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***  me  ***

elNémo ID: 20042320254371417

Job options:

ID        	=	 20042320254371417
JOBID     	=	 me
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 me

REMARK Date 2018-02-03 Time 17:09:49 GMT +0000 (1517677789.62 s)                
REMARK PHENIX refinement                                                        
REMARK                                                                          
REMARK ****************** INPUT FILES AND LABELS ****************************** 
REMARK Reflections:                                                             
REMARK   file name      : /Users/u1457114/Downloads/mx14692v30_xBd1833MEBcsB62_f
REMARK   labels         : ['IMEAN,SIGIMEAN']                                    
REMARK R-free flags:                                                            
REMARK   file name      : /Users/u1457114/Downloads/mx14692v30_xBd1833MEBcsB62_f
REMARK   label          : FreeR_flag                                            
REMARK   test_flag_value: 0                                                     
REMARK Model file name(s):                                                      
REMARK   /Users/u1457114/Desktop/Diamond/Bd1833/ME_domain/BCS_B6/Refine_15/Bd183
REMARK                                                                          
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS ******************* 
REMARK Start: r_work = 0.1986 r_free = 0.2255 bonds = 0.012 angles = 1.332      
REMARK Final: r_work = 0.1702 r_free = 0.2039 bonds = 0.007 angles = 1.109      
REMARK ************************************************************************ 
REMARK                                                                          
REMARK ****************** REFINEMENT STATISTICS STEP BY STEP ****************** 
REMARK leading digit, like 1_, means number of macro-cycle                      
REMARK   0  : statistics at the very beginning when nothing is done yet         
REMARK   1 s: bulk solvent correction and/or (anisotropic) scaling              
REMARK   1 z: refinement of coordinates                                         
REMARK   1 p: refinement of ADPs (Atomic Displacement Parameters)               
REMARK   1 t: ordered solvent update (add / remove)                             
REMARK   1 c: refinement of occupancies                                         
REMARK ------------------------------------------------------------------------ 
REMARK  stage       r-work r-free bonds angles b_min b_max b_ave n_water shift  
REMARK       0    : 0.3403 0.2692 0.012  1.33   8.2  79.2  31.8 554      0.000  
REMARK       1_bss: 0.1986 0.2255 0.012  1.33   8.3  79.3  31.8 554      0.000  
REMARK   1 ttarget: 0.1986 0.2255 0.012  1.33   8.3  79.3  31.8 554      0.000  
REMARK   1 dcbetar: 0.1986 0.2255 0.012  1.33   8.3  79.3  31.8 554      0.000  
REMARK    1_weight: 0.1986 0.2255 0.012  1.33   8.3  79.3  31.8 554      0.000  
REMARK       1_nqh: 0.1986 0.2255 0.012  1.33   8.3  79.3  31.8 554      0.001  
REMARK    1_xyzrec: 0.1981 0.2359 0.007  1.10   8.3  79.3  31.8 554      0.077  
REMARK       1_adp: 0.1829 0.2243 0.007  1.10   7.5 111.4  35.4 554      0.077  
REMARK       1_occ: 0.1829 0.2243 0.007  1.10   7.5 111.4  35.4 554      0.077  
REMARK       2_bss: 0.1823 0.2243 0.007  1.10   7.9 111.7  35.8 554      0.077  
REMARK   2 ttarget: 0.1823 0.2243 0.007  1.10   7.9 111.7  35.8 554      0.077  
REMARK       2_sol: 0.1826 0.2196 0.007  1.10   7.9 111.7  35.9 610       n/a   
REMARK       2_ion: 0.1826 0.2196 0.007  1.10   7.9 111.7  35.9 610       n/a   
REMARK   2 realsrl: 0.1835 0.2200 0.007  1.16   7.9 111.7  35.9 610       n/a   
REMARK    2_weight: 0.1835 0.2200 0.007  1.16   7.9 111.7  35.9 610       n/a   
REMARK       2_nqh: 0.1835 0.2200 0.007  1.16   7.9 111.7  35.9 610       n/a   
REMARK    2_xyzrec: 0.1795 0.2209 0.007  1.09   7.9 111.7  35.9 610       n/a   
REMARK       2_adp: 0.1751 0.2167 0.007  1.09   8.3 109.1  37.1 610       n/a   
REMARK       2_occ: 0.1751 0.2166 0.007  1.09   8.3 109.1  37.1 610       n/a   
REMARK       3_bss: 0.1749 0.2169 0.007  1.09   8.4 109.2  37.3 610       n/a   
REMARK   3 ttarget: 0.1749 0.2169 0.007  1.09   8.4 109.2  37.3 610       n/a   
REMARK       3_sol: 0.1770 0.2136 0.007  1.09   8.4 109.2  37.3 617       n/a   
REMARK       3_ion: 0.1770 0.2136 0.007  1.09   8.4 109.2  37.3 617       n/a   
REMARK   3 realsrl: 0.1775 0.2142 0.007  1.11   8.4 109.2  37.3 617       n/a   
REMARK    3_weight: 0.1775 0.2142 0.007  1.11   8.4 109.2  37.3 617       n/a   
REMARK       3_nqh: 0.1775 0.2142 0.007  1.11   8.4 109.2  37.3 617       n/a   
REMARK    3_xyzrec: 0.1760 0.2100 0.008  1.13   8.4 109.2  37.3 617       n/a   
REMARK       3_adp: 0.1735 0.2067 0.008  1.13   8.5 112.8  37.8 617       n/a   
REMARK       3_occ: 0.1735 0.2067 0.008  1.13   8.5 112.8  37.8 617       n/a   
REMARK       4_bss: 0.1734 0.2065 0.008  1.13   8.5 112.7  37.8 617       n/a   
REMARK   4 ttarget: 0.1734 0.2065 0.008  1.13   8.5 112.7  37.8 617       n/a   
REMARK       4_sol: 0.1733 0.2036 0.008  1.13   8.5 112.7  37.8 707       n/a   
REMARK       4_ion: 0.1733 0.2036 0.008  1.13   8.5 112.7  37.8 707       n/a   
REMARK   4 realsrl: 0.1738 0.2049 0.008  1.20   8.5 112.7  37.8 707       n/a   
REMARK    4_weight: 0.1738 0.2049 0.008  1.20   8.5 112.7  37.8 707       n/a   
REMARK       4_nqh: 0.1738 0.2049 0.008  1.20   8.5 112.7  37.8 707       n/a   
REMARK    4_xyzrec: 0.1714 0.2057 0.007  1.10   8.5 112.7  37.8 707       n/a   
REMARK       4_adp: 0.1705 0.2044 0.007  1.10   8.5 108.3  37.4 707       n/a   
REMARK       4_occ: 0.1705 0.2044 0.007  1.10   8.5 108.3  37.4 707       n/a   
REMARK       5_bss: 0.1705 0.2045 0.007  1.10   8.4 108.2  37.3 707       n/a   
REMARK   5 ttarget: 0.1705 0.2045 0.007  1.10   8.4 108.2  37.3 707       n/a   
REMARK       5_sol: 0.1717 0.2045 0.007  1.10   8.4 108.2  37.3 722       n/a   
REMARK       5_ion: 0.1717 0.2045 0.007  1.10   8.4 108.2  37.3 722       n/a   
REMARK   5 realsrl: 0.1722 0.2054 0.007  1.13   8.4 108.2  37.3 722       n/a   
REMARK    5_weight: 0.1722 0.2054 0.007  1.13   8.4 108.2  37.3 722       n/a   
REMARK       5_nqh: 0.1722 0.2054 0.007  1.13   8.4 108.2  37.3 722       n/a   
REMARK    5_xyzrec: 0.1707 0.2064 0.007  1.11   8.4 108.2  37.3 722       n/a   
REMARK       5_adp: 0.1706 0.2068 0.007  1.11   8.4 108.0  37.2 722       n/a   
REMARK       5_occ: 0.1706 0.2068 0.007  1.11   8.4 108.0  37.2 722       n/a   
REMARK         end: 0.1702 0.2039 0.007  1.11   8.4 108.0  37.0 680       n/a   
REMARK ------------------------------------------------------------------------ 
REMARK MODEL CONTENT.                                                           
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM                        
REMARK        S                       34           34.00                        
REMARK        C                     3880         3878.00                        
REMARK       Mg                        2            2.00                        
REMARK        O                     1839         1838.00                        
REMARK        N                     1053         1053.00                        
REMARK    TOTAL                     6808         6805.00                        
REMARK -----------------------------------------------------------------------  
REMARK r_free_flags.md5.hexdigest fde3e669b606bebdb94a752950454d99              
REMARK                                                                          
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.        
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (phenix.refine: 1.9_1692)                     
REMARK   3   AUTHORS     : Adams,Afonine,Burnley,Chen,Davis,Echols,Gildea,      
REMARK   3               : Gopal,Gros,Grosse-Kunstleve,Headd,Hung,Immormino,    
REMARK   3               : Ioerger,McCoy,McKee,Moriarty,Pai,Read,Richardson,    
REMARK   3               : Richardson,Romo,Sacchettini,Sauter,Smith,Storoni,    
REMARK   3               : Terwilliger,Zwart                                    
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ML                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.679                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.019                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.33                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.35                          
REMARK   3   NUMBER OF REFLECTIONS             : 94172                          
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 94172                      
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1718                          
REMARK   3   R VALUE            (WORKING SET) : 0.1702                          
REMARK   3   FREE R VALUE                     : 0.2039                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.93                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4646                            
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 48.0385 -  5.2152    0.99     3138   155  0.1421 0.1644        
REMARK   3     2  5.2152 -  4.1402    1.00     3110   148  0.1285 0.1640        
REMARK   3     3  4.1402 -  3.6170    0.99     3053   163  0.1350 0.1683        
REMARK   3     4  3.6170 -  3.2864    0.99     3052   174  0.1557 0.1929        
REMARK   3     5  3.2864 -  3.0509    0.99     3076   138  0.1653 0.2021        
REMARK   3     6  3.0509 -  2.8710    0.99     3032   168  0.1652 0.2140        
REMARK   3     7  2.8710 -  2.7273    0.99     2999   179  0.1741 0.2084        
REMARK   3     8  2.7273 -  2.6086    0.98     2972   197  0.1647 0.1966        
REMARK   3     9  2.6086 -  2.5081    0.99     2999   167  0.1718 0.2210        
REMARK   3    10  2.5081 -  2.4216    0.99     3016   175  0.1660 0.1952        
REMARK   3    11  2.4216 -  2.3459    0.97     2983   177  0.1719 0.1992        
REMARK   3    12  2.3459 -  2.2788    0.99     3010   145  0.1724 0.2183        
REMARK   3    13  2.2788 -  2.2188    0.97     2965   187  0.1721 0.2078        
REMARK   3    14  2.2188 -  2.1647    0.98     2993   169  0.1733 0.1956        
REMARK   3    15  2.1647 -  2.1155    0.98     2980   152  0.1833 0.2044        
REMARK   3    16  2.1155 -  2.0705    0.98     3019   138  0.1835 0.2232        
REMARK   3    17  2.0705 -  2.0291    0.97     2959   137  0.1946 0.2426        
REMARK   3    18  2.0291 -  1.9908    0.98     3018   120  0.1904 0.2314        
REMARK   3    19  1.9908 -  1.9552    0.96     2979   139  0.1867 0.2030        
REMARK   3    20  1.9552 -  1.9221    0.99     2978   168  0.1950 0.2277        
REMARK   3    21  1.9221 -  1.8911    0.95     2911   170  0.2033 0.2391        
REMARK   3    22  1.8911 -  1.8620    0.96     2921   160  0.2180 0.2223        
REMARK   3    23  1.8620 -  1.8346    0.97     2955   147  0.2245 0.2402        
REMARK   3    24  1.8346 -  1.8087    0.95     2918   165  0.2379 0.3035        
REMARK   3    25  1.8087 -  1.7843    0.96     2925   137  0.2501 0.2381        
REMARK   3    26  1.7843 -  1.7611    0.96     2918   155  0.2587 0.2704        
REMARK   3    27  1.7611 -  1.7391    0.95     2917   139  0.2693 0.3114        
REMARK   3    28  1.7391 -  1.7182    0.96     2946   134  0.2941 0.3561        
REMARK   3    29  1.7182 -  1.6982    0.95     2942   123  0.3149 0.3462        
REMARK   3    30  1.6982 -  1.6791    0.92     2842   120  0.3362 0.3915        
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   GRID STEP FACTOR   : 4.00                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.19             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.88            
REMARK   3                                                                      
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT                       
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD     MAX  COUNT                                  
REMARK   3   BOND      :  0.007   0.053   6235                                  
REMARK   3   ANGLE     :  1.109   9.078   8443                                  
REMARK   3   CHIRALITY :  0.046   0.165    969                                  
REMARK   3   PLANARITY :  0.005   0.058   1106                                  
REMARK   3   DIHEDRAL  : 13.374  79.845   2317                                  
REMARK   3   MIN NONBONDED DISTANCE : 1.701                                     
REMARK   3                                                                      
REMARK   3  MOLPROBITY STATISTICS.                                              
REMARK   3   ALL-ATOM CLASHSCORE : 5.02                                         
REMARK   3   RAMACHANDRAN PLOT:                                                 
REMARK   3     OUTLIERS : 0.00  %                                               
REMARK   3     ALLOWED  : 3.20  %                                               
REMARK   3     FAVORED  : 96.80 %                                               
REMARK   3   ROTAMER OUTLIERS : 0.31 %                                          
REMARK   3   CBETA DEVIATIONS : 0                                               
REMARK   3                                                                      
REMARK   3  ATOMIC DISPLACEMENT PARAMETERS.                                     
REMARK   3   WILSON B : None                                                    
REMARK   3   RMS(B_ISO_OR_EQUIVALENT_BONDED) : 4.55                             
REMARK   3   ATOMS          NUMBER OF ATOMS                                     
REMARK   3                    ISO.  ANISO.                                      
REMARK   3    ALL         :   6808    6126                                      
REMARK   3    ALL (NO H)  :   6808    6126                                      
REMARK   3    SOLVENT     :    680       0                                      
REMARK   3    NON-SOLVENT :   6128    6126                                      
REMARK   3    HYDROGENS   :      0       0                                      
REMARK   3                                                                      
REMARK   3  TLS DETAILS.                                                        
REMARK   3   NUMBER OF TLS GROUPS: 13                                           
REMARK   3   ORIGIN: CENTER OF MASS                                             
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid   16  through   37 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0523  38.9147  25.8124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1750 T22:   0.1454                                     
REMARK   3      T33:   0.2995 T12:  -0.0004                                     
REMARK   3      T13:   0.0499 T23:  -0.1152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1112 L22:   0.1791                                     
REMARK   3      L33:   0.6731 L12:  -0.1403                                     
REMARK   3      L13:   0.0119 L23:   0.0234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0185 S12:  -0.0655 S13:   0.1267                       
REMARK   3      S21:   0.1308 S22:   0.0183 S23:   0.0518                       
REMARK   3      S31:  -0.0962 S32:   0.0197 S33:  -0.2057                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid   38  through   65 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1162  24.7882   8.6342              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1216 T22:   0.2035                                     
REMARK   3      T33:   0.2089 T12:   0.0038                                     
REMARK   3      T13:   0.0035 T23:  -0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0601 L22:   0.0114                                     
REMARK   3      L33:   0.0375 L12:   0.0209                                     
REMARK   3      L13:   0.0315 L23:   0.0160                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0030 S12:   0.0167 S13:   0.0455                       
REMARK   3      S21:  -0.0521 S22:   0.0573 S23:  -0.0543                       
REMARK   3      S31:   0.0329 S32:   0.2664 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid   66  through  193 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3666  15.9724  26.5293              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1678 T22:   0.1976                                     
REMARK   3      T33:   0.1462 T12:  -0.0057                                     
REMARK   3      T13:   0.0137 T23:  -0.0261                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1288 L22:   0.1579                                     
REMARK   3      L33:   0.3996 L12:   0.0036                                     
REMARK   3      L13:  -0.1532 L23:  -0.1283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0420 S12:  -0.2268 S13:   0.0009                       
REMARK   3      S21:   0.1149 S22:  -0.0177 S23:   0.0697                       
REMARK   3      S31:   0.1642 S32:   0.0367 S33:  -0.0012                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid  194  through  232 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5465   5.6679  48.9439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3862 T22:   0.5243                                     
REMARK   3      T33:   0.1997 T12:  -0.0259                                     
REMARK   3      T13:   0.0149 T23:   0.0673                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0112 L22:   0.0540                                     
REMARK   3      L33:   0.0230 L12:  -0.0216                                     
REMARK   3      L13:   0.0134 L23:  -0.0178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0200 S12:  -0.1068 S13:  -0.1369                       
REMARK   3      S21:   0.1281 S22:  -0.0313 S23:   0.0816                       
REMARK   3      S31:   0.1583 S32:  -0.1453 S33:   0.0005                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid  233  through  261 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -23.9656   1.5479  41.9050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5077 T22:   0.5701                                     
REMARK   3      T33:   0.4519 T12:  -0.0998                                     
REMARK   3      T13:  -0.0721 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0165 L22:   0.0305                                     
REMARK   3      L33:   0.0155 L12:   0.0093                                     
REMARK   3      L13:  -0.0068 L23:   0.0136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0841 S12:  -0.0980 S13:  -0.2002                       
REMARK   3      S21:  -0.0577 S22:   0.0300 S23:   0.0965                       
REMARK   3      S31:   0.1436 S32:  -0.1225 S33:   0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid  262  through  321 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8689  17.7637  54.4874              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4569 T22:   0.6903                                     
REMARK   3      T33:   0.2592 T12:  -0.0043                                     
REMARK   3      T13:   0.1449 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0542 L22:   0.4906                                     
REMARK   3      L33:   0.1292 L12:  -0.0780                                     
REMARK   3      L13:   0.0800 L23:  -0.0564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1106 S12:  -0.1437 S13:   0.0503                       
REMARK   3      S21:   0.2100 S22:   0.0032 S23:   0.2841                       
REMARK   3      S31:  -0.1199 S32:  -0.3156 S33:   0.0456                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resid  322  through  398 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4834  21.1213  44.8802              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2847 T22:   0.4706                                     
REMARK   3      T33:   0.1242 T12:  -0.0223                                     
REMARK   3      T13:   0.0039 T23:  -0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2173 L22:   0.0189                                     
REMARK   3      L33:   0.0456 L12:  -0.0483                                     
REMARK   3      L13:   0.0570 L23:  -0.0285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0689 S12:  -0.2981 S13:   0.0359                       
REMARK   3      S21:   0.0854 S22:  -0.0456 S23:  -0.0379                       
REMARK   3      S31:  -0.0831 S32:   0.2692 S33:  -0.0027                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resid  399  through  422 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1838  12.3774  37.7501              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2737 T22:   0.4530                                     
REMARK   3      T33:   0.1780 T12:   0.0923                                     
REMARK   3      T13:  -0.0497 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0504 L22:   0.0759                                     
REMARK   3      L33:   0.0608 L12:   0.0522                                     
REMARK   3      L13:  -0.0547 L23:  -0.0519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0838 S12:  -0.2691 S13:  -0.0747                       
REMARK   3      S21:   0.0021 S22:  -0.1301 S23:  -0.1109                       
REMARK   3      S31:   0.0568 S32:   0.2757 S33:  -0.0054                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resid   15  through   37 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  20.1706  24.0796  14.5724              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0646 T22:   0.2298                                     
REMARK   3      T33:   0.1800 T12:   0.0144                                     
REMARK   3      T13:  -0.0158 T23:  -0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4716 L22:   0.1762                                     
REMARK   3      L33:   0.1862 L12:   0.0477                                     
REMARK   3      L13:  -0.1297 L23:  -0.1736                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0378 S12:  -0.1133 S13:   0.0063                       
REMARK   3      S21:   0.0203 S22:   0.0060 S23:  -0.0733                       
REMARK   3      S31:  -0.0140 S32:   0.1241 S33:   0.0861                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resid   38  through  193 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9636  25.1628   8.4920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1068 T22:   0.0932                                     
REMARK   3      T33:   0.1308 T12:  -0.0019                                     
REMARK   3      T13:  -0.0192 T23:  -0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2601 L22:   0.5131                                     
REMARK   3      L33:   0.3950 L12:   0.1262                                     
REMARK   3      L13:  -0.1963 L23:  -0.0939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0045 S12:  -0.0263 S13:   0.0776                       
REMARK   3      S21:  -0.0821 S22:   0.0007 S23:   0.0707                       
REMARK   3      S31:   0.0139 S32:  -0.0502 S33:   0.0506                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'B' and (resid  194  through  287 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4601  20.9307 -22.4133              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7510 T22:   0.2426                                     
REMARK   3      T33:   0.3163 T12:  -0.0231                                     
REMARK   3      T13:   0.0598 T23:  -0.1143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2547 L22:   0.3091                                     
REMARK   3      L33:   0.5568 L12:  -0.1033                                     
REMARK   3      L13:  -0.0956 L23:  -0.3326                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0508 S12:   0.2684 S13:  -0.2757                       
REMARK   3      S21:  -0.7027 S22:   0.0633 S23:  -0.1955                       
REMARK   3      S31:   0.4231 S32:  -0.0121 S33:   0.2621                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'B' and (resid  288  through  331 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4833  29.8309 -16.3707              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3617 T22:   0.2170                                     
REMARK   3      T33:   0.3831 T12:   0.0734                                     
REMARK   3      T13:   0.1949 T23:  -0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1644 L22:   0.0890                                     
REMARK   3      L33:   0.0556 L12:   0.1207                                     
REMARK   3      L13:   0.0242 L23:   0.0213                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0010 S12:   0.1483 S13:  -0.0819                       
REMARK   3      S21:  -0.3406 S22:   0.0260 S23:  -0.4305                       
REMARK   3      S31:   0.0428 S32:   0.1804 S33:   0.1115                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'B' and (resid  332  through  422 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3716  40.1100  -3.8043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1537 T22:   0.1022                                     
REMARK   3      T33:   0.1889 T12:  -0.0001                                     
REMARK   3      T13:  -0.0165 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0056 L22:   0.5160                                     
REMARK   3      L33:   0.2764 L12:  -0.0339                                     
REMARK   3      L13:  -0.0118 L23:  -0.2091                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0361 S12:   0.0433 S13:   0.0244                       
REMARK   3      S21:  -0.1095 S22:   0.0183 S23:   0.0545                       
REMARK   3      S31:  -0.1082 S32:  -0.0238 S33:   0.0682                       
REMARK   3                                                                      
CRYST1   48.028   92.654   96.956  90.00  91.10  90.00 P 1 21 1                 
SCALE1      0.020821  0.000000  0.000401        0.00000                         
SCALE2      0.000000  0.010793  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010316        0.00000                         
ATOM      1  N   THR A  16     -21.747  41.826  33.561  1.00 72.68           N  
ANISOU    1  N   THR A  16     8946   8694   9974    308    784  -1103       N  
ATOM      2  CA  THR A  16     -20.611  41.715  34.468  1.00 70.76           C  
ANISOU    2  CA  THR A  16     8748   8435   9702    294    768  -1117       C  
ATOM      3  CB  THR A  16     -20.204  40.238  34.695  1.00 68.04           C  
ANISOU    3  CB  THR A  16     8395   8114   9344    260    776  -1109       C  
ATOM      4  OG1 THR A  16     -21.224  39.568  35.443  1.00 70.99           O  
ANISOU    4  OG1 THR A  16     8756   8518   9698    273    816  -1109       O  
ATOM      5  CG2 THR A  16     -18.910  40.145  35.474  1.00 64.11           C  
ANISOU    5  CG2 THR A  16     7942   7602   8817    248    753  -1122       C  
ATOM      6  C   THR A  16     -19.423  42.502  33.920  1.00 71.88           C  
ANISOU    6  C   THR A  16     8914   8541   9858    279    728  -1121       C  
ATOM      7  O   THR A  16     -19.075  42.381  32.745  1.00 71.12           O  
ANISOU    7  O   THR A  16     8792   8439   9792    255    710  -1107       O  
ATOM      8  N   ASN A  17     -18.816  43.319  34.776  1.00 67.41           N  
ANISOU    8  N   ASN A  17     8396   7949   9267    292    714  -1142       N  
ATOM      9  CA  ASN A  17     -17.631  44.082  34.402  1.00 63.15           C  
ANISOU    9  CA  ASN A  17     7882   7375   8737    273    677  -1150       C  
ATOM     10  CB  ASN A  17     -17.347  45.172  35.438  1.00 72.15           C  
ANISOU   10  CB  ASN A  17     9079   8486   9850    297    668  -1175       C  
ATOM     11  CG  ASN A  17     -18.551  46.060  35.695  1.00 80.17           C  
ANISOU   11  CG  ASN A  17    10105   9494  10861    347    689  -1181       C  
ATOM     12  OD1 ASN A  17     -19.407  46.233  34.826  1.00 84.20           O  
ANISOU   12  OD1 ASN A  17    10584  10011  11398    361    700  -1166       O  
ATOM     13  ND2 ASN A  17     -18.624  46.627  36.895  1.00 80.62           N  
ANISOU   13  ND2 ASN A  17    10208   9539  10883    377    693  -1202       N  
ATOM     14  C   ASN A  17     -16.410  43.181  34.246  1.00 54.12           C  
ANISOU   14  C   ASN A  17     6733   6239   7590    230    656  -1146       C  
ATOM     15  O   ASN A  17     -15.489  43.489  33.490  1.00 37.88           O  
ANISOU   15  O   ASN A  17     4675   4165   5552    204    628  -1144       O  
ATOM     16  N   PHE A  18     -16.403  42.068  34.972  1.00 48.08           N  
ANISOU   16  N   PHE A  18     5968   5502   6798    225    671  -1145       N  
ATOM     17  CA  PHE A  18     -15.315  41.109  34.863  1.00 47.97           C  
ANISOU   17  CA  PHE A  18     5951   5501   6774    192    654  -1141       C  
ATOM     18  CB  PHE A  18     -15.343  40.131  36.031  1.00 53.71           C  
ANISOU   18  CB  PHE A  18     6696   6252   7459    198    672  -1145       C  
ATOM     19  CG  PHE A  18     -14.195  39.172  36.035  1.00 56.20           C  
ANISOU   19  CG  PHE A  18     7017   6580   7756    172    653  -1143       C  
ATOM     20  CD1 PHE A  18     -12.936  39.584  36.446  1.00 54.36           C  
ANISOU   20  CD1 PHE A  18     6813   6336   7505    163    623  -1161       C  
ATOM     21  CE1 PHE A  18     -11.872  38.700  36.451  1.00 55.55           C  
ANISOU   21  CE1 PHE A  18     6967   6504   7635    144    605  -1160       C  
ATOM     22  CZ  PHE A  18     -12.059  37.390  36.039  1.00 47.97           C  
ANISOU   22  CZ  PHE A  18     5987   5568   6673    134    617  -1139       C  
ATOM     23  CE2 PHE A  18     -13.307  36.971  35.624  1.00 50.70           C  
ANISOU   23  CE2 PHE A  18     6306   5919   7037    138    647  -1121       C  
ATOM     24  CD2 PHE A  18     -14.368  37.859  35.621  1.00 56.05           C  
ANISOU   24  CD2 PHE A  18     6975   6585   7736    157    665  -1124       C  
ATOM     25  C   PHE A  18     -15.367  40.339  33.544  1.00 45.96           C  
ANISOU   25  C   PHE A  18     5651   5260   6551    167    652  -1117       C  
ATOM     26  O   PHE A  18     -14.324  40.027  32.958  1.00 34.39           O  
ANISOU   26  O   PHE A  18     4180   3794   5093    140    626  -1112       O  
ATOM     27  N   ASP A  19     -16.571  40.020  33.080  1.00 39.12           N  
ANISOU   27  N   ASP A  19     4752   4407   5704    177    678  -1102       N  
ATOM     28  CA  ASP A  19     -16.715  39.367  31.782  1.00 39.61           C  
ANISOU   28  CA  ASP A  19     4772   4480   5798    156    674  -1080       C  
ATOM     29  CB  ASP A  19     -18.170  38.966  31.514  1.00 44.72           C  
ANISOU   29  CB  ASP A  19     5384   5148   6460    168    708  -1069       C  
ATOM     30  CG  ASP A  19     -18.575  37.697  32.247  1.00 49.88           C  
ANISOU   30  CG  ASP A  19     6036   5828   7086    161    736  -1067       C  
