PHE A 206     -23.251  13.253 -19.059  1.00 57.31           H  
ATOM   2770  HZ  PHE A 206     -21.858  13.943 -20.769  1.00 54.72           H  
ATOM   2771  N   PHE A 207     -21.327  20.037 -15.732  1.00 42.19           N  
ANISOU 2771  N   PHE A 207     3557   6997   5478    258    115   1573       N  
ATOM   2772  CA  PHE A 207     -21.305  21.312 -15.024  1.00 41.77           C  
ANISOU 2772  CA  PHE A 207     3483   6946   5442    315    205   1541       C  
ATOM   2773  C   PHE A 207     -22.174  22.285 -15.816  1.00 41.07           C  
ANISOU 2773  C   PHE A 207     3319   6891   5397    394    242   1563       C  
ATOM   2774  O   PHE A 207     -21.733  22.846 -16.821  1.00 47.02           O  
ANISOU 2774  O   PHE A 207     4074   7598   6194    444    230   1582       O  
ATOM   2775  CB  PHE A 207     -19.854  21.772 -14.909  1.00 49.62           C  
ANISOU 2775  CB  PHE A 207     4548   7849   6457    341    203   1500       C  
ATOM   2776  CG  PHE A 207     -19.644  23.011 -14.089  1.00 44.62           C  
ANISOU 2776  CG  PHE A 207     3920   7175   5858    391    254   1449       C  
ATOM   2777  CD1 PHE A 207     -19.811  24.266 -14.646  1.00 47.34           C  
ANISOU 2777  CD1 PHE A 207     4237   7469   6279    464    265   1456       C  
ATOM   2778  CD2 PHE A 207     -19.214  22.917 -12.779  1.00 46.04           C  
ANISOU 2778  CD2 PHE A 207     4139   7355   5998    370    268   1392       C  
ATOM   2779  CE1 PHE A 207     -19.590  25.406 -13.896  1.00 51.59           C  
ANISOU 2779  CE1 PHE A 207     4800   7932   6869    518    271   1392       C  
ATOM   2780  CE2 PHE A 207     -18.991  24.049 -12.026  1.00 49.99           C  
ANISOU 2780  CE2 PHE A 207     4653   7810   6530    431    289   1317       C  
ATOM   2781  CZ  PHE A 207     -19.175  25.297 -12.585  1.00 50.67           C  
ANISOU 2781  CZ  PHE A 207     4724   7819   6708    508    281   1309       C  
ATOM   2782  H   PHE A 207     -20.779  20.015 -16.395  1.00 50.63           H  
ATOM   2783  HA  PHE A 207     -21.676  21.206 -14.134  1.00 50.12           H  
ATOM   2784  HB2 PHE A 207     -19.336  21.061 -14.501  1.00 59.55           H  
ATOM   2785  HB3 PHE A 207     -19.516  21.950 -15.800  1.00 59.55           H  
ATOM   2786  HD1 PHE A 207     -20.090  24.344 -15.530  1.00 56.80           H  
ATOM   2787  HD2 PHE A 207     -19.087  22.079 -12.396  1.00 55.25           H  
ATOM   2788  HE1 PHE A 207     -19.717  26.245 -14.276  1.00 61.90           H  
ATOM   2789  HE2 PHE A 207     -18.713  23.972 -11.141  1.00 59.98           H  
ATOM   2790  HZ  PHE A 207     -19.029  26.062 -12.077  1.00 60.80           H  
ATOM   2791  N   ALA A 208     -23.417  22.472 -15.376  1.00 42.22           N  
ANISOU 2791  N   ALA A 208     3384   7139   5519    407    282   1572       N  
ATOM   2792  CA  ALA A 208     -24.409  23.239 -16.127  1.00 47.57           C  
ANISOU 2792  CA  ALA A 208     3980   7866   6229    488    305   1594       C  
ATOM   2793  C   ALA A 208     -24.503  24.657 -15.570  1.00 45.35           C  
ANISOU 2793  C   ALA A 208     3691   7553   5987    609    348   1527       C  
ATOM   2794  O   ALA A 208     -25.085  24.875 -14.501  1.00 43.10           O  
ANISOU 2794  O   ALA A 208     3362   7365   5649    651    389   1473       O  
ATOM   2795  CB  ALA A 208     -25.772  22.552 -16.080  1.00 45.24           C  
ANISOU 2795  CB  ALA A 208     3581   7728   5878    438    306   1646       C  
ATOM   2796  H   ALA A 208     -23.715  22.159 -14.632  1.00 50.66           H  
ATOM   2797  HA  ALA A 208     -24.131  23.297 -17.055  1.00 57.08           H  
ATOM   2798  HB1 ALA A 208     -26.409  23.081 -16.584  1.00 54.28           H  
ATOM   2799  HB2 ALA A 208     -25.693  21.668 -16.470  1.00 54.28           H  
ATOM   2800  HB3 ALA A 208     -26.058  22.482 -15.155  1.00 54.28           H  
ATOM   2801  N   GLN A 209     -23.957  25.619 -16.310  1.00 43.29           N  
ANISOU 2801  N   GLN A 209     3466   7167   5814    672    324   1536       N  
ATOM   2802  CA  GLN A 209     -23.982  27.013 -15.891  1.00 46.98           C  
ANISOU 2802  CA  GLN A 209     3951   7546   6354    788    318   1472       C  
ATOM   2803  C   GLN A 209     -25.324  27.651 -16.233  1.00 50.53           C  
ANISOU 2803  C   GLN A 209     4313   8071   6816    904    329   1469       C  
ATOM   2804  O   GLN A 209     -25.894  27.403 -17.301  1.00 46.86           O  
ANISOU 2804  O   GLN A 209     3790   7662   6351    894    326   1554       O  
ATOM   2805  CB  GLN A 209     -22.845  27.787 -16.560  1.00 43.70           C  
ANISOU 2805  CB  GLN A 209     3604   6955   6044    778    261   1520       C  
ATOM   2806  CG  GLN A 209     -22.686  29.222 -16.070  1.00 46.78           C  
ANISOU 2806  CG  GLN A 209     4042   7190   6542    876    207   1456       C  
ATOM   2807  CD  GLN A 209     -22.238  29.292 -14.625  1.00 47.08           C  
ANISOU 2807  CD  GLN A 209     4136   7202   6552    892    208   1320       C  
ATOM   2808  OE1 GLN A 209     -21.897  28.276 -14.020  1.00 45.74           O  
ANISOU 2808  OE1 GLN A 209     3971   7124   6283    812    255   1301       O  
ATOM   2809  NE2 GLN A 209     -22.232  30.497 -14.065  1.00 48.27           N  
ANISOU 2809  NE2 GLN A 209     4332   7218   6789   1002    138   1222       N  
ATOM   2810  H   GLN A 209     -23.565  25.487 -17.064  1.00 51.94           H  
ATOM   2811  HA  GLN A 209     -23.858  27.061 -14.930  1.00 56.38           H  
ATOM   2812  HB2 GLN A 209     -22.010  27.323 -16.389  1.00 52.44           H  
ATOM   2813  HB3 GLN A 209     -23.011  27.818 -17.516  1.00 52.44           H  
ATOM   2814  HG2 GLN A 209     -22.020  29.670 -16.614  1.00 56.14           H  
ATOM   2815  HG3 GLN A 209     -23.538  29.678 -16.144  1.00 56.14           H  
ATOM   2816 HE21 GLN A 209     -22.474  31.184 -14.521  1.00 57.92           H  
ATOM   2817 HE22 GLN A 209     -21.985  30.589 -13.246  1.00 57.92           H  
ATOM   2818  N   ILE A 210     -25.818  28.493 -15.323  1.00 51.87           N  
ANISOU 2818  N   ILE A 210     4468   8253   6986   1035    331   1358       N  
ATOM   2819  CA  ILE A 210     -27.159  29.061 -15.427  1.00 56.89           C  
ANISOU 2819  CA  ILE A 210     5007   9003   7607   1179    342   1326       C  
ATOM   2820  C   ILE A 210     -27.094  30.583 -15.413  1.00 56.78           C  
ANISOU 2820  C   ILE A 210     5050   8808   7715   1347    260   1245       C  
ATOM   2821  O   ILE A 210     -27.541  31.240 -16.359  1.00 58.07           O  
ANISOU 2821  O   ILE A 210     5196   8906   7962   1417    215   1304       O  
ATOM   2822  CB  ILE A 210     -28.054  28.536 -14.289  1.00 58.44           C  
ANISOU 2822  CB  ILE A 210     5097   9456   7651   1213    411   1257       C  
ATOM   2823  CG1 ILE A 210     -28.335  27.047 -14.490  1.00 51.71           C  
ANISOU 2823  CG1 ILE A 210     4179   8761   6706   1029    455   1377       C  
ATOM   2824  CG2 ILE A 210     -29.368  29.312 -14.216  1.00 57.88           C  
ANISOU 2824  CG2 ILE A 210     4913   9531   7548   1408    418   1189       C  
ATOM   2825  CD1 ILE A 210     -28.886  26.370 -13.269  1.00 50.70           C  
ANISOU 2825  CD1 ILE A 210     3956   8880   6429    995    511   1362       C  
ATOM   2826  H   ILE A 210     -25.386  28.754 -14.626  1.00 62.24           H  
ATOM   2827  HA  ILE A 210     -27.553  28.786 -16.269  1.00 68.27           H  
ATOM   2828  HB  ILE A 210     -27.583  28.650 -13.449  1.00 70.13           H  
ATOM   2829 HG12 ILE A 210     -28.982  26.944 -15.205  1.00 62.05           H  
ATOM   2830 HG13 ILE A 210     -27.507  26.601 -14.729  1.00 62.05           H  
ATOM   2831 HG21 ILE A 210     -29.905  28.956 -13.491  1.00 69.46           H  
ATOM   2832 HG22 ILE A 210     -29.173  30.248 -14.055  1.00 69.46           H  
ATOM   2833 HG23 ILE A 210     -29.840  29.212 -15.058  1.00 69.46           H  
ATOM   2834 HD11 ILE A 210     -29.038  25.433 -13.470  1.00 60.84           H  
ATOM   2835 HD12 ILE A 210     -28.245  26.454 -12.546  1.00 60.84           H  
ATOM   2836 HD13 ILE A 210     -29.722  26.796 -13.023  1.00 60.84           H  
ATOM   2837  N   LYS A 211     -26.563  31.153 -14.334  1.00 55.34           N  
ANISOU 2837  N   LYS A 211     4938   8537   7550   1418    222   1108       N  
ATOM   2838  CA  LYS A 211     -26.464  32.597 -14.174  1.00 52.97           C  
ANISOU 2838  CA  LYS A 211     4714   8028   7383   1584    103   1004       C  
ATOM   2839  C   LYS A 211     -25.018  32.982 -13.902  1.00 52.49           C  
ANISOU 2839  C   LYS A 211     4790   7722   7432   1494     20    996       C  
ATOM   2840  O   LYS A 211     -24.299  32.268 -13.197  1.00 50.60           O  
ANISOU 2840  O   LYS A 211     4574   7535   7116   1390     69    971       O  
ATOM   2841  CB  LYS A 211     -27.357  33.089 -13.029  1.00 54.57           C  
ANISOU 2841  CB  LYS A 211     4862   8376   7497   1810    100    796       C  
ATOM   2842  CG  LYS A 211     -27.429  34.604 -12.906  1.00 57.64           C  
ANISOU 2842  CG  LYS A 211     5335   8534   8032   2026    -61    656       C  
ATOM   2843  CD  LYS A 211     -28.378  35.030 -11.800  1.00 60.79           C  
ANISOU 2843  CD  LYS A 211     5660   9130   8307   2295    -65    420       C  
ATOM   2844  CE  LYS A 211     -28.988  36.394 -12.086  1.00 66.53           C  
ANISOU 2844  CE  LYS A 211     6426   9686   9165   2553   -223    305       C  
ATOM   2845  NZ  LYS A 211     -27.968  37.473 -12.169  1.00 67.30           N  
ANISOU 2845  NZ  LYS A 211     6715   9359   9499   2557   -427    267       N  
ATOM   2846  H   LYS A 211     -26.246  30.712 -13.667  1.00 66.40           H  
ATOM   2847  HA  LYS A 211     -26.748  33.032 -14.992  1.00 63.56           H  
ATOM   2848  HB2 LYS A 211     -28.258  32.761 -13.173  1.00 65.49           H  
ATOM   2849  HB3 LYS A 211     -27.011  32.740 -12.192  1.00 65.49           H  
ATOM   2850  HG2 LYS A 211     -26.547  34.951 -12.699  1.00 69.17           H  
ATOM   2851  HG3 LYS A 211     -27.749  34.978 -13.742  1.00 69.17           H  
ATOM   2852  HD2 LYS A 211     -29.098  34.384 -11.729  1.00 72.95           H  
ATOM   2853  HD3 LYS A 211     -27.892  35.084 -10.963  1.00 72.95           H  
ATOM   2854  HE2 LYS A 211     -29.458  36.359 -12.934  1.00 79.83           H  
ATOM   2855  HE3 LYS A 211     -29.606  36.620 -11.373  1.00 79.83           H  
ATOM   2856  HZ1 LYS A 211     -28.362  38.252 -12.337  1.00 80.77           H  
ATOM   2857  HZ2 LYS A 211     -27.525  37.532 -11.399  1.00 80.77           H  
ATOM   2858  HZ3 LYS A 211     -27.390  37.294 -12.822  1.00 80.77           H  
ATOM   2859  N   GLY A 212     -24.597  34.113 -14.464  1.00 54.29           N  
ANISOU 2859  N   GLY A 212     5101   7684   7844   1526   -118   1035       N  
ATOM   2860  CA  GLY A 212     -23.240  34.581 -14.276  1.00 56.41           C  
ANISOU 2860  CA  GLY A 212     5485   7716   8233   1423   -220   1054       C  
ATOM   2861  C   GLY A 212     -22.234  33.767 -15.079  1.00 57.02           C  
ANISOU 2861  C   GLY A 212     5552   7816   8295   1194   -163   1253       C  
ATOM   2862  O   GLY A 212     -22.576  32.895 -15.881  1.00 54.41           O  
ANISOU 2862  O   GLY A 212     5142   7654   7877   1126    -65   1369       O  
ATOM   2863  H   GLY A 212     -25.082  34.623 -14.957  1.00 65.15           H  
ATOM   2864  HA2 GLY A 212     -23.176  35.508 -14.553  1.00 67.69           H  
ATOM   2865  HA3 GLY A 212     -23.004  34.522 -13.337  1.00 67.69           H  
ATOM   2866  N   TYR A 213     -20.960  34.071 -14.836  1.00 54.51           N  
ANISOU 2866  N   TYR A 213     5314   7338   8060   1086   -240   1280       N  
ATOM   2867  CA  TYR A 213     -19.858  33.445 -15.552  1.00 54.07           C  
ANISOU 2867  CA  TYR A 213     5242   7315   7986    892   -207   1458       C  
ATOM   2868  C   TYR A 213     -18.844  32.893 -14.563  1.00 49.24           C  
ANISOU 2868  C   TYR A 213     4676   6723   7311    812   -182   1374       C  
ATOM   2869  O   TYR A 213     -18.545  33.524 -13.545  1.00 47.08           O  
ANISOU 2869  O   TYR A 213     4475   6318   7094    863   -263   1233       O  
ATOM   2870  CB  TYR A 213     -19.183  34.440 -16.502  1.00 56.44           C  
ANISOU 2870  CB  TYR A 213     5562   7427   8456    808   -340   1647       C  
ATOM   2871  CG  TYR A 213     -20.071  34.855 -17.653  1.00 61.16           C  
ANISOU 2871  CG  TYR A 213     6104   8033   9101    865   -359   1775       C  
ATOM   2872  CD1 TYR A 213     -20.985  35.893 -17.513  1.00 62.80           C  
ANISOU 2872  CD1 TYR A 213     6349   8087   9424   1024   -463   1698       C  
ATOM   2873  CD2 TYR A 213     -20.007  34.200 -18.875  1.00 60.19           C  
ANISOU 2873  CD2 TYR A 213     5887   8084   8897    779   -281   1959       C  
ATOM   2874  CE1 TYR A 213     -21.804  36.271 -18.561  1.00 62.86           C  
ANISOU 2874  CE1 TYR A 213     6304   8106   9474   1082   -484   1820       C  
ATOM   2875  CE2 TYR A 213     -20.823  34.571 -19.929  1.00 60.80           C  
ANISOU 2875  CE2 TYR A 213     5906   8188   9006    834   -299   2078       C  
ATOM   2876  CZ  TYR A 213     -21.719  35.604 -19.766  1.00 62.62           C  
ANISOU 2876  CZ  TYR A 213     6176   8257   9359    978   -397   2017       C  
ATOM   2877  OH  TYR A 213     -22.527  35.973 -20.817  1.00 66.96           O  
ANISOU 2877  OH  TYR A 213     6667   8836   9940   1036   -419   2142       O  
ATOM   2878  H   TYR A 213     -20.707  34.647 -14.250  1.00 65.41           H  
ATOM   2879  HA  TYR A 213     -20.200  32.706 -16.080  1.00 64.88           H  
ATOM   2880  HB2 TYR A 213     -18.945  35.238 -16.005  1.00 67.73           H  
ATOM   2881  HB3 TYR A 213     -18.385  34.031 -16.872  1.00 67.73           H  
ATOM   2882  HD1 TYR A 213     -21.045  36.343 -16.701  1.00 75.36           H  
ATOM   2883  HD2 TYR A 213     -19.404  33.501 -18.988  1.00 72.22           H  
ATOM   2884  HE1 TYR A 213     -22.409  36.969 -18.454  1.00 75.43           H  
ATOM   2885  HE2 TYR A 213     -20.767  34.125 -20.743  1.00 72.96           H  
ATOM   2886  HH  TYR A 213     -22.371  35.488 -21.484  1.00 80.35           H  
ATOM   2887  N   LYS A 214     -18.323  31.707 -14.871  1.00 46.84           N  
ANISOU 2887  N   LYS A 214     4329   6582   6887    700    -83   1450       N  
ATOM   2888  CA  LYS A 214     -17.333  31.039 -14.038  1.00 50.00           C  
ANISOU 2888  CA  LYS A 214     4764   7021   7214    622    -56   1391       C  
ATOM   2889  C   LYS A 214     -16.142  30.643 -14.895  1.00 50.17           C  
ANISOU 2889  C   LYS A 214     4757   7080   7225    483    -60   1554       C  
ATOM   2890  O   LYS A 214     -16.312  30.054 -15.968  1.00 45.39           O  
ANISOU 2890  O   LYS A 214     4084   6602   6561    459    -12   1668       O  
ATOM   2891  CB  LYS A 214     -17.918  29.798 -13.357  1.00 49.09           C  
ANISOU 2891  CB  LYS A 214     4623   7096   6934    648     58   1297       C  
ATOM   2892  CG  LYS A 214     -18.713  30.089 -12.098  1.00 47.59           C  
ANISOU 2892  CG  LYS A 214     4445   6932   6703    772     68   1119       C  
ATOM   2893  CD  LYS A 214     -19.178  28.801 -11.454  1.00 44.44           C  
ANISOU 2893  CD  LYS A 214     4002   6746   6136    753    172   1086       C  
ATOM   2894  CE  LYS A 214     -19.739  29.040 -10.072  1.00 47.32           C  
ANISOU 2894  CE  LYS A 214     4359   7199   6423    866    187    921       C  
ATOM   2895  NZ  LYS A 214     -20.170  27.762  -9.443  1.00 52.39           N  
ANISOU 2895  NZ  LYS A 214     4941   8065   6898    814    279    938       N  
ATOM   2896  H   LYS A 214     -18.533  31.261 -15.575  1.00 56.21           H  
ATOM   2897  HA  LYS A 214     -17.026  31.650 -13.350  1.00 60.00           H  
ATOM   2898  HB2 LYS A 214     -18.510  29.351 -13.983  1.00 58.91           H  
ATOM   2899  HB3 LYS A 214     -17.190  29.205 -13.115  1.00 58.91           H  
ATOM   2900  HG2 LYS A 214     -18.153  30.565 -11.465  1.00 57.10           H  
ATOM   2901  HG3 LYS A 214     -19.494  30.618 -12.325  1.00 57.10           H  
ATOM   2902  HD2 LYS A 214     -19.874  28.403 -11.999  1.00 53.33           H  
ATOM   2903  HD3 LYS A 214     -18.425  28.194 -11.375  1.00 53.33           H  
ATOM   2904  HE2 LYS A 214     -19.056  29.441  -9.512  1.00 56.79           H  
ATOM   2905  HE3 LYS A 214     -20.511  29.625 -10.135  1.00 56.79           H  
ATOM   2906  HZ1 LYS A 214     -20.498  27.919  -8.631  1.00 62.86           H  
ATOM   2907  HZ2 LYS A 214     -20.799  27.376  -9.940  1.00 62.86           H  
ATOM   2908  HZ3 LYS A 214     -19.476  27.209  -9.374  1.00 62.86           H  
ATOM   2909  N   ARG A 215     -14.946  30.977 -14.422  1.00 53.30           N  
ANISOU 2909  N   ARG A 215     5193   7390   7669    402   -125   1557       N  
ATOM   2910  CA  ARG A 215     -13.708  30.550 -15.058  1.00 47.90           C  
ANISOU 2910  CA  ARG A 215     4462   6794   6944    280   -124   1697       C  
ATOM   2911  C   ARG A 215     -13.301  29.207 -14.466  1.00 44.65           C  
ANISOU 2911  C   ARG A 215     4058   6531   6378    273    -40   1607       C  
ATOM   2912  O   ARG A 215     -13.114  29.090 -13.250  1.00 41.13           O  
ANISOU 2912  O   ARG A 215     3673   6043   5912    286    -41   1471       O  
ATOM   2913  CB  ARG A 215     -12.611  31.591 -14.847  1.00 51.07           C  
ANISOU 2913  CB  ARG A 215     4887   7041   7477    181   -250   1765       C  
ATOM   2914  CG  ARG A 215     -11.278  31.255 -15.501  1.00 51.98           C  
ANISOU 2914  CG  ARG A 215     4921   7292   7538     52   -253   1930       C  
ATOM   2915  CD  ARG A 215     -10.140  31.934 -14.771  1.00 54.66           C  
ANISOU 2915  CD  ARG A 215     5294   7505   7968    -53   -362   1935       C  
ATOM   2916  NE  ARG A 215      -8.923  31.969 -15.572  1.00 54.81           N  
ANISOU 2916  NE  ARG A 215     5203   7660   7964   -192   -393   2150       N  
ATOM   2917  CZ  ARG A 215      -7.783  32.511 -15.163  1.00 56.33           C  
ANISOU 2917  CZ  ARG A 215     5386   7792   8227   -321   -493   2212       C  
ATOM   2918  NH1 ARG A 215      -7.704  33.061 -13.958  1.00 58.04           N  
ANISOU 2918  NH1 ARG A 215     5715   7789   8548   -319   -583   2054       N  
ATOM   2919  NH2 ARG A 215      -6.722  32.502 -15.957  1.00 54.91           N  
ANISOU 2919  NH2 ARG A 215     5071   7795   7999   -446   -511   2430       N  
ATOM   2920  H   ARG A 215     -14.825  31.460 -13.721  1.00 63.96           H  
ATOM   2921  HA  ARG A 215     -13.851  30.439 -16.010  1.00 57.48           H  
ATOM   2922  HB2 ARG A 215     -12.912  32.436 -15.214  1.00 61.29           H  
ATOM   2923  HB3 ARG A 215     -12.454  31.686 -13.895  1.00 61.29           H  
ATOM   2924  HG2 ARG A 215     -11.135  30.296 -15.468  1.00 62.38           H  
ATOM   2925  HG3 ARG A 215     -11.282  31.565 -16.420  1.00 62.38           H  
ATOM   2926  HD2 ARG A 215     -10.393  32.847 -14.566  1.00 65.59           H  
ATOM   2927  HD3 ARG A 215      -9.950  31.448 -13.954  1.00 65.59           H  
ATOM   2928  HE  ARG A 215      -8.967  31.688 -16.383  1.00 65.78           H  
ATOM   2929 HH11 ARG A 215      -8.392  33.068 -13.442  1.00 69.65           H  
ATOM   2930 HH12 ARG A 215      -6.965  33.412 -13.693  1.00 69.65           H  
ATOM   2931 HH21 ARG A 215      -6.772  32.145 -16.738  1.00 65.90           H  
ATOM   2932 HH22 ARG A 215      -5.983  32.853 -15.691  1.00 65.90           H  
ATOM   2933  N   CYS A 216     -13.169  28.198 -15.324  1.00 43.14           N  
ANISOU 2933  N   CYS A 216     3806   6509   6076    262     16   1679       N  
ATOM   2934  CA  CYS A 216     -12.848  26.841 -14.903  1.00 40.78           C  
ANISOU 2934  CA  CYS A 216     3523   6328   5642    266     66   1602       C  
ATOM   2935  C   CYS A 216     -11.480  26.463 -15.450  1.00 44.43           C  
ANISOU 2935  C   CYS A 216     3935   6905   6042    214     45   1683       C  
ATOM   2936  O   CYS A 216     -11.275  26.457 -16.669  1.00 44.79           O  
ANISOU 2936  O   CYS A 216     3895   7066   6056    214     41   1804       O  
ATOM   2937  CB  CYS A 216     -13.913  25.860 -15.388  1.00 42.51           C  
ANISOU 2937  CB  CYS A 216     3725   6644   5784    322    116   1583       C  
ATOM   2938  SG  CYS A 216     -15.600  26.395 -14.994  1.00 45.23           S  
ANISOU 2938  SG  CYS A 216     4078   6924   6185    390    146   1523       S  
ATOM   2939  H   CYS A 216     -13.263  28.279 -16.175  1.00 51.77           H  
ATOM   2940  HA  CYS A 216     -12.812  26.803 -13.934  1.00 48.93           H  
ATOM   2941  HB2 CYS A 216     -13.844  25.770 -16.351  1.00 51.02           H  
ATOM   2942  HB3 CYS A 216     -13.765  25.000 -14.964  1.00 51.02           H  
ATOM   2943  HG  CYS A 216     -16.375  25.577 -15.405  1.00 54.28           H  
ATOM   2944  N   ILE A 217     -10.550  26.159 -14.550  1.00 46.23           N  
ANISOU 2944  N   ILE A 217     4201   7129   6235    181     32   1618       N  
ATOM   2945  CA  ILE A 217      -9.214  25.702 -14.909  1.00 41.67           C  
ANISOU 2945  CA  ILE A 217     3567   6690   5575    149     13   1674       C  
ATOM   2946  C   ILE A 217      -9.107  24.242 -14.495  1.00 38.75           C  
ANISOU 2946  C   ILE A 217     3243   6400   5081    208     34   1563       C  
ATOM   2947  O   ILE A 217      -9.200  23.918 -13.305  1.00 37.88           O  
ANISOU 2947  O   ILE A 217     3214   6214   4965    204     39   1459       O  
ATOM   2948  CB  ILE A 217      -8.121  26.550 -14.240  1.00 44.44           C  
ANISOU 2948  CB  ILE A 217     3919   6974   5994     58    -42   1700       C  
ATOM   2949  CG1 ILE A 217      -8.361  28.042 -14.502  1.00 48.15           C  
ANISOU 2949  CG1 ILE A 217     4375   7294   6627     -8   -105   1802       C  
ATOM   2950  CG2 ILE A 217      -6.753  26.130 -14.756  1.00 41.64           C  
ANISOU 2950  CG2 ILE A 217     3468   6816   5537     28    -58   1783       C  
ATOM   2951  CD1 ILE A 217      -7.376  28.966 -13.803  1.00 42.35           C  
ANISOU 2951  CD1 ILE A 217     3655   6446   5992   -114   -199   1824       C  
ATOM   2952  H   ILE A 217     -10.674  26.212 -13.701  1.00 55.47           H  
ATOM   2953  HA  ILE A 217      -9.101  25.758 -15.871  1.00 50.01           H  
ATOM   2954  HB  ILE A 217      -8.152  26.395 -13.283  1.00 53.33           H  
ATOM   2955 HG12 ILE A 217      -8.292  28.205 -15.456  1.00 57.79           H  
ATOM   2956 HG13 ILE A 217      -9.251  28.273 -14.194  1.00 57.79           H  
ATOM   2957 HG21 ILE A 217      -6.074  26.673 -14.325  1.00 49.97           H  
ATOM   2958 HG22 ILE A 217      -6.610  25.194 -14.546  1.00 49.97           H  
ATOM   2959 HG23 ILE A 217      -6.723  26.263 -15.716  1.00 49.97           H  
ATOM   2960 HD11 ILE A 217      -7.597  29.886 -14.021  1.00 50.83           H  
ATOM   2961 HD12 ILE A 217      -7.440  28.828 -12.845  1.00 50.83           H  
ATOM   2962 HD13 ILE A 217      -6.479  28.761 -14.109  1.00 50.83           H  
ATOM   2963  N   LEU A 218      -8.922  23.363 -15.474  1.00 44.06           N  
ANISOU 2963  N   LEU A 218     3864   7227   5650    270     29   1585       N  
ATOM   2964  CA  LEU A 218      -8.823  21.932 -15.239  1.00 43.17           C  
ANISOU 2964  CA  LEU A 218     3804   7162   5436    338      7   1483       C  
ATOM   2965  C   LEU A 218      -7.386  21.464 -15.428  1.00 45.32           C  
ANISOU 2965  C   LEU A 218     4027   7589   5605    374    -30   1479       C  
ATOM   2966  O   LEU A 218      -6.623  22.040 -16.209  1.00 46.02           O  
ANISOU 2966  O   LEU A 218     4000   7824   5663    365    -30   1580       O  
ATOM   2967  CB  LEU A 218      -9.738  21.151 -16.187  1.00 44.49           C  
ANISOU 2967  CB  LEU A 218     3964   7376   5562    413     -7   1469       C  
ATOM   2968  CG  LEU A 218     -11.203  20.989 -15.768  1.00 49.07           C  
ANISOU 2968  CG  LEU A 218     4608   7831   6204    392     13   1437       C  
ATOM   2969  CD1 LEU A 218     -11.882  22.329 -15.543  1.00 44.68           C  
ANISOU 2969  CD1 LEU A 218     4033   7189   5755    342     68   1490       C  
ATOM   2970  CD2 LEU A 218     -11.961  20.184 -16.812  1.00 47.39           C  
ANISOU 2970  CD2 LEU A 218     4379   7676   5951    457    -26   1427       C  
ATOM   2971  H   LEU A 218      -8.848  23.580 -16.303  1.00 52.87           H  
ATOM   2972  HA  LEU A 218      -9.090  21.737 -14.328  1.00 51.80           H  
ATOM   2973  HB2 LEU A 218      -9.736  21.601 -17.046  1.00 53.38           H  
ATOM   2974  HB3 LEU A 218      -9.371  20.260 -16.293  1.00 53.38           H  
ATOM   2975  HG  LEU A 218     -11.235  20.496 -14.933  1.00 58.88           H  
ATOM   2976 HD11 LEU A 218     -12.803  22.175 -15.280  1.00 53.62           H  
ATOM   2977 HD12 LEU A 218     -11.413  22.806 -14.841  1.00 53.62           H  
ATOM   2978 HD13 LEU A 218     -11.854  22.839 -16.367  1.00 53.62           H  
ATOM   2979 HD21 LEU A 218     -12.884  20.092 -16.530  1.00 56.87           H  
ATOM   2980 HD22 LEU A 218     -11.919  20.651 -17.661  1.00 56.87           H  
ATOM   2981 HD23 LEU A 218     -11.550  19.309 -16.895  1.00 56.87           H  
ATOM   2982  N   PHE A 219      -7.024  20.408 -14.702  1.00 39.60           N  
ANISOU 2982  N   PHE A 219     3379   6848   4820    415    -68   1376       N  
ATOM   2983  CA  PHE A 219      -5.738  19.757 -14.885  1.00 43.23           C  
ANISOU 2983  CA  PHE A 219     3797   7464   5164    490   -118   1343       C  
ATOM   2984  C   PHE A 219      -5.964  18.255 -14.999  1.00 47.42           C  
ANISOU 2984  C   PHE A 219     4408   7987   5624    608   -200   1229       C  
ATOM   2985  O   PHE A 219      -6.780  17.697 -14.254  1.00 44.21           O  
ANISOU 2985  O   PHE A 219     4115   7414   5269    574   -221   1183       O  
ATOM   2986  CB  PHE A 219      -4.782  20.053 -13.719  1.00 41.28           C  
ANISOU 2986  CB  PHE A 219     3572   7187   4926    423   -117   1328       C  
ATOM   2987  CG  PHE A 219      -4.615  21.516 -13.429  1.00 43.48           C  
ANISOU 2987  CG  PHE A 219     3802   7411   5306    295    -77   1420       C  
ATOM   2988  CD1 PHE A 219      -3.650  22.257 -14.088  1.00 40.40           C  
ANISOU 2988  CD1 PHE A 219     3278   7176   4897    253    -83   1538       C  
ATOM   2989  CD2 PHE A 219      -5.423  22.153 -12.502  1.00 44.81           C  
ANISOU 2989  CD2 PHE A 219     4054   7384   5586    222    -51   1393       C  
ATOM   2990  CE1 PHE A 219      -3.493  23.602 -13.831  1.00 43.12           C  
ANISOU 2990  CE1 PHE A 219     3591   7431   5361    118    -86   1635       C  
ATOM   2991  CE2 PHE A 219      -5.270  23.500 -12.240  1.00 43.53           C  
ANISOU 2991  CE2 PHE A 219     3867   7139   5533    125    -53   1452       C  
ATOM   2992  CZ  PHE A 219      -4.303  24.225 -12.906  1.00 45.38           C  
ANISOU 2992  CZ  PHE A 219     3987   7480   5778     62    -81   1578       C  
ATOM   2993  H   PHE A 219      -7.513  20.049 -14.093  1.00 47.52           H  
ATOM   2994  HA  PHE A 219      -5.329  20.071 -15.706  1.00 51.88           H  
ATOM   2995  HB2 PHE A 219      -5.126  19.630 -12.917  1.00 49.54           H  
ATOM   2996  HB3 PHE A 219      -3.908  19.691 -13.932  1.00 49.54           H  
ATOM   2997  HD1 PHE A 219      -3.101  21.842 -14.714  1.00 48.48           H  
ATOM   2998  HD2 PHE A 219      -6.077  21.668 -12.052  1.00 53.77           H  
ATOM   2999  HE1 PHE A 219      -2.840  24.088 -14.280  1.00 51.74           H  
ATOM   3000  HE2 PHE A 219      -5.817  23.918 -11.615  1.00 52.24           H  
ATOM   3001  HZ  PHE A 219      -4.197  25.132 -12.730  1.00 54.46           H  
ATOM   3002  N   PRO A 220      -5.282  17.572 -15.918  1.00 46.35           N  
ANISOU 3002  N   PRO A 220     4212   8034   5367    750   -263   1184       N  
ATOM   3003  CA  PRO A 220      -5.512  16.128 -16.083  1.00 45.56           C  
ANISOU 3003  CA  PRO A 220     4206   7889   5217    881   -386   1054       C  
ATOM   3004  C   PRO A 220      -5.063  15.348 -14.861  1.00 47.96           C  
ANISOU 3004  C   PRO A 220     4627   8067   5527    874   -453    984       C  
ATOM   3005  O   PRO A 220      -4.298  15.860 -14.028  1.00 44.33           O  
ANISOU 3005  O   PRO A 220     4150   7625   5067    807   -402   1015       O  
ATOM   3006  CB  PRO A 220      -4.663  15.768 -17.312  1.00 46.21           C  
ANISOU 3006  CB  PRO A 220     4171   8244   5144   1066   -441   1005       C  
ATOM   3007  CG  PRO A 220      -4.470  17.042 -18.028  1.00 51.96           C  
ANISOU 3007  CG  PRO A 220     4734   9153   5855   1001   -330   1151       C  
ATOM   3008  CD  PRO A 220      -4.393  18.097 -16.970  1.00 52.03           C  
ANISOU 3008  CD  PRO A 220     4760   9025   5982    808   -241   1254       C  
ATOM   3009  HA  PRO A 220      -6.447  15.946 -16.264  1.00 54.68           H  
ATOM   3010  HB2 PRO A 220      -3.812  15.401 -17.027  1.00 55.46           H  
ATOM   3011  HB3 PRO A 220      -5.143  15.132 -17.866  1.00 55.46           H  
ATOM   3012  HG2 PRO A 220      -3.643  17.008 -18.535  1.00 62.35           H  
ATOM   3013  HG3 PRO A 220      -5.224  17.203 -18.615  1.00 62.35           H  
ATOM   3014  HD2 PRO A 220      -3.485  18.179 -16.637  1.00 62.43           H  
ATOM   3015  HD3 PRO A 220      -4.728  18.942 -17.308  1.00 62.43           H  
ATOM   3016  N   PRO A 221      -5.515  14.098 -14.718  1.00 47.43           N  
ANISOU 3016  N   PRO A 221     4684   7865   5472    936   -584    898       N  
ATOM   3017  CA  PRO A 221      -5.052  13.279 -13.587  1.00 45.34           C  
ANISOU 3017  CA  PRO A 221     4534   7483   5211    933   -670    851       C  
ATOM   3018  C   PRO A 221      -3.554  13.041 -13.574  1.00 45.64           C  
ANISOU 3018  C   PRO A 221     4523   7684   5133   1066   -713    781       C  
ATOM   3019  O   PRO A 221      -2.983  12.850 -12.493  1.00 45.97           O  
ANISOU 3019  O   PRO A 221     4620   7672   5176   1028   -727    778       O  
ATOM   3020  CB  PRO A 221      -5.821  11.963 -13.772  1.00 47.54           C  
ANISOU 3020  CB  PRO A 221     4941   7591   5532    985   -845    786       C  
ATOM   3021  CG  PRO A 221      -7.003  12.319 -14.564  1.00 48.79           C  
ANISOU 3021  CG  PRO A 221     5064   7730   5743    936   -803    830       C  
ATOM   3022  CD  PRO A 221      -6.582  13.424 -15.478  1.00 46.28           C  
ANISOU 3022  CD  PRO A 221     4588   7636   5359    980   -673    860       C  
ATOM   3023  HA  PRO A 221      -5.317  13.688 -12.748  1.00 54.41           H  
ATOM   3024  HB2 PRO A 221      -5.267  11.325 -14.249  1.00 57.05           H  
ATOM   3025  HB3 PRO A 221      -6.081  11.612 -12.906  1.00 57.05           H  
ATOM   3026  HG2 PRO A 221      -7.293  11.547 -15.076  1.00 58.55           H  
ATOM   3027  HG3 PRO A 221      -7.711  12.619 -13.972  1.00 58.55           H  
ATOM   3028  HD2 PRO A 221      -6.231  13.063 -16.307  1.00 55.53           H  
ATOM   3029  HD3 PRO A 221      -7.320  14.032 -15.637  1.00 55.53           H  
ATOM   3030  N   ASP A 222      -2.895  13.027 -14.737  1.00 53.94           N  
ANISOU 3030  N   ASP A 222     5460   8966   6068   1230   -735    726       N  
ATOM   3031  CA  ASP A 222      -1.466  12.732 -14.769  1.00 50.24           C  
ANISOU 3031  CA  ASP A 222     4922   8703   5464   1381   -783    655       C  
ATOM   3032  C   ASP A 222      -0.622  13.839 -14.158  1.00 47.35           C  
ANISOU 3032  C   ASP A 222     4446   8460   5084   1254   -648    763       C  
ATOM   3033  O   ASP A 222       0.585  13.643 -13.984  1.00 55.86           O  
ANISOU 3033  O   ASP A 222     5459   9709   6055   1348   -680    722       O  
ATOM   3034  CB  ASP A 222      -0.998  12.458 -16.206  1.00 49.76           C  
ANISOU 3034  CB  ASP A 222     4734   8923   5249   1607   -838    570       C  
ATOM   3035  CG  ASP A 222      -1.086  13.679 -17.111  1.00 54.51           C  
ANISOU 3035  CG  ASP A 222     5150   9749   5814   1535   -689    705       C  
ATOM   3036  OD1 ASP A 222      -0.893  14.817 -16.638  1.00 59.15           O  
ANISOU 3036  OD1 ASP A 222     5665  10351   6457   1348   -556    855       O  
ATOM   3037  OD2 ASP A 222      -1.334  13.492 -18.319  1.00 62.22           O  
ANISOU 3037  OD2 ASP A 222     6051  10887   6704   1673   -723    662       O  
ATOM   3038  H   ASP A 222      -3.248  13.183 -15.505  1.00 64.72           H  
ATOM   3039  HA  ASP A 222      -1.308  11.926 -14.253  1.00 60.29           H  
ATOM   3040  HB2 ASP A 222      -0.072  12.169 -16.185  1.00 59.71           H  
ATOM   3041  HB3 ASP A 222      -1.553  11.762 -16.590  1.00 59.71           H  
ATOM   3042  N   GLN A 223      -1.212  14.991 -13.842  1.00 45.22           N  
ANISOU 3042  N   GLN A 223     4151   8109   4921   1052   -517    891       N  
ATOM   3043  CA  GLN A 223      -0.501  16.056 -13.151  1.00 45.68           C  
ANISOU 3043  CA  GLN A 223     4134   8223   5001    913   -425    983       C  
ATOM   3044  C   GLN A 223      -0.665  15.975 -11.636  1.00 41.63           C  
ANISOU 3044  C   GLN A 223     3753   7495   4569    803   -424    966       C  
ATOM   3045  O   GLN A 223      -0.519  16.991 -10.948  1.00 43.73           O  
ANISOU 3045  O   GLN A 223     3992   7726   4897    660   -349   1032       O  
ATOM   3046  CB  GLN A 223      -0.960  17.421 -13.671  1.00 47.53           C  
ANISOU 3046  CB  GLN A 223     4268   8483   5310    774   -317   1122       C  
ATOM   3047  CG  GLN A 223      -0.535  17.696 -15.107  1.00 51.36           C  
ANISOU 3047  CG  GLN A 223     4575   9252   5687    859   -306   1186       C  
ATOM   3048  CD  GLN A 223      -0.773  19.133 -15.518  1.00 59.95           C  
ANISOU 3048  CD  GLN A 223     5555  10365   6857    696   -219   1361       C  
ATOM   3049  OE1 GLN A 223      -0.690  20.047 -14.700  1.00 60.52           O  
ANISOU 3049  OE1 GLN A 223     5648  10306   7041    533   -184   1430       O  
ATOM   3050  NE2 GLN A 223      -1.081  19.339 -16.792  1.00 64.87           N  
ANISOU 3050  NE2 GLN A 223     6070  11151   7428    747   -203   1432       N  
ATOM   3051  H   GLN A 223      -2.032  15.179 -14.020  1.00 54.27           H  
ATOM   3052  HA  GLN A 223       0.445  15.972 -13.347  1.00 54.82           H  
ATOM   3053  HB2 GLN A 223      -1.928  17.461 -13.635  1.00 57.04           H  
ATOM   3054  HB3 GLN A 223      -0.579  18.114 -13.110  1.00 57.04           H  
ATOM   3055  HG2 GLN A 223       0.413  17.512 -15.197  1.00 61.63           H  
ATOM   3056  HG3 GLN A 223      -1.043  17.125 -15.703  1.00 61.63           H  
ATOM   3057 HE21 GLN A 223      -1.136  18.674 -17.335  1.00 77.85           H  
ATOM   3058 HE22 GLN A 223      -1.226  20.138 -17.076  1.00 77.85           H  
ATOM   3059  N   PHE A 224      -0.961  14.785 -11.108  1.00 42.71           N  
ANISOU 3059  N   PHE A 224     4030   7492   4706    870   -523    883       N  
ATOM   3060  CA  PHE A 224      -0.984  14.579  -9.662  1.00 41.97           C  
ANISOU 3060  CA  PHE A 224     4043   7250   4652    781   -532    880       C  
ATOM   3061  C   PHE A 224       0.296  15.083  -9.007  1.00 47.21           C  
ANISOU 3061  C   PHE A 224     4636   8040   5260    760   -505    883       C  
ATOM   3062  O   PHE A 224       0.253  15.726  -7.951  1.00 44.66           O  
ANISOU 3062  O   PHE A 224     4336   7646   4986    632   -448    913       O  
ATOM   3063  CB  PHE A 224      -1.183  13.091  -9.364  1.00 39.28           C  
ANISOU 3063  CB  PHE A 224     3842   6781   4300    875   -683    812       C  