ATOM     31  OD1 ASP A  19     -17.703  37.056  32.872  1.00 44.63           O  
ANISOU   31  OD1 ASP A  19     5399   5166   6392    149    728  -1072       O  
ATOM     32  OD2 ASP A  19     -19.772  37.336  32.194  1.00 61.27           O  
ANISOU   32  OD2 ASP A  19     7451   7291   8538    169    768  -1061       O  
ATOM     33  C   ASP A  19     -16.208  40.303  30.691  1.00 33.15           C  
ANISOU   33  C   ASP A  19     3945   3638   5014    148    646  -1076       C  
ATOM     34  O   ASP A  19     -15.537  39.870  29.745  1.00 32.42           O  
ANISOU   34  O   ASP A  19     3833   3546   4938    123    627  -1064       O  
ATOM     35  N   GLN A  20     -16.505  41.590  30.833  1.00 27.96           N  
ANISOU   35  N   GLN A  20     3306   2956   4363    171    644  -1087       N  
ATOM     36  CA  GLN A  20     -16.047  42.567  29.856  1.00 31.10           C  
ANISOU   36  CA  GLN A  20     3701   3324   4789    165    620  -1084       C  
ATOM     37  CB  GLN A  20     -16.710  43.926  30.093  1.00 45.77           C  
ANISOU   37  CB  GLN A  20     5584   5157   6651    199    625  -1095       C  
ATOM     38  CG  GLN A  20     -16.688  44.793  28.850  1.00 53.52           C  
ANISOU   38  CG  GLN A  20     6556   6112   7666    200    609  -1085       C  
ATOM     39  CD  GLN A  20     -17.327  44.088  27.666  1.00 61.05           C  
ANISOU   39  CD  GLN A  20     7458   7089   8649    195    616  -1059       C  
ATOM     40  OE1 GLN A  20     -18.396  43.489  27.792  1.00 67.16           O  
ANISOU   40  OE1 GLN A  20     8206   7892   9421    211    641  -1052       O  
ATOM     41  NE2 GLN A  20     -16.662  44.133  26.517  1.00 61.78           N  
ANISOU   41  NE2 GLN A  20     7535   7171   8769    172    594  -1046       N  
ATOM     42  C   GLN A  20     -14.526  42.718  29.879  1.00 33.22           C  
ANISOU   42  C   GLN A  20     3992   3579   5052    136    589  -1094       C  
ATOM     43  O   GLN A  20     -13.893  42.891  28.836  1.00 37.79           O  
ANISOU   43  O   GLN A  20     4556   4147   5656    115    568  -1085       O  
ATOM     44  N   GLU A  21     -13.945  42.639  31.069  1.00 30.82           N  
ANISOU   44  N   GLU A  21     3722   3276   4713    136    586  -1114       N  
ATOM     45  CA  GLU A  21     -12.496  42.685  31.204  1.00 29.80           C  
ANISOU   45  CA  GLU A  21     3610   3141   4573    108    557  -1127       C  
ATOM     46  CB  GLU A  21     -12.093  42.697  32.677  1.00 34.47           C  
ANISOU   46  CB  GLU A  21     4241   3734   5121    117    558  -1151       C  
ATOM     47  CG  GLU A  21     -10.640  43.073  32.912  1.00 47.04           C  
ANISOU   47  CG  GLU A  21     5855   5316   6702     91    526  -1171       C  
ATOM     48  CD  GLU A  21     -10.218  42.959  34.371  1.00 58.43           C  
ANISOU   48  CD  GLU A  21     7337   6766   8099    101    525  -1195       C  
ATOM     49  OE1 GLU A  21     -11.097  42.756  35.238  1.00 56.06           O  
ANISOU   49  OE1 GLU A  21     7052   6473   7777    130    549  -1196       O  
ATOM     50  OE2 GLU A  21      -9.001  43.072  34.645  1.00 61.15           O  
ANISOU   50  OE2 GLU A  21     7695   7110   8429     79    499  -1213       O  
ATOM     51  C   GLU A  21     -11.863  41.481  30.490  1.00 25.98           C  
ANISOU   51  C   GLU A  21     3094   2683   4093     82    548  -1110       C  
ATOM     52  O   GLU A  21     -10.828  41.610  29.828  1.00 25.27           O  
ANISOU   52  O   GLU A  21     2996   2588   4016     58    523  -1111       O  
ATOM     53  N   ALA A  22     -12.493  40.317  30.639  1.00 23.56           N  
ANISOU   53  N   ALA A  22     2772   2405   3776     88    569  -1097       N  
ATOM     54  CA  ALA A  22     -11.986  39.089  30.021  1.00 21.49           C  
ANISOU   54  CA  ALA A  22     2487   2166   3512     69    562  -1082       C  
ATOM     55  CB  ALA A  22     -12.732  37.899  30.561  1.00 22.51           C  
ANISOU   55  CB  ALA A  22     2615   2321   3619     77    589  -1073       C  
ATOM     56  C   ALA A  22     -12.086  39.132  28.495  1.00 28.01           C  
ANISOU   56  C   ALA A  22     3275   2988   4380     57    552  -1061       C  
ATOM     57  O   ALA A  22     -11.171  38.708  27.790  1.00 22.46           O  
ANISOU   57  O   ALA A  22     2560   2292   3683     37    532  -1054       O  
ATOM     58  N   LEU A  23     -13.204  39.629  27.978  1.00 22.52           N  
ANISOU   58  N   LEU A  23     2562   2283   3712     71    567  -1051       N  
ATOM     59  CA  LEU A  23     -13.369  39.742  26.530  1.00 23.52           C  
ANISOU   59  CA  LEU A  23     2655   2404   3878     64    558  -1031       C  
ATOM     60  CB  LEU A  23     -14.778  40.260  26.186  1.00 23.67           C  
ANISOU   60  CB  LEU A  23     2656   2417   3918     88    579  -1022       C  
ATOM     61  CG  LEU A  23     -15.920  39.269  26.464  1.00 25.05           C  
ANISOU   61  CG  LEU A  23     2812   2620   4086     97    608  -1015       C  
ATOM     62  CD1 LEU A  23     -17.285  39.931  26.249  1.00 31.50           C  
ANISOU   62  CD1 LEU A  23     3613   3436   4922    124    628  -1011       C  
ATOM     63  CD2 LEU A  23     -15.826  37.954  25.667  1.00 22.49           C  
ANISOU   63  CD2 LEU A  23     2459   2317   3769     76    606   -996       C  
ATOM     64  C   LEU A  23     -12.294  40.656  25.937  1.00 30.70           C  
ANISOU   64  C   LEU A  23     3571   3290   4805     49    530  -1036       C  
ATOM     65  O   LEU A  23     -11.657  40.305  24.934  1.00 25.49           O  
ANISOU   65  O   LEU A  23     2889   2635   4161     32    513  -1023       O  
ATOM     66  N   LEU A  24     -12.086  41.811  26.565  1.00 27.22           N  
ANISOU   66  N   LEU A  24     3162   2823   4358     56    525  -1055       N  
ATOM     67  CA  LEU A  24     -11.077  42.761  26.108  1.00 26.88           C  
ANISOU   67  CA  LEU A  24     3130   2753   4330     37    500  -1064       C  
ATOM     68  CB  LEU A  24     -11.154  44.069  26.897  1.00 27.54           C  
ANISOU   68  CB  LEU A  24     3256   2804   4405     48    500  -1086       C  
ATOM     69  CG  LEU A  24     -12.459  44.843  26.703  1.00 43.26           C  
ANISOU   69  CG  LEU A  24     5251   4776   6410     81    518  -1079       C  
ATOM     70  CD1 LEU A  24     -12.428  46.173  27.437  1.00 47.90           C  
ANISOU   70  CD1 LEU A  24     5888   5327   6987     94    514  -1101       C  
ATOM     71  CD2 LEU A  24     -12.747  45.037  25.217  1.00 49.93           C  
ANISOU   71  CD2 LEU A  24     6065   5613   7293     80    513  -1055       C  
ATOM     72  C   LEU A  24      -9.670  42.174  26.212  1.00 26.61           C  
ANISOU   72  C   LEU A  24     3095   2734   4280      9    479  -1073       C  
ATOM     73  O   LEU A  24      -8.849  42.390  25.330  1.00 26.67           O  
ANISOU   73  O   LEU A  24     3090   2736   4308    -13    460  -1069       O  
ATOM     74  N   TYR A  25      -9.401  41.442  27.292  1.00 23.05           N  
ANISOU   74  N   TYR A  25     2660   2306   3792     11    484  -1086       N  
ATOM     75  CA  TYR A  25      -8.122  40.764  27.457  1.00 25.13           C  
ANISOU   75  CA  TYR A  25     2923   2592   4035    -10    464  -1097       C  
ATOM     76  CB  TYR A  25      -8.142  39.897  28.725  1.00 24.69           C  
ANISOU   76  CB  TYR A  25     2888   2560   3933      2    475  -1107       C  
ATOM     77  CG  TYR A  25      -6.871  39.089  28.970  1.00 25.45           C  
ANISOU   77  CG  TYR A  25     2987   2684   4000    -11    456  -1119       C  
ATOM     78  CD2 TYR A  25      -6.728  37.812  28.442  1.00 23.06           C  
ANISOU   78  CD2 TYR A  25     2664   2408   3688    -11    456  -1101       C  
ATOM     79  CE2 TYR A  25      -5.581  37.060  28.662  1.00 26.97           C  
ANISOU   79  CE2 TYR A  25     3163   2931   4152    -17    439  -1112       C  
ATOM     80  CZ  TYR A  25      -4.558  37.579  29.431  1.00 22.66           C  
ANISOU   80  CZ  TYR A  25     2636   2389   3585    -26    421  -1143       C  
ATOM     81  OH  TYR A  25      -3.419  36.820  29.652  1.00 25.44           O  
ANISOU   81  OH  TYR A  25     2989   2774   3903    -28    403  -1157       O  
ATOM     82  CE1 TYR A  25      -4.678  38.845  29.980  1.00 25.20           C  
ANISOU   82  CE1 TYR A  25     2977   2682   3916    -31    419  -1162       C  
ATOM     83  CD1 TYR A  25      -5.829  39.596  29.751  1.00 26.55           C  
ANISOU   83  CD1 TYR A  25     3148   2822   4116    -22    437  -1149       C  
ATOM     84  C   TYR A  25      -7.802  39.918  26.222  1.00 23.18           C  
ANISOU   84  C   TYR A  25     2640   2363   3806    -21    456  -1075       C  
ATOM     85  O   TYR A  25      -6.679  39.961  25.714  1.00 21.47           O  
ANISOU   85  O   TYR A  25     2412   2150   3594    -42    433  -1081       O  
ATOM     86  N   HIS A  26      -8.804  39.187  25.726  1.00 19.62           N  
ANISOU   86  N   HIS A  26     2168   1922   3364     -8    473  -1051       N  
ATOM     87  CA  HIS A  26      -8.620  38.271  24.595  1.00 19.91           C  
ANISOU   87  CA  HIS A  26     2174   1977   3415    -15    466  -1029       C  
ATOM     88  CB  HIS A  26      -9.740  37.213  24.571  1.00 22.19           C  
ANISOU   88  CB  HIS A  26     2453   2283   3697     -1    488  -1010       C  
ATOM     89  CG  HIS A  26      -9.583  36.157  25.618  1.00 20.71           C  
ANISOU   89  CG  HIS A  26     2287   2117   3464      3    497  -1017       C  
ATOM     90  ND1 HIS A  26      -9.919  36.362  26.942  1.00 19.31           N  
ANISOU   90  ND1 HIS A  26     2139   1938   3260     14    513  -1034       N  
ATOM     91  CE1 HIS A  26      -9.644  35.261  27.627  1.00 17.37           C  
ANISOU   91  CE1 HIS A  26     1912   1714   2975     17    518  -1035       C  
ATOM     92  NE2 HIS A  26      -9.162  34.356  26.794  1.00 20.75           N  
ANISOU   92  NE2 HIS A  26     2325   2157   3403      9    506  -1021       N  
ATOM     93  CD2 HIS A  26      -9.107  34.893  25.533  1.00 19.24           C  
ANISOU   93  CD2 HIS A  26     2103   1955   3254      0    493  -1010       C  
ATOM     94  C   HIS A  26      -8.591  38.983  23.253  1.00 23.60           C  
ANISOU   94  C   HIS A  26     2617   2425   3926    -22    455  -1015       C  
ATOM     95  O   HIS A  26      -7.898  38.563  22.319  1.00 25.50           O  
ANISOU   95  O   HIS A  26     2836   2675   4177    -33    439  -1005       O  
ATOM     96  N   GLN A  27      -9.380  40.044  23.163  1.00 25.61           N  
ANISOU   96  N   GLN A  27     2876   2652   4202    -12    464  -1013       N  
ATOM     97  CA  GLN A  27      -9.619  40.747  21.909  1.00 23.97           C  
ANISOU   97  CA  GLN A  27     2649   2424   4034    -12    458   -996       C  
ATOM     98  CB  GLN A  27     -11.003  41.414  21.960  1.00 27.51           C  
ANISOU   98  CB  GLN A  27     3101   2857   4496     13    478   -990       C  
ATOM     99  CG  GLN A  27     -11.444  42.079  20.675  1.00 37.11           C  
ANISOU   99  CG  GLN A  27     4299   4054   5749     20    473   -971       C  
ATOM    100  CD  GLN A  27     -12.836  42.682  20.796  1.00 54.20           C  
ANISOU  100  CD  GLN A  27     6466   6208   7920     50    493   -968       C  
ATOM    101  OE1 GLN A  27     -13.174  43.288  21.816  1.00 52.32           O  
ANISOU  101  OE1 GLN A  27     6257   5958   7665     64    504   -986       O  
ATOM    102  NE2 GLN A  27     -13.655  42.504  19.763  1.00 63.07           N  
ANISOU  102  NE2 GLN A  27     7560   7338   9066     64    497   -946       N  
ATOM    103  C   GLN A  27      -8.565  41.803  21.579  1.00 22.94           C  
ANISOU  103  C   GLN A  27     2530   2268   3919    -33    437  -1008       C  
ATOM    104  O   GLN A  27      -8.259  42.020  20.405  1.00 29.98           O  
ANISOU  104  O   GLN A  27     3402   3151   4839    -42    426   -993       O  
ATOM    105  N   GLN A  28      -8.033  42.460  22.615  1.00 25.85           N  
ANISOU  105  N   GLN A  28     2930   2623   4267    -42    433  -1035       N  
ATOM    106  CA  GLN A  28      -7.074  43.559  22.470  1.00 30.17           C  
ANISOU  106  CA  GLN A  28     3495   3143   4826    -68    414  -1050       C  
ATOM    107  CB  GLN A  28      -6.902  44.295  23.807  1.00 30.79           C  
ANISOU  107  CB  GLN A  28     3615   3205   4878    -70    414  -1079       C  
ATOM    108  CG  GLN A  28      -5.697  43.784  24.617  1.00 53.84           C  
ANISOU  108  CG  GLN A  28     6541   6150   7766    -92    399  -1104       C  
ATOM    109  CD  GLN A  28      -5.742  44.133  26.102  1.00 65.13           C  
ANISOU  109  CD  GLN A  28     8009   7574   9162    -84    402  -1131       C  
ATOM    110  OE1 GLN A  28      -6.759  44.600  26.624  1.00 59.36           O  
ANISOU  110  OE1 GLN A  28     7302   6826   8428    -58    420  -1130       O  
ATOM    111  NE2 GLN A  28      -4.629  43.894  26.790  1.00 70.16           N  
ANISOU  111  NE2 GLN A  28     8655   8230   9773   -105    386  -1156       N  
ATOM    112  C   GLN A  28      -5.706  43.085  21.985  1.00 30.59           C  
ANISOU  112  C   GLN A  28     3528   3215   4879    -98    392  -1055       C  
ATOM    113  O   GLN A  28      -5.354  41.923  22.151  1.00 31.38           O  
ANISOU  113  O   GLN A  28     3613   3351   4960    -96    390  -1056       O  
ATOM    114  N   GLY A  29      -4.924  43.995  21.412  1.00 28.69           N  
ANISOU  114  N   GLY A  29     3291   2951   4659   -127    375  -1059       N  
ATOM    115  CA  GLY A  29      -3.610  43.644  20.909  1.00 25.31           C  
ANISOU  115  CA  GLY A  29     2842   2543   4233   -159    353  -1065       C  
ATOM    116  C   GLY A  29      -3.675  42.567  19.844  1.00 26.55           C  
ANISOU  116  C   GLY A  29     2960   2725   4404   -148    353  -1041       C  
ATOM    117  O   GLY A  29      -4.493  42.620  18.929  1.00 30.72           O  
ANISOU  117  O   GLY A  29     3474   3240   4958   -129    363  -1014       O  
ATOM    118  N   LYS A  30      -2.803  41.577  19.958  1.00 27.31           N  
ANISOU  118  N   LYS A  30     3039   2858   4478   -156    342  -1052       N  
ATOM    119  CA  LYS A  30      -2.868  40.431  19.071  1.00 22.06           C  
ANISOU  119  CA  LYS A  30     2344   2229   3810   -139    339  -1020       C  
ATOM    120  CB  LYS A  30      -1.549  39.653  19.109  1.00 33.75           C  
ANISOU  120  CB  LYS A  30     3809   3764   5251   -153    314  -1015       C  
ATOM    121  CG  LYS A  30      -1.469  38.517  18.122  1.00 46.44           C  
ANISOU  121  CG  LYS A  30     5388   5407   6850   -135    306   -981       C  
ATOM    122  CD  LYS A  30      -0.100  37.851  18.169  1.00 47.72           C  
ANISOU  122  CD  LYS A  30     5536   5626   6969   -145    281   -978       C  
ATOM    123  CE  LYS A  30       0.023  36.788  17.087  1.00 48.40           C  
ANISOU  123  CE  LYS A  30     5599   5745   7047   -125    272   -942       C  
ATOM    124  NZ  LYS A  30      -0.826  35.571  17.337  1.00 49.55           N  
ANISOU  124  NZ  LYS A  30     5757   5893   7175    -91    287   -937       N  
ATOM    125  C   LYS A  30      -4.054  39.575  19.547  1.00 23.75           C  
ANISOU  125  C   LYS A  30     2564   2445   4014   -104    363  -1018       C  
ATOM    126  O   LYS A  30      -4.089  39.185  20.711  1.00 25.16           O  
ANISOU  126  O   LYS A  30     2763   2638   4157    -97    369  -1034       O  
ATOM    127  N   PRO A  31      -5.053  39.325  18.678  1.00 23.97           N  
ANISOU  127  N   PRO A  31     2575   2467   4064    -85    374   -987       N  
ATOM    128  CA  PRO A  31      -6.185  38.482  19.122  1.00 22.67           C  
ANISOU  128  CA  PRO A  31     2414   2317   3882    -61    393   -974       C  
ATOM    129  CB  PRO A  31      -6.981  38.242  17.833  1.00 23.08           C  
ANISOU  129  CB  PRO A  31     2439   2365   3963    -48    397   -942       C  
ATOM    130  CG  PRO A  31      -6.610  39.414  16.956  1.00 27.07           C  
ANISOU  130  CG  PRO A  31     2938   2842   4506    -59    386   -938       C  
ATOM    131  CD  PRO A  31      -5.183  39.733  17.271  1.00 28.54           C  
ANISOU  131  CD  PRO A  31     3132   3028   4683    -86    368   -963       C  
ATOM    132  C   PRO A  31      -5.723  37.148  19.722  1.00 18.36           C  
ANISOU  132  C   PRO A  31     1875   1807   3295    -56    392   -981       C  
ATOM    133  O   PRO A  31      -4.795  36.529  19.210  1.00 20.93           O  
ANISOU  133  O   PRO A  31     2188   2152   3614    -60    375   -982       O  
ATOM    134  N   GLY A  32      -6.387  36.693  20.780  1.00 20.19           N  
ANISOU  134  N   GLY A  32     2127   2047   3499    -44    409   -985       N  
ATOM    135  CA  GLY A  32      -6.025  35.425  21.382  1.00 20.27           C  
ANISOU  135  CA  GLY A  32     2149   2087   3465    -37    409   -989       C  
ATOM    136  C   GLY A  32      -4.874  35.610  22.353  1.00 18.49           C  
ANISOU  136  C   GLY A  32     1944   1874   3209    -46    396  -1021       C  
ATOM    137  O   GLY A  32      -4.556  36.737  22.729  1.00 22.60           O  
ANISOU  137  O   GLY A  32     2471   2375   3740    -59    391  -1041       O  
ATOM    138  N   LYS A  33      -4.250  34.503  22.755  1.00 17.41           N  
ANISOU  138  N   LYS A  33     1818   1767   3030    -37    390  -1027       N  
ATOM    139  CA  LYS A  33      -3.297  34.572  23.855  1.00 19.15           C  
ANISOU  139  CA  LYS A  33     2060   2004   3213    -40    380  -1059       C  
ATOM    140  CB  LYS A  33      -3.851  33.850  25.079  1.00 17.98           C  
ANISOU  140  CB  LYS A  33     1945   1865   3022    -23    398  -1059       C  
ATOM    141  CG  LYS A  33      -5.034  34.581  25.699  1.00 17.84           C  
ANISOU  141  CG  LYS A  33     1939   1819   3018    -21    421  -1056       C  
ATOM    142  CD  LYS A  33      -5.650  33.758  26.824  1.00 16.88           C  
ANISOU  142  CD  LYS A  33     1850   1708   2856     -4    441  -1054       C  
ATOM    143  CE  LYS A  33      -6.249  32.444  26.313  1.00 21.15           C  
ANISOU  143  CE  LYS A  33     2388   2260   3388      4    453  -1027       C  
ATOM    144  NZ  LYS A  33      -7.438  32.017  27.109  1.00 20.28           N  
ANISOU  144  NZ  LYS A  33     2298   2145   3264     13    484  -1020       N  
ATOM    145  C   LYS A  33      -1.950  33.976  23.506  1.00 21.45           C  
ANISOU  145  C   LYS A  33     2340   2332   3479    -41    355  -1065       C  
ATOM    146  O   LYS A  33      -1.055  33.998  24.332  1.00 22.68           O  
ANISOU  146  O   LYS A  33     2508   2511   3597    -43    341  -1088       O  
ATOM    147  N   ILE A  34      -1.813  33.423  22.309  1.00 15.34           N  
ANISOU  147  N   ILE A  34     1542   1573   2712    -38    343  -1033       N  
ATOM    148  CA  ILE A  34      -0.543  32.756  21.963  1.00 18.80           C  
ANISOU  148  CA  ILE A  34     1971   2061   3111    -34    314  -1022       C  
ATOM    149  CB  ILE A  34      -0.712  31.239  21.824  1.00 23.19           C  
ANISOU  149  CB  ILE A  34     2543   2638   3631     -5    317  -1003       C  
ATOM    150  CG1 ILE A  34      -1.683  30.883  20.689  1.00 18.60           C  
ANISOU  150  CG1 ILE A  34     1948   2035   3085     -1    327   -972       C  
ATOM    151  CD1 ILE A  34      -1.029  30.373  19.413  1.00 30.14           C  
ANISOU  151  CD1 ILE A  34     3386   3524   4540      5    303   -940       C  
ATOM    152  CG2 ILE A  34      -1.209  30.652  23.146  1.00 23.92           C  
ANISOU  152  CG2 ILE A  34     2675   2723   3689     11    339  -1025       C  
ATOM    153  C   ILE A  34       0.074  33.305  20.704  1.00 20.98           C  
ANISOU  153  C   ILE A  34     2210   2347   3414    -51    291   -999       C  
ATOM    154  O   ILE A  34      -0.594  33.910  19.858  1.00 20.73           O  
ANISOU  154  O   ILE A  34     2162   2284   3431    -61    299   -983       O  
ATOM    155  N   GLU A  35       1.383  33.121  20.629  1.00 19.44           N  
ANISOU  155  N   GLU A  35     2002   2199   3185    -55    264   -999       N  
ATOM    156  CA  GLU A  35       2.195  33.528  19.501  1.00 20.56           C  
ANISOU  156  CA  GLU A  35     2108   2364   3341    -71    241   -977       C  
ATOM    157  CB  GLU A  35       2.820  34.906  19.761  1.00 21.75           C  
ANISOU  157  CB  GLU A  35     2246   2507   3511   -111    231   -997       C  
ATOM    158  CG  GLU A  35       3.692  35.383  18.646  1.00 37.99           C  
ANISOU  158  CG  GLU A  35     4266   4589   5582   -133    209   -974       C  
ATOM    159  CD  GLU A  35       4.153  36.814  18.826  1.00 45.76           C  
ANISOU  159  CD  GLU A  35     5243   5554   6590   -179    202   -992       C  
ATOM    160  OE1 GLU A  35       3.786  37.449  19.839  1.00 55.56           O  
ANISOU  160  OE1 GLU A  35     6510   6763   7838   -190    213  -1024       O  
ATOM    161  OE2 GLU A  35       4.890  37.294  17.943  1.00 44.90           O  
ANISOU  161  OE2 GLU A  35     5103   5464   6493   -204    186   -974       O  
ATOM    162  C   GLU A  35       3.262  32.451  19.332  1.00 20.27           C  
ANISOU  162  C   GLU A  35     2063   2388   3249    -49    218   -965       C  
ATOM    163  O   GLU A  35       3.749  31.910  20.336  1.00 20.97           O  
ANISOU  163  O   GLU A  35     2172   2506   3289    -34    214   -987       O  
ATOM    164  N   VAL A  36       3.609  32.105  18.090  1.00 14.87           N  
ANISOU  164  N   VAL A  36     1354   1728   2570    -42    204   -932       N  
ATOM    165  CA  VAL A  36       4.719  31.189  17.846  1.00 15.65           C  
ANISOU  165  CA  VAL A  36     1443   1890   2614    -19    180   -921       C  
ATOM    166  CB  VAL A  36       4.388  30.118  16.788  1.00 14.00           C  
ANISOU  166  CB  VAL A  36     1235   1686   2398     13    179   -885       C  
ATOM    167  CG1 VAL A  36       5.612  29.215  16.542  1.00 20.15           C  
ANISOU  167  CG1 VAL A  36     2005   2534   3116     43    152   -874       C  
ATOM    168  CG2 VAL A  36       3.145  29.308  17.200  1.00 14.77           C  
ANISOU  168  CG2 VAL A  36     1373   1744   2496     34    203   -887       C  
ATOM    169  C   VAL A  36       5.920  31.999  17.369  1.00 22.73           C  
ANISOU  169  C   VAL A  36     2298   2826   3513    -47    157   -917       C  
ATOM    170  O   VAL A  36       5.798  32.769  16.419  1.00 23.45           O  
ANISOU  170  O   VAL A  36     2363   2898   3648    -71    157   -899       O  
ATOM    171  N   ILE A  37       7.067  31.848  18.032  1.00 16.43           N  
ANISOU  171  N   ILE A  37     1492   2084   2665    -45    138   -936       N  
ATOM    172  CA  ILE A  37       8.262  32.594  17.638  1.00 18.24           C  
ANISOU  172  CA  ILE A  37     1678   2360   2893    -76    115   -934       C  
ATOM    173  CB  ILE A  37       8.683  33.634  18.699  1.00 18.02           C  
ANISOU  173  CB  ILE A  37     1651   2329   2868   -117    111   -972       C  
ATOM    174  CG1 ILE A  37       9.054  32.921  19.997  1.00 21.32           C  
ANISOU  174  CG1 ILE A  37     2094   2780   3228    -89    106  -1003       C  
ATOM    175  CD1 ILE A  37       9.604  33.853  21.069  1.00 30.05           C  
ANISOU  175  CD1 ILE A  37     3198   3893   4327   -126     97  -1043       C  
ATOM    176  CG2 ILE A  37       7.549  34.658  18.962  1.00 18.81           C  
ANISOU  176  CG2 ILE A  37     1774   2348   3027   -146    135   -985       C  
ATOM    177  C   ILE A  37       9.448  31.673  17.396  1.00 20.31           C  
ANISOU  177  C   ILE A  37     1919   2703   3093    -45     90   -923       C  
ATOM    178  O   ILE A  37       9.443  30.512  17.791  1.00 18.62           O  
ANISOU  178  O   ILE A  37     1732   2510   2832      1     89   -924       O  
ATOM    179  N   SER A  38      10.467  32.207  16.739  1.00 17.10           N  
ANISOU  179  N   SER A  38     1694   2015   2789   -269    -31   -167       N  
ATOM    180  CA  SER A  38      11.683  31.443  16.534  1.00 18.78           C  
ANISOU  180  CA  SER A  38     1875   2294   2965   -230    -26   -188       C  
ATOM    181  CB  SER A  38      12.483  31.995  15.357  1.00 21.90           C  
ANISOU  181  CB  SER A  38     2248   2725   3347   -262     -3   -191       C  
ATOM    182  OG  SER A  38      13.647  31.197  15.144  1.00 24.14           O  
ANISOU  182  OG  SER A  38     2503   3074   3595   -221      2   -212       O  
ATOM    183  C   SER A  38      12.536  31.466  17.786  1.00 18.89           C  
ANISOU  183  C   SER A  38     1844   2361   2973   -216    -29   -216       C  
ATOM    184  O   SER A  38      12.670  32.501  18.430  1.00 24.00           O  
ANISOU  184  O   SER A  38     2465   3016   3639   -256    -23   -224       O  
ATOM    185  N   SER A  39      13.144  30.329  18.105  1.00 18.45           N  
ANISOU  185  N   SER A  39     1779   2343   2890   -159    -38   -231       N  
ATOM    186  CA  SER A  39      14.094  30.270  19.214  1.00 18.12           C  
ANISOU  186  CA  SER A  39     1690   2358   2836   -141    -40   -260       C  
ATOM    187  CB  SER A  39      13.973  28.939  19.954  1.00 22.05           C  
ANISOU  187  CB  SER A  39     2202   2856   3320    -76    -62   -265       C  
ATOM    188  OG  SER A  39      14.326  27.849  19.109  1.00 21.12           O  
ANISOU  188  OG  SER A  39     2097   2755   3174    -32    -63   -264       O  
ATOM    189  C   SER A  39      15.536  30.454  18.729  1.00 22.45           C  
ANISOU  189  C   SER A  39     2189   2981   3358   -146    -20   -282       C  
ATOM    190  O   SER A  39      16.460  30.413  19.537  1.00 25.16           O  
ANISOU  190  O   SER A  39     2491   3379   3690   -132    -20   -307       O  
ATOM    191  N   LYS A  40      15.711  30.646  17.420  1.00 19.88           N  
ANISOU  191  N   LYS A  40     1871   2659   3025   -165     -5   -274       N  
ATOM    192  CA  LYS A  40      17.033  30.738  16.780  1.00 17.76           C  
ANISOU  192  CA  LYS A  40     1559   2459   2728   -167     14   -293       C  
ATOM    193  CB  LYS A  40      17.351  29.467  15.970  1.00 19.71           C  
ANISOU  193  CB  LYS A  40     1822   2724   2945   -115     11   -294       C  
ATOM    194  CG  LYS A  40      17.204  28.135  16.693  1.00 23.78           C  
ANISOU  194  CG  LYS A  40     2352   3236   3447    -48    -12   -299       C  
ATOM    195  CD  LYS A  40      18.247  27.979  17.790  1.00 22.95           C  
ANISOU  195  CD  LYS A  40     2199   3194   3328    -26    -14   -329       C  
ATOM    196  CE  LYS A  40      17.790  26.932  18.800  1.00 22.51           C  
ANISOU  196  CE  LYS A  40     2163   3119   3272     28    -39   -330       C  
ATOM    197  NZ  LYS A  40      18.120  25.571  18.344  1.00 24.74           N  
ANISOU  197  NZ  LYS A  40     2456   3419   3525     88    -48   -334       N  
ATOM    198  C   LYS A  40      17.096  31.942  15.843  1.00 20.25           C  
ANISOU  198  C   LYS A  40     1867   2771   3055   -230     35   -284       C  
ATOM    199  O   LYS A  40      16.068  32.398  15.339  1.00 20.18           O  
ANISOU  199  O   LYS A  40     1895   2702   3069   -261     35   -259       O  
ATOM    200  N   PRO A  41      18.310  32.462  15.586  1.00 17.15           N  
ANISOU  200  N   PRO A  41     1427   2443   2647   -250     54   -304       N  
ATOM    201  CA  PRO A  41      18.432  33.572  14.633  1.00 21.65           C  
ANISOU  201  CA  PRO A  41     1988   3013   3225   -310     74   -296       C  
ATOM    202  CB  PRO A  41      19.949  33.743  14.483  1.00 23.26           C  
ANISOU  202  CB  PRO A  41     2136   3300   3402   -311     92   -323       C  
ATOM    203  CG  PRO A  41      20.514  33.167  15.726  1.00 21.79           C  
ANISOU  203  CG  PRO A  41     1922   3151   3205   -270     80   -347       C  
ATOM    204  CD  PRO A  41      19.607  32.095  16.197  1.00 17.95           C  
ANISOU  204  CD  PRO A  41     1478   2619   2722   -221     57   -336       C  
ATOM    205  C   PRO A  41      17.807  33.251  13.276  1.00 19.93           C  
ANISOU  205  C   PRO A  41     1812   2756   3003   -311     78   -271       C  
ATOM    206  O   PRO A  41      18.045  32.171  12.731  1.00 22.65           O  
ANISOU  206  O   PRO A  41     2169   3116   3323   -265     74   -273       O  
ATOM    207  N   CYS A  42      17.051  34.183  12.718  1.00 20.03           N  
ANISOU  207  N   CYS A  42     1847   2723   3042   -363     84   -249       N  
ATOM    208  CA  CYS A  42      16.373  33.887  11.456  1.00 25.37           C  
ANISOU  208  CA  CYS A  42     2566   3358   3717   -365     86   -225       C  
ATOM    209  CB  CYS A  42      15.037  33.197  11.744  1.00 22.08           C  
ANISOU  209  CB  CYS A  42     2203   2870   3315   -337     65   -203       C  
ATOM    210  SG  CYS A  42      13.903  34.166  12.774  1.00 27.96           S  
ANISOU  210  SG  CYS A  42     2965   3553   4105   -377     54   -190       S  
ATOM    211  C   CYS A  42      16.164  35.148  10.617  1.00 32.50           C  
ANISOU  211  C   CYS A  42     3470   4242   4637   -433    103   -210       C  
ATOM    212  O   CYS A  42      15.178  35.266   9.886  1.00 27.53           O  
ANISOU  212  O   CYS A  42     2882   3555   4022   -450    101   -183       O  
ATOM    213  N   ALA A  43      17.117  36.066  10.700  1.00 27.13           N  
ANISOU  213  N   ALA A  43     2742   3612   3954   -470    120   -226       N  
ATOM    214  CA  ALA A  43      17.000  37.368  10.046  1.00 34.19           C  
ANISOU  214  CA  ALA A  43     3631   4493   4868   -537    136   -214       C  
ATOM    215  CB  ALA A  43      17.460  38.459  10.999  1.00 39.85           C  
ANISOU  215  CB  ALA A  43     4306   5234   5601   -576    142   -230       C  
ATOM    216  C   ALA A  43      17.774  37.483   8.727  1.00 32.54           C  
ANISOU  216  C   ALA A  43     3406   4322   4634   -553    156   -215       C  
ATOM    217  O   ALA A  43      17.457  38.329   7.890  1.00 39.88           O  
ANISOU  217  O   ALA A  43     4347   5229   5577   -603    167   -198       O  
ATOM    218  N   THR A  44      18.798  36.657   8.544  1.00 26.09           N  
ANISOU  218  N   THR A  44     2564   3566   3782   -512    160   -236       N  
ATOM    219  CA  THR A  44      19.662  36.803   7.374  1.00 29.90           C  
ANISOU  219  CA  THR A  44     3026   4094   4240   -528    180   -240       C  
ATOM    220  CB  THR A  44      21.146  36.927   7.758  1.00 27.41           C  
ANISOU  220  CB  THR A  44     2650   3863   3901   -523    192   -273       C  
ATOM    221  OG1 THR A  44      21.605  35.712   8.375  1.00 21.49           O  
ANISOU  221  OG1 THR A  44     1892   3145   3128   -457    180   -292       O  
ATOM    222  CG2 THR A  44      21.373  38.110   8.707  1.00 26.96           C  
ANISOU  222  CG2 THR A  44     2559   3816   3867   -567    197   -283       C  
ATOM    223  C   THR A  44      19.532  35.636   6.419  1.00 27.16           C  
ANISOU  223  C   THR A  44     2709   3743   3869   -484    177   -232       C  
ATOM    224  O   THR A  44      19.005  34.586   6.770  1.00 23.82           O  
ANISOU  224  O   THR A  44     2314   3294   3442   -434    159   -229       O  
ATOM    225  N   GLU A  45      20.037  35.838   5.207  1.00 27.58           N  
ANISOU  225  N   GLU A  45     2753   3821   3904   -505    194   -230       N  
ATOM    226  CA  GLU A  45      20.156  34.769   4.232  1.00 27.39           C  
ANISOU  226  CA  GLU A  45     2749   3807   3853   -465    195   -227       C  
ATOM    227  CB  GLU A  45      20.913  35.270   2.993  1.00 30.48           C  
ANISOU  227  CB  GLU A  45     3118   4238   4225   -499    218   -228       C  
ATOM    228  CG  GLU A  45      21.054  34.237   1.887  1.00 49.40           C  
ANISOU  228  CG  GLU A  45     5532   6645   6592   -462    220   -224       C  
ATOM    229  CD  GLU A  45      19.902  34.283   0.899  1.00 67.41           C  
ANISOU  229  CD  GLU A  45     7866   8859   8887   -480    218   -191       C  
ATOM    230  OE1 GLU A  45      19.720  35.340   0.256  1.00 73.99           O  
ANISOU  230  OE1 GLU A  45     8701   9678   9735   -539    231   -177       O  
ATOM    231  OE2 GLU A  45      19.182  33.269   0.763  1.00 69.78           O  
ANISOU  231  OE2 GLU A  45     8207   9121   9184   -437    203   -180       O  
ATOM    232  C   GLU A  45      20.879  33.563   4.850  1.00 23.28           C  
ANISOU  232  C   GLU A  45     2209   3331   3304   -398    185   -252       C  
ATOM    233  O   GLU A  45      20.423  32.423   4.726  1.00 23.62           O  
ANISOU  233  O   GLU A  45     2285   3353   3338   -348    171   -246       O  
ATOM    234  N   LYS A  46      21.995  33.822   5.536  1.00 22.18           N  
ANISOU  234  N   LYS A  46     2018   3256   3154   -397    192   -280       N  
ATOM    235  CA  LYS A  46      22.762  32.739   6.160  1.00 24.75           C  
ANISOU  235  CA  LYS A  46     2322   3630   3453   -336    184   -305       C  
ATOM    236  CB  LYS A  46      24.039  33.285   6.798  1.00 29.93           C  
ANISOU  236  CB  LYS A  46     2916   4358   4098   -349    195   -335       C  
ATOM    237  CG  LYS A  46      24.891  32.237   7.512  1.00 36.60           C  
ANISOU  237  CG  LYS A  46     3735   5255   4918   -287    187   -363       C  
ATOM    238  CD  LYS A  46      25.361  31.152   6.561  1.00 34.12           C  
ANISOU  238  CD  LYS A  46     3426   4969   4569   -244    189   -368       C  
ATOM    239  CE  LYS A  46      25.985  29.974   7.304  1.00 49.31           C  
ANISOU  239  CE  LYS A  46     5333   6932   6471   -177    176   -392       C  
ATOM    240  NZ  LYS A  46      27.203  30.354   8.065  1.00 55.82           N  
ANISOU  240  NZ  LYS A  46     6099   7827   7284   -181    184   -422       N  
ATOM    241  C   LYS A  46      21.923  31.985   7.212  1.00 21.73           C  
ANISOU  241  C   LYS A  46     1968   3203   3084   -293    159   -300       C  
ATOM    242  O   LYS A  46      21.889  30.743   7.202  1.00 20.06           O  
ANISOU  242  O   LYS A  46     1775   2993   2855   -235    146   -304       O  
ATOM    243  N   ASP A  47      21.276  32.731   8.113  1.00 18.36           N  
ANISOU  243  N   ASP A  47     1547   2739   2689   -322    152   -293       N  
ATOM    244  CA  ASP A  47      20.389  32.153   9.143  1.00 19.02           C  
ANISOU  244  CA  ASP A  47     1660   2776   2789   -288    128   -286       C  
ATOM    245  CB  ASP A  47      19.597  33.230   9.913  1.00 20.68           C  
ANISOU  245  CB  ASP A  47     1878   2941   3038   -335    124   -275       C  
ATOM    246  CG  ASP A  47      20.464  34.137  10.771  1.00 32.14           C  
ANISOU  246  CG  ASP A  47     3278   4441   4495   -364    133   -297       C  
ATOM    247  OD1 ASP A  47      21.601  33.760  11.099  1.00 25.24           O  
ANISOU  247  OD1 ASP A  47     2362   3633   3595   -338    138   -324       O  
ATOM    248  OD2 ASP A  47      19.966  35.223  11.149  1.00 28.98           O  
ANISOU  248  OD2 ASP A  47     2877   4010   4124   -413    136   -288       O  
ATOM    249  C   ASP A  47      19.376  31.212   8.509  1.00 18.28           C  
ANISOU  249  C   ASP A  47     1624   2627   2696   -256    115   -263       C  
ATOM    250  O   ASP A  47      19.170  30.070   8.957  1.00 19.10           O  
ANISOU  250  O   ASP A  47     1744   2723   2789   -199     98   -266       O  
ATOM    251  N   LEU A  48      18.722  31.706   7.463  1.00 18.54           N  
ANISOU  251  N   LEU A  48     1686   2620   2740   -293    123   -239       N  
ATOM    252  CA  LEU A  48      17.642  30.950   6.847  1.00 20.19           C  
ANISOU  252  CA  LEU A  48     1950   2768   2952   -269    112   -214       C  
ATOM    253  CB  LEU A  48      16.725  31.901   6.062  1.00 20.71           C  
ANISOU  253  CB  LEU A  48     2047   2779   3044   -326    119   -186       C  
ATOM    254  CG  LEU A  48      15.957  32.875   6.970  1.00 19.07           C  
ANISOU  254  CG  LEU A  48     1845   2527   2874   -366    113   -176       C  
ATOM    255  CD1 LEU A  48      15.088  33.830   6.155  1.00 29.59           C  
ANISOU  255  CD1 LEU A  48     3206   3806   4231   -423    120   -148       C  
ATOM    256  CD2 LEU A  48      15.101  32.127   7.991  1.00 21.42           C  
ANISOU  256  CD2 LEU A  48     2173   2782   3185   -325     88   -171       C  
ATOM    257  C   LEU A  48      18.154  29.822   5.955  1.00 19.69           C  
ANISOU  257  C   LEU A  48     1891   2735   2854   -223    113   -220       C  
ATOM    258  O   LEU A  48      17.393  28.919   5.603  1.00 20.61           O  
ANISOU  258  O   LEU A  48     2051   2811   2968   -189    100   -205       O  
ATOM    259  N   SER A  49      19.439  29.854   5.599  1.00 16.72           N  
ANISOU  259  N   SER A  49     1470   2431   2451   -222    129   -243       N  
ATOM    260  CA  SER A  49      20.049  28.737   4.880  1.00 20.82           C  
ANISOU  260  CA  SER A  49     1989   2987   2936   -174    130   -253       C  
ATOM    261  CB  SER A  49      21.374  29.143   4.223  1.00 20.71           C  
ANISOU  261  CB  SER A  49     1925   3045   2896   -193    153   -274       C  
ATOM    262  OG  SER A  49      22.427  29.163   5.171  1.00 23.59           O  
ANISOU  262  OG  SER A  49     2242   3472   3250   -179    154   -303       O  
ATOM    263  C   SER A  49      20.289  27.555   5.812  1.00 19.64           C  
ANISOU  263  C   SER A  49     1835   2854   2772   -108    112   -271       C  
ATOM    264  O   SER A  49      20.581  26.447   5.352  1.00 22.26           O  
ANISOU  264  O   SER A  49     2175   3204   3079    -59    107   -277       O  
ATOM    265  N   LEU A  50      20.169  27.802   7.113  1.00 19.62           N  
ANISOU  265  N   LEU A  50     1821   2847   2787   -107    101   -278       N  
ATOM    266  CA  LEU A  50      20.268  26.739   8.120  1.00 15.02           C  
ANISOU  266  CA  LEU A  50     1238   2273   2195    -46     81   -292       C  
ATOM    267  CB  LEU A  50      21.146  27.197   9.287  1.00 17.79           C  
ANISOU  267  CB  LEU A  50     1538   2675   2546    -51     83   -318       C  
ATOM    268  CG  LEU A  50      22.591  27.581   8.917  1.00 17.93           C  
ANISOU  268  CG  LEU A  50     1501   2773   2540    -65    104   -344       C  
ATOM    269  CD1 LEU A  50      23.304  28.085  10.149  1.00 25.95           C  
ANISOU  269  CD1 LEU A  50     2471   3830   3560    -73    104   -367       C  
ATOM    270  CD2 LEU A  50      23.376  26.402   8.284  1.00 23.74           C  
ANISOU  270  CD2 LEU A  50     2228   3554   3239    -12    105   -359       C  
ATOM    271  C   LEU A  50      18.892  26.343   8.631  1.00 16.21           C  
ANISOU  271  C   LEU A  50     1440   2349   2370    -30     59   -269       C  
ATOM    272  O   LEU A  50      18.600  25.151   8.735  1.00 19.24           O  
ANISOU  272  O   LEU A  50     1850   2719   2743     24     43   -267       O  
ATOM    273  N   ALA A  51      18.056  27.339   8.919  1.00 14.08           N  
ANISOU  273  N   ALA A  51     1185   2031   2132    -79     60   -252       N  
ATOM    274  CA  ALA A  51      16.674  27.092   9.378  1.00 13.62           C  
ANISOU  274  CA  ALA A  51     1177   1897   2100    -70     40   -228       C  
ATOM    275  CB  ALA A  51      16.005  28.429   9.842  1.00 13.42           C  
ANISOU  275  CB  ALA A  51     1154   1833   2110   -131     44   -215       C  
ATOM    276  C   ALA A  51      15.822  26.436   8.292  1.00 16.70           C  
ANISOU  276  C   ALA A  51     1618   2238   2487    -55     35   -204       C  
ATOM    277  O   ALA A  51      14.854  25.704   8.585  1.00 16.96           O  
ANISOU  277  O   ALA A  51     1694   2220   2530    -24     16   -189       O  
ATOM    278  N   TYR A  52      16.142  26.722   7.033  1.00 14.27           N  
ANISOU  278  N   TYR A  52     1308   1946   2168    -79     53   -199       N  
ATOM    279  CA  TYR A  52      15.425  26.097   5.935  1.00 14.89           C  
ANISOU  279  CA  TYR A  52     1433   1983   2242    -64     50   -177       C  
ATOM    280  CB  TYR A  52      14.385  27.063   5.350  1.00 19.10           C  
ANISOU  280  CB  TYR A  52     1998   2455   2804   -121     56   -148       C  
ATOM    281  CG  TYR A  52      13.274  26.343   4.592  1.00 16.68           C  
ANISOU  281  CG  TYR A  52     1750   2087   2501   -101     45   -121       C  
ATOM    282  CD1 TYR A  52      12.426  25.433   5.239  1.00 16.57           C  
ANISOU  282  CD1 TYR A  52     1773   2030   2495    -57     22   -113       C  
ATOM    283  CE1 TYR A  52      11.420  24.768   4.541  1.00 19.52           C  
ANISOU  283  CE1 TYR A  52     2198   2346   2870    -38     12    -88       C  
ATOM    284  CZ  TYR A  52      11.265  25.002   3.186  1.00 24.07           C  
ANISOU  284  CZ  TYR A  52     2792   2912   3443    -63     26    -73       C  
ATOM    285  OH  TYR A  52      10.280  24.355   2.480  1.00 26.38           O  
ANISOU  285  OH  TYR A  52     3137   3149   3738    -46     16    -50       O  
ATOM    286  CE2 TYR A  52      12.091  25.886   2.530  1.00 25.83           C  
ANISOU  286  CE2 TYR A  52     2980   3177   3658   -106     48    -81       C  
ATOM    287  CD2 TYR A  52      13.090  26.553   3.232  1.00 22.53           C  
ANISOU  287  CD2 TYR A  52     2509   2814   3237   -125     58   -105       C  
ATOM    288  C   TYR A  52      16.408  25.589   4.877  1.00 20.12           C  
ANISOU  288  C   TYR A  52     2075   2699   2869    -46     64   -190       C  
ATOM    289  O   TYR A  52      17.542  25.278   5.205  1.00 18.22           O  
ANISOU  289  O   TYR A  52     1794   2523   2606    -22     68   -217       O  
ATOM    290  N   SER A  53      15.989  25.469   3.621  1.00 21.75           N  
ANISOU  290  N   SER A  53     2312   2881   3072    -55     70   -171       N  
ATOM    291  C   SER A  53      18.077  25.761   2.315  1.00 21.46           C  
ANISOU  291  C   SER A  53     2206   2960   2988    -71    105   -203       C  
ATOM    292  O   SER A  53      17.967  26.983   2.268  1.00 27.02           O  
ANISOU  292  O   SER A  53     2899   3655   3711   -129    117   -195       O  
ATOM    293  CA ASER A  53      16.855  24.885   2.595  0.45 21.90           C  
ANISOU  293  CA ASER A  53     2316   2949   3057    -33     82   -183       C  
ATOM    294  CB ASER A  53      16.062  24.654   1.310  0.45 25.13           C  
ANISOU  294  CB ASER A  53     2770   3311   3465    -40     84   -157       C  
ATOM    295  OG ASER A  53      15.620  25.883   0.769  0.45 28.76           O  
ANISOU  295  OG ASER A  53     3237   3744   3947   -106     98   -139       O  
ATOM    296  CA BSER A  53      16.846  24.887   2.582  0.55 21.66           C  
ANISOU  296  CA BSER A  53     2286   2917   3026    -34     82   -183       C  
ATOM    297  CB BSER A  53      16.041  24.684   1.292  0.55 25.06           C  
ANISOU  297  CB BSER A  53     2762   3301   3457    -42     84   -157       C  
ATOM    298  OG BSER A  53      16.709  23.820   0.386  0.55 22.91           O  
ANISOU  298  OG BSER A  53     2485   3068   3153     -7     90   -167       O  
ATOM    299  N   PRO A  54      19.253  25.137   2.112  1.00 24.31           N  
ANISOU  299  N   PRO A  54     2532   3388   3316    -37    111   -228       N  
ATOM    300  CA  PRO A  54      19.514  23.696   2.034  1.00 25.79           C  
ANISOU  300  CA  PRO A  54     2729   3592   3478     32     99   -239       C  
ATOM    301  CB  PRO A  54      20.650  23.627   1.018  1.00 28.17           C  
ANISOU  301  CB  PRO A  54     2998   3958   3748     31    119   -256       C  
ATOM    302  CG  PRO A  54      21.465  24.865   1.370  1.00 26.40           C  
ANISOU  302  CG  PRO A  54     2723   3778   3528    -20    136   -271       C  
ATOM    303  CD  PRO A  54      20.456  25.917   1.750  1.00 29.41           C  
ANISOU  303  CD  PRO A  54     3126   4100   3947    -71    134   -248       C  
ATOM    304  C   PRO A  54      19.957  23.034   3.343  1.00 21.13           C  
ANISOU  304  C   PRO A  54     2117   3029   2882     79     83   -261       C  
ATOM    305  O   PRO A  54      19.937  21.805   3.427  1.00 24.58           O  
ANISOU  305  O   PRO A  54     2569   3466   3302    137     69   -267       O  
ATOM    306  N   GLY A  55      20.330  23.820   4.348  1.00 18.29           N  
ANISOU  306  N   GLY A  55     1725   2691   2535     54     86   -274       N  
ATOM    307  CA  GLY A  55      20.873  23.264   5.579  1.00 19.94           C  
ANISOU  307  CA  GLY A  55     1908   2932   2737     95     73   -297       C  
ATOM    308  C   GLY A  55      19.932  22.384   6.380  1.00 19.95           C  
ANISOU  308  C   GLY A  55     1948   2882   2750    139     46   -286       C  
ATOM    309  O   GLY A  55      20.362  21.438   7.047  1.00 18.42           O  
ANISOU  309  O   GLY A  55     1743   2714   2540    192     33   -303       O  
ATOM    310  N   VAL A  56      18.637  22.685   6.317  1.00 17.66           N  
ANISOU  310  N   VAL A  56     1703   2519   2487    117     39   -257       N  
ATOM    311  CA  VAL A  56      17.663  21.961   7.115  1.00 16.71           C  
ANISOU  311  CA  VAL A  56     1622   2347   2382    152     14   -245       C  
ATOM    312  CB  VAL A  56      16.278  22.661   7.026  1.00 14.70           C  
ANISOU  312  CB  VAL A  56     1411   2015   2162    111     10   -214       C  
ATOM    313  CG1 VAL A  56      15.654  22.420   5.662  1.00 16.39           C  
ANISOU  313  CG1 VAL A  56     1664   2191   2372    105     15   -191       C  
ATOM    314  CG2 VAL A  56      15.328  22.185   8.176  1.00 15.74           C  
ANISOU  314  CG2 VAL A  56     1572   2096   2312    138    -15   -204       C  
ATOM    315  C   VAL A  56      17.578  20.478   6.695  1.00 16.33           C  
ANISOU  315  C   VAL A  56     1599   2294   2311    217      0   -245       C  
ATOM    316  O   VAL A  56      17.070  19.651   7.452  1.00 16.99           O  
ANISOU  316  O   VAL A  56     1705   2351   2398    259    -22   -242       O  
ATOM    317  N   ALA A  57      18.120  20.134   5.524  1.00 16.64           N  
ANISOU  317  N   ALA A  57     1634   2362   2326    225     12   -249       N  
ATOM    318  CA  ALA A  57      18.176  18.726   5.113  1.00 17.58           C  
ANISOU  318  CA  ALA A  57     1774   2485   2422    288      0   -253       C  
ATOM    319  CB  ALA A  57      18.743  18.594   3.698  1.00 22.39           C  
ANISOU  319  CB  ALA A  57     2376   3124   3007    284     18   -256       C  
ATOM    320  C   ALA A  57      19.015  17.900   6.084  1.00 20.67           C  
ANISOU  320  C   ALA A  57     2135   2925   2796    341    -12   -280       C  
ATOM    321  O   ALA A  57      18.776  16.705   6.266  1.00 16.55           O  
ANISOU  321  O   ALA A  57     1636   2389   2264    397    -31   -280       O  
ATOM    322  N   ALA A  58      20.015  18.530   6.702  1.00 19.13           N  
ANISOU  322  N   ALA A  58     1887   2786   2595    323     -2   -303       N  
ATOM    323  CA  ALA A  58      20.940  17.782   7.556  1.00 19.69           C  
ANISOU  323  CA  ALA A  58     1925   2910   2647    372    -11   -331       C  
ATOM    324  CB  ALA A  58      22.095  18.683   8.012  1.00 21.10           C  
ANISOU  324  CB  ALA A  58     2044   3153   2820    341      6   -356       C  
ATOM    325  C   ALA A  58      20.253  17.121   8.765  1.00 17.28           C  
ANISOU  325  C   ALA A  58     1643   2568   2355    409    -38   -327       C  
ATOM    326  O   ALA A  58      20.433  15.919   8.970  1.00 17.17           O  
ANISOU  326  O   ALA A  58     1636   2564   2324    469    -53   -335       O  
ATOM    327  N   PRO A  59      19.476  17.879   9.578  1.00 15.92           N  
ANISOU  327  N   PRO A  59     1482   2354   2213    376    -43   -313       N  
ATOM    328  CA  PRO A  59      18.798  17.145  10.654  1.00 17.68           C  
ANISOU  328  CA  PRO A  59     1729   2541   2446    415    -69   -308       C  
ATOM    329  CB  PRO A  59      18.170  18.264  11.507  1.00 17.57           C  
ANISOU  329  CB  PRO A  59     1716   2495   2464    366    -69   -297       C  
ATOM    330  CG  PRO A  59      18.042  19.445  10.571  1.00 18.49           C  
ANISOU  330  CG  PRO A  59     1831   2602   2593    303    -46   -285       C  
ATOM    331  CD  PRO A  59      19.313  19.334   9.732  1.00 16.04           C  
ANISOU  331  CD  PRO A  59     1482   2359   2251    309    -28   -306       C  
ATOM    332  C   PRO A  59      17.730  16.169  10.160  1.00 18.32           C  
ANISOU  332  C   PRO A  59     1869   2562   2530    449    -86   -284       C  
ATOM    333  O   PRO A  59      17.488  15.153  10.822  1.00 18.39           O  
ANISOU  333  O   PRO A  59     1894   2559   2534    500   -107   -286       O  
ATOM    334  N   CYS A  60      17.103  16.451   9.021  1.00 14.65           N  
ANISOU  334  N   CYS A  60     1435   2060   2071    422    -76   -263       N  
ATOM    335  CA  CYS A  60      16.121  15.510   8.477  1.00 17.99           C  
ANISOU  335  CA  CYS A  60     1912   2427   2494    454    -91   -241       C  
ATOM    336  CB  CYS A  60      15.499  16.059   7.200  1.00 16.23           C  
ANISOU  336  CB  CYS A  60     1719   2169   2281    414    -77   -218       C  
ATOM    337  SG  CYS A  60      14.496  17.517   7.502  1.00 19.10           S  
ANISOU  337  SG  CYS A  60     2097   2477   2683    342    -71   -195       S  
ATOM    338  C   CYS A  60      16.789  14.168   8.203  1.00 17.54           C  
ANISOU  338  C   CYS A  60     1851   2407   2407    519   -100   -258       C  
ATOM    339  O   CYS A  60      16.304  13.114   8.599  1.00 20.95           O  
ANISOU  339  O   CYS A  60     2312   2813   2837    567   -122   -252       O  
ATOM    340  N   LYS A  61      17.926  14.224   7.529  1.00 20.53           N  
ANISOU  340  N   LYS A  61     2192   2847   2761    518    -82   -278       N  
ATOM    341  CA  LYS A  61      18.664  13.010   7.220  1.00 21.12           C  
ANISOU  341  CA  LYS A  61     2258   2961   2805    577    -89   -296       C  
ATOM    342  CB  LYS A  61      19.845  13.354   6.316  1.00 19.39           C  
ANISOU  342  CB  LYS A  61     1998   2807   2562    562    -65   -315       C  
ATOM    343  CG  LYS A  61      19.397  13.522   4.870  1.00 22.41           C  
ANISOU  343  CG  LYS A  61     2408   3163   2943    538    -52   -297       C  
ATOM    344  CD  LYS A  61      20.568  13.667   3.909  1.00 34.97           C  
ANISOU  344  CD  LYS A  61     3961   4819   4507    530    -30   -316       C  
ATOM    345  CE  LYS A  61      21.141  15.051   3.935  1.00 40.78           C  
ANISOU  345  CE  LYS A  61     4657   5587   5249    469     -7   -323       C  
ATOM    346  NZ  LYS A  61      21.989  15.283   2.734  1.00 46.37           N  
ANISOU  346  NZ  LYS A  61     5340   6343   5934    452     15   -334       N  
ATOM    347  C   LYS A  61      19.127  12.284   8.489  1.00 20.29           C  
ANISOU  347  C   LYS A  61     2133   2882   2692    625   -108   -315       C  
ATOM    348  O   LYS A  61      19.102  11.058   8.551  1.00 25.35           O  
ANISOU  348  O   LYS A  61     2791   3521   3320    683   -125   -319       O  
ATOM    349  N   ALA A  62      19.510  13.039   9.512  1.00 19.07           N  
ANISOU  349  N   ALA A  62     1944   2752   2549    601   -105   -327       N  
ATOM    350  CA  ALA A  62      19.927  12.427  10.779  1.00 21.77           C  
ANISOU  350  CA  ALA A  62     2267   3119   2886    643   -123   -345       C  
ATOM    351  CB  ALA A  62      20.488  13.483  11.739  1.00 19.41           C  
ANISOU  351  CB  ALA A  62     1924   2855   2598    606   -113   -360       C  
ATOM    352  C   ALA A  62      18.775  11.676  11.433  1.00 21.97           C  
ANISOU  352  C   ALA A  62     2340   3082   2926    675   -149   -326       C  
ATOM    353  O   ALA A  62      18.950  10.586  11.969  1.00 23.81           O  
ANISOU  353  O   ALA A  62     2575   3323   3146    731   -168   -335       O  
ATOM    354  N   ILE A  63      17.586  12.260  11.395  1.00 18.35           N  
ANISOU  354  N   ILE A  63     1918   2558   2495    639   -151   -298       N  
ATOM    355  CA  ILE A  63      16.420  11.662  12.032  1.00 17.88           C  
ANISOU  355  CA  ILE A  63     1905   2436   2453    663   -175   -278       C  
ATOM    356  CB  ILE A  63      15.268  12.675  12.148  1.00 17.16           C  
ANISOU  356  CB  ILE A  63     1842   2284   2395    609   -172   -252       C  
ATOM    357  CG1 ILE A  63      15.683  13.844  13.060  1.00 14.41           C  
ANISOU  357  CG1 ILE A  63     1453   1962   2061    565   -162   -264       C  
ATOM    358  CD1 ILE A  63      14.700  15.036  13.004  1.00 16.85           C  
ANISOU  358  CD1 ILE A  63     1783   2218   2402    503   -154   -241       C  
ATOM    359  CG2 ILE A  63      13.995  12.006  12.679  1.00 21.48           C  
ANISOU  359  CG2 ILE A  63     2441   2763   2959    634   -197   -230       C  
ATOM    360  C   ILE A  63      15.962  10.437  11.243  1.00 27.31           C  
ANISOU  360  C   ILE A  63     3141   3602   3634    709   -188   -267       C  
ATOM    361  O   ILE A  63      15.549   9.439  11.826  1.00 26.15           O  
ANISOU  361  O   ILE A  63     3017   3432   3485    757   -211   -263       O  
ATOM    362  N   ALA A  64      16.042  10.520   9.918  1.00 18.68           N  
ANISOU  362  N   ALA A  64     2056   2510   2531    696   -172   -261       N  
ATOM    363  CA  ALA A  64      15.676   9.399   9.049  1.00 20.95           C  
ANISOU  363  CA  ALA A  64     2381   2775   2805    738   -182   -251       C  
ATOM    364  CB  ALA A  64      15.876   9.768   7.601  1.00 22.92           C  
ANISOU  364  CB  ALA A  64     2631   3032   3045    711   -160   -247       C  
ATOM    365  C   ALA A  64      16.513   8.176   9.397  1.00 32.33           C  
ANISOU  365  C   ALA A  64     3804   4260   4220    804   -196   -275       C  
ATOM    366  O   ALA A  64      16.021   7.049   9.415  1.00 29.35           O  
ANISOU  366  O   ALA A  64     3461   3854   3838    852   -216   -267       O  
ATOM    367  N   LYS A  65      17.789   8.421   9.660  1.00 26.09           N  
ANISOU  367  N   LYS A  65     2959   3540   3413    804   -185   -303       N  
ATOM    368  CA  LYS A  65      18.718   7.351  10.000  1.00 31.03           C  
ANISOU  368  CA  LYS A  65     3562   4216   4014    864   -196   -328       C  
ATOM    369  CB  LYS A  65      20.148   7.822   9.786  1.00 25.94           C  
ANISOU  369  CB  LYS A  65     2857   3650   3348    851   -175   -358       C  
ATOM    370  CG  LYS A  65      21.171   6.729  10.046  1.00 41.79           C  
ANISOU  370  CG  LYS A  65     4839   5713   5328    912   -185   -385       C  
ATOM    371  CD  LYS A  65      22.589   7.189   9.781  1.00 46.89           C  
ANISOU  371  CD  LYS A  65     5426   6437   5953    900   -164   -414       C  
ATOM    372  CE  LYS A  65      23.570   6.066  10.100  1.00 53.18           C  
ANISOU  372  CE  LYS A  65     6197   7286   6723    963   -176   -441       C  
ATOM    373  NZ  LYS A  65      24.945   6.394   9.650  1.00 60.15           N  
ANISOU  373  NZ  LYS A  65     7026   8245   7583    955   -155   -470       N  
ATOM    374  C   LYS A  65      18.542   6.857  11.442  1.00 40.76           C  
ANISOU  374  C   LYS A  65     4793   5440   5252    896   -220   -332       C  
ATOM    375  O   LYS A  65      18.638   5.658  11.714  1.00 41.52           O  
ANISOU  375  O   LYS A  65     4900   5539   5336    954   -240   -339       O  
ATOM    376  N   ASP A  66      18.291   7.788  12.360  1.00 28.28           N  
ANISOU  376  N   ASP A  66     3847   3601   3297    729    -66    501       N  
ATOM    377  CA  ASP A  66      18.119   7.469  13.783  1.00 26.20           C  
ANISOU  377  CA  ASP A  66     3592   3390   2974    756    -53    529       C  
ATOM    378  CB  ASP A  66      19.400   7.801  14.560  1.00 36.92           C  
ANISOU  378  CB  ASP A  66     4897   4834   4299    779    -70    543       C  
ATOM    379  CG  ASP A  66      20.578   6.903  14.168  1.00 61.34           C  
ANISOU  379  CG  ASP A  66     8000   7917   7388    795    -45    572       C  
ATOM    380  OD1 ASP A  66      20.468   5.667  14.338  1.00 71.91           O  
ANISOU  380  OD1 ASP A  66     9389   9229   8704    811     -3    601       O  
ATOM    381  OD2 ASP A  66      21.608   7.425  13.683  1.00 57.18           O  
ANISOU  381  OD2 ASP A  66     7433   7411   6880    791    -65    563       O  
ATOM    382  C   ASP A  66      16.924   8.236  14.379  1.00 33.42           C  
ANISOU  382  C   ASP A  66     4500   4318   3882    750    -73    507       C  
ATOM    383  O   ASP A  66      17.078   9.382  14.800  1.00 31.15           O  
ANISOU  383  O   ASP A  66     4152   4091   3591    750   -114    481       O  
ATOM    384  N   PRO A  67      15.736   7.606  14.409  1.00 29.35           N  
ANISOU  384  N   PRO A  67     4044   3747   3362    741    -44    514       N  
ATOM    385  CA  PRO A  67      14.459   8.237  14.782  1.00 28.09           C  
ANISOU  385  CA  PRO A  67     3877   3582   3215    702    -54    470       C  
ATOM    386  CB  PRO A  67      13.505   7.040  14.877  1.00 29.83           C  
ANISOU  386  CB  PRO A  67     4175   3738   3421    689     -4    492       C  
ATOM    387  CG  PRO A  67      14.059   6.067  13.902  1.00 35.29           C  
ANISOU  387  CG  PRO A  67     4914   4371   4124    710     21    528       C  
ATOM    388  CD  PRO A  67      15.551   6.198  14.016  1.00 36.57           C  
ANISOU  388  CD  PRO A  67     5026   4595   4274    735      5    540       C  
ATOM    389  C   PRO A  67      14.463   9.016  16.100  1.00 30.23           C  
ANISOU  389  C   PRO A  67     4088   3943   3456    684    -75    439       C  
ATOM    390  O   PRO A  67      13.766  10.035  16.213  1.00 24.13           O  
ANISOU  390  O   PRO A  67     3270   3181   2716    632    -98    373       O  
ATOM    391  N   ALA A  68      15.229   8.548  17.082  1.00 26.28           N  
ANISOU  391  N   ALA A  68     3588   3506   2890    728    -67    488       N  
ATOM    392  CA  ALA A  68      15.281   9.207  18.385  1.00 30.12           C  
ANISOU  392  CA  ALA A  68     4023   4081   3341    713    -85    463       C  
ATOM    393  CB  ALA A  68      16.103   8.365  19.366  1.00 34.12           C  
ANISOU  393  CB  ALA A  68     4547   4645   3771    769    -67    531       C  
ATOM    394  C   ALA A  68      15.846  10.624  18.309  1.00 30.87           C  
ANISOU  394  C   ALA A  68     4037   4232   3459    697   -137    416       C  
ATOM    395  O   ALA A  68      15.640  11.430  19.221  1.00 27.01           O  
ANISOU  395  O   ALA A  68     3503   3805   2957    666   -157    374       O  
ATOM    396  N   LYS A  69      16.548  10.936  17.225  1.00 22.69           N  
ANISOU  396  N   LYS A  69     2987   3176   2459    717   -159    422       N  
ATOM    397  CA  LYS A  69      17.151  12.252  17.097  1.00 23.31           C  
ANISOU  397  CA  LYS A  69     2992   3305   2559    703   -207    381       C  
ATOM    398  CB  LYS A  69      18.199  12.252  15.999  1.00 23.79           C  
ANISOU  398  CB  LYS A  69     3048   3346   2647    734   -220    407       C  
ATOM    399  CG  LYS A  69      19.457  11.420  16.370  1.00 22.23           C  
ANISOU  399  CG  LYS A  69     2859   3174   2415    756   -195    455       C  
ATOM    400  CD  LYS A  69      20.635  11.857  15.522  1.00 29.54           C  
ANISOU  400  CD  LYS A  69     3751   4093   3378    743   -209    446       C  
ATOM    401  CE  LYS A  69      21.895  11.062  15.863  1.00 40.34           C  
ANISOU  401  CE  LYS A  69     5124   5488   4714    767   -186    490       C  
ATOM    402  NZ  LYS A  69      22.977  11.310  14.859  1.00 38.51           N  
ANISOU  402  NZ  LYS A  69     4875   5237   4522    756   -194    485       N  
ATOM    403  C   LYS A  69      16.113  13.355  16.831  1.00 17.98           C  
ANISOU  403  C   LYS A  69     2286   2605   1942    636   -225    298       C  
ATOM    404  O   LYS A  69      16.470  14.536  16.806  1.00 19.91           O  
ANISOU  404  O   LYS A  69     2470   2890   2206    616   -263    255       O  
ATOM    405  N   VAL A  70      14.858  12.979  16.610  1.00 19.61           N  
ANISOU  405  N   VAL A  70     2532   2745   2175    601   -197    276       N  
ATOM    406  CA  VAL A  70      13.795  13.992  16.449  1.00 19.14           C  
ANISOU  406  CA  VAL A  70     2442   2666   2166    539   -210    200       C  
ATOM    407  CB  VAL A  70      12.405  13.351  16.134  1.00 19.62           C  
ANISOU  407  CB  VAL A  70     2553   2649   2252    504   -175    189       C  
ATOM    408  CG1 VAL A  70      11.923  12.489  17.291  1.00 19.99           C  
ANISOU  408  CG1 VAL A  70     2635   2715   2245    505   -140    214       C  
ATOM    409  CG2 VAL A  70      11.343  14.434  15.764  1.00 17.53           C  
ANISOU  409  CG2 VAL A  70     2254   2360   2048    444   -190    113       C  
ATOM    410  C   VAL A  70      13.737  14.831  17.724  1.00 20.99           C  
ANISOU  410  C   VAL A  70     2626   2979   2369    514   -227    162       C  
ATOM    411  O   VAL A  70      13.436  16.019  17.677  1.00 20.81           O  
ANISOU  411  O   VAL A  70     2556   2970   2380    476   -253    101       O  
ATOM    412  N   TYR A  71      14.069  14.213  18.860  1.00 19.10           N  
ANISOU  412  N   TYR A  71     2399   2794   2063    538   -212    200       N  
ATOM    413  CA  TYR A  71      14.121  14.903  20.140  1.00 20.78           C  
ANISOU  413  CA  TYR A  71     2569   3088   2237    519   -227    171       C  
ATOM    414  CB  TYR A  71      14.148  13.869  21.271  1.00 19.59           C  
ANISOU  414  CB  TYR A  71     2454   2972   2017    545   -197    220       C  
ATOM    415  CG  TYR A  71      12.813  13.221  21.580  1.00 24.45           C  
ANISOU  415  CG  TYR A  71     3116   3540   2636    516   -156    212       C  
ATOM    416  CD1 TYR A  71      11.900  13.846  22.410  1.00 24.06           C  
ANISOU  416  CD1 TYR A  71     3045   3513   2585    470   -154    159       C  