ATOM   3064  CG  PHE A 224      -1.351  12.771  -7.904  1.00 40.65           C  
ANISOU 3064  CG  PHE A 224     4122   6817   4507    776   -701    841       C  
ATOM   3065  CD1 PHE A 224      -0.252  12.688  -7.064  1.00 40.24           C  
ANISOU 3065  CD1 PHE A 224     4067   6831   4392    799   -721    816       C  
ATOM   3066  CD2 PHE A 224      -2.608  12.525  -7.378  1.00 40.10           C  
ANISOU 3066  CD2 PHE A 224     4138   6581   4515    662   -702    905       C  
ATOM   3067  CE1 PHE A 224      -0.405  12.385  -5.725  1.00 39.58           C  
ANISOU 3067  CE1 PHE A 224     4071   6647   4320    714   -740    852       C  
ATOM   3068  CE2 PHE A 224      -2.767  12.218  -6.040  1.00 40.53           C  
ANISOU 3068  CE2 PHE A 224     4267   6560   4574    571   -718    954       C  
ATOM   3069  CZ  PHE A 224      -1.664  12.148  -5.213  1.00 39.40           C  
ANISOU 3069  CZ  PHE A 224     4127   6480   4365    600   -736    925       C  
ATOM   3070  H   PHE A 224      -1.151  14.082 -11.566  1.00 51.25           H  
ATOM   3071  HA  PHE A 224      -1.731  15.067  -9.283  1.00 50.36           H  
ATOM   3072  HB2 PHE A 224      -1.979  12.785  -9.827  1.00 47.13           H  
ATOM   3073  HB3 PHE A 224      -0.410  12.603  -9.687  1.00 47.13           H  
ATOM   3074  HD1 PHE A 224       0.599  12.848  -7.405  1.00 48.29           H  
ATOM   3075  HD2 PHE A 224      -3.354  12.571  -7.931  1.00 48.11           H  
ATOM   3076  HE1 PHE A 224       0.340  12.338  -5.170  1.00 47.50           H  
ATOM   3077  HE2 PHE A 224      -3.616  12.060  -5.697  1.00 48.64           H  
ATOM   3078  HZ  PHE A 224      -1.769  11.943  -4.312  1.00 47.28           H  
ATOM   3079  N   GLU A 225       1.448  14.796  -9.620  1.00 56.39           N  
ANISOU 3079  N   GLU A 225     5703   9414   6310    896   -552    843       N  
ATOM   3080  CA  GLU A 225       2.735  15.139  -9.024  1.00 59.32           C  
ANISOU 3080  CA  GLU A 225     5994   9931   6614    883   -545    847       C  
ATOM   3081  C   GLU A 225       2.930  16.642  -8.875  1.00 56.01           C  
ANISOU 3081  C   GLU A 225     5466   9558   6256    704   -439    952       C  
ATOM   3082  O   GLU A 225       3.791  17.068  -8.097  1.00 52.68           O  
ANISOU 3082  O   GLU A 225     5004   9191   5819    638   -436    963       O  
ATOM   3083  CB  GLU A 225       3.871  14.566  -9.873  1.00 65.11           C  
ANISOU 3083  CB  GLU A 225     6609  10936   7192   1082   -614    790       C  
ATOM   3084  CG  GLU A 225       3.755  13.080 -10.164  1.00 70.13           C  
ANISOU 3084  CG  GLU A 225     7356  11518   7771   1299   -761    657       C  
ATOM   3085  CD  GLU A 225       4.215  12.728 -11.563  1.00 76.72           C  
ANISOU 3085  CD  GLU A 225     8064  12616   8470   1514   -810    592       C  
ATOM   3086  OE1 GLU A 225       5.171  11.934 -11.692  1.00 79.09           O  
ANISOU 3086  OE1 GLU A 225     8332  13079   8637   1726   -917    481       O  
ATOM   3087  OE2 GLU A 225       3.633  13.260 -12.534  1.00 80.68           O  
ANISOU 3087  OE2 GLU A 225     8488  13183   8982   1485   -745    647       O  
ATOM   3088  H   GLU A 225       1.508  14.403 -10.383  1.00 67.67           H  
ATOM   3089  HA  GLU A 225       2.790  14.741  -8.141  1.00 71.18           H  
ATOM   3090  HB2 GLU A 225       3.888  15.032 -10.723  1.00 78.13           H  
ATOM   3091  HB3 GLU A 225       4.709  14.710  -9.406  1.00 78.13           H  
ATOM   3092  HG2 GLU A 225       4.306  12.590  -9.533  1.00 84.15           H  
ATOM   3093  HG3 GLU A 225       2.827  12.811 -10.075  1.00 84.15           H  
ATOM   3094  N   CYS A 226       2.160  17.452  -9.602  1.00 54.28           N  
ANISOU 3094  N   CYS A 226     5204   9307   6115    623   -373   1030       N  
ATOM   3095  CA  CYS A 226       2.341  18.897  -9.613  1.00 48.07           C  
ANISOU 3095  CA  CYS A 226     4318   8539   5406    458   -311   1141       C  
ATOM   3096  C   CYS A 226       1.403  19.639  -8.668  1.00 47.09           C  
ANISOU 3096  C   CYS A 226     4304   8164   5424    321   -272   1137       C  
ATOM   3097  O   CYS A 226       1.644  20.819  -8.390  1.00 46.99           O  
ANISOU 3097  O   CYS A 226     4242   8117   5493    189   -259   1196       O  
ATOM   3098  CB  CYS A 226       2.138  19.440 -11.034  1.00 46.57           C  
ANISOU 3098  CB  CYS A 226     3998   8484   5213    457   -278   1247       C  
ATOM   3099  SG  CYS A 226       3.036  18.545 -12.318  1.00 50.54           S  
ANISOU 3099  SG  CYS A 226     4349   9342   5510    667   -321   1230       S  
ATOM   3100  H   CYS A 226       1.517  17.181 -10.103  1.00 65.14           H  
ATOM   3101  HA  CYS A 226       3.251  19.100  -9.346  1.00 57.68           H  
ATOM   3102  HB2 CYS A 226       1.193  19.395 -11.251  1.00 55.89           H  
ATOM   3103  HB3 CYS A 226       2.434  20.364 -11.058  1.00 55.89           H  
ATOM   3104  HG  CYS A 226       2.805  19.052 -13.381  1.00 60.65           H  
ATOM   3105  N   LEU A 227       0.347  18.991  -8.170  1.00 43.81           N  
ANISOU 3105  N   LEU A 227     4026   7583   5037    351   -268   1072       N  
ATOM   3106  CA  LEU A 227      -0.688  19.681  -7.413  1.00 44.17           C  
ANISOU 3106  CA  LEU A 227     4148   7446   5187    254   -223   1064       C  
ATOM   3107  C   LEU A 227      -0.763  19.275  -5.946  1.00 44.36           C  
ANISOU 3107  C   LEU A 227     4274   7394   5189    241   -236    991       C  
ATOM   3108  O   LEU A 227      -1.482  19.927  -5.180  1.00 46.14           O  
ANISOU 3108  O   LEU A 227     4542   7518   5473    179   -201    967       O  
ATOM   3109  CB  LEU A 227      -2.050  19.459  -8.083  1.00 45.15           C  
ANISOU 3109  CB  LEU A 227     4312   7486   5357    278   -193   1082       C  
ATOM   3110  CG  LEU A 227      -2.174  20.225  -9.406  1.00 46.54           C  
ANISOU 3110  CG  LEU A 227     4385   7723   5576    264   -166   1169       C  
ATOM   3111  CD1 LEU A 227      -3.264  19.647 -10.292  1.00 45.27           C  
ANISOU 3111  CD1 LEU A 227     4248   7536   5418    328   -157   1175       C  
ATOM   3112  CD2 LEU A 227      -2.449  21.694  -9.135  1.00 44.89           C  
ANISOU 3112  CD2 LEU A 227     4155   7413   5489    148   -137   1214       C  
ATOM   3113  H   LEU A 227       0.210  18.147  -8.260  1.00 52.57           H  
ATOM   3114  HA  LEU A 227      -0.502  20.633  -7.440  1.00 53.00           H  
ATOM   3115  HB2 LEU A 227      -2.162  18.514  -8.270  1.00 54.18           H  
ATOM   3116  HB3 LEU A 227      -2.751  19.767  -7.488  1.00 54.18           H  
ATOM   3117  HG  LEU A 227      -1.334  20.161  -9.886  1.00 55.85           H  
ATOM   3118 HD11 LEU A 227      -3.307  20.160 -11.114  1.00 54.33           H  
ATOM   3119 HD12 LEU A 227      -3.052  18.721 -10.491  1.00 54.33           H  
ATOM   3120 HD13 LEU A 227      -4.112  19.699  -9.825  1.00 54.33           H  
ATOM   3121 HD21 LEU A 227      -2.524  22.162  -9.981  1.00 53.87           H  
ATOM   3122 HD22 LEU A 227      -3.278  21.773  -8.637  1.00 53.87           H  
ATOM   3123 HD23 LEU A 227      -1.715  22.062  -8.618  1.00 53.87           H  
ATOM   3124  N   TYR A 228      -0.057  18.223  -5.538  1.00 38.84           N  
ANISOU 3124  N   TYR A 228     3607   6755   4396    312   -293    953       N  
ATOM   3125  CA  TYR A 228       0.176  17.917  -4.131  1.00 40.57           C  
ANISOU 3125  CA  TYR A 228     3895   6946   4573    293   -314    905       C  
ATOM   3126  C   TYR A 228      -1.102  17.933  -3.297  1.00 46.35           C  
ANISOU 3126  C   TYR A 228     4707   7569   5335    245   -275    900       C  
ATOM   3127  O   TYR A 228      -1.270  18.807  -2.435  1.00 44.59           O  
ANISOU 3127  O   TYR A 228     4482   7326   5133    187   -240    863       O  
ATOM   3128  CB  TYR A 228       1.182  18.911  -3.548  1.00 45.38           C  
ANISOU 3128  CB  TYR A 228     4441   7613   5188    227   -314    884       C  
ATOM   3129  CG  TYR A 228       2.515  18.918  -4.266  1.00 43.10           C  
ANISOU 3129  CG  TYR A 228     4041   7487   4849    259   -351    913       C  
ATOM   3130  CD1 TYR A 228       3.530  18.049  -3.894  1.00 41.35           C  
ANISOU 3130  CD1 TYR A 228     3815   7377   4519    341   -411    877       C  
ATOM   3131  CD2 TYR A 228       2.755  19.793  -5.317  1.00 46.18           C  
ANISOU 3131  CD2 TYR A 228     4314   7942   5289    209   -332    990       C  
ATOM   3132  CE1 TYR A 228       4.751  18.051  -4.548  1.00 41.67           C  
ANISOU 3132  CE1 TYR A 228     3727   7617   4490    387   -442    902       C  
ATOM   3133  CE2 TYR A 228       3.971  19.804  -5.977  1.00 47.23           C  
ANISOU 3133  CE2 TYR A 228     4310   8284   5350    233   -362   1040       C  
ATOM   3134  CZ  TYR A 228       4.965  18.931  -5.588  1.00 46.94           C  
ANISOU 3134  CZ  TYR A 228     4260   8382   5192    328   -412    989       C  
ATOM   3135  OH  TYR A 228       6.174  18.946  -6.248  1.00 47.50           O  
ANISOU 3135  OH  TYR A 228     4170   8708   5169    367   -438   1038       O  
ATOM   3136  H   TYR A 228       0.307  17.657  -6.074  1.00 46.61           H  
ATOM   3137  HA  TYR A 228       0.562  17.030  -4.063  1.00 48.68           H  
ATOM   3138  HB2 TYR A 228       0.808  19.805  -3.607  1.00 54.46           H  
ATOM   3139  HB3 TYR A 228       1.346  18.684  -2.620  1.00 54.46           H  
ATOM   3140  HD1 TYR A 228       3.389  17.455  -3.193  1.00 49.62           H  
ATOM   3141  HD2 TYR A 228       2.087  20.384  -5.582  1.00 55.41           H  
ATOM   3142  HE1 TYR A 228       5.423  17.463  -4.287  1.00 50.01           H  
ATOM   3143  HE2 TYR A 228       4.117  20.396  -6.679  1.00 56.67           H  
ATOM   3144  HH  TYR A 228       6.689  18.370  -5.918  1.00 57.00           H  
ATOM   3145  N   PRO A 229      -2.011  16.983  -3.501  1.00 43.22           N  
ANISOU 3145  N   PRO A 229     4372   7118   4933    270   -293    934       N  
ATOM   3146  CA  PRO A 229      -3.197  16.912  -2.642  1.00 45.51           C  
ANISOU 3146  CA  PRO A 229     4708   7361   5224    216   -257    956       C  
ATOM   3147  C   PRO A 229      -2.834  16.598  -1.200  1.00 43.94           C  
ANISOU 3147  C   PRO A 229     4545   7210   4941    198   -278    942       C  
ATOM   3148  O   PRO A 229      -1.807  15.981  -0.910  1.00 45.40           O  
ANISOU 3148  O   PRO A 229     4752   7428   5070    236   -346    930       O  
ATOM   3149  CB  PRO A 229      -4.022  15.776  -3.260  1.00 46.01           C  
ANISOU 3149  CB  PRO A 229     4821   7362   5300    232   -310   1021       C  
ATOM   3150  CG  PRO A 229      -3.048  14.975  -4.052  1.00 40.89           C  
ANISOU 3150  CG  PRO A 229     4188   6720   4629    326   -406    998       C  
ATOM   3151  CD  PRO A 229      -2.015  15.940  -4.539  1.00 39.75           C  
ANISOU 3151  CD  PRO A 229     3953   6668   4483    352   -363    953       C  
ATOM   3152  HA  PRO A 229      -3.700  17.740  -2.681  1.00 54.62           H  
ATOM   3153  HB2 PRO A 229      -4.417  15.238  -2.556  1.00 55.22           H  
ATOM   3154  HB3 PRO A 229      -4.709  16.147  -3.836  1.00 55.22           H  
ATOM   3155  HG2 PRO A 229      -2.643  14.303  -3.482  1.00 49.07           H  
ATOM   3156  HG3 PRO A 229      -3.504  14.558  -4.799  1.00 49.07           H  
ATOM   3157  HD2 PRO A 229      -1.147  15.510  -4.590  1.00 47.70           H  
ATOM   3158  HD3 PRO A 229      -2.278  16.314  -5.395  1.00 47.70           H  
ATOM   3159  N   TYR A 230      -3.702  17.033  -0.288  1.00 45.94           N  
ANISOU 3159  N   TYR A 230     4793   7492   5170    153   -220    940       N  
ATOM   3160  CA  TYR A 230      -3.538  16.696   1.114  1.00 45.78           C  
ANISOU 3160  CA  TYR A 230     4792   7557   5045    139   -233    941       C  
ATOM   3161  C   TYR A 230      -3.572  15.179   1.295  1.00 44.03           C  
ANISOU 3161  C   TYR A 230     4634   7317   4777    128   -322   1052       C  
ATOM   3162  O   TYR A 230      -4.027  14.448   0.411  1.00 44.12           O  
ANISOU 3162  O   TYR A 230     4679   7240   4846    128   -373   1116       O  
ATOM   3163  CB  TYR A 230      -4.645  17.333   1.953  1.00 45.09           C  
ANISOU 3163  CB  TYR A 230     4667   7553   4914    116   -156    926       C  
ATOM   3164  CG  TYR A 230      -4.536  18.832   2.119  1.00 48.37           C  
ANISOU 3164  CG  TYR A 230     5040   7970   5367    146   -110    788       C  
ATOM   3165  CD1 TYR A 230      -5.081  19.700   1.181  1.00 46.08           C  
ANISOU 3165  CD1 TYR A 230     4726   7593   5190    154    -75    760       C  
ATOM   3166  CD2 TYR A 230      -3.902  19.379   3.226  1.00 51.75           C  
ANISOU 3166  CD2 TYR A 230     5460   8475   5726    169   -123    684       C  
ATOM   3167  CE1 TYR A 230      -4.987  21.072   1.339  1.00 48.43           C  
ANISOU 3167  CE1 TYR A 230     5002   7853   5546    180    -71    638       C  
ATOM   3168  CE2 TYR A 230      -3.803  20.746   3.392  1.00 49.76           C  
ANISOU 3168  CE2 TYR A 230     5187   8190   5529    198   -121    545       C  
ATOM   3169  CZ  TYR A 230      -4.347  21.588   2.446  1.00 49.55           C  
ANISOU 3169  CZ  TYR A 230     5147   8049   5631    202   -103    525       C  
ATOM   3170  OH  TYR A 230      -4.248  22.950   2.610  1.00 50.77           O  
ANISOU 3170  OH  TYR A 230     5296   8131   5863    231   -138    391       O  
ATOM   3171  H   TYR A 230      -4.388  17.522  -0.458  1.00 55.13           H  
ATOM   3172  HA  TYR A 230      -2.682  17.026   1.430  1.00 54.94           H  
ATOM   3173  HB2 TYR A 230      -5.498  17.147   1.530  1.00 54.11           H  
ATOM   3174  HB3 TYR A 230      -4.628  16.938   2.838  1.00 54.11           H  
ATOM   3175  HD1 TYR A 230      -5.513  19.354   0.434  1.00 55.30           H  
ATOM   3176  HD2 TYR A 230      -3.533  18.814   3.866  1.00 62.10           H  
ATOM   3177  HE1 TYR A 230      -5.353  21.642   0.702  1.00 58.11           H  
ATOM   3178  HE2 TYR A 230      -3.372  21.097   4.137  1.00 59.71           H  
ATOM   3179  HH  TYR A 230      -3.837  23.125   3.322  1.00 60.92           H  
ATOM   3180  N   PRO A 231      -3.098  14.681   2.437  1.00 43.18           N  
ANISOU 3180  N   PRO A 231     4550   7284   4572    121   -363   1076       N  
ATOM   3181  CA  PRO A 231      -3.289  13.260   2.747  1.00 48.46           C  
ANISOU 3181  CA  PRO A 231     5285   7919   5208     90   -470   1212       C  
ATOM   3182  C   PRO A 231      -4.760  12.874   2.684  1.00 45.19           C  
ANISOU 3182  C   PRO A 231     4861   7497   4811      4   -458   1343       C  
ATOM   3183  O   PRO A 231      -5.649  13.696   2.908  1.00 47.82           O  
ANISOU 3183  O   PRO A 231     5120   7925   5124    -25   -347   1330       O  
ATOM   3184  CB  PRO A 231      -2.740  13.130   4.172  1.00 47.08           C  
ANISOU 3184  CB  PRO A 231     5107   7873   4909     81   -483   1225       C  
ATOM   3185  CG  PRO A 231      -1.761  14.245   4.302  1.00 46.06           C  
ANISOU 3185  CG  PRO A 231     4934   7799   4768    139   -427   1062       C  
ATOM   3186  CD  PRO A 231      -2.311  15.371   3.475  1.00 44.78           C  
ANISOU 3186  CD  PRO A 231     4722   7595   4696    138   -336    984       C  
ATOM   3187  HA  PRO A 231      -2.774  12.702   2.143  1.00 58.15           H  
ATOM   3188  HB2 PRO A 231      -3.462  13.229   4.812  1.00 56.50           H  
ATOM   3189  HB3 PRO A 231      -2.301  12.271   4.278  1.00 56.50           H  
ATOM   3190  HG2 PRO A 231      -1.690  14.509   5.233  1.00 55.27           H  
ATOM   3191  HG3 PRO A 231      -0.898  13.961   3.961  1.00 55.27           H  
ATOM   3192  HD2 PRO A 231      -2.884  15.937   4.014  1.00 53.73           H  
ATOM   3193  HD3 PRO A 231      -1.589  15.877   3.071  1.00 53.73           H  
ATOM   3194  N   VAL A 232      -5.014  11.635   2.350  1.00 43.48           N  
ANISOU 3194  N   VAL A 232     4717   7167   4636    -34   -592   1470       N  
ATOM   3195  CA  VAL A 232      -6.359  11.175   2.298  1.00 47.77           C  
ANISOU 3195  CA  VAL A 232     5246   7694   5209   -142   -609   1621       C  
ATOM   3196  C   VAL A 232      -7.090  11.327   3.626  1.00 52.94           C  
ANISOU 3196  C   VAL A 232     5814   8563   5738   -234   -530   1734       C  
ATOM   3197  O   VAL A 232      -8.238  11.647   3.624  1.00 56.16           O  
ANISOU 3197  O   VAL A 232     6137   9070   6130   -293   -447   1791       O  
ATOM   3198  CB  VAL A 232      -6.442   9.732   1.868  1.00 52.13           C  
ANISOU 3198  CB  VAL A 232     5909   8058   5840   -175   -817   1741       C  
ATOM   3199  CG1 VAL A 232      -7.818   9.217   2.163  1.00 57.80           C  
ANISOU 3199  CG1 VAL A 232     6604   8777   6581   -333   -864   1947       C  
ATOM   3200  CG2 VAL A 232      -6.148   9.594   0.406  1.00 43.05           C  
ANISOU 3200  CG2 VAL A 232     4817   6745   4796    -59   -882   1609       C  
ATOM   3201  H   VAL A 232      -4.422  11.044   2.150  1.00 52.18           H  
ATOM   3202  HA  VAL A 232      -6.843  11.709   1.634  1.00 57.32           H  
ATOM   3203  HB  VAL A 232      -5.792   9.199   2.371  1.00 62.55           H  
ATOM   3204 HG11 VAL A 232      -7.943   8.381   1.708  1.00 69.36           H  
ATOM   3205 HG12 VAL A 232      -7.908   9.091   3.110  1.00 69.36           H  
ATOM   3206 HG13 VAL A 232      -8.464   9.857   1.855  1.00 69.36           H  
ATOM   3207 HG21 VAL A 232      -6.203   8.667   0.163  1.00 51.66           H  
ATOM   3208 HG22 VAL A 232      -6.793  10.102  -0.091  1.00 51.66           H  
ATOM   3209 HG23 VAL A 232      -5.264   9.927   0.233  1.00 51.66           H  
ATOM   3210  N   HIS A 233      -6.454  11.101   4.763  1.00 51.66           N  
ANISOU 3210  N   HIS A 233     5656   8505   5466   -236   -555   1767       N  
ATOM   3211  CA  HIS A 233      -7.134  11.256   6.013  1.00 53.11           C  
ANISOU 3211  CA  HIS A 233     5740   8945   5493   -307   -485   1879       C  
ATOM   3212  C   HIS A 233      -7.243  12.694   6.452  1.00 51.18           C  
ANISOU 3212  C   HIS A 233     5396   8892   5158   -221   -317   1698       C  
ATOM   3213  O   HIS A 233      -7.905  12.980   7.413  1.00 50.38           O  
ANISOU 3213  O   HIS A 233     5190   9050   4904   -243   -245   1753       O  
ATOM   3214  CB  HIS A 233      -6.431  10.425   7.069  1.00 58.04           C  
ANISOU 3214  CB  HIS A 233     6406   9623   6024   -337   -588   1992       C  
ATOM   3215  CG  HIS A 233      -6.338   8.979   6.716  1.00 64.42           C  
ANISOU 3215  CG  HIS A 233     7317  10239   6920   -430   -789   2195       C  
ATOM   3216  ND1 HIS A 233      -7.371   8.098   6.918  1.00 64.64           N  
ANISOU 3216  ND1 HIS A 233     7481  10032   7049   -351   -941   2132       N  
ATOM   3217  CD2 HIS A 233      -5.347   8.265   6.142  1.00 64.36           C  
ANISOU 3217  CD2 HIS A 233     7296  10236   6923   -592   -887   2460       C  
ATOM   3218  CE1 HIS A 233      -7.017   6.902   6.498  1.00 63.99           C  
ANISOU 3218  CE1 HIS A 233     7484   9785   7045   -446  -1138   2330       C  
ATOM   3219  NE2 HIS A 233      -5.792   6.978   6.022  1.00 65.01           N  
ANISOU 3219  NE2 HIS A 233     7526  10045   7130   -612  -1114   2545       N  
ATOM   3220  H   HIS A 233      -5.651  10.813   4.875  1.00 61.99           H  
ATOM   3221  HA  HIS A 233      -8.044  10.906   5.918  1.00 63.73           H  
ATOM   3222  HB2 HIS A 233      -5.529  10.762   7.185  1.00 69.65           H  
ATOM   3223  HB3 HIS A 233      -6.921  10.497   7.903  1.00 69.65           H  
ATOM   3224  HD1 HIS A 233      -8.130   8.296   7.269  1.00 77.57           H  
ATOM   3225  HD2 HIS A 233      -4.514   8.588   5.882  1.00 77.23           H  
ATOM   3226  HE1 HIS A 233      -7.541   6.135   6.534  1.00 76.79           H  
ATOM   3227  N   HIS A 234      -6.624  13.610   5.739  1.00 52.31           N  
ANISOU 3227  N   HIS A 234     5564   8925   5387   -119   -270   1488       N  
ATOM   3228  CA  HIS A 234      -6.710  15.014   6.117  1.00 53.69           C  
ANISOU 3228  CA  HIS A 234     5664   9223   5510    -36   -153   1306       C  
ATOM   3229  C   HIS A 234      -8.084  15.571   5.741  1.00 49.79           C  
ANISOU 3229  C   HIS A 234     5091   8797   5031    -41    -66   1314       C  
ATOM   3230  O   HIS A 234      -8.631  15.208   4.698  1.00 49.42           O  
ANISOU 3230  O   HIS A 234     5065   8615   5098    -88    -85   1389       O  
ATOM   3231  CB  HIS A 234      -5.615  15.824   5.421  1.00 54.24           C  
ANISOU 3231  CB  HIS A 234     5783   9135   5691     42   -159   1120       C  
ATOM   3232  CG  HIS A 234      -5.404  17.186   6.007  1.00 53.10           C  
ANISOU 3232  CG  HIS A 234     5591   9079   5507    120    -97    929       C  
ATOM   3233  ND1 HIS A 234      -6.201  18.267   5.694  1.00 50.67           N  
ANISOU 3233  ND1 HIS A 234     5235   8773   5243    166    -30    828       N  
ATOM   3234  CD2 HIS A 234      -4.482  17.643   6.887  1.00 54.87           C  
ANISOU 3234  CD2 HIS A 234     5814   9376   5657    166   -117    811       C  
ATOM   3235  CE1 HIS A 234      -5.782  19.329   6.359  1.00 52.15           C  
ANISOU 3235  CE1 HIS A 234     5405   9012   5396    242    -26    648       C  
ATOM   3236  NE2 HIS A 234      -4.740  18.977   7.090  1.00 54.80           N  
ANISOU 3236  NE2 HIS A 234     5766   9396   5660    238    -77    634       N  
ATOM   3237  H   HIS A 234      -6.141  13.459   5.044  1.00 62.77           H  
ATOM   3238  HA  HIS A 234      -6.594  15.100   7.076  1.00 64.42           H  
ATOM   3239  HB2 HIS A 234      -4.778  15.340   5.488  1.00 65.09           H  
ATOM   3240  HB3 HIS A 234      -5.855  15.937   4.488  1.00 65.09           H  
ATOM   3241  HD2 HIS A 234      -3.803  17.145   7.283  1.00 65.84           H  
ATOM   3242  HE1 HIS A 234      -6.156  20.179   6.318  1.00 62.58           H  
ATOM   3243  HE2 HIS A 234      -4.294  19.499   7.608  1.00 65.76           H  
ATOM   3244  N   PRO A 235      -8.666  16.447   6.567  1.00 54.03           N  
ANISOU 3244  N   PRO A 235     5530   9553   5446     23     22   1225       N  
ATOM   3245  CA  PRO A 235      -9.994  16.990   6.232  1.00 52.57           C  
ANISOU 3245  CA  PRO A 235     5256   9458   5260     43    102   1222       C  
ATOM   3246  C   PRO A 235     -10.088  17.576   4.833  1.00 51.31           C  
ANISOU 3246  C   PRO A 235     5143   9061   5291     70    109   1138       C  
ATOM   3247  O   PRO A 235     -11.164  17.527   4.223  1.00 50.38           O  
ANISOU 3247  O   PRO A 235     4978   8955   5211     42    143   1212       O  
ATOM   3248  CB  PRO A 235     -10.208  18.063   7.308  1.00 55.85           C  
ANISOU 3248  CB  PRO A 235     5582  10115   5523    174    169   1048       C  
ATOM   3249  CG  PRO A 235      -9.414  17.586   8.469  1.00 56.18           C  
ANISOU 3249  CG  PRO A 235     5628  10297   5421    164    133   1075       C  
ATOM   3250  CD  PRO A 235      -8.204  16.903   7.891  1.00 56.26           C  
ANISOU 3250  CD  PRO A 235     5769  10042   5564     95     41   1121       C  
ATOM   3251  HA  PRO A 235     -10.670  16.302   6.333  1.00 63.08           H  
ATOM   3252  HB2 PRO A 235      -9.876  18.918   6.991  1.00 67.02           H  
ATOM   3253  HB3 PRO A 235     -11.150  18.120   7.533  1.00 67.02           H  
ATOM   3254  HG2 PRO A 235      -9.149  18.344   9.014  1.00 67.42           H  
ATOM   3255  HG3 PRO A 235      -9.943  16.961   8.989  1.00 67.42           H  
ATOM   3256  HD2 PRO A 235      -7.473  17.534   7.796  1.00 67.51           H  
ATOM   3257  HD3 PRO A 235      -7.950  16.145   8.440  1.00 67.51           H  
ATOM   3258  N   CYS A 236      -8.996  18.129   4.300  1.00 54.87           N  
ANISOU 3258  N   CYS A 236     5674   9318   5857    115     75   1003       N  
ATOM   3259  CA  CYS A 236      -8.985  18.702   2.960  1.00 48.86           C  
ANISOU 3259  CA  CYS A 236     4945   8355   5265    133     77    948       C  
ATOM   3260  C   CYS A 236      -8.625  17.676   1.892  1.00 45.50           C  
ANISOU 3260  C   CYS A 236     4584   7767   4936     65     12   1067       C  
ATOM   3261  O   CYS A 236      -8.074  18.040   0.843  1.00 43.18           O  
ANISOU 3261  O   CYS A 236     4323   7323   4759     87     -7   1016       O  
ATOM   3262  CB  CYS A 236      -8.027  19.892   2.919  1.00 46.84           C  
ANISOU 3262  CB  CYS A 236     4716   8001   5079    203     60    767       C  
ATOM   3263  SG  CYS A 236      -8.468  21.189   4.101  1.00 55.36           S  
ANISOU 3263  SG  CYS A 236     5738   9231   6065    323     93    573       S  
ATOM   3264  H   CYS A 236      -8.240  18.184   4.705  1.00 65.85           H  
ATOM   3265  HA  CYS A 236      -9.874  19.034   2.759  1.00 58.63           H  
ATOM   3266  HB2 CYS A 236      -7.132  19.584   3.132  1.00 56.20           H  
ATOM   3267  HB3 CYS A 236      -8.042  20.279   2.030  1.00 56.20           H  
ATOM   3268  HG  CYS A 236      -9.570  21.591   3.847  1.00 66.43           H  
ATOM   3269  N   ASP A 237      -8.929  16.402   2.136  1.00 50.99           N  
ANISOU 3269  N   ASP A 237     5295   8498   5581    -14    -39   1227       N  
ATOM   3270  CA  ASP A 237      -8.685  15.351   1.157  1.00 49.58           C  
ANISOU 3270  CA  ASP A 237     5190   8155   5493    -56   -135   1319       C  
ATOM   3271  C   ASP A 237      -9.205  15.764  -0.214  1.00 45.83           C  
ANISOU 3271  C   ASP A 237     4705   7572   5137    -35   -112   1290       C  
ATOM   3272  O   ASP A 237     -10.302  16.313  -0.342  1.00 44.16           O  
ANISOU 3272  O   ASP A 237     4425   7423   4930    -40    -39   1299       O  
ATOM   3273  CB  ASP A 237      -9.364  14.055   1.614  1.00 48.25           C  
ANISOU 3273  CB  ASP A 237     5030   8028   5276   -164   -211   1515       C  
ATOM   3274  CG  ASP A 237      -9.225  12.922   0.609  1.00 50.84           C  
ANISOU 3274  CG  ASP A 237     5448   8157   5711   -195   -351   1592       C  
ATOM   3275  OD1 ASP A 237      -8.199  12.855  -0.103  1.00 51.28           O  
ANISOU 3275  OD1 ASP A 237     5571   8085   5827   -113   -405   1492       O  
ATOM   3276  OD2 ASP A 237     -10.151  12.085   0.540  1.00 51.31           O  
ANISOU 3276  OD2 ASP A 237     5506   8202   5790   -298   -421   1751       O  
ATOM   3277  H   ASP A 237      -9.281  16.121   2.868  1.00 61.19           H  
ATOM   3278  HA  ASP A 237      -7.731  15.190   1.088  1.00 59.50           H  
ATOM   3279  HB2 ASP A 237      -8.961  13.766   2.448  1.00 57.90           H  
ATOM   3280  HB3 ASP A 237     -10.310  14.224   1.745  1.00 57.90           H  
ATOM   3281  N   ARG A 238      -8.395  15.508  -1.238  1.00 46.63           N  
ANISOU 3281  N   ARG A 238     4863   7536   5320      4   -174   1254       N  
ATOM   3282  CA  ARG A 238      -8.685  15.722  -2.649  1.00 45.33           C  
ANISOU 3282  CA  ARG A 238     4691   7280   5254     33   -173   1237       C  
ATOM   3283  C   ARG A 238      -8.430  17.171  -3.068  1.00 42.88           C  
ANISOU 3283  C   ARG A 238     4329   6971   4991     85    -87   1133       C  
ATOM   3284  O   ARG A 238      -8.522  17.472  -4.259  1.00 40.50           O  
ANISOU 3284  O   ARG A 238     4010   6613   4763    112    -83   1127       O  
ATOM   3285  CB  ARG A 238     -10.126  15.332  -3.040  1.00 47.79           C  
ANISOU 3285  CB  ARG A 238     4974   7591   5592    -27   -171   1336       C  
ATOM   3286  CG  ARG A 238     -10.596  14.020  -2.418  1.00 54.45           C  
ANISOU 3286  CG  ARG A 238     5851   8441   6396   -123   -267   1480       C  
ATOM   3287  CD  ARG A 238     -11.347  13.143  -3.410  1.00 54.25           C  
ANISOU 3287  CD  ARG A 238     5854   8307   6450   -169   -368   1564       C  
ATOM   3288  NE  ARG A 238     -12.517  13.805  -3.978  1.00 56.83           N  
ANISOU 3288  NE  ARG A 238     6096   8687   6808   -184   -279   1576       N  
ATOM   3289  CZ  ARG A 238     -13.718  13.840  -3.405  1.00 61.36           C  
ANISOU 3289  CZ  ARG A 238     6586   9392   7337   -271   -230   1684       C  
ATOM   3290  NH1 ARG A 238     -13.922  13.261  -2.229  1.00 63.74           N  
ANISOU 3290  NH1 ARG A 238     6866   9800   7551   -365   -255   1807       N  
ATOM   3291  NH2 ARG A 238     -14.719  14.467  -4.008  1.00 60.08           N  
ANISOU 3291  NH2 ARG A 238     6345   9281   7203   -262   -154   1679       N  
ATOM   3292  H   ARG A 238      -7.607  15.182  -1.123  1.00 55.96           H  
ATOM   3293  HA  ARG A 238      -8.086  15.163  -3.169  1.00 54.40           H  
ATOM   3294  HB2 ARG A 238     -10.731  16.032  -2.747  1.00 57.34           H  
ATOM   3295  HB3 ARG A 238     -10.174  15.237  -4.004  1.00 57.34           H  
ATOM   3296  HG2 ARG A 238      -9.824  13.525  -2.103  1.00 65.34           H  
ATOM   3297  HG3 ARG A 238     -11.192  14.216  -1.678  1.00 65.34           H  
ATOM   3298  HD2 ARG A 238     -10.751  12.910  -4.139  1.00 65.09           H  
ATOM   3299  HD3 ARG A 238     -11.647  12.340  -2.957  1.00 65.09           H  
ATOM   3300  HE  ARG A 238     -12.424  14.201  -4.736  1.00 68.19           H  
ATOM   3301 HH11 ARG A 238     -13.277  12.853  -1.833  1.00 76.49           H  
ATOM   3302 HH12 ARG A 238     -14.700  13.290  -1.865  1.00 76.49           H  
ATOM   3303 HH21 ARG A 238     -14.593  14.847  -4.769  1.00 72.10           H  
ATOM   3304 HH22 ARG A 238     -15.495  14.494  -3.638  1.00 72.10           H  
ATOM   3305  N   GLN A 239      -8.110  18.073  -2.145  1.00 44.48           N  
ANISOU 3305  N   GLN A 239     4509   7232   5158     99    -38   1055       N  
ATOM   3306  CA  GLN A 239      -7.793  19.453  -2.479  1.00 43.96           C  
ANISOU 3306  CA  GLN A 239     4411   7129   5163    135     -1    964       C  
ATOM   3307  C   GLN A 239      -6.284  19.647  -2.556  1.00 47.52           C  
ANISOU 3307  C   GLN A 239     4876   7555   5626    142    -48    920       C  
ATOM   3308  O   GLN A 239      -5.515  18.973  -1.865  1.00 42.80           O  
ANISOU 3308  O   GLN A 239     4309   6999   4955    140    -89    917       O  
ATOM   3309  CB  GLN A 239      -8.384  20.410  -1.445  1.00 48.64           C  
ANISOU 3309  CB  GLN A 239     4974   7787   5722    163     49    879       C  
ATOM   3310  CG  GLN A 239      -9.895  20.392  -1.395  1.00 53.39           C  
ANISOU 3310  CG  GLN A 239     5527   8461   6296    171    106    917       C  
ATOM   3311  CD  GLN A 239     -10.445  21.321  -0.334  1.00 57.06           C  
ANISOU 3311  CD  GLN A 239     5949   9035   6696    242    146    805       C  
ATOM   3312  OE1 GLN A 239     -10.966  22.396  -0.638  1.00 64.05           O  
ANISOU 3312  OE1 GLN A 239     6811   9878   7649    308    163    723       O  
ATOM   3313  NE2 GLN A 239     -10.333  20.912   0.920  1.00 56.32           N  
ANISOU 3313  NE2 GLN A 239     5842   9091   6464    243    151    795       N  
ATOM   3314  H   GLN A 239      -8.069  17.904  -1.303  1.00 53.37           H  
ATOM   3315  HA  GLN A 239      -8.172  19.668  -3.345  1.00 52.75           H  
ATOM   3316  HB2 GLN A 239      -8.055  20.164  -0.566  1.00 58.37           H  
ATOM   3317  HB3 GLN A 239      -8.105  21.314  -1.660  1.00 58.37           H  
ATOM   3318  HG2 GLN A 239     -10.245  20.675  -2.255  1.00 64.06           H  
ATOM   3319  HG3 GLN A 239     -10.196  19.492  -1.193  1.00 64.06           H  
ATOM   3320 HE21 GLN A 239      -9.963  20.155   1.094  1.00 67.58           H  
ATOM   3321 HE22 GLN A 239     -10.629  21.403   1.560  1.00 67.58           H  
ATOM   3322  N   SER A 240      -5.868  20.583  -3.405  1.00 48.02           N  
ANISOU 3322  N   SER A 240     4904   7561   5779    145    -48    904       N  
ATOM   3323  CA  SER A 240      -4.454  20.878  -3.573  1.00 47.17           C  
ANISOU 3323  CA  SER A 240     4777   7463   5683    133    -94    889       C  
ATOM   3324  C   SER A 240      -3.925  21.659  -2.378  1.00 42.93           C  
ANISOU 3324  C   SER A 240     4248   6926   5135    116   -113    796       C  
ATOM   3325  O   SER A 240      -4.620  22.511  -1.816  1.00 41.11           O  
ANISOU 3325  O   SER A 240     4025   6659   4937    128    -96    725       O  
ATOM   3326  CB  SER A 240      -4.222  21.673  -4.859  1.00 46.62           C  
ANISOU 3326  CB  SER A 240     4646   7357   5709    115    -97    941       C  
ATOM   3327  OG  SER A 240      -2.864  22.074  -4.973  1.00 47.50           O  
ANISOU 3327  OG  SER A 240     4711   7511   5828     81   -144    952       O  
ATOM   3328  H   SER A 240      -6.388  21.061  -3.894  1.00 57.62           H  
ATOM   3329  HA  SER A 240      -3.959  20.046  -3.636  1.00 56.61           H  
ATOM   3330  HB2 SER A 240      -4.451  21.117  -5.620  1.00 55.94           H  
ATOM   3331  HB3 SER A 240      -4.784  22.464  -4.846  1.00 55.94           H  
ATOM   3332  HG  SER A 240      -2.365  21.398  -4.985  1.00 57.00           H  
ATOM   3333  N   GLN A 241      -2.687  21.355  -1.984  1.00 41.94           N  
ANISOU 3333  N   GLN A 241     4121   6856   4959    106   -159    783       N  
ATOM   3334  CA  GLN A 241      -2.018  22.114  -0.935  1.00 43.54           C  
ANISOU 3334  CA  GLN A 241     4325   7061   5156     85   -197    690       C  
ATOM   3335  C   GLN A 241      -1.428  23.420  -1.445  1.00 44.43           C  
ANISOU 3335  C   GLN A 241     4392   7093   5395     24   -249    686       C  
ATOM   3336  O   GLN A 241      -1.083  24.287  -0.635  1.00 45.32           O  
ANISOU 3336  O   GLN A 241     4516   7161   5541      2   -306    592       O  
ATOM   3337  CB  GLN A 241      -0.896  21.284  -0.307  1.00 44.54           C  
ANISOU 3337  CB  GLN A 241     4458   7286   5178     92   -236    685       C  
ATOM   3338  CG  GLN A 241      -1.361  20.085   0.488  1.00 45.78           C  
ANISOU 3338  CG  GLN A 241     4670   7508   5217    132   -220    698       C  
ATOM   3339  CD  GLN A 241      -0.201  19.289   1.047  1.00 44.09           C  
ANISOU 3339  CD  GLN A 241     4467   7375   4910    150   -276    699       C  
ATOM   3340  OE1 GLN A 241       0.222  19.499   2.183  1.00 45.97           O  
ANISOU 3340  OE1 GLN A 241     4711   7670   5083    147   -295    633       O  
ATOM   3341  NE2 GLN A 241       0.325  18.371   0.247  1.00 46.42           N  
ANISOU 3341  NE2 GLN A 241     4762   7686   5190    187   -312    760       N  
ATOM   3342  H   GLN A 241      -2.216  20.713  -2.310  1.00 50.33           H  
ATOM   3343  HA  GLN A 241      -2.660  22.326  -0.240  1.00 52.24           H  
ATOM   3344  HB2 GLN A 241      -0.317  20.960  -1.015  1.00 53.44           H  
ATOM   3345  HB3 GLN A 241      -0.389  21.854   0.292  1.00 53.44           H  
ATOM   3346  HG2 GLN A 241      -1.906  20.387   1.231  1.00 54.94           H  
ATOM   3347  HG3 GLN A 241      -1.877  19.501  -0.090  1.00 54.94           H  
ATOM   3348 HE21 GLN A 241       0.005  18.255  -0.543  1.00 55.71           H  
ATOM   3349 HE22 GLN A 241       0.986  17.892   0.518  1.00 55.71           H  
ATOM   3350  N   VAL A 242      -1.298  23.575  -2.759  1.00 44.03           N  
ANISOU 3350  N   VAL A 242     4287   7029   5413     -7   -246    792       N  
ATOM   3351  CA  VAL A 242      -0.623  24.732  -3.334  1.00 46.60           C  
ANISOU 3351  CA  VAL A 242     4550   7300   5858    -96   -312    846       C  
ATOM   3352  C   VAL A 242      -1.549  25.936  -3.263  1.00 47.58           C  
ANISOU 3352  C   VAL A 242     4711   7252   6115   -107   -340    797       C  