ATOM    417  CE1 TYR A  71      10.673  13.259  22.712  1.00 28.41           C  
ANISOU  417  CE1 TYR A  71     3634   4022   3137    443   -116    153       C  
ATOM    418  CZ  TYR A  71      10.362  12.022  22.195  1.00 32.80           C  
ANISOU  418  CZ  TYR A  71     4253   4514   3695    460    -80    200       C  
ATOM    419  OH  TYR A  71       9.147  11.439  22.514  1.00 33.24           O  
ANISOU  419  OH  TYR A  71     4347   4531   3752    430    -43    194       O  
ATOM    420  CE2 TYR A  71      11.267  11.366  21.377  1.00 26.55           C  
ANISOU  420  CE2 TYR A  71     3489   3696   2904    507    -80    252       C  
ATOM    421  CD2 TYR A  71      12.487  11.960  21.081  1.00 28.76           C  
ANISOU  421  CD2 TYR A  71     3727   4018   3181    537   -118    259       C  
ATOM    422  C   TYR A  71      15.313  15.872  20.274  1.00 19.55           C  
ANISOU  422  C   TYR A  71     2353   3004   2070    531   -272    160       C  
ATOM    423  O   TYR A  71      15.310  16.761  21.122  1.00 22.61           O  
ANISOU  423  O   TYR A  71     2698   3453   2440    504   -292    119       O  
ATOM    424  N   ASP A  72      16.338  15.712  19.444  1.00 20.31           N  
ANISOU  424  N   ASP A  72     2446   3096   2176    571   -287    198       N  
ATOM    425  CA  ASP A  72      17.509  16.575  19.537  1.00 17.53           C  
ANISOU  425  CA  ASP A  72     2036   2813   1812    582   -329    193       C  
ATOM    426  CB  ASP A  72      18.761  15.793  19.166  1.00 24.53           C  
ANISOU  426  CB  ASP A  72     2934   3715   2670    646   -330    268       C  
ATOM    427  CG  ASP A  72      19.022  14.624  20.101  1.00 29.32           C  
ANISOU  427  CG  ASP A  72     3576   4357   3207    688   -301    333       C  
ATOM    428  OD1 ASP A  72      18.878  14.790  21.335  1.00 33.41           O  
ANISOU  428  OD1 ASP A  72     4078   4938   3678    672   -302    321       O  
ATOM    429  OD2 ASP A  72      19.366  13.537  19.597  1.00 33.92           O  
ANISOU  429  OD2 ASP A  72     4205   4900   3783    732   -273    393       O  
ATOM    430  C   ASP A  72      17.432  17.810  18.644  1.00 17.65           C  
ANISOU  430  C   ASP A  72     2010   2803   1892    547   -360    133       C  
ATOM    431  O   ASP A  72      18.060  18.837  18.934  1.00 24.32           O  
ANISOU  431  O   ASP A  72     2801   3708   2732    533   -395    103       O  
ATOM    432  N   TYR A  73      16.707  17.704  17.537  1.00 15.91           N  
ANISOU  432  N   TYR A  73     1817   2497   1732    534   -347    117       N  
ATOM    433  CA  TYR A  73      16.753  18.751  16.518  1.00 15.71           C  
ANISOU  433  CA  TYR A  73     1757   2442   1769    511   -375     71       C  
ATOM    434  CB  TYR A  73      17.213  18.193  15.166  1.00 12.36           C  
ANISOU  434  CB  TYR A  73     1360   1957   1379    547   -372    111       C  
ATOM    435  CG  TYR A  73      18.588  17.586  15.209  1.00 16.33           C  
ANISOU  435  CG  TYR A  73     1865   2499   1842    600   -374    178       C  
ATOM    436  CD1 TYR A  73      19.686  18.346  15.600  1.00 20.53           C  
ANISOU  436  CD1 TYR A  73     2354   3083   2364    578   -391    169       C  
ATOM    437  CE1 TYR A  73      20.974  17.779  15.637  1.00 22.97           C  
ANISOU  437  CE1 TYR A  73     2672   3405   2650    598   -377    221       C  
ATOM    438  CZ  TYR A  73      21.130  16.454  15.297  1.00 26.94           C  
ANISOU  438  CZ  TYR A  73     3228   3868   3140    634   -343    277       C  
ATOM    439  OH  TYR A  73      22.383  15.884  15.338  1.00 28.09           O  
ANISOU  439  OH  TYR A  73     3380   4028   3265    652   -328    321       O  
ATOM    440  CE2 TYR A  73      20.048  15.687  14.914  1.00 29.29           C  
ANISOU  440  CE2 TYR A  73     3574   4109   3446    651   -322    288       C  
ATOM    441  CD2 TYR A  73      18.780  16.259  14.870  1.00 20.15           C  
ANISOU  441  CD2 TYR A  73     2407   2938   2310    636   -339    241       C  
ATOM    442  C   TYR A  73      15.424  19.454  16.299  1.00 15.29           C  
ANISOU  442  C   TYR A  73     1700   2342   1767    456   -370      3       C  
ATOM    443  O   TYR A  73      15.338  20.308  15.433  1.00 15.27           O  
ANISOU  443  O   TYR A  73     1672   2309   1819    436   -390    -36       O  
ATOM    444  N   THR A  74      14.386  19.056  17.035  1.00 11.95           N  
ANISOU  444  N   THR A  74     1302   1910   1328    433   -342     -8       N  
ATOM    445  CA  THR A  74      13.055  19.678  16.911  1.00 14.48           C  
ANISOU  445  CA  THR A  74     1618   2191   1694    381   -334    -70       C  
ATOM    446  CB  THR A  74      12.018  18.756  16.220  1.00 12.69           C  
ANISOU  446  CB  THR A  74     1445   1881   1497    374   -300    -55       C  
ATOM    447  OG1 THR A  74      11.585  17.751  17.153  1.00 14.88           O  
ANISOU  447  OG1 THR A  74     1760   2169   1724    380   -266    -23       O  
ATOM    448  CG2 THR A  74      12.605  18.110  14.971  1.00 14.30           C  
ANISOU  448  CG2 THR A  74     1677   2032   1724    410   -300    -11       C  
ATOM    449  C   THR A  74      12.524  20.031  18.294  1.00 14.15           C  
ANISOU  449  C   THR A  74     1561   2202   1613    352   -326   -101       C  
ATOM    450  O   THR A  74      13.138  19.700  19.309  1.00 16.78           O  
ANISOU  450  O   THR A  74     1891   2599   1884    372   -326    -72       O  
ATOM    451  N   ALA A  75      11.373  20.684  18.343  1.00 13.78           N  
ANISOU  451  N   ALA A  75     1503   2130   1601    307   -319   -158       N  
ATOM    452  CA  ALA A  75      10.766  21.026  19.619  1.00 13.03           C  
ANISOU  452  CA  ALA A  75     1397   2081   1473    279   -308   -189       C  
ATOM    453  CB  ALA A  75       9.842  22.230  19.433  1.00 17.48           C  
ANISOU  453  CB  ALA A  75     1930   2624   2086    232   -314   -262       C  
ATOM    454  C   ALA A  75       9.991  19.884  20.295  1.00 17.24           C  
ANISOU  454  C   ALA A  75     1976   2602   1971    281   -268   -158       C  
ATOM    455  O   ALA A  75       9.392  20.098  21.354  1.00 16.48           O  
ANISOU  455  O   ALA A  75     1874   2539   1848    258   -255   -182       O  
ATOM    456  N   LYS A  76      10.015  18.688  19.708  1.00 14.31           N  
ANISOU  456  N   LYS A  76     1652   2184   1600    308   -247   -104       N  
ATOM    457  CA  LYS A  76       9.168  17.583  20.160  1.00 17.61           C  
ANISOU  457  CA  LYS A  76     2119   2576   1995    305   -206    -76       C  
ATOM    458  CB  LYS A  76       9.522  16.303  19.398  1.00 17.00           C  
ANISOU  458  CB  LYS A  76     2095   2450   1916    343   -188    -12       C  
ATOM    459  CG  LYS A  76       8.535  15.153  19.643  1.00 16.72           C  
ANISOU  459  CG  LYS A  76     2116   2372   1867    333   -144     14       C  
ATOM    460  CD  LYS A  76       8.993  13.876  18.955  1.00 19.57           C  
ANISOU  460  CD  LYS A  76     2533   2685   2217    373   -124     79       C  
ATOM    461  CE  LYS A  76       8.221  12.668  19.470  1.00 24.26           C  
ANISOU  461  CE  LYS A  76     3185   3252   2781    369    -78    112       C  
ATOM    462  NZ  LYS A  76       6.921  12.500  18.753  1.00 19.10           N  
ANISOU  462  NZ  LYS A  76     2555   2526   2178    325    -59     87       N  
ATOM    463  C   LYS A  76       9.269  17.313  21.660  1.00 19.91           C  
ANISOU  463  C   LYS A  76     2412   2936   2218    311   -194    -63       C  
ATOM    464  O   LYS A  76       8.251  17.130  22.349  1.00 16.28           O  
ANISOU  464  O   LYS A  76     1965   2472   1747    285   -167    -79       O  
ATOM    465  N   GLY A  77      10.497  17.317  22.172  1.00 17.99           N  
ANISOU  465  N   GLY A  77     2152   2756   1926    346   -214    -34       N  
ATOM    466  CA  GLY A  77      10.720  17.017  23.579  1.00 15.57           C  
ANISOU  466  CA  GLY A  77     1848   2519   1550    356   -204    -16       C  
ATOM    467  C   GLY A  77      10.235  18.051  24.580  1.00 19.55           C  
ANISOU  467  C   GLY A  77     2314   3072   2040    316   -213    -75       C  
ATOM    468  O   GLY A  77      10.346  17.844  25.788  1.00 24.37           O  
ANISOU  468  O   GLY A  77     2927   3741   2592    321   -204    -64       O  
ATOM    469  N   ASN A  78       9.712  19.171  24.100  1.00 14.61           N  
ANISOU  469  N   ASN A  78     1657   2425   1469    278   -228   -138       N  
ATOM    470  CA  ASN A  78       9.154  20.170  24.991  1.00 17.83           C  
ANISOU  470  CA  ASN A  78     2034   2871   1868    239   -231   -197       C  
ATOM    471  CB  ASN A  78      10.067  21.394  25.092  1.00 19.52           C  
ANISOU  471  CB  ASN A  78     2197   3138   2079    233   -273   -233       C  
ATOM    472  CG  ASN A  78       9.760  22.236  26.309  1.00 20.69           C  
ANISOU  472  CG  ASN A  78     2322   3344   2195    201   -275   -281       C  
ATOM    473  OD1 ASN A  78       9.669  21.707  27.415  1.00 20.78           O  
ANISOU  473  OD1 ASN A  78     2350   3398   2149    207   -257   -261       O  
ATOM    474  ND2 ASN A  78       9.523  23.526  26.107  1.00 19.65           N  
ANISOU  474  ND2 ASN A  78     2156   3209   2100    167   -292   -345       N  
ATOM    475  C   ASN A  78       7.770  20.602  24.522  1.00 17.47           C  
ANISOU  475  C   ASN A  78     1989   2766   1882    198   -213   -245       C  
ATOM    476  O   ASN A  78       7.282  21.640  24.927  1.00 17.57           O  
ANISOU  476  O   ASN A  78     1972   2796   1907    165   -218   -302       O  
ATOM    477  N   LEU A  79       7.142  19.783  23.690  1.00 14.58           N  
ANISOU  477  N   LEU A  79     1658   2331   1551    201   -191   -221       N  
ATOM    478  CA  LEU A  79       5.903  20.183  23.034  1.00 13.08           C  
ANISOU  478  CA  LEU A  79     1465   2082   1423    164   -178   -262       C  
ATOM    479  CB  LEU A  79       6.115  20.238  21.519  1.00 17.42           C  
ANISOU  479  CB  LEU A  79     2015   2572   2032    171   -194   -257       C  
ATOM    480  CG  LEU A  79       4.971  20.774  20.657  1.00 16.72           C  
ANISOU  480  CG  LEU A  79     1916   2425   2012    135   -187   -300       C  
ATOM    481  CD1 LEU A  79       4.710  22.260  20.982  1.00 17.28           C  
ANISOU  481  CD1 LEU A  79     1938   2524   2104    106   -204   -368       C  
ATOM    482  CD2 LEU A  79       5.377  20.593  19.205  1.00 17.12           C  
ANISOU  482  CD2 LEU A  79     1975   2420   2109    150   -203   -282       C  
ATOM    483  C   LEU A  79       4.767  19.234  23.375  1.00 14.04           C  
ANISOU  483  C   LEU A  79     1626   2172   1536    150   -135   -244       C  
ATOM    484  O   LEU A  79       4.823  18.043  23.078  1.00 17.25           O  
ANISOU  484  O   LEU A  79     2076   2547   1931    171   -116   -192       O  
ATOM    485  N   VAL A  80       3.731  19.773  24.002  1.00 13.49           N  
ANISOU  485  N   VAL A  80     1542   2112   1473    115   -119   -287       N  
ATOM    486  CA  VAL A  80       2.563  19.008  24.366  1.00 15.92           C  
ANISOU  486  CA  VAL A  80     1881   2394   1775     97    -79   -276       C  
ATOM    487  CB  VAL A  80       2.292  19.121  25.882  1.00 13.43           C  
ANISOU  487  CB  VAL A  80     1561   2138   1404     88    -62   -287       C  
ATOM    488  CG1 VAL A  80       0.871  18.661  26.221  1.00 13.65           C  
ANISOU  488  CG1 VAL A  80     1609   2139   1440     59    -21   -292       C  
ATOM    489  CG2 VAL A  80       3.328  18.309  26.648  1.00 16.87           C  
ANISOU  489  CG2 VAL A  80     2020   2621   1770    127    -62   -235       C  
ATOM    490  C   VAL A  80       1.370  19.518  23.553  1.00 12.25           C  
ANISOU  490  C   VAL A  80     1401   1875   1377     59    -71   -316       C  
ATOM    491  O   VAL A  80       1.217  20.726  23.346  1.00 13.94           O  
ANISOU  491  O   VAL A  80     1574   2096   1627     41    -89   -368       O  
ATOM    492  N   ALA A  81       0.540  18.604  23.066  1.00 12.72           N  
ANISOU  492  N   ALA A  81     1495   1881   1457     47    -44   -291       N  
ATOM    493  CA  ALA A  81      -0.719  19.002  22.471  1.00 14.13           C  
ANISOU  493  CA  ALA A  81     1660   2018   1692      9    -32   -326       C  
ATOM    494  CB  ALA A  81      -1.112  18.022  21.361  1.00 14.30           C  
ANISOU  494  CB  ALA A  81     1717   1970   1744      5    -20   -292       C  
ATOM    495  C   ALA A  81      -1.809  19.052  23.540  1.00 16.72           C  
ANISOU  495  C   ALA A  81     1984   2369   2001    -18      0   -345       C  
ATOM    496  O   ALA A  81      -1.994  18.081  24.270  1.00 16.86           O  
ANISOU  496  O   ALA A  81     2035   2395   1974    -14     27   -310       O  
ATOM    497  N   VAL A  82      -2.513  20.178  23.654  1.00 12.60           N  
ANISOU  497  N   VAL A  82     1421   1857   1510    -45     -2   -399       N  
ATOM    498  CA  VAL A  82      -3.741  20.212  24.450  1.00 14.70           C  
ANISOU  498  CA  VAL A  82     1683   2134   1769    -73     32   -417       C  
ATOM    499  CB  VAL A  82      -3.892  21.518  25.242  1.00 12.77           C  
ANISOU  499  CB  VAL A  82     1397   1935   1519    -84     27   -472       C  
ATOM    500  CG1 VAL A  82      -5.311  21.629  25.820  1.00 17.68           C  
ANISOU  500  CG1 VAL A  82     2010   2558   2148   -115     64   -493       C  
ATOM    501  CG2 VAL A  82      -2.832  21.596  26.354  1.00 13.14           C  
ANISOU  501  CG2 VAL A  82     1448   2045   1501    -59     16   -465       C  
ATOM    502  C   VAL A  82      -4.873  20.033  23.463  1.00 14.58           C  
ANISOU  502  C   VAL A  82     1667   2062   1812   -103     45   -422       C  
ATOM    503  O   VAL A  82      -5.119  20.903  22.610  1.00 14.81           O  
ANISOU  503  O   VAL A  82     1663   2068   1895   -114     28   -456       O  
ATOM    504  N   ILE A  83      -5.547  18.892  23.565  1.00 12.19           N  
ANISOU  504  N   ILE A  83     1400   1734   1496   -115     76   -386       N  
ATOM    505  CA  ILE A  83      -6.485  18.463  22.521  1.00 12.72           C  
ANISOU  505  CA  ILE A  83     1475   1744   1612   -143     87   -379       C  
ATOM    506  CB  ILE A  83      -6.060  17.148  21.862  1.00 12.44           C  
ANISOU  506  CB  ILE A  83     1494   1666   1568   -131     91   -325       C  
ATOM    507  CG1 ILE A  83      -4.624  17.277  21.338  1.00 14.29           C  
ANISOU  507  CG1 ILE A  83     1732   1900   1796    -92     56   -312       C  
ATOM    508  CD1 ILE A  83      -4.215  16.157  20.407  1.00 15.97           C  
ANISOU  508  CD1 ILE A  83     1994   2061   2013    -79     57   -265       C  
ATOM    509  CG2 ILE A  83      -7.035  16.786  20.721  1.00 14.39           C  
ANISOU  509  CG2 ILE A  83     1748   1854   1867   -165     99   -322       C  
ATOM    510  C   ILE A  83      -7.884  18.288  23.097  1.00 17.14           C  
ANISOU  510  C   ILE A  83     2031   2307   2174   -178    124   -387       C  
ATOM    511  O   ILE A  83      -8.058  17.621  24.118  1.00 17.16           O  
ANISOU  511  O   ILE A  83     2059   2333   2128   -178    152   -366       O  
ATOM    512  N   SER A  84      -8.874  18.887  22.437  1.00 13.52           N  
ANISOU  512  N   SER A  84     1540   1826   1769   -208    126   -417       N  
ATOM    513  CA  SER A  84     -10.254  18.841  22.932  1.00 15.20           C  
ANISOU  513  CA  SER A  84     1741   2046   1990   -242    161   -427       C  
ATOM    514  CB  SER A  84     -10.563  20.069  23.794  1.00 15.85           C  
ANISOU  514  CB  SER A  84     1778   2174   2069   -243    165   -475       C  
ATOM    515  OG  SER A  84     -11.881  19.981  24.354  1.00 18.04           O  
ANISOU  515  OG  SER A  84     2044   2461   2348   -273    201   -481       O  
ATOM    516  C   SER A  84     -11.226  18.792  21.771  1.00 17.03           C  
ANISOU  516  C   SER A  84     1960   2232   2280   -275    162   -431       C  
ATOM    517  O   SER A  84     -10.932  19.324  20.701  1.00 18.57           O  
ANISOU  517  O   SER A  84     2137   2402   2518   -271    134   -446       O  
ATOM    518  N   ASN A  85     -12.391  18.189  21.985  1.00 16.19           N  
ANISOU  518  N   ASN A  85     1860   2117   2174   -308    195   -418       N  
ATOM    519  CA  ASN A  85     -13.457  18.373  21.009  1.00 14.16           C  
ANISOU  519  CA  ASN A  85     1577   1828   1973   -343    196   -429       C  
ATOM    520  CB  ASN A  85     -14.063  17.017  20.595  1.00 13.95           C  
ANISOU  520  CB  ASN A  85     1594   1763   1944   -374    217   -387       C  
ATOM    521  CG  ASN A  85     -14.664  16.236  21.767  1.00 18.90           C  
ANISOU  521  CG  ASN A  85     2243   2412   2525   -389    258   -366       C  
ATOM    522  OD1 ASN A  85     -14.764  16.724  22.901  1.00 17.20           O  
ANISOU  522  OD1 ASN A  85     2010   2243   2283   -379    273   -383       O  
ATOM    523  ND2 ASN A  85     -15.080  15.001  21.483  1.00 21.45           N  
ANISOU  523  ND2 ASN A  85     2610   2700   2839   -415    278   -327       N  
ATOM    524  C   ASN A  85     -14.541  19.321  21.536  1.00 18.59           C  
ANISOU  524  C   ASN A  85     2087   2421   2553   -362    215   -466       C  
ATOM    525  O   ASN A  85     -15.589  19.469  20.905  1.00 17.90           O  
ANISOU  525  O   ASN A  85     1974   2318   2509   -393    222   -474       O  
ATOM    526  N   GLY A  86     -14.273  19.958  22.676  1.00 16.01           N  
ANISOU  526  N   GLY A  86     1747   2142   2196   -342    222   -488       N  
ATOM    527  CA  GLY A  86     -15.180  20.954  23.252  1.00 18.46           C  
ANISOU  527  CA  GLY A  86     2011   2484   2520   -353    241   -526       C  
ATOM    528  C   GLY A  86     -16.518  20.397  23.742  1.00 20.08           C  
ANISOU  528  C   GLY A  86     2213   2696   2721   -387    282   -511       C  
ATOM    529  O   GLY A  86     -17.514  21.139  23.798  1.00 21.29           O  
ANISOU  529  O   GLY A  86     2322   2863   2903   -403    297   -537       O  
ATOM    530  N   THR A  87     -16.564  19.119  24.119  1.00 15.84           N  
ANISOU  530  N   THR A  87     1721   2150   2147   -398    302   -470       N  
ATOM    531  CA  THR A  87     -17.851  18.537  24.531  1.00 19.71           C  
ANISOU  531  CA  THR A  87     2209   2645   2634   -434    341   -454       C  
ATOM    532  CB  THR A  87     -17.969  17.039  24.133  1.00 24.52           C  
ANISOU  532  CB  THR A  87     2870   3216   3230   -458    352   -406       C  
ATOM    533  OG1 THR A  87     -16.837  16.290  24.609  1.00 19.98           O  
ANISOU  533  OG1 THR A  87     2348   2641   2604   -429    348   -378       O  
ATOM    534  CG2 THR A  87     -18.071  16.906  22.627  1.00 23.05           C  
ANISOU  534  CG2 THR A  87     2682   2984   3094   -476    327   -401       C  
ATOM    535  C   THR A  87     -18.115  18.691  26.039  1.00 19.65           C  
ANISOU  535  C   THR A  87     2200   2687   2581   -427    373   -462       C  
ATOM    536  O   THR A  87     -19.233  18.415  26.533  1.00 20.72           O  
ANISOU  536  O   THR A  87     2326   2835   2714   -454    409   -455       O  
ATOM    537  N   ALA A  88     -17.107  19.152  26.771  1.00 20.31           N  
ANISOU  537  N   ALA A  88     2291   2798   2628   -391    361   -477       N  
ATOM    538  CA  ALA A  88     -17.286  19.469  28.193  1.00 22.78           C  
ANISOU  538  CA  ALA A  88     2599   3160   2897   -382    388   -490       C  
ATOM    539  CB  ALA A  88     -17.067  18.240  29.056  1.00 25.90           C  
ANISOU  539  CB  ALA A  88     3044   3563   3233   -380    411   -448       C  
ATOM    540  C   ALA A  88     -16.337  20.578  28.609  1.00 22.75           C  
ANISOU  540  C   ALA A  88     2580   3186   2880   -348    364   -527       C  
ATOM    541  O   ALA A  88     -15.386  20.349  29.352  1.00 20.45           O  
ANISOU  541  O   ALA A  88     2315   2918   2536   -324    358   -518       O  
ATOM    542  N   VAL A  89     -16.613  21.786  28.138  1.00 19.24           N  
ANISOU  542  N   VAL A  89     2090   2742   2480   -348    352   -568       N  
ATOM    543  CA  VAL A  89     -15.722  22.922  28.358  1.00 20.68           C  
ANISOU  543  CA  VAL A  89     2256   2947   2656   -321    327   -607       C  
ATOM    544  CB  VAL A  89     -15.853  23.951  27.232  1.00 18.57           C  
ANISOU  544  CB  VAL A  89     1949   2655   2452   -322    304   -640       C  
ATOM    545  CG1 VAL A  89     -14.947  25.142  27.483  1.00 22.76           C  
ANISOU  545  CG1 VAL A  89     2465   3207   2976   -297    280   -681       C  
ATOM    546  CG2 VAL A  89     -15.524  23.296  25.896  1.00 19.20           C  
ANISOU  546  CG2 VAL A  89     2042   2688   2566   -327    277   -612       C  
ATOM    547  C   VAL A  89     -16.061  23.557  29.693  1.00 21.95           C  
ANISOU  547  C   VAL A  89     2405   3153   2780   -316    355   -634       C  
ATOM    548  O   VAL A  89     -17.191  24.032  29.876  1.00 24.72           O  
ANISOU  548  O   VAL A  89     2727   3512   3154   -332    384   -652       O  
ATOM    549  N   LEU A  90     -15.088  23.543  30.604  1.00 23.61           N  
ANISOU  549  N   LEU A  90     2639   3396   2934   -294    347   -636       N  
ATOM    550  CA  LEU A  90     -15.262  24.073  31.962  1.00 22.23           C  
ANISOU  550  CA  LEU A  90     2462   3268   2716   -288    372   -660       C  
ATOM    551  CB  LEU A  90     -15.189  25.606  31.964  1.00 25.53           C  
ANISOU  551  CB  LEU A  90     2844   3699   3156   -280    362   -716       C  
ATOM    552  CG  LEU A  90     -13.797  26.174  31.620  1.00 25.53           C  
ANISOU  552  CG  LEU A  90     2848   3702   3150   -259    317   -734       C  
ATOM    553  CD1 LEU A  90     -13.800  27.688  31.522  1.00 27.08           C  
ANISOU  553  CD1 LEU A  90     3011   3903   3373   -256    310   -790       C  
ATOM    554  CD2 LEU A  90     -12.728  25.703  32.608  1.00 25.38           C  
ANISOU  554  CD2 LEU A  90     2863   3721   3060   -242    307   -718       C  
ATOM    555  C   LEU A  90     -16.589  23.569  32.526  1.00 28.34           C  
ANISOU  555  C   LEU A  90     3234   4049   3486   -310    419   -644       C  
ATOM    556  O   LEU A  90     -16.829  22.366  32.535  1.00 29.50           O  
ANISOU  556  O   LEU A  90     3407   4183   3617   -321    433   -601       O  
ATOM    557  N   GLY A  91     -17.453  24.485  32.956  1.00 27.28           N  
ANISOU  557  N   GLY A  91     3067   3932   3365   -317    445   -679       N  
ATOM    558  CA  GLY A  91     -18.795  24.126  33.383  1.00 36.99           C  
ANISOU  558  CA  GLY A  91     4287   5167   4599   -338    490   -666       C  
ATOM    559  C   GLY A  91     -19.853  24.512  32.363  1.00 35.36           C  
ANISOU  559  C   GLY A  91     4040   4934   4462   -358    497   -674       C  
ATOM    560  O   GLY A  91     -21.044  24.571  32.672  1.00 32.29           O  
ANISOU  560  O   GLY A  91     3630   4555   4085   -374    534   -673       O  
ATOM    561  N   LEU A  92     -19.413  24.767  31.135  1.00 28.49           N  
ANISOU  561  N   LEU A  92     3159   4031   3637   -356    460   -679       N  
ATOM    562  CA  LEU A  92     -20.295  25.226  30.068  1.00 27.33           C  
ANISOU  562  CA  LEU A  92     2970   3857   3556   -371    460   -688       C  
ATOM    563  CB  LEU A  92     -19.515  26.142  29.117  1.00 26.02           C  
ANISOU  563  CB  LEU A  92     2788   3671   3428   -355    419   -717       C  
ATOM    564  CG  LEU A  92     -18.904  27.414  29.692  1.00 23.88           C  
ANISOU  564  CG  LEU A  92     2507   3424   3142   -330    413   -765       C  
ATOM    565  CD1 LEU A  92     -18.137  28.156  28.614  1.00 25.94           C  
ANISOU  565  CD1 LEU A  92     2755   3659   3443   -317    371   -787       C  
ATOM    566  CD2 LEU A  92     -20.003  28.298  30.285  1.00 29.20           C  
ANISOU  566  CD2 LEU A  92     3149   4120   3827   -332    453   -794       C  
ATOM    567  C   LEU A  92     -20.932  24.090  29.275  1.00 27.83           C  
ANISOU  567  C   LEU A  92     3040   3891   3644   -401    464   -645       C  
ATOM    568  O   LEU A  92     -21.867  24.311  28.496  1.00 27.63           O  
ANISOU  568  O   LEU A  92     2979   3850   3669   -420    470   -646       O  
ATOM    569  N   GLY A  93     -20.421  22.874  29.448  1.00 27.60           N  
ANISOU  569  N   GLY A  93     3056   3853   3578   -405    460   -607       N  
ATOM    570  CA  GLY A  93     -20.964  21.725  28.739  1.00 26.25           C  
ANISOU  570  CA  GLY A  93     2899   3651   3425   -435    465   -566       C  
ATOM    571  C   GLY A  93     -20.498  21.626  27.298  1.00 23.61           C  
ANISOU  571  C   GLY A  93     2564   3272   3133   -438    426   -560       C  
ATOM    572  O   GLY A  93     -19.381  22.034  26.957  1.00 22.25           O  
ANISOU  572  O   GLY A  93     2402   3093   2961   -412    392   -574       O  
ATOM    573  N   ASN A  94     -21.372  21.109  26.446  1.00 22.34           N  
ANISOU  573  N   ASN A  94     2393   3086   3010   -471    432   -540       N  
ATOM    574  CA  ASN A  94     -21.023  20.774  25.071  1.00 24.84           C  
ANISOU  574  CA  ASN A  94     2718   3358   3363   -480    398   -527       C  
ATOM    575  CB  ASN A  94     -21.886  19.584  24.609  1.00 27.06           C  
ANISOU  575  CB  ASN A  94     3015   3615   3652   -523    415   -487       C  
ATOM    576  CG  ASN A  94     -21.486  19.049  23.246  1.00 26.02           C  
ANISOU  576  CG  ASN A  94     2903   3434   3549   -534    384   -469       C  
ATOM    577  OD1 ASN A  94     -20.558  19.546  22.611  1.00 22.26           O  
ANISOU  577  OD1 ASN A  94     2427   2941   3088   -508    349   -484       O  
ATOM    578  ND2 ASN A  94     -22.186  18.021  22.791  1.00 31.25           N  
ANISOU  578  ND2 ASN A  94     3584   4073   4218   -575    397   -437       N  
ATOM    579  C   ASN A  94     -21.188  21.963  24.139  1.00 24.40           C  
ANISOU  579  C   ASN A  94     2613   3294   3364   -474    376   -561       C  
ATOM    580  O   ASN A  94     -22.217  22.105  23.469  1.00 30.61           O  
ANISOU  580  O   ASN A  94     3365   4072   4194   -500    383   -560       O  
ATOM    581  N   ILE A  95     -20.177  22.823  24.090  1.00 19.07           N  
ANISOU  581  N   ILE A  95     1934   2622   2689   -440    348   -590       N  
ATOM    582  CA  ILE A  95     -20.273  24.021  23.275  1.00 20.96           C  
ANISOU  582  CA  ILE A  95     2129   2854   2981   -430    329   -624       C  
ATOM    583  CB  ILE A  95     -19.806  25.263  24.048  1.00 20.98           C  
ANISOU  583  CB  ILE A  95     2115   2888   2970   -399    329   -667       C  
ATOM    584  CG1 ILE A  95     -18.343  25.107  24.517  1.00 20.89           C  
ANISOU  584  CG1 ILE A  95     2142   2882   2913   -371    306   -667       C  
ATOM    585  CD1 ILE A  95     -17.776  26.360  25.182  1.00 22.35           C  
ANISOU  585  CD1 ILE A  95     2312   3095   3085   -344    301   -712       C  
ATOM    586  CG2 ILE A  95     -20.749  25.525  25.222  1.00 25.39           C  
ANISOU  586  CG2 ILE A  95     2656   3485   3507   -405    373   -677       C  
ATOM    587  C   ILE A  95     -19.502  23.899  21.964  1.00 21.77           C  
ANISOU  587  C   ILE A  95     2242   2915   3114   -425    287   -618       C  
ATOM    588  O   ILE A  95     -19.578  24.782  21.116  1.00 20.43           O  
ANISOU  588  O   ILE A  95     2039   2733   2991   -419    268   -641       O  
ATOM    589  N   GLY A  96     -18.792  22.790  21.776  1.00 19.75           N  
ANISOU  589  N   GLY A  96     2035   2637   2832   -426    274   -584       N  
ATOM    590  CA  GLY A  96     -18.112  22.555  20.503  1.00 19.09           C  
ANISOU  590  CA  GLY A  96     1965   2511   2775   -422    238   -573       C  
ATOM    591  C   GLY A  96     -16.664  23.025  20.441  1.00 15.60           C  
ANISOU  591  C   GLY A  96     1538   2068   2320   -384    205   -588       C  
ATOM    592  O   GLY A  96     -16.207  23.775  21.298  1.00 17.67           O  
ANISOU  592  O   GLY A  96     1791   2364   2560   -361    207   -614       O  
ATOM    593  N   PRO A  97     -15.937  22.580  19.409  1.00 16.36           N  
ANISOU  593  N   PRO A  97     1658   2127   2432   -379    175   -570       N  
ATOM    594  CA  PRO A  97     -14.476  22.750  19.398  1.00 15.93           C  
ANISOU  594  CA  PRO A  97     1625   2072   2357   -343    146   -573       C  
ATOM    595  CB  PRO A  97     -14.029  21.944  18.168  1.00 17.74           C  
ANISOU  595  CB  PRO A  97     1884   2252   2605   -346    123   -542       C  
ATOM    596  CG  PRO A  97     -15.237  21.744  17.339  1.00 19.19           C  
ANISOU  596  CG  PRO A  97     2050   2410   2831   -383    132   -537       C  
ATOM    597  CD  PRO A  97     -16.428  21.748  18.295  1.00 16.84           C  
ANISOU  597  CD  PRO A  97     1732   2145   2521   -407    171   -542       C  
ATOM    598  C   PRO A  97     -14.048  24.208  19.295  1.00 18.16           C  
ANISOU  598  C   PRO A  97     1867   2369   2664   -321    126   -618       C  
ATOM    599  O   PRO A  97     -13.142  24.621  20.015  1.00 17.66           O  
ANISOU  599  O   PRO A  97     1810   2333   2568   -295    117   -632       O  
ATOM    600  N   ALA A  98     -14.687  25.003  18.438  1.00 15.18           N  
ANISOU  600  N   ALA A  98     1450   1976   2341   -330    119   -641       N  
ATOM    601  CA  ALA A  98     -14.232  26.393  18.286  1.00 19.22           C  
ANISOU  601  CA  ALA A  98     1927   2497   2876   -308    101   -684       C  
ATOM    602  CB  ALA A  98     -14.939  27.050  17.104  1.00 21.70           C  
ANISOU  602  CB  ALA A  98     2209   2785   3249   -314     93   -694       C  
ATOM    603  C   ALA A  98     -14.446  27.219  19.567  1.00 19.99           C  
ANISOU  603  C   ALA A  98     2007   2640   2948   -301    124   -717       C  
ATOM    604  O   ALA A  98     -13.590  28.023  19.976  1.00 17.80           O  
ANISOU  604  O   ALA A  98     1726   2381   2656   -278    110   -744       O  
ATOM    605  N   ALA A  99     -15.577  26.997  20.220  1.00 18.38           N  
ANISOU  605  N   ALA A  99     1793   2454   2736   -321    160   -713       N  
ATOM    606  CA  ALA A  99     -15.891  27.746  21.430  1.00 19.87           C  
ANISOU  606  CA  ALA A  99     1966   2684   2900   -314    186   -742       C  
ATOM    607  CB  ALA A  99     -17.364  27.586  21.784  1.00 21.29           C  
ANISOU  607  CB  ALA A  99     2125   2876   3090   -339    226   -736       C  
ATOM    608  C   ALA A  99     -15.011  27.309  22.588  1.00 18.87           C  
ANISOU  608  C   ALA A  99     1875   2586   2707   -300    188   -734       C  
ATOM    609  O   ALA A  99     -14.858  28.042  23.553  1.00 18.60           O  
ANISOU  609  O   ALA A  99     1834   2586   2648   -289    199   -763       O  