ATOM   3353  O   VAL A 242      -2.713  25.865  -3.669  1.00 48.69           O  
ANISOU 3353  O   VAL A 242     4874   7353   6273    -53   -282    804       O  
ATOM   3354  CB  VAL A 242      -0.204  24.451  -4.786  1.00 46.13           C  
ANISOU 3354  CB  VAL A 242     4397   7335   5797   -118   -296    996       C  
ATOM   3355  CG1 VAL A 242       0.516  25.653  -5.379  1.00 43.63           C  
ANISOU 3355  CG1 VAL A 242     3992   6989   5597   -240   -372   1101       C  
ATOM   3356  CG2 VAL A 242       0.672  23.208  -4.867  1.00 42.43           C  
ANISOU 3356  CG2 VAL A 242     3894   7043   5183    -61   -285   1011       C  
ATOM   3357  H   VAL A 242      -1.595  23.019  -3.343  1.00 52.83           H  
ATOM   3358  HA  VAL A 242       0.175  24.929  -2.818  1.00 55.93           H  
ATOM   3359  HB  VAL A 242      -1.000  24.289  -5.316  1.00 55.36           H  
ATOM   3360 HG11 VAL A 242       0.769  25.450  -6.293  1.00 52.36           H  
ATOM   3361 HG12 VAL A 242      -0.081  26.418  -5.363  1.00 52.36           H  
ATOM   3362 HG13 VAL A 242       1.307  25.840  -4.850  1.00 52.36           H  
ATOM   3363 HG21 VAL A 242       0.920  23.057  -5.792  1.00 50.91           H  
ATOM   3364 HG22 VAL A 242       1.468  23.347  -4.329  1.00 50.91           H  
ATOM   3365 HG23 VAL A 242       0.173  22.448  -4.529  1.00 50.91           H  
ATOM   3366  N   ASP A 243      -1.029  27.049  -2.756  1.00 52.26           N  
ANISOU 3366  N   ASP A 243     5312   7737   6808   -170   -447    743       N  
ATOM   3367  CA  ASP A 243      -1.741  28.322  -2.801  1.00 52.09           C  
ANISOU 3367  CA  ASP A 243     5330   7519   6943   -174   -521    695       C  
ATOM   3368  C   ASP A 243      -1.496  28.944  -4.170  1.00 51.99           C  
ANISOU 3368  C   ASP A 243     5245   7448   7059   -280   -565    884       C  
ATOM   3369  O   ASP A 243      -0.434  29.518  -4.422  1.00 50.50           O  
ANISOU 3369  O   ASP A 243     4997   7244   6948   -410   -665    982       O  
ATOM   3370  CB  ASP A 243      -1.268  29.239  -1.681  1.00 53.27           C  
ANISOU 3370  CB  ASP A 243     5530   7552   7157   -191   -657    545       C  
ATOM   3371  CG  ASP A 243      -2.085  30.511  -1.584  1.00 56.90           C  
ANISOU 3371  CG  ASP A 243     6056   7789   7776   -149   -764    446       C  
ATOM   3372  OD1 ASP A 243      -2.764  30.867  -2.570  1.00 57.43           O  
ANISOU 3372  OD1 ASP A 243     6111   7773   7937   -154   -752    546       O  
ATOM   3373  OD2 ASP A 243      -2.044  31.160  -0.518  1.00 59.60           O  
ANISOU 3373  OD2 ASP A 243     6462   8039   8144    -96   -874    256       O  
ATOM   3374  H   ASP A 243      -0.258  27.094  -2.377  1.00 62.71           H  
ATOM   3375  HA  ASP A 243      -2.693  28.168  -2.695  1.00 62.51           H  
ATOM   3376  HB2 ASP A 243      -1.341  28.770  -0.836  1.00 63.92           H  
ATOM   3377  HB3 ASP A 243      -0.344  29.487  -1.845  1.00 63.92           H  
ATOM   3378  N   PHE A 244      -2.479  28.828  -5.068  1.00 48.92           N  
ANISOU 3378  N   PHE A 244     4849   7050   6690   -234   -493    954       N  
ATOM   3379  CA  PHE A 244      -2.310  29.366  -6.414  1.00 48.98           C  
ANISOU 3379  CA  PHE A 244     4775   7037   6797   -327   -526   1152       C  
ATOM   3380  C   PHE A 244      -1.942  30.845  -6.386  1.00 53.30           C  
ANISOU 3380  C   PHE A 244     5332   7373   7546   -443   -701   1193       C  
ATOM   3381  O   PHE A 244      -1.247  31.328  -7.288  1.00 51.63           O  
ANISOU 3381  O   PHE A 244     5024   7181   7411   -583   -766   1399       O  
ATOM   3382  CB  PHE A 244      -3.585  29.157  -7.235  1.00 47.44           C  
ANISOU 3382  CB  PHE A 244     4586   6836   6603   -244   -439   1188       C  
ATOM   3383  CG  PHE A 244      -3.743  27.763  -7.778  1.00 48.55           C  
ANISOU 3383  CG  PHE A 244     4687   7180   6581   -179   -310   1227       C  
ATOM   3384  CD1 PHE A 244      -3.242  26.669  -7.092  1.00 48.70           C  
ANISOU 3384  CD1 PHE A 244     4721   7325   6457   -137   -265   1152       C  
ATOM   3385  CD2 PHE A 244      -4.391  27.550  -8.985  1.00 49.07           C  
ANISOU 3385  CD2 PHE A 244     4705   7298   6644   -153   -255   1335       C  
ATOM   3386  CE1 PHE A 244      -3.392  25.390  -7.596  1.00 44.21           C  
ANISOU 3386  CE1 PHE A 244     4134   6901   5762    -70   -188   1177       C  
ATOM   3387  CE2 PHE A 244      -4.542  26.273  -9.492  1.00 45.62           C  
ANISOU 3387  CE2 PHE A 244     4242   7023   6069    -82   -171   1348       C  
ATOM   3388  CZ  PHE A 244      -4.041  25.193  -8.796  1.00 43.46           C  
ANISOU 3388  CZ  PHE A 244     3998   6844   5671    -40   -147   1266       C  
ATOM   3389  H   PHE A 244      -3.237  28.449  -4.923  1.00 58.71           H  
ATOM   3390  HA  PHE A 244      -1.590  28.889  -6.855  1.00 58.77           H  
ATOM   3391  HB2 PHE A 244      -4.352  29.345  -6.672  1.00 56.93           H  
ATOM   3392  HB3 PHE A 244      -3.574  29.768  -7.989  1.00 56.93           H  
ATOM   3393  HD1 PHE A 244      -2.805  26.795  -6.281  1.00 58.44           H  
ATOM   3394  HD2 PHE A 244      -4.732  28.275  -9.457  1.00 58.89           H  
ATOM   3395  HE1 PHE A 244      -3.053  24.663  -7.126  1.00 53.05           H  
ATOM   3396  HE2 PHE A 244      -4.980  26.143 -10.302  1.00 54.74           H  
ATOM   3397  HZ  PHE A 244      -4.140  24.334  -9.137  1.00 52.15           H  
ATOM   3398  N   ASP A 245      -2.394  31.578  -5.365  1.00 59.09           N  
ANISOU 3398  N   ASP A 245     6175   7913   8366   -386   -795   1005       N  
ATOM   3399  CA  ASP A 245      -2.090  33.004  -5.284  1.00 62.75           C  
ANISOU 3399  CA  ASP A 245     6674   8122   9046   -484  -1006   1019       C  
ATOM   3400  C   ASP A 245      -0.645  33.254  -4.874  1.00 66.29           C  
ANISOU 3400  C   ASP A 245     7077   8584   9526   -641  -1125   1067       C  
ATOM   3401  O   ASP A 245      -0.094  34.317  -5.181  1.00 68.83           O  
ANISOU 3401  O   ASP A 245     7382   8736  10035   -799  -1312   1187       O  
ATOM   3402  CB  ASP A 245      -3.038  33.689  -4.299  1.00 66.80           C  
ANISOU 3402  CB  ASP A 245     7320   8435   9627   -332  -1090    761       C  
ATOM   3403  CG  ASP A 245      -4.486  33.635  -4.744  1.00 63.30           C  
ANISOU 3403  CG  ASP A 245     6904   7975   9174   -185   -998    727       C  
ATOM   3404  OD1 ASP A 245      -4.743  33.784  -5.958  1.00 62.24           O  
ANISOU 3404  OD1 ASP A 245     6716   7825   9108   -246   -978    924       O  
ATOM   3405  OD2 ASP A 245      -5.367  33.444  -3.878  1.00 64.22           O  
ANISOU 3405  OD2 ASP A 245     7080   8121   9200     -8   -946    511       O  
ATOM   3406  H   ASP A 245      -2.871  31.277  -4.716  1.00 70.91           H  
ATOM   3407  HA  ASP A 245      -2.227  33.404  -6.157  1.00 75.30           H  
ATOM   3408  HB2 ASP A 245      -2.972  33.247  -3.438  1.00 80.16           H  
ATOM   3409  HB3 ASP A 245      -2.785  34.621  -4.214  1.00 80.16           H  
ATOM   3410  N   ASN A 246      -0.021  32.304  -4.179  1.00 67.32           N  
ANISOU 3410  N   ASN A 246     7185   8911   9481   -609  -1036    987       N  
ATOM   3411  CA  ASN A 246       1.360  32.452  -3.713  1.00 66.77           C  
ANISOU 3411  CA  ASN A 246     7063   8889   9417   -745  -1140   1019       C  
ATOM   3412  C   ASN A 246       1.970  31.065  -3.559  1.00 60.94           C  
ANISOU 3412  C   ASN A 246     6256   8450   8449   -697   -982   1027       C  
ATOM   3413  O   ASN A 246       2.114  30.548  -2.445  1.00 61.48           O  
ANISOU 3413  O   ASN A 246     6379   8574   8406   -612   -955    851       O  
ATOM   3414  CB  ASN A 246       1.414  33.225  -2.394  1.00 71.28           C  
ANISOU 3414  CB  ASN A 246     7750   9259  10074   -713  -1304    785       C  
ATOM   3415  CG  ASN A 246       2.831  33.548  -1.956  1.00 73.75           C  
ANISOU 3415  CG  ASN A 246     8008   9588  10427   -878  -1447    827       C  
ATOM   3416  OD1 ASN A 246       3.744  33.647  -2.778  1.00 73.04           O  
ANISOU 3416  OD1 ASN A 246     7786   9590  10374  -1061  -1482   1073       O  
ATOM   3417  ND2 ASN A 246       3.019  33.719  -0.651  1.00 76.06           N  
ANISOU 3417  ND2 ASN A 246     8385   9818  10697   -812  -1534    589       N  
ATOM   3418  H   ASN A 246      -0.380  31.554  -3.961  1.00 80.78           H  
ATOM   3419  HA  ASN A 246       1.873  32.940  -4.375  1.00 80.12           H  
ATOM   3420  HB2 ASN A 246       0.934  34.062  -2.499  1.00 85.54           H  
ATOM   3421  HB3 ASN A 246       1.000  32.691  -1.698  1.00 85.54           H  
ATOM   3422 HD21 ASN A 246       3.803  33.903  -0.350  1.00 91.27           H  
ATOM   3423 HD22 ASN A 246       2.356  33.644  -0.107  1.00 91.27           H  
ATOM   3424  N   PRO A 247       2.339  30.425  -4.670  1.00 54.56           N  
ANISOU 3424  N   PRO A 247     5324   7848   7558   -736   -886   1224       N  
ATOM   3425  CA  PRO A 247       2.833  29.040  -4.596  1.00 50.33           C  
ANISOU 3425  CA  PRO A 247     4737   7579   6807   -652   -754   1211       C  
ATOM   3426  C   PRO A 247       4.158  28.960  -3.851  1.00 52.06           C  
ANISOU 3426  C   PRO A 247     4904   7903   6973   -724   -825   1189       C  
ATOM   3427  O   PRO A 247       5.072  29.751  -4.094  1.00 52.54           O  
ANISOU 3427  O   PRO A 247     4871   7964   7128   -893   -947   1319       O  
ATOM   3428  CB  PRO A 247       2.992  28.637  -6.070  1.00 46.47           C  
ANISOU 3428  CB  PRO A 247     4113   7280   6263   -673   -681   1421       C  
ATOM   3429  CG  PRO A 247       2.221  29.646  -6.851  1.00 51.14           C  
ANISOU 3429  CG  PRO A 247     4711   7697   7021   -737   -730   1528       C  
ATOM   3430  CD  PRO A 247       2.268  30.910  -6.057  1.00 51.80           C  
ANISOU 3430  CD  PRO A 247     4876   7509   7296   -835   -900   1460       C  
ATOM   3431  HA  PRO A 247       2.179  28.465  -4.168  1.00 60.40           H  
ATOM   3432  HB2 PRO A 247       3.931  28.662  -6.314  1.00 55.76           H  
ATOM   3433  HB3 PRO A 247       2.628  27.749  -6.206  1.00 55.76           H  
ATOM   3434  HG2 PRO A 247       2.638  29.772  -7.717  1.00 61.36           H  
ATOM   3435  HG3 PRO A 247       1.305  29.343  -6.955  1.00 61.36           H  
ATOM   3436  HD2 PRO A 247       3.062  31.421  -6.279  1.00 62.16           H  
ATOM   3437  HD3 PRO A 247       1.459  31.428  -6.195  1.00 62.16           H  
ATOM   3438  N   ASP A 248       4.260  27.984  -2.947  1.00 51.87           N  
ANISOU 3438  N   ASP A 248     4934   7978   6797   -607   -757   1041       N  
ATOM   3439  CA  ASP A 248       5.505  27.710  -2.229  1.00 56.69           C  
ANISOU 3439  CA  ASP A 248     5493   8724   7324   -646   -808   1012       C  
ATOM   3440  C   ASP A 248       6.304  26.717  -3.061  1.00 57.71           C  
ANISOU 3440  C   ASP A 248     5486   9139   7302   -616   -732   1145       C  
ATOM   3441  O   ASP A 248       6.202  25.502  -2.888  1.00 56.69           O  
ANISOU 3441  O   ASP A 248     5389   9130   7020   -471   -642   1078       O  
ATOM   3442  CB  ASP A 248       5.218  27.175  -0.832  1.00 54.12           C  
ANISOU 3442  CB  ASP A 248     5288   8374   6903   -527   -784    799       C  
ATOM   3443  CG  ASP A 248       6.475  26.985  -0.006  1.00 56.29           C  
ANISOU 3443  CG  ASP A 248     5515   8773   7099   -565   -850    757       C  
ATOM   3444  OD1 ASP A 248       7.589  27.078  -0.567  1.00 56.86           O  
ANISOU 3444  OD1 ASP A 248     5450   8988   7166   -670   -895    898       O  
ATOM   3445  OD2 ASP A 248       6.348  26.736   1.213  1.00 58.21           O  
ANISOU 3445  OD2 ASP A 248     5846   9000   7271   -488   -856    590       O  
ATOM   3446  H   ASP A 248       3.613  27.461  -2.729  1.00 62.25           H  
ATOM   3447  HA  ASP A 248       6.020  28.528  -2.147  1.00 68.03           H  
ATOM   3448  HB2 ASP A 248       4.644  27.802  -0.365  1.00 64.95           H  
ATOM   3449  HB3 ASP A 248       4.776  26.315  -0.908  1.00 64.95           H  
ATOM   3450  N   TYR A 249       7.123  27.243  -3.974  1.00 55.85           N  
ANISOU 3450  N   TYR A 249     5090   9027   7105   -751   -784   1341       N  
ATOM   3451  CA  TYR A 249       7.862  26.381  -4.887  1.00 56.54           C  
ANISOU 3451  CA  TYR A 249     5020   9434   7029   -696   -717   1462       C  
ATOM   3452  C   TYR A 249       8.911  25.546  -4.168  1.00 54.66           C  
ANISOU 3452  C   TYR A 249     4741   9393   6632   -627   -720   1385       C  
ATOM   3453  O   TYR A 249       9.416  24.579  -4.747  1.00 58.70           O  
ANISOU 3453  O   TYR A 249     5157  10168   6979   -508   -663   1419       O  
ATOM   3454  CB  TYR A 249       8.525  27.214  -5.985  1.00 57.62           C  
ANISOU 3454  CB  TYR A 249     4959   9711   7223   -869   -775   1715       C  
ATOM   3455  CG  TYR A 249       7.544  27.914  -6.898  1.00 58.14           C  
ANISOU 3455  CG  TYR A 249     5043   9625   7422   -923   -769   1827       C  
ATOM   3456  CD1 TYR A 249       6.577  27.199  -7.590  1.00 53.52           C  
ANISOU 3456  CD1 TYR A 249     4506   9061   6767   -764   -651   1794       C  
ATOM   3457  CD2 TYR A 249       7.594  29.287  -7.077  1.00 59.49           C  
ANISOU 3457  CD2 TYR A 249     5184   9623   7796  -1135   -902   1972       C  
ATOM   3458  CE1 TYR A 249       5.681  27.835  -8.430  1.00 53.67           C  
ANISOU 3458  CE1 TYR A 249     4535   8956   6901   -806   -646   1897       C  
ATOM   3459  CE2 TYR A 249       6.704  29.932  -7.913  1.00 56.29           C  
ANISOU 3459  CE2 TYR A 249     4797   9073   7516  -1177   -909   2083       C  
ATOM   3460  CZ  TYR A 249       5.751  29.202  -8.587  1.00 55.46           C  
ANISOU 3460  CZ  TYR A 249     4732   9018   7324  -1008   -771   2044       C  
ATOM   3461  OH  TYR A 249       4.864  29.842  -9.421  1.00 57.95           O  
ANISOU 3461  OH  TYR A 249     5060   9203   7757  -1044   -778   2155       O  
ATOM   3462  H   TYR A 249       7.265  28.085  -4.082  1.00 67.03           H  
ATOM   3463  HA  TYR A 249       7.239  25.771  -5.312  1.00 67.85           H  
ATOM   3464  HB2 TYR A 249       9.080  27.893  -5.571  1.00 69.14           H  
ATOM   3465  HB3 TYR A 249       9.074  26.630  -6.532  1.00 69.14           H  
ATOM   3466  HD1 TYR A 249       6.528  26.276  -7.486  1.00 64.22           H  
ATOM   3467  HD2 TYR A 249       8.237  29.783  -6.623  1.00 71.39           H  
ATOM   3468  HE1 TYR A 249       5.037  27.343  -8.886  1.00 64.40           H  
ATOM   3469  HE2 TYR A 249       6.749  30.855  -8.021  1.00 67.54           H  
ATOM   3470  HH  TYR A 249       5.018  30.668  -9.423  1.00 69.54           H  
ATOM   3471  N   GLU A 250       9.251  25.894  -2.926  1.00 52.44           N  
ANISOU 3471  N   GLU A 250     4531   9000   6393   -680   -797   1269       N  
ATOM   3472  CA  GLU A 250      10.193  25.079  -2.167  1.00 53.87           C  
ANISOU 3472  CA  GLU A 250     4684   9361   6421   -604   -802   1189       C  
ATOM   3473  C   GLU A 250       9.554  23.759  -1.752  1.00 54.38           C  
ANISOU 3473  C   GLU A 250     4884   9421   6358   -391   -709   1048       C  
ATOM   3474  O   GLU A 250      10.152  22.689  -1.916  1.00 54.31           O  
ANISOU 3474  O   GLU A 250     4824   9620   6193   -262   -681   1043       O  
ATOM   3475  CB  GLU A 250      10.692  25.850  -0.943  1.00 59.29           C  
ANISOU 3475  CB  GLU A 250     5411   9930   7186   -720   -920   1100       C  
ATOM   3476  CG  GLU A 250      11.673  26.968  -1.268  1.00 60.89           C  
ANISOU 3476  CG  GLU A 250     5456  10182   7499   -950  -1052   1260       C  
ATOM   3477  H   GLU A 250       8.956  26.585  -2.508  1.00 62.93           H  
ATOM   3478  HA  GLU A 250      10.959  24.878  -2.727  1.00 64.64           H  
ATOM   3479  HB2 GLU A 250       9.929  26.247  -0.494  1.00 71.15           H  
ATOM   3480  HB3 GLU A 250      11.138  25.230  -0.346  1.00 71.15           H  
ATOM   3481  N   ARG A 251       8.330  23.815  -1.219  1.00 58.35           N  
ANISOU 3481  N   ARG A 251     5552   9692   6925   -349   -675    940       N  
ATOM   3482  CA  ARG A 251       7.618  22.598  -0.842  1.00 57.08           C  
ANISOU 3482  CA  ARG A 251     5512   9516   6660   -184   -602    847       C  
ATOM   3483  C   ARG A 251       6.994  21.900  -2.041  1.00 53.29           C  
ANISOU 3483  C   ARG A 251     5023   9072   6151    -90   -532    915       C  
ATOM   3484  O   ARG A 251       6.880  20.670  -2.045  1.00 53.60           O  
ANISOU 3484  O   ARG A 251     5113   9170   6082     50   -509    878       O  
ATOM   3485  CB  ARG A 251       6.518  22.916   0.170  1.00 56.31           C  
ANISOU 3485  CB  ARG A 251     5563   9214   6618   -177   -590    724       C  
ATOM   3486  CG  ARG A 251       6.995  23.567   1.451  1.00 58.26           C  
ANISOU 3486  CG  ARG A 251     5836   9422   6878   -235   -669    615       C  
ATOM   3487  CD  ARG A 251       5.816  23.858   2.358  1.00 61.32           C  
ANISOU 3487  CD  ARG A 251     6349   9660   7288   -190   -649    484       C  
ATOM   3488  NE  ARG A 251       5.091  22.637   2.702  1.00 64.11           N  
ANISOU 3488  NE  ARG A 251     6777  10065   7517    -70   -564    469       N  
ATOM   3489  CZ  ARG A 251       3.837  22.603   3.144  1.00 66.84           C  
ANISOU 3489  CZ  ARG A 251     7202  10339   7854    -18   -512    413       C  
ATOM   3490  NH1 ARG A 251       3.144  23.725   3.295  1.00 63.96           N  
ANISOU 3490  NH1 ARG A 251     6862   9849   7591    -41   -532    335       N  
ATOM   3491  NH2 ARG A 251       3.270  21.438   3.427  1.00 70.18           N  
ANISOU 3491  NH2 ARG A 251     7675  10822   8168     59   -454    441       N  
ATOM   3492  H   ARG A 251       7.896  24.541  -1.067  1.00 70.01           H  
ATOM   3493  HA  ARG A 251       8.242  21.982  -0.426  1.00 68.50           H  
ATOM   3494  HB2 ARG A 251       5.882  23.519  -0.246  1.00 67.57           H  
ATOM   3495  HB3 ARG A 251       6.072  22.089   0.410  1.00 67.57           H  
ATOM   3496  HG2 ARG A 251       7.599  22.966   1.914  1.00 69.91           H  
ATOM   3497  HG3 ARG A 251       7.439  24.404   1.244  1.00 69.91           H  
ATOM   3498  HD2 ARG A 251       6.136  24.263   3.179  1.00 73.58           H  
ATOM   3499  HD3 ARG A 251       5.203  24.458   1.904  1.00 73.58           H  
ATOM   3500  HE  ARG A 251       5.504  21.889   2.612  1.00 76.93           H  
ATOM   3501 HH11 ARG A 251       3.508  24.482   3.111  1.00 76.75           H  
ATOM   3502 HH12 ARG A 251       2.334  23.694   3.580  1.00 76.75           H  
ATOM   3503 HH21 ARG A 251       3.715  20.708   3.329  1.00 84.21           H  
ATOM   3504 HH22 ARG A 251       2.459  21.412   3.712  1.00 84.21           H  
ATOM   3505  N   PHE A 252       6.578  22.661  -3.053  1.00 51.34           N  
ANISOU 3505  N   PHE A 252     4719   8783   6005   -164   -516   1014       N  
ATOM   3506  CA  PHE A 252       5.802  22.143  -4.179  1.00 50.22           C  
ANISOU 3506  CA  PHE A 252     4578   8655   5848    -80   -453   1065       C  
ATOM   3507  C   PHE A 252       6.512  22.449  -5.494  1.00 49.55           C  
ANISOU 3507  C   PHE A 252     4311   8777   5739   -114   -458   1217       C  
ATOM   3508  O   PHE A 252       5.969  23.140  -6.364  1.00 52.75           O  
ANISOU 3508  O   PHE A 252     4675   9136   6233   -181   -440   1317       O  
ATOM   3509  CB  PHE A 252       4.399  22.742  -4.163  1.00 48.58           C  
ANISOU 3509  CB  PHE A 252     4474   8216   5769   -116   -417   1044       C  
ATOM   3510  CG  PHE A 252       3.741  22.701  -2.814  1.00 47.62           C  
ANISOU 3510  CG  PHE A 252     4492   7944   5659    -98   -414    909       C  
ATOM   3511  CD1 PHE A 252       3.535  21.494  -2.164  1.00 47.16           C  
ANISOU 3511  CD1 PHE A 252     4515   7917   5488      8   -392    840       C  
ATOM   3512  CD2 PHE A 252       3.327  23.868  -2.197  1.00 49.10           C  
ANISOU 3512  CD2 PHE A 252     4722   7970   5964   -179   -450    855       C  
ATOM   3513  CE1 PHE A 252       2.931  21.457  -0.923  1.00 50.15           C  
ANISOU 3513  CE1 PHE A 252     4994   8212   5851     20   -384    744       C  
ATOM   3514  CE2 PHE A 252       2.721  23.836  -0.958  1.00 49.50           C  
ANISOU 3514  CE2 PHE A 252     4876   7939   5992   -136   -445    720       C  
ATOM   3515  CZ  PHE A 252       2.523  22.630  -0.319  1.00 49.91           C  
ANISOU 3515  CZ  PHE A 252     4987   8068   5910    -43   -402    676       C  
ATOM   3516  H   PHE A 252       6.738  23.504  -3.110  1.00 61.61           H  
ATOM   3517  HA  PHE A 252       5.721  21.180  -4.095  1.00 60.26           H  
ATOM   3518  HB2 PHE A 252       4.452  23.671  -4.440  1.00 58.30           H  
ATOM   3519  HB3 PHE A 252       3.840  22.246  -4.782  1.00 58.30           H  
ATOM   3520  HD1 PHE A 252       3.809  20.702  -2.567  1.00 56.60           H  
ATOM   3521  HD2 PHE A 252       3.458  24.684  -2.623  1.00 58.92           H  
ATOM   3522  HE1 PHE A 252       2.798  20.642  -0.495  1.00 60.19           H  
ATOM   3523  HE2 PHE A 252       2.448  24.628  -0.553  1.00 59.40           H  
ATOM   3524  HZ  PHE A 252       2.115  22.607   0.516  1.00 59.90           H  
ATOM   3525  N   PRO A 253       7.726  21.924  -5.680  1.00 52.89           N  
ANISOU 3525  N   PRO A 253     4609   9461   6027    -60   -484   1243       N  
ATOM   3526  CA  PRO A 253       8.515  22.309  -6.863  1.00 48.48           C  
ANISOU 3526  CA  PRO A 253     3832   9172   5415   -104   -491   1409       C  
ATOM   3527  C   PRO A 253       7.850  21.983  -8.189  1.00 49.72           C  
ANISOU 3527  C   PRO A 253     3949   9409   5534     -8   -436   1466       C  
ATOM   3528  O   PRO A 253       7.934  22.785  -9.128  1.00 46.77           O  
ANISOU 3528  O   PRO A 253     3433   9143   5195   -113   -431   1635       O  
ATOM   3529  CB  PRO A 253       9.820  21.524  -6.675  1.00 46.26           C  
ANISOU 3529  CB  PRO A 253     3441   9181   4957      2   -522   1378       C  
ATOM   3530  CG  PRO A 253       9.477  20.410  -5.744  1.00 45.16           C  
ANISOU 3530  CG  PRO A 253     3487   8904   4767    158   -525   1194       C  
ATOM   3531  CD  PRO A 253       8.428  20.944  -4.835  1.00 49.70           C  
ANISOU 3531  CD  PRO A 253     4242   9146   5497     55   -512   1133       C  
ATOM   3532  HA  PRO A 253       8.712  23.259  -6.834  1.00 58.17           H  
ATOM   3533  HB2 PRO A 253      10.118  21.176  -7.530  1.00 55.52           H  
ATOM   3534  HB3 PRO A 253      10.496  22.100  -6.285  1.00 55.52           H  
ATOM   3535  HG2 PRO A 253       9.136  19.656  -6.251  1.00 54.19           H  
ATOM   3536  HG3 PRO A 253      10.265  20.153  -5.240  1.00 54.19           H  
ATOM   3537  HD2 PRO A 253       7.824  20.237  -4.562  1.00 59.64           H  
ATOM   3538  HD3 PRO A 253       8.834  21.384  -4.071  1.00 59.64           H  
ATOM   3539  N   ASN A 254       7.202  20.824  -8.308  1.00 54.43           N  
ANISOU 3539  N   ASN A 254     4661   9961   6059    183   -409   1340       N  
ATOM   3540  CA  ASN A 254       6.612  20.438  -9.586  1.00 54.32           C  
ANISOU 3540  CA  ASN A 254     4607  10038   5996    293   -375   1371       C  
ATOM   3541  C   ASN A 254       5.398  21.276  -9.970  1.00 51.94           C  
ANISOU 3541  C   ASN A 254     4364   9521   5851    179   -333   1441       C  
ATOM   3542  O   ASN A 254       4.881  21.100 -11.079  1.00 50.62           O  
ANISOU 3542  O   ASN A 254     4149   9434   5649    251   -304   1484       O  
ATOM   3543  CB  ASN A 254       6.234  18.958  -9.559  1.00 51.61           C  
ANISOU 3543  CB  ASN A 254     4389   9662   5558    518   -397   1209       C  
ATOM   3544  CG  ASN A 254       7.444  18.051  -9.673  1.00 56.78           C  
ANISOU 3544  CG  ASN A 254     4949  10598   6027    697   -454   1144       C  
ATOM   3545  OD1 ASN A 254       7.695  17.215  -8.804  1.00 57.35           O  
ANISOU 3545  OD1 ASN A 254     5133  10594   6063    788   -508   1025       O  
ATOM   3546  ND2 ASN A 254       8.210  18.220 -10.748  1.00 55.36           N  
ANISOU 3546  ND2 ASN A 254     4549  10767   5717    754   -448   1230       N  
ATOM   3547  H   ASN A 254       7.092  20.253  -7.674  1.00 65.32           H  
ATOM   3548  HA  ASN A 254       7.279  20.557 -10.280  1.00 65.19           H  
ATOM   3549  HB2 ASN A 254       5.787  18.759  -8.722  1.00 61.93           H  
ATOM   3550  HB3 ASN A 254       5.644  18.767 -10.305  1.00 61.93           H  
ATOM   3551 HD21 ASN A 254       8.908  17.730 -10.859  1.00 66.43           H  
ATOM   3552 HD22 ASN A 254       8.007  18.818 -11.331  1.00 66.43           H  
ATOM   3553  N   PHE A 255       4.931  22.179  -9.107  1.00 44.76           N  
ANISOU 3553  N   PHE A 255     3550   8353   5103     24   -339   1442       N  
ATOM   3554  CA  PHE A 255       3.877  23.099  -9.515  1.00 48.08           C  
ANISOU 3554  CA  PHE A 255     4007   8588   5673    -74   -316   1513       C  
ATOM   3555  C   PHE A 255       4.349  24.049 -10.608  1.00 49.39           C  
ANISOU 3555  C   PHE A 255     3986   8914   5865   -192   -332   1725       C  
ATOM   3556  O   PHE A 255       3.516  24.646 -11.299  1.00 47.36           O  
ANISOU 3556  O   PHE A 255     3730   8562   5700   -238   -315   1811       O  
ATOM   3557  CB  PHE A 255       3.376  23.890  -8.306  1.00 50.77           C  
ANISOU 3557  CB  PHE A 255     4482   8640   6167   -183   -342   1441       C  
ATOM   3558  CG  PHE A 255       2.175  24.742  -8.597  1.00 48.16           C  
ANISOU 3558  CG  PHE A 255     4215   8097   5988   -239   -330   1473       C  
ATOM   3559  CD1 PHE A 255       0.931  24.164  -8.788  1.00 51.83           C  
ANISOU 3559  CD1 PHE A 255     4777   8471   6447   -135   -268   1403       C  
ATOM   3560  CD2 PHE A 255       2.288  26.119  -8.672  1.00 49.81           C  
ANISOU 3560  CD2 PHE A 255     4384   8190   6350   -398   -400   1577       C  
ATOM   3561  CE1 PHE A 255      -0.178  24.945  -9.055  1.00 50.00           C  
ANISOU 3561  CE1 PHE A 255     4591   8065   6343   -171   -257   1427       C  
ATOM   3562  CE2 PHE A 255       1.184  26.905  -8.937  1.00 51.24           C  
ANISOU 3562  CE2 PHE A 255     4629   8166   6673   -426   -405   1596       C  
ATOM   3563  CZ  PHE A 255      -0.051  26.317  -9.129  1.00 51.15           C  
ANISOU 3563  CZ  PHE A 255     4703   8094   6637   -304   -325   1516       C  
ATOM   3564  H   PHE A 255       5.202  22.277  -8.296  1.00 53.71           H  
ATOM   3565  HA  PHE A 255       3.132  22.587  -9.866  1.00 57.70           H  
ATOM   3566  HB2 PHE A 255       3.135  23.267  -7.603  1.00 60.92           H  
ATOM   3567  HB3 PHE A 255       4.086  24.474  -7.999  1.00 60.92           H  
ATOM   3568  HD1 PHE A 255       0.841  23.240  -8.740  1.00 62.20           H  
ATOM   3569  HD2 PHE A 255       3.117  26.520  -8.544  1.00 59.77           H  
ATOM   3570  HE1 PHE A 255      -1.008  24.546  -9.183  1.00 60.00           H  
ATOM   3571  HE2 PHE A 255       1.272  27.829  -8.987  1.00 61.48           H  
ATOM   3572  HZ  PHE A 255      -0.795  26.845  -9.308  1.00 61.38           H  
ATOM   3573  N   GLN A 256       5.663  24.201 -10.778  1.00 54.02           N  
ANISOU 3573  N   GLN A 256     4400   9759   6366   -247   -370   1829       N  
ATOM   3574  CA  GLN A 256       6.211  24.998 -11.868  1.00 60.61           C  
ANISOU 3574  CA  GLN A 256     5018  10818   7191   -369   -389   2073       C  
ATOM   3575  C   GLN A 256       6.092  24.303 -13.216  1.00 52.94           C  
ANISOU 3575  C   GLN A 256     3923  10143   6049   -209   -329   2122       C  
ATOM   3576  O   GLN A 256       6.446  24.907 -14.234  1.00 55.64           O  
ANISOU 3576  O   GLN A 256     4066  10720   6355   -295   -333   2342       O  
ATOM   3577  CB  GLN A 256       7.680  25.320 -11.593  1.00 63.60           C  
ANISOU 3577  CB  GLN A 256     5225  11429   7511   -484   -451   2182       C  
ATOM   3578  CG  GLN A 256       7.907  26.091 -10.306  1.00 63.78           C  
ANISOU 3578  CG  GLN A 256     5354  11179   7702   -652   -537   2136       C  
ATOM   3579  CD  GLN A 256       9.378  26.266  -9.976  1.00 70.05           C  
ANISOU 3579  CD  GLN A 256     5977  12214   8425   -756   -605   2226       C  
ATOM   3580  OE1 GLN A 256       9.918  27.372 -10.059  1.00 73.27           O  
ANISOU 3580  OE1 GLN A 256     6272  12620   8948   -992   -701   2422       O  
ATOM   3581  NE2 GLN A 256      10.034  25.175  -9.593  1.00 65.97           N  
ANISOU 3581  NE2 GLN A 256     5441  11898   7724   -586   -571   2090       N  
ATOM   3582  H   GLN A 256       6.260  23.849 -10.270  1.00 64.82           H  
ATOM   3583  HA  GLN A 256       5.725  25.836 -11.920  1.00 72.73           H  
ATOM   3584  HB2 GLN A 256       8.176  24.489 -11.532  1.00 76.32           H  
ATOM   3585  HB3 GLN A 256       8.024  25.856 -12.324  1.00 76.32           H  
ATOM   3586  HG2 GLN A 256       7.512  26.972 -10.392  1.00 76.54           H  
ATOM   3587  HG3 GLN A 256       7.491  25.611  -9.573  1.00 76.54           H  
ATOM   3588 HE21 GLN A 256       9.623  24.422  -9.542  1.00 79.16           H  
ATOM   3589 HE22 GLN A 256      10.870  25.223  -9.395  1.00 79.16           H  
ATOM   3590  N   ASN A 257       5.628  23.055 -13.243  1.00 50.00           N  
ANISOU 3590  N   ASN A 257     3656   9774   5569     19   -290   1928       N  
ATOM   3591  CA  ASN A 257       5.420  22.311 -14.478  1.00 50.67           C  
ANISOU 3591  CA  ASN A 257     3651  10108   5492    206   -256   1922       C  
ATOM   3592  C   ASN A 257       3.945  22.116 -14.791  1.00 45.34           C  
ANISOU 3592  C   ASN A 257     3135   9186   4908    263   -223   1847       C  
ATOM   3593  O   ASN A 257       3.612  21.396 -15.738  1.00 51.05           O  
ANISOU 3593  O   ASN A 257     3821  10064   5510    435   -210   1801       O  
ATOM   3594  CB  ASN A 257       6.106  20.947 -14.399  1.00 49.17           C  
ANISOU 3594  CB  ASN A 257     3451  10129   5101    449   -279   1748       C  
ATOM   3595  CG  ASN A 257       7.533  21.042 -13.931  1.00 48.96           C  
ANISOU 3595  CG  ASN A 257     3281  10341   4980    411   -312   1793       C  
ATOM   3596  OD1 ASN A 257       7.893  20.496 -12.888  1.00 52.89           O  
ANISOU 3596  OD1 ASN A 257     3889  10730   5476    458   -345   1652       O  
ATOM   3597  ND2 ASN A 257       8.360  21.736 -14.700  1.00 55.78           N  
ANISOU 3597  ND2 ASN A 257     3884  11552   5758    319   -307   2007       N  
ATOM   3598  H   ASN A 257       5.421  22.608 -12.537  1.00 60.00           H  
ATOM   3599  HA  ASN A 257       5.818  22.804 -15.212  1.00 60.80           H  
ATOM   3600  HB2 ASN A 257       5.622  20.385 -13.774  1.00 59.00           H  
ATOM   3601  HB3 ASN A 257       6.106  20.541 -15.280  1.00 59.00           H  
ATOM   3602 HD21 ASN A 257       9.186  21.821 -14.476  1.00 66.94           H  
ATOM   3603 HD22 ASN A 257       8.070  22.102 -15.422  1.00 66.94           H  
ATOM   3604  N   VAL A 258       3.059  22.730 -14.020  1.00 46.95           N  
ANISOU 3604  N   VAL A 258     3503   9027   5309    136   -218   1825       N  
ATOM   3605  CA  VAL A 258       1.628  22.498 -14.164  1.00 52.43           C  
ANISOU 3605  CA  VAL A 258     4345   9493   6084    189   -187   1746       C  
ATOM   3606  C   VAL A 258       1.112  23.243 -15.386  1.00 52.25           C  
ANISOU 3606  C   VAL A 258     4214   9545   6093    139   -163   1913       C  
ATOM   3607  O   VAL A 258       1.494  24.391 -15.645  1.00 50.31           O  
ANISOU 3607  O   VAL A 258     3856   9335   5923    -27   -182   2105       O  
ATOM   3608  CB  VAL A 258       0.886  22.926 -12.884  1.00 50.15           C  
ANISOU 3608  CB  VAL A 258     4242   8848   5967     92   -188   1660       C  
ATOM   3609  CG1 VAL A 258       0.677  24.436 -12.848  1.00 51.94           C  
ANISOU 3609  CG1 VAL A 258     4443   8925   6365    -93   -208   1798       C  
ATOM   3610  CG2 VAL A 258      -0.437  22.200 -12.775  1.00 53.75           C  
ANISOU 3610  CG2 VAL A 258     4849   9127   6447    190   -159   1536       C  
ATOM   3611  H   VAL A 258       3.262  23.292 -13.401  1.00 56.34           H  
ATOM   3612  HA  VAL A 258       1.472  21.550 -14.300  1.00 62.92           H  
ATOM   3613  HB  VAL A 258       1.423  22.682 -12.114  1.00 60.19           H  
ATOM   3614 HG11 VAL A 258       0.208  24.670 -12.031  1.00 62.32           H  
ATOM   3615 HG12 VAL A 258       1.542  24.874 -12.870  1.00 62.32           H  
ATOM   3616 HG13 VAL A 258       0.152  24.700 -13.619  1.00 62.32           H  
ATOM   3617 HG21 VAL A 258      -0.887  22.484 -11.964  1.00 64.50           H  
ATOM   3618 HG22 VAL A 258      -0.981  22.416 -13.548  1.00 64.50           H  
ATOM   3619 HG23 VAL A 258      -0.270  21.245 -12.743  1.00 64.50           H  
ATOM   3620  N   VAL A 259       0.233  22.587 -16.143  1.00 54.78           N  
ANISOU 3620  N   VAL A 259     4569   9883   6362    275   -138   1851       N  
ATOM   3621  CA  VAL A 259      -0.401  23.176 -17.319  1.00 53.51           C  
ANISOU 3621  CA  VAL A 259     4318   9795   6219    252   -113   1993       C  
ATOM   3622  C   VAL A 259      -1.876  22.805 -17.277  1.00 55.04           C  
ANISOU 3622  C   VAL A 259     4674   9743   6496    313    -92   1877       C  
ATOM   3623  O   VAL A 259      -2.219  21.617 -17.239  1.00 52.19           O  
ANISOU 3623  O   VAL A 259     4399   9373   6058    463   -104   1712       O  
ATOM   3624  CB  VAL A 259       0.235  22.694 -18.636  1.00 54.32           C  
ANISOU 3624  CB  VAL A 259     4219  10316   6103    388   -110   2057       C  
ATOM   3625  CG1 VAL A 259      -0.450  23.346 -19.834  1.00 53.97           C  
ANISOU 3625  CG1 VAL A 259     4076  10359   6072    357    -85   2222       C  
ATOM   3626  CG2 VAL A 259       1.726  22.992 -18.651  1.00 56.37           C  
ANISOU 3626  CG2 VAL A 259     4288  10876   6254    332   -129   2182       C  
ATOM   3627  H   VAL A 259      -0.017  21.778 -15.990  1.00 65.74           H  
ATOM   3628  HA  VAL A 259      -0.326  24.142 -17.277  1.00 64.21           H  
ATOM   3629  HB  VAL A 259       0.119  21.733 -18.710  1.00 65.18           H  
ATOM   3630 HG11 VAL A 259      -0.031  23.027 -20.649  1.00 64.77           H  
ATOM   3631 HG12 VAL A 259      -1.390  23.108 -19.829  1.00 64.77           H  
ATOM   3632 HG13 VAL A 259      -0.352  24.309 -19.767  1.00 64.77           H  
ATOM   3633 HG21 VAL A 259       2.101  22.679 -19.489  1.00 67.64           H  
ATOM   3634 HG22 VAL A 259       1.857  23.949 -18.566  1.00 67.64           H  
ATOM   3635 HG23 VAL A 259       2.147  22.533 -17.908  1.00 67.64           H  
ATOM   3636  N   GLY A 260      -2.748  23.812 -17.288  1.00 55.95           N  
ANISOU 3636  N   GLY A 260     4828   9658   6771    198    -76   1966       N  
ATOM   3637  CA  GLY A 260      -4.169  23.594 -17.151  1.00 55.88           C  
ANISOU 3637  CA  GLY A 260     4955   9430   6845    239    -53   1870       C  
ATOM   3638  C   GLY A 260      -4.938  23.759 -18.451  1.00 56.51           C  
ANISOU 3638  C   GLY A 260     4960   9605   6904    284    -33   1960       C  
ATOM   3639  O   GLY A 260      -4.439  24.295 -19.438  1.00 56.59           O  
ANISOU 3639  O   GLY A 260     4810   9831   6859    257    -36   2130       O  