ATOM    610  N   GLY A 100     -14.440  26.110  22.506  1.00 16.16           N  
ANISOU  610  N   GLY A 100     1572   2231   2337   -300    178   -694       N  
ATOM    611  CA  GLY A 100     -13.470  25.699  23.507  1.00 18.99           C  
ANISOU  611  CA  GLY A 100     1964   2618   2633   -282    175   -683       C  
ATOM    612  C   GLY A 100     -12.055  26.237  23.293  1.00 17.88           C  
ANISOU  612  C   GLY A 100     1828   2481   2484   -255    137   -697       C  
ATOM    613  O   GLY A 100     -11.224  26.148  24.198  1.00 16.35           O  
ANISOU  613  O   GLY A 100     1654   2320   2239   -239    133   -695       O  
ATOM    614  N   LYS A 101     -11.780  26.830  22.134  1.00 15.99           N  
ANISOU  614  N   LYS A 101     1569   2212   2295   -250    110   -712       N  
ATOM    615  CA  LYS A 101     -10.397  27.247  21.809  1.00 17.00           C  
ANISOU  615  CA  LYS A 101     1702   2340   2417   -225     72   -721       C  
ATOM    616  CB  LYS A 101     -10.342  27.839  20.394  1.00 15.81           C  
ANISOU  616  CB  LYS A 101     1528   2149   2328   -224     47   -734       C  
ATOM    617  CG  LYS A 101      -8.924  28.231  19.909  1.00 17.35           C  
ANISOU  617  CG  LYS A 101     1728   2341   2524   -200      7   -740       C  
ATOM    618  CD  LYS A 101      -8.889  28.490  18.394  1.00 15.53           C  
ANISOU  618  CD  LYS A 101     1483   2064   2354   -200    -17   -741       C  
ATOM    619  CE  LYS A 101      -7.477  28.823  17.884  1.00 14.69           C  
ANISOU  619  CE  LYS A 101     1382   1953   2247   -174    -54   -742       C  
ATOM    620  NZ  LYS A 101      -6.546  27.615  17.864  1.00 17.42           N  
ANISOU  620  NZ  LYS A 101     1767   2296   2556   -161    -68   -696       N  
ATOM    621  C   LYS A 101      -9.778  28.223  22.832  1.00 14.16           C  
ANISOU  621  C   LYS A 101     1333   2025   2023   -212     69   -758       C  
ATOM    622  O   LYS A 101      -8.603  28.086  23.189  1.00 14.67           O  
ANISOU  622  O   LYS A 101     1415   2109   2049   -194     48   -750       O  
ATOM    623  N   PRO A 102     -10.542  29.215  23.339  1.00 14.66           N  
ANISOU  623  N   PRO A 102     1368   2104   2097   -221     91   -798       N  
ATOM    624  CA  PRO A 102      -9.897  30.058  24.346  1.00 14.53           C  
ANISOU  624  CA  PRO A 102     1349   2128   2041   -210     88   -832       C  
ATOM    625  CB  PRO A 102     -11.012  31.079  24.710  1.00 17.10           C  
ANISOU  625  CB  PRO A 102     1646   2461   2390   -221    120   -873       C  
ATOM    626  CG  PRO A 102     -11.843  31.144  23.473  1.00 15.81           C  
ANISOU  626  CG  PRO A 102     1459   2256   2293   -230    121   -868       C  
ATOM    627  CD  PRO A 102     -11.887  29.725  22.982  1.00 18.15           C  
ANISOU  627  CD  PRO A 102     1779   2530   2586   -237    116   -816       C  
ATOM    628  C   PRO A 102      -9.447  29.281  25.592  1.00 16.62           C  
ANISOU  628  C   PRO A 102     1646   2435   2235   -205     98   -809       C  
ATOM    629  O   PRO A 102      -8.444  29.626  26.204  1.00 17.20           O  
ANISOU  629  O   PRO A 102     1727   2540   2269   -193     81   -822       O  
ATOM    630  N   VAL A 103     -10.196  28.256  25.966  1.00 15.02           N  
ANISOU  630  N   VAL A 103     1460   2231   2015   -216    126   -776       N  
ATOM    631  CA  VAL A 103      -9.830  27.473  27.128  1.00 14.58           C  
ANISOU  631  CA  VAL A 103     1436   2213   1892   -210    138   -752       C  
ATOM    632  CB  VAL A 103     -10.988  26.520  27.557  1.00 19.18           C  
ANISOU  632  CB  VAL A 103     2031   2791   2464   -227    178   -722       C  
ATOM    633  CG1 VAL A 103     -10.497  25.458  28.508  1.00 19.21           C  
ANISOU  633  CG1 VAL A 103     2073   2823   2402   -218    187   -685       C  
ATOM    634  CG2 VAL A 103     -12.095  27.310  28.241  1.00 19.13           C  
ANISOU  634  CG2 VAL A 103     2000   2803   2464   -241    213   -758       C  
ATOM    635  C   VAL A 103      -8.555  26.678  26.842  1.00 17.51           C  
ANISOU  635  C   VAL A 103     1834   2582   2237   -190    107   -715       C  
ATOM    636  O   VAL A 103      -7.679  26.582  27.698  1.00 17.02           O  
ANISOU  636  O   VAL A 103     1788   2559   2120   -176     98   -710       O  
ATOM    637  N   MET A 104      -8.448  26.124  25.638  1.00 17.81           N  
ANISOU  637  N   MET A 104     1878   2576   2313   -189     90   -688       N  
ATOM    638  CA  MET A 104      -7.280  25.300  25.311  1.00 15.92           C  
ANISOU  638  CA  MET A 104     1668   2331   2050   -168     65   -649       C  
ATOM    639  CB  MET A 104      -7.513  24.485  24.028  1.00 16.83           C  
ANISOU  639  CB  MET A 104     1797   2391   2207   -173     59   -615       C  
ATOM    640  CG  MET A 104      -8.765  23.585  24.034  1.00 18.00           C  
ANISOU  640  CG  MET A 104     1959   2516   2362   -197     94   -590       C  
ATOM    641  SD  MET A 104      -8.988  22.739  25.605  1.00 21.88           S  
ANISOU  641  SD  MET A 104     2481   3050   2782   -197    130   -565       S  
ATOM    642  CE  MET A 104     -10.765  22.977  25.855  1.00 20.92           C  
ANISOU  642  CE  MET A 104     2336   2924   2689   -233    171   -585       C  
ATOM    643  C   MET A 104      -6.030  26.193  25.179  1.00 15.35           C  
ANISOU  643  C   MET A 104     1581   2279   1974   -149     27   -673       C  
ATOM    644  O   MET A 104      -4.951  25.820  25.630  1.00 17.35           O  
ANISOU  644  O   MET A 104     1852   2560   2180   -129     10   -652       O  
ATOM    645  N   GLU A 105      -6.169  27.364  24.564  1.00 16.00           N  
ANISOU  645  N   GLU A 105     1630   2347   2104   -156     14   -716       N  
ATOM    646  CA  GLU A 105      -5.072  28.343  24.580  1.00 15.28           C  
ANISOU  646  CA  GLU A 105     1522   2277   2005   -143    -18   -746       C  
ATOM    647  CB  GLU A 105      -5.464  29.647  23.861  1.00 18.49           C  
ANISOU  647  CB  GLU A 105     1894   2661   2471   -153    -25   -795       C  
ATOM    648  CG  GLU A 105      -5.584  29.502  22.327  1.00 17.98           C  
ANISOU  648  CG  GLU A 105     1822   2542   2470   -152    -41   -781       C  
ATOM    649  CD  GLU A 105      -5.633  30.836  21.562  1.00 22.21           C  
ANISOU  649  CD  GLU A 105     2324   3057   3059   -155    -55   -827       C  
ATOM    650  OE1 GLU A 105      -5.601  31.929  22.183  1.00 21.18           O  
ANISOU  650  OE1 GLU A 105     2176   2951   2920   -159    -51   -871       O  
ATOM    651  OE2 GLU A 105      -5.699  30.782  20.312  1.00 16.71           O  
ANISOU  651  OE2 GLU A 105     1620   2318   2413   -153    -69   -818       O  
ATOM    652  C   GLU A 105      -4.648  28.661  26.021  1.00 16.64           C  
ANISOU  652  C   GLU A 105     1699   2510   2114   -141    -12   -763       C  
ATOM    653  O   GLU A 105      -3.464  28.682  26.328  1.00 17.57           O  
ANISOU  653  O   GLU A 105     1823   2658   2194   -126    -38   -756       O  
ATOM    654  N   GLY A 106      -5.625  28.885  26.901  1.00 15.14           N  
ANISOU  654  N   GLY A 106     1507   2337   1910   -156     22   -783       N  
ATOM    655  CA  GLY A 106      -5.325  29.175  28.290  1.00 20.09           C  
ANISOU  655  CA  GLY A 106     2140   3019   2474   -156     31   -799       C  
ATOM    656  C   GLY A 106      -4.665  28.011  29.013  1.00 18.28           C  
ANISOU  656  C   GLY A 106     1942   2821   2181   -141     29   -752       C  
ATOM    657  O   GLY A 106      -3.767  28.214  29.814  1.00 16.46           O  
ANISOU  657  O   GLY A 106     1717   2639   1900   -133     14   -757       O  
ATOM    658  N   LYS A 107      -5.125  26.788  28.765  1.00 17.75           N  
ANISOU  658  N   LYS A 107     1898   2730   2117   -139     46   -705       N  
ATOM    659  CA  LYS A 107      -4.479  25.619  29.368  1.00 17.52           C  
ANISOU  659  CA  LYS A 107     1902   2726   2029   -121     47   -655       C  
ATOM    660  CB  LYS A 107      -5.183  24.325  28.953  1.00 21.24           C  
ANISOU  660  CB  LYS A 107     2400   3158   2512   -124     71   -607       C  
ATOM    661  CG  LYS A 107      -4.650  23.078  29.630  1.00 23.87           C  
ANISOU  661  CG  LYS A 107     2771   3513   2784   -105     79   -554       C  
ATOM    662  CD  LYS A 107      -5.201  22.942  31.039  1.00 32.47           C  
ANISOU  662  CD  LYS A 107     3870   4644   3821   -112    112   -558       C  
ATOM    663  CE  LYS A 107      -4.906  21.562  31.611  1.00 33.14           C  
ANISOU  663  CE  LYS A 107     3998   4742   3853    -95    128   -500       C  
ATOM    664  NZ  LYS A 107      -5.792  21.278  32.777  1.00 38.80           N  
ANISOU  664  NZ  LYS A 107     4726   5484   4533   -108    168   -500       N  
ATOM    665  C   LYS A 107      -3.024  25.589  28.935  1.00 20.28           C  
ANISOU  665  C   LYS A 107     2253   3087   2365    -97      6   -638       C  
ATOM    666  O   LYS A 107      -2.119  25.277  29.726  1.00 16.98           O  
ANISOU  666  O   LYS A 107     1849   2716   1888    -81     -5   -619       O  
ATOM    667  N   GLY A 108      -2.800  25.935  27.673  1.00 18.39           N  
ANISOU  667  N   GLY A 108     1998   2806   2182    -96    -18   -645       N  
ATOM    668  CA  GLY A 108      -1.446  25.967  27.148  1.00 16.75           C  
ANISOU  668  CA  GLY A 108     1789   2606   1969    -74    -57   -630       C  
ATOM    669  C   GLY A 108      -0.581  27.000  27.867  1.00 19.53           C  
ANISOU  669  C   GLY A 108     2121   3013   2288    -73    -80   -666       C  
ATOM    670  O   GLY A 108       0.603  26.763  28.105  1.00 19.57           O  
ANISOU  670  O   GLY A 108     2131   3054   2253    -53   -105   -643       O  
ATOM    671  N   ILE A 109      -1.167  28.155  28.189  1.00 19.16           N  
ANISOU  671  N   ILE A 109     2051   2973   2257    -95    -71   -722       N  
ATOM    672  CA  ILE A 109      -0.483  29.177  28.975  1.00 18.15           C  
ANISOU  672  CA  ILE A 109     1907   2895   2093   -101    -88   -762       C  
ATOM    673  CB  ILE A 109      -1.384  30.408  29.222  1.00 19.28           C  
ANISOU  673  CB  ILE A 109     2030   3032   2263   -126    -69   -824       C  
ATOM    674  CG1 ILE A 109      -1.742  31.092  27.901  1.00 32.24           C  
ANISOU  674  CG1 ILE A 109     3650   4618   3983   -132    -77   -848       C  
ATOM    675  CD1 ILE A 109      -0.558  31.544  27.125  1.00 36.76           C  
ANISOU  675  CD1 ILE A 109     4208   5187   4571   -122   -119   -851       C  
ATOM    676  CG2 ILE A 109      -0.725  31.394  30.190  1.00 26.60           C  
ANISOU  676  CG2 ILE A 109     2949   4013   3144   -136    -82   -866       C  
ATOM    677  C   ILE A 109      -0.035  28.615  30.329  1.00 21.56           C  
ANISOU  677  C   ILE A 109     2359   3390   2445    -93    -82   -740       C  
ATOM    678  O   ILE A 109       1.099  28.849  30.773  1.00 20.59           O  
ANISOU  678  O   ILE A 109     2232   3315   2279    -85   -110   -740       O  
ATOM    679  N   LEU A 110      -0.918  27.865  30.983  1.00 19.85           N  
ANISOU  679  N   LEU A 110     2162   3173   2206    -96    -46   -721       N  
ATOM    680  CA  LEU A 110      -0.566  27.249  32.263  1.00 17.55           C  
ANISOU  680  CA  LEU A 110     1892   2938   1838    -87    -37   -696       C  
ATOM    681  CB  LEU A 110      -1.765  26.514  32.854  1.00 18.13           C  
ANISOU  681  CB  LEU A 110     1987   3001   1901    -94      9   -680       C  
ATOM    682  CG  LEU A 110      -2.992  27.388  33.155  1.00 19.02           C  
ANISOU  682  CG  LEU A 110     2084   3102   2040   -121     39   -731       C  
ATOM    683  CD1 LEU A 110      -4.060  26.533  33.819  1.00 21.67           C  
ANISOU  683  CD1 LEU A 110     2442   3435   2357   -126     83   -708       C  
ATOM    684  CD2 LEU A 110      -2.613  28.571  34.052  1.00 24.70           C  
ANISOU  684  CD2 LEU A 110     2791   3870   2725   -132     30   -783       C  
ATOM    685  C   LEU A 110       0.613  26.291  32.115  1.00 17.97           C  
ANISOU  685  C   LEU A 110     1960   3010   1857    -57    -61   -640       C  
ATOM    686  O   LEU A 110       1.490  26.249  32.966  1.00 19.74           O  
ANISOU  686  O   LEU A 110     2188   3293   2019    -47    -76   -630       O  
ATOM    687  N   PHE A 111       0.643  25.519  31.031  1.00 17.28           N  
ANISOU  687  N   PHE A 111     1884   2873   1808    -42    -65   -601       N  
ATOM    688  CA  PHE A 111       1.769  24.633  30.802  1.00 16.34           C  
ANISOU  688  CA  PHE A 111     1780   2768   1660    -11    -86   -546       C  
ATOM    689  CB  PHE A 111       1.562  23.825  29.518  1.00 16.06           C  
ANISOU  689  CB  PHE A 111     1761   2666   1675      1    -82   -509       C  
ATOM    690  CG  PHE A 111       0.891  22.501  29.724  1.00 18.63           C  
ANISOU  690  CG  PHE A 111     2125   2969   1986      7    -47   -462       C  
ATOM    691  CD1 PHE A 111       1.641  21.378  30.062  1.00 19.60           C  
ANISOU  691  CD1 PHE A 111     2278   3112   2057     39    -45   -403       C  
ATOM    692  CE1 PHE A 111       1.034  20.148  30.206  1.00 18.66           C  
ANISOU  692  CE1 PHE A 111     2198   2967   1924     44    -11   -359       C  
ATOM    693  CZ  PHE A 111      -0.351  20.031  30.018  1.00 20.71           C  
ANISOU  693  CZ  PHE A 111     2465   3183   2222     15     22   -375       C  
ATOM    694  CE2 PHE A 111      -1.099  21.137  29.686  1.00 20.56           C  
ANISOU  694  CE2 PHE A 111     2412   3147   2253    -15     19   -432       C  
ATOM    695  CD2 PHE A 111      -0.480  22.362  29.531  1.00 18.11           C  
ANISOU  695  CD2 PHE A 111     2065   2859   1955    -17    -14   -475       C  
ATOM    696  C   PHE A 111       3.091  25.398  30.695  1.00 17.65           C  
ANISOU  696  C   PHE A 111     1922   2974   1813     -2   -130   -560       C  
ATOM    697  O   PHE A 111       4.108  24.994  31.246  1.00 18.63           O  
ANISOU  697  O   PHE A 111     2050   3148   1881     20   -146   -528       O  
ATOM    698  N   LYS A 112       3.061  26.501  29.959  1.00 18.59           N  
ANISOU  698  N   LYS A 112     2011   3068   1983    -19   -148   -607       N  
ATOM    699  CA  LYS A 112       4.256  27.307  29.759  1.00 21.04           C  
ANISOU  699  CA  LYS A 112     2297   3411   2288    -16   -189   -624       C  
ATOM    700  CB  LYS A 112       3.992  28.357  28.680  1.00 22.79           C  
ANISOU  700  CB  LYS A 112     2493   3585   2583    -33   -201   -670       C  
ATOM    701  CG  LYS A 112       5.225  29.174  28.267  1.00 26.87           C  
ANISOU  701  CG  LYS A 112     2983   4125   3103    -30   -244   -686       C  
ATOM    702  CD  LYS A 112       6.246  28.321  27.551  1.00 31.38           C  
ANISOU  702  CD  LYS A 112     3559   4692   3671      3   -267   -629       C  
ATOM    703  CE  LYS A 112       7.319  29.183  26.903  1.00 29.35           C  
ANISOU  703  CE  LYS A 112     3272   4445   3433      3   -308   -647       C  
ATOM    704  NZ  LYS A 112       8.133  28.366  25.988  1.00 35.34           N  
ANISOU  704  NZ  LYS A 112     4038   5187   4204     37   -326   -591       N  
ATOM    705  C   LYS A 112       4.705  27.976  31.062  1.00 22.10           C  
ANISOU  705  C   LYS A 112     2421   3618   2360    -29   -197   -654       C  
ATOM    706  O   LYS A 112       5.877  27.913  31.428  1.00 19.83           O  
ANISOU  706  O   LYS A 112     2126   3383   2025    -15   -225   -634       O  
ATOM    707  N   GLN A 113       3.764  28.611  31.755  1.00 20.25           N  
ANISOU  707  N   GLN A 113     2185   3386   2123    -55   -172   -700       N  
ATOM    708  CA  GLN A 113       4.100  29.385  32.947  1.00 18.59           C  
ANISOU  708  CA  GLN A 113     1966   3239   1856    -73   -178   -737       C  
ATOM    709  CB  GLN A 113       2.894  30.230  33.370  1.00 21.62           C  
ANISOU  709  CB  GLN A 113     2349   3606   2260   -102   -147   -794       C  
ATOM    710  CG  GLN A 113       2.593  31.335  32.387  1.00 33.57           C  
ANISOU  710  CG  GLN A 113     3840   5072   3844   -119   -154   -842       C  
ATOM    711  CD  GLN A 113       3.838  32.128  32.032  1.00 42.82           C  
ANISOU  711  CD  GLN A 113     4989   6266   5014   -122   -198   -860       C  
ATOM    712  OE1 GLN A 113       4.355  32.048  30.907  1.00 41.95           O  
ANISOU  712  OE1 GLN A 113     4868   6126   4947   -110   -221   -843       O  
ATOM    713  NE2 GLN A 113       4.337  32.889  32.998  1.00 34.71           N  
ANISOU  713  NE2 GLN A 113     3956   5295   3936   -141   -209   -895       N  
ATOM    714  C   GLN A 113       4.558  28.523  34.111  1.00 22.45           C  
ANISOU  714  C   GLN A 113     2475   3791   2265    -57   -174   -696       C  
ATOM    715  O   GLN A 113       5.479  28.896  34.853  1.00 27.17           O  
ANISOU  715  O   GLN A 113     3063   4453   2807    -60   -198   -704       O  
ATOM    716  N   PHE A 114       3.930  27.369  34.274  1.00 21.21           N  
ANISOU  716  N   PHE A 114     2345   3616   2099    -41   -144   -652       N  
ATOM    717  CA  PHE A 114       4.210  26.521  35.425  1.00 24.04           C  
ANISOU  717  CA  PHE A 114     2724   4028   2381    -25   -133   -614       C  
ATOM    718  CB  PHE A 114       2.914  25.881  35.918  1.00 23.30           C  
ANISOU  718  CB  PHE A 114     2657   3911   2286    -31    -85   -605       C  
ATOM    719  CG  PHE A 114       2.029  26.832  36.666  1.00 25.18           C  
ANISOU  719  CG  PHE A 114     2889   4158   2522    -62    -63   -665       C  
ATOM    720  CD2 PHE A 114       2.117  26.937  38.045  1.00 32.18           C  
ANISOU  720  CD2 PHE A 114     3784   5107   3337    -68    -54   -675       C  
ATOM    721  CE2 PHE A 114       1.299  27.816  38.735  1.00 28.64           C  
ANISOU  721  CE2 PHE A 114     3332   4664   2885    -96    -31   -730       C  
ATOM    722  CZ  PHE A 114       0.401  28.606  38.054  1.00 28.02           C  
ANISOU  722  CZ  PHE A 114     3240   4532   2874   -116    -16   -774       C  
ATOM    723  CE1 PHE A 114       0.307  28.519  36.684  1.00 30.21           C  
ANISOU  723  CE1 PHE A 114     3506   4750   3222   -111    -27   -764       C  
ATOM    724  CD1 PHE A 114       1.127  27.636  35.993  1.00 26.37           C  
ANISOU  724  CD1 PHE A 114     3025   4256   2739    -85    -50   -711       C  
ATOM    725  C   PHE A 114       5.252  25.443  35.170  1.00 27.01           C  
ANISOU  725  C   PHE A 114     3111   4422   2729     13   -152   -545       C  
ATOM    726  O   PHE A 114       5.878  24.944  36.113  1.00 26.71           O  
ANISOU  726  O   PHE A 114     3083   4446   2621     29   -156   -514       O  
ATOM    727  N   ALA A 115       5.465  25.090  33.907  1.00 20.39           N  
ANISOU  727  N   ALA A 115     2272   3533   1944     28   -162   -520       N  
ATOM    728  CA  ALA A 115       6.408  24.020  33.607  1.00 23.62           C  
ANISOU  728  CA  ALA A 115     2695   3952   2328     68   -175   -452       C  
ATOM    729  CB  ALA A 115       5.665  22.747  33.263  1.00 27.45           C  
ANISOU  729  CB  ALA A 115     3217   4384   2828     85   -140   -404       C  
ATOM    730  C   ALA A 115       7.376  24.352  32.488  1.00 22.47           C  
ANISOU  730  C   ALA A 115     2526   3793   2219     81   -213   -446       C  
ATOM    731  O   ALA A 115       8.246  23.539  32.173  1.00 23.32           O  
ANISOU  731  O   ALA A 115     2643   3910   2308    116   -226   -389       O  
ATOM    732  N   GLY A 116       7.227  25.522  31.878  1.00 18.72           N  
ANISOU  732  N   GLY A 116     2024   3294   1795     54   -230   -502       N  
ATOM    733  CA  GLY A 116       8.054  25.867  30.731  1.00 20.42           C  
ANISOU  733  CA  GLY A 116     2219   3489   2052     64   -263   -498       C  
ATOM    734  C   GLY A 116       7.851  24.980  29.512  1.00 20.43           C  
ANISOU  734  C   GLY A 116     2240   3421   2103     88   -254   -456       C  
ATOM    735  O   GLY A 116       8.745  24.847  28.672  1.00 21.27           O  
ANISOU  735  O   GLY A 116     2337   3518   2225    110   -279   -430       O  
ATOM    736  N   ILE A 117       6.672  24.377  29.414  1.00 18.36           N  
ANISOU  736  N   ILE A 117     2004   3109   1863     81   -217   -450       N  
ATOM    737  CA  ILE A 117       6.328  23.490  28.297  1.00 18.06           C  
ANISOU  737  CA  ILE A 117     1990   3002   1871     98   -203   -412       C  
ATOM    738  CB  ILE A 117       5.431  22.312  28.793  1.00 18.65           C  
ANISOU  738  CB  ILE A 117     2105   3057   1923    102   -160   -377       C  
ATOM    739  CG1 ILE A 117       6.249  21.393  29.711  1.00 17.41           C  
ANISOU  739  CG1 ILE A 117     1969   2956   1690    135   -158   -322       C  
ATOM    740  CD1 ILE A 117       5.428  20.398  30.505  1.00 21.92           C  
ANISOU  740  CD1 ILE A 117     2579   3524   2227    136   -116   -294       C  
ATOM    741  CG2 ILE A 117       4.859  21.512  27.612  1.00 16.71           C  
ANISOU  741  CG2 ILE A 117     1886   2732   1730    108   -143   -349       C  
ATOM    742  C   ILE A 117       5.606  24.271  27.198  1.00 16.11           C  
ANISOU  742  C   ILE A 117     1726   2692   1704     73   -205   -457       C  
ATOM    743  O   ILE A 117       4.677  25.033  27.476  1.00 20.69           O  
ANISOU  743  O   ILE A 117     2294   3264   2304     41   -191   -507       O  
ATOM    744  N   ASP A 118       6.026  24.078  25.950  1.00 14.88           N  
ANISOU  744  N   ASP A 118     1570   2492   1591     89   -222   -437       N  
ATOM    745  CA  ASP A 118       5.327  24.671  24.808  1.00 16.78           C  
ANISOU  745  CA  ASP A 118     1798   2669   1908     69   -222   -471       C  
ATOM    746  CB  ASP A 118       6.264  24.754  23.597  1.00 17.55           C  
ANISOU  746  CB  ASP A 118     1886   2742   2039     90   -253   -454       C  
ATOM    747  CG  ASP A 118       7.475  25.660  23.864  1.00 28.51           C  
ANISOU  747  CG  ASP A 118     3240   4187   3405     94   -291   -473       C  
ATOM    748  OD1 ASP A 118       7.274  26.891  24.016  1.00 26.27           O  
ANISOU  748  OD1 ASP A 118     2928   3915   3141     66   -301   -531       O  
ATOM    749  OD2 ASP A 118       8.623  25.150  23.912  1.00 28.75           O  
ANISOU  749  OD2 ASP A 118     3274   4251   3400    125   -309   -429       O  
ATOM    750  C   ASP A 118       4.086  23.852  24.454  1.00 14.59           C  
ANISOU  750  C   ASP A 118     1551   2334   1658     60   -186   -455       C  
ATOM    751  O   ASP A 118       4.124  22.620  24.494  1.00 16.75           O  
ANISOU  751  O   ASP A 118     1860   2596   1908     80   -169   -402       O  
ATOM    752  N   VAL A 119       2.991  24.536  24.113  1.00 14.24           N  
ANISOU  752  N   VAL A 119     1492   2255   1664     29   -174   -500       N  
ATOM    753  CA  VAL A 119       1.771  23.850  23.739  1.00 13.39           C  
ANISOU  753  CA  VAL A 119     1406   2095   1585     15   -142   -489       C  
ATOM    754  CB  VAL A 119       0.693  24.010  24.857  1.00 17.97           C  
ANISOU  754  CB  VAL A 119     1986   2698   2144    -10   -109   -514       C  
ATOM    755  CG1 VAL A 119      -0.681  23.570  24.382  1.00 14.86           C  
ANISOU  755  CG1 VAL A 119     1604   2251   1791    -32    -78   -513       C  
ATOM    756  CG2 VAL A 119       1.092  23.233  26.104  1.00 19.08           C  
ANISOU  756  CG2 VAL A 119     2150   2889   2209      6    -96   -480       C  
ATOM    757  C   VAL A 119       1.186  24.319  22.388  1.00 14.02           C  
ANISOU  757  C   VAL A 119     1472   2113   1742      0   -148   -512       C  
ATOM    758  O   VAL A 119       1.083  25.520  22.106  1.00 16.07           O  
ANISOU  758  O   VAL A 119     1696   2372   2037    -15   -162   -561       O  
ATOM    759  N   PHE A 120       0.813  23.343  21.561  1.00 13.70           N  
ANISOU  759  N   PHE A 120     1460   2020   1725      4   -136   -475       N  
ATOM    760  CA  PHE A 120      -0.114  23.549  20.447  1.00 11.66           C  
ANISOU  760  CA  PHE A 120     1194   1703   1534    -17   -130   -492       C  
ATOM    761  CB  PHE A 120       0.253  22.711  19.210  1.00 16.70           C  
ANISOU  761  CB  PHE A 120     1859   2289   2197     -1   -139   -451       C  
ATOM    762  CG  PHE A 120       1.516  23.120  18.508  1.00 15.50           C  
ANISOU  762  CG  PHE A 120     1695   2138   2056     25   -176   -447       C  
ATOM    763  CD1 PHE A 120       2.203  24.277  18.848  1.00 14.21           C  
ANISOU  763  CD1 PHE A 120     1494   2017   1889     28   -201   -484       C  
ATOM    764  CE1 PHE A 120       3.378  24.630  18.160  1.00 14.40           C  
ANISOU  764  CE1 PHE A 120     1505   2042   1924     51   -234   -478       C  
ATOM    765  CZ  PHE A 120       3.873  23.811  17.138  1.00 16.76           C  
ANISOU  765  CZ  PHE A 120     1830   2301   2238     74   -242   -434       C  
ATOM    766  CE2 PHE A 120       3.198  22.650  16.795  1.00 13.94           C  
ANISOU  766  CE2 PHE A 120     1513   1899   1883     73   -216   -398       C  
ATOM    767  CD2 PHE A 120       2.011  22.318  17.482  1.00 13.66           C  
ANISOU  767  CD2 PHE A 120     1490   1863   1838     46   -183   -406       C  
ATOM    768  C   PHE A 120      -1.499  23.128  20.931  1.00 15.51           C  
ANISOU  768  C   PHE A 120     1693   2179   2021    -44    -92   -495       C  
ATOM    769  O   PHE A 120      -1.706  21.957  21.282  1.00 13.28           O  
ANISOU  769  O   PHE A 120     1448   1892   1708    -41    -69   -453       O  
ATOM    770  N   ASP A 121      -2.445  24.062  20.954  1.00 15.32           N  
ANISOU  770  N   ASP A 121     1637   2152   2031    -71    -84   -542       N  
ATOM    771  CA  ASP A 121      -3.824  23.720  21.274  1.00 16.72           C  
ANISOU  771  CA  ASP A 121     1820   2317   2217    -98    -48   -545       C  
ATOM    772  CB  ASP A 121      -4.538  24.925  21.891  1.00 18.86           C  
ANISOU  772  CB  ASP A 121     2053   2614   2499   -118    -38   -600       C  
ATOM    773  CG  ASP A 121      -4.625  26.103  20.926  1.00 21.79           C  
ANISOU  773  CG  ASP A 121     2387   2961   2931   -124    -58   -641       C  
ATOM    774  OD1 ASP A 121      -3.594  26.778  20.713  1.00 19.56           O  
ANISOU  774  OD1 ASP A 121     2092   2691   2649   -108    -88   -656       O  
ATOM    775  OD2 ASP A 121      -5.716  26.351  20.365  1.00 20.36           O  
ANISOU  775  OD2 ASP A 121     2190   2750   2796   -145    -44   -656       O  
ATOM    776  C   ASP A 121      -4.532  23.260  20.002  1.00 17.32           C  
ANISOU  776  C   ASP A 121     1903   2331   2346   -113    -44   -531       C  
ATOM    777  O   ASP A 121      -4.470  23.926  18.963  1.00 21.63           O  
ANISOU  777  O   ASP A 121     2427   2848   2942   -115    -65   -552       O  
ATOM    778  N   ILE A 122      -5.153  22.094  20.062  1.00 13.92           N  
ANISOU  778  N   ILE A 122     1507   1879   1902   -124    -18   -495       N  
ATOM    779  CA  ILE A 122      -5.765  21.495  18.890  1.00 12.10           C  
ANISOU  779  CA  ILE A 122     1291   1592   1715   -140    -14   -476       C  
ATOM    780  CB  ILE A 122      -5.096  20.153  18.516  1.00 17.21           C  
ANISOU  780  CB  ILE A 122     1992   2212   2337   -122    -14   -420       C  
ATOM    781  CG1 ILE A 122      -3.579  20.312  18.387  1.00 19.57           C  
ANISOU  781  CG1 ILE A 122     2295   2526   2616    -82    -45   -408       C  
ATOM    782  CD1 ILE A 122      -3.131  21.242  17.241  1.00 22.87           C  
ANISOU  782  CD1 ILE A 122     2682   2922   3086    -76    -79   -435       C  
ATOM    783  CG2 ILE A 122      -5.726  19.579  17.244  1.00 17.50           C  
ANISOU  783  CG2 ILE A 122     2045   2186   2417   -142    -11   -404       C  
ATOM    784  C   ILE A 122      -7.228  21.247  19.212  1.00 14.58           C  
ANISOU  784  C   ILE A 122     1602   1900   2039   -176     20   -481       C  
ATOM    785  O   ILE A 122      -7.528  20.470  20.123  1.00 16.82           O  
ANISOU  785  O   ILE A 122     1911   2201   2279   -181     48   -458       O  
ATOM    786  N   GLU A 123      -8.130  21.933  18.511  1.00 13.59           N  
ANISOU  786  N   GLU A 123     1442   1754   1967   -200     20   -511       N  
ATOM    787  CA  GLU A 123      -9.568  21.745  18.704  1.00 17.80           C  
ANISOU  787  CA  GLU A 123     1966   2282   2515   -235     51   -515       C  
ATOM    788  CB  GLU A 123     -10.283  23.097  18.780  1.00 17.94           C  
ANISOU  788  CB  GLU A 123     1929   2318   2568   -246     53   -566       C  
ATOM    789  CG  GLU A 123      -9.824  23.980  19.963  1.00 17.36           C  
ANISOU  789  CG  GLU A 123     1838   2296   2462   -229     54   -597       C  
ATOM    790  CD  GLU A 123      -8.504  24.692  19.742  1.00 20.37           C  
ANISOU  790  CD  GLU A 123     2211   2687   2840   -200     18   -614       C  
ATOM    791  OE1 GLU A 123      -8.237  25.190  18.618  1.00 17.15           O  
ANISOU  791  OE1 GLU A 123     1788   2250   2479   -195     -7   -625       O  
ATOM    792  OE2 GLU A 123      -7.717  24.766  20.711  1.00 19.60           O  
ANISOU  792  OE2 GLU A 123     2123   2629   2694   -182     15   -615       O  
ATOM    793  C   GLU A 123     -10.083  20.887  17.547  1.00 19.27           C  
ANISOU  793  C   GLU A 123     2174   2414   2732   -256     52   -487       C  
ATOM    794  O   GLU A 123      -9.875  21.223  16.368  1.00 18.93           O  
ANISOU  794  O   GLU A 123     2121   2340   2733   -254     27   -494       O  
ATOM    795  N   VAL A 124     -10.729  19.769  17.898  1.00 13.76           N  
ANISOU  795  N   VAL A 124     1509   1707   2011   -278     82   -455       N  
ATOM    796  CA  VAL A 124     -11.075  18.716  16.945  1.00 12.17           C  
ANISOU  796  CA  VAL A 124     1344   1456   1825   -299     86   -421       C  
ATOM    797  CB  VAL A 124     -10.500  17.353  17.408  1.00 17.02           C  
ANISOU  797  CB  VAL A 124     2020   2060   2385   -287    102   -372       C  
ATOM    798  CG1 VAL A 124     -10.930  16.236  16.475  1.00 20.59           C  
ANISOU  798  CG1 VAL A 124     2515   2458   2851   -313    111   -339       C  
ATOM    799  CG2 VAL A 124      -8.969  17.432  17.526  1.00 19.03           C  
ANISOU  799  CG2 VAL A 124     2291   2326   2612   -239     77   -362       C  
ATOM    800  C   VAL A 124     -12.581  18.569  16.767  1.00 20.80           C  
ANISOU  800  C   VAL A 124     2419   2539   2945   -345    110   -426       C  
ATOM    801  O   VAL A 124     -13.305  18.298  17.729  1.00 18.87           O  
ANISOU  801  O   VAL A 124     2174   2320   2675   -362    141   -422       O  
ATOM    802  N   ALA A 125     -13.046  18.706  15.533  1.00 17.96           N  
ANISOU  802  N   ALA A 125     2046   2144   2635   -365     95   -431       N  