ATOM   3640  H   GLY A 260      -2.530  24.639 -17.375  1.00 67.13           H  
ATOM   3641  HA2 GLY A 260      -4.323  22.696 -16.819  1.00 67.05           H  
ATOM   3642  HA3 GLY A 260      -4.527  24.222 -16.504  1.00 67.05           H  
ATOM   3643  N   TYR A 261      -6.170  23.262 -18.434  1.00 55.21           N  
ANISOU 3643  N   TYR A 261     4902   9301   6775    349    -18   1855       N  
ATOM   3644  CA  TYR A 261      -7.141  23.496 -19.493  1.00 50.47           C  
ANISOU 3644  CA  TYR A 261     4256   8734   6185    383     -1   1923       C  
ATOM   3645  C   TYR A 261      -8.150  24.516 -18.984  1.00 48.59           C  
ANISOU 3645  C   TYR A 261     4096   8236   6130    288     16   1961       C  
ATOM   3646  O   TYR A 261      -8.730  24.332 -17.909  1.00 44.68           O  
ANISOU 3646  O   TYR A 261     3728   7543   5706    278     25   1838       O  
ATOM   3647  CB  TYR A 261      -7.847  22.199 -19.891  1.00 55.16           C  
ANISOU 3647  CB  TYR A 261     4906   9364   6690    527    -17   1777       C  
ATOM   3648  CG  TYR A 261      -6.943  21.172 -20.538  1.00 58.49           C  
ANISOU 3648  CG  TYR A 261     5254  10044   6924    672    -63   1707       C  
ATOM   3649  CD1 TYR A 261      -6.050  20.422 -19.782  1.00 60.95           C  
ANISOU 3649  CD1 TYR A 261     5615  10366   7176    715   -102   1597       C  
ATOM   3650  CD2 TYR A 261      -6.993  20.944 -21.905  1.00 61.58           C  
ANISOU 3650  CD2 TYR A 261     5524  10685   7186    788    -78   1739       C  
ATOM   3651  CE1 TYR A 261      -5.226  19.480 -20.374  1.00 60.72           C  
ANISOU 3651  CE1 TYR A 261     5520  10579   6970    882   -161   1509       C  
ATOM   3652  CE2 TYR A 261      -6.176  20.007 -22.506  1.00 62.46           C  
ANISOU 3652  CE2 TYR A 261     5564  11061   7108    960   -134   1644       C  
ATOM   3653  CZ  TYR A 261      -5.295  19.278 -21.738  1.00 62.19           C  
ANISOU 3653  CZ  TYR A 261     5585  11021   7023   1014   -179   1524       C  
ATOM   3654  OH  TYR A 261      -4.483  18.345 -22.341  1.00 63.30           O  
ANISOU 3654  OH  TYR A 261     5653  11429   6969   1219   -251   1407       O  
ATOM   3655  H   TYR A 261      -6.475  22.770 -17.798  1.00 66.25           H  
ATOM   3656  HA  TYR A 261      -6.695  23.861 -20.273  1.00 60.56           H  
ATOM   3657  HB2 TYR A 261      -8.229  21.796 -19.095  1.00 66.20           H  
ATOM   3658  HB3 TYR A 261      -8.553  22.410 -20.522  1.00 66.20           H  
ATOM   3659  HD1 TYR A 261      -6.002  20.559 -18.863  1.00 73.14           H  
ATOM   3660  HD2 TYR A 261      -7.586  21.434 -22.428  1.00 73.89           H  
ATOM   3661  HE1 TYR A 261      -4.630  18.987 -19.857  1.00 72.86           H  
ATOM   3662  HE2 TYR A 261      -6.220  19.868 -23.424  1.00 74.95           H  
ATOM   3663  HH  TYR A 261      -4.630  18.328 -23.168  1.00 75.96           H  
ATOM   3664  N   GLU A 262      -8.355  25.586 -19.748  1.00 47.42           N  
ANISOU 3664  N   GLU A 262     3864   8104   6048    227     11   2132       N  
ATOM   3665  CA  GLU A 262      -9.089  26.744 -19.263  1.00 49.82           C  
ANISOU 3665  CA  GLU A 262     4235   8157   6538    147     -4   2174       C  
ATOM   3666  C   GLU A 262     -10.300  27.035 -20.140  1.00 50.89           C  
ANISOU 3666  C   GLU A 262     4348   8278   6708    193     11   2230       C  
ATOM   3667  O   GLU A 262     -10.307  26.750 -21.341  1.00 51.52           O  
ANISOU 3667  O   GLU A 262     4321   8571   6684    243     22   2319       O  
ATOM   3668  CB  GLU A 262      -8.180  27.978 -19.212  1.00 49.80           C  
ANISOU 3668  CB  GLU A 262     4172   8114   6637      5    -69   2347       C  
ATOM   3669  CG  GLU A 262      -8.875  29.232 -18.714  1.00 54.00           C  
ANISOU 3669  CG  GLU A 262     4788   8353   7377    -58   -128   2371       C  
ATOM   3670  CD  GLU A 262      -7.904  30.354 -18.427  1.00 50.75           C  
ANISOU 3670  CD  GLU A 262     4350   7842   7091   -212   -233   2512       C  
ATOM   3671  OE1 GLU A 262      -6.687  30.139 -18.594  1.00 55.76           O  
ANISOU 3671  OE1 GLU A 262     4884   8664   7638   -283   -242   2605       O  
ATOM   3672  OE2 GLU A 262      -8.355  31.448 -18.030  1.00 52.23           O  
ANISOU 3672  OE2 GLU A 262     4615   7765   7466   -259   -321   2526       O  
ATOM   3673  H   GLU A 262      -8.075  25.663 -20.557  1.00 56.90           H  
ATOM   3674  HA  GLU A 262      -9.405  26.565 -18.364  1.00 59.79           H  
ATOM   3675  HB2 GLU A 262      -7.437  27.795 -18.617  1.00 59.76           H  
ATOM   3676  HB3 GLU A 262      -7.848  28.159 -20.106  1.00 59.76           H  
ATOM   3677  HG2 GLU A 262      -9.498  29.540 -19.391  1.00 64.80           H  
ATOM   3678  HG3 GLU A 262      -9.349  29.027 -17.893  1.00 64.80           H  
ATOM   3679  N   THR A 263     -11.327  27.608 -19.518  1.00 47.36           N  
ANISOU 3679  N   THR A 263     3997   7602   6396    192      8   2170       N  
ATOM   3680  CA  THR A 263     -12.503  28.090 -20.230  1.00 47.20           C  
ANISOU 3680  CA  THR A 263     3958   7542   6433    233     12   2228       C  
ATOM   3681  C   THR A 263     -13.342  28.920 -19.272  1.00 42.90           C  
ANISOU 3681  C   THR A 263     3517   6741   6044    237    -12   2147       C  
ATOM   3682  O   THR A 263     -13.227  28.796 -18.049  1.00 46.27           O  
ANISOU 3682  O   THR A 263     4031   7058   6492    235    -10   2005       O  
ATOM   3683  CB  THR A 263     -13.340  26.940 -20.807  1.00 48.60           C  
ANISOU 3683  CB  THR A 263     4122   7852   6490    336     63   2143       C  
ATOM   3684  OG1 THR A 263     -14.271  27.456 -21.763  1.00 48.79           O  
ANISOU 3684  OG1 THR A 263     4091   7898   6548    370     61   2241       O  
ATOM   3685  CG2 THR A 263     -14.109  26.217 -19.714  1.00 44.93           C  
ANISOU 3685  CG2 THR A 263     3766   7275   6030    373     93   1956       C  
ATOM   3686  H   THR A 263     -11.365  27.731 -18.667  1.00 56.83           H  
ATOM   3687  HA  THR A 263     -12.223  28.660 -20.963  1.00 56.64           H  
ATOM   3688  HB  THR A 263     -12.754  26.301 -21.242  1.00 58.32           H  
ATOM   3689  HG1 THR A 263     -14.732  26.830 -22.082  1.00 58.55           H  
ATOM   3690 HG21 THR A 263     -14.631  25.495 -20.098  1.00 53.91           H  
ATOM   3691 HG22 THR A 263     -13.492  25.848 -19.063  1.00 53.91           H  
ATOM   3692 HG23 THR A 263     -14.708  26.834 -19.266  1.00 53.91           H  
ATOM   3693  N   VAL A 264     -14.192  29.766 -19.847  1.00 45.25           N  
ANISOU 3693  N   VAL A 264     3796   6962   6434    261    -41   2230       N  
ATOM   3694  CA  VAL A 264     -15.186  30.527 -19.099  1.00 47.37           C  
ANISOU 3694  CA  VAL A 264     4148   7019   6829    317    -70   2132       C  
ATOM   3695  C   VAL A 264     -16.557  30.088 -19.592  1.00 45.01           C  
ANISOU 3695  C   VAL A 264     3824   6799   6481    418    -11   2091       C  
ATOM   3696  O   VAL A 264     -16.874  30.243 -20.778  1.00 46.55           O  
ANISOU 3696  O   VAL A 264     3941   7083   6664    429    -15   2226       O  
ATOM   3697  CB  VAL A 264     -14.996  32.042 -19.270  1.00 48.24           C  
ANISOU 3697  CB  VAL A 264     4272   6933   7123    267   -195   2262       C  
ATOM   3698  CG1 VAL A 264     -16.098  32.810 -18.550  1.00 49.30           C  
ANISOU 3698  CG1 VAL A 264     4494   6861   7378    377   -243   2124       C  
ATOM   3699  CG2 VAL A 264     -13.636  32.464 -18.747  1.00 48.30           C  
ANISOU 3699  CG2 VAL A 264     4300   6862   7190    144   -273   2309       C  
ATOM   3700  H   VAL A 264     -14.212  29.919 -20.693  1.00 54.30           H  
ATOM   3701  HA  VAL A 264     -15.115  30.313 -18.156  1.00 56.84           H  
ATOM   3702  HB  VAL A 264     -15.040  32.264 -20.214  1.00 57.88           H  
ATOM   3703 HG11 VAL A 264     -15.953  33.761 -18.674  1.00 59.16           H  
ATOM   3704 HG12 VAL A 264     -16.956  32.554 -18.922  1.00 59.16           H  
ATOM   3705 HG13 VAL A 264     -16.069  32.592 -17.605  1.00 59.16           H  
ATOM   3706 HG21 VAL A 264     -13.536  33.422 -18.864  1.00 57.96           H  
ATOM   3707 HG22 VAL A 264     -13.576  32.237 -17.806  1.00 57.96           H  
ATOM   3708 HG23 VAL A 264     -12.947  31.996 -19.245  1.00 57.96           H  
ATOM   3709  N   VAL A 265     -17.361  29.527 -18.692  1.00 45.47           N  
ANISOU 3709  N   VAL A 265     3930   6847   6498    484     42   1919       N  
ATOM   3710  CA  VAL A 265     -18.707  29.069 -19.021  1.00 48.65           C  
ANISOU 3710  CA  VAL A 265     4298   7337   6852    563     93   1880       C  
ATOM   3711  C   VAL A 265     -19.699  30.157 -18.640  1.00 47.35           C  
ANISOU 3711  C   VAL A 265     4153   7043   6795    655     59   1833       C  
ATOM   3712  O   VAL A 265     -19.520  30.859 -17.635  1.00 45.89           O  
ANISOU 3712  O   VAL A 265     4037   6714   6686    683     13   1738       O  
ATOM   3713  CB  VAL A 265     -19.047  27.739 -18.315  1.00 40.83           C  
ANISOU 3713  CB  VAL A 265     3323   6448   5743    563    158   1756       C  
ATOM   3714  CG1 VAL A 265     -18.158  26.620 -18.832  1.00 45.88           C  
ANISOU 3714  CG1 VAL A 265     3949   7203   6280    507    162   1786       C  
ATOM   3715  CG2 VAL A 265     -18.916  27.871 -16.808  1.00 44.95           C  
ANISOU 3715  CG2 VAL A 265     3914   6890   6276    569    164   1624       C  
ATOM   3716  H   VAL A 265     -17.145  29.399 -17.869  1.00 54.56           H  
ATOM   3717  HA  VAL A 265     -18.768  28.926 -19.978  1.00 58.39           H  
ATOM   3718  HB  VAL A 265     -19.967  27.505 -18.515  1.00 49.00           H  
ATOM   3719 HG11 VAL A 265     -18.390  25.797 -18.375  1.00 55.05           H  
ATOM   3720 HG12 VAL A 265     -18.300  26.521 -19.787  1.00 55.05           H  
ATOM   3721 HG13 VAL A 265     -17.232  26.847 -18.657  1.00 55.05           H  
ATOM   3722 HG21 VAL A 265     -19.136  27.020 -16.397  1.00 53.95           H  
ATOM   3723 HG22 VAL A 265     -18.003  28.117 -16.591  1.00 53.95           H  
ATOM   3724 HG23 VAL A 265     -19.527  28.557 -16.497  1.00 53.95           H  
ATOM   3725  N   GLY A 266     -20.740  30.309 -19.453  1.00 44.72           N  
ANISOU 3725  N   GLY A 266     3760   6766   6464    721     68   1886       N  
ATOM   3726  CA  GLY A 266     -21.794  31.251 -19.181  1.00 47.85           C  
ANISOU 3726  CA  GLY A 266     4163   7072   6946    841     33   1830       C  
ATOM   3727  C   GLY A 266     -23.142  30.573 -19.276  1.00 49.87           C  
ANISOU 3727  C   GLY A 266     4347   7494   7106    913    108   1775       C  
ATOM   3728  O   GLY A 266     -23.238  29.357 -19.474  1.00 49.64           O  
ANISOU 3728  O   GLY A 266     4280   7620   6962    852    171   1777       O  
ATOM   3729  H   GLY A 266     -20.852  29.864 -20.180  1.00 53.66           H  
ATOM   3730  HA2 GLY A 266     -21.687  31.616 -18.289  1.00 57.42           H  
ATOM   3731  HA3 GLY A 266     -21.761  31.977 -19.824  1.00 57.42           H  
ATOM   3732  N   PRO A 267     -24.214  31.349 -19.136  1.00 46.97           N  
ANISOU 3732  N   PRO A 267     3959   7099   6789   1045     84   1723       N  
ATOM   3733  CA  PRO A 267     -25.561  30.770 -19.196  1.00 45.94           C  
ANISOU 3733  CA  PRO A 267     3736   7157   6562   1111    152   1682       C  
ATOM   3734  C   PRO A 267     -25.768  29.932 -20.450  1.00 48.11           C  
ANISOU 3734  C   PRO A 267     3939   7568   6772   1038    183   1806       C  
ATOM   3735  O   PRO A 267     -25.519  30.384 -21.571  1.00 48.46           O  
ANISOU 3735  O   PRO A 267     3968   7577   6867   1032    139   1935       O  
ATOM   3736  CB  PRO A 267     -26.469  32.003 -19.183  1.00 46.34           C  
ANISOU 3736  CB  PRO A 267     3774   7133   6701   1284     92   1640       C  
ATOM   3737  CG  PRO A 267     -25.673  33.041 -18.459  1.00 49.41           C  
ANISOU 3737  CG  PRO A 267     4274   7288   7213   1324     -6   1570       C  
ATOM   3738  CD  PRO A 267     -24.240  32.792 -18.839  1.00 47.43           C  
ANISOU 3738  CD  PRO A 267     4078   6947   6996   1150    -26   1688       C  
ATOM   3739  HA  PRO A 267     -25.736  30.229 -18.410  1.00 55.13           H  
ATOM   3740  HB2 PRO A 267     -26.657  32.284 -20.092  1.00 55.61           H  
ATOM   3741  HB3 PRO A 267     -27.289  31.802 -18.706  1.00 55.61           H  
ATOM   3742  HG2 PRO A 267     -25.953  33.925 -18.745  1.00 59.29           H  
ATOM   3743  HG3 PRO A 267     -25.795  32.937 -17.502  1.00 59.29           H  
ATOM   3744  HD2 PRO A 267     -24.006  33.304 -19.629  1.00 56.92           H  
ATOM   3745  HD3 PRO A 267     -23.652  32.996 -18.095  1.00 56.92           H  
ATOM   3746  N   GLY A 268     -26.221  28.693 -20.251  1.00 47.76           N  
ANISOU 3746  N   GLY A 268     3848   7686   6612    981    242   1771       N  
ATOM   3747  CA  GLY A 268     -26.484  27.770 -21.331  1.00 46.94           C  
ANISOU 3747  CA  GLY A 268     3684   7708   6441    922    246   1848       C  
ATOM   3748  C   GLY A 268     -25.357  26.798 -21.620  1.00 50.02           C  
ANISOU 3748  C   GLY A 268     4122   8103   6781    814    233   1868       C  
ATOM   3749  O   GLY A 268     -25.592  25.776 -22.277  1.00 48.10           O  
ANISOU 3749  O   GLY A 268     3843   7965   6466    772    218   1883       O  
ATOM   3750  H   GLY A 268     -26.384  28.364 -19.474  1.00 57.31           H  
ATOM   3751  HA2 GLY A 268     -27.278  27.254 -21.119  1.00 56.33           H  
ATOM   3752  HA3 GLY A 268     -26.661  28.274 -22.141  1.00 56.33           H  
ATOM   3753  N   ASP A 269     -24.147  27.085 -21.148  1.00 48.65           N  
ANISOU 3753  N   ASP A 269     4026   7819   6641    778    222   1858       N  
ATOM   3754  CA  ASP A 269     -23.011  26.208 -21.389  1.00 47.52           C  
ANISOU 3754  CA  ASP A 269     3918   7698   6439    701    206   1867       C  
ATOM   3755  C   ASP A 269     -22.986  25.064 -20.382  1.00 48.18           C  
ANISOU 3755  C   ASP A 269     4045   7801   6460    638    219   1772       C  
ATOM   3756  O   ASP A 269     -23.362  25.220 -19.216  1.00 49.84           O  
ANISOU 3756  O   ASP A 269     4273   7984   6679    638    251   1707       O  
ATOM   3757  CB  ASP A 269     -21.697  26.986 -21.302  1.00 48.19           C  
ANISOU 3757  CB  ASP A 269     4049   7681   6580    677    184   1914       C  
ATOM   3758  CG  ASP A 269     -21.587  28.077 -22.350  1.00 51.97           C  
ANISOU 3758  CG  ASP A 269     4481   8141   7125    706    148   2056       C  
ATOM   3759  OD1 ASP A 269     -22.201  27.939 -23.429  1.00 53.85           O  
ANISOU 3759  OD1 ASP A 269     4644   8491   7323    743    145   2124       O  
ATOM   3760  OD2 ASP A 269     -20.876  29.072 -22.094  1.00 54.21           O  
ANISOU 3760  OD2 ASP A 269     4799   8296   7503    683    109   2111       O  
ATOM   3761  H   ASP A 269     -23.959  27.784 -20.684  1.00 58.38           H  
ATOM   3762  HA  ASP A 269     -23.082  25.830 -22.279  1.00 57.02           H  
ATOM   3763  HB2 ASP A 269     -21.634  27.403 -20.428  1.00 57.83           H  
ATOM   3764  HB3 ASP A 269     -20.957  26.372 -21.430  1.00 57.83           H  
ATOM   3765  N   VAL A 270     -22.526  23.904 -20.846  1.00 43.65           N  
ANISOU 3765  N   VAL A 270     3486   7284   5817    593    180   1764       N  
ATOM   3766  CA  VAL A 270     -22.357  22.724 -20.007  1.00 42.14           C  
ANISOU 3766  CA  VAL A 270     3348   7084   5578    522    158   1697       C  
ATOM   3767  C   VAL A 270     -20.923  22.238 -20.168  1.00 44.75           C  
ANISOU 3767  C   VAL A 270     3738   7392   5872    511    118   1675       C  
ATOM   3768  O   VAL A 270     -20.514  21.857 -21.272  1.00 41.38           O  
ANISOU 3768  O   VAL A 270     3289   7036   5399    550     70   1689       O  
ATOM   3769  CB  VAL A 270     -23.349  21.607 -20.369  1.00 42.83           C  
ANISOU 3769  CB  VAL A 270     3402   7243   5627    483    104   1694       C  
ATOM   3770  CG1 VAL A 270     -23.072  20.353 -19.546  1.00 42.56           C  
ANISOU 3770  CG1 VAL A 270     3436   7172   5562    392     45   1654       C  
ATOM   3771  CG2 VAL A 270     -24.785  22.078 -20.151  1.00 46.76           C  
ANISOU 3771  CG2 VAL A 270     3816   7808   6144    492    150   1724       C  
ATOM   3772  H   VAL A 270     -22.301  23.774 -21.666  1.00 52.39           H  
ATOM   3773  HA  VAL A 270     -22.495  22.966 -19.078  1.00 50.56           H  
ATOM   3774  HB  VAL A 270     -23.245  21.381 -21.307  1.00 51.39           H  
ATOM   3775 HG11 VAL A 270     -23.710  19.666 -19.794  1.00 51.07           H  
ATOM   3776 HG12 VAL A 270     -22.169  20.049 -19.730  1.00 51.07           H  
ATOM   3777 HG13 VAL A 270     -23.164  20.567 -18.605  1.00 51.07           H  
ATOM   3778 HG21 VAL A 270     -25.392  21.359 -20.385  1.00 56.12           H  
ATOM   3779 HG22 VAL A 270     -24.899  22.318 -19.218  1.00 56.12           H  
ATOM   3780 HG23 VAL A 270     -24.952  22.850 -20.714  1.00 56.12           H  
ATOM   3781  N   LEU A 271     -20.165  22.255 -19.075  1.00 45.97           N  
ANISOU 3781  N   LEU A 271     3956   7476   6033    474    135   1635       N  
ATOM   3782  CA  LEU A 271     -18.792  21.771 -19.060  1.00 39.39           C  
ANISOU 3782  CA  LEU A 271     3173   6634   5158    467     97   1608       C  
ATOM   3783  C   LEU A 271     -18.769  20.350 -18.520  1.00 40.14           C  
ANISOU 3783  C   LEU A 271     3332   6712   5207    422     31   1546       C  
ATOM   3784  O   LEU A 271     -19.297  20.084 -17.435  1.00 37.31           O  
ANISOU 3784  O   LEU A 271     3000   6317   4860    359     46   1534       O  
ATOM   3785  CB  LEU A 271     -17.899  22.673 -18.205  1.00 38.44           C  
ANISOU 3785  CB  LEU A 271     3086   6442   5080    449    138   1606       C  
ATOM   3786  CG  LEU A 271     -16.493  22.151 -17.884  1.00 38.61           C  
ANISOU 3786  CG  LEU A 271     3154   6463   5052    432    106   1572       C  
ATOM   3787  CD1 LEU A 271     -15.662  22.032 -19.155  1.00 40.83           C  
ANISOU 3787  CD1 LEU A 271     3380   6859   5274    482     71   1616       C  
ATOM   3788  CD2 LEU A 271     -15.811  23.050 -16.873  1.00 38.55           C  
ANISOU 3788  CD2 LEU A 271     3178   6372   5095    399    137   1561       C  
ATOM   3789  H   LEU A 271     -20.432  22.550 -18.313  1.00 55.16           H  
ATOM   3790  HA  LEU A 271     -18.442  21.761 -19.965  1.00 47.26           H  
ATOM   3791  HB2 LEU A 271     -17.791  23.518 -18.668  1.00 46.13           H  
ATOM   3792  HB3 LEU A 271     -18.347  22.826 -17.359  1.00 46.13           H  
ATOM   3793  HG  LEU A 271     -16.568  21.266 -17.493  1.00 46.33           H  
ATOM   3794 HD11 LEU A 271     -14.780  21.701 -18.925  1.00 48.99           H  
ATOM   3795 HD12 LEU A 271     -16.100  21.415 -19.762  1.00 48.99           H  
ATOM   3796 HD13 LEU A 271     -15.590  22.907 -19.568  1.00 48.99           H  
ATOM   3797 HD21 LEU A 271     -14.926  22.700 -16.687  1.00 46.26           H  
ATOM   3798 HD22 LEU A 271     -15.743  23.945 -17.242  1.00 46.26           H  
ATOM   3799 HD23 LEU A 271     -16.338  23.067 -16.059  1.00 46.26           H  
ATOM   3800  N   TYR A 272     -18.159  19.445 -19.276  1.00 42.54           N  
ANISOU 3800  N   TYR A 272     3655   7052   5454    463    -55   1509       N  
ATOM   3801  CA  TYR A 272     -17.945  18.077 -18.823  1.00 43.10           C  
ANISOU 3801  CA  TYR A 272     3809   7070   5498    434   -160   1446       C  
ATOM   3802  C   TYR A 272     -16.630  18.037 -18.056  1.00 44.78           C  
ANISOU 3802  C   TYR A 272     4078   7251   5685    436   -153   1410       C  
ATOM   3803  O   TYR A 272     -15.560  18.254 -18.634  1.00 46.68           O  
ANISOU 3803  O   TYR A 272     4297   7563   5878    510   -156   1393       O  
ATOM   3804  CB  TYR A 272     -17.925  17.108 -20.002  1.00 40.61           C  
ANISOU 3804  CB  TYR A 272     3499   6797   5135    511   -288   1388       C  
ATOM   3805  CG  TYR A 272     -17.448  15.720 -19.632  1.00 39.60           C  
ANISOU 3805  CG  TYR A 272     3475   6582   4990    510   -438   1305       C  
ATOM   3806  CD1 TYR A 272     -18.027  15.024 -18.580  1.00 44.12           C  
ANISOU 3806  CD1 TYR A 272     4113   7035   5615    385   -491   1335       C  
ATOM   3807  CD2 TYR A 272     -16.422  15.106 -20.336  1.00 43.36           C  
ANISOU 3807  CD2 TYR A 272     3977   7107   5391    641   -539   1205       C  
ATOM   3808  CE1 TYR A 272     -17.592  13.756 -18.235  1.00 46.87           C  
ANISOU 3808  CE1 TYR A 272     4568   7274   5967    375   -655   1280       C  
ATOM   3809  CE2 TYR A 272     -15.982  13.836 -20.000  1.00 43.20           C  
ANISOU 3809  CE2 TYR A 272     4066   6982   5365    663   -704   1116       C  
ATOM   3810  CZ  TYR A 272     -16.569  13.167 -18.947  1.00 43.04           C  
ANISOU 3810  CZ  TYR A 272     4128   6801   5424    522   -769   1160       C  
ATOM   3811  OH  TYR A 272     -16.136  11.905 -18.608  1.00 41.51           O  
ANISOU 3811  OH  TYR A 272     4054   6474   5244    535   -959   1090       O  
ATOM   3812  H   TYR A 272     -17.857  19.600 -20.066  1.00 51.04           H  
ATOM   3813  HA  TYR A 272     -18.661  17.818 -18.222  1.00 51.72           H  
ATOM   3814  HB2 TYR A 272     -18.824  17.028 -20.357  1.00 48.73           H  
ATOM   3815  HB3 TYR A 272     -17.330  17.455 -20.684  1.00 48.73           H  
ATOM   3816  HD1 TYR A 272     -18.715  15.419 -18.095  1.00 52.94           H  
ATOM   3817  HD2 TYR A 272     -16.022  15.555 -21.045  1.00 52.03           H  
ATOM   3818  HE1 TYR A 272     -17.989  13.303 -17.526  1.00 56.24           H  
ATOM   3819  HE2 TYR A 272     -15.292  13.439 -20.480  1.00 51.84           H  
ATOM   3820  HH  TYR A 272     -16.579  11.615 -17.955  1.00 49.81           H  
ATOM   3821  N   ILE A 273     -16.710  17.777 -16.755  1.00 43.92           N  
ANISOU 3821  N   ILE A 273     4025   7068   5596    354   -143   1410       N  
ATOM   3822  CA  ILE A 273     -15.518  17.584 -15.934  1.00 40.08           C  
ANISOU 3822  CA  ILE A 273     3599   6549   5081    351   -152   1371       C  
ATOM   3823  C   ILE A 273     -15.373  16.086 -15.699  1.00 45.34           C  
ANISOU 3823  C   ILE A 273     4352   7148   5726    337   -295   1331       C  
ATOM   3824  O   ILE A 273     -16.108  15.524 -14.873  1.00 46.68           O  
ANISOU 3824  O   ILE A 273     4556   7259   5921    237   -328   1374       O  
ATOM   3825  CB  ILE A 273     -15.607  18.354 -14.608  1.00 41.84           C  
ANISOU 3825  CB  ILE A 273     3824   6745   5328    285    -57   1392       C  
ATOM   3826  CG1 ILE A 273     -15.833  19.843 -14.882  1.00 41.77           C  
ANISOU 3826  CG1 ILE A 273     3746   6758   5365    312     42   1419       C  
ATOM   3827  CG2 ILE A 273     -14.332  18.137 -13.795  1.00 43.25           C  
ANISOU 3827  CG2 ILE A 273     4061   6900   5473    284    -74   1350       C  
ATOM   3828  CD1 ILE A 273     -15.991  20.695 -13.642  1.00 42.63           C  
ANISOU 3828  CD1 ILE A 273     3859   6839   5499    284    113   1402       C  
ATOM   3829  H   ILE A 273     -17.448  17.707 -16.320  1.00 52.71           H  
ATOM   3830  HA  ILE A 273     -14.738  17.897 -16.419  1.00 48.10           H  
ATOM   3831  HB  ILE A 273     -16.361  18.013 -14.101  1.00 50.21           H  
ATOM   3832 HG12 ILE A 273     -15.072  20.185 -15.378  1.00 50.12           H  
ATOM   3833 HG13 ILE A 273     -16.639  19.942 -15.412  1.00 50.12           H  
ATOM   3834 HG21 ILE A 273     -14.403  18.628 -12.961  1.00 51.90           H  
ATOM   3835 HG22 ILE A 273     -14.231  17.189 -13.614  1.00 51.90           H  
ATOM   3836 HG23 ILE A 273     -13.574  18.459 -14.307  1.00 51.90           H  
ATOM   3837 HD11 ILE A 273     -16.129  21.618 -13.909  1.00 51.16           H  
ATOM   3838 HD12 ILE A 273     -16.757  20.379 -13.138  1.00 51.16           H  
ATOM   3839 HD13 ILE A 273     -15.188  20.622 -13.104  1.00 51.16           H  
ATOM   3840  N   PRO A 274     -14.461  15.397 -16.386  1.00 47.20           N  
ANISOU 3840  N   PRO A 274     4622   7399   5914    438   -398   1255       N  
ATOM   3841  CA  PRO A 274     -14.336  13.952 -16.173  1.00 43.71           C  
ANISOU 3841  CA  PRO A 274     4284   6853   5471    442   -575   1203       C  
ATOM   3842  C   PRO A 274     -13.844  13.651 -14.765  1.00 46.91           C  
ANISOU 3842  C   PRO A 274     4758   7185   5880    365   -577   1226       C  
ATOM   3843  O   PRO A 274     -13.164  14.460 -14.129  1.00 48.87           O  
ANISOU 3843  O   PRO A 274     4980   7485   6104    359   -461   1234       O  
ATOM   3844  CB  PRO A 274     -13.314  13.510 -17.231  1.00 42.57           C  
ANISOU 3844  CB  PRO A 274     4142   6783   5250    619   -671   1087       C  
ATOM   3845  CG  PRO A 274     -13.099  14.691 -18.126  1.00 41.12           C  
ANISOU 3845  CG  PRO A 274     3832   6770   5021    681   -537   1114       C  
ATOM   3846  CD  PRO A 274     -13.456  15.901 -17.337  1.00 40.02           C  
ANISOU 3846  CD  PRO A 274     3650   6617   4939    560   -372   1218       C  
ATOM   3847  HA  PRO A 274     -15.183  13.506 -16.328  1.00 52.45           H  
ATOM   3848  HB2 PRO A 274     -12.484  13.259 -16.795  1.00 51.08           H  
ATOM   3849  HB3 PRO A 274     -13.672  12.763 -17.735  1.00 51.08           H  
ATOM   3850  HG2 PRO A 274     -12.168  14.726 -18.396  1.00 49.34           H  
ATOM   3851  HG3 PRO A 274     -13.673  14.614 -18.904  1.00 49.34           H  
ATOM   3852  HD2 PRO A 274     -12.680  16.238 -16.863  1.00 48.02           H  
ATOM   3853  HD3 PRO A 274     -13.844  16.579 -17.913  1.00 48.02           H  
ATOM   3854  N   MET A 275     -14.196  12.462 -14.280  1.00 51.22           N  
ANISOU 3854  N   MET A 275     5395   7606   6461    298   -729   1245       N  
ATOM   3855  CA  MET A 275     -13.813  12.068 -12.930  1.00 52.11           C  
ANISOU 3855  CA  MET A 275     5571   7659   6571    215   -748   1292       C  
ATOM   3856  C   MET A 275     -12.297  12.112 -12.774  1.00 45.37           C  
ANISOU 3856  C   MET A 275     4748   6835   5655    331   -749   1200       C  
ATOM   3857  O   MET A 275     -11.551  11.797 -13.704  1.00 45.53           O  
ANISOU 3857  O   MET A 275     4779   6883   5636    481   -830   1094       O  
ATOM   3858  CB  MET A 275     -14.342  10.667 -12.615  1.00 53.35           C  
ANISOU 3858  CB  MET A 275     5824   7661   6785    124   -958   1347       C  
ATOM   3859  CG  MET A 275     -13.921   9.589 -13.601  1.00 59.16           C  
ANISOU 3859  CG  MET A 275     6653   8282   7542    252  -1187   1228       C  
ATOM   3860  SD  MET A 275     -14.551   7.966 -13.125  1.00 66.64           S  
ANISOU 3860  SD  MET A 275     7736   8989   8597    114  -1483   1315       S  
ATOM   3861  CE  MET A 275     -13.921   6.945 -14.461  1.00 67.23           C  
ANISOU 3861  CE  MET A 275     7921   8939   8686    343  -1756   1098       C  
ATOM   3862  H   MET A 275     -14.653  11.872 -14.707  1.00 61.47           H  
ATOM   3863  HA  MET A 275     -14.211  12.686 -12.298  1.00 62.54           H  
ATOM   3864  HB2 MET A 275     -14.020  10.405 -11.739  1.00 64.02           H  
ATOM   3865  HB3 MET A 275     -15.312  10.697 -12.610  1.00 64.02           H  
ATOM   3866  HG2 MET A 275     -14.271   9.805 -14.480  1.00 70.99           H  
ATOM   3867  HG3 MET A 275     -12.952   9.543 -13.629  1.00 70.99           H  
ATOM   3868  HE1 MET A 275     -14.200   6.028 -14.315  1.00 80.68           H  
ATOM   3869  HE2 MET A 275     -14.279   7.271 -15.302  1.00 80.68           H  
ATOM   3870  HE3 MET A 275     -12.953   7.000 -14.470  1.00 80.68           H  
ATOM   3871  N   TYR A 276     -11.847  12.524 -11.589  1.00 46.29           N  
ANISOU 3871  N   TYR A 276     4865   6975   5747    270   -660   1238       N  
ATOM   3872  CA  TYR A 276     -10.441  12.622 -11.197  1.00 46.46           C  
ANISOU 3872  CA  TYR A 276     4907   7037   5710    350   -651   1172       C  
ATOM   3873  C   TYR A 276      -9.693  13.745 -11.908  1.00 42.52           C  
ANISOU 3873  C   TYR A 276     4312   6674   5171    439   -532   1122       C  
ATOM   3874  O   TYR A 276      -8.482  13.884 -11.702  1.00 45.89           O  
ANISOU 3874  O   TYR A 276     4730   7165   5543    502   -526   1075       O  
ATOM   3875  CB  TYR A 276      -9.678  11.307 -11.414  1.00 45.02           C  
ANISOU 3875  CB  TYR A 276     4826   6771   5510    454   -855   1095       C  
ATOM   3876  CG  TYR A 276     -10.075  10.224 -10.440  1.00 51.21           C  
ANISOU 3876  CG  TYR A 276     5716   7402   6338    347   -996   1173       C  
ATOM   3877  CD1 TYR A 276      -9.568  10.211  -9.148  1.00 50.69           C  
ANISOU 3877  CD1 TYR A 276     5676   7342   6241    283   -965   1225       C  
ATOM   3878  CD2 TYR A 276     -10.959   9.216 -10.807  1.00 54.57           C  
ANISOU 3878  CD2 TYR A 276     6211   7684   6840    297  -1174   1211       C  
ATOM   3879  CE1 TYR A 276      -9.930   9.227  -8.247  1.00 54.96           C  
ANISOU 3879  CE1 TYR A 276     6303   7765   6816    171  -1099   1332       C  
ATOM   3880  CE2 TYR A 276     -11.326   8.227  -9.913  1.00 55.25           C  
ANISOU 3880  CE2 TYR A 276     6387   7628   6978    169  -1324   1324       C  
ATOM   3881  CZ  TYR A 276     -10.809   8.237  -8.635  1.00 55.63           C  
ANISOU 3881  CZ  TYR A 276     6452   7700   6985    105  -1281   1394       C  
ATOM   3882  OH  TYR A 276     -11.174   7.251  -7.746  1.00 59.43           O  
ANISOU 3882  OH  TYR A 276     7011   8059   7511    -35  -1436   1539       O  
ATOM   3883  H   TYR A 276     -12.376  12.768 -10.956  1.00 55.55           H  
ATOM   3884  HA  TYR A 276     -10.409  12.816 -10.247  1.00 55.76           H  
ATOM   3885  HB2 TYR A 276      -9.858  10.983 -12.310  1.00 54.03           H  
ATOM   3886  HB3 TYR A 276      -8.728  11.473 -11.306  1.00 54.03           H  
ATOM   3887  HD1 TYR A 276      -8.976  10.878  -8.882  1.00 60.82           H  
ATOM   3888  HD2 TYR A 276     -11.311   9.208 -11.668  1.00 65.49           H  
ATOM   3889  HE1 TYR A 276      -9.582   9.231  -7.384  1.00 65.95           H  
ATOM   3890  HE2 TYR A 276     -11.918   7.559 -10.172  1.00 66.30           H  
ATOM   3891  HH  TYR A 276     -10.790   7.373  -7.009  1.00 71.32           H  
ATOM   3892  N   TRP A 277     -10.360  14.553 -12.727  1.00 45.95           N  
ANISOU 3892  N   TRP A 277     4665   7163   5631    435   -446   1148       N  
ATOM   3893  CA  TRP A 277      -9.740  15.755 -13.265  1.00 41.73           C  
ANISOU 3893  CA  TRP A 277     4032   6748   5076    475   -336   1151       C  
ATOM   3894  C   TRP A 277      -9.811  16.869 -12.232  1.00 43.46           C  
ANISOU 3894  C   TRP A 277     4228   6951   5332    378   -215   1195       C  
ATOM   3895  O   TRP A 277     -10.878  17.143 -11.673  1.00 39.27           O  
ANISOU 3895  O   TRP A 277     3704   6371   4846    302   -166   1233       O  
ATOM   3896  CB  TRP A 277     -10.432  16.200 -14.551  1.00 42.50           C  
ANISOU 3896  CB  TRP A 277     4055   6905   5189    511   -308   1176       C  
ATOM   3897  CG  TRP A 277      -9.965  15.479 -15.765  1.00 41.08           C  
ANISOU 3897  CG  TRP A 277     3856   6816   4937    653   -410   1108       C  
ATOM   3898  CD1 TRP A 277     -10.106  14.150 -16.033  1.00 42.46           C  
ANISOU 3898  CD1 TRP A 277     4113   6926   5095    727   -570   1026       C  
ATOM   3899  CD2 TRP A 277      -9.284  16.047 -16.889  1.00 40.44           C  
ANISOU 3899  CD2 TRP A 277     3659   6924   4782    750   -375   1114       C  
ATOM   3900  NE1 TRP A 277      -9.553  13.852 -17.254  1.00 47.20           N  
ANISOU 3900  NE1 TRP A 277     4659   7670   5605    894   -638    946       N  
ATOM   3901  CE2 TRP A 277      -9.041  15.001 -17.801  1.00 44.53           C  
ANISOU 3901  CE2 TRP A 277     4186   7517   5216    907   -508   1010       C  
ATOM   3902  CE3 TRP A 277      -8.855  17.338 -17.213  1.00 43.57           C  
ANISOU 3902  CE3 TRP A 277     3940   7440   5174    715   -262   1208       C  
ATOM   3903  CZ2 TRP A 277      -8.388  15.205 -19.014  1.00 39.35           C  
ANISOU 3903  CZ2 TRP A 277     3408   7101   4442   1046   -509    992       C  
ATOM   3904  CZ3 TRP A 277      -8.207  17.539 -18.417  1.00 42.53           C  
ANISOU 3904  CZ3 TRP A 277     3686   7533   4942    819   -266   1227       C  
ATOM   3905  CH2 TRP A 277      -7.979  16.477 -19.303  1.00 41.72           C  
ANISOU 3905  CH2 TRP A 277     3576   7551   4726    990   -377   1117       C  
ATOM   3906  H   TRP A 277     -11.170  14.427 -12.985  1.00 55.14           H  
ATOM   3907  HA  TRP A 277      -8.807  15.578 -13.462  1.00 50.08           H  
ATOM   3908  HB2 TRP A 277     -11.385  16.046 -14.462  1.00 51.00           H  
ATOM   3909  HB3 TRP A 277     -10.264  17.146 -14.685  1.00 51.00           H  
ATOM   3910  HD1 TRP A 277     -10.517  13.534 -15.470  1.00 50.95           H  
ATOM   3911  HE1 TRP A 277      -9.531  13.073 -17.616  1.00 56.64           H  
ATOM   3912  HE3 TRP A 277      -9.003  18.047 -16.629  1.00 52.28           H  
ATOM   3913  HZ2 TRP A 277      -8.235  14.502 -19.604  1.00 47.22           H  
ATOM   3914  HZ3 TRP A 277      -7.917  18.393 -18.643  1.00 51.04           H  
ATOM   3915  HH2 TRP A 277      -7.541  16.642 -20.107  1.00 50.07           H  
ATOM   3916  N   TRP A 278      -8.674  17.507 -11.975  1.00 41.50           N  
ANISOU 3916  N   TRP A 278     3948   6762   5060    388   -179   1183       N  
ATOM   3917  CA  TRP A 278      -8.670  18.670 -11.105  1.00 41.43           C  
ANISOU 3917  CA  TRP A 278     3920   6724   5097    313    -93   1202       C  
ATOM   3918  C   TRP A 278      -9.485  19.789 -11.742  1.00 39.25           C  
ANISOU 3918  C   TRP A 278     3582   6437   4894    293    -27   1252       C  
ATOM   3919  O   TRP A 278      -9.553  19.912 -12.968  1.00 39.56           O  
ANISOU 3919  O   TRP A 278     3563   6534   4935    334    -32   1291       O  
ATOM   3920  CB  TRP A 278      -7.240  19.148 -10.854  1.00 42.57           C  
ANISOU 3920  CB  TRP A 278     4033   6930   5213    316    -95   1189       C  
ATOM   3921  CG  TRP A 278      -6.342  18.115 -10.242  1.00 41.43           C  
ANISOU 3921  CG  TRP A 278     3942   6809   4991    354   -164   1136       C  
ATOM   3922  CD1 TRP A 278      -5.714  17.085 -10.883  1.00 40.99           C  
ANISOU 3922  CD1 TRP A 278     3891   6820   4861    455   -249   1100       C  
ATOM   3923  CD2 TRP A 278      -5.962  18.022  -8.866  1.00 40.06           C  
ANISOU 3923  CD2 TRP A 278     3822   6599   4798    310   -166   1104       C  
ATOM   3924  NE1 TRP A 278      -4.970  16.355  -9.989  1.00 43.20           N  
ANISOU 3924  NE1 TRP A 278     4234   7089   5091    475   -309   1054       N  
ATOM   3925  CE2 TRP A 278      -5.104  16.910  -8.744  1.00 42.29           C  
ANISOU 3925  CE2 TRP A 278     4146   6916   5005    378   -254   1065       C  
ATOM   3926  CE3 TRP A 278      -6.263  18.770  -7.725  1.00 40.94           C  
ANISOU 3926  CE3 TRP A 278     3950   6665   4939    239   -111   1091       C  
ATOM   3927  CZ2 TRP A 278      -4.548  16.529  -7.525  1.00 41.10           C  
ANISOU 3927  CZ2 TRP A 278     4050   6751   4814    358   -282   1038       C  
ATOM   3928  CZ3 TRP A 278      -5.709  18.390  -6.518  1.00 40.11           C  
ANISOU 3928  CZ3 TRP A 278     3892   6567   4780    225   -135   1055       C  
ATOM   3929  CH2 TRP A 278      -4.861  17.281  -6.427  1.00 40.49           C  
ANISOU 3929  CH2 TRP A 278     3980   6647   4760    275   -216   1040       C  
ATOM   3930  H   TRP A 278      -7.903  17.289 -12.288  1.00 49.80           H  
ATOM   3931  HA  TRP A 278      -9.073  18.441 -10.253  1.00 49.71           H  
ATOM   3932  HB2 TRP A 278      -6.849  19.414 -11.701  1.00 51.09           H  
ATOM   3933  HB3 TRP A 278      -7.268  19.908 -10.253  1.00 51.09           H  
ATOM   3934  HD1 TRP A 278      -5.782  16.904 -11.793  1.00 49.18           H  
ATOM   3935  HE1 TRP A 278      -4.496  15.663 -10.180  1.00 51.84           H  
ATOM   3936  HE3 TRP A 278      -6.825  19.509  -7.777  1.00 49.12           H  
ATOM   3937  HZ2 TRP A 278      -3.984  15.792  -7.461  1.00 49.31           H  
ATOM   3938  HZ3 TRP A 278      -5.903  18.881  -5.752  1.00 48.13           H  
ATOM   3939  HH2 TRP A 278      -4.504  17.048  -5.601  1.00 48.59           H  
ATOM   3940  N   HIS A 279     -10.123  20.602 -10.903  1.00 37.63           N  
ANISOU 3940  N   HIS A 279     3386   6169   4742    247     27   1243       N  
ATOM   3941  CA  HIS A 279     -10.778  21.807 -11.393  1.00 42.96           C  
ANISOU 3941  CA  HIS A 279     4012   6811   5500    244     70   1278       C  
ATOM   3942  C   HIS A 279     -10.641  22.922 -10.369  1.00 43.02           C  
ANISOU 3942  C   HIS A 279     4035   6748   5561    220     87   1231       C  
ATOM   3943  O   HIS A 279     -10.806  22.701  -9.165  1.00 42.35           O  
ANISOU 3943  O   HIS A 279     3993   6662   5438    215     98   1164       O  
ATOM   3944  CB  HIS A 279     -12.260  21.566 -11.739  1.00 40.98           C  
ANISOU 3944  CB  HIS A 279     3750   6558   5263    258     95   1297       C  
ATOM   3945  CG  HIS A 279     -12.997  20.697 -10.765  1.00 44.53           C  
ANISOU 3945  CG  HIS A 279     4239   7019   5663    231     97   1272       C  
ATOM   3946  ND1 HIS A 279     -12.798  19.336 -10.683  1.00 48.41           N  
ANISOU 3946  ND1 HIS A 279     4775   7521   6097    213     34   1280       N  
ATOM   3947  CD2 HIS A 279     -13.964  20.990  -9.862  1.00 38.18           C  
ANISOU 3947  CD2 HIS A 279     3423   6234   4851    220    143   1255       C  
ATOM   3948  CE1 HIS A 279     -13.594  18.831  -9.757  1.00 42.52           C  
ANISOU 3948  CE1 HIS A 279     4043   6793   5320    163     39   1298       C  
ATOM   3949  NE2 HIS A 279     -14.313  19.814  -9.244  1.00 37.73           N  
ANISOU 3949  NE2 HIS A 279     3390   6219   4728    171    116   1282       N  
ATOM   3950  H   HIS A 279     -10.191  20.478 -10.055  1.00 45.15           H  
ATOM   3951  HA  HIS A 279     -10.330  22.095 -12.204  1.00 51.55           H  
ATOM   3952  HB2 HIS A 279     -12.714  22.422 -11.770  1.00 49.18           H  
ATOM   3953  HB3 HIS A 279     -12.309  21.139 -12.608  1.00 49.18           H  
ATOM   3954  HD1 HIS A 279     -12.237  18.886 -11.154  1.00 58.09           H  
ATOM   3955  HD2 HIS A 279     -14.318  21.832  -9.686  1.00 45.82           H  
ATOM   3956  HE1 HIS A 279     -13.641  17.936  -9.509  1.00 51.03           H  
ATOM   3957  N   HIS A 280     -10.304  24.109 -10.865  1.00 45.26           N  
ANISOU 3957  N   HIS A 280     4283   6981   5934    205     71   1272       N  
ATOM   3958  CA  HIS A 280     -10.246  25.340 -10.088  1.00 45.89           C  
ANISOU 3958  CA  HIS A 280     4386   6951   6100    194     47   1218       C  
ATOM   3959  C   HIS A 280     -11.324  26.253 -10.658  1.00 45.67           C  
ANISOU 3959  C   HIS A 280     4337   6849   6167    231     49   1243       C  
ATOM   3960  O   HIS A 280     -11.235  26.674 -11.815  1.00 49.29           O  
ANISOU 3960  O   HIS A 280     4745   7299   6682    211     30   1356       O  
ATOM   3961  CB  HIS A 280      -8.852  25.962 -10.184  1.00 47.61           C  
ANISOU 3961  CB  HIS A 280     4585   7141   6365    126    -16   1263       C  
ATOM   3962  CG  HIS A 280      -8.791  27.408  -9.797  1.00 46.81           C  
ANISOU 3962  CG  HIS A 280     4505   6882   6400    101    -89   1239       C  
ATOM   3963  ND1 HIS A 280      -8.269  27.833  -8.595  1.00 47.92           N  
ANISOU 3963  ND1 HIS A 280     4697   6951   6558     90   -141   1127       N  
ATOM   3964  CD2 HIS A 280      -9.155  28.527 -10.466  1.00 48.45           C  
ANISOU 3964  CD2 HIS A 280     4695   6973   6741     87   -143   1310       C  
ATOM   3965  CE1 HIS A 280      -8.331  29.152  -8.532  1.00 48.95           C  
ANISOU 3965  CE1 HIS A 280     4850   6912   6836     77   -237   1113       C  
ATOM   3966  NE2 HIS A 280      -8.866  29.597  -9.655  1.00 49.50           N  
ANISOU 3966  NE2 HIS A 280     4881   6942   6984     71   -244   1231       N  
ATOM   3967  H   HIS A 280     -10.094  24.228 -11.690  1.00 54.32           H  
ATOM   3968  HA  HIS A 280     -10.447  25.155  -9.157  1.00 55.07           H  
ATOM   3969  HB2 HIS A 280      -8.254  25.475  -9.597  1.00 57.14           H  
ATOM   3970  HB3 HIS A 280      -8.542  25.889 -11.100  1.00 57.14           H  
ATOM   3971  HD2 HIS A 280      -9.540  28.564 -11.312  1.00 58.14           H  
ATOM   3972  HE1 HIS A 280      -8.046  29.677  -7.819  1.00 58.74           H  
ATOM   3973  HE2 HIS A 280      -9.007  30.423  -9.847  1.00 59.40           H  
ATOM   3974  N   ILE A 281     -12.357  26.528  -9.865  1.00 47.96           N  
ANISOU 3974  N   ILE A 281     4652   7113   6457    297     71   1145       N  
ATOM   3975  CA  ILE A 281     -13.516  27.295 -10.311  1.00 48.68           C  
ANISOU 3975  CA  ILE A 281     4722   7155   6621    363     73   1148       C  
ATOM   3976  C   ILE A 281     -13.519  28.634  -9.590  1.00 48.15           C  
ANISOU 3976  C   ILE A 281     4697   6942   6655    417     -4   1043       C  
ATOM   3977  O   ILE A 281     -13.345  28.687  -8.367  1.00 54.78           O  
ANISOU 3977  O   ILE A 281     5574   7790   7448    452    -15    911       O  
ATOM   3978  CB  ILE A 281     -14.835  26.549 -10.045  1.00 43.53           C  
ANISOU 3978  CB  ILE A 281     4040   6625   5874    419    149   1114       C  
ATOM   3979  CG1 ILE A 281     -14.758  25.088 -10.504  1.00 45.68           C  
ANISOU 3979  CG1 ILE A 281     4297   7007   6053    359    185   1191       C  
ATOM   3980  CG2 ILE A 281     -15.978  27.268 -10.736  1.00 48.20           C  
ANISOU 3980  CG2 ILE A 281     4591   7189   6533    491    152   1135       C  
ATOM   3981  CD1 ILE A 281     -14.566  24.896 -11.990  1.00 42.68           C  
ANISOU 3981  CD1 ILE A 281     3881   6631   5704    337    170   1302       C  
ATOM   3982  H   ILE A 281     -12.410  26.275  -9.045  1.00 57.55           H  
ATOM   3983  HA  ILE A 281     -13.445  27.461 -11.264  1.00 58.42           H  
ATOM   3984  HB  ILE A 281     -15.003  26.559  -9.090  1.00 52.23           H  
ATOM   3985 HG12 ILE A 281     -14.010  24.662 -10.056  1.00 54.82           H  
ATOM   3986 HG13 ILE A 281     -15.583  24.642 -10.256  1.00 54.82           H  
ATOM   3987 HG21 ILE A 281     -16.803  26.789 -10.561  1.00 57.84           H  
ATOM   3988 HG22 ILE A 281     -16.039  28.171 -10.387  1.00 57.84           H  
ATOM   3989 HG23 ILE A 281     -15.805  27.292 -11.690  1.00 57.84           H  
ATOM   3990 HD11 ILE A 281     -14.529  23.947 -12.184  1.00 51.21           H  
ATOM   3991 HD12 ILE A 281     -15.312  25.301 -12.459  1.00 51.21           H  
ATOM   3992 HD13 ILE A 281     -13.736  25.322 -12.259  1.00 51.21           H  
ATOM   3993  N   GLU A 282     -13.736  29.711 -10.341  1.00 49.38           N  
ANISOU 3993  N   GLU A 282     4849   6964   6949    431    -73   1099       N  
ATOM   3994  CA  GLU A 282     -13.837  31.039  -9.753  1.00 55.09           C  
ANISOU 3994  CA  GLU A 282     5630   7506   7798    501   -189    989       C  
ATOM   3995  C   GLU A 282     -14.932  31.821 -10.462  1.00 56.20           C  
ANISOU 3995  C   GLU A 282     5755   7567   8032    592   -222   1014       C  
ATOM   3996  O   GLU A 282     -15.015  31.804 -11.694  1.00 56.42           O  
ANISOU 3996  O   GLU A 282     5736   7600   8103    536   -211   1183       O  
ATOM   3997  CB  GLU A 282     -12.500  31.787  -9.838  1.00 55.91           C  
ANISOU 3997  CB  GLU A 282     5768   7446   8028    385   -317   1053       C  
ATOM   3998  CG  GLU A 282     -12.009  32.036 -11.253  1.00 57.39           C  
ANISOU 3998  CG  GLU A 282     5900   7606   8301    266   -349   1287       C  
ATOM   3999  CD  GLU A 282     -10.583  32.557 -11.296  1.00 58.05           C  
ANISOU 3999  CD  GLU A 282     5983   7601   8473    117   -461   1388       C  
ATOM   4000  OE1 GLU A 282      -9.704  31.928 -10.673  1.00 58.30           O  
ANISOU 4000  OE1 GLU A 282     6013   7723   8414     66   -430   1344       O  
ATOM   4001  OE2 GLU A 282     -10.341  33.594 -11.948  1.00 59.42           O  
ANISOU 4001  OE2 GLU A 282     6149   7619   8808     42   -589   1527       O  
ATOM   4002  H   GLU A 282     -13.829  29.697 -11.196  1.00 59.26           H  
ATOM   4003  HA  GLU A 282     -14.080  30.957  -8.818  1.00 66.11           H  
ATOM   4004  HB2 GLU A 282     -12.598  32.649  -9.404  1.00 67.09           H  
ATOM   4005  HB3 GLU A 282     -11.823  31.265  -9.379  1.00 67.09           H  
ATOM   4006  HG2 GLU A 282     -12.040  31.204 -11.750  1.00 68.87           H  
ATOM   4007  HG3 GLU A 282     -12.582  32.696 -11.675  1.00 68.87           H  
ATOM   4008  N   SER A 283     -15.777  32.486  -9.680  1.00 53.63           N  
ANISOU 4008  N   SER A 283     5460   7194   7723    750   -265    838       N  
ATOM   4009  CA  SER A 283     -16.781  33.382 -10.232  1.00 52.79           C  
ANISOU 4009  CA  SER A 283     5350   6987   7719    868   -327    832       C  
ATOM   4010  C   SER A 283     -16.131  34.720 -10.556  1.00 59.81           C  
ANISOU 4010  C   SER A 283     6317   7577   8833    832   -526    875       C  
ATOM   4011  O   SER A 283     -15.446  35.304  -9.711  1.00 66.44           O  
ANISOU 4011  O   SER A 283     7233   8270   9741    835   -649    756       O  
ATOM   4012  CB  SER A 283     -17.929  33.571  -9.243  1.00 56.04           C  
ANISOU 4012  CB  SER A 283     5752   7498   8043   1081   -307    612       C  
ATOM   4013  OG  SER A 283     -18.603  32.349  -9.000  1.00 50.10           O  
ANISOU 4013  OG  SER A 283     4910   7034   7092   1084   -137    620       O  
ATOM   4014  H   SER A 283     -15.787  32.434  -8.822  1.00 64.36           H  
ATOM   4015  HA  SER A 283     -17.138  33.005 -11.052  1.00 63.34           H  
ATOM   4016  HB2 SER A 283     -17.571  33.905  -8.406  1.00 67.25           H  
ATOM   4017  HB3 SER A 283     -18.560  34.210  -9.612  1.00 67.25           H  
ATOM   4018  HG  SER A 283     -19.231  32.470  -8.455  1.00 60.12           H  
ATOM   4019  N   LEU A 284     -16.346  35.203 -11.777  1.00 63.54           N  
ANISOU 4019  N   LEU A 284     6766   7957   9421    789   -575   1055       N  
ATOM   4020  CA  LEU A 284     -15.624  36.378 -12.247  1.00 65.55           C  
ANISOU 4020  CA  LEU A 284     7077   7933   9896    697   -776   1174       C  
ATOM   4021  C   LEU A 284     -15.829  37.558 -11.307  1.00 66.57           C  
ANISOU 4021  C   LEU A 284     7323   7804  10168    843   -976    957       C  
ATOM   4022  O   LEU A 284     -16.913  37.756 -10.751  1.00 65.36           O  
ANISOU 4022  O   LEU A 284     7184   7681   9967   1066   -970    750       O  
ATOM   4023  CB  LEU A 284     -16.072  36.752 -13.661  1.00 61.36           C  
ANISOU 4023  CB  LEU A 284     6495   7367   9453    662   -798   1400       C  
ATOM   4024  CG  LEU A 284     -15.956  35.671 -14.739  1.00 57.49           C  
ANISOU 4024  CG  LEU A 284     5886   7136   8822    551   -626   1601       C  
ATOM   4025  CD1 LEU A 284     -15.925  36.313 -16.116  1.00 58.25           C  
ANISOU 4025  CD1 LEU A 284     5933   7166   9035    467   -705   1864       C  
ATOM   4026  CD2 LEU A 284     -14.734  34.788 -14.535  1.00 56.48           C  
ANISOU 4026  CD2 LEU A 284     5726   7149   8585    402   -550   1649       C  
ATOM   4027  H   LEU A 284     -16.899  34.872 -12.346  1.00 76.25           H  
ATOM   4028  HA  LEU A 284     -14.675  36.176 -12.275  1.00 78.66           H  
ATOM   4029  HB2 LEU A 284     -17.004  37.017 -13.621  1.00 73.63           H  
ATOM   4030  HB3 LEU A 284     -15.538  37.507 -13.956  1.00 73.63           H  
ATOM   4031  HG  LEU A 284     -16.741  35.103 -14.695  1.00 68.99           H  
ATOM   4032 HD11 LEU A 284     -15.852  35.617 -16.787  1.00 69.91           H  
ATOM   4033 HD12 LEU A 284     -16.744  36.816 -16.248  1.00 69.91           H  
ATOM   4034 HD13 LEU A 284     -15.160  36.907 -16.169  1.00 69.91           H  
ATOM   4035 HD21 LEU A 284     -14.705  34.122 -15.240  1.00 67.77           H  
ATOM   4036 HD22 LEU A 284     -13.937  35.341 -14.569  1.00 67.77           H  
ATOM   4037 HD23 LEU A 284     -14.800  34.353 -13.671  1.00 67.77           H  
ATOM   4038  N   LEU A 285     -14.768  38.341 -11.132  1.00 69.16           N  
ANISOU 4038  N   LEU A 285     7723   7888  10665    721  -1168   1001       N  
ATOM   4039  CA  LEU A 285     -14.833  39.532 -10.300  1.00 72.17           C  
ANISOU 4039  CA  LEU A 285     8234   7973  11215    850  -1413    790       C  
ATOM   4040  C   LEU A 285     -15.772  40.557 -10.920  1.00 72.06           C  
ANISOU 4040  C   LEU A 285     8264   7744  11371    984  -1568    806       C  
ATOM   4041  O   LEU A 285     -15.798  40.743 -12.139  1.00 69.04           O  
ANISOU 4041  O   LEU A 285     7835   7318  11077    864  -1581   1079       O  
ATOM   4042  CB  LEU A 285     -13.436  40.131 -10.132  1.00 72.12           C  
ANISOU 4042  CB  LEU A 285     8289   7736  11378    645  -1610    882       C  
ATOM   4043  CG  LEU A 285     -12.404  39.208  -9.481  1.00 72.73           C  
ANISOU 4043  CG  LEU A 285     8326   8009  11299    519  -1484    862       C  
ATOM   4044  CD1 LEU A 285     -10.993  39.645  -9.830  1.00 74.58           C  
ANISOU 4044  CD1 LEU A 285     8558   8093  11685    249  -1636   1083       C  
ATOM   4045  CD2 LEU A 285     -12.596  39.178  -7.974  1.00 75.60           C  
ANISOU 4045  CD2 LEU A 285     8761   8394  11570    708  -1503    511       C  
ATOM   4046  H   LEU A 285     -13.997  38.201 -11.487  1.00 82.99           H  
ATOM   4047  HA  LEU A 285     -15.173  39.295  -9.423  1.00 86.61           H  
ATOM   4048  HB2 LEU A 285     -13.098  40.374 -11.008  1.00 86.55           H  
ATOM   4049  HB3 LEU A 285     -13.506  40.925  -9.579  1.00 86.55           H  
ATOM   4050  HG  LEU A 285     -12.530  38.307  -9.817  1.00 87.27           H  
ATOM   4051 HD11 LEU A 285     -10.362  39.043  -9.405  1.00 89.49           H  
ATOM   4052 HD12 LEU A 285     -10.882  39.614 -10.793  1.00 89.49           H  
ATOM   4053 HD13 LEU A 285     -10.855  40.550  -9.509  1.00 89.49           H  
ATOM   4054 HD21 LEU A 285     -11.932  38.588  -7.584  1.00 90.72           H  
ATOM   4055 HD22 LEU A 285     -12.487  40.076  -7.625  1.00 90.72           H  
ATOM   4056 HD23 LEU A 285     -13.487  38.851  -7.776  1.00 90.72           H  
ATOM   4057  N   ASN A 286     -16.554  41.221 -10.071  1.00 78.94           N  
ANISOU 4057  N   ASN A 286     9220   8500  12275   1251  -1692    507       N  
ATOM   4058  CA  ASN A 286     -17.501  42.244 -10.506  1.00 84.31           C  
ANISOU 4058  CA  ASN A 286     9957   8961  13115   1433  -1867    467       C  
ATOM   4059  C   ASN A 286     -18.515  41.701 -11.508  1.00 81.46           C  
ANISOU 4059  C   ASN A 286     9477   8828  12644   1473  -1671    618       C  
ATOM   4060  O   ASN A 286     -19.104  42.469 -12.275  1.00 85.04           O  
ANISOU 4060  O   ASN A 286     9956   9106  13249   1540  -1802    709       O  
ATOM   4061  CB  ASN A 286     -16.769  43.449 -11.107  1.00 86.17           C  
ANISOU 4061  CB  ASN A 286    10299   8768  13674   1274  -2182    657       C  
ATOM   4062  CG  ASN A 286     -15.717  44.014 -10.175  1.00 91.13           C  
ANISOU 4062  CG  ASN A 286    11045   9147  14435   1204  -2407    526       C  
ATOM   4063  OD1 ASN A 286     -15.906  44.054  -8.959  1.00 93.09           O  
ANISOU 4063  OD1 ASN A 286    11351   9418  14600   1412  -2440    181       O  
ATOM   4064  ND2 ASN A 286     -14.596  44.450 -10.741  1.00 93.52           N  
ANISOU 4064  ND2 ASN A 286    11365   9235  14931    906  -2566    809       N  
ATOM   4065  H   ASN A 286     -16.553  41.094  -9.221  1.00 94.73           H  
ATOM   4066  HA  ASN A 286     -17.994  42.557  -9.731  1.00101.17           H  
ATOM   4067  HB2 ASN A 286     -16.329  43.176 -11.927  1.00103.41           H  
ATOM   4068  HB3 ASN A 286     -17.413  44.150 -11.293  1.00103.41           H  
ATOM   4069 HD21 ASN A 286     -13.969  44.780 -10.255  1.00112.22           H  
ATOM   4070 HD22 ASN A 286     -14.499  44.402 -11.594  1.00112.22           H  
ATOM   4071  N   GLY A 287     -18.729  40.388 -11.518  1.00 73.71           N  
ANISOU 4071  N   GLY A 287     8372   8225  11411   1431  -1378    649       N  
ATOM   4072  CA  GLY A 287     -19.649  39.748 -12.433  1.00 65.76           C  
ANISOU 4072  CA  GLY A 287     7248   7452  10288   1451  -1193    784       C  
ATOM   4073  C   GLY A 287     -20.993  39.393 -11.840  1.00 67.66           C  
ANISOU 4073  C   GLY A 287     7424   7937  10348   1712  -1070    556       C  
ATOM   4074  O   GLY A 287     -21.775  38.694 -12.496  1.00 67.54           O  
ANISOU 4074  O   GLY A 287     7295   8157  10209   1715   -900    659       O  
ATOM   4075  H   GLY A 287     -18.338  39.837 -10.986  1.00 88.46           H  
ATOM   4076  HA2 GLY A 287     -19.802  40.338 -13.188  1.00 78.92           H  
ATOM   4077  HA3 GLY A 287     -19.244  38.932 -12.766  1.00 78.92           H  
ATOM   4078  N   GLY A 288     -21.293  39.848 -10.628  1.00 71.96           N  
ANISOU 4078  N   GLY A 288     8022   8459  10861   1934  -1157    253       N  
ATOM   4079  CA  GLY A 288     -22.538  39.499  -9.984  1.00 72.28           C  
ANISOU 4079  CA  GLY A 288     7970   8799  10696   2185  -1035     43       C  
ATOM   4080  C   GLY A 288     -22.524  38.072  -9.472  1.00 72.27           C  
ANISOU 4080  C   GLY A 288     7851   9176  10432   2086   -776     60       C  
ATOM   4081  O   GLY A 288     -21.490  37.396  -9.426  1.00 71.67           O  
ANISOU 4081  O   GLY A 288     7789   9109  10332   1861   -709    176       O  
ATOM   4082  H   GLY A 288     -20.786  40.362 -10.161  1.00 86.35           H  
ATOM   4083  HA2 GLY A 288     -22.695  40.095  -9.235  1.00 86.74           H  
ATOM   4084  HA3 GLY A 288     -23.269  39.594 -10.615  1.00 86.74           H  
ATOM   4085  N   ILE A 289     -23.710  37.607  -9.078  1.00 73.58           N  
ANISOU 4085  N   ILE A 289     7891   9669  10396   2259   -640    -47       N  
ATOM   4086  CA  ILE A 289     -23.817  36.254  -8.554  1.00 70.55           C  
ANISOU 4086  CA  ILE A 289     7391   9647   9769   2161   -418    -11       C  
ATOM   4087  C   ILE A 289     -23.719  35.247  -9.695  1.00 66.89           C  
ANISOU 4087  C   ILE A 289     6865   9256   9292   1914   -277    276       C  
ATOM   4088  O   ILE A 289     -24.013  35.541 -10.861  1.00 68.09           O  
ANISOU 4088  O   ILE A 289     7014   9299   9559   1882   -307    423       O  
ATOM   4089  CB  ILE A 289     -25.119  36.062  -7.758  1.00 72.64           C  
ANISOU 4089  CB  ILE A 289     7514  10276   9810   2401   -326   -185       C  
ATOM   4090  CG1 ILE A 289     -26.347  36.099  -8.675  1.00 75.45           C  
ANISOU 4090  CG1 ILE A 289     7764  10746  10157   2482   -277    -94       C  
ATOM   4091  CG2 ILE A 289     -25.244  37.132  -6.678  1.00 75.37           C  
ANISOU 4091  CG2 ILE A 289     7917  10564  10156   2697   -487   -506       C  
ATOM   4092  CD1 ILE A 289     -27.567  35.484  -8.051  1.00 74.76           C  
ANISOU 4092  CD1 ILE A 289     7484  11114   9808   2618   -128   -164       C  
ATOM   4093  H   ILE A 289     -24.449  38.045  -9.104  1.00 88.29           H  
ATOM   4094  HA  ILE A 289     -23.074  36.093  -7.952  1.00 84.67           H  
ATOM   4095  HB  ILE A 289     -25.087  35.195  -7.325  1.00 87.17           H  
ATOM   4096 HG12 ILE A 289     -26.554  37.023  -8.887  1.00 90.54           H  
ATOM   4097 HG13 ILE A 289     -26.148  35.609  -9.488  1.00 90.54           H  
ATOM   4098 HG21 ILE A 289     -26.070  36.992  -6.190  1.00 90.44           H  
ATOM   4099 HG22 ILE A 289     -24.487  37.062  -6.076  1.00 90.44           H  
ATOM   4100 HG23 ILE A 289     -25.252  38.006  -7.100  1.00 90.44           H  
ATOM   4101 HD11 ILE A 289     -28.304  35.539  -8.679  1.00 89.72           H  
ATOM   4102 HD12 ILE A 289     -27.380  34.556  -7.841  1.00 89.72           H  
ATOM   4103 HD13 ILE A 289     -27.786  35.969  -7.240  1.00 89.72           H  
ATOM   4104  N   THR A 290     -23.306  34.035  -9.343  1.00 60.07           N  
ANISOU 4104  N   THR A 290     5956   8585   8284   1750   -136    349       N  
ATOM   4105  CA  THR A 290     -23.260  32.920 -10.272  1.00 54.33           C  
ANISOU 4105  CA  THR A 290     5169   7961   7514   1545    -13    578       C  
ATOM   4106  C   THR A 290     -24.174  31.809  -9.777  1.00 51.64           C  
ANISOU 4106  C   THR A 290     4691   7973   6955   1545    138    583       C  
ATOM   4107  O   THR A 290     -24.320  31.598  -8.570  1.00 51.20           O  
ANISOU 4107  O   THR A 290     4597   8098   6758   1619    175    454       O  
ATOM   4108  CB  THR A 290     -21.839  32.380 -10.427  1.00 53.06           C  
ANISOU 4108  CB  THR A 290     5083   7683   7395   1327    -13    689       C  
ATOM   4109  OG1 THR A 290     -21.368  31.902  -9.160  1.00 54.09           O  
ANISOU 4109  OG1 THR A 290     5226   7921   7406   1318     22    574       O  
ATOM   4110  CG2 THR A 290     -20.908  33.468 -10.939  1.00 56.03           C  
ANISOU 4110  CG2 THR A 290     5568   7738   7982   1290   -170    727       C  
ATOM   4111  H   THR A 290     -23.040  33.832  -8.551  1.00 72.09           H  
ATOM   4112  HA  THR A 290     -23.575  33.211 -11.142  1.00 65.20           H  
ATOM   4113  HB  THR A 290     -21.839  31.650 -11.067  1.00 63.67           H  
ATOM   4114  HG1 THR A 290     -20.587  31.603  -9.238  1.00 64.91           H  
ATOM   4115 HG21 THR A 290     -20.008  33.117 -11.035  1.00 67.23           H  
ATOM   4116 HG22 THR A 290     -21.214  33.787 -11.802  1.00 67.23           H  
ATOM   4117 HG23 THR A 290     -20.891  34.211 -10.315  1.00 67.23           H  
ATOM   4118  N   ILE A 291     -24.789  31.100 -10.720  1.00 52.87           N  
ANISOU 4118  N   ILE A 291     4767   8238   7084   1456    214    744       N  
ATOM   4119  CA  ILE A 291     -25.661  29.973 -10.414  1.00 54.93           C  
ANISOU 4119  CA  ILE A 291     4894   8814   7165   1406    333    800       C  
ATOM   4120  C   ILE A 291     -25.258  28.805 -11.301  1.00 52.82           C  
ANISOU 4120  C   ILE A 291     4633   8530   6906   1182    373    991       C  
ATOM   4121  O   ILE A 291     -25.093  28.968 -12.515  1.00 51.77           O  
ANISOU 4121  O   ILE A 291     4530   8258   6882   1137    339   1089       O  
ATOM   4122  CB  ILE A 291     -27.148  30.325 -10.612  1.00 56.22           C  
ANISOU 4122  CB  ILE A 291     4922   9170   7268   1566    359    772       C  
ATOM   4123  CG1 ILE A 291     -27.526  31.525  -9.737  1.00 59.61           C  
ANISOU 4123  CG1 ILE A 291     5350   9616   7683   1837    295    545       C  
ATOM   4124  CG2 ILE A 291     -28.029  29.126 -10.261  1.00 55.98           C  
ANISOU 4124  CG2 ILE A 291     4734   9485   7052   1477    470    864       C  
ATOM   4125  CD1 ILE A 291     -28.929  32.047  -9.963  1.00 59.06           C  
ANISOU 4125  CD1 ILE A 291     5152   9725   7562   2042    301    491       C  
ATOM   4126  H   ILE A 291     -24.714  31.257 -11.562  1.00 63.45           H  
ATOM   4127  HA  ILE A 291     -25.532  29.711  -9.489  1.00 65.92           H  
ATOM   4128  HB  ILE A 291     -27.293  30.557 -11.542  1.00 67.46           H  
ATOM   4129 HG12 ILE A 291     -27.455  31.265  -8.806  1.00 71.53           H  
ATOM   4130 HG13 ILE A 291     -26.909  32.250  -9.922  1.00 71.53           H  
ATOM   4131 HG21 ILE A 291     -28.959  29.369 -10.393  1.00 67.18           H  
ATOM   4132 HG22 ILE A 291     -27.796  28.383 -10.839  1.00 67.18           H  
ATOM   4133 HG23 ILE A 291     -27.878  28.884  -9.334  1.00 67.18           H  
ATOM   4134 HD11 ILE A 291     -29.083  32.802  -9.374  1.00 70.87           H  
ATOM   4135 HD12 ILE A 291     -29.016  32.327 -10.888  1.00 70.87           H  
ATOM   4136 HD13 ILE A 291     -29.564  31.340  -9.770  1.00 70.87           H  
ATOM   4137  N   THR A 292     -25.097  27.632 -10.693  1.00 48.36           N  
ANISOU 4137  N   THR A 292     4039   8113   6223   1052    430   1040       N  
ATOM   4138  CA  THR A 292     -24.701  26.427 -11.403  1.00 45.76           C  
ANISOU 4138  CA  THR A 292     3729   7762   5897    861    438   1190       C  
ATOM   4139  C   THR A 292     -25.472  25.241 -10.842  1.00 51.48           C  
ANISOU 4139  C   THR A 292     4349   8733   6479    764    488   1266       C  
ATOM   4140  O   THR A 292     -25.824  25.213  -9.659  1.00 53.38           O  
ANISOU 4140  O   THR A 292     4523   9160   6599    806    528   1215       O  
ATOM   4141  CB  THR A 292     -23.192  26.163 -11.273  1.00 50.09           C  
ANISOU 4141  CB  THR A 292     4402   8139   6491    765    401   1189       C  
ATOM   4142  OG1 THR A 292     -22.461  27.362 -11.560  1.00 52.85           O  
ANISOU 4142  OG1 THR A 292     4832   8281   6968    839    341   1130       O  
ATOM   4143  CG2 THR A 292     -22.749  25.062 -12.227  1.00 44.10           C  
ANISOU 4143  CG2 THR A 292     3670   7338   5748    619    383   1314       C  
ATOM   4144  H   THR A 292     -25.215  27.510  -9.850  1.00 58.03           H  
ATOM   4145  HA  THR A 292     -24.918  26.519 -12.344  1.00 54.92           H  
ATOM   4146  HB  THR A 292     -22.995  25.878 -10.367  1.00 60.11           H  
ATOM   4147  HG1 THR A 292     -22.626  27.619 -12.342  1.00 63.42           H  
ATOM   4148 HG21 THR A 292     -21.796  24.907 -12.134  1.00 52.92           H  
ATOM   4149 HG22 THR A 292     -23.223  24.240 -12.028  1.00 52.92           H  
ATOM   4150 HG23 THR A 292     -22.938  25.321 -13.143  1.00 52.92           H  
ATOM   4151  N   VAL A 293     -25.735  24.262 -11.704  1.00 47.57           N  
ANISOU 4151  N   VAL A 293     3833   8248   5995    632    472   1397       N  
ATOM   4152  CA  VAL A 293     -26.287  22.976 -11.295  1.00 49.57           C  
ANISOU 4152  CA  VAL A 293     4012   8673   6151    485    475   1509       C  
ATOM   4153  C   VAL A 293     -25.361  21.886 -11.814  1.00 49.62           C  
ANISOU 4153  C   VAL A 293     4128   8518   6209    335    402   1579       C  
ATOM   4154  O   VAL A 293     -25.026  21.864 -13.004  1.00 50.54           O  
ANISOU 4154  O   VAL A 293     4299   8495   6411    335    357   1590       O  
ATOM   4155  CB  VAL A 293     -27.725  22.772 -11.812  1.00 53.11           C  
ANISOU 4155  CB  VAL A 293     4313   9305   6563    474    489   1594       C  
ATOM   4156  CG1 VAL A 293     -28.198  21.338 -11.581  1.00 50.82           C  
ANISOU 4156  CG1 VAL A 293     3959   9143   6209    271    450   1750       C  
ATOM   4157  CG2 VAL A 293     -28.672  23.742 -11.119  1.00 53.71           C  
ANISOU 4157  CG2 VAL A 293     4258   9598   6551    645    559   1514       C  
ATOM   4158  H   VAL A 293     -25.599  24.322 -12.551  1.00 57.09           H  
ATOM   4159  HA  VAL A 293     -26.302  22.927 -10.326  1.00 59.49           H  
ATOM   4160  HB  VAL A 293     -27.751  22.950 -12.765  1.00 63.74           H  
ATOM   4161 HG11 VAL A 293     -29.103  21.247 -11.917  1.00 60.99           H  
ATOM   4162 HG12 VAL A 293     -27.606  20.731 -12.053  1.00 60.99           H  
ATOM   4163 HG13 VAL A 293     -28.177  21.149 -10.630  1.00 60.99           H  
ATOM   4164 HG21 VAL A 293     -29.570  23.601 -11.455  1.00 64.45           H  
ATOM   4165 HG22 VAL A 293     -28.646  23.579 -10.163  1.00 64.45           H  
ATOM   4166 HG23 VAL A 293     -28.386  24.650 -11.308  1.00 64.45           H  
ATOM   4167  N   ASN A 294     -24.939  20.996 -10.921  1.00 52.77           N  
ANISOU 4167  N   ASN A 294     4554   8951   6546    224    381   1621       N  
ATOM   4168  CA  ASN A 294     -24.060  19.891 -11.271  1.00 55.51           C  
ANISOU 4168  CA  ASN A 294     5010   9146   6933    104    290   1670       C  
ATOM   4169  C   ASN A 294     -24.857  18.598 -11.348  1.00 51.96           C  
ANISOU 4169  C   ASN A 294     4508   8773   6460    -58    212   1813       C  
ATOM   4170  O   ASN A 294     -25.799  18.389 -10.579  1.00 56.89           O  
ANISOU 4170  O   ASN A 294     5011   9605   7000   -121    242   1902       O  
ATOM   4171  CB  ASN A 294     -22.933  19.735 -10.249  1.00 59.09           C  
ANISOU 4171  CB  ASN A 294     5550   9549   7353     87    288   1626       C  
ATOM   4172  CG  ASN A 294     -21.808  20.724 -10.461  1.00 59.73           C  
ANISOU 4172  CG  ASN A 294     5720   9481   7496    199    309   1505       C  
ATOM   4173  OD1 ASN A 294     -21.469  21.067 -11.595  1.00 60.66           O  
ANISOU 4173  OD1 ASN A 294     5872   9483   7694    241    287   1489       O  
ATOM   4174  ND2 ASN A 294     -21.216  21.183  -9.366  1.00 63.51           N  
ANISOU 4174  ND2 ASN A 294     6224   9977   7930    239    343   1430       N  
ATOM   4175  H   ASN A 294     -25.155  21.013 -10.089  1.00 63.33           H  
ATOM   4176  HA  ASN A 294     -23.664  20.058 -12.141  1.00 66.61           H  
ATOM   4177  HB2 ASN A 294     -23.292  19.876  -9.359  1.00 70.91           H  
ATOM   4178  HB3 ASN A 294     -22.564  18.840 -10.320  1.00 70.91           H  
ATOM   4179 HD21 ASN A 294     -20.570  21.748  -9.431  1.00 76.22           H  
ATOM   4180 HD22 ASN A 294     -21.477  20.916  -8.592  1.00 76.22           H  
ATOM   4181  N   PHE A 295     -24.467  17.736 -12.281  1.00 50.70           N  
ANISOU 4181  N   PHE A 295     4434   8457   6374   -121     96   1837       N  
ATOM   4182  CA  PHE A 295     -25.050  16.408 -12.441  1.00 52.33           C  
ANISOU 4182  CA  PHE A 295     4629   8661   6593   -286    -35   1963       C  
ATOM   4183  C   PHE A 295     -23.949  15.394 -12.157  1.00 53.51           C  
ANISOU 4183  C   PHE A 295     4921   8643   6768   -354   -156   1962       C  
ATOM   4184  O   PHE A 295     -23.010  15.258 -12.948  1.00 54.23           O  
ANISOU 4184  O   PHE A 295     5122   8572   6911   -278   -217   1866       O  
ATOM   4185  CB  PHE A 295     -25.622  16.223 -13.846  1.00 55.04           C  
ANISOU 4185  CB  PHE A 295     4956   8955   7003   -275   -107   1962       C  
ATOM   4186  CG  PHE A 295     -26.744  17.171 -14.181  1.00 58.39           C  
ANISOU 4186  CG  PHE A 295     5238   9544   7405   -203     -2   1970       C  
ATOM   4187  CD1 PHE A 295     -26.505  18.528 -14.331  1.00 57.81           C  
ANISOU 4187  CD1 PHE A 295     5153   9481   7330    -33    121   1868       C  
ATOM   4188  CD2 PHE A 295     -28.035  16.701 -14.364  1.00 62.37           C  
ANISOU 4188  CD2 PHE A 295     5619  10182   7897   -309    -45   2086       C  
ATOM   4189  CE1 PHE A 295     -27.534  19.398 -14.643  1.00 59.73           C  
ANISOU 4189  CE1 PHE A 295     5276   9861   7560     54    197   1867       C  
ATOM   4190  CE2 PHE A 295     -29.067  17.566 -14.675  1.00 58.88           C  
ANISOU 4190  CE2 PHE A 295     5038   9908   7425   -226     48   2087       C  
ATOM   4191  CZ  PHE A 295     -28.816  18.915 -14.816  1.00 59.36           C  
ANISOU 4191  CZ  PHE A 295     5100   9971   7485    -33    168   1971       C  
ATOM   4192  H   PHE A 295     -23.847  17.903 -12.853  1.00 60.84           H  
ATOM   4193  HA  PHE A 295     -25.763  16.283 -11.795  1.00 62.80           H  
ATOM   4194  HB2 PHE A 295     -24.913  16.364 -14.493  1.00 66.05           H  
ATOM   4195  HB3 PHE A 295     -25.965  15.320 -13.927  1.00 66.05           H  
ATOM   4196  HD1 PHE A 295     -25.644  18.859 -14.214  1.00 69.37           H  
ATOM   4197  HD2 PHE A 295     -28.210  15.792 -14.268  1.00 74.84           H  
ATOM   4198  HE1 PHE A 295     -27.363  20.307 -14.738  1.00 71.68           H  
ATOM   4199  HE2 PHE A 295     -29.930  17.239 -14.792  1.00 70.65           H  
ATOM   4200  HZ  PHE A 295     -29.510  19.498 -15.026  1.00 71.24           H  
ATOM   4201  N   TRP A 296     -24.058  14.693 -11.031  1.00 55.67           N  
ANISOU 4201  N   TRP A 296     5181   8978   6995   -488   -194   2076       N  
ATOM   4202  CA  TRP A 296     -23.030  13.761 -10.586  1.00 61.58           C  
ANISOU 4202  CA  TRP A 296     6063   9572   7762   -547   -313   2086       C  
ATOM   4203  C   TRP A 296     -23.411  12.339 -10.973  1.00 61.21           C  
ANISOU 4203  C   TRP A 296     6066   9399   7791   -706   -535   2202       C  
ATOM   4204  O   TRP A 296     -24.526  11.891 -10.688  1.00 62.96           O  
ANISOU 4204  O   TRP A 296     6183   9735   8005   -866   -580   2370       O  
ATOM   4205  CB  TRP A 296     -22.833  13.853  -9.071  1.00 65.09           C  
ANISOU 4205  CB  TRP A 296     6470  10154   8107   -596   -239   2150       C  
ATOM   4206  CG  TRP A 296     -22.420  15.212  -8.601  1.00 62.91           C  
ANISOU 4206  CG  TRP A 296     6161   9975   7765   -436    -59   2015       C  
ATOM   4207  CD1 TRP A 296     -23.215  16.152  -8.013  1.00 66.52           C  
ANISOU 4207  CD1 TRP A 296     6479  10661   8134   -378     82   2009       C  
ATOM   4208  CD2 TRP A 296     -21.111  15.787  -8.683  1.00 60.37           C  
ANISOU 4208  CD2 TRP A 296     5948   9525   7467   -308    -24   1862       C  
ATOM   4209  NE1 TRP A 296     -22.482  17.277  -7.721  1.00 66.09           N  
ANISOU 4209  NE1 TRP A 296     6459  10591   8063   -220    182   1849       N  
ATOM   4210  CE2 TRP A 296     -21.188  17.079  -8.123  1.00 61.47           C  
ANISOU 4210  CE2 TRP A 296     6020   9788   7549   -193    122   1772       C  
ATOM   4211  CE3 TRP A 296     -19.883  15.337  -9.174  1.00 58.93           C  
ANISOU 4211  CE3 TRP A 296     5902   9149   7342   -273   -114   1791       C  
ATOM   4212  CZ2 TRP A 296     -20.084  17.922  -8.040  1.00 60.09           C  
ANISOU 4212  CZ2 TRP A 296     5917   9523   7393    -77    168   1633       C  
ATOM   4213  CZ3 TRP A 296     -18.789  16.175  -9.090  1.00 57.00           C  
ANISOU 4213  CZ3 TRP A 296     5706   8859   7094   -157    -44   1664       C  
ATOM   4214  CH2 TRP A 296     -18.896  17.453  -8.528  1.00 58.83           C  
ANISOU 4214  CH2 TRP A 296     5875   9190   7287    -75     90   1596       C  
ATOM   4215  H   TRP A 296     -24.732  14.742 -10.499  1.00 66.81           H  
ATOM   4216  HA  TRP A 296     -22.189  13.980 -11.017  1.00 73.89           H  
ATOM   4217  HB2 TRP A 296     -23.669  13.629  -8.633  1.00 78.11           H  
ATOM   4218  HB3 TRP A 296     -22.143  13.225  -8.806  1.00 78.11           H  
ATOM   4219  HD1 TRP A 296     -24.122  16.047  -7.835  1.00 79.82           H  
ATOM   4220  HE1 TRP A 296     -22.786  17.990  -7.348  1.00 79.31           H  
ATOM   4221  HE3 TRP A 296     -19.804  14.489  -9.548  1.00 70.72           H  
ATOM   4222  HZ2 TRP A 296     -20.152  18.772  -7.667  1.00 72.11           H  
ATOM   4223  HZ3 TRP A 296     -17.966  15.886  -9.413  1.00 68.40           H  