ATOM    803  CA  ALA A 125     -14.472  18.550  15.251  1.00 20.15           C  
ANISOU  803  CA  ALA A 125     2303   2413   2939   -411    115   -433       C  
ATOM    804  CB  ALA A 125     -14.849  19.354  14.019  1.00 19.17           C  
ANISOU  804  CB  ALA A 125     2140   2269   2877   -422     91   -456       C  
ATOM    805  C   ALA A 125     -14.857  17.073  15.077  1.00 20.23           C  
ANISOU  805  C   ALA A 125     2368   2390   2929   -441    136   -389       C  
ATOM    806  O   ALA A 125     -15.238  16.635  13.982  1.00 21.36           O  
ANISOU  806  O   ALA A 125     2523   2492   3100   -468    128   -377       O  
ATOM    807  N   ALA A 126     -14.756  16.313  16.166  1.00 19.52           N  
ANISOU  807  N   ALA A 126     2313   2317   2788   -438    163   -366       N  
ATOM    808  CA  ALA A 126     -15.162  14.906  16.178  1.00 22.94           C  
ANISOU  808  CA  ALA A 126     2801   2721   3196   -467    189   -325       C  
ATOM    809  CB  ALA A 126     -13.985  14.008  15.827  1.00 18.68           C  
ANISOU  809  CB  ALA A 126     2325   2146   2628   -440    180   -291       C  
ATOM    810  C   ALA A 126     -15.730  14.525  17.534  1.00 23.24           C  
ANISOU  810  C   ALA A 126     2844   2794   3192   -478    227   -317       C  
ATOM    811  O   ALA A 126     -15.032  14.625  18.545  1.00 21.00           O  
ANISOU  811  O   ALA A 126     2569   2542   2869   -444    232   -316       O  
ATOM    812  N   THR A 127     -16.985  14.070  17.551  1.00 23.49           N  
ANISOU  812  N   THR A 127     2871   2822   3233   -527    253   -309       N  
ATOM    813  CA  THR A 127     -17.620  13.610  18.782  1.00 29.70           C  
ANISOU  813  CA  THR A 127     3665   3638   3981   -542    292   -297       C  
ATOM    814  CB  THR A 127     -19.076  14.112  18.885  1.00 34.21           C  
ANISOU  814  CB  THR A 127     4182   4233   4584   -583    309   -317       C  
ATOM    815  OG1 THR A 127     -19.811  13.658  17.742  1.00 32.91           O  
ANISOU  815  OG1 THR A 127     4019   4030   4454   -629    304   -306       O  
ATOM    816  CG2 THR A 127     -19.126  15.637  18.941  1.00 35.81           C  
ANISOU  816  CG2 THR A 127     4317   4472   4819   -561    291   -362       C  
ATOM    817  C   THR A 127     -17.638  12.083  18.919  1.00 28.86           C  
ANISOU  817  C   THR A 127     3630   3499   3837   -561    318   -250       C  
ATOM    818  O   THR A 127     -17.763  11.564  20.030  1.00 33.07           O  
ANISOU  818  O   THR A 127     4184   4054   4327   -560    349   -234       O  
ATOM    819  N   ASP A 128     -17.541  11.363  17.802  1.00 22.51           N  
ANISOU  819  N   ASP A 128     2863   2641   3048   -580    308   -230       N  
ATOM    820  CA  ASP A 128     -17.525   9.909  17.867  1.00 25.67           C  
ANISOU  820  CA  ASP A 128     3337   3004   3412   -599    335   -186       C  
ATOM    821  CB  ASP A 128     -17.837   9.276  16.503  1.00 37.62           C  
ANISOU  821  CB  ASP A 128     4879   4460   4954   -638    325   -172       C  
ATOM    822  CG  ASP A 128     -17.559   7.765  16.476  1.00 64.08           C  
ANISOU  822  CG  ASP A 128     8319   7764   8266   -648    351   -126       C  
ATOM    823  OD1 ASP A 128     -16.397   7.347  16.258  1.00 68.64           O  
ANISOU  823  OD1 ASP A 128     8944   8314   8821   -607    342   -105       O  
ATOM    824  OD2 ASP A 128     -18.514   6.989  16.702  1.00 73.71           O  
ANISOU  824  OD2 ASP A 128     9558   8973   9474   -698    382   -109       O  
ATOM    825  C   ASP A 128     -16.159   9.453  18.355  1.00 25.00           C  
ANISOU  825  C   ASP A 128     3302   2916   3281   -545    334   -162       C  
ATOM    826  O   ASP A 128     -15.134   9.929  17.854  1.00 24.04           O  
ANISOU  826  O   ASP A 128     3178   2788   3170   -505    302   -170       O  
ATOM    827  N   VAL A 129     -16.146   8.528  19.313  1.00 23.81           N  
ANISOU  827  N   VAL A 129     3197   2769   3080   -543    369   -131       N  
ATOM    828  CA  VAL A 129     -14.896   8.103  19.940  1.00 26.99           C  
ANISOU  828  CA  VAL A 129     3644   3178   3433   -489    371   -105       C  
ATOM    829  CB  VAL A 129     -15.145   6.993  20.986  1.00 28.11           C  
ANISOU  829  CB  VAL A 129     3837   3322   3521   -496    417    -68       C  
ATOM    830  CG1 VAL A 129     -13.840   6.300  21.376  1.00 26.56           C  
ANISOU  830  CG1 VAL A 129     3699   3119   3274   -442    421    -32       C  
ATOM    831  CG2 VAL A 129     -15.835   7.586  22.217  1.00 23.84           C  
ANISOU  831  CG2 VAL A 129     3249   2841   2967   -504    435    -90       C  
ATOM    832  C   VAL A 129     -13.887   7.628  18.893  1.00 27.47           C  
ANISOU  832  C   VAL A 129     3751   3189   3498   -464    350    -84       C  
ATOM    833  O   VAL A 129     -12.730   8.076  18.865  1.00 22.40           O  
ANISOU  833  O   VAL A 129     3103   2558   2848   -413    325    -86       O  
ATOM    834  N   ASP A 130     -14.316   6.751  17.996  1.00 25.24           N  
ANISOU  834  N   ASP A 130     3513   2849   3228   -501    360    -63       N  
ATOM    835  CA  ASP A 130     -13.332   6.174  17.093  1.00 24.53           C  
ANISOU  835  CA  ASP A 130     3477   2709   3134   -475    347    -37       C  
ATOM    836  CB  ASP A 130     -13.885   4.899  16.461  1.00 33.14           C  
ANISOU  836  CB  ASP A 130     4636   3737   4220   -520    373     -6       C  
ATOM    837  CG  ASP A 130     -13.745   3.686  17.396  1.00 56.10           C  
ANISOU  837  CG  ASP A 130     7611   6635   7068   -513    417     38       C  
ATOM    838  OD1 ASP A 130     -13.122   3.834  18.477  1.00 58.83           O  
ANISOU  838  OD1 ASP A 130     7951   7024   7376   -467    424     46       O  
ATOM    839  OD2 ASP A 130     -14.244   2.587  17.057  1.00 59.03           O  
ANISOU  839  OD2 ASP A 130     8042   6957   7428   -552    445     65       O  
ATOM    840  C   ASP A 130     -12.840   7.177  16.039  1.00 28.42           C  
ANISOU  840  C   ASP A 130     3928   3197   3675   -458    300    -67       C  
ATOM    841  O   ASP A 130     -11.654   7.155  15.678  1.00 23.17           O  
ANISOU  841  O   ASP A 130     3285   2518   3001   -410    282    -54       O  
ATOM    842  N   VAL A 131     -13.719   8.068  15.578  1.00 24.48           N  
ANISOU  842  N   VAL A 131     3367   2711   3225   -492    283   -105       N  
ATOM    843  CA  VAL A 131     -13.319   9.100  14.628  1.00 24.62           C  
ANISOU  843  CA  VAL A 131     3340   2727   3288   -476    241   -136       C  
ATOM    844  CB  VAL A 131     -14.514   9.934  14.129  1.00 22.89           C  
ANISOU  844  CB  VAL A 131     3056   2519   3121   -522    230   -173       C  
ATOM    845  CG1 VAL A 131     -14.032  11.004  13.184  1.00 24.29           C  
ANISOU  845  CG1 VAL A 131     3191   2694   3344   -500    188   -203       C  
ATOM    846  CG2 VAL A 131     -15.572   9.032  13.435  1.00 27.06           C  
ANISOU  846  CG2 VAL A 131     3615   3004   3661   -585    248   -156       C  
ATOM    847  C   VAL A 131     -12.302  10.043  15.279  1.00 19.44           C  
ANISOU  847  C   VAL A 131     2647   2117   2621   -419    220   -154       C  
ATOM    848  O   VAL A 131     -11.270  10.357  14.690  1.00 18.93           O  
ANISOU  848  O   VAL A 131     2586   2042   2565   -381    192   -154       O  
ATOM    849  N   PHE A 132     -12.607  10.476  16.498  1.00 18.61           N  
ANISOU  849  N   PHE A 132     2510   2066   2495   -415    235   -168       N  
ATOM    850  CA  PHE A 132     -11.708  11.360  17.255  1.00 16.27           C  
ANISOU  850  CA  PHE A 132     2181   1819   2182   -366    218   -186       C  
ATOM    851  CB  PHE A 132     -12.301  11.676  18.640  1.00 16.49           C  
ANISOU  851  CB  PHE A 132     2180   1902   2184   -373    242   -200       C  
ATOM    852  CG  PHE A 132     -11.430  12.570  19.495  1.00 17.54           C  
ANISOU  852  CG  PHE A 132     2282   2089   2295   -328    226   -221       C  
ATOM    853  CD1 PHE A 132     -10.394  12.050  20.263  1.00 19.54           C  
ANISOU  853  CD1 PHE A 132     2572   2360   2493   -286    231   -192       C  
ATOM    854  CE1 PHE A 132      -9.590  12.888  21.044  1.00 16.45           C  
ANISOU  854  CE1 PHE A 132     2150   2022   2080   -249    214   -211       C  
ATOM    855  CZ  PHE A 132      -9.834  14.249  21.073  1.00 18.37           C  
ANISOU  855  CZ  PHE A 132     2329   2295   2355   -253    194   -262       C  
ATOM    856  CE2 PHE A 132     -10.855  14.783  20.317  1.00 19.05           C  
ANISOU  856  CE2 PHE A 132     2381   2362   2497   -290    191   -290       C  
ATOM    857  CD2 PHE A 132     -11.655  13.946  19.534  1.00 19.19           C  
ANISOU  857  CD2 PHE A 132     2424   2330   2536   -327    206   -269       C  
ATOM    858  C   PHE A 132     -10.340  10.693  17.398  1.00 16.70           C  
ANISOU  858  C   PHE A 132     2288   1864   2194   -316    214   -150       C  
ATOM    859  O   PHE A 132      -9.300  11.305  17.139  1.00 17.99           O  
ANISOU  859  O   PHE A 132     2435   2039   2362   -276    184   -159       O  
ATOM    860  N   CYS A 133     -10.340   9.437  17.839  1.00 16.62           N  
ANISOU  860  N   CYS A 133     2340   1836   2141   -318    247   -107       N  
ATOM    861  CA  CYS A 133      -9.082   8.749  18.079  1.00 16.37           C  
ANISOU  861  CA  CYS A 133     2359   1798   2064   -268    249    -68       C  
ATOM    862  CB  CYS A 133      -9.316   7.393  18.733  1.00 20.66           C  
ANISOU  862  CB  CYS A 133     2968   2324   2558   -275    293    -23       C  
ATOM    863  SG  CYS A 133      -9.876   7.476  20.451  1.00 24.25           S  
ANISOU  863  SG  CYS A 133     3403   2842   2970   -281    324    -28       S  
ATOM    864  C   CYS A 133      -8.289   8.547  16.810  1.00 15.20           C  
ANISOU  864  C   CYS A 133     2237   1601   1937   -248    226    -54       C  
ATOM    865  O   CYS A 133      -7.071   8.634  16.832  1.00 16.31           O  
ANISOU  865  O   CYS A 133     2385   1752   2058   -197    209    -39       O  
ATOM    866  N   ASN A 134      -8.973   8.242  15.711  1.00 18.20           N  
ANISOU  866  N   ASN A 134     2633   1929   2355   -288    226    -56       N  
ATOM    867  CA  ASN A 134      -8.257   8.005  14.463  1.00 17.94           C  
ANISOU  867  CA  ASN A 134     2629   1845   2341   -271    205    -42       C  
ATOM    868  CB  ASN A 134      -9.172   7.346  13.435  1.00 19.41           C  
ANISOU  868  CB  ASN A 134     2849   1971   2555   -324    217    -36       C  
ATOM    869  CG  ASN A 134      -9.373   5.855  13.714  1.00 22.40           C  
ANISOU  869  CG  ASN A 134     3309   2312   2891   -339    259     10       C  
ATOM    870  OD1 ASN A 134      -8.585   5.225  14.441  1.00 22.50           O  
ANISOU  870  OD1 ASN A 134     3363   2332   2854   -298    278     45       O  
ATOM    871  ND2 ASN A 134     -10.425   5.289  13.151  1.00 20.84           N  
ANISOU  871  ND2 ASN A 134     3134   2073   2710   -398    276     12       N  
ATOM    872  C   ASN A 134      -7.649   9.293  13.904  1.00 19.08           C  
ANISOU  872  C   ASN A 134     2715   2011   2525   -246    161    -77       C  
ATOM    873  O   ASN A 134      -6.626   9.254  13.225  1.00 20.91           O  
ANISOU  873  O   ASN A 134     2965   2222   2759   -209    141    -63       O  
ATOM    874  N   ALA A 135      -8.253  10.437  14.217  1.00 14.33           N  
ANISOU  874  N   ALA A 135     2043   1451   1951   -263    147   -122       N  
ATOM    875  CA  ALA A 135      -7.666  11.706  13.816  1.00 14.43           C  
ANISOU  875  CA  ALA A 135     2000   1487   1997   -239    108   -157       C  
ATOM    876  CB  ALA A 135      -8.705  12.812  13.855  1.00 15.72           C  
ANISOU  876  CB  ALA A 135     2095   1677   2202   -273     99   -206       C  
ATOM    877  C   ALA A 135      -6.474  12.079  14.691  1.00 19.16           C  
ANISOU  877  C   ALA A 135     2587   2133   2558   -185     97   -153       C  
ATOM    878  O   ALA A 135      -5.457  12.562  14.201  1.00 22.30           O  
ANISOU  878  O   ALA A 135     2973   2533   2966   -150     67   -156       O  
ATOM    879  N   VAL A 136      -6.589  11.855  15.995  1.00 14.14           N  
ANISOU  879  N   VAL A 136     1955   1540   1879   -181    120   -145       N  
ATOM    880  CA  VAL A 136      -5.547  12.286  16.926  1.00 17.96           C  
ANISOU  880  CA  VAL A 136     2422   2077   2324   -135    109   -144       C  
ATOM    881  CB  VAL A 136      -6.104  12.370  18.364  1.00 18.34           C  
ANISOU  881  CB  VAL A 136     2455   2177   2336   -146    134   -153       C  
ATOM    882  CG1 VAL A 136      -4.974  12.535  19.389  1.00 18.82           C  
ANISOU  882  CG1 VAL A 136     2513   2293   2346    -99    126   -142       C  
ATOM    883  CG2 VAL A 136      -7.100  13.505  18.462  1.00 20.47           C  
ANISOU  883  CG2 VAL A 136     2663   2470   2646   -180    127   -206       C  
ATOM    884  C   VAL A 136      -4.308  11.379  16.907  1.00 15.65           C  
ANISOU  884  C   VAL A 136     2183   1773   1990    -88    111    -94       C  
ATOM    885  O   VAL A 136      -3.168  11.855  16.994  1.00 15.98           O  
ANISOU  885  O   VAL A 136     2208   1843   2019    -45     86    -93       O  
ATOM    886  N   ARG A 137      -4.511  10.087  16.770  1.00 15.94           N  
ANISOU  886  N   ARG A 137     2286   1767   2005    -94    141    -50       N  
ATOM    887  CA  ARG A 137      -3.378   9.226  16.854  1.00 20.11           C  
ANISOU  887  CA  ARG A 137     2867   2287   2487    -46    150      1       C  
ATOM    888  CB  ARG A 137      -3.772   7.788  16.981  1.00 19.85           C  
ANISOU  888  CB  ARG A 137     2908   2210   2426    -62    194     45       C  
ATOM    889  CG  ARG A 137      -4.424   7.189  15.804  1.00 20.64           C  
ANISOU  889  CG  ARG A 137     3046   2235   2561    -92    199     52       C  
ATOM    890  CD  ARG A 137      -5.108   5.959  16.355  1.00 27.07           C  
ANISOU  890  CD  ARG A 137     3930   3006   3350   -125    246     87       C  
ATOM    891  NE  ARG A 137      -5.890   5.229  15.418  1.00 44.95           N  
ANISOU  891  NE  ARG A 137     6265   5211   5605   -101    255    129       N  
ATOM    892  CZ  ARG A 137      -5.435   4.240  14.691  1.00 46.09           C  
ANISOU  892  CZ  ARG A 137     6471   5289   5753   -134    280    150       C  
ATOM    893  NH1 ARG A 137      -6.227   3.620  13.887  1.00 36.66           N  
ANISOU  893  NH1 ARG A 137     5275   4078   4576   -198    297    132       N  
ATOM    894  NH2 ARG A 137      -4.200   3.886  14.792  1.00 64.98           N  
ANISOU  894  NH2 ARG A 137     8925   7630   8134   -104    287    188       N  
ATOM    895  C   ARG A 137      -2.329   9.389  15.792  1.00 16.22           C  
ANISOU  895  C   ARG A 137     2379   1769   2016    -11    120     11       C  
ATOM    896  O   ARG A 137      -1.202   9.118  16.029  1.00 19.45           O  
ANISOU  896  O   ARG A 137     2804   2196   2391     40    114     42       O  
ATOM    897  N   VAL A 138      -2.730   9.845  14.637  1.00 13.02           N  
ANISOU  897  N   VAL A 138     1953   1326   1667    -37    100    -17       N  
ATOM    898  CA  VAL A 138      -1.735  10.026  13.587  1.00 14.80           C  
ANISOU  898  CA  VAL A 138     2183   1526   1913     -4     72     -8       C  
ATOM    899  CB  VAL A 138      -2.361   9.984  12.194  1.00 17.62           C  
ANISOU  899  CB  VAL A 138     2551   1820   2322    -38     65    -21       C  
ATOM    900  CG1 VAL A 138      -2.922   8.576  11.922  1.00 17.75           C  
ANISOU  900  CG1 VAL A 138     2644   1778   2321    -61    103     17       C  
ATOM    901  CG2 VAL A 138      -3.449  11.055  12.028  1.00 17.56           C  
ANISOU  901  CG2 VAL A 138     2482   1827   2365    -85     50    -77       C  
ATOM    902  C   VAL A 138      -0.927  11.321  13.770  1.00 15.36           C  
ANISOU  902  C   VAL A 138     2189   1652   1996     25     33    -40       C  
ATOM    903  O   VAL A 138       0.000  11.581  13.011  1.00 14.55           O  
ANISOU  903  O   VAL A 138     2082   1537   1908     56      8    -33       O  
ATOM    904  N   LEU A 139      -1.247  12.123  14.792  1.00 15.73           N  
ANISOU  904  N   LEU A 139     2187   1757   2034     14     30    -73       N  
ATOM    905  CA  LEU A 139      -0.446  13.325  15.068  1.00 16.32           C  
ANISOU  905  CA  LEU A 139     2203   1884   2113     39     -5   -103       C  
ATOM    906  CB  LEU A 139      -1.281  14.390  15.782  1.00 15.88           C  
ANISOU  906  CB  LEU A 139     2091   1871   2073      6     -8   -156       C  
ATOM    907  CG  LEU A 139      -2.613  14.757  15.129  1.00 14.60           C  
ANISOU  907  CG  LEU A 139     1909   1674   1964    -45     -4   -191       C  
ATOM    908  CD1 LEU A 139      -3.290  15.828  15.976  1.00 18.95           C  
ANISOU  908  CD1 LEU A 139     2404   2274   2522    -67     -5   -239       C  
ATOM    909  CD2 LEU A 139      -2.434  15.213  13.677  1.00 24.45           C  
ANISOU  909  CD2 LEU A 139     3145   2879   3267    -46    -32   -204       C  
ATOM    910  C   LEU A 139       0.771  13.042  15.926  1.00 16.49           C  
ANISOU  910  C   LEU A 139     2236   1953   2078     88     -7    -69       C  
ATOM    911  O   LEU A 139       1.562  13.956  16.213  1.00 16.14           O  
ANISOU  911  O   LEU A 139     2147   1957   2030    110    -35    -89       O  
ATOM    912  N   GLU A 140       0.927  11.791  16.344  1.00 13.09           N  
ANISOU  912  N   GLU A 140     1862   1510   1601    106     24    -18       N  
ATOM    913  CA  GLU A 140       2.024  11.418  17.251  1.00 18.58           C  
ANISOU  913  CA  GLU A 140     2570   2254   2237    154     27     20       C  
ATOM    914  CB  GLU A 140       2.110   9.886  17.377  1.00 20.12           C  
ANISOU  914  CB  GLU A 140     2841   2414   2390    173     66     81       C  
ATOM    915  CG  GLU A 140       3.227   9.432  18.319  1.00 20.60           C  
ANISOU  915  CG  GLU A 140     2915   2526   2385    227     71    126       C  
ATOM    916  CD  GLU A 140       3.207   7.945  18.627  1.00 36.17           C  
ANISOU  916  CD  GLU A 140     4962   4468   4312    245    115    186       C  
ATOM    917  OE1 GLU A 140       2.136   7.313  18.528  1.00 31.50           O  
ANISOU  917  OE1 GLU A 140     4408   3831   3730    207    146    186       O  
ATOM    918  OE2 GLU A 140       4.279   7.407  18.975  1.00 40.46           O  
ANISOU  918  OE2 GLU A 140     5528   5035   4810    299    119    234       O  
ATOM    919  C   GLU A 140       3.416  11.968  16.888  1.00 14.84           C  
ANISOU  919  C   GLU A 140     2070   1806   1762    199     -9     27       C  
ATOM    920  O   GLU A 140       4.133  12.430  17.794  1.00 16.89           O  
ANISOU  920  O   GLU A 140     2299   2133   1986    223    -23     25       O  
ATOM    921  N   PRO A 141       3.815  11.928  15.595  1.00 15.31           N  
ANISOU  921  N   PRO A 141     2141   1817   1859    211    -24     35       N  
ATOM    922  CA  PRO A 141       5.186  12.384  15.299  1.00 13.98           C  
ANISOU  922  CA  PRO A 141     1949   1676   1685    256    -56     47       C  
ATOM    923  CB  PRO A 141       5.278  12.293  13.770  1.00 18.48           C  
ANISOU  923  CB  PRO A 141     2537   2179   2305    257    -66     50       C  
ATOM    924  CG  PRO A 141       4.244  11.290  13.368  1.00 16.43           C  
ANISOU  924  CG  PRO A 141     2335   1854   2054    227    -31     65       C  
ATOM    925  CD  PRO A 141       3.119  11.475  14.371  1.00 16.65           C  
ANISOU  925  CD  PRO A 141     2346   1909   2073    184    -14     35       C  
ATOM    926  C   PRO A 141       5.459  13.824  15.738  1.00 17.42           C  
ANISOU  926  C   PRO A 141     2311   2173   2133    248    -91     -4       C  
ATOM    927  O   PRO A 141       6.599  14.186  15.973  1.00 18.85           O  
ANISOU  927  O   PRO A 141     2468   2401   2293    283   -115      7       O  
ATOM    928  N   THR A 142       4.400  14.616  15.845  1.00 13.99           N  
ANISOU  928  N   THR A 142     1843   1739   1733    201    -94    -58       N  
ATOM    929  CA  THR A 142       4.513  16.044  16.141  1.00 13.50           C  
ANISOU  929  CA  THR A 142     1715   1725   1690    188   -125   -112       C  
ATOM    930  CB  THR A 142       3.153  16.747  15.865  1.00 13.41           C  
ANISOU  930  CB  THR A 142     1678   1689   1729    135   -121   -166       C  
ATOM    931  OG1 THR A 142       2.692  16.458  14.540  1.00 14.56           O  
ANISOU  931  OG1 THR A 142     1844   1764   1924    122   -120   -164       O  
ATOM    932  CG2 THR A 142       3.249  18.239  16.032  1.00 16.18           C  
ANISOU  932  CG2 THR A 142     1965   2078   2104    123   -150   -223       C  
ATOM    933  C   THR A 142       4.914  16.348  17.593  1.00 13.08           C  
ANISOU  933  C   THR A 142     1638   1749   1582    198   -126   -117       C  
ATOM    934  O   THR A 142       5.637  17.306  17.868  1.00 15.62           O  
ANISOU  934  O   THR A 142     1916   2120   1900    207   -155   -141       O  
ATOM    935  N   PHE A 143       4.437  15.513  18.515  1.00 13.05           N  
ANISOU  935  N   PHE A 143     1667   1757   1535    195    -93    -93       N  
ATOM    936  CA  PHE A 143       4.360  15.877  19.929  1.00 14.18           C  
ANISOU  936  CA  PHE A 143     1788   1968   1634    189    -89   -109       C  
ATOM    937  CB  PHE A 143       2.887  15.866  20.376  1.00 15.21           C  
ANISOU  937  CB  PHE A 143     1922   2084   1776    143    -60   -138       C  
ATOM    938  CG  PHE A 143       2.039  16.846  19.638  1.00 14.17           C  
ANISOU  938  CG  PHE A 143     1754   1922   1709    105    -71   -193       C  
ATOM    939  CD1 PHE A 143       2.226  18.196  19.838  1.00 13.55           C  
ANISOU  939  CD1 PHE A 143     1621   1882   1647     95    -98   -243       C  
ATOM    940  CE1 PHE A 143       1.444  19.137  19.162  1.00 15.16           C  
ANISOU  940  CE1 PHE A 143     1791   2058   1910     63   -107   -293       C  
ATOM    941  CZ  PHE A 143       0.478  18.719  18.282  1.00 13.60           C  
ANISOU  941  CZ  PHE A 143     1611   1799   1756     39    -92   -291       C  
ATOM    942  CE2 PHE A 143       0.255  17.354  18.079  1.00 16.15           C  
ANISOU  942  CE2 PHE A 143     1990   2085   2063     43    -66   -242       C  
ATOM    943  CD2 PHE A 143       1.055  16.419  18.757  1.00 14.37           C  
ANISOU  943  CD2 PHE A 143     1800   1882   1777     77    -55   -193       C  
ATOM    944  C   PHE A 143       5.131  14.985  20.876  1.00 15.39           C  
ANISOU  944  C   PHE A 143     1970   2162   1715    227    -75    -56       C  
ATOM    945  O   PHE A 143       5.294  13.785  20.628  1.00 16.63           O  
ANISOU  945  O   PHE A 143     2179   2285   1853    251    -52     -2       O  
ATOM    946  N   GLY A 144       5.540  15.578  21.998  1.00 13.74           N  
ANISOU  946  N   GLY A 144     1728   2027   1466    232    -87    -72       N  
ATOM    947  CA  GLY A 144       6.186  14.850  23.067  1.00 14.70           C  
ANISOU  947  CA  GLY A 144     1871   2199   1516    265    -74    -26       C  
ATOM    948  C   GLY A 144       5.176  14.220  24.016  1.00 17.65           C  
ANISOU  948  C   GLY A 144     2273   2575   1860    245    -34    -21       C  
ATOM    949  O   GLY A 144       5.480  13.263  24.718  1.00 20.07           O  
ANISOU  949  O   GLY A 144     2615   2900   2111    272    -12     28       O  
ATOM    950  N   GLY A 145       3.963  14.760  24.037  1.00 15.79           N  
ANISOU  950  N   GLY A 145     2021   2318   1659    198    -24    -70       N  
ATOM    951  CA  GLY A 145       2.908  14.193  24.865  1.00 14.82           C  
ANISOU  951  CA  GLY A 145     1923   2193   1514    175     15    -66       C  
ATOM    952  C   GLY A 145       1.578  14.849  24.512  1.00 14.07           C  
ANISOU  952  C   GLY A 145     1807   2065   1474    124     22   -120       C  
ATOM    953  O   GLY A 145       1.559  15.906  23.859  1.00 15.52           O  
ANISOU  953  O   GLY A 145     1950   2242   1706    109     -5   -164       O  
ATOM    954  N   ILE A 146       0.494  14.219  24.951  1.00 15.69           N  
ANISOU  954  N   ILE A 146     2038   2251   1671     99     60   -113       N  
ATOM    955  CA  ILE A 146      -0.872  14.673  24.685  1.00 16.69           C  
ANISOU  955  CA  ILE A 146     2148   2348   1847     51     73   -156       C  
ATOM    956  CB  ILE A 146      -1.681  13.647  23.851  1.00 14.30           C  
ANISOU  956  CB  ILE A 146     1889   1972   1571     31    100   -129       C  
ATOM    957  CG1 ILE A 146      -0.930  13.220  22.584  1.00 22.70           C  
ANISOU  957  CG1 ILE A 146     2977   2989   2660     54     83   -100       C  
ATOM    958  CD1 ILE A 146      -0.741  14.306  21.589  1.00 20.20           C  
ANISOU  958  CD1 ILE A 146     2617   2659   2400     47     46   -141       C  
ATOM    959  CG2 ILE A 146      -3.075  14.202  23.542  1.00 18.51           C  
ANISOU  959  CG2 ILE A 146     2396   2482   2156    -19    110   -173       C  
ATOM    960  C   ILE A 146      -1.636  14.887  25.988  1.00 17.27           C  
ANISOU  960  C   ILE A 146     2210   2465   1889     30     97   -177       C  
ATOM    961  O   ILE A 146      -1.774  13.955  26.775  1.00 16.40           O  
ANISOU  961  O   ILE A 146     2137   2365   1731     38    127   -141       O  
ATOM    962  N   ASN A 147      -2.132  16.106  26.199  1.00 13.41           N  
ANISOU  962  N   ASN A 147     1672   1998   1425      5     86   -234       N  
ATOM    963  CA  ASN A 147      -3.042  16.411  27.298  1.00 16.48           C  
ANISOU  963  CA  ASN A 147     2048   2420   1794    -20    111   -260       C  
ATOM    964  CB  ASN A 147      -2.640  17.708  28.021  1.00 18.36           C  
ANISOU  964  CB  ASN A 147     2240   2717   2018    -18     89   -308       C  
ATOM    965  CG  ASN A 147      -3.553  18.033  29.201  1.00 22.09           C  
ANISOU  965  CG  ASN A 147     2702   3225   2467    -41    117   -334       C  
ATOM    966  OD1 ASN A 147      -3.355  17.540  30.312  1.00 26.82           O  
ANISOU  966  OD1 ASN A 147     3321   3865   3005    -28    134   -312       O  
ATOM    967  ND2 ASN A 147      -4.553  18.878  28.964  1.00 22.76           N  
ANISOU  967  ND2 ASN A 147     2756   3295   2598    -73    123   -381       N  
ATOM    968  C   ASN A 147      -4.455  16.548  26.729  1.00 14.66           C  
ANISOU  968  C   ASN A 147     1808   2145   1619    -62    131   -285       C  
ATOM    969  O   ASN A 147      -4.776  17.548  26.062  1.00 16.26           O  
ANISOU  969  O   ASN A 147     1971   2333   1873    -80    113   -328       O  
ATOM    970  N   LEU A 148      -5.272  15.525  26.933  1.00 17.43           N  
ANISOU  970  N   LEU A 148     2194   2470   1958    -78    168   -255       N  
ATOM    971  CA  LEU A 148      -6.678  15.585  26.548  1.00 19.02           C  
ANISOU  971  CA  LEU A 148     2385   2638   2205   -122    190   -275       C  
ATOM    972  CB  LEU A 148      -7.306  14.182  26.565  1.00 15.43           C  
ANISOU  972  CB  LEU A 148     1981   2146   1733   -136    228   -229       C  
ATOM    973  CG  LEU A 148      -6.703  13.204  25.559  1.00 17.39           C  
ANISOU  973  CG  LEU A 148     2275   2343   1989   -120    221   -184       C  
ATOM    974  CD1 LEU A 148      -7.238  11.794  25.851  1.00 21.25           C  
ANISOU  974  CD1 LEU A 148     2821   2804   2448   -132    263   -137       C  
ATOM    975  CD2 LEU A 148      -7.055  13.625  24.135  1.00 22.14           C  
ANISOU  975  CD2 LEU A 148     2858   2896   2659   -142    200   -206       C  
ATOM    976  C   LEU A 148      -7.392  16.505  27.525  1.00 19.89           C  
ANISOU  976  C   LEU A 148     2457   2793   2309   -140    203   -319       C  
ATOM    977  O   LEU A 148      -7.049  16.530  28.709  1.00 18.25           O  
ANISOU  977  O   LEU A 148     2254   2635   2047   -124    211   -316       O  
ATOM    978  N   GLU A 149      -8.337  17.299  27.038  1.00 16.55           N  
ANISOU  978  N   GLU A 149     1996   2353   1938   -170    203   -359       N  
ATOM    979  CA  GLU A 149      -8.998  18.261  27.910  1.00 17.72           C  
ANISOU  979  CA  GLU A 149     2107   2542   2083   -184    216   -402       C  
ATOM    980  CB  GLU A 149      -8.255  19.601  27.888  1.00 20.04           C  
ANISOU  980  CB  GLU A 149     2362   2864   2387   -169    181   -447       C  
ATOM    981  CG  GLU A 149      -8.741  20.608  28.908  1.00 25.68           C  
ANISOU  981  CG  GLU A 149     3046   3624   3088   -178    195   -491       C  
ATOM    982  CD  GLU A 149      -8.261  20.310  30.329  1.00 33.18           C  
ANISOU  982  CD  GLU A 149     4016   4628   3964   -162    207   -478       C  
ATOM    983  OE1 GLU A 149      -7.200  19.659  30.496  1.00 24.50           O  
ANISOU  983  OE1 GLU A 149     2944   3541   2824   -135    193   -443       O  
ATOM    984  OE2 GLU A 149      -8.958  20.724  31.278  1.00 27.99           O  
ANISOU  984  OE2 GLU A 149     3346   4000   3288   -174    232   -502       O  
ATOM    985  C   GLU A 149     -10.432  18.471  27.491  1.00 19.00           C  
ANISOU  985  C   GLU A 149     2247   2677   2294   -223    238   -421       C  
ATOM    986  O   GLU A 149     -10.726  18.541  26.300  1.00 17.22           O  
ANISOU  986  O   GLU A 149     2012   2409   2122   -237    225   -425       O  
ATOM    987  N   ASP A 150     -11.324  18.547  28.478  1.00 17.59           N  
ANISOU  987  N   ASP A 150     2061   2527   2096   -240    271   -432       N  
ATOM    988  CA  ASP A 150     -12.695  19.033  28.253  1.00 19.19           C  
ANISOU  988  CA  ASP A 150     2230   2718   2344   -274    292   -458       C  
ATOM    989  CB  ASP A 150     -12.648  20.538  27.911  1.00 17.81           C  
ANISOU  989  CB  ASP A 150     2005   2554   2208   -270    269   -512       C  
ATOM    990  CG  ASP A 150     -12.354  21.385  29.151  1.00 22.61           C  
ANISOU  990  CG  ASP A 150     2598   3216   2776   -255    274   -544       C  
ATOM    991  OD1 ASP A 150     -11.943  20.790  30.176  1.00 24.22           O  
ANISOU  991  OD1 ASP A 150     2831   3451   2919   -242    286   -522       O  
ATOM    992  OD2 ASP A 150     -12.516  22.623  29.123  1.00 22.93           O  
ANISOU  992  OD2 ASP A 150     2600   3269   2841   -256    266   -590       O  
ATOM    993  C   ASP A 150     -13.446  18.222  27.205  1.00 20.63           C  
ANISOU  993  C   ASP A 150     2424   2848   2566   -302    301   -431       C  
ATOM    994  O   ASP A 150     -14.072  18.746  26.275  1.00 20.25           O  
ANISOU  994  O   ASP A 150     2344   2775   2574   -322    292   -452       O  
ATOM    995  N   ILE A 151     -13.389  16.914  27.430  1.00 16.07           N  
ANISOU  995  N   ILE A 151     1895   2256   1954   -304    320   -385       N  
ATOM    996  CA  ILE A 151     -14.116  15.913  26.679  1.00 15.94           C  
ANISOU  996  CA  ILE A 151     1903   2193   1960   -335    336   -353       C  
ATOM    997  CB  ILE A 151     -13.190  14.851  26.118  1.00 18.44           C  
ANISOU  997  CB  ILE A 151     2273   2474   2259   -318    324   -310       C  
ATOM    998  CG1 ILE A 151     -12.169  15.508  25.185  1.00 17.88           C  
ANISOU  998  CG1 ILE A 151     2188   2390   2216   -292    279   -325       C  
ATOM    999  CD1 ILE A 151     -11.088  14.523  24.715  1.00 18.52           C  
ANISOU  999  CD1 ILE A 151     2322   2441   2275   -266    267   -282       C  
ATOM   1000  CG2 ILE A 151     -13.961  13.789  25.341  1.00 20.31           C  
ANISOU 1000  CG2 ILE A 151     2541   2659   2517   -354    342   -278       C  
ATOM   1001  C   ILE A 151     -15.099  15.290  27.647  1.00 21.46           C  
ANISOU 1001  C   ILE A 151     2615   2909   2631   -359    381   -337       C  
ATOM   1002  O   ILE A 151     -14.713  14.890  28.747  1.00 21.96           O  
ANISOU 1002  O   ILE A 151     2704   3002   2638   -341    398   -321       O  
ATOM   1003  N   LYS A 152     -16.351  15.189  27.233  1.00 19.03           N  
ANISOU 1003  N   LYS A 152     2289   2582   2359   -400    400   -340       N  
ATOM   1004  CA  LYS A 152     -17.383  14.715  28.160  1.00 26.53           C  
ANISOU 1004  CA  LYS A 152     3244   3552   3286   -426    445   -328       C  
ATOM   1005  CB  LYS A 152     -18.789  15.046  27.647  1.00 23.85           C  
ANISOU 1005  CB  LYS A 152     2862   3203   2998   -469    459   -344       C  
ATOM   1006  CG  LYS A 152     -19.187  14.309  26.378  1.00 26.68           C  
ANISOU 1006  CG  LYS A 152     3236   3509   3393   -503    452   -321       C  
ATOM   1007  CD  LYS A 152     -20.608  14.644  25.951  1.00 33.17           C  
ANISOU 1007  CD  LYS A 152     4012   4330   4262   -546    467   -334       C  
ATOM   1008  CE  LYS A 152     -21.646  13.972  26.849  1.00 40.97           C  
ANISOU 1008  CE  LYS A 152     5008   5336   5223   -577    514   -314       C  
ATOM   1009  NZ  LYS A 152     -21.717  12.493  26.623  1.00 39.45           N  
ANISOU 1009  NZ  LYS A 152     4874   5104   5009   -604    531   -268       N  
ATOM   1010  C   LYS A 152     -17.274  13.213  28.421  1.00 23.31           C  
ANISOU 1010  C   LYS A 152     2899   3122   2837   -432    469   -276       C  
ATOM   1011  O   LYS A 152     -16.724  12.452  27.611  1.00 21.91           O  
ANISOU 1011  O   LYS A 152     2760   2901   2663   -430    455   -248       O  
ATOM   1012  N   ALA A 153     -17.794  12.799  29.578  1.00 22.12           N  
ANISOU 1012  N   ALA A 153     2760   2998   2645   -440    507   -263       N  
ATOM   1013  CA  ALA A 153     -17.976  11.383  29.886  1.00 30.43           C  
ANISOU 1013  CA  ALA A 153     3870   4029   3662   -454    539   -214       C  
ATOM   1014  CB  ALA A 153     -18.023  11.175  31.400  1.00 33.75           C  
ANISOU 1014  CB  ALA A 153     4304   4495   4025   -440    572   -205       C  
ATOM   1015  C   ALA A 153     -19.255  10.844  29.229  1.00 31.71           C  
ANISOU 1015  C   ALA A 153     4029   4158   3861   -510    561   -203       C  
ATOM   1016  O   ALA A 153     -20.214  11.589  29.016  1.00 29.86           O  
ANISOU 1016  O   ALA A 153     3742   3936   3668   -536    563   -232       O  
ATOM   1017  N   PRO A 154     -19.278   9.548  28.888  1.00 25.67           N  
ANISOU 1017  N   PRO A 154     3321   3350   3082   -529    577   -160       N  
ATOM   1018  CA  PRO A 154     -18.245   8.525  29.060  1.00 26.72           C  
ANISOU 1018  CA  PRO A 154     3522   3462   3169   -500    580   -120       C  
ATOM   1019  CB  PRO A 154     -19.059   7.234  29.096  1.00 35.84           C  
ANISOU 1019  CB  PRO A 154     4723   4583   4310   -542    621    -81       C  
ATOM   1020  CG  PRO A 154     -20.155   7.503  28.151  1.00 33.51           C  
ANISOU 1020  CG  PRO A 154     4392   4268   4074   -595    617    -99       C  
ATOM   1021  CD  PRO A 154     -20.515   8.962  28.337  1.00 30.39           C  
ANISOU 1021  CD  PRO A 154     3919   3918   3709   -588    600   -148       C  
ATOM   1022  C   PRO A 154     -17.247   8.472  27.919  1.00 26.55           C  
ANISOU 1022  C   PRO A 154     3519   3401   3167   -478    542   -114       C  
ATOM   1023  O   PRO A 154     -16.334   7.654  27.977  1.00 26.19           O  
ANISOU 1023  O   PRO A 154     3529   3336   3084   -449    544    -79       O  
ATOM   1024  N   GLU A 155     -17.428   9.306  26.901  1.00 22.48           N  
ANISOU 1024  N   GLU A 155     2960   2874   2708   -490    511   -146       N  
ATOM   1025  CA  GLU A 155     -16.549   9.260  25.740  1.00 26.03           C  
ANISOU 1025  CA  GLU A 155     3428   3284   3180   -472    475   -141       C  
ATOM   1026  CB  GLU A 155     -16.948  10.319  24.713  1.00 24.94           C  
ANISOU 1026  CB  GLU A 155     3231   3139   3106   -489    444   -182       C  
ATOM   1027  CG  GLU A 155     -18.210   9.963  23.927  1.00 30.41           C  
ANISOU 1027  CG  GLU A 155     3915   3799   3838   -549    457   -179       C  
ATOM   1028  CD  GLU A 155     -19.480  10.586  24.511  1.00 35.63           C  
ANISOU 1028  CD  GLU A 155     4521   4500   4517   -580    478   -204       C  
ATOM   1029  OE1 GLU A 155     -19.531  10.862  25.731  1.00 35.30           O  
ANISOU 1029  OE1 GLU A 155     4468   4503   4441   -563    498   -211       O  
ATOM   1030  OE2 GLU A 155     -20.432  10.810  23.734  1.00 44.32           O  
ANISOU 1030  OE2 GLU A 155     5589   5587   5663   -621    475   -216       O  
ATOM   1031  C   GLU A 155     -15.089   9.437  26.158  1.00 28.62           C  
ANISOU 1031  C   GLU A 155     3771   3632   3470   -412    454   -135       C  
ATOM   1032  O   GLU A 155     -14.196   8.810  25.587  1.00 22.58           O  
ANISOU 1032  O   GLU A 155     3051   2834   2696   -389    442   -107       O  
ATOM   1033  N   CYS A 156     -14.854  10.269  27.168  1.00 22.07           N  
ANISOU 1033  N   CYS A 156     2908   2860   2619   -387    451   -160       N  
ATOM   1034  CA  CYS A 156     -13.484  10.581  27.570  1.00 22.24           C  
ANISOU 1034  CA  CYS A 156     2935   2909   2607   -333    427   -159       C  
ATOM   1035  CB  CYS A 156     -13.472  11.729  28.583  1.00 23.43           C  
ANISOU 1035  CB  CYS A 156     3036   3122   2743   -318    422   -198       C  
ATOM   1036  SG  CYS A 156     -14.360  11.370  30.117  1.00 25.13           S  
ANISOU 1036  SG  CYS A 156     3258   3378   2912   -333    472   -190       S  
ATOM   1037  C   CYS A 156     -12.774   9.355  28.146  1.00 21.49           C  
ANISOU 1037  C   CYS A 156     2906   2808   2452   -306    448   -107       C  
ATOM   1038  O   CYS A 156     -11.552   9.217  28.024  1.00 20.31           O  
ANISOU 1038  O   CYS A 156     2778   2659   2280   -263    426    -89       O  
ATOM   1039  N   PHE A 157     -13.526   8.456  28.777  1.00 20.33           N  
ANISOU 1039  N   PHE A 157     2792   2656   2278   -330    490    -80       N  
ATOM   1040  CA  PHE A 157     -12.894   7.246  29.291  1.00 19.35           C  
ANISOU 1040  CA  PHE A 157     2734   2522   2097   -304    514    -28       C  
ATOM   1041  CB  PHE A 157     -13.846   6.447  30.165  1.00 22.15           C  
ANISOU 1041  CB  PHE A 157     3115   2879   2421   -333    563     -6       C  
ATOM   1042  CG  PHE A 157     -14.425   7.228  31.305  1.00 22.63           C  
ANISOU 1042  CG  PHE A 157     3130   3000   2468   -338    576    -37       C  
ATOM   1043  CD1 PHE A 157     -13.619   8.005  32.119  1.00 27.47           C  
ANISOU 1043  CD1 PHE A 157     3717   3669   3050   -296    557    -55       C  
ATOM   1044  CE1 PHE A 157     -14.167   8.721  33.179  1.00 28.59           C  
ANISOU 1044  CE1 PHE A 157     3822   3864   3177   -302    571    -84       C  
ATOM   1045  CZ  PHE A 157     -15.533   8.661  33.429  1.00 32.35           C  
ANISOU 1045  CZ  PHE A 157     4283   4338   3671   -347    604    -94       C  
ATOM   1046  CE2 PHE A 157     -16.344   7.880  32.625  1.00 34.75           C  
ANISOU 1046  CE2 PHE A 157     4609   4589   4006   -389    622    -74       C  
ATOM   1047  CD2 PHE A 157     -15.788   7.172  31.567  1.00 28.05           C  
ANISOU 1047  CD2 PHE A 157     3800   3687   3171   -386    607    -46       C  
ATOM   1048  C   PHE A 157     -12.435   6.378  28.131  1.00 21.03           C  
ANISOU 1048  C   PHE A 157     2996   2670   2323   -302    507      5       C  
ATOM   1049  O   PHE A 157     -11.318   5.859  28.125  1.00 23.94           O  
ANISOU 1049  O   PHE A 157     3405   3032   2659   -258    501     38       O  
ATOM   1050  N   GLU A 158     -13.310   6.206  27.153  1.00 18.91           N  
ANISOU 1050  N   GLU A 158     2727   2355   2102   -349    510     -2       N  
ATOM   1051  CA  GLU A 158     -12.984   5.340  26.025  1.00 23.09           C  
ANISOU 1051  CA  GLU A 158     3309   2819   2645   -354    507     28       C  
ATOM   1052  CB  GLU A 158     -14.225   5.070  25.174  1.00 29.67           C  
ANISOU 1052  CB  GLU A 158     4141   3608   3524   -418    519     20       C  
ATOM   1053  CG  GLU A 158     -14.057   3.914  24.191  1.00 51.11           C  
ANISOU 1053  CG  GLU A 158     6926   6252   6242   -432    528     58       C  
ATOM   1054  CD  GLU A 158     -15.341   3.588  23.449  1.00 63.25           C  
ANISOU 1054  CD  GLU A 158     8463   7751   7817   -502    542     51       C  
ATOM   1055  OE1 GLU A 158     -16.416   4.069  23.877  1.00 66.39           O  
ANISOU 1055  OE1 GLU A 158     8813   8179   8232   -539    552     26       O  
ATOM   1056  OE2 GLU A 158     -15.274   2.858  22.435  1.00 63.04           O  
ANISOU 1056  OE2 GLU A 158     8485   7665   7804   -520    542     71       O  
ATOM   1057  C   GLU A 158     -11.869   5.948  25.166  1.00 20.72           C  
ANISOU 1057  C   GLU A 158     2993   2511   2367   -315    461     17       C  
ATOM   1058  O   GLU A 158     -11.004   5.227  24.657  1.00 21.70           O  
ANISOU 1058  O   GLU A 158     3168   2600   2476   -287    458     52       O  
ATOM   1059  N   ILE A 159     -11.896   7.266  25.005  1.00 20.72           N  
ANISOU 1059  N   ILE A 159     2925   2544   2403   -314    428    -31       N  
ATOM   1060  CA  ILE A 159     -10.874   7.960  24.211  1.00 17.95           C  
ANISOU 1060  CA  ILE A 159     2554   2190   2076   -280    384    -46       C  
ATOM   1061  CB  ILE A 159     -11.242   9.427  24.005  1.00 18.43           C  
ANISOU 1061  CB  ILE A 159     2538   2282   2184   -292    354   -103       C  
ATOM   1062  CG1 ILE A 159     -12.346   9.535  22.947  1.00 16.93           C  
ANISOU 1062  CG1 ILE A 159     2330   2051   2051   -344    353   -121       C  
ATOM   1063  CD1 ILE A 159     -13.042  10.886  22.920  1.00 19.64           C  
ANISOU 1063  CD1 ILE A 159     2598   2426   2438   -363    337   -174       C  
ATOM   1064  CG2 ILE A 159     -10.017  10.251  23.596  1.00 22.32           C  
ANISOU 1064  CG2 ILE A 159     3006   2789   2685   -248    311   -119       C  
ATOM   1065  C   ILE A 159      -9.509   7.848  24.874  1.00 19.49           C  
ANISOU 1065  C   ILE A 159     2768   2418   2220   -220    375    -23       C  
ATOM   1066  O   ILE A 159      -8.522   7.460  24.225  1.00 18.66           O  
ANISOU 1066  O   ILE A 159     2694   2286   2111   -187    359      3       O  
ATOM   1067  N   GLU A 160      -9.430   8.159  26.163  1.00 17.75           N  
ANISOU 1067  N   GLU A 160     2529   2256   1959   -204    385    -29       N  
ATOM   1068  CA  GLU A 160      -8.128   8.070  26.822  1.00 22.03           C  
ANISOU 1068  CA  GLU A 160     3085   2835   2449   -147    374     -6       C  
ATOM   1069  CB  GLU A 160      -8.190   8.577  28.259  1.00 21.52           C  
ANISOU 1069  CB  GLU A 160     2993   2840   2344   -138    383    -22       C  
ATOM   1070  CG  GLU A 160      -6.790   8.892  28.778  1.00 22.88           C  
ANISOU 1070  CG  GLU A 160     3159   3060   2474    -83    358    -13       C  
ATOM   1071  CD  GLU A 160      -6.709   9.029  30.282  1.00 27.16           C  
ANISOU 1071  CD  GLU A 160     3692   3667   2958    -68    373    -13       C  
ATOM   1072  OE1 GLU A 160      -7.415   8.285  30.996  1.00 34.87           O  
ANISOU 1072  OE1 GLU A 160     4699   4643   3907    -83    413      8       O  
ATOM   1073  OE2 GLU A 160      -5.902   9.858  30.747  1.00 23.99           O  
ANISOU 1073  OE2 GLU A 160     3257   3319   2538    -41    344    -34       O  
ATOM   1074  C   GLU A 160      -7.583   6.634  26.791  1.00 20.38           C  
ANISOU 1074  C   GLU A 160     2953   2592   2200   -123    400     56       C  
ATOM   1075  O   GLU A 160      -6.395   6.411  26.505  1.00 21.16           O  
ANISOU 1075  O   GLU A 160     3072   2688   2281    -78    382     83       O  
ATOM   1076  N   GLU A 161      -8.462   5.669  27.030  1.00 22.64           N  
ANISOU 1076  N   GLU A 161     3281   2848   2473   -154    442     81       N  
ATOM   1077  CA  GLU A 161      -8.061   4.270  27.073  1.00 23.26           C  
ANISOU 1077  CA  GLU A 161     3437   2890   2511   -134    473    140       C  
ATOM   1078  CB  GLU A 161      -9.237   3.386  27.477  1.00 31.83           C  
ANISOU 1078  CB  GLU A 161     4558   3950   3585   -179    521    157       C  
ATOM   1079  CG  GLU A 161      -8.870   1.948  27.741  1.00 49.48           C  
ANISOU 1079  CG  GLU A 161     6876   6153   5771   -158    560    219       C  
ATOM   1080  CD  GLU A 161     -10.055   1.144  28.242  1.00 67.98           C  
ANISOU 1080  CD  GLU A 161     9252   8476   8102   -205    609    232       C  
ATOM   1081  OE1 GLU A 161     -11.124   1.184  27.590  1.00 72.25           O  
ANISOU 1081  OE1 GLU A 161     9782   8982   8686   -263    614    211       O  
ATOM   1082  OE2 GLU A 161      -9.928   0.489  29.297  1.00 72.78           O  
ANISOU 1082  OE2 GLU A 161     9893   9104   8654   -184    642    265       O  
ATOM   1083  C   GLU A 161      -7.510   3.823  25.727  1.00 25.40           C  
ANISOU 1083  C   GLU A 161     3743   3099   2809   -125    459    160       C  
ATOM   1084  O   GLU A 161      -6.459   3.187  25.659  1.00 24.62           O  
ANISOU 1084  O   GLU A 161     3688   2991   2678    -77    460    202       O  
ATOM   1085  N   ARG A 162      -8.206   4.182  24.655  1.00 24.49           N  
ANISOU 1085  N   ARG A 162     3607   2944   2752   -168    444    131       N  
ATOM   1086  CA  ARG A 162      -7.767   3.763  23.335  1.00 26.46           C  
ANISOU 1086  CA  ARG A 162     3892   3132   3029   -163    431    147       C  
ATOM   1087  CB  ARG A 162      -8.845   3.992  22.285  1.00 28.17           C  
ANISOU 1087  CB  ARG A 162     4092   3306   3306   -223    425    117       C  
ATOM   1088  CG  ARG A 162      -8.506   3.199  21.031  1.00 37.24           C  
ANISOU 1088  CG  ARG A 162     5298   4381   4470   -223    425    145       C  
ATOM   1089  CD  ARG A 162      -9.397   3.471  19.856  1.00 42.01           C  
ANISOU 1089  CD  ARG A 162     5885   4943   5133   -278    411    116       C  
ATOM   1090  NE  ARG A 162      -8.747   3.015  18.627  1.00 33.73           N  
ANISOU 1090  NE  ARG A 162     4881   3836   4100   -264    399    136       N  
ATOM   1091  CZ  ARG A 162      -9.171   3.325  17.409  1.00 47.46           C  
ANISOU 1091  CZ  ARG A 162     6605   5537   5890   -298    378    112       C  
ATOM   1092  NH1 ARG A 162     -10.247   4.086  17.260  1.00 44.96           N  
ANISOU 1092  NH1 ARG A 162     6231   5237   5615   -347    367     70       N  
ATOM   1093  NH2 ARG A 162      -8.518   2.881  16.342  1.00 51.97           N  
ANISOU 1093  NH2 ARG A 162     7220   6054   6470   -281    368    133       N  
ATOM   1094  C   ARG A 162      -6.482   4.466  22.899  1.00 29.29           C  
ANISOU 1094  C   ARG A 162     4224   3511   3395   -111    388    141       C  
ATOM   1095  O   ARG A 162      -5.592   3.828  22.330  1.00 26.17           O  
ANISOU 1095  O   ARG A 162     3875   3082   2987    -76    387    178       O  
ATOM   1096  N   LEU A 163      -6.363   5.765  23.169  1.00 21.25           N  
ANISOU 1096  N   LEU A 163     3133   2545   2395   -107    355     96       N  
ATOM   1097  CA  LEU A 163      -5.163   6.482  22.723  1.00 18.85           C  
ANISOU 1097  CA  LEU A 163     2801   2260   2100    -62    313     87       C  
ATOM   1098  CB  LEU A 163      -5.357   7.996  22.840  1.00 17.59           C  
ANISOU 1098  CB  LEU A 163     2561   2147   1975    -75    279     27       C  
ATOM   1099  CG  LEU A 163      -6.310   8.562  21.777  1.00 17.40           C  
ANISOU 1099  CG  LEU A 163     2506   2085   2018   -123    265    -12       C  
ATOM   1100  CD1 LEU A 163      -6.521  10.055  21.980  1.00 19.22           C  
ANISOU 1100  CD1 LEU A 163     2660   2362   2280   -132    237    -69       C  
ATOM   1101  CD2 LEU A 163      -5.831   8.255  20.344  1.00 20.14           C  
ANISOU 1101  CD2 LEU A 163     2881   2373   2399   -116    248      3       C  
ATOM   1102  C   LEU A 163      -3.940   6.027  23.506  1.00 26.72           C  
ANISOU 1102  C   LEU A 163     3824   3293   3036     -2    317    129       C  
ATOM   1103  O   LEU A 163      -2.840   5.973  22.956  1.00 22.97           O  
ANISOU 1103  O   LEU A 163     3360   2811   2558     40    296    150       O  
ATOM   1104  N   LYS A 164      -4.127   5.688  24.780  1.00 23.27           N  
ANISOU 1104  N   LYS A 164     3397   2896   2549      3    344    144       N  
ATOM   1105  CA  LYS A 164      -3.015   5.214  25.600  1.00 29.73           C  
ANISOU 1105  CA  LYS A 164     4238   3752   3304     60    350    187       C  
ATOM   1106  CB  LYS A 164      -3.434   5.054  27.076  1.00 25.01           C  
ANISOU 1106  CB  LYS A 164     3641   3206   2657     57    378    191       C  
ATOM   1107  CG  LYS A 164      -3.448   6.376  27.833  1.00 28.75           C  
ANISOU 1107  CG  LYS A 164     4042   3752   3131     53    350    141       C  
ATOM   1108  CD  LYS A 164      -4.007   6.248  29.251  1.00 30.96           C  
ANISOU 1108  CD  LYS A 164     4321   4077   3365     43    380    141       C  
ATOM   1109  CE  LYS A 164      -3.026   5.563  30.182  1.00 35.28           C  
ANISOU 1109  CE  LYS A 164     4901   4665   3840     96    392    191       C  
ATOM   1110  NZ  LYS A 164      -3.621   5.398  31.541  1.00 38.38           N  
ANISOU 1110  NZ  LYS A 164     5295   5099   4188     86    423    192       N  
ATOM   1111  C   LYS A 164      -2.484   3.902  25.028  1.00 33.07           C  
ANISOU 1111  C   LYS A 164     4739   4120   3708     88    373    248       C  
ATOM   1112  O   LYS A 164      -1.291   3.626  25.114  1.00 33.93           O  
ANISOU 1112  O   LYS A 164     4864   4246   3783    144    365    284       O  
ATOM   1113  N   LYS A 165      -3.361   3.117  24.406  1.00 28.25           N  
ANISOU 1113  N   LYS A 165     4174   3441   3118     49    402    258       N  
ATOM   1114  CA  LYS A 165      -2.945   1.854  23.802  1.00 36.26           C  
ANISOU 1114  CA  LYS A 165     5268   4393   4116     71    429    313       C  
ATOM   1115  CB  LYS A 165      -4.134   0.897  23.691  1.00 43.30           C  
ANISOU 1115  CB  LYS A 165     6214   5228   5012     19    473    324       C  
ATOM   1116  CG  LYS A 165      -4.614   0.365  25.033  1.00 46.27           C  
ANISOU 1116  CG  LYS A 165     6609   5635   5338     14    513    343       C  
ATOM   1117  CD  LYS A 165      -5.655  -0.735  24.865  1.00 50.70           C  
ANISOU 1117  CD  LYS A 165     7233   6133   5899    -34    560    363       C  
ATOM   1118  CE  LYS A 165      -6.874  -0.247  24.104  1.00 51.63           C  
ANISOU 1118  CE  LYS A 165     7318   6221   6077   -105    550    316       C  
ATOM   1119  NZ  LYS A 165      -8.083  -1.049  24.434  1.00 54.97           N  
ANISOU 1119  NZ  LYS A 165     7780   6615   6493   -160    595    325       N  
ATOM   1120  C   LYS A 165      -2.313   2.048  22.425  1.00 32.94           C  
ANISOU 1120  C   LYS A 165     4850   3930   3736     85    399    311       C  
ATOM   1121  O   LYS A 165      -1.366   1.351  22.066  1.00 39.85           O  
ANISOU 1121  O   LYS A 165     5772   4781   4587    132    406    358       O  
ATOM   1122  N   GLU A 166      -2.841   2.990  21.654  1.00 24.01           N  
ANISOU 1122  N   GLU A 166     3669   2790   2664     47    368    260       N  
ATOM   1123  CA  GLU A 166      -2.429   3.142  20.260  1.00 24.91           C  
ANISOU 1123  CA  GLU A 166     3787   2855   2820     51    343    256       C  
ATOM   1124  CB  GLU A 166      -3.572   3.743  19.419  1.00 34.64           C  
ANISOU 1124  CB  GLU A 166     4987   4057   4117    -13    329    206       C  
ATOM   1125  CG  GLU A 166      -4.849   2.891  19.338  1.00 37.28           C  
ANISOU 1125  CG  GLU A 166     5366   4343   4456    -71    368    212       C  
ATOM   1126  CD  GLU A 166      -4.969   2.062  18.061  1.00 42.45           C  
ANISOU 1126  CD  GLU A 166     6082   4915   5132    -89    379    233       C  
ATOM   1127  OE1 GLU A 166      -3.936   1.619  17.499  1.00 42.83           O  
ANISOU 1127  OE1 GLU A 166     6171   4935   5169    -43    375    267       O  
ATOM   1128  OE2 GLU A 166      -6.118   1.842  17.621  1.00 44.44           O  
ANISOU 1128  OE2 GLU A 166     6343   5130   5412   -150    392    217       O  
ATOM   1129  C   GLU A 166      -1.181   4.002  20.097  1.00 29.94           C  
ANISOU 1129  C   GLU A 166     4380   3535   3461    102    300    248       C  
ATOM   1130  O   GLU A 166      -0.435   3.831  19.127  1.00 29.08           O  
ANISOU 1130  O   GLU A 166     4291   3391   3366    129    286    267       O  
ATOM   1131  N   MET A 167      -0.963   4.942  21.017  1.00 25.53           N  
ANISOU 1131  N   MET A 167     3760   3051   2890    112    278    221       N  
ATOM   1132  CA  MET A 167       0.122   5.914  20.851  1.00 17.58           C  
ANISOU 1132  CA  MET A 167     2702   2088   1891    150    234    205       C  
ATOM   1133  CB  MET A 167      -0.373   7.328  21.163  1.00 21.33           C  
ANISOU 1133  CB  MET A 167     3097   2609   2397    119    204    140       C  
ATOM   1134  CG  MET A 167      -1.587   7.727  20.325  1.00 21.39           C  
ANISOU 1134  CG  MET A 167     3087   2572   2466     60    202     98       C  
ATOM   1135  SD  MET A 167      -2.097   9.434  20.529  1.00 21.74           S  
ANISOU 1135  SD  MET A 167     3041   2666   2553     29    167     23       S  
ATOM   1136  CE  MET A 167      -0.720  10.240  19.687  1.00 20.25           C  
ANISOU 1136  CE  MET A 167     2821   2487   2386     72    118     16       C  
ATOM   1137  C   MET A 167       1.338   5.589  21.716  1.00 21.07           C  
ANISOU 1137  C   MET A 167     3153   2582   2270    212    235    249       C  
ATOM   1138  O   MET A 167       1.196   5.013  22.796  1.00 27.74           O  
ANISOU 1138  O   MET A 167     4021   3454   3065    220    265    273       O  
ATOM   1139  N   ASN A 168       2.530   5.938  21.220  1.00 19.48           N  
ANISOU 1139  N   ASN A 168     2935   2395   2072    256    204    260       N  
ATOM   1140  CA  ASN A 168       3.781   5.660  21.929  1.00 23.21           C  
ANISOU 1140  CA  ASN A 168     3412   2920   2487    318    202    304       C  
ATOM   1141  CB  ASN A 168       4.824   5.066  20.966  1.00 26.97           C  
ANISOU 1141  CB  ASN A 168     3926   3358   2963    366    198    351       C  
ATOM   1142  CG  ASN A 168       5.925   4.306  21.690  1.00 41.78           C  
ANISOU 1142  CG  ASN A 168     5830   5272   4771    431    214    415       C  
ATOM   1143  OD1 ASN A 168       5.666   3.563  22.640  1.00 44.02           O  
ANISOU 1143  OD1 ASN A 168     6148   5570   5007    438    248    445       O  
ATOM   1144  ND2 ASN A 168       7.165   4.498  21.246  1.00 46.48           N  
ANISOU 1144  ND2 ASN A 168     6411   5886   5362    481    188    439       N  
ATOM   1145  C   ASN A 168       4.351   6.906  22.597  1.00 20.58           C  
ANISOU 1145  C   ASN A 168     3003   2670   2145    327    161    269       C  
ATOM   1146  O   ASN A 168       5.568   7.009  22.808  1.00 20.41           O  
ANISOU 1146  O   ASN A 168     2968   2694   2093    377    142    295       O  
ATOM   1147  N   ILE A 169       3.469   7.858  22.910  1.00 20.37           N  
ANISOU 1147  N   ILE A 169     2929   2664   2147    279    149    209       N  
ATOM   1148  CA  ILE A 169       3.821   9.029  23.704  1.00 18.23           C  
ANISOU 1148  CA  ILE A 169     2592   2471   1864    279    118    170       C  
ATOM   1149  CB  ILE A 169       3.871  10.334  22.860  1.00 19.52           C  
ANISOU 1149  CB  ILE A 169     2698   2632   2088    258     75    114       C  
ATOM   1150  CG1 ILE A 169       2.534  10.598  22.154  1.00 14.55           C  
ANISOU 1150  CG1 ILE A 169     2065   1946   1518    203     83     72       C  
ATOM   1151  CD1 ILE A 169       2.516  11.984  21.458  1.00 19.21           C  
ANISOU 1151  CD1 ILE A 169     2593   2540   2165    182     43     14       C  
ATOM   1152  CG2 ILE A 169       5.063  10.307  21.857  1.00 17.66           C  
ANISOU 1152  CG2 ILE A 169     2465   2381   1866    300     49    140       C  
ATOM   1153  C   ILE A 169       2.778   9.156  24.816  1.00 14.84           C  
ANISOU 1153  C   ILE A 169     2154   2070   1416    243    141    144       C  
ATOM   1154  O   ILE A 169       1.695   8.564  24.708  1.00 22.53           O  
ANISOU 1154  O   ILE A 169     3161   2997   2404    209    173    145       O  
ATOM   1155  N   PRO A 170       3.102   9.896  25.895  1.00 18.51           N  
ANISOU 1155  N   PRO A 170     2575   2611   1847    249    125    122       N  
ATOM   1156  CA  PRO A 170       2.149  10.028  27.002  1.00 23.46           C  
ANISOU 1156  CA  PRO A 170     3195   3267   2453    217    148     98       C  
ATOM   1157  CB  PRO A 170       2.857  10.982  27.961  1.00 22.81           C  
ANISOU 1157  CB  PRO A 170     3062   3269   2334    231    119     74       C  
ATOM   1158  CG  PRO A 170       4.317  10.755  27.681  1.00 21.83           C  
ANISOU 1158  CG  PRO A 170     2941   3168   2186    284     95    116       C  
ATOM   1159  CD  PRO A 170       4.370  10.582  26.197  1.00 21.47           C  
ANISOU 1159  CD  PRO A 170     2910   3050   2196    284     87    122       C  
ATOM   1160  C   PRO A 170       0.816  10.605  26.573  1.00 25.43           C  
ANISOU 1160  C   PRO A 170     3423   3479   2760    160    153     45       C  
ATOM   1161  O   PRO A 170       0.778  11.552  25.799  1.00 18.35           O  
ANISOU 1161  O   PRO A 170     2487   2571   1914    144    123      3       O  
ATOM   1162  N   VAL A 171      -0.259  10.019  27.082  1.00 18.53           N  
ANISOU 1162  N   VAL A 171     2576   2588   1876    132    192     50       N  
ATOM   1163  CA  VAL A 171      -1.605  10.507  26.854  1.00 18.62           C  
ANISOU 1163  CA  VAL A 171     2566   2573   1935     78    202      4       C  
ATOM   1164  CB  VAL A 171      -2.426   9.581  25.943  1.00 22.22           C  
ANISOU 1164  CB  VAL A 171     3067   2951   2424     51    229     24       C  
ATOM   1165  CG1 VAL A 171      -3.856  10.121  25.832  1.00 21.97           C  
ANISOU 1165  CG1 VAL A 171     3007   2904   2438     -6    239    -22       C  
ATOM   1166  CG2 VAL A 171      -1.789   9.487  24.574  1.00 20.35           C  
ANISOU 1166  CG2 VAL A 171     2842   2666   2225     67    205     36       C  
ATOM   1167  C   VAL A 171      -2.260  10.608  28.217  1.00 23.70           C  
ANISOU 1167  C   VAL A 171     3200   3264   2540     62    226    -10       C  
ATOM   1168  O   VAL A 171      -2.279   9.641  28.977  1.00 23.74           O  
ANISOU 1168  O   VAL A 171     3248   3278   2496     75    258     32       O  
ATOM   1169  N   PHE A 172      -2.786  11.779  28.534  1.00 17.32           N  
ANISOU 1169  N   PHE A 172     2339   2486   1754     35    213    -66       N  
ATOM   1170  CA  PHE A 172      -3.256  12.061  29.898  1.00 17.38           C  
ANISOU 1170  CA  PHE A 172     2333   2547   1722     24    232    -84       C  
ATOM   1171  CB  PHE A 172      -2.096  12.664  30.704  1.00 17.65           C  
ANISOU 1171  CB  PHE A 172     2343   2654   1710     59    204    -89       C  
ATOM   1172  CG  PHE A 172      -2.421  13.052  32.128  1.00 21.98           C  
ANISOU 1172  CG  PHE A 172     2876   3264   2212     51    219   -109       C  
ATOM   1173  CD2 PHE A 172      -2.248  12.146  33.174  1.00 22.42           C  
ANISOU 1173  CD2 PHE A 172     2967   3349   2201     72    246    -66       C  
ATOM   1174  CE2 PHE A 172      -2.489  12.531  34.495  1.00 20.72           C  
ANISOU 1174  CE2 PHE A 172     2738   3193   1941     67    258    -85       C  
ATOM   1175  CZ  PHE A 172      -2.886  13.815  34.778  1.00 27.01           C  
ANISOU 1175  CZ  PHE A 172     3487   4018   2758     41    243   -147       C  
ATOM   1176  CE1 PHE A 172      -3.043  14.736  33.750  1.00 25.39           C  
ANISOU 1176  CE1 PHE A 172     3246   3783   2618     22    217   -190       C  
ATOM   1177  CD1 PHE A 172      -2.799  14.348  32.434  1.00 21.38           C  
ANISOU 1177  CD1 PHE A 172     2750   3218   2155     27    204   -170       C  
ATOM   1178  C   PHE A 172      -4.442  13.000  29.820  1.00 19.85           C  
ANISOU 1178  C   PHE A 172     2605   2855   2082    -22    235   -141       C  
ATOM   1179  O   PHE A 172      -4.330  14.094  29.270  1.00 18.93           O  
ANISOU 1179  O   PHE A 172     2445   2741   2007    -30    204   -184       O  
ATOM   1180  N   HIS A 173      -5.586  12.575  30.352  1.00 19.06           N  
ANISOU 1180  N   HIS A 173     2519   2747   1977    -51    274   -140       N  
ATOM   1181  CA  HIS A 173      -6.752  13.465  30.393  1.00 19.27           C  
ANISOU 1181  CA  HIS A 173     2504   2775   2044    -92    281   -191       C  
ATOM   1182  CB  HIS A 173      -8.047  12.699  30.103  1.00 18.04           C  
ANISOU 1182  CB  HIS A 173     2370   2571   1912   -130    319   -177       C  
ATOM   1183  CG  HIS A 173      -9.269  13.577  30.049  1.00 18.31           C  
ANISOU 1183  CG  HIS A 173     2360   2606   1991   -171    327   -226       C  
ATOM   1184  ND1 HIS A 173     -10.554  13.075  30.010  1.00 24.46           N  
ANISOU 1184  ND1 HIS A 173     3148   3359   2788   -210    362   -220       N  
ATOM   1185  CE1 HIS A 173     -11.417  14.079  29.977  1.00 20.60           C  
ANISOU 1185  CE1 HIS A 173     2609   2880   2337   -236    362   -266       C  
ATOM   1186  NE2 HIS A 173     -10.737  15.215  29.976  1.00 21.94           N  
ANISOU 1186  NE2 HIS A 173     2743   3079   2515   -216    329   -303       N  
ATOM   1187  CD2 HIS A 173      -9.393  14.928  30.018  1.00 22.58           C  
ANISOU 1187  CD2 HIS A 173     2847   3171   2561   -177    306   -279       C  
ATOM   1188  C   HIS A 173      -6.830  14.148  31.748  1.00 23.31           C  
ANISOU 1188  C   HIS A 173     2991   3352   2514    -90    288   -219       C  