ATOM   4224  HH2 TRP A 296     -18.142  17.996  -8.485  1.00 70.59           H  
ATOM   4225  N   TYR A 297     -22.480  11.632 -11.611  1.00 56.77           N  
ANISOU 4225  N   TYR A 297     5658   8611   7302   -658   -688   2111       N  
ATOM   4226  CA  TYR A 297     -22.687  10.253 -12.034  1.00 58.03           C  
ANISOU 4226  CA  TYR A 297     5903   8590   7554   -777   -949   2178       C  
ATOM   4227  C   TYR A 297     -21.506   9.407 -11.587  1.00 57.47           C  
ANISOU 4227  C   TYR A 297     5992   8335   7510   -766  -1094   2145       C  
ATOM   4228  O   TYR A 297     -20.351   9.780 -11.815  1.00 57.90           O  
ANISOU 4228  O   TYR A 297     6122   8338   7538   -594  -1042   1982       O  
ATOM   4229  CB  TYR A 297     -22.844  10.149 -13.555  1.00 57.09           C  
ANISOU 4229  CB  TYR A 297     5817   8372   7501   -676  -1043   2055       C  
ATOM   4230  CG  TYR A 297     -24.125  10.735 -14.092  1.00 59.34           C  
ANISOU 4230  CG  TYR A 297     5953   8813   7780   -708   -955   2109       C  
ATOM   4231  CD1 TYR A 297     -24.210  12.080 -14.421  1.00 57.63           C  
ANISOU 4231  CD1 TYR A 297     5646   8746   7504   -564   -734   2027       C  
ATOM   4232  CD2 TYR A 297     -25.248   9.941 -14.280  1.00 62.33           C  
ANISOU 4232  CD2 TYR A 297     6281   9183   8219   -886  -1111   2249       C  
ATOM   4233  CE1 TYR A 297     -25.381  12.620 -14.915  1.00 58.40           C  
ANISOU 4233  CE1 TYR A 297     5608   8987   7594   -575   -661   2072       C  
ATOM   4234  CE2 TYR A 297     -26.421  10.471 -14.775  1.00 58.81           C  
ANISOU 4234  CE2 TYR A 297     5687   8901   7759   -910  -1032   2298       C  
ATOM   4235  CZ  TYR A 297     -26.482  11.811 -15.091  1.00 57.40           C  
ANISOU 4235  CZ  TYR A 297     5422   8876   7512   -743   -802   2203       C  
ATOM   4236  OH  TYR A 297     -27.649  12.346 -15.584  1.00 61.42           O  
ANISOU 4236  OH  TYR A 297     5784   9549   8006   -749   -730   2248       O  
ATOM   4237  H   TYR A 297     -21.702  11.939 -11.814  1.00 68.13           H  
ATOM   4238  HA  TYR A 297     -23.490   9.904 -11.617  1.00 69.63           H  
ATOM   4239  HB2 TYR A 297     -22.106  10.618 -13.976  1.00 68.50           H  
ATOM   4240  HB3 TYR A 297     -22.821   9.212 -13.806  1.00 68.50           H  
ATOM   4241  HD1 TYR A 297     -23.468  12.628 -14.303  1.00 69.16           H  
ATOM   4242  HD2 TYR A 297     -25.209   9.036 -14.068  1.00 74.80           H  
ATOM   4243  HE1 TYR A 297     -25.425  13.523 -15.130  1.00 70.08           H  
ATOM   4244  HE2 TYR A 297     -27.167   9.928 -14.894  1.00 70.58           H  
ATOM   4245  HH  TYR A 297     -28.237  11.748 -15.641  1.00 73.71           H  
ATOM   4246  N   LYS A 298     -21.796   8.272 -10.957  1.00 70.48           N  
ANISOU 4246  N   LYS A 298     6782   9350  10646   -827  -2528    209       N  
ATOM   4247  CA  LYS A 298     -20.749   7.306 -10.666  1.00 68.71           C  
ANISOU 4247  CA  LYS A 298     6749   9061  10297   -840  -2491    187       C  
ATOM   4248  C   LYS A 298     -20.131   6.817 -11.969  1.00 66.35           C  
ANISOU 4248  C   LYS A 298     6663   8691   9856   -778  -2709     69       C  
ATOM   4249  O   LYS A 298     -20.837   6.507 -12.932  1.00 70.71           O  
ANISOU 4249  O   LYS A 298     7192   9178  10499   -803  -2942     12       O  
ATOM   4250  CB  LYS A 298     -21.312   6.128  -9.870  1.00 72.14           C  
ANISOU 4250  CB  LYS A 298     7082   9397  10930   -992  -2468    263       C  
ATOM   4251  CG  LYS A 298     -21.733   6.482  -8.452  1.00 73.16           C  
ANISOU 4251  CG  LYS A 298     7039   9600  11159  -1034  -2213    393       C  
ATOM   4252  H   LYS A 298     -22.581   8.042 -10.692  1.00 84.57           H  
ATOM   4253  HA  LYS A 298     -20.055   7.730 -10.138  1.00 82.45           H  
ATOM   4254  HB2 LYS A 298     -22.092   5.784 -10.332  1.00 86.57           H  
ATOM   4255  HB3 LYS A 298     -20.633   5.438  -9.813  1.00 86.57           H  
ATOM   4256  N   GLY A 299     -18.807   6.762 -11.999  1.00 62.67           N  
ANISOU 4256  N   GLY A 299     6408   8237   9167   -688  -2634     33       N  
ATOM   4257  CA  GLY A 299     -18.102   6.384 -13.208  1.00 62.68           C  
ANISOU 4257  CA  GLY A 299     6629   8185   9003   -599  -2805    -72       C  
ATOM   4258  C   GLY A 299     -18.464   4.986 -13.672  1.00 72.64           C  
ANISOU 4258  C   GLY A 299     7944   9294  10362   -694  -3012   -128       C  
ATOM   4259  O   GLY A 299     -19.066   4.182 -12.962  1.00 76.50           O  
ANISOU 4259  O   GLY A 299     8314   9706  11045   -837  -3004    -76       O  
ATOM   4260  H   GLY A 299     -18.295   6.939 -11.332  1.00 75.20           H  
ATOM   4261  HA2 GLY A 299     -18.318   7.009 -13.918  1.00 75.22           H  
ATOM   4262  HA3 GLY A 299     -17.146   6.417 -13.049  1.00 75.22           H  
ATOM   4263  N   ALA A 300     -18.080   4.702 -14.910  1.00 73.05           N  
ANISOU 4263  N   ALA A 300     8182   9298  10277   -604  -3203   -236       N  
ATOM   4264  CA  ALA A 300     -18.302   3.376 -15.461  1.00 71.90           C  
ANISOU 4264  CA  ALA A 300     8125   8996  10198   -672  -3424   -316       C  
ATOM   4265  C   ALA A 300     -17.531   2.345 -14.640  1.00 77.31           C  
ANISOU 4265  C   ALA A 300     8898   9601  10875   -738  -3307   -286       C  
ATOM   4266  O   ALA A 300     -16.414   2.622 -14.186  1.00 73.65           O  
ANISOU 4266  O   ALA A 300     8546   9198  10242   -663  -3116   -254       O  
ATOM   4267  CB  ALA A 300     -17.858   3.320 -16.922  1.00 71.71           C  
ANISOU 4267  CB  ALA A 300     8324   8947   9974   -527  -3626   -444       C  
ATOM   4268  H   ALA A 300     -17.694   5.253 -15.445  1.00 87.67           H  
ATOM   4269  HA  ALA A 300     -19.246   3.161 -15.418  1.00 86.28           H  
ATOM   4270  HB1 ALA A 300     -18.016   2.427 -17.265  1.00 86.05           H  
ATOM   4271  HB2 ALA A 300     -18.370   3.966 -17.432  1.00 86.05           H  
ATOM   4272  HB3 ALA A 300     -16.912   3.532 -16.973  1.00 86.05           H  
ATOM   4273  N   PRO A 301     -18.084   1.152 -14.432  1.00 88.08           N  
ANISOU 4273  N   PRO A 301    10211  10823  12432   -877  -3422   -290       N  
ATOM   4274  CA  PRO A 301     -17.394   0.165 -13.596  1.00 89.46           C  
ANISOU 4274  CA  PRO A 301    10455  10920  12616   -945  -3304   -247       C  
ATOM   4275  C   PRO A 301     -16.095  -0.304 -14.233  1.00 90.36           C  
ANISOU 4275  C   PRO A 301    10856  10990  12487   -827  -3334   -337       C  
ATOM   4276  O   PRO A 301     -15.955  -0.357 -15.458  1.00 90.43           O  
ANISOU 4276  O   PRO A 301    11018  10966  12375   -726  -3524   -455       O  
ATOM   4277  CB  PRO A 301     -18.409  -0.978 -13.482  1.00 89.19           C  
ANISOU 4277  CB  PRO A 301    10292  10726  12868  -1112  -3469   -239       C  
ATOM   4278  CG  PRO A 301     -19.263  -0.849 -14.693  1.00 90.76           C  
ANISOU 4278  CG  PRO A 301    10471  10881  13130  -1093  -3754   -344       C  
ATOM   4279  CD  PRO A 301     -19.339   0.622 -14.993  1.00 91.67           C  
ANISOU 4279  CD  PRO A 301    10545  11169  13118   -977  -3681   -334       C  
ATOM   4280  HA  PRO A 301     -17.212   0.530 -12.716  1.00107.35           H  
ATOM   4281  HB2 PRO A 301     -17.944  -1.830 -13.477  1.00107.02           H  
ATOM   4282  HB3 PRO A 301     -18.936  -0.869 -12.675  1.00107.02           H  
ATOM   4283  HG2 PRO A 301     -18.853  -1.326 -15.431  1.00108.91           H  
ATOM   4284  HG3 PRO A 301     -20.146  -1.204 -14.506  1.00108.91           H  
ATOM   4285  HD2 PRO A 301     -19.370   0.770 -15.951  1.00110.01           H  
ATOM   4286  HD3 PRO A 301     -20.104   1.019 -14.547  1.00110.01           H  
ATOM   4287  N   THR A 302     -15.140  -0.644 -13.377  1.00 93.38           N  
ANISOU 4287  N   THR A 302    11311  11374  12796   -833  -3141   -275       N  
ATOM   4288  CA  THR A 302     -13.827  -1.063 -13.847  1.00 96.96           C  
ANISOU 4288  CA  THR A 302    12023  11789  13030   -719  -3132   -338       C  
ATOM   4289  C   THR A 302     -13.961  -2.296 -14.740  1.00101.20           C  
ANISOU 4289  C   THR A 302    12693  12154  13602   -739  -3381   -456       C  
ATOM   4290  O   THR A 302     -14.656  -3.250 -14.365  1.00107.08           O  
ANISOU 4290  O   THR A 302    13338  12776  14570   -889  -3470   -442       O  
ATOM   4291  CB  THR A 302     -12.902  -1.363 -12.665  1.00 93.95           C  
ANISOU 4291  CB  THR A 302    11668  11416  12611   -750  -2900   -241       C  
ATOM   4292  OG1 THR A 302     -11.674  -1.915 -13.150  1.00 93.01           O  
ANISOU 4292  OG1 THR A 302    11792  11236  12310   -650  -2906   -299       O  
ATOM   4293  CG2 THR A 302     -13.545  -2.347 -11.683  1.00 95.83           C  
ANISOU 4293  CG2 THR A 302    11765  11561  13086   -930  -2878   -164       C  
ATOM   4294  H   THR A 302     -15.226  -0.641 -12.521  1.00112.06           H  
ATOM   4295  HA  THR A 302     -13.431  -0.349 -14.371  1.00116.36           H  
ATOM   4296  HB  THR A 302     -12.716  -0.539 -12.189  1.00112.74           H  
ATOM   4297  HG1 THR A 302     -11.160  -2.083 -12.507  1.00111.61           H  
ATOM   4298 HG21 THR A 302     -12.941  -2.521 -10.945  1.00115.00           H  
ATOM   4299 HG22 THR A 302     -14.371  -1.976 -11.334  1.00115.00           H  
ATOM   4300 HG23 THR A 302     -13.742  -3.184 -12.133  1.00115.00           H  
ATOM   4301  N   PRO A 303     -13.327  -2.318 -15.915  1.00 95.84           N  
ANISOU 4301  N   PRO A 303    12240  11458  12718   -586  -3499   -570       N  
ATOM   4302  CA  PRO A 303     -13.446  -3.492 -16.790  1.00 94.93           C  
ANISOU 4302  CA  PRO A 303    12273  11174  12622   -589  -3749   -701       C  
ATOM   4303  C   PRO A 303     -12.898  -4.751 -16.134  1.00 97.09           C  
ANISOU 4303  C   PRO A 303    12610  11313  12968   -678  -3700   -679       C  
ATOM   4304  O   PRO A 303     -12.167  -4.707 -15.141  1.00 93.05           O  
ANISOU 4304  O   PRO A 303    12081  10846  12427   -700  -3465   -572       O  
ATOM   4305  CB  PRO A 303     -12.619  -3.107 -18.025  1.00 95.72           C  
ANISOU 4305  CB  PRO A 303    12624  11317  12430   -369  -3807   -801       C  
ATOM   4306  CG  PRO A 303     -12.549  -1.628 -17.998  1.00 94.66           C  
ANISOU 4306  CG  PRO A 303    12408  11367  12193   -278  -3662   -730       C  
ATOM   4307  CD  PRO A 303     -12.548  -1.242 -16.553  1.00 92.66           C  
ANISOU 4307  CD  PRO A 303    11959  11183  12063   -395  -3420   -584       C  
ATOM   4308  HA  PRO A 303     -14.370  -3.633 -17.048  1.00113.91           H  
ATOM   4309  HB2 PRO A 303     -11.732  -3.494 -17.958  1.00114.87           H  
ATOM   4310  HB3 PRO A 303     -13.068  -3.415 -18.828  1.00114.87           H  
ATOM   4311  HG2 PRO A 303     -11.732  -1.335 -18.430  1.00113.60           H  
ATOM   4312  HG3 PRO A 303     -13.324  -1.259 -18.449  1.00113.60           H  
ATOM   4313  HD2 PRO A 303     -11.642  -1.229 -16.206  1.00111.19           H  
ATOM   4314  HD3 PRO A 303     -12.989  -0.387 -16.431  1.00111.19           H  
ATOM   4315  N   LYS A 304     -13.263  -5.895 -16.719  1.00107.62           N  
ANISOU 4315  N   LYS A 304    14019  12470  14400   -726  -3938   -788       N  
ATOM   4316  CA  LYS A 304     -12.791  -7.180 -16.215  1.00110.84           C  
ANISOU 4316  CA  LYS A 304    14494  12727  14894   -808  -3921   -778       C  
ATOM   4317  C   LYS A 304     -11.369  -7.471 -16.679  1.00111.46           C  
ANISOU 4317  C   LYS A 304    14853  12789  14708   -647  -3855   -835       C  
ATOM   4318  O   LYS A 304     -10.568  -8.033 -15.923  1.00108.88           O  
ANISOU 4318  O   LYS A 304    14568  12422  14378   -681  -3696   -764       O  
ATOM   4319  CB  LYS A 304     -13.735  -8.297 -16.662  1.00112.90           C  
ANISOU 4319  CB  LYS A 304    14721  12788  15388   -922  -4213   -875       C  
ATOM   4320  H   LYS A 304     -13.780  -5.951 -17.404  1.00129.14           H  
ATOM   4321  HA  LYS A 304     -12.791  -7.159 -15.245  1.00133.01           H  
ATOM   4322  N   ARG A 305     -11.041  -7.096 -17.915  1.00116.11           N  
ANISOU 4322  N   ARG A 305    15634  13408  15073   -466  -3968   -954       N  
ATOM   4323  CA  ARG A 305      -9.704  -7.284 -18.477  1.00116.32           C  
ANISOU 4323  CA  ARG A 305    15930  13427  14838   -285  -3898  -1002       C  
ATOM   4324  C   ARG A 305      -8.968  -5.949 -18.405  1.00111.00           C  
ANISOU 4324  C   ARG A 305    15263  12947  13964   -148  -3672   -911       C  
ATOM   4325  O   ARG A 305      -9.129  -5.090 -19.276  1.00111.07           O  
ANISOU 4325  O   ARG A 305    15316  13051  13833    -15  -3732   -956       O  
ATOM   4326  CB  ARG A 305      -9.788  -7.801 -19.910  1.00117.98           C  
ANISOU 4326  CB  ARG A 305    16366  13538  14924   -153  -4166  -1188       C  
ATOM   4327  H   ARG A 305     -11.590  -6.721 -18.461  1.00139.33           H  
ATOM   4328  HA  ARG A 305      -9.217  -7.933 -17.944  1.00139.58           H  
ATOM   4329  N   ILE A 306      -8.153  -5.780 -17.363  1.00105.80           N  
ANISOU 4329  N   ILE A 306    14559  12341  13299   -177  -3419   -781       N  
ATOM   4330  CA  ILE A 306      -7.422  -4.533 -17.171  1.00103.35           C  
ANISOU 4330  CA  ILE A 306    14235  12196  12836    -62  -3205   -686       C  
ATOM   4331  C   ILE A 306      -6.350  -4.404 -18.243  1.00103.37           C  
ANISOU 4331  C   ILE A 306    14489  12208  12581    165  -3194   -740       C  
ATOM   4332  O   ILE A 306      -5.548  -5.322 -18.459  1.00108.79           O  
ANISOU 4332  O   ILE A 306    15354  12785  13195    219  -3194   -778       O  
ATOM   4333  CB  ILE A 306      -6.810  -4.482 -15.763  1.00 98.78           C  
ANISOU 4333  CB  ILE A 306    13555  11654  12324   -152  -2963   -544       C  
ATOM   4334  CG1 ILE A 306      -7.896  -4.683 -14.705  1.00 98.37           C  
ANISOU 4334  CG1 ILE A 306    13264  11592  12519   -363  -2964   -481       C  
ATOM   4335  CG2 ILE A 306      -6.110  -3.154 -15.530  1.00 95.37           C  
ANISOU 4335  CG2 ILE A 306    13093  11380  11765    -42  -2765   -453       C  
ATOM   4336  H   ILE A 306      -8.008  -6.372 -16.757  1.00126.96           H  
ATOM   4337  HA  ILE A 306      -8.034  -3.787 -17.262  1.00124.02           H  
ATOM   4338  HB  ILE A 306      -6.158  -5.196 -15.680  1.00118.54           H  
ATOM   4339 HG21 ILE A 306      -5.734  -3.149 -14.636  1.00114.45           H  
ATOM   4340 HG22 ILE A 306      -5.404  -3.050 -16.187  1.00114.45           H  
ATOM   4341 HG23 ILE A 306      -6.757  -2.437 -15.621  1.00114.45           H  
ATOM   4342  N   GLU A 307      -6.326  -3.257 -18.915  1.00 94.11           N  
ANISOU 4342  N   GLU A 307    13325  11163  11272    307  -3173   -734       N  
ATOM   4343  CA  GLU A 307      -5.349  -2.979 -19.959  1.00 92.82           C  
ANISOU 4343  CA  GLU A 307    13381  11026  10860    543  -3139   -760       C  
ATOM   4344  C   GLU A 307      -4.211  -2.162 -19.362  1.00 91.50           C  
ANISOU 4344  C   GLU A 307    13186  10954  10625    616  -2868   -616       C  
ATOM   4345  O   GLU A 307      -4.444  -1.088 -18.796  1.00 88.14           O  
ANISOU 4345  O   GLU A 307    12584  10647  10259    578  -2761   -528       O  
ATOM   4346  CB  GLU A 307      -5.994  -2.232 -21.126  1.00 97.39           C  
ANISOU 4346  CB  GLU A 307    13992  11681  11329    669  -3285   -830       C  
ATOM   4347  H   GLU A 307      -6.877  -2.611 -18.780  1.00112.94           H  
ATOM   4348  HA  GLU A 307      -4.986  -3.815 -20.293  1.00111.38           H  
ATOM   4349  N   TYR A 308      -2.989  -2.673 -19.483  1.00 94.59           N  
ANISOU 4349  N   TYR A 308    13750  11286  10904    721  -2766   -593       N  
ATOM   4350  CA  TYR A 308      -1.815  -1.984 -18.959  1.00 90.15           C  
ANISOU 4350  CA  TYR A 308    13169  10791  10293    796  -2524   -454       C  
ATOM   4351  C   TYR A 308      -1.074  -1.262 -20.082  1.00 90.59           C  
ANISOU 4351  C   TYR A 308    13366  10911  10144   1047  -2467   -433       C  
ATOM   4352  O   TYR A 308      -1.161  -1.672 -21.237  1.00 90.96           O  
ANISOU 4352  O   TYR A 308    13593  10917  10049   1180  -2596   -532       O  
ATOM   4353  CB  TYR A 308      -0.877  -2.970 -18.266  1.00 89.50           C  
ANISOU 4353  CB  TYR A 308    13160  10601  10243    749  -2425   -414       C  
ATOM   4354  CG  TYR A 308      -1.451  -3.574 -17.008  1.00 89.36           C  
ANISOU 4354  CG  TYR A 308    12990  10535  10427    513  -2432   -394       C  
ATOM   4355  CD1 TYR A 308      -2.340  -4.637 -17.072  1.00 90.87           C  
ANISOU 4355  CD1 TYR A 308    13186  10616  10723    388  -2613   -494       C  
ATOM   4356  CD2 TYR A 308      -1.105  -3.082 -15.758  1.00 87.13           C  
ANISOU 4356  CD2 TYR A 308    12558  10314  10234    424  -2260   -271       C  
ATOM   4357  CE1 TYR A 308      -2.869  -5.193 -15.926  1.00 90.53           C  
ANISOU 4357  CE1 TYR A 308    12995  10529  10874    181  -2604   -454       C  
ATOM   4358  CE2 TYR A 308      -1.629  -3.632 -14.605  1.00 85.80           C  
ANISOU 4358  CE2 TYR A 308    12258  10111  10233    226  -2253   -241       C  
ATOM   4359  CZ  TYR A 308      -2.510  -4.686 -14.694  1.00 88.01           C  
ANISOU 4359  CZ  TYR A 308    12537  10285  10620    106  -2416   -324       C  
ATOM   4360  OH  TYR A 308      -3.033  -5.236 -13.547  1.00 88.33           O  
ANISOU 4360  OH  TYR A 308    12437  10289  10837    -83  -2393   -273       O  
ATOM   4361  H   TYR A 308      -2.813  -3.422 -19.868  1.00113.51           H  
ATOM   4362  HA  TYR A 308      -2.097  -1.323 -18.308  1.00108.18           H  
ATOM   4363  HB2 TYR A 308      -0.676  -3.694 -18.878  1.00107.40           H  
ATOM   4364  HB3 TYR A 308      -0.059  -2.507 -18.025  1.00107.40           H  
ATOM   4365  HD1 TYR A 308      -2.584  -4.980 -17.901  1.00109.04           H  
ATOM   4366  HD2 TYR A 308      -0.510  -2.370 -15.695  1.00104.55           H  
ATOM   4367  HE1 TYR A 308      -3.464  -5.905 -15.984  1.00108.64           H  
ATOM   4368  HE2 TYR A 308      -1.388  -3.292 -13.774  1.00102.97           H  
ATOM   4369  HH  TYR A 308      -2.732  -4.835 -12.873  1.00106.00           H  
ATOM   4370  N   PRO A 309      -0.341  -0.182 -19.755  0.80 92.01           N  
ANISOU 4370  N   PRO A 309    13465  11186  10309   1120  -2276   -300       N  
ATOM   4371  CA  PRO A 309      -0.250   0.440 -18.429  0.80 90.27           C  
ANISOU 4371  CA  PRO A 309    13039  11021  10239    984  -2137   -194       C  
ATOM   4372  C   PRO A 309      -1.551   1.125 -18.033  0.80 86.89           C  
ANISOU 4372  C   PRO A 309    12408  10677   9930    852  -2212   -215       C  
ATOM   4373  O   PRO A 309      -2.351   1.481 -18.897  0.80 88.28           O  
ANISOU 4373  O   PRO A 309    12587  10896  10059    904  -2342   -281       O  
ATOM   4374  CB  PRO A 309       0.884   1.461 -18.588  0.80 88.41           C  
ANISOU 4374  CB  PRO A 309    12809  10851   9931   1151  -1954    -68       C  
ATOM   4375  CG  PRO A 309       1.638   1.026 -19.799  0.80 90.18           C  
ANISOU 4375  CG  PRO A 309    13262  11025   9976   1360  -1957    -87       C  
ATOM   4376  CD  PRO A 309       0.612   0.422 -20.700  0.80 93.56           C  
ANISOU 4376  CD  PRO A 309    13791  11425  10332   1365  -2175   -239       C  
ATOM   4377  HA  PRO A 309      -0.007  -0.216 -17.758  0.80108.32           H  
ATOM   4378  HB2 PRO A 309       0.510   2.347 -18.718  0.80106.09           H  
ATOM   4379  HB3 PRO A 309       1.454   1.441 -17.804  0.80106.09           H  
ATOM   4380  HG2 PRO A 309       2.054   1.795 -20.220  0.80108.21           H  
ATOM   4381  HG3 PRO A 309       2.305   0.368 -19.550  0.80108.21           H  
ATOM   4382  HD2 PRO A 309       0.176   1.110 -21.228  0.80112.27           H  
ATOM   4383  HD3 PRO A 309       1.012  -0.260 -21.261  0.80112.27           H  
ATOM   4384  N   LEU A 310      -1.755   1.296 -16.731  1.00 80.06           N  
ANISOU 4384  N   LEU A 310    11372   9834   9213    691  -2131   -157       N  
ATOM   4385  CA  LEU A 310      -3.012   1.822 -16.229  1.00 78.98           C  
ANISOU 4385  CA  LEU A 310    11037   9767   9205    556  -2188   -171       C  
ATOM   4386  C   LEU A 310      -3.162   3.299 -16.581  1.00 76.39           C  
ANISOU 4386  C   LEU A 310    10612   9564   8847    656  -2140   -127       C  
ATOM   4387  O   LEU A 310      -2.185   4.015 -16.819  1.00 76.48           O  
ANISOU 4387  O   LEU A 310    10665   9615   8780    798  -2019    -53       O  
ATOM   4388  CB  LEU A 310      -3.092   1.638 -14.714  1.00 77.76           C  
ANISOU 4388  CB  LEU A 310    10742   9609   9195    384  -2088   -109       C  
ATOM   4389  CG  LEU A 310      -2.902   0.208 -14.206  1.00 76.85           C  
ANISOU 4389  CG  LEU A 310    10700   9370   9129    275  -2112   -128       C  
ATOM   4390  CD1 LEU A 310      -2.800   0.195 -12.690  1.00 76.25           C  
ANISOU 4390  CD1 LEU A 310    10496   9312   9165    142  -1981    -41       C  
ATOM   4391  CD2 LEU A 310      -4.039  -0.681 -14.675  1.00 77.23           C  
ANISOU 4391  CD2 LEU A 310    10752   9343   9249    182  -2309   -231       C  
ATOM   4392  H   LEU A 310      -1.178   1.114 -16.120  1.00 96.07           H  
ATOM   4393  HA  LEU A 310      -3.747   1.336 -16.634  1.00 94.78           H  
ATOM   4394  HB2 LEU A 310      -2.406   2.186 -14.303  1.00 93.31           H  
ATOM   4395  HB3 LEU A 310      -3.965   1.938 -14.416  1.00 93.31           H  
ATOM   4396  HG  LEU A 310      -2.075  -0.147 -14.565  1.00 92.22           H  
ATOM   4397 HD11 LEU A 310      -2.680  -0.720 -12.391  1.00 91.50           H  
ATOM   4398 HD12 LEU A 310      -2.041   0.734 -12.420  1.00 91.50           H  
ATOM   4399 HD13 LEU A 310      -3.617   0.561 -12.316  1.00 91.50           H  
ATOM   4400 HD21 LEU A 310      -3.894  -1.580 -14.340  1.00 92.68           H  
ATOM   4401 HD22 LEU A 310      -4.876  -0.331 -14.332  1.00 92.68           H  
ATOM   4402 HD23 LEU A 310      -4.055  -0.688 -15.645  1.00 92.68           H  
ATOM   4403  N   LYS A 311      -4.414   3.751 -16.618  1.00 71.16           N  
ANISOU 4403  N   LYS A 311     9809   8960   8267    580  -2237   -165       N  
ATOM   4404  CA  LYS A 311      -4.685   5.171 -16.765  1.00 70.44           C  
ANISOU 4404  CA  LYS A 311     9593   8988   8183    647  -2188   -118       C  
ATOM   4405  C   LYS A 311      -4.179   5.930 -15.542  1.00 67.55           C  
ANISOU 4405  C   LYS A 311     9094   8673   7898    602  -2006    -21       C  
ATOM   4406  O   LYS A 311      -4.017   5.373 -14.453  1.00 64.78           O  
ANISOU 4406  O   LYS A 311     8708   8283   7621    481  -1942      1       O  
ATOM   4407  CB  LYS A 311      -6.181   5.430 -16.937  1.00 72.01           C  
ANISOU 4407  CB  LYS A 311     9653   9231   8479    557  -2328   -175       C  
ATOM   4408  CG  LYS A 311      -6.825   4.750 -18.130  1.00 73.16           C  
ANISOU 4408  CG  LYS A 311     9912   9323   8561    594  -2544   -284       C  
ATOM   4409  CD  LYS A 311      -8.287   5.160 -18.242  1.00 76.34           C  
ANISOU 4409  CD  LYS A 311    10148   9773   9085    505  -2678   -322       C  
ATOM   4410  CE  LYS A 311      -9.059   4.294 -19.225  1.00 78.82           C  
ANISOU 4410  CE  LYS A 311    10557  10009   9382    499  -2927   -443       C  
ATOM   4411  NZ  LYS A 311     -10.507   4.646 -19.231  1.00 77.72           N  
ANISOU 4411  NZ  LYS A 311    10229   9903   9396    394  -3061   -469       N  
ATOM   4412  H   LYS A 311      -5.116   3.258 -16.560  1.00 85.39           H  
ATOM   4413  HA  LYS A 311      -4.223   5.509 -17.549  1.00 84.53           H  
ATOM   4414  HB2 LYS A 311      -6.640   5.118 -16.141  1.00 86.42           H  
ATOM   4415  HB3 LYS A 311      -6.319   6.385 -17.037  1.00 86.42           H  
ATOM   4416  HG2 LYS A 311      -6.367   5.017 -18.942  1.00 87.79           H  
ATOM   4417  HG3 LYS A 311      -6.782   3.788 -18.016  1.00 87.79           H  
ATOM   4418  HD2 LYS A 311      -8.708   5.076 -17.372  1.00 91.61           H  
ATOM   4419  HD3 LYS A 311      -8.336   6.079 -18.548  1.00 91.61           H  
ATOM   4420  HE2 LYS A 311      -8.708   4.431 -20.118  1.00 94.58           H  
ATOM   4421  HE3 LYS A 311      -8.973   3.362 -18.968  1.00 94.58           H  
ATOM   4422  HZ1 LYS A 311     -10.943   4.130 -19.811  1.00 93.26           H  
ATOM   4423  HZ2 LYS A 311     -10.853   4.525 -18.420  1.00 93.26           H  
ATOM   4424  HZ3 LYS A 311     -10.612   5.498 -19.466  1.00 93.26           H  
ATOM   4425  N   ALA A 312      -3.939   7.228 -15.731  1.00 66.83           N  
ANISOU 4425  N   ALA A 312     8931   8669   7794    707  -1928     38       N  
ATOM   4426  CA  ALA A 312      -3.455   8.053 -14.630  1.00 50.92           C  
ANISOU 4426  CA  ALA A 312     6794   6696   5857    680  -1776    117       C  
ATOM   4427  C   ALA A 312      -4.420   8.015 -13.451  1.00 53.31           C  
ANISOU 4427  C   ALA A 312     6936   7027   6294    504  -1771    102       C  
ATOM   4428  O   ALA A 312      -4.002   7.867 -12.297  1.00 52.15           O  
ANISOU 4428  O   ALA A 312     6754   6866   6194    431  -1672    140       O  
ATOM   4429  CB  ALA A 312      -3.235   9.489 -15.105  1.00 47.01           C  
ANISOU 4429  CB  ALA A 312     6227   6281   5353    815  -1719    175       C  
ATOM   4430  H   ALA A 312      -4.048   7.647 -16.473  1.00 80.20           H  
ATOM   4431  HA  ALA A 312      -2.601   7.704 -14.328  1.00 61.11           H  
ATOM   4432  HB1 ALA A 312      -2.913  10.022 -14.360  1.00 56.41           H  
ATOM   4433  HB2 ALA A 312      -2.579   9.489 -15.819  1.00 56.41           H  
ATOM   4434  HB3 ALA A 312      -4.077   9.847 -15.428  1.00 56.41           H  
ATOM   4435  N   HIS A 313      -5.722   8.140 -13.721  1.00 54.88           N  
ANISOU 4435  N   HIS A 313     7034   7264   6554    440  -1876     53       N  
ATOM   4436  CA  HIS A 313      -6.698   8.158 -12.638  1.00 57.06           C  
ANISOU 4436  CA  HIS A 313     7144   7570   6966    286  -1855     54       C  
ATOM   4437  C   HIS A 313      -6.803   6.810 -11.938  1.00 56.92           C  
ANISOU 4437  C   HIS A 313     7165   7471   6992    150  -1869     41       C  
ATOM   4438  O   HIS A 313      -7.243   6.757 -10.785  1.00 57.12           O  
ANISOU 4438  O   HIS A 313     7075   7517   7113     38  -1796     73       O  
ATOM   4439  CB  HIS A 313      -8.069   8.594 -13.166  1.00 61.35           C  
ANISOU 4439  CB  HIS A 313     7561   8165   7583    255  -1968     15       C  
ATOM   4440  CG  HIS A 313      -8.829   7.512 -13.868  1.00 62.91           C  
ANISOU 4440  CG  HIS A 313     7812   8292   7797    192  -2145    -57       C  
ATOM   4441  ND1 HIS A 313      -9.532   6.537 -13.193  1.00 67.43           N  
ANISOU 4441  ND1 HIS A 313     8326   8806   8487     32  -2184    -70       N  
ATOM   4442  CD2 HIS A 313      -9.014   7.264 -15.186  1.00 66.11           C  
ANISOU 4442  CD2 HIS A 313     8324   8670   8123    272  -2303   -121       C  
ATOM   4443  CE1 HIS A 313     -10.108   5.729 -14.065  1.00 70.10           C  
ANISOU 4443  CE1 HIS A 313     8725   9074   8836      8  -2368   -143       C  
ATOM   4444  NE2 HIS A 313      -9.810   6.149 -15.282  1.00 68.83           N  
ANISOU 4444  NE2 HIS A 313     8673   8933   8546    155  -2449   -182       N  
ATOM   4445  H   HIS A 313      -6.058   8.215 -14.509  1.00 65.86           H  
ATOM   4446  HA  HIS A 313      -6.416   8.810 -11.978  1.00 68.47           H  
ATOM   4447  HB2 HIS A 313      -8.608   8.896 -12.418  1.00 73.62           H  
ATOM   4448  HB3 HIS A 313      -7.943   9.322 -13.794  1.00 73.62           H  
ATOM   4449  HD1 HIS A 313      -9.584   6.464 -12.338  1.00 80.91           H  
ATOM   4450  HD2 HIS A 313      -8.663   7.754 -15.895  1.00 79.33           H  
ATOM   4451  HE1 HIS A 313     -10.635   4.991 -13.858  1.00 84.12           H  
ATOM   4452  N   GLN A 314      -6.407   5.723 -12.602  1.00 57.38           N  
ANISOU 4452  N   GLN A 314     7384   7435   6983    166  -1954      0       N  
ATOM   4453  CA  GLN A 314      -6.352   4.432 -11.925  1.00 57.90           C  
ANISOU 4453  CA  GLN A 314     7492   7410   7096     45  -1957     -1       C  
ATOM   4454  C   GLN A 314      -5.214   4.394 -10.913  1.00 58.10           C  
ANISOU 4454  C   GLN A 314     7556   7427   7090     50  -1798     70       C  
ATOM   4455  O   GLN A 314      -5.364   3.835  -9.820  1.00 58.58           O  
ANISOU 4455  O   GLN A 314     7566   7469   7224    -67  -1739    105       O  
ATOM   4456  CB  GLN A 314      -6.197   3.310 -12.950  1.00 57.93           C  
ANISOU 4456  CB  GLN A 314     7666   7306   7037     73  -2099    -74       C  
ATOM   4457  CG  GLN A 314      -7.382   3.157 -13.883  1.00 57.28           C  
ANISOU 4457  CG  GLN A 314     7554   7211   6998     51  -2291   -156       C  
ATOM   4458  CD  GLN A 314      -7.215   1.990 -14.830  1.00 58.86           C  
ANISOU 4458  CD  GLN A 314     7938   7293   7133     82  -2446   -244       C  
ATOM   4459  OE1 GLN A 314      -6.333   1.997 -15.690  1.00 61.57           O  
ANISOU 4459  OE1 GLN A 314     8455   7620   7317    235  -2450   -267       O  
ATOM   4460  NE2 GLN A 314      -8.053   0.973 -14.671  1.00 59.77           N  
ANISOU 4460  NE2 GLN A 314     8015   7317   7379    -58  -2571   -289       N  
ATOM   4461  H   GLN A 314      -6.169   5.707 -13.428  1.00 68.86           H  
ATOM   4462  HA  GLN A 314      -7.184   4.289 -11.447  1.00 69.48           H  
ATOM   4463  HB2 GLN A 314      -5.414   3.491 -13.493  1.00 69.51           H  
ATOM   4464  HB3 GLN A 314      -6.082   2.471 -12.478  1.00 69.51           H  
ATOM   4465  HG2 GLN A 314      -8.183   3.006 -13.358  1.00 68.73           H  
ATOM   4466  HG3 GLN A 314      -7.477   3.964 -14.412  1.00 68.73           H  
ATOM   4467 HE21 GLN A 314      -8.651   1.001 -14.053  1.00 71.73           H  
ATOM   4468 HE22 GLN A 314      -7.998   0.286 -15.185  1.00 71.73           H  
ATOM   4469  N   LYS A 315      -4.067   4.984 -11.258  1.00 53.86           N  
ANISOU 4469  N   LYS A 315     7107   6904   6454    189  -1728    101       N  
ATOM   4470  CA  LYS A 315      -2.967   5.069 -10.304  1.00 52.98           C  
ANISOU 4470  CA  LYS A 315     7019   6783   6327    200  -1591    170       C  
ATOM   4471  C   LYS A 315      -3.333   5.963  -9.127  1.00 50.02           C  
ANISOU 4471  C   LYS A 315     6484   6495   6028    145  -1497    209       C  
ATOM   4472  O   LYS A 315      -2.947   5.685  -7.985  1.00 47.10           O  
ANISOU 4472  O   LYS A 315     6103   6114   5677     85  -1412    251       O  
ATOM   4473  CB  LYS A 315      -1.708   5.583 -11.003  1.00 51.64           C  
ANISOU 4473  CB  LYS A 315     6956   6602   6063    366  -1543    205       C  
ATOM   4474  CG  LYS A 315      -1.148   4.632 -12.049  1.00 53.93           C  
ANISOU 4474  CG  LYS A 315     7430   6801   6259    441  -1606    175       C  
ATOM   4475  CD  LYS A 315       0.072   5.220 -12.737  1.00 55.82           C  
ANISOU 4475  CD  LYS A 315     7759   7037   6415    621  -1535    232       C  
ATOM   4476  CE  LYS A 315       0.659   4.252 -13.747  1.00 58.52           C  
ANISOU 4476  CE  LYS A 315     8297   7290   6649    713  -1581    206       C  
ATOM   4477  NZ  LYS A 315       1.818   4.840 -14.466  1.00 60.10           N  
ANISOU 4477  NZ  LYS A 315     8576   7488   6773    902  -1495    280       N  
ATOM   4478  H   LYS A 315      -3.905   5.337 -12.025  1.00 64.63           H  
ATOM   4479  HA  LYS A 315      -2.778   4.182  -9.960  1.00 63.57           H  
ATOM   4480  HB2 LYS A 315      -1.917   6.420 -11.446  1.00 61.97           H  
ATOM   4481  HB3 LYS A 315      -1.018   5.728 -10.336  1.00 61.97           H  
ATOM   4482  HG2 LYS A 315      -0.886   3.803 -11.620  1.00 64.71           H  
ATOM   4483  HG3 LYS A 315      -1.826   4.462 -12.722  1.00 64.71           H  
ATOM   4484  HD2 LYS A 315      -0.184   6.030 -13.206  1.00 66.99           H  
ATOM   4485  HD3 LYS A 315       0.751   5.416 -12.073  1.00 66.99           H  
ATOM   4486  HE2 LYS A 315       0.962   3.454 -13.285  1.00 70.22           H  
ATOM   4487  HE3 LYS A 315      -0.020   4.023 -14.401  1.00 70.22           H  
ATOM   4488  HZ1 LYS A 315       2.142   4.253 -15.051  1.00 72.12           H  
ATOM   4489  HZ2 LYS A 315       1.564   5.573 -14.902  1.00 72.12           H  
ATOM   4490  HZ3 LYS A 315       2.458   5.056 -13.886  1.00 72.12           H  
ATOM   4491  N   VAL A 316      -4.076   7.042  -9.382  1.00 48.40           N  
ANISOU 4491  N   VAL A 316     6157   6374   5858    174  -1511    194       N  
ATOM   4492  CA  VAL A 316      -4.571   7.874  -8.289  1.00 49.43           C  
ANISOU 4492  CA  VAL A 316     6135   6585   6060    126  -1427    218       C  
ATOM   4493  C   VAL A 316      -5.480   7.057  -7.382  1.00 49.32           C  
ANISOU 4493  C   VAL A 316     6052   6567   6122    -25  -1421    222       C  
ATOM   4494  O   VAL A 316      -5.421   7.169  -6.152  1.00 51.55           O  
ANISOU 4494  O   VAL A 316     6281   6879   6426    -71  -1320    260       O  
ATOM   4495  CB  VAL A 316      -5.292   9.117  -8.846  1.00 45.99           C  
ANISOU 4495  CB  VAL A 316     5581   6233   5660    184  -1454    200       C  
ATOM   4496  CG1 VAL A 316      -5.854   9.968  -7.716  1.00 50.14           C  
ANISOU 4496  CG1 VAL A 316     5952   6838   6260    142  -1366    216       C  
ATOM   4497  CG2 VAL A 316      -4.344   9.943  -9.698  1.00 46.03           C  
ANISOU 4497  CG2 VAL A 316     5647   6242   5602    341  -1444    219       C  
ATOM   4498  H   VAL A 316      -4.304   7.309 -10.168  1.00 58.08           H  
ATOM   4499  HA  VAL A 316      -3.818   8.179  -7.760  1.00 59.31           H  
ATOM   4500  HB  VAL A 316      -6.031   8.831  -9.406  1.00 55.19           H  
ATOM   4501 HG11 VAL A 316      -6.301  10.741  -8.095  1.00 60.16           H  
ATOM   4502 HG12 VAL A 316      -6.486   9.437  -7.205  1.00 60.16           H  
ATOM   4503 HG13 VAL A 316      -5.125  10.254  -7.144  1.00 60.16           H  
ATOM   4504 HG21 VAL A 316      -4.819  10.718 -10.037  1.00 55.24           H  
ATOM   4505 HG22 VAL A 316      -3.595  10.227  -9.151  1.00 55.24           H  
ATOM   4506 HG23 VAL A 316      -4.029   9.399 -10.437  1.00 55.24           H  
ATOM   4507  N   ALA A 317      -6.333   6.220  -7.973  1.00 49.33           N  
ANISOU 4507  N   ALA A 317     6050   6523   6169    -98  -1530    186       N  
ATOM   4508  CA  ALA A 317      -7.181   5.341  -7.177  1.00 49.37           C  
ANISOU 4508  CA  ALA A 317     5981   6505   6273   -243  -1525    207       C  
ATOM   4509  C   ALA A 317      -6.346   4.385  -6.337  1.00 49.12           C  
ANISOU 4509  C   ALA A 317     6045   6410   6209   -288  -1454    252       C  
ATOM   4510  O   ALA A 317      -6.654   4.146  -5.163  1.00 51.21           O  
ANISOU 4510  O   ALA A 317     6237   6696   6523   -367  -1364    306       O  
ATOM   4511  CB  ALA A 317      -8.128   4.563  -8.089  1.00 50.08           C  
ANISOU 4511  CB  ALA A 317     6060   6532   6435   -308  -1683    157       C  
ATOM   4512  H   ALA A 317      -6.437   6.143  -8.824  1.00 59.19           H  
ATOM   4513  HA  ALA A 317      -7.718   5.880  -6.575  1.00 59.25           H  
ATOM   4514  HB1 ALA A 317      -8.685   3.984  -7.546  1.00 60.09           H  
ATOM   4515  HB2 ALA A 317      -8.681   5.192  -8.579  1.00 60.09           H  
ATOM   4516  HB3 ALA A 317      -7.603   4.032  -8.709  1.00 60.09           H  
ATOM   4517  N   ILE A 318      -5.290   3.819  -6.924  1.00 49.36           N  
ANISOU 4517  N   ILE A 318     6238   6361   6155   -229  -1488    237       N  
ATOM   4518  CA  ILE A 318      -4.407   2.927  -6.176  1.00 50.94           C  
ANISOU 4518  CA  ILE A 318     6533   6495   6326   -262  -1423    284       C  
ATOM   4519  C   ILE A 318      -3.779   3.669  -5.003  1.00 49.04           C  
ANISOU 4519  C   ILE A 318     6260   6322   6051   -231  -1287    340       C  
ATOM   4520  O   ILE A 318      -3.805   3.197  -3.861  1.00 51.41           O  
ANISOU 4520  O   ILE A 318     6537   6624   6372   -305  -1212    393       O  
ATOM   4521  CB  ILE A 318      -3.335   2.329  -7.106  1.00 52.92           C  
ANISOU 4521  CB  ILE A 318     6964   6653   6492   -181  -1477    259       C  
ATOM   4522  CG1 ILE A 318      -3.983   1.366  -8.104  1.00 53.97           C  
ANISOU 4522  CG1 ILE A 318     7148   6701   6656   -222  -1624    192       C  
ATOM   4523  CG2 ILE A 318      -2.258   1.605  -6.297  1.00 54.84           C  
ANISOU 4523  CG2 ILE A 318     7300   6835   6702   -196  -1396    317       C  
ATOM   4524  CD1 ILE A 318      -3.046   0.852  -9.182  1.00 53.69           C  
ANISOU 4524  CD1 ILE A 318     7301   6580   6520   -117  -1684    152       C  
ATOM   4525  H   ILE A 318      -5.065   3.934  -7.747  1.00 59.23           H  
ATOM   4526  HA  ILE A 318      -4.932   2.194  -5.818  1.00 61.12           H  
ATOM   4527  HB  ILE A 318      -2.917   3.052  -7.600  1.00 63.51           H  
ATOM   4528 HG12 ILE A 318      -4.323   0.598  -7.619  1.00 64.76           H  
ATOM   4529 HG13 ILE A 318      -4.716   1.824  -8.545  1.00 64.76           H  
ATOM   4530 HG21 ILE A 318      -1.598   1.240  -6.907  1.00 65.81           H  
ATOM   4531 HG22 ILE A 318      -1.837   2.238  -5.694  1.00 65.81           H  
ATOM   4532 HG23 ILE A 318      -2.672   0.890  -5.790  1.00 65.81           H  
ATOM   4533 HD11 ILE A 318      -3.536   0.252  -9.767  1.00 64.43           H  
ATOM   4534 HD12 ILE A 318      -2.706   1.605  -9.690  1.00 64.43           H  
ATOM   4535 HD13 ILE A 318      -2.312   0.377  -8.762  1.00 64.43           H  
ATOM   4536  N   MET A 319      -3.199   4.841  -5.270  1.00 45.85           N  
ANISOU 4536  N   MET A 319     5855   5970   5597   -117  -1260    332       N  
ATOM   4537  CA  MET A 319      -2.572   5.612  -4.202  1.00 44.78           C  
ANISOU 4537  CA  MET A 319     5692   5887   5437    -78  -1157    370       C  
ATOM   4538  C   MET A 319      -3.557   5.894  -3.074  1.00 51.16           C  
ANISOU 4538  C   MET A 319     6369   6775   6293   -153  -1090    387       C  
ATOM   4539  O   MET A 319      -3.213   5.763  -1.893  1.00 57.09           O  
ANISOU 4539  O   MET A 319     7130   7541   7019   -174  -1009    428       O  
ATOM   4540  CB  MET A 319      -2.005   6.918  -4.762  1.00 43.90           C  
ANISOU 4540  CB  MET A 319     5567   5811   5302     51  -1154    356       C  
ATOM   4541  CG  MET A 319      -0.768   6.732  -5.635  1.00 44.81           C  
ANISOU 4541  CG  MET A 319     5813   5849   5364    150  -1177    371       C  
ATOM   4542  SD  MET A 319       0.065   8.275  -6.060  1.00 46.24           S  
ANISOU 4542  SD  MET A 319     5961   6061   5548    304  -1148    390       S  
ATOM   4543  CE  MET A 319      -1.059   8.965  -7.268  1.00 47.43           C  
ANISOU 4543  CE  MET A 319     6032   6275   5716    341  -1218    342       C  
ATOM   4544  H   MET A 319      -3.157   5.204  -6.048  1.00 55.02           H  
ATOM   4545  HA  MET A 319      -1.830   5.100  -3.844  1.00 53.74           H  
ATOM   4546  HB2 MET A 319      -2.687   7.347  -5.303  1.00 52.68           H  
ATOM   4547  HB3 MET A 319      -1.761   7.495  -4.022  1.00 52.68           H  
ATOM   4548  HG2 MET A 319      -0.133   6.172  -5.161  1.00 53.77           H  
ATOM   4549  HG3 MET A 319      -1.032   6.300  -6.463  1.00 53.77           H  
ATOM   4550  HE1 MET A 319      -0.707   9.816  -7.575  1.00 56.92           H  
ATOM   4551  HE2 MET A 319      -1.137   8.350  -8.013  1.00 56.92           H  
ATOM   4552  HE3 MET A 319      -1.926   9.096  -6.853  1.00 56.92           H  
ATOM   4553  N   ARG A 320      -4.789   6.278  -3.415  1.00 56.31           N  
ANISOU 4553  N   ARG A 320     6902   7481   7014   -186  -1122    360       N  
ATOM   4554  CA  ARG A 320      -5.791   6.529  -2.385  1.00 56.15           C  
ANISOU 4554  CA  ARG A 320     6751   7537   7048   -248  -1045    386       C  
ATOM   4555  C   ARG A 320      -6.026   5.287  -1.535  1.00 58.21           C  
ANISOU 4555  C   ARG A 320     7025   7759   7333   -356  -1000    446       C  
ATOM   4556  O   ARG A 320      -6.115   5.375  -0.305  1.00 49.40           O  
ANISOU 4556  O   ARG A 320     5875   6696   6199   -370   -893    493       O  
ATOM   4557  CB  ARG A 320      -7.100   6.992  -3.023  1.00 47.43           C  
ANISOU 4557  CB  ARG A 320     5510   6478   6035   -274  -1098    356       C  
ATOM   4558  CG  ARG A 320      -7.058   8.408  -3.587  1.00 46.75           C  
ANISOU 4558  CG  ARG A 320     5372   6453   5936   -168  -1112    313       C  
ATOM   4559  CD  ARG A 320      -8.449   8.904  -3.972  1.00 48.63           C  
ANISOU 4559  CD  ARG A 320     5455   6747   6274   -199  -1147    296       C  
ATOM   4560  NE  ARG A 320      -9.335   8.977  -2.813  1.00 48.41           N  
ANISOU 4560  NE  ARG A 320     5305   6780   6308   -261  -1044    338       N  
ATOM   4561  CZ  ARG A 320      -9.378   9.994  -1.956  1.00 50.00           C  
ANISOU 4561  CZ  ARG A 320     5444   7063   6491   -205   -940    341       C  
ATOM   4562  NH1 ARG A 320      -8.586  11.047  -2.112  1.00 48.52           N  
ANISOU 4562  NH1 ARG A 320     5292   6898   6247    -95   -937    303       N  
ATOM   4563  NH2 ARG A 320     -10.217   9.955  -0.931  1.00 54.74           N  
ANISOU 4563  NH2 ARG A 320     5944   7718   7136   -251   -838    385       N  
ATOM   4564  H   ARG A 320      -5.063   6.399  -4.221  1.00 67.57           H  
ATOM   4565  HA  ARG A 320      -5.475   7.236  -1.801  1.00 67.38           H  
ATOM   4566  HB2 ARG A 320      -7.320   6.391  -3.751  1.00 56.92           H  
ATOM   4567  HB3 ARG A 320      -7.800   6.963  -2.352  1.00 56.92           H  
ATOM   4568  HG2 ARG A 320      -6.697   9.009  -2.916  1.00 56.10           H  
ATOM   4569  HG3 ARG A 320      -6.502   8.419  -4.381  1.00 56.10           H  
ATOM   4570  HD2 ARG A 320      -8.377   9.792  -4.355  1.00 58.35           H  
ATOM   4571  HD3 ARG A 320      -8.840   8.292  -4.614  1.00 58.35           H  
ATOM   4572  HE  ARG A 320      -9.868   8.316  -2.675  1.00 58.09           H  
ATOM   4573 HH11 ARG A 320      -8.037  11.078  -2.774  1.00 58.23           H  
ATOM   4574 HH12 ARG A 320      -8.622  11.699  -1.553  1.00 58.23           H  
ATOM   4575 HH21 ARG A 320     -10.734   9.276  -0.824  1.00 65.69           H  
ATOM   4576 HH22 ARG A 320     -10.249  10.612  -0.377  1.00 65.69           H  
ATOM   4577  N   ASN A 321      -6.121   4.117  -2.175  1.00 62.17           N  
ANISOU 4577  N   ASN A 321     7580   8167   7876   -424  -1082    446       N  
ATOM   4578  CA  ASN A 321      -6.406   2.888  -1.441  1.00 66.56           C  
ANISOU 4578  CA  ASN A 321     8134   8672   8483   -532  -1046    512       C  
ATOM   4579  C   ASN A 321      -5.271   2.531  -0.488  1.00 63.30           C  
ANISOU 4579  C   ASN A 321     7830   8243   7977   -509   -961    564       C  
ATOM   4580  O   ASN A 321      -5.519   2.096   0.643  1.00 65.55           O  
ANISOU 4580  O   ASN A 321     8081   8551   8272   -562   -867    638       O  
ATOM   4581  CB  ASN A 321      -6.660   1.738  -2.418  1.00 66.88           C  
ANISOU 4581  CB  ASN A 321     8219   8595   8596   -601  -1175    487       C  
ATOM   4582  CG  ASN A 321      -7.916   1.942  -3.251  1.00 71.36           C  
ANISOU 4582  CG  ASN A 321     8668   9169   9274   -640  -1276    443       C  
ATOM   4583  OD1 ASN A 321      -8.877   2.575  -2.807  1.00 71.55           O  
ANISOU 4583  OD1 ASN A 321     8542   9275   9368   -664  -1224    468       O  
ATOM   4584  ND2 ASN A 321      -7.916   1.398  -4.467  1.00 72.69           N  
ANISOU 4584  ND2 ASN A 321     8910   9250   9460   -641  -1426    375       N  
ATOM   4585  H   ASN A 321      -6.025   4.013  -3.023  1.00 74.61           H  
ATOM   4586  HA  ASN A 321      -7.210   3.015  -0.914  1.00 79.87           H  
ATOM   4587  HB2 ASN A 321      -5.907   1.667  -3.025  1.00 80.25           H  
ATOM   4588  HB3 ASN A 321      -6.763   0.914  -1.917  1.00 80.25           H  
ATOM   4589 HD21 ASN A 321      -8.602   1.485  -4.977  1.00 87.23           H  
ATOM   4590 HD22 ASN A 321      -7.228   0.960  -4.742  1.00 87.23           H  
ATOM   4591  N   ILE A 322      -4.022   2.698  -0.926  1.00 52.77           N  
ANISOU 4591  N   ILE A 322     6624   6870   6557   -426   -992    534       N  
ATOM   4592  CA  ILE A 322      -2.884   2.404  -0.058  1.00 52.86           C  
ANISOU 4592  CA  ILE A 322     6735   6859   6490   -400   -926    583       C  
ATOM   4593  C   ILE A 322      -2.971   3.231   1.218  1.00 52.02           C  
ANISOU 4593  C   ILE A 322     6571   6857   6338   -368   -822    611       C  
ATOM   4594  O   ILE A 322      -2.852   2.706   2.331  1.00 52.79           O  
ANISOU 4594  O   ILE A 322     6688   6965   6404   -402   -745    677       O  
ATOM   4595  CB  ILE A 322      -1.559   2.661  -0.800  1.00 52.06           C  
ANISOU 4595  CB  ILE A 322     6755   6701   6325   -301   -973    552       C  
ATOM   4596  CG1 ILE A 322      -1.446   1.785  -2.054  1.00 52.34           C  
ANISOU 4596  CG1 ILE A 322     6871   6633   6383   -314  -1070    520       C  
ATOM   4597  CG2 ILE A 322      -0.368   2.422   0.124  1.00 47.10           C  
ANISOU 4597  CG2 ILE A 322     6216   6046   5632   -273   -916    606       C  
ATOM   4598  CD1 ILE A 322      -1.389   0.300  -1.790  1.00 55.34           C  
ANISOU 4598  CD1 ILE A 322     7312   6918   6795   -406  -1078    562       C  
ATOM   4599  H   ILE A 322      -3.810   2.976  -1.712  1.00 63.33           H  
ATOM   4600  HA  ILE A 322      -2.911   1.467   0.191  1.00 63.43           H  
ATOM   4601  HB  ILE A 322      -1.544   3.590  -1.078  1.00 62.47           H  
ATOM   4602 HG12 ILE A 322      -2.217   1.953  -2.617  1.00 62.81           H  
ATOM   4603 HG13 ILE A 322      -0.636   2.029  -2.529  1.00 62.81           H  
ATOM   4604 HG21 ILE A 322       0.451   2.591  -0.367  1.00 56.52           H  
ATOM   4605 HG22 ILE A 322      -0.430   3.026   0.881  1.00 56.52           H  
ATOM   4606 HG23 ILE A 322      -0.387   1.502   0.432  1.00 56.52           H  
ATOM   4607 HD11 ILE A 322      -1.318  -0.168  -2.636  1.00 66.40           H  
ATOM   4608 HD12 ILE A 322      -0.613   0.107  -1.239  1.00 66.40           H  
ATOM   4609 HD13 ILE A 322      -2.198   0.030  -1.328  1.00 66.40           H  
ATOM   4610  N   GLU A 323      -3.178   4.541   1.072  1.00 46.68           N  
ANISOU 4610  N   GLU A 323     5827   6258   5651   -294   -818    560       N  
ATOM   4611  CA  GLU A 323      -3.262   5.409   2.241  1.00 46.70           C  
ANISOU 4611  CA  GLU A 323     5784   6355   5603   -247   -730    568       C  
ATOM   4612  C   GLU A 323      -4.419   5.001   3.142  1.00 47.69           C  
ANISOU 4612  C   GLU A 323     5819   6540   5759   -320   -640    625       C  
ATOM   4613  O   GLU A 323      -4.267   4.937   4.367  1.00 52.55           O  
ANISOU 4613  O   GLU A 323     6459   7202   6306   -306   -551    671       O  
ATOM   4614  CB  GLU A 323      -3.407   6.865   1.798  1.00 45.61           C  
ANISOU 4614  CB  GLU A 323     5578   6277   5477   -160   -752    499       C  
ATOM   4615  CG  GLU A 323      -2.265   7.350   0.927  1.00 49.39           C  
ANISOU 4615  CG  GLU A 323     6130   6696   5940    -75   -824    463       C  
ATOM   4616  CD  GLU A 323      -2.502   8.737   0.369  1.00 44.01           C  
ANISOU 4616  CD  GLU A 323     5364   6064   5292      6   -848    408       C  
ATOM   4617  OE1 GLU A 323      -2.792   9.663   1.154  1.00 44.13           O  
ANISOU 4617  OE1 GLU A 323     5314   6152   5300     46   -799    386       O  
ATOM   4618  OE2 GLU A 323      -2.398   8.902  -0.863  1.00 43.64           O  
ANISOU 4618  OE2 GLU A 323     5321   5983   5276     37   -915    387       O  
ATOM   4619  H   GLU A 323      -3.270   4.945   0.318  1.00 56.02           H  
ATOM   4620  HA  GLU A 323      -2.441   5.331   2.752  1.00 56.03           H  
ATOM   4621  HB2 GLU A 323      -4.228   6.957   1.290  1.00 54.74           H  
ATOM   4622  HB3 GLU A 323      -3.441   7.430   2.586  1.00 54.74           H  
ATOM   4623  HG2 GLU A 323      -1.452   7.375   1.456  1.00 59.27           H  
ATOM   4624  HG3 GLU A 323      -2.156   6.741   0.180  1.00 59.27           H  
ATOM   4625  N   LYS A 324      -5.581   4.715   2.552  1.00 53.41           N  
ANISOU 4625  N   LYS A 324     6438   7264   6591   -394   -663    629       N  
ATOM   4626  CA  LYS A 324      -6.734   4.285   3.338  1.00 55.27           C  
ANISOU 4626  CA  LYS A 324     6565   7546   6888   -466   -571    703       C  
ATOM   4627  C   LYS A 324      -6.418   3.022   4.130  1.00 58.79           C  
ANISOU 4627  C   LYS A 324     7078   7944   7317   -529   -516    797       C  
ATOM   4628  O   LYS A 324      -6.732   2.925   5.321  1.00 60.41           O  
ANISOU 4628  O   LYS A 324     7256   8213   7485   -526   -393    873       O  
ATOM   4629  CB  LYS A 324      -7.933   4.047   2.420  1.00 55.97           C  
ANISOU 4629  CB  LYS A 324     6530   7611   7127   -545   -638    696       C  
ATOM   4630  CG  LYS A 324      -8.558   5.309   1.849  1.00 57.67           C  
ANISOU 4630  CG  LYS A 324     6642   7894   7375   -490   -665    628       C  
ATOM   4631  CD  LYS A 324      -9.654   4.970   0.847  1.00 62.07           C  
ANISOU 4631  CD  LYS A 324     7090   8412   8083   -570   -761    618       C  
ATOM   4632  CE  LYS A 324     -10.464   6.193   0.455  1.00 62.97           C  
ANISOU 4632  CE  LYS A 324     7076   8605   8246   -523   -769    573       C  
ATOM   4633  NZ  LYS A 324     -11.559   5.846  -0.492  1.00 66.04           N  
ANISOU 4633  NZ  LYS A 324     7352   8951   8788   -602   -877    566       N  
ATOM   4634  H   LYS A 324      -5.725   4.761   1.706  1.00 64.09           H  
ATOM   4635  HA  LYS A 324      -6.969   4.984   3.967  1.00 66.32           H  
ATOM   4636  HB2 LYS A 324      -7.647   3.498   1.673  1.00 67.17           H  
ATOM   4637  HB3 LYS A 324      -8.620   3.581   2.922  1.00 67.17           H  
ATOM   4638  HG2 LYS A 324      -8.951   5.827   2.568  1.00 69.20           H  
ATOM   4639  HG3 LYS A 324      -7.877   5.828   1.393  1.00 69.20           H  
ATOM   4640  HD2 LYS A 324      -9.251   4.604   0.045  1.00 74.49           H  
ATOM   4641  HD3 LYS A 324     -10.258   4.321   1.243  1.00 74.49           H  
ATOM   4642  HE2 LYS A 324     -10.862   6.581   1.250  1.00 75.56           H  
ATOM   4643  HE3 LYS A 324      -9.882   6.837   0.023  1.00 75.56           H  
ATOM   4644  HZ1 LYS A 324     -12.018   6.577  -0.707  1.00 79.24           H  
ATOM   4645  HZ2 LYS A 324     -11.218   5.491  -1.234  1.00 79.24           H  
ATOM   4646  HZ3 LYS A 324     -12.111   5.257  -0.117  1.00 79.24           H  
ATOM   4647  N   MET A 325      -5.795   2.039   3.478  1.00 65.46           N  
ANISOU 4647  N   MET A 325     8013   8675   8185   -576   -602    798       N  
ATOM   4648  CA  MET A 325      -5.518   0.767   4.135  1.00 71.15           C  
ANISOU 4648  CA  MET A 325     8789   9334   8910   -643   -558    892       C  
ATOM   4649  C   MET A 325      -4.505   0.933   5.261  1.00 71.16           C  
ANISOU 4649  C   MET A 325     8895   9377   8766   -572   -479    927       C  
ATOM   4650  O   MET A 325      -4.691   0.396   6.360  1.00 72.32           O  
ANISOU 4650  O   MET A 325     9037   9554   8888   -596   -376   1025       O  
ATOM   4651  CB  MET A 325      -5.026  -0.248   3.105  1.00 74.36           C  
ANISOU 4651  CB  MET A 325     9278   9602   9372   -697   -677    868       C  
ATOM   4652  CG  MET A 325      -6.136  -1.102   2.503  1.00 80.93           C  
ANISOU 4652  CG  MET A 325    10013  10363  10373   -810   -738    886       C  
ATOM   4653  SD  MET A 325      -5.822  -1.592   0.793  1.00 89.88           S  
ANISOU 4653  SD  MET A 325    11231  11365  11555   -821   -927    779       S  
ATOM   4654  CE  MET A 325      -4.079  -2.006   0.841  1.00 84.64           C  
ANISOU 4654  CE  MET A 325    10768  10634  10758   -754   -927    777       C  
ATOM   4655  H   MET A 325      -5.526   2.085   2.663  1.00 78.56           H  
ATOM   4656  HA  MET A 325      -6.345   0.426   4.511  1.00 85.38           H  
ATOM   4657  HB2 MET A 325      -4.592   0.229   2.380  1.00 89.23           H  
ATOM   4658  HB3 MET A 325      -4.392  -0.844   3.532  1.00 89.23           H  
ATOM   4659  HG2 MET A 325      -6.231  -1.910   3.031  1.00 97.11           H  
ATOM   4660  HG3 MET A 325      -6.964  -0.598   2.520  1.00 97.11           H  
ATOM   4661  HE1 MET A 325      -3.797  -2.289  -0.043  1.00101.57           H  
ATOM   4662  HE2 MET A 325      -3.576  -1.223   1.114  1.00101.57           H  
ATOM   4663  HE3 MET A 325      -3.943  -2.726   1.477  1.00101.57           H  
ATOM   4664  N   LEU A 326      -3.420   1.672   5.010  1.00 62.83           N  
ANISOU 4664  N   LEU A 326     7933   8320   7620   -480   -530    855       N  
ATOM   4665  CA  LEU A 326      -2.435   1.896   6.063  1.00 60.67           C  
ANISOU 4665  CA  LEU A 326     7756   8077   7219   -408   -482    879       C  
ATOM   4666  C   LEU A 326      -3.051   2.602   7.261  1.00 59.41           C  
ANISOU 4666  C   LEU A 326     7540   8045   6990   -359   -371    901       C  
ATOM   4667  O   LEU A 326      -2.585   2.425   8.392  1.00 62.29           O  
ANISOU 4667  O   LEU A 326     7975   8442   7249   -322   -308    953       O  
ATOM   4668  CB  LEU A 326      -1.256   2.705   5.524  1.00 62.36           C  
ANISOU 4668  CB  LEU A 326     8049   8261   7385   -316   -564    799       C  
ATOM   4669  CG  LEU A 326      -0.261   1.949   4.643  1.00 61.31           C  
ANISOU 4669  CG  LEU A 326     8016   8003   7278   -330   -647    799       C  
ATOM   4670  CD1 LEU A 326       0.737   2.917   4.041  1.00 60.51           C  
ANISOU 4670  CD1 LEU A 326     7957   7879   7154   -229   -712    733       C  
ATOM   4671  CD2 LEU A 326       0.465   0.869   5.433  1.00 62.45           C  
ANISOU 4671  CD2 LEU A 326     8255   8092   7380   -362   -616    884       C  
ATOM   4672  H   LEU A 326      -3.237   2.045   4.257  1.00 75.39           H  
ATOM   4673  HA  LEU A 326      -2.096   1.038   6.364  1.00 72.80           H  
ATOM   4674  HB2 LEU A 326      -1.607   3.440   4.997  1.00 74.84           H  
ATOM   4675  HB3 LEU A 326      -0.760   3.059   6.279  1.00 74.84           H  
ATOM   4676  HG  LEU A 326      -0.741   1.521   3.918  1.00 73.58           H  
ATOM   4677 HD11 LEU A 326       1.360   2.423   3.485  1.00 72.61           H  
ATOM   4678 HD12 LEU A 326       0.259   3.569   3.503  1.00 72.61           H  
ATOM   4679 HD13 LEU A 326       1.214   3.365   4.757  1.00 72.61           H  
ATOM   4680 HD21 LEU A 326       1.086   0.412   4.845  1.00 74.94           H  
ATOM   4681 HD22 LEU A 326       0.947   1.285   6.166  1.00 74.94           H  
ATOM   4682 HD23 LEU A 326      -0.187   0.241   5.780  1.00 74.94           H  
ATOM   4683  N   GLY A 327      -4.091   3.407   7.039  1.00 57.76           N  
ANISOU 4683  N   GLY A 327     7210   7908   6830   -349   -346    862       N  
ATOM   4684  CA  GLY A 327      -4.780   4.029   8.157  1.00 59.44           C  
ANISOU 4684  CA  GLY A 327     7367   8240   6978   -295   -226    886       C  
ATOM   4685  C   GLY A 327      -5.489   3.015   9.034  1.00 61.07           C  
ANISOU 4685  C   GLY A 327     7536   8469   7198   -358   -105   1019       C  
ATOM   4686  O   GLY A 327      -5.471   3.123  10.263  1.00 61.40           O  
ANISOU 4686  O   GLY A 327     7616   8590   7123   -295      2   1071       O  
ATOM   4687  H   GLY A 327      -4.408   3.603   6.264  1.00 69.32           H  
ATOM   4688  HA2 GLY A 327      -4.141   4.513   8.702  1.00 71.33           H  
ATOM   4689  HA3 GLY A 327      -5.438   4.658   7.821  1.00 71.33           H  
ATOM   4690  N   GLU A 328      -6.124   2.015   8.417  1.00 70.07           N  
ANISOU 4690  N   GLU A 328     8603   9535   8484   -475   -122   1080       N  
ATOM   4691  CA  GLU A 328      -6.775   0.955   9.177  1.00 76.65           C  
ANISOU 4691  CA  GLU A 328     9386  10369   9367   -545    -10   1226       C  
ATOM   4692  C   GLU A 328      -5.758  -0.024   9.747  1.00 72.52           C  
ANISOU 4692  C   GLU A 328     8998   9788   8767   -555     -4   1295       C  
ATOM   4693  O   GLU A 328      -5.843  -0.396  10.923  1.00 76.24           O  
ANISOU 4693  O   GLU A 328     9490  10316   9163   -531    120   1404       O  
ATOM   4694  CB  GLU A 328      -7.778   0.213   8.292  1.00 79.59           C  
ANISOU 4694  CB  GLU A 328     9627  10662   9953   -671    -55   1263       C  
ATOM   4695  CG  GLU A 328      -8.924   1.074   7.788  1.00 81.99           C  
ANISOU 4695  CG  GLU A 328     9776  11021  10355   -671    -56   1218       C  
ATOM   4696  CD  GLU A 328      -9.788   0.357   6.768  1.00 86.04           C  
ANISOU 4696  CD  GLU A 328    10172  11436  11085   -795   -147   1233       C  
ATOM   4697  OE1 GLU A 328      -9.505  -0.824   6.471  1.00 87.01           O  
ANISOU 4697  OE1 GLU A 328    10335  11442  11281   -881   -208   1274       O  
ATOM   4698  OE2 GLU A 328     -10.749   0.976   6.261  1.00 87.27           O  
ANISOU 4698  OE2 GLU A 328    10194  11624  11343   -805   -168   1200       O  
ATOM   4699  H   GLU A 328      -6.189   1.931   7.564  1.00 84.08           H  
ATOM   4700  HA  GLU A 328      -7.262   1.349   9.918  1.00 91.98           H  
ATOM   4701  HB2 GLU A 328      -7.309  -0.136   7.517  1.00 95.51           H  
ATOM   4702  HB3 GLU A 328      -8.160  -0.519   8.800  1.00 95.51           H  
ATOM   4703  HG2 GLU A 328      -9.488   1.320   8.538  1.00 98.38           H  
ATOM   4704  HG3 GLU A 328      -8.562   1.870   7.369  1.00 98.38           H  
ATOM   4705  N   ALA A 329      -4.791  -0.445   8.930  1.00 66.50           N  
ANISOU 4705  N   ALA A 329     8331   8917   8020   -583   -132   1240       N  
ATOM   4706  CA  ALA A 329      -3.812  -1.429   9.377  1.00 63.38           C  
ANISOU 4706  CA  ALA A 329     8057   8452   7572   -600   -135   1308       C  
ATOM   4707  C   ALA A 329      -3.051  -0.931  10.599  1.00 62.74           C  
ANISOU 4707  C   ALA A 329     8079   8456   7301   -490    -72   1323       C  
ATOM   4708  O   ALA A 329      -2.891  -1.659  11.585  1.00 66.27           O  
ANISOU 4708  O   ALA A 329     8573   8917   7689   -492     12   1437       O  
ATOM   4709  CB  ALA A 329      -2.846  -1.757   8.239  1.00 60.95           C  
ANISOU 4709  CB  ALA A 329     7837   8019   7302   -621   -279   1231       C  
ATOM   4710  H   ALA A 329      -4.683  -0.178   8.120  1.00 79.81           H  
ATOM   4711  HA  ALA A 329      -4.273  -2.246   9.624  1.00 76.05           H  
ATOM   4712  HB1 ALA A 329      -2.201  -2.412   8.551  1.00 73.14           H  
ATOM   4713  HB2 ALA A 329      -3.349  -2.118   7.492  1.00 73.14           H  
ATOM   4714  HB3 ALA A 329      -2.389  -0.945   7.969  1.00 73.14           H  
ATOM   4715  N   LEU A 330      -2.569   0.310  10.549  1.00 58.57           N  
ANISOU 4715  N   LEU A 330     7590   7982   6682   -389   -119   1210       N  
ATOM   4716  CA  LEU A 330      -1.827   0.880  11.665  1.00 58.76           C  
ANISOU 4716  CA  LEU A 330     7718   8076   6532   -276    -91   1201       C  
ATOM   4717  C   LEU A 330      -2.731   1.384  12.780  1.00 62.30           C  
ANISOU 4717  C   LEU A 330     8120   8664   6889   -210     47   1240       C  
ATOM   4718  O   LEU A 330      -2.226   1.749  13.847  1.00 61.26           O  
ANISOU 4718  O   LEU A 330     8084   8598   6593   -109     79   1241       O  
ATOM   4719  CB  LEU A 330      -0.938   2.022  11.168  1.00 54.74           C  
ANISOU 4719  CB  LEU A 330     7260   7553   5986   -193   -208   1064       C  
ATOM   4720  CG  LEU A 330       0.037   1.644  10.051  1.00 56.16           C  
ANISOU 4720  CG  LEU A 330     7491   7601   6245   -231   -332   1029       C  
ATOM   4721  CD1 LEU A 330       0.797   2.868   9.570  1.00 54.00           C  
ANISOU 4721  CD1 LEU A 330     7240   7318   5958   -142   -428    914       C  
ATOM   4722  CD2 LEU A 330       1.002   0.560  10.509  1.00 54.01           C  
ANISOU 4722  CD2 LEU A 330     7331   7255   5935   -255   -342   1113       C  
ATOM   4723  H   LEU A 330      -2.659   0.841   9.879  1.00 70.28           H  
ATOM   4724  HA  LEU A 330      -1.250   0.195  12.038  1.00 70.51           H  
ATOM   4725  HB2 LEU A 330      -1.507   2.732  10.832  1.00 65.69           H  
ATOM   4726  HB3 LEU A 330      -0.414   2.352  11.914  1.00 65.69           H  
ATOM   4727  HG  LEU A 330      -0.468   1.294   9.300  1.00 67.39           H  
ATOM   4728 HD11 LEU A 330       1.407   2.603   8.864  1.00 64.80           H  
ATOM   4729 HD12 LEU A 330       0.164   3.521   9.233  1.00 64.80           H  
ATOM   4730 HD13 LEU A 330       1.295   3.242  10.314  1.00 64.80           H  
ATOM   4731 HD21 LEU A 330       1.604   0.345   9.780  1.00 64.81           H  
ATOM   4732 HD22 LEU A 330       1.507   0.889  11.269  1.00 64.81           H  
ATOM   4733 HD23 LEU A 330       0.495  -0.226  10.764  1.00 64.81           H  
ATOM   4734  N   GLY A 331      -4.044   1.410  12.564  1.00 67.63           N  
ANISOU 4734  N   GLY A 331     8651   9380   7664   -257    128   1275       N  
ATOM   4735  CA  GLY A 331      -4.956   1.894  13.577  1.00 69.56           C  
ANISOU 4735  CA  GLY A 331     8843   9757   7831   -185    278   1323       C  
ATOM   4736  C   GLY A 331      -4.815   3.361  13.902  1.00 70.41           C  
ANISOU 4736  C   GLY A 331     8981   9952   7818    -51    263   1196       C  
ATOM   4737  O   GLY A 331      -5.274   3.796  14.961  1.00 72.83           O  
ANISOU 4737  O   GLY A 331     9297  10371   8002     46    384   1223       O  
ATOM   4738  H   GLY A 331      -4.425   1.152  11.837  1.00 81.15           H  
ATOM   4739  HA2 GLY A 331      -5.867   1.738  13.282  1.00 83.48           H  
ATOM   4740  HA3 GLY A 331      -4.815   1.391  14.395  1.00 83.48           H  
ATOM   4741  N   ASN A 332      -4.191   4.141  13.026  1.00 70.12           N  
ANISOU 4741  N   ASN A 332     8961   9865   7816    -35    122   1060       N  
ATOM   4742  CA  ASN A 332      -4.011   5.562  13.283  1.00 71.59           C  
ANISOU 4742  CA  ASN A 332     9170  10117   7915     89     91    934       C  
ATOM   4743  C   ASN A 332      -3.567   6.276  12.012  1.00 70.34           C  
ANISOU 4743  C   ASN A 332     8979   9884   7863     75    -54    817       C  
ATOM   4744  O   ASN A 332      -2.477   5.997  11.498  1.00 70.13           O  
ANISOU 4744  O   ASN A 332     9029   9762   7854     55   -166    794       O  
ATOM   4745  CB  ASN A 332      -2.985   5.778  14.396  1.00 70.40           C  
ANISOU 4745  CB  ASN A 332     9179   9991   7576    200     70    911       C  
ATOM   4746  CG  ASN A 332      -2.839   7.236  14.776  1.00 70.83           C  
ANISOU 4746  CG  ASN A 332     9261  10106   7545    335     31    776       C  
ATOM   4747  OD1 ASN A 332      -3.648   8.077  14.383  1.00 71.24           O  
ANISOU 4747  OD1 ASN A 332     9205  10201   7661    355     58    716       O  
ATOM   4748  ND2 ASN A 332      -1.808   7.543  15.553  1.00 72.53           N  
ANISOU 4748  ND2 ASN A 332     9618  10318   7623    431    -40    725       N  
ATOM   4749  H   ASN A 332      -3.863   3.872  12.277  1.00 84.14           H  
ATOM   4750  HA  ASN A 332      -4.855   5.945  13.569  1.00 85.91           H  
ATOM   4751  HB2 ASN A 332      -3.266   5.288  15.185  1.00 84.48           H  
ATOM   4752  HB3 ASN A 332      -2.120   5.457  14.096  1.00 84.48           H  
ATOM   4753 HD21 ASN A 332      -1.681   8.358  15.797  1.00 87.04           H  
ATOM   4754 HD22 ASN A 332      -1.266   6.927  15.812  1.00 87.04           H  
ATOM   4755  N   PRO A 333      -4.374   7.194  11.472  1.00 68.28           N  
ANISOU 4755  N   PRO A 333     8602   9664   7678     91    -48    751       N  
ATOM   4756  CA  PRO A 333      -3.935   7.944  10.282  1.00 69.49           C  
ANISOU 4756  CA  PRO A 333     8727   9754   7924     94   -179    648       C  
ATOM   4757  C   PRO A 333      -2.607   8.659  10.453  1.00 68.55           C  
ANISOU 4757  C   PRO A 333     8717   9594   7736    186   -284    564       C  
ATOM   4758  O   PRO A 333      -1.880   8.845   9.469  1.00 65.34           O  
ANISOU 4758  O   PRO A 333     8317   9101   7407    174   -394    522       O  
ATOM   4759  CB  PRO A 333      -5.081   8.941  10.064  1.00 69.16           C  
ANISOU 4759  CB  PRO A 333     8549   9788   7941    126   -130    600       C  
ATOM   4760  CG  PRO A 333      -6.269   8.276  10.636  1.00 70.11           C  
ANISOU 4760  CG  PRO A 333     8591   9974   8073     78     14    706       C  
ATOM   4761  CD  PRO A 333      -5.774   7.496  11.820  1.00 69.93           C  
ANISOU 4761  CD  PRO A 333     8687   9970   7912    101     84    785       C  
ATOM   4762  HA  PRO A 333      -3.880   7.351   9.516  1.00 83.39           H  
ATOM   4763  HB2 PRO A 333      -4.890   9.768  10.533  1.00 83.00           H  
ATOM   4764  HB3 PRO A 333      -5.200   9.103   9.115  1.00 83.00           H  
ATOM   4765  HG2 PRO A 333      -6.913   8.946  10.914  1.00 84.13           H  
ATOM   4766  HG3 PRO A 333      -6.658   7.682   9.975  1.00 84.13           H  
ATOM   4767  HD2 PRO A 333      -5.813   8.039  12.623  1.00 83.91           H  
ATOM   4768  HD3 PRO A 333      -6.282   6.676  11.920  1.00 83.91           H  
ATOM   4769  N   GLN A 334      -2.268   9.078  11.673  1.00 73.03           N  
ANISOU 4769  N   GLN A 334     9368  10217   8164    285   -257    540       N  
ATOM   4770  CA  GLN A 334      -1.043   9.839  11.889  1.00 76.84           C  
ANISOU 4770  CA  GLN A 334     9942  10651   8602    375   -375    453       C  
ATOM   4771  C   GLN A 334       0.213   9.021  11.605  1.00 75.15           C  
ANISOU 4771  C   GLN A 334     9822  10328   8403    331   -466    497       C  
ATOM   4772  O   GLN A 334       1.272   9.607  11.356  1.00 76.39           O  
ANISOU 4772  O   GLN A 334    10019  10412   8593    382   -583    437       O  
ATOM   4773  CB  GLN A 334      -1.002  10.366  13.326  1.00 81.74           C  
ANISOU 4773  CB  GLN A 334    10648  11354   9057    495   -338    413       C  
ATOM   4774  CG  GLN A 334      -2.220  11.193  13.740  1.00 86.61           C  
ANISOU 4774  CG  GLN A 334    11185  12084   9641    560   -232    370       C  
ATOM   4775  CD  GLN A 334      -2.223  12.594  13.148  1.00 89.15           C  
ANISOU 4775  CD  GLN A 334    11433  12387  10053    621   -313    244       C  
ATOM   4776  OE1 GLN A 334      -2.000  13.577  13.857  1.00 89.17           O  
ANISOU 4776  OE1 GLN A 334    11484  12416   9980    741   -348    145       O  
ATOM   4777  NE2 GLN A 334      -2.489  12.692  11.849  1.00 88.51           N  
ANISOU 4777  NE2 GLN A 334    11238  12258  10133    544   -347    247       N  
ATOM   4778  H   GLN A 334      -2.728   8.936  12.385  1.00 87.64           H  
ATOM   4779  HA  GLN A 334      -1.040  10.603  11.292  1.00 92.21           H  
ATOM   4780  HB2 GLN A 334      -0.941   9.610  13.931  1.00 98.09           H  
ATOM   4781  HB3 GLN A 334      -0.218  10.928  13.427  1.00 98.09           H  
ATOM   4782  HG2 GLN A 334      -3.024  10.741  13.440  1.00103.94           H  
ATOM   4783  HG3 GLN A 334      -2.229  11.277  14.706  1.00103.94           H  
ATOM   4784 HE21 GLN A 334      -2.649  11.984  11.388  1.00106.21           H  
ATOM   4785 HE22 GLN A 334      -2.502  13.464  11.470  1.00106.21           H  
ATOM   4786  N   GLU A 335       0.126   7.691  11.636  1.00 71.94           N  
ANISOU 4786  N   GLU A 335     9443   9900   7990    241   -413    605       N  
ATOM   4787  CA  GLU A 335       1.280   6.838  11.382  1.00 67.82           C  
ANISOU 4787  CA  GLU A 335     9011   9273   7486    201   -487    654       C  
ATOM   4788  C   GLU A 335       1.502   6.547   9.904  1.00 62.79           C  
ANISOU 4788  C   GLU A 335     8326   8539   6993    129   -549    655       C  
ATOM   4789  O   GLU A 335       2.530   5.955   9.557  1.00 64.42           O  
ANISOU 4789  O   GLU A 335     8603   8648   7227    110   -613    688       O  
ATOM   4790  CB  GLU A 335       1.135   5.504  12.123  1.00 71.03           C  
ANISOU 4790  CB  GLU A 335     9475   9692   7821    142   -402    774       C  
ATOM   4791  CG  GLU A 335       1.306   5.586  13.628  1.00 72.53           C  
ANISOU 4791  CG  GLU A 335     9759   9960   7839    229   -357    793       C  
ATOM   4792  CD  GLU A 335       1.544   4.222  14.248  1.00 76.68           C  
ANISOU 4792  CD  GLU A 335    10360  10470   8307    176   -302    924       C  
ATOM   4793  OE1 GLU A 335       2.454   3.507  13.773  1.00 76.14           O  
ANISOU 4793  OE1 GLU A 335    10340  10293   8296    123   -375    961       O  
ATOM   4794  OE2 GLU A 335       0.817   3.859  15.197  1.00 78.73           O  
ANISOU 4794  OE2 GLU A 335    10625  10821   8466    194   -177    999       O  
ATOM   4795  H   GLU A 335      -0.598   7.257  11.803  1.00 86.32           H  
ATOM   4796  HA  GLU A 335       2.075   7.281  11.719  1.00 81.39           H  
ATOM   4797  HB2 GLU A 335       0.250   5.148  11.948  1.00 85.24           H  
ATOM   4798  HB3 GLU A 335       1.805   4.889  11.786  1.00 85.24           H  
ATOM   4799  HG2 GLU A 335       2.069   6.148  13.832  1.00 87.04           H  
ATOM   4800  HG3 GLU A 335       0.501   5.960  14.020  1.00 87.04           H  
ATOM   4801  N   VAL A 336       0.573   6.936   9.030  1.00 56.92           N  
ANISOU 4801  N   VAL A 336     7470   7819   6337     99   -532    622       N  
ATOM   4802  CA  VAL A 336       0.712   6.625   7.609  1.00 54.53           C  
ANISOU 4802  CA  VAL A 336     7136   7433   6150     44   -593    620       C  
ATOM   4803  C   VAL A 336       1.966   7.282   7.046  1.00 50.03           C  
ANISOU 4803  C   VAL A 336     6608   6782   5617    115   -695    575       C  
ATOM   4804  O   VAL A 336       2.758   6.648   6.339  1.00 49.98           O  
ANISOU 4804  O   VAL A 336     6655   6681   5655     92   -742    609       O  
ATOM   4805  CB  VAL A 336      -0.549   7.059   6.840  1.00 56.16           C  
ANISOU 4805  CB  VAL A 336     7214   7690   6436     14   -568    587       C  
ATOM   4806  CG1 VAL A 336      -0.388   6.804   5.348  1.00 55.17           C  
ANISOU 4806  CG1 VAL A 336     7073   7483   6409    -23   -643    575       C  
ATOM   4807  CG2 VAL A 336      -1.769   6.318   7.367  1.00 57.77           C  
ANISOU 4807  CG2 VAL A 336     7359   7955   6636    -63   -466    652       C  
ATOM   4808  H   VAL A 336      -0.138   7.376   9.232  1.00 68.30           H  
ATOM   4809  HA  VAL A 336       0.808   5.665   7.506  1.00 65.44           H  
ATOM   4810  HB  VAL A 336      -0.692   8.009   6.971  1.00 67.40           H  
ATOM   4811 HG11 VAL A 336      -1.195   7.086   4.890  1.00 66.21           H  
ATOM   4812 HG12 VAL A 336       0.372   7.311   5.021  1.00 66.21           H  
ATOM   4813 HG13 VAL A 336      -0.240   5.856   5.204  1.00 66.21           H  
ATOM   4814 HG21 VAL A 336      -2.551   6.605   6.870  1.00 69.33           H  
ATOM   4815 HG22 VAL A 336      -1.634   5.365   7.250  1.00 69.33           H  
ATOM   4816 HG23 VAL A 336      -1.881   6.524   8.308  1.00 69.33           H  
ATOM   4817  N   GLY A 337       2.164   8.560   7.352  1.00 51.30           N  
ANISOU 4817  N   GLY A 337     6743   6976   5773    206   -727    503       N  
ATOM   4818  CA  GLY A 337       3.305   9.294   6.862  1.00 49.45           C  
ANISOU 4818  CA  GLY A 337     6524   6660   5604    277   -822    470       C  
ATOM   4819  C   GLY A 337       4.627   8.659   7.249  1.00 48.98           C  
ANISOU 4819  C   GLY A 337     6573   6513   5525    286   -871    522       C  
ATOM   4820  O   GLY A 337       5.448   8.313   6.394  1.00 48.10           O  
ANISOU 4820  O   GLY A 337     6485   6304   5486    282   -914    560       O  
ATOM   4821  H   GLY A 337       1.640   9.024   7.851  1.00 61.56           H  
ATOM   4822  HA2 GLY A 337       3.262   9.345   5.894  1.00 59.34           H  
ATOM   4823  HA3 GLY A 337       3.284  10.196   7.217  1.00 59.34           H  
ATOM   4824  N   PRO A 338       4.865   8.508   8.553  1.00 46.88           N  
ANISOU 4824  N   PRO A 338     6378   6279   5156    308   -866    527       N  
ATOM   4825  CA  PRO A 338       6.140   7.917   8.995  1.00 49.11           C  
ANISOU 4825  CA  PRO A 338     6762   6476   5422    319   -924    580       C  
ATOM   4826  C   PRO A 338       6.445   6.573   8.355  1.00 46.57           C  
ANISOU 4826  C   PRO A 338     6482   6081   5130    237   -899    671       C  
ATOM   4827  O   PRO A 338       7.597   6.317   7.986  1.00 45.15           O  
ANISOU 4827  O   PRO A 338     6347   5797   5012    253   -959    710       O  
ATOM   4828  CB  PRO A 338       5.954   7.801  10.515  1.00 50.39           C  
ANISOU 4828  CB  PRO A 338     6994   6716   5436    346   -897    577       C  
ATOM   4829  CG  PRO A 338       4.997   8.887  10.857  1.00 50.27           C  
ANISOU 4829  CG  PRO A 338     6914   6803   5385    400   -866    489       C  
ATOM   4830  CD  PRO A 338       4.063   9.008   9.684  1.00 47.71           C  
ANISOU 4830  CD  PRO A 338     6476   6497   5153    347   -814    482       C  
ATOM   4831  HA  PRO A 338       6.871   8.528   8.812  1.00 58.94           H  
ATOM   4832  HB2 PRO A 338       5.583   6.932  10.735  1.00 60.47           H  
ATOM   4833  HB3 PRO A 338       6.804   7.937  10.961  1.00 60.47           H  
ATOM   4834  HG2 PRO A 338       4.507   8.645  11.659  1.00 60.33           H  
ATOM   4835  HG3 PRO A 338       5.483   9.716  10.993  1.00 60.33           H  
ATOM   4836  HD2 PRO A 338       3.281   8.450   9.816  1.00 57.25           H  
ATOM   4837  HD3 PRO A 338       3.819   9.936   9.541  1.00 57.25           H  
ATOM   4838  N   LEU A 339       5.443   5.704   8.204  1.00 46.05           N  
ANISOU 4838  N   LEU A 339     6398   6060   5037    152   -815    708       N  
ATOM   4839  CA  LEU A 339       5.701   4.387   7.632  1.00 51.16           C  
ANISOU 4839  CA  LEU A 339     7092   6629   5719     74   -801    785       C  
ATOM   4840  C   LEU A 339       6.002   4.465   6.141  1.00 50.90           C  
ANISOU 4840  C   LEU A 339     7032   6515   5791     78   -842    770       C  
ATOM   4841  O   LEU A 339       6.782   3.655   5.628  1.00 49.13           O  
ANISOU 4841  O   LEU A 339     6872   6194   5603     62   -861    821       O  
ATOM   4842  CB  LEU A 339       4.511   3.462   7.880  1.00 51.74           C  
ANISOU 4842  CB  LEU A 339     7140   6758   5759    -19   -712    829       C  
ATOM   4843  CG  LEU A 339       4.716   2.029   7.390  1.00 53.62           C  
ANISOU 4843  CG  LEU A 339     7427   6905   6040   -103   -703    904       C  
ATOM   4844  CD1 LEU A 339       4.158   1.044   8.397  1.00 56.64           C  
ANISOU 4844  CD1 LEU A 339     7827   7327   6365   -169   -623    987       C  
ATOM   4845  CD2 LEU A 339       4.063   1.823   6.032  1.00 54.62           C  
ANISOU 4845  CD2 LEU A 339     7498   6999   6258   -151   -717    873       C  
ATOM   4846  H   LEU A 339       4.624   5.850   8.420  1.00 55.26           H  
ATOM   4847  HA  LEU A 339       6.474   4.001   8.071  1.00 61.40           H  
ATOM   4848  HB2 LEU A 339       4.339   3.426   8.834  1.00 62.08           H  
ATOM   4849  HB3 LEU A 339       3.736   3.823   7.421  1.00 62.08           H  
ATOM   4850  HG  LEU A 339       5.666   1.858   7.297  1.00 64.34           H  
ATOM   4851 HD11 LEU A 339       4.298   0.143   8.068  1.00 67.96           H  
ATOM   4852 HD12 LEU A 339       4.617   1.163   9.243  1.00 67.96           H  
ATOM   4853 HD13 LEU A 339       3.209   1.212   8.509  1.00 67.96           H  
ATOM   4854 HD21 LEU A 339       4.209   0.907   5.748  1.00 65.55           H  
ATOM   4855 HD22 LEU A 339       3.112   1.998   6.109  1.00 65.55           H  
ATOM   4856 HD23 LEU A 339       4.462   2.435   5.394  1.00 65.55           H  
ATOM   4857  N   LEU A 340       5.393   5.417   5.428  1.00 51.45           N  
ANISOU 4857  N   LEU A 340     7016   6627   5906    108   -850    704       N  
ATOM   4858  CA  LEU A 340       5.678   5.568   4.004  1.00 48.14           C  
ANISOU 4858  CA  LEU A 340     6579   6142   5569    132   -886    694       C  
ATOM   4859  C   LEU A 340       7.088   6.100   3.779  1.00 51.37           C  
ANISOU 4859  C   LEU A 340     7018   6464   6036    220   -942    713       C  
ATOM   4860  O   LEU A 340       7.783   5.657   2.857  1.00 50.10           O  
ANISOU 4860  O   LEU A 340     6898   6215   5925    239   -955    754       O  
ATOM   4861  CB  LEU A 340       4.651   6.494   3.355  1.00 51.68           C  
ANISOU 4861  CB  LEU A 340     6923   6663   6051    148   -881    627       C  
ATOM   4862  CG  LEU A 340       3.223   5.956   3.229  1.00 54.71           C  
ANISOU 4862  CG  LEU A 340     7256   7112   6421     59   -837    616       C  
ATOM   4863  CD1 LEU A 340       2.300   7.040   2.691  1.00 55.29           C  
ANISOU 4863  CD1 LEU A 340     7217   7258   6534     88   -841    552       C  
ATOM   4864  CD2 LEU A 340       3.169   4.724   2.335  1.00 54.01           C  
ANISOU 4864  CD2 LEU A 340     7217   6948   6356     -5   -850    649       C  
ATOM   4865  H   LEU A 340       4.820   5.977   5.741  1.00 61.74           H  
ATOM   4866  HA  LEU A 340       5.614   4.700   3.576  1.00 57.76           H  
ATOM   4867  HB2 LEU A 340       4.604   7.309   3.878  1.00 62.02           H  
ATOM   4868  HB3 LEU A 340       4.957   6.705   2.459  1.00 62.02           H  
ATOM   4869  HG  LEU A 340       2.903   5.701   4.109  1.00 65.66           H  
ATOM   4870 HD11 LEU A 340       1.401   6.681   2.619  1.00 66.35           H  
ATOM   4871 HD12 LEU A 340       2.308   7.792   3.303  1.00 66.35           H  
ATOM   4872 HD13 LEU A 340       2.617   7.319   1.818  1.00 66.35           H  
ATOM   4873 HD21 LEU A 340       2.252   4.414   2.280  1.00 64.81           H  
ATOM   4874 HD22 LEU A 340       3.492   4.962   1.452  1.00 64.81           H  
ATOM   4875 HD23 LEU A 340       3.731   4.032   2.718  1.00 64.81           H  
ATOM   4876  N   ASN A 341       7.528   7.052   4.605  1.00 53.32           N  
ANISOU 4876  N   ASN A 341     7245   6729   6285    282   -978    685       N  
ATOM   4877  CA  ASN A 341       8.888   7.562   4.475  1.00 50.69           C  
ANISOU 4877  CA  ASN A 341     6924   6299   6036    361  -1042    713       C  
ATOM   4878  C   ASN A 341       9.910   6.482   4.797  1.00 47.12           C  
ANISOU 4878  C   ASN A 341     6568   5758   5576    340  -1052    795       C  
ATOM   4879  O   ASN A 341      10.910   6.334   4.085  1.00 49.58           O  
ANISOU 4879  O   ASN A 341     6899   5967   5974    380  -1071    852       O  
ATOM   4880  CB  ASN A 341       9.087   8.775   5.381  1.00 52.22           C  
ANISOU 4880  CB  ASN A 341     7078   6521   6243    427  -1100    655       C  
ATOM   4881  CG  ASN A 341       8.368  10.003   4.872  1.00 53.45           C  
ANISOU 4881  CG  ASN A 341     7127   6733   6450    470  -1101    584       C  
ATOM   4882  OD1 ASN A 341       8.784  10.620   3.892  1.00 55.70           O  
ANISOU 4882  OD1 ASN A 341     7356   6962   6847    525  -1122    598       O  
ATOM   4883  ND2 ASN A 341       7.283  10.370   5.542  1.00 57.67           N  
ANISOU 4883  ND2 ASN A 341     7631   7377   6906    453  -1069    516       N  
ATOM   4884  H   ASN A 341       7.066   7.412   5.235  1.00 63.99           H  
ATOM   4885  HA  ASN A 341       9.032   7.846   3.558  1.00 60.83           H  
ATOM   4886  HB2 ASN A 341       8.744   8.570   6.265  1.00 62.67           H  
ATOM   4887  HB3 ASN A 341      10.034   8.981   5.431  1.00 62.67           H  
ATOM   4888 HD21 ASN A 341       6.837  11.062   5.293  1.00 69.21           H  
ATOM   4889 HD22 ASN A 341       7.025   9.916   6.225  1.00 69.21           H  
ATOM   4890  N   THR A 342       9.680   5.723   5.873  1.00 46.46           N  
ANISOU 4890  N   THR A 342     6546   5713   5393    283  -1032    811       N  
ATOM   4891  CA  THR A 342      10.549   4.596   6.194  1.00 44.61           C  
ANISOU 4891  CA  THR A 342     6403   5398   5149    254  -1036    895       C  
ATOM   4892  C   THR A 342      10.672   3.639   5.018  1.00 47.65           C  
ANISOU 4892  C   THR A 342     6818   5709   5579    220   -999    945       C  
ATOM   4893  O   THR A 342      11.719   3.007   4.833  1.00 45.49           O  
ANISOU 4893  O   THR A 342     6602   5332   5350    233  -1012   1016       O  
ATOM   4894  CB  THR A 342      10.007   3.850   7.417  1.00 46.68           C  
ANISOU 4894  CB  THR A 342     6718   5730   5287    193   -998    914       C  
ATOM   4895  OG1 THR A 342       9.994   4.727   8.551  1.00 51.60           O  
ANISOU 4895  OG1 THR A 342     7337   6420   5848    247  -1038    863       O  
ATOM   4896  CG2 THR A 342      10.862   2.633   7.741  1.00 44.53           C  
ANISOU 4896  CG2 THR A 342     6537   5374   5009    160  -1000   1008       C  
ATOM   4897  H   THR A 342       9.032   5.841   6.426  1.00 55.75           H  
ATOM   4898  HA  THR A 342      11.435   4.927   6.409  1.00 53.53           H  
ATOM   4899  HB  THR A 342       9.103   3.548   7.235  1.00 56.01           H  
ATOM   4900  HG1 THR A 342       9.504   5.391   8.394  1.00 61.92           H  
ATOM   4901 HG21 THR A 342      10.504   2.174   8.517  1.00 53.44           H  
ATOM   4902 HG22 THR A 342      10.867   2.022   6.987  1.00 53.44           H  
ATOM   4903 HG23 THR A 342      11.772   2.909   7.929  1.00 53.44           H  
ATOM   4904  N   MET A 343       9.618   3.527   4.211  1.00 48.40           N  
ANISOU 4904  N   MET A 343     6876   5851   5664    182   -958    905       N  
ATOM   4905  CA  MET A 343       9.587   2.561   3.122  1.00 45.30           C  
ANISOU 4905  CA  MET A 343     6526   5391   5295    151   -934    933       C  
ATOM   4906  C   MET A 343      10.403   3.012   1.914  1.00 49.83           C  
ANISOU 4906  C   MET A 343     7098   5887   5948    243   -952    947       C  
ATOM   4907  O   MET A 343      11.008   2.170   1.241  1.00 48.41           O  
ANISOU 4907  O   MET A 343     6988   5615   5790    253   -939    996       O  
ATOM   4908  CB  MET A 343       8.135   2.315   2.711  1.00 45.72           C  
ANISOU 4908  CB  MET A 343     6538   5517   5316     81   -905    880       C  
ATOM   4909  CG  MET A 343       7.861   0.924   2.175  1.00 54.74           C  
ANISOU 4909  CG  MET A 343     7741   6598   6458      8   -890    906       C  
ATOM   4910  SD  MET A 343       6.208   0.732   1.465  1.00 55.67           S  
ANISOU 4910  SD  MET A 343     7795   6777   6580    -66   -888    839       S  
ATOM   4911  CE  MET A 343       5.184   1.546   2.687  1.00 56.43           C  
ANISOU 4911  CE  MET A 343     7789   7015   6639    -98   -849    815       C  
ATOM   4912  H   MET A 343       8.905   4.004   4.276  1.00 58.08           H  
ATOM   4913  HA  MET A 343       9.948   1.721   3.444  1.00 54.36           H  
ATOM   4914  HB2 MET A 343       7.567   2.449   3.486  1.00 54.86           H  
ATOM   4915  HB3 MET A 343       7.897   2.950   2.018  1.00 54.86           H  
ATOM   4916  HG2 MET A 343       8.507   0.723   1.480  1.00 65.68           H  
ATOM   4917  HG3 MET A 343       7.949   0.286   2.900  1.00 65.68           H  
ATOM   4918  HE1 MET A 343       4.258   1.501   2.402  1.00 67.72           H  
ATOM   4919  HE2 MET A 343       5.290   1.094   3.539  1.00 67.72           H  
ATOM   4920  HE3 MET A 343       5.462   2.472   2.765  1.00 67.72           H  
ATOM   4921  N   ILE A 344      10.442   4.315   1.623  1.00 46.42           N  
ANISOU 4921  N   ILE A 344     6588   5486   5564    318   -974    912       N  
ATOM   4922  CA  ILE A 344      11.065   4.797   0.393  1.00 49.21           C  
ANISOU 4922  CA  ILE A 344     6926   5777   5995    414   -974    938       C  
ATOM   4923  C   ILE A 344      12.454   5.364   0.671  1.00 46.23           C  
ANISOU 4923  C   ILE A 344     6533   5314   5718    495  -1003   1006       C  
ATOM   4924  O   ILE A 344      13.349   5.269  -0.177  1.00 49.29           O  
ANISOU 4924  O   ILE A 344     6940   5612   6177    570   -984   1076       O  
ATOM   4925  CB  ILE A 344      10.179   5.847  -0.314  1.00 55.27           C  
ANISOU 4925  CB  ILE A 344     7605   6624   6773    449   -975    873       C  
ATOM   4926  CG1 ILE A 344      10.140   7.165   0.461  1.00 59.31           C  
ANISOU 4926  CG1 ILE A 344     8022   7186   7327    482  -1009    836       C  
ATOM   4927  CG2 ILE A 344       8.759   5.328  -0.509  1.00 54.15           C  
ANISOU 4927  CG2 ILE A 344     7461   6562   6552    362   -960    808       C  
ATOM   4928  CD1 ILE A 344      11.046   8.244  -0.125  1.00 58.75           C  
ANISOU 4928  CD1 ILE A 344     7889   7054   7382    596  -1030    876       C  
ATOM   4929  H   ILE A 344      10.115   4.936   2.121  1.00 55.70           H  
ATOM   4930  HA  ILE A 344      11.171   4.048  -0.213  1.00 59.05           H  
ATOM   4931  HB  ILE A 344      10.559   6.022  -1.189  1.00 66.33           H  
ATOM   4932 HG12 ILE A 344       9.231   7.504   0.456  1.00 71.17           H  
ATOM   4933 HG13 ILE A 344      10.425   7.000   1.373  1.00 71.17           H  
ATOM   4934 HG21 ILE A 344       8.232   6.009  -0.954  1.00 64.98           H  
ATOM   4935 HG22 ILE A 344       8.788   4.524  -1.052  1.00 64.98           H  
ATOM   4936 HG23 ILE A 344       8.375   5.127   0.359  1.00 64.98           H  
ATOM   4937 HD11 ILE A 344      10.971   9.047   0.414  1.00 70.51           H  
ATOM   4938 HD12 ILE A 344      11.962   7.925  -0.118  1.00 70.51           H  
ATOM   4939 HD13 ILE A 344      10.768   8.429  -1.036  1.00 70.51           H  
ATOM   4940  N   LYS A 345      12.652   5.953   1.852  1.00 44.26           N  
ANISOU 4940  N   LYS A 345     6249   5087   5480    489  -1052    987       N  
ATOM   4941  CA  LYS A 345      13.907   6.634   2.161  1.00 39.51           C  
ANISOU 4941  CA  LYS A 345     5613   4398   5000    565  -1108   1040       C  
ATOM   4942  C   LYS A 345      15.111   5.720   1.969  1.00 44.03           C  
ANISOU 4942  C   LYS A 345     6254   4849   5627    583  -1096   1148       C  
ATOM   4943  O   LYS A 345      15.295   4.753   2.716  1.00 44.79           O  
ANISOU 4943  O   LYS A 345     6427   4930   5663    521  -1101   1172       O  
ATOM   4944  CB  LYS A 345      13.897   7.172   3.594  1.00 44.26           C  
ANISOU 4944  CB  LYS A 345     6199   5040   5578    549  -1181    990       C  
ATOM   4945  CG  LYS A 345      13.265   8.543   3.740  1.00 46.49           C  
ANISOU 4945  CG  LYS A 345     6386   5392   5884    586  -1215    902       C  
ATOM   4946  CD  LYS A 345      13.418   9.076   5.158  1.00 50.23           C  
ANISOU 4946  CD  LYS A 345     6864   5888   6332    593  -1300    848       C  
ATOM   4947  H   LYS A 345      12.075   5.971   2.490  1.00 53.11           H  
ATOM   4948  HA  LYS A 345      14.009   7.389   1.560  1.00 47.41           H  
ATOM   4949  HB2 LYS A 345      13.400   6.556   4.154  1.00 53.11           H  
ATOM   4950  HB3 LYS A 345      14.813   7.234   3.909  1.00 53.11           H  
ATOM   4951  HG2 LYS A 345      13.699   9.163   3.133  1.00 55.78           H  
ATOM   4952  HG3 LYS A 345      12.318   8.483   3.538  1.00 55.78           H  
ATOM   4953  N   GLY A 346      15.945   6.034   0.981  1.00 46.09           N  
ANISOU 4953  N   GLY A 346     6484   5021   6008    674  -1074   1223       N  
ATOM   4954  CA  GLY A 346      17.127   5.244   0.709  1.00 40.25           C  
ANISOU 4954  CA  GLY A 346     5798   4159   5337    708  -1050   1335       C  
ATOM   4955  C   GLY A 346      16.858   3.895   0.089  1.00 44.16           C  
ANISOU 4955  C   GLY A 346     6402   4643   5735    670   -978   1350       C  
ATOM   4956  O   GLY A 346      17.781   3.081  -0.008  1.00 42.98           O  
ANISOU 4956  O   GLY A 346     6311   4394   5627    689   -954   1438       O  
ATOM   4957  H   GLY A 346      15.843   6.706   0.453  1.00 55.31           H  
ATOM   4958  HA2 GLY A 346      17.706   5.739   0.108  1.00 48.30           H  
ATOM   4959  HA3 GLY A 346      17.608   5.101   1.539  1.00 48.30           H  
ATOM   4960  N   ARG A 347      15.626   3.632  -0.331  1.00 46.71           N  
ANISOU 4960  N   ARG A 347     6749   5057   5942    620   -950   1265       N  
ATOM   4961  CA  ARG A 347      15.264   2.366  -0.955  1.00 48.89           C  
ANISOU 4961  CA  ARG A 347     7128   5315   6134    581   -902   1261       C  
ATOM   4962  C   ARG A 347      14.609   2.547  -2.312  1.00 47.66           C  
ANISOU 4962  C   ARG A 347     6978   5191   5939    634   -866   1218       C  
ATOM   4963  O   ARG A 347      14.868   1.759  -3.224  1.00 44.39           O  
ANISOU 4963  O   ARG A 347     6650   4715   5502    675   -825   1244       O  
ATOM   4964  CB  ARG A 347      14.327   1.571  -0.031  1.00 47.86           C  
ANISOU 4964  CB  ARG A 347     7034   5251   5901    449   -918   1202       C  
ATOM   4965  CG  ARG A 347      14.703   1.675   1.434  1.00 46.68           C  
ANISOU 4965  CG  ARG A 347     6869   5110   5757    405   -962   1224       C  
ATOM   4966  CD  ARG A 347      14.220   0.494   2.261  1.00 47.35           C  
ANISOU 4966  CD  ARG A 347     7020   5215   5756    295   -952   1225       C  
ATOM   4967  NE  ARG A 347      12.809   0.176   2.040  1.00 52.63           N  
ANISOU 4967  NE  ARG A 347     7682   5969   6346    219   -927   1151       N  
ATOM   4968  CZ  ARG A 347      12.348  -0.876   1.362  1.00 44.65           C  
ANISOU 4968  CZ  ARG A 347     6729   4924   5312    172   -900   1144       C  
ATOM   4969  NH1 ARG A 347      13.168  -1.757   0.809  1.00 47.31           N  
ANISOU 4969  NH1 ARG A 347     7147   5147   5681    198   -883   1200       N  
ATOM   4970  NH2 ARG A 347      11.042  -1.053   1.235  1.00 43.64           N  
ANISOU 4970  NH2 ARG A 347     6574   4869   5137    100   -895   1078       N  
ATOM   4971  H   ARG A 347      14.969   4.182  -0.265  1.00 56.05           H  
ATOM   4972  HA  ARG A 347      16.069   1.841  -1.083  1.00 58.67           H  
ATOM   4973  HB2 ARG A 347      13.424   1.911  -0.132  1.00 57.44           H  
ATOM   4974  HB3 ARG A 347      14.358   0.635  -0.281  1.00 57.44           H  
ATOM   4975  HG2 ARG A 347      15.669   1.716   1.509  1.00 56.02           H  
ATOM   4976  HG3 ARG A 347      14.308   2.480   1.805  1.00 56.02           H  
ATOM   4977  HD2 ARG A 347      14.743  -0.289   2.027  1.00 56.82           H  
ATOM   4978  HD3 ARG A 347      14.336   0.700   3.201  1.00 56.82           H  
ATOM   4979  HE  ARG A 347      12.228   0.713   2.376  1.00 63.16           H  
ATOM   4980 HH11 ARG A 347      14.019  -1.657   0.882  1.00 56.77           H  
ATOM   4981 HH12 ARG A 347      12.850  -2.428   0.376  1.00 56.77           H  
ATOM   4982 HH21 ARG A 347      10.496  -0.490   1.588  1.00 52.37           H  
ATOM   4983 HH22 ARG A 347      10.740  -1.729   0.799  1.00 52.37           H  
ATOM   4984  N   TYR A 348      13.773   3.573  -2.472  1.00 50.02           N  
ANISOU 4984  N   TYR A 348     7193   5585   6228    641   -886   1150       N  
ATOM   4985  CA  TYR A 348      13.138   3.874  -3.749  1.00 50.97           C  
ANISOU 4985  CA  TYR A 348     7312   5743   6310    699   -864   1111       C  
ATOM   4986  C   TYR A 348      13.417   5.296  -4.220  1.00 54.23           C  
ANISOU 4986  C   TYR A 348     7622   6174   6811    807   -859   1139       C  
ATOM   4987  O   TYR A 348      12.830   5.734  -5.217  1.00 48.79           O  
ANISOU 4987  O   TYR A 348     6916   5532   6089    862   -845   1108       O  
ATOM   4988  CB  TYR A 348      11.627   3.654  -3.656  1.00 50.87           C  
ANISOU 4988  CB  TYR A 348     7292   5833   6204    597   -893   1002       C  
ATOM   4989  CG  TYR A 348      11.215   2.207  -3.595  1.00 51.58           C  
ANISOU 4989  CG  TYR A 348     7480   5893   6223    506   -896    978       C  
ATOM   4990  CD1 TYR A 348      11.187   1.429  -4.741  1.00 41.90           C  
ANISOU 4990  CD1 TYR A 348     6351   4614   4953    546   -887    967       C  
ATOM   4991  CD2 TYR A 348      10.837   1.623  -2.396  1.00 44.42           C  
ANISOU 4991  CD2 TYR A 348     6573   5010   5296    386   -909    966       C  
ATOM   4992  CE1 TYR A 348      10.804   0.108  -4.696  1.00 41.49           C  
ANISOU 4992  CE1 TYR A 348     6385   4520   4857    461   -902    939       C  
ATOM   4993  CE2 TYR A 348      10.451   0.300  -2.340  1.00 44.23           C  
ANISOU 4993  CE2 TYR A 348     6625   4948   5231    299   -911    955       C  
ATOM   4994  CZ  TYR A 348      10.435  -0.452  -3.495  1.00 45.22           C  
ANISOU 4994  CZ  TYR A 348     6840   5009   5333    333   -914    938       C  
ATOM   4995  OH  TYR A 348      10.053  -1.773  -3.455  1.00 49.90           O  
ANISOU 4995  OH  TYR A 348     7506   5550   5905    247   -928    921       O  
ATOM   4996  H   TYR A 348      13.556   4.117  -1.843  1.00 60.03           H  
ATOM   4997  HA  TYR A 348      13.485   3.267  -4.421  1.00 61.16           H  
ATOM   4998  HB2 TYR A 348      11.299   4.088  -2.853  1.00 61.04           H  
ATOM   4999  HB3 TYR A 348      11.207   4.048  -4.436  1.00 61.04           H  
ATOM   5000  HD1 TYR A 348      11.435   1.805  -5.555  1.00 50.27           H  
ATOM   5001  HD2 TYR A 348      10.846   2.131  -1.617  1.00 53.31           H  
ATOM   5002  HE1 TYR A 348      10.793  -0.403  -5.473  1.00 49.78           H  
ATOM   5003  HE2 TYR A 348      10.202  -0.082  -1.529  1.00 53.07           H  
ATOM   5004  HH  TYR A 348       9.854  -1.991  -2.668  1.00 59.88           H  
ATOM   5005  N   ASN A 349      14.289   6.027  -3.533  1.00 60.35           N  
ANISOU 5005  N   ASN A 349     8323   6906   7702    839   -877   1197       N  
ATOM   5006  CA  ASN A 349      14.640   7.384  -3.933  1.00 60.21           C  
ANISOU 5006  CA  ASN A 349     8192   6882   7801    940   -877   1236       C  
ATOM   5007  C   ASN A 349      16.148   7.584  -3.839  1.00 64.68           C  
ANISOU 5007  C   ASN A 349     8729   7323   8523   1023   -865   1364       C  
ATOM   5008  O   ASN A 349      16.845   6.834  -3.152  1.00 62.56           O  
ANISOU 5008  O   ASN A 349     8513   6987   8271    983   -880   1405       O  
ATOM   5009  CB  ASN A 349      13.915   8.409  -3.061  1.00 57.84           C  
ANISOU 5009  CB  ASN A 349     7791   6667   7519    889   -940   1150       C  
ATOM   5010  CG  ASN A 349      14.407   8.408  -1.625  1.00 59.45           C  
ANISOU 5010  CG  ASN A 349     7985   6842   7762    830  -1003   1145       C  
ATOM   5011  OD1 ASN A 349      15.115   7.496  -1.196  1.00 59.40           O  
ANISOU 5011  OD1 ASN A 349     8052   6767   7749    803  -1003   1196       O  
ATOM   5012  ND2 ASN A 349      14.025   9.430  -0.871  1.00 59.29           N  
ANISOU 5012  ND2 ASN A 349     7879   6873   7776    818  -1061   1079       N  
ATOM   5013  OXT ASN A 349      16.699   8.500  -4.448  1.00 70.22           O  
ANISOU 5013  OXT ASN A 349     9347   7984   9350   1131   -842   1440       O  
ATOM   5014  H   ASN A 349      14.694   5.757  -2.824  1.00 72.42           H  
ATOM   5015  HA  ASN A 349      14.372   7.525  -4.854  1.00 72.25           H  
ATOM   5016  HB2 ASN A 349      14.061   9.296  -3.427  1.00 69.41           H  
ATOM   5017  HB3 ASN A 349      12.967   8.205  -3.054  1.00 69.41           H  
ATOM   5018 HD21 ASN A 349      14.277   9.477  -0.050  1.00 71.15           H  
ATOM   5019 HD22 ASN A 349      13.526  10.047  -1.204  1.00 71.15           H  
TER    5020      ASN A 349                                                      
HETATM 5100  O   HOH A 501      -6.222  32.002  -2.291  1.00 96.86           O  
HETATM 5101  O   HOH A 502      -6.145  13.558  -1.259  1.00 41.34           O  
HETATM 5102  O   HOH A 503       7.536  16.872  -6.091  1.00 45.75           O  
HETATM 5103  O   HOH A 504     -11.887  35.467 -11.339  1.00 51.32           O  
HETATM 5104  O   HOH A 505     -24.546  28.138 -24.744  1.00 45.78           O  
HETATM 5105  O   HOH A 506     -11.299  10.504 -15.890  1.00 50.34           O  
HETATM 5106  O   HOH A 507     -12.930  15.817 -10.894  1.00 42.09           O  
HETATM 5107  O   HOH A 508     -28.017  24.749 -23.770  1.00 51.25           O  
HETATM 5108  O   HOH A 509     -19.186  36.550 -10.618  1.00 52.08           O  
HETATM 5109  O   HOH A 510     -11.249   7.074  -2.952  1.00 74.87           O  
HETATM 5110  O   HOH A 511     -16.637   6.358 -16.279  1.00 78.08           O  
HETATM 5111  O   HOH A 512       1.117  12.614 -11.659  1.00 54.34           O  
HETATM 5112  O   HOH A 513       4.331   4.134  12.080  1.00 82.82           O  
HETATM 5113  O   HOH A 514      -6.635   9.388 -16.371  1.00 56.18           O  
HETATM 5114  O   HOH A 515     -23.859  32.057 -22.708  1.00 70.21           O  
HETATM 5115  O   HOH A 516     -25.115  23.420 -23.353  1.00 40.00           O  
HETATM 5116  O   HOH A 517      -4.460  13.766  -9.992  1.00 41.30           O  
HETATM 5117  O   HOH A 518      14.136   4.063   5.005  1.00 42.55           O  
HETATM 5118  O   HOH A 519      -6.680  26.945  -6.637  1.00 45.19           O  
HETATM 5119  O   HOH A 520      -7.045  13.027  -9.610  1.00 45.94           O  
HETATM 5120  O   HOH A 521     -19.126  22.072 -33.003  1.00 48.03           O  
HETATM 5121  O   HOH A 522     -12.002  17.138   1.606  1.00 50.42           O  
HETATM 5122  O   HOH A 523     -29.401  33.264 -17.115  1.00 47.98           O  
HETATM 5123  O   HOH A 524     -37.692  16.864 -20.005  1.00 60.17           O  
HETATM 5124  O   HOH A 525       1.373  15.371  -5.474  1.00 46.56           O  
HETATM 5125  O   HOH A 526     -15.607  15.297 -12.174  1.00 42.71           O  
HETATM 5126  O   HOH A 527     -22.159  29.212  -8.199  1.00 45.62           O  
HETATM 5127  O   HOH A 528       7.066  27.591 -14.413  1.00 47.04           O  
HETATM 5128  O   HOH A 529     -26.185  25.319 -19.092  1.00 49.04           O  
HETATM 5129  O   HOH A 530       3.176  27.270 -12.225  1.00104.44           O  
HETATM 5130  O   HOH A 531      -5.090  12.413  -3.058  1.00 45.64           O  
HETATM 5131  O   HOH A 532       1.743  27.567  -1.757  1.00 47.89           O  
HETATM 5132  O   HOH A 533       3.372  26.296 -14.685  1.00 43.22           O  
HETATM 5133  O   HOH A 534     -12.521  35.253  -8.924  1.00 50.35           O  
HETATM 5134  O   HOH A 535     -20.285  36.311 -13.202  1.00 47.77           O  
HETATM 5135  O   HOH A 536     -21.388  31.738 -23.070  1.00 53.31           O  
HETATM 5136  O   HOH A 537      -4.129  12.331 -17.321  1.00 48.80           O  
HETATM 5137  O   HOH A 538       5.845  15.397  -6.827  1.00 49.60           O  
HETATM 5138  O   HOH A 539      -9.127  10.920 -17.551  1.00 46.89           O  
HETATM 5139  O   HOH A 540      -5.252  27.898  -4.382  1.00 60.80           O  
HETATM 5140  O   HOH A 541      -3.142  11.077   7.871  1.00 46.14           O  
HETATM 5141  O   HOH A 542     -28.499  24.530 -20.328  1.00 57.60           O  
HETATM 5142  O   HOH A 543     -16.392  17.261 -11.078  1.00 42.00           O  
HETATM 5143  O   HOH A 544      -9.875  18.775 -23.987  1.00 79.10           O  
HETATM 5144  O   HOH A 545     -12.555   8.731   1.900  1.00 73.02           O  
HETATM 5145  O   HOH A 546     -19.058  21.331 -36.818  1.00 82.09           O  
CONECT 2647 5021                                                                
CONECT 2683 5021                                                                
CONECT 3949 5021                                                                
CONECT 5021 2647 2683 3949 5042                                                 
CONECT 5021 5050                                                                
CONECT 5022 5023 5024 5025 5026                                                 
CONECT 5023 5022                                                                
CONECT 5024 5022                                                                
CONECT 5025 5022                                                                
CONECT 5026 5022                                                                
CONECT 5027 5028 5029 5030 5031                                                 
CONECT 5028 5027                                                                
CONECT 5029 5027                                                                
CONECT 5030 5027                                                                
CONECT 5031 5027                                                                
CONECT 5032 5033                                                                
CONECT 5033 5032 5034 5052                                                      
CONECT 5034 5033 5035 5041                                                      
CONECT 5035 5034 5036 5040 5060                                                 
CONECT 5036 5035 5037 5061 5062                                                 
CONECT 5037 5036 5038 5063 5064                                                 
CONECT 5038 5037 5039 5065 5066                                                 
CONECT 5039 5038 5040 5067 5068                                                 
CONECT 5040 5035 5039 5069 5070                                                 
CONECT 5041 5034 5042 5043                                                      
CONECT 5042 5021 5041 5071                                                      
CONECT 5043 5041 5044 5051                                                      
CONECT 5044 5043 5045 5050                                                      
CONECT 5045 5044 5046 5072                                                      
CONECT 5046 5045 5047 5073 5074                                                 
CONECT 5047 5046 5048 5049                                                      
CONECT 5048 5047                                                                
CONECT 5049 5047                                                                
CONECT 5050 5021 5044                                                           
CONECT 5051 5043 5052 5059                                                      
CONECT 5052 5033 5051 5053                                                      
CONECT 5053 5052 5054 5058 5075                                                 
CONECT 5054 5053 5055 5076 5077                                                 
CONECT 5055 5054 5056 5078 5079                                                 
CONECT 5056 5055 5057 5080 5081                                                 
CONECT 5057 5056 5058 5082 5083                                                 
CONECT 5058 5053 5057 5084 5085                                                 
CONECT 5059 5051                                                                
CONECT 5060 5035                                                                
CONECT 5061 5036                                                                
CONECT 5062 5036                                                                
CONECT 5063 5037                                                                
CONECT 5064 5037                                                                
CONECT 5065 5038                                                                
CONECT 5066 5038                                                                
CONECT 5067 5039                                                                
CONECT 5068 5039                                                                
CONECT 5069 5040                                                                
CONECT 5070 5040                                                                
CONECT 5071 5042                                                                
CONECT 5072 5045                                                                
CONECT 5073 5046                                                                
CONECT 5074 5046                                                                
CONECT 5075 5053                                                                
CONECT 5076 5054                                                                
CONECT 5077 5054                                                                
CONECT 5078 5055                                                                
CONECT 5079 5055                                                                
CONECT 5080 5056                                                                
CONECT 5081 5056                                                                
CONECT 5082 5057                                                                
CONECT 5083 5057                                                                
CONECT 5084 5058                                                                
CONECT 5085 5058                                                                
CONECT 5086 5087 5088 5092 5093                                                 
CONECT 5087 5086 5094                                                           
CONECT 5088 5086 5089 5090 5095                                                 
CONECT 5089 5088 5096                                                           
CONECT 5090 5088 5091 5097 5098                                                 
CONECT 5091 5090 5099                                                           
CONECT 5092 5086                                                                
CONECT 5093 5086                                                                
CONECT 5094 5087                                                                
CONECT 5095 5088                                                                
CONECT 5096 5089                                                                
CONECT 5097 5090                                                                
CONECT 5098 5090                                                                
CONECT 5099 5091                                                                
MASTER      449    0    5   16   14    0    9    6 2710    1   83   27          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.