ATOM   1189  O   HIS A 173      -7.269  13.541  32.734  1.00 21.99           O  
ANISOU 1189  O   HIS A 173     2847   3205   2305    -93    322   -199       O  
ATOM   1190  N   ASP A 174      -6.409  15.413  31.802  1.00 19.58           N  
ANISOU 1190  N   ASP A 174     2473   2913   2053    -85    257   -265       N  
ATOM   1191  CA  ASP A 174      -6.276  16.085  33.093  1.00 21.16           C  
ANISOU 1191  CA  ASP A 174     2654   3178   2208    -80    259   -291       C  
ATOM   1192  CB  ASP A 174      -5.631  17.462  32.928  1.00 26.13           C  
ANISOU 1192  CB  ASP A 174     3238   3836   2854    -75    220   -340       C  
ATOM   1193  CG  ASP A 174      -5.353  18.134  34.273  1.00 32.00           C  
ANISOU 1193  CG  ASP A 174     3967   4648   3544    -69    219   -366       C  
ATOM   1194  OD1 ASP A 174      -4.549  17.582  35.054  1.00 33.58           O  
ANISOU 1194  OD1 ASP A 174     4190   4889   3681    -42    218   -334       O  
ATOM   1195  OD2 ASP A 174      -5.959  19.192  34.572  1.00 30.70           O  
ANISOU 1195  OD2 ASP A 174     3770   4498   3397    -90    223   -418       O  
ATOM   1196  C   ASP A 174      -7.607  16.229  33.864  1.00 24.97           C  
ANISOU 1196  C   ASP A 174     3129   3670   2690   -111    298   -312       C  
ATOM   1197  O   ASP A 174      -7.613  16.207  35.089  1.00 23.65           O  
ANISOU 1197  O   ASP A 174     2968   3550   2469   -105    316   -312       O  
ATOM   1198  N   ASP A 175      -8.736  16.362  33.175  1.00 20.05           N  
ANISOU 1198  N   ASP A 175     2491   3005   2123   -145    313   -329       N  
ATOM   1199  CA  ASP A 175      -9.996  16.492  33.906  1.00 19.79           C  
ANISOU 1199  CA  ASP A 175     2448   2983   2088   -173    352   -347       C  
ATOM   1200  CB  ASP A 175     -11.142  16.843  32.957  1.00 25.12           C  
ANISOU 1200  CB  ASP A 175     3096   3614   2834   -208    359   -370       C  
ATOM   1201  CG  ASP A 175     -10.856  18.103  32.164  1.00 20.63           C  
ANISOU 1201  CG  ASP A 175     2484   3040   2314   -207    323   -416       C  
ATOM   1202  OD1 ASP A 175     -11.124  19.208  32.684  1.00 27.82           O  
ANISOU 1202  OD1 ASP A 175     3360   3982   3228   -212    324   -461       O  
ATOM   1203  OD2 ASP A 175     -10.326  17.993  31.035  1.00 22.86           O  
ANISOU 1203  OD2 ASP A 175     2768   3286   2630   -201    295   -406       O  
ATOM   1204  C   ASP A 175     -10.311  15.221  34.668  1.00 26.52           C  
ANISOU 1204  C   ASP A 175     3345   3837   2893   -172    390   -299       C  
ATOM   1205  O   ASP A 175     -10.994  15.258  35.697  1.00 26.56           O  
ANISOU 1205  O   ASP A 175     3349   3873   2871   -183    422   -307       O  
ATOM   1206  N   GLN A 176      -9.805  14.098  34.168  1.00 22.00           N  
ANISOU 1206  N   GLN A 176     2815   3233   2311   -158    390   -249       N  
ATOM   1207  CA  GLN A 176     -10.028  12.815  34.819  1.00 22.27           C  
ANISOU 1207  CA  GLN A 176     2898   3263   2299   -156    427   -200       C  
ATOM   1208  CB  GLN A 176      -9.740  11.653  33.866  1.00 22.49           C  
ANISOU 1208  CB  GLN A 176     2972   3235   2340   -151    429   -151       C  
ATOM   1209  CG  GLN A 176     -10.883  11.303  32.954  1.00 26.78           C  
ANISOU 1209  CG  GLN A 176     3517   3720   2938   -194    447   -151       C  
ATOM   1210  CD  GLN A 176     -10.611  10.037  32.187  1.00 25.70           C  
ANISOU 1210  CD  GLN A 176     3435   3528   2801   -190    455   -100       C  
ATOM   1211  OE1 GLN A 176     -10.339   8.990  32.773  1.00 29.73           O  
ANISOU 1211  OE1 GLN A 176     3994   4039   3262   -173    480    -55       O  
ATOM   1212  NE2 GLN A 176     -10.666  10.123  30.872  1.00 22.13           N  
ANISOU 1212  NE2 GLN A 176     2977   3027   2403   -204    434   -107       N  
ATOM   1213  C   GLN A 176      -9.163  12.647  36.042  1.00 26.58           C  
ANISOU 1213  C   GLN A 176     3462   3867   2772   -120    428   -182       C  
ATOM   1214  O   GLN A 176      -9.617  12.109  37.035  1.00 28.85           O  
ANISOU 1214  O   GLN A 176     3771   4176   3017   -123    464   -164       O  
ATOM   1215  N   HIS A 177      -7.910  13.084  35.967  1.00 24.37           N  
ANISOU 1215  N   HIS A 177     3171   3614   2473    -87    390   -185       N  
ATOM   1216  CA  HIS A 177      -6.928  12.644  36.958  1.00 22.02           C  
ANISOU 1216  CA  HIS A 177     2897   3366   2102    -50    389   -153       C  
ATOM   1217  CB  HIS A 177      -5.764  11.951  36.240  1.00 22.28           C  
ANISOU 1217  CB  HIS A 177     2959   3379   2128    -14    366   -109       C  
ATOM   1218  CG  HIS A 177      -6.209  10.864  35.316  1.00 27.53           C  
ANISOU 1218  CG  HIS A 177     3663   3973   2823    -25    387    -70       C  
ATOM   1219  ND1 HIS A 177      -6.981   9.802  35.742  1.00 30.77           N  
ANISOU 1219  ND1 HIS A 177     4116   4362   3213    -38    433    -36       N  
ATOM   1220  CE1 HIS A 177      -7.243   9.013  34.713  1.00 35.50           C  
ANISOU 1220  CE1 HIS A 177     4747   4896   3847    -49    443     -9       C  
ATOM   1221  NE2 HIS A 177      -6.668   9.525  33.638  1.00 32.68           N  
ANISOU 1221  NE2 HIS A 177     4369   4517   3531    -42    405    -25       N  
ATOM   1222  CD2 HIS A 177      -6.019  10.684  33.988  1.00 29.73           C  
ANISOU 1222  CD2 HIS A 177     3949   4197   3151    -27    370    -63       C  
ATOM   1223  C   HIS A 177      -6.376  13.722  37.883  1.00 28.71           C  
ANISOU 1223  C   HIS A 177     3712   4284   2915    -38    367   -191       C  
ATOM   1224  O   HIS A 177      -5.852  13.403  38.943  1.00 29.85           O  
ANISOU 1224  O   HIS A 177     3872   4477   2992    -15    373   -170       O  
ATOM   1225  N   GLY A 178      -6.481  14.984  37.487  1.00 27.53           N  
ANISOU 1225  N   GLY A 178     3516   4138   2807    -54    341   -247       N  
ATOM   1226  CA  GLY A 178      -5.864  16.064  38.239  1.00 29.63           C  
ANISOU 1226  CA  GLY A 178     3751   4465   3041    -46    316   -286       C  
ATOM   1227  C   GLY A 178      -6.429  16.186  39.644  1.00 32.34           C  
ANISOU 1227  C   GLY A 178     4098   4856   3335    -54    347   -299       C  
ATOM   1228  O   GLY A 178      -5.682  16.280  40.621  1.00 31.77           O  
ANISOU 1228  O   GLY A 178     4030   4842   3200    -33    338   -294       O  
ATOM   1229  N   THR A 179      -7.752  16.173  39.742  1.00 26.53           N  
ANISOU 1229  N   THR A 179     3358   4095   2625    -84    384   -313       N  
ATOM   1230  CA  THR A 179      -8.429  16.265  41.030  1.00 32.08           C  
ANISOU 1230  CA  THR A 179     4066   4837   3287    -93    419   -325       C  
ATOM   1231  CB  THR A 179      -9.959  16.304  40.854  1.00 31.30           C  
ANISOU 1231  CB  THR A 179     3957   4702   3234   -129    457   -341       C  
ATOM   1232  OG1 THR A 179     -10.325  17.565  40.289  1.00 31.80           O  
ANISOU 1232  OG1 THR A 179     3976   4756   3352   -148    440   -398       O  
ATOM   1233  CG2 THR A 179     -10.662  16.144  42.194  1.00 33.61           C  
ANISOU 1233  CG2 THR A 179     4260   5031   3478   -136    499   -341       C  
ATOM   1234  C   THR A 179      -8.045  15.103  41.936  1.00 30.97           C  
ANISOU 1234  C   THR A 179     3969   4723   3076    -69    440   -270       C  
ATOM   1235  O   THR A 179      -7.799  15.294  43.131  1.00 32.68           O  
ANISOU 1235  O   THR A 179     4188   4996   3232    -59    446   -276       O  
ATOM   1236  N   ALA A 180      -7.972  13.909  41.359  1.00 28.21           N  
ANISOU 1236  N   ALA A 180     3654   4331   2732    -60    451   -217       N  
ATOM   1237  CA  ALA A 180      -7.621  12.707  42.116  1.00 32.28           C  
ANISOU 1237  CA  ALA A 180     4216   4864   3185    -35    474   -159       C  
ATOM   1238  CB  ALA A 180      -7.756  11.473  41.233  1.00 26.86           C  
ANISOU 1238  CB  ALA A 180     3569   4115   2522    -33    490   -108       C  
ATOM   1239  C   ALA A 180      -6.208  12.782  42.691  1.00 31.63           C  
ANISOU 1239  C   ALA A 180     4137   4841   3041      5    443   -143       C  
ATOM   1240  O   ALA A 180      -5.968  12.432  43.850  1.00 30.07           O  
ANISOU 1240  O   ALA A 180     3958   4692   2777     23    459   -123       O  
ATOM   1241  N   ILE A 181      -5.273  13.229  41.867  1.00 24.37           N  
ANISOU 1241  N   ILE A 181     3198   3916   2144     19    399   -151       N  
ATOM   1242  CA  ILE A 181      -3.879  13.321  42.275  1.00 28.49           C  
ANISOU 1242  CA  ILE A 181     3717   4494   2613     56    365   -135       C  
ATOM   1243  CB  ILE A 181      -2.988  13.689  41.081  1.00 27.05           C  
ANISOU 1243  CB  ILE A 181     3516   4291   2472     68    320   -139       C  
ATOM   1244  CG1 ILE A 181      -2.819  12.460  40.188  1.00 24.92           C  
ANISOU 1244  CG1 ILE A 181     3286   3964   2220     87    332    -81       C  
ATOM   1245  CD1 ILE A 181      -2.319  12.755  38.777  1.00 28.23           C  
ANISOU 1245  CD1 ILE A 181     3688   4339   2698     89    297    -87       C  
ATOM   1246  CG2 ILE A 181      -1.637  14.240  41.548  1.00 26.26           C  
ANISOU 1246  CG2 ILE A 181     3395   4259   2323     96    279   -142       C  
ATOM   1247  C   ILE A 181      -3.701  14.338  43.401  1.00 27.08           C  
ANISOU 1247  C   ILE A 181     3511   4387   2391     51    354   -178       C  
ATOM   1248  O   ILE A 181      -3.046  14.059  44.405  1.00 34.78           O  
ANISOU 1248  O   ILE A 181     4499   5420   3295     75    353   -155       O  
ATOM   1249  N   VAL A 182      -4.283  15.518  43.240  1.00 25.71           N  
ANISOU 1249  N   VAL A 182     3301   4209   2258     19    346   -241       N  
ATOM   1250  CA  VAL A 182      -4.039  16.585  44.198  1.00 25.54           C  
ANISOU 1250  CA  VAL A 182     3254   4250   2198     13    332   -288       C  
ATOM   1251  CB  VAL A 182      -4.387  17.960  43.611  1.00 25.92           C  
ANISOU 1251  CB  VAL A 182     3262   4282   2305    -17    312   -356       C  
ATOM   1252  CG1 VAL A 182      -4.232  19.041  44.668  1.00 26.30           C  
ANISOU 1252  CG1 VAL A 182     3290   4392   2311    -27    304   -405       C  
ATOM   1253  CG2 VAL A 182      -3.488  18.270  42.400  1.00 27.14           C  
ANISOU 1253  CG2 VAL A 182     3396   4413   2501     -7    267   -357       C  
ATOM   1254  C   VAL A 182      -4.824  16.313  45.486  1.00 30.86           C  
ANISOU 1254  C   VAL A 182     3948   4954   2824      5    375   -286       C  
ATOM   1255  O   VAL A 182      -4.308  16.520  46.588  1.00 30.33           O  
ANISOU 1255  O   VAL A 182     3883   4952   2690     16    370   -289       O  
ATOM   1256  N   SER A 183      -6.045  15.805  45.358  1.00 28.05           N  
ANISOU 1256  N   SER A 183     3606   4553   2499    -14    418   -278       N  
ATOM   1257  CA  SER A 183      -6.845  15.497  46.551  1.00 28.97           C  
ANISOU 1257  CA  SER A 183     3741   4694   2572    -22    462   -274       C  
ATOM   1258  CB  SER A 183      -8.319  15.295  46.197  1.00 33.35           C  
ANISOU 1258  CB  SER A 183     4297   5195   3180    -53    504   -281       C  
ATOM   1259  OG  SER A 183      -8.550  14.035  45.599  1.00 33.14           O  
ANISOU 1259  OG  SER A 183     4303   5119   3171    -49    524   -227       O  
ATOM   1260  C   SER A 183      -6.287  14.259  47.253  1.00 31.95           C  
ANISOU 1260  C   SER A 183     4161   5098   2882     10    477   -209       C  
ATOM   1261  O   SER A 183      -6.412  14.117  48.473  1.00 29.87           O  
ANISOU 1261  O   SER A 183     3911   4881   2557     16    499   -203       O  
ATOM   1262  N   GLY A 184      -5.664  13.369  46.485  1.00 31.23           N  
ANISOU 1262  N   GLY A 184     4090   4976   2799     33    466   -159       N  
ATOM   1263  CA  GLY A 184      -4.974  12.220  47.053  1.00 29.19           C  
ANISOU 1263  CA  GLY A 184     3871   4742   2476     70    476    -95       C  
ATOM   1264  C   GLY A 184      -3.867  12.654  48.005  1.00 36.33           C  
ANISOU 1264  C   GLY A 184     4766   5730   3310     96    447    -97       C  
ATOM   1265  O   GLY A 184      -3.742  12.138  49.120  1.00 32.16           O  
ANISOU 1265  O   GLY A 184     4260   5247   2712    114    467    -69       O  
ATOM   1266  N   ALA A 185      -3.071  13.623  47.570  1.00 30.11           N  
ANISOU 1266  N   ALA A 185     3942   4963   2537     96    399   -132       N  
ATOM   1267  CA  ALA A 185      -2.016  14.188  48.410  1.00 26.28           C  
ANISOU 1267  CA  ALA A 185     3440   4559   1987    113    366   -142       C  
ATOM   1268  CB  ALA A 185      -1.171  15.166  47.596  1.00 30.76           C  
ANISOU 1268  CB  ALA A 185     3969   5132   2588    109    312   -177       C  
ATOM   1269  C   ALA A 185      -2.588  14.875  49.661  1.00 34.74           C  
ANISOU 1269  C   ALA A 185     4505   5679   3017     91    383   -185       C  
ATOM   1270  O   ALA A 185      -2.063  14.714  50.766  1.00 34.28           O  
ANISOU 1270  O   ALA A 185     4456   5686   2882    109    383   -168       O  
ATOM   1271  N   ALA A 186      -3.664  15.639  49.497  1.00 33.08           N  
ANISOU 1271  N   ALA A 186     4277   5437   2856     55    400   -238       N  
ATOM   1272  CA  ALA A 186      -4.303  16.287  50.644  1.00 32.27           C  
ANISOU 1272  CA  ALA A 186     4170   5372   2718     35    423   -279       C  
ATOM   1273  CB  ALA A 186      -5.408  17.239  50.182  1.00 30.28           C  
ANISOU 1273  CB  ALA A 186     3893   5077   2533     -3    436   -340       C  
ATOM   1274  C   ALA A 186      -4.867  15.249  51.615  1.00 37.24           C  
ANISOU 1274  C   ALA A 186     4838   6013   3297     46    471   -236       C  
ATOM   1275  O   ALA A 186      -4.783  15.416  52.838  1.00 37.56           O  
ANISOU 1275  O   ALA A 186     4886   6113   3271     50    480   -243       O  
ATOM   1276  N   LEU A 187      -5.445  14.183  51.068  1.00 30.09           N  
ANISOU 1276  N   LEU A 187     3958   5051   2423     50    502   -192       N  
ATOM   1277  CA  LEU A 187      -5.996  13.101  51.884  1.00 36.63           C  
ANISOU 1277  CA  LEU A 187     4825   5882   3208     60    550   -146       C  
ATOM   1278  CB  LEU A 187      -6.751  12.101  51.003  1.00 37.40           C  
ANISOU 1278  CB  LEU A 187     4947   5903   3360     53    581   -109       C  
ATOM   1279  CG  LEU A 187      -7.388  10.891  51.695  1.00 37.65           C  
ANISOU 1279  CG  LEU A 187     5023   5926   3356     60    635    -59       C  
ATOM   1280  CD1 LEU A 187      -8.274  11.337  52.859  1.00 32.16           C  
ANISOU 1280  CD1 LEU A 187     4324   5265   2631     40    669    -90       C  
ATOM   1281  CD2 LEU A 187      -8.197  10.065  50.706  1.00 34.28           C  
ANISOU 1281  CD2 LEU A 187     4615   5418   2990     43    663    -32       C  
ATOM   1282  C   LEU A 187      -4.905  12.386  52.686  1.00 36.50           C  
ANISOU 1282  C   LEU A 187     4834   5925   3109    101    540    -94       C  
ATOM   1283  O   LEU A 187      -5.100  12.048  53.860  1.00 38.54           O  
ANISOU 1283  O   LEU A 187     5114   6225   3305    109    568    -79       O  
ATOM   1284  N   LEU A 188      -3.760  12.159  52.050  1.00 31.21           N  
ANISOU 1284  N   LEU A 188     4161   5260   2438    128    502    -66       N  
ATOM   1285  CA  LEU A 188      -2.596  11.597  52.730  1.00 32.75           C  
ANISOU 1285  CA  LEU A 188     4372   5518   2555    170    486    -18       C  
ATOM   1286  CB  LEU A 188      -1.402  11.516  51.776  1.00 42.86           C  
ANISOU 1286  CB  LEU A 188     5639   6793   3851    196    441      6       C  
ATOM   1287  CG  LEU A 188      -1.136  10.209  51.037  1.00 47.32           C  
ANISOU 1287  CG  LEU A 188     6240   7309   4429    228    456     76       C  
ATOM   1288  CD1 LEU A 188       0.087  10.380  50.148  1.00 47.02           C  
ANISOU 1288  CD1 LEU A 188     6182   7277   4408    251    406     89       C  
ATOM   1289  CD2 LEU A 188      -0.930   9.077  52.031  1.00 43.77           C  
ANISOU 1289  CD2 LEU A 188     5833   6893   3905    263    488    140       C  
ATOM   1290  C   LEU A 188      -2.200  12.414  53.948  1.00 36.56           C  
ANISOU 1290  C   LEU A 188     4837   6085   2970    168    469    -51       C  
ATOM   1291  O   LEU A 188      -1.902  11.869  55.012  1.00 36.77           O  
ANISOU 1291  O   LEU A 188     4885   6163   2921    191    483    -16       O  
ATOM   1292  N   ASN A 189      -2.189  13.730  53.794  1.00 38.77           N  
ANISOU 1292  N   ASN A 189     5079   6377   3275    139    440   -118       N  
ATOM   1293  CA  ASN A 189      -1.747  14.583  54.879  1.00 40.26           C  
ANISOU 1293  CA  ASN A 189     5252   6645   3401    132    420   -154       C  
ATOM   1294  CB  ASN A 189      -1.332  15.952  54.339  1.00 37.77           C  
ANISOU 1294  CB  ASN A 189     4894   6337   3120    107    374   -219       C  
ATOM   1295  CG  ASN A 189       0.046  15.919  53.676  1.00 37.07           C  
ANISOU 1295  CG  ASN A 189     4787   6270   3028    131    322   -194       C  
ATOM   1296  OD1 ASN A 189       0.853  15.020  53.938  1.00 36.20           O  
ANISOU 1296  OD1 ASN A 189     4694   6194   2868    169    316   -132       O  
ATOM   1297  ND2 ASN A 189       0.322  16.902  52.826  1.00 36.30           N  
ANISOU 1297  ND2 ASN A 189     4656   6154   2983    111    286   -240       N  
ATOM   1298  C   ASN A 189      -2.826  14.708  55.957  1.00 40.02           C  
ANISOU 1298  C   ASN A 189     5237   6627   3343    113    466   -178       C  
ATOM   1299  O   ASN A 189      -2.521  14.741  57.149  1.00 41.86           O  
ANISOU 1299  O   ASN A 189     5480   6928   3499    122    468   -174       O  
ATOM   1300  N   ALA A 190      -4.087  14.753  55.537  1.00 33.26           N  
ANISOU 1300  N   ALA A 190     4383   5706   2548     86    502   -199       N  
ATOM   1301  CA  ALA A 190      -5.205  14.813  56.476  1.00 32.34           C  
ANISOU 1301  CA  ALA A 190     4281   5595   2412     68    551   -218       C  
ATOM   1302  CB  ALA A 190      -6.521  14.972  55.721  1.00 28.93           C  
ANISOU 1302  CB  ALA A 190     3842   5088   2064     38    582   -243       C  
ATOM   1303  C   ALA A 190      -5.254  13.576  57.373  1.00 41.08           C  
ANISOU 1303  C   ALA A 190     5429   6725   3455     96    587   -155       C  
ATOM   1304  O   ALA A 190      -5.582  13.666  58.563  1.00 37.58           O  
ANISOU 1304  O   ALA A 190     4999   6326   2955     94    611   -163       O  
ATOM   1305  N   CYS A 191      -4.935  12.422  56.796  1.00 39.74           N  
ANISOU 1305  N   CYS A 191     5282   6523   3294    122    592    -92       N  
ATOM   1306  CA  CYS A 191      -4.907  11.171  57.546  1.00 47.20           C  
ANISOU 1306  CA  CYS A 191     6270   7484   4181    152    626    -26       C  
ATOM   1307  CB  CYS A 191      -4.771   9.975  56.602  1.00 38.57           C  
ANISOU 1307  CB  CYS A 191     5202   6331   3120    173    637     36       C  
ATOM   1308  SG  CYS A 191      -6.299   9.554  55.731  1.00 43.78           S  
ANISOU 1308  SG  CYS A 191     5875   6893   3868    138    684     31       S  
ATOM   1309  C   CYS A 191      -3.768  11.171  58.550  1.00 53.11           C  
ANISOU 1309  C   CYS A 191     7021   8321   4837    183    600     -6       C  
ATOM   1310  O   CYS A 191      -3.930  10.731  59.688  1.00 57.31           O  
ANISOU 1310  O   CYS A 191     7577   8894   5303    196    629     17       O  
ATOM   1311  N   SER A 192      -2.614  11.660  58.112  1.00 49.54           N  
ANISOU 1311  N   SER A 192     6542   7900   4381    195    546    -13       N  
ATOM   1312  CA  SER A 192      -1.440  11.767  58.969  1.00 59.67           C  
ANISOU 1312  CA  SER A 192     7820   9272   5580    221    513      4       C  
ATOM   1313  CB  SER A 192      -0.268  12.352  58.179  1.00 64.80           C  
ANISOU 1313  CB  SER A 192     8435   9940   6246    228    452     -7       C  
ATOM   1314  OG  SER A 192       0.836  12.615  59.024  1.00 72.18           O  
ANISOU 1314  OG  SER A 192     9358  10938   7128    241    412      0       O  
ATOM   1315  C   SER A 192      -1.730  12.623  60.202  1.00 59.67           C  
ANISOU 1315  C   SER A 192     7813   9318   5540    197    515    -46       C  
ATOM   1316  O   SER A 192      -1.349  12.281  61.322  1.00 59.70           O  
ANISOU 1316  O   SER A 192     7834   9355   5492    213    514    -19       O  
ATOM   1317  N   ILE A 193      -2.424  13.730  59.980  1.00 51.05           N  
ANISOU 1317  N   ILE A 193     6698   8217   4482    158    517   -118       N  
ATOM   1318  CA  ILE A 193      -2.729  14.692  61.026  1.00 52.74           C  
ANISOU 1318  CA  ILE A 193     6906   8467   4667    131    517   -172       C  
ATOM   1319  CB  ILE A 193      -3.219  16.007  60.391  1.00 58.12           C  
ANISOU 1319  CB  ILE A 193     7555   9127   5403     91    506   -252       C  
ATOM   1320  CG1 ILE A 193      -2.059  16.670  59.654  1.00 61.07           C  
ANISOU 1320  CG1 ILE A 193     7896   9518   5791     91    444   -270       C  
ATOM   1321  CD1 ILE A 193      -2.452  17.903  58.910  1.00 69.26           C  
ANISOU 1321  CD1 ILE A 193     8902  10516   6897     53    429   -341       C  
ATOM   1322  CG2 ILE A 193      -3.780  16.957  61.422  1.00 61.11           C  
ANISOU 1322  CG2 ILE A 193     7933   9531   5756     63    521   -309       C  
ATOM   1323  C   ILE A 193      -3.760  14.151  62.022  1.00 53.36           C  
ANISOU 1323  C   ILE A 193     7018   8537   4720    130    575   -158       C  
ATOM   1324  O   ILE A 193      -3.725  14.485  63.209  1.00 63.08           O  
ANISOU 1324  O   ILE A 193     8258   9803   5907    125    575   -173       O  
ATOM   1325  N   THR A 194      -4.659  13.292  61.548  1.00 40.78           N  
ANISOU 1325  N   THR A 194     5589   6812   3093     15    154    836       N  
ATOM   1326  CA  THR A 194      -5.704  12.740  62.408  1.00 43.08           C  
ANISOU 1326  CA  THR A 194     5883   7131   3356    -30    190    863       C  
ATOM   1327  CB  THR A 194      -7.090  12.867  61.748  1.00 45.18           C  
ANISOU 1327  CB  THR A 194     6096   7450   3618    -57    217    845       C  
ATOM   1328  OG1 THR A 194      -7.103  12.166  60.496  1.00 43.59           O  
ANISOU 1328  OG1 THR A 194     5884   7253   3427    -67    205    845       O  
ATOM   1329  CG2 THR A 194      -7.419  14.325  61.514  1.00 37.98           C  
ANISOU 1329  CG2 THR A 194     5143   6563   2724    -28    219    799       C  
ATOM   1330  C   THR A 194      -5.462  11.278  62.789  1.00 41.38           C  
ANISOU 1330  C   THR A 194     5710   6891   3121    -62    192    912       C  
ATOM   1331  O   THR A 194      -6.406  10.555  63.117  1.00 39.00           O  
ANISOU 1331  O   THR A 194     5405   6613   2798   -108    221    937       O  
ATOM   1332  N   ASN A 195      -4.197  10.862  62.757  1.00 38.81           N  
ANISOU 1332  N   ASN A 195     5424   6517   2805    -40    161    927       N  
ATOM   1333  CA  ASN A 195      -3.796   9.526  63.204  1.00 42.63           C  
ANISOU 1333  CA  ASN A 195     5955   6970   3274    -66    158    974       C  
ATOM   1334  CB  ASN A 195      -3.911   9.430  64.726  1.00 44.30           C  
ANISOU 1334  CB  ASN A 195     6196   7174   3462    -81    179    999       C  
ATOM   1335  CG  ASN A 195      -3.156   8.251  65.295  1.00 51.12           C  
ANISOU 1335  CG  ASN A 195     7114   7993   4315    -95    168   1044       C  
ATOM   1336  OD1 ASN A 195      -2.048   7.938  64.854  1.00 51.96           O  
ANISOU 1336  OD1 ASN A 195     7246   8059   4438    -71    135   1048       O  
ATOM   1337  ND2 ASN A 195      -3.753   7.586  66.281  1.00 53.29           N  
ANISOU 1337  ND2 ASN A 195     7408   8274   4566   -133    196   1077       N  
ATOM   1338  C   ASN A 195      -4.607   8.416  62.545  1.00 42.88           C  
ANISOU 1338  C   ASN A 195     5974   7020   3300   -112    172    995       C  
ATOM   1339  O   ASN A 195      -5.079   7.491  63.208  1.00 46.05           O  
ANISOU 1339  O   ASN A 195     6396   7409   3694   -153    192   1024       O  
ATOM   1340  N   ARG A 196      -4.777   8.523  61.230  1.00 42.69           N  
ANISOU 1340  N   ARG A 196     5917   6993   3312   -104    159    961       N  
ATOM   1341  CA  ARG A 196      -5.575   7.564  60.479  1.00 42.79           C  
ANISOU 1341  CA  ARG A 196     5913   6986   3359   -144    169    955       C  
ATOM   1342  CB  ARG A 196      -6.623   8.287  59.627  1.00 44.87           C  
ANISOU 1342  CB  ARG A 196     6118   7293   3638   -148    183    914       C  
ATOM   1343  CG  ARG A 196      -7.862   8.787  60.360  1.00 40.33           C  
ANISOU 1343  CG  ARG A 196     5515   6772   3036   -174    223    913       C  
ATOM   1344  CD  ARG A 196      -8.767   9.491  59.360  1.00 36.49           C  
ANISOU 1344  CD  ARG A 196     4972   6324   2571   -172    232    869       C  
ATOM   1345  NE  ARG A 196     -10.145   9.642  59.815  1.00 40.09           N  
ANISOU 1345  NE  ARG A 196     5398   6824   3013   -209    272    867       N  
ATOM   1346  CZ  ARG A 196     -10.680  10.793  60.207  1.00 41.02           C  
ANISOU 1346  CZ  ARG A 196     5486   6996   3103   -196    291    851       C  
ATOM   1347  NH1 ARG A 196      -9.955  11.901  60.205  1.00 40.84           N  
ANISOU 1347  NH1 ARG A 196     5461   6993   3065   -149    273    835       N  
ATOM   1348  NH2 ARG A 196     -11.942  10.837  60.597  1.00 44.31           N  
ANISOU 1348  NH2 ARG A 196     5876   7450   3510   -232    327    851       N  
ATOM   1349  C   ARG A 196      -4.703   6.698  59.574  1.00 45.32           C  
ANISOU 1349  C   ARG A 196     6255   7247   3716   -136    135    957       C  
ATOM   1350  O   ARG A 196      -3.708   7.171  59.032  1.00 47.92           O  
ANISOU 1350  O   ARG A 196     6590   7563   4055    -93    105    943       O  
ATOM   1351  N   LYS A 197      -5.088   5.435  59.409  1.00 45.33           N  
ANISOU 1351  N   LYS A 197     6269   7214   3739   -177    142    974       N  
ATOM   1352  CA  LYS A 197      -4.427   4.541  58.460  1.00 50.10           C  
ANISOU 1352  CA  LYS A 197     6890   7764   4382   -174    113    973       C  
ATOM   1353  CB  LYS A 197      -4.107   3.191  59.099  1.00 57.58           C  
ANISOU 1353  CB  LYS A 197     7885   8663   5328   -205    113   1016       C  
ATOM   1354  CG  LYS A 197      -2.809   3.163  59.894  1.00 65.77           C  
ANISOU 1354  CG  LYS A 197     8972   9674   6343   -176     92   1045       C  
ATOM   1355  CD  LYS A 197      -2.594   1.816  60.577  1.00 71.64           C  
ANISOU 1355  CD  LYS A 197     9763  10373   7085   -210     95   1087       C  
ATOM   1356  CE  LYS A 197      -3.900   1.053  60.773  1.00 74.57           C  
ANISOU 1356  CE  LYS A 197    10119  10752   7460   -266    129   1096       C  
ATOM   1357  NZ  LYS A 197      -3.665  -0.377  61.121  1.00 77.41           N  
ANISOU 1357  NZ  LYS A 197    10522  11061   7829   -299    127   1133       N  
ATOM   1358  C   LYS A 197      -5.330   4.351  57.251  1.00 41.34           C  
ANISOU 1358  C   LYS A 197     5738   6659   3310   -193    118    941       C  
ATOM   1359  O   LYS A 197      -6.527   4.126  57.403  1.00 46.60           O  
ANISOU 1359  O   LYS A 197     6381   7349   3976   -233    149    940       O  
ATOM   1360  N   MET A 198      -4.761   4.441  56.053  1.00 47.32           N  
ANISOU 1360  N   MET A 198     6485   7394   4099   -166     89    916       N  
ATOM   1361  CA  MET A 198      -5.569   4.453  54.833  1.00 46.02           C  
ANISOU 1361  CA  MET A 198     6278   7240   3970   -177     92    881       C  
ATOM   1362  CB  MET A 198      -4.679   4.639  53.600  1.00 41.66           C  
ANISOU 1362  CB  MET A 198     5721   6661   3449   -137     55    855       C  
ATOM   1363  CG  MET A 198      -4.208   6.077  53.375  1.00 45.96           C  
ANISOU 1363  CG  MET A 198     6244   7240   3980    -86     43    827       C  
ATOM   1364  SD  MET A 198      -5.551   7.263  53.102  1.00 57.00           S  
ANISOU 1364  SD  MET A 198     7577   8708   5371    -91     71    788       S  
ATOM   1365  CE  MET A 198      -5.847   7.080  51.345  1.00 47.31           C  
ANISOU 1365  CE  MET A 198     6314   7466   4195    -88     55    748       C  
ATOM   1366  C   MET A 198      -6.427   3.199  54.665  1.00 44.67           C  
ANISOU 1366  C   MET A 198     6107   7045   3820   -231    108    894       C  
ATOM   1367  O   MET A 198      -7.552   3.278  54.171  1.00 48.22           O  
ANISOU 1367  O   MET A 198     6517   7521   4285   -256    128    872       O  
ATOM   1368  N   GLU A 199      -5.924   2.047  55.090  1.00 41.58           N  
ANISOU 1368  N   GLU A 199     5761   6606   3432   -250    101    929       N  
ATOM   1369  CA  GLU A 199      -6.661   0.806  54.867  1.00 47.20           C  
ANISOU 1369  CA  GLU A 199     6475   7292   4167   -299    114    941       C  
ATOM   1370  CB  GLU A 199      -5.763  -0.407  55.122  1.00 50.83           C  
ANISOU 1370  CB  GLU A 199     6988   7690   4634   -307     95    976       C  
ATOM   1371  CG  GLU A 199      -5.336  -0.575  56.562  1.00 61.16           C  
ANISOU 1371  CG  GLU A 199     8338   8996   5904   -312    105   1017       C  
ATOM   1372  CD  GLU A 199      -3.904  -0.145  56.789  1.00 69.57           C  
ANISOU 1372  CD  GLU A 199     9435  10042   6956   -264     75   1025       C  
ATOM   1373  OE1 GLU A 199      -3.412   0.707  56.015  1.00 67.20           O  
ANISOU 1373  OE1 GLU A 199     9115   9752   6665   -222     54    995       O  
ATOM   1374  OE2 GLU A 199      -3.274  -0.660  57.740  1.00 72.06           O  
ANISOU 1374  OE2 GLU A 199     9795  10333   7250   -267     72   1062       O  
ATOM   1375  C   GLU A 199      -7.937   0.685  55.711  1.00 47.11           C  
ANISOU 1375  C   GLU A 199     6449   7315   4136   -345    155    954       C  
ATOM   1376  O   GLU A 199      -8.697  -0.263  55.535  1.00 50.09           O  
ANISOU 1376  O   GLU A 199     6823   7677   4533   -389    169    962       O  
ATOM   1377  N   THR A 200      -8.184   1.635  56.613  1.00 46.36           N  
ANISOU 1377  N   THR A 200     6344   7267   4003   -335    174    956       N  
ATOM   1378  CA  THR A 200      -9.407   1.595  57.421  1.00 47.27           C  
ANISOU 1378  CA  THR A 200     6443   7419   4099   -376    214    968       C  
ATOM   1379  CB  THR A 200      -9.092   1.448  58.927  1.00 54.32           C  
ANISOU 1379  CB  THR A 200     7376   8314   4951   -384    228   1008       C  
ATOM   1380  OG1 THR A 200      -8.313   2.566  59.373  1.00 54.34           O  
ANISOU 1380  OG1 THR A 200     7385   8339   4924   -337    217   1003       O  
ATOM   1381  CG2 THR A 200      -8.325   0.161  59.190  1.00 55.76           C  
ANISOU 1381  CG2 THR A 200     7610   8435   5141   -398    212   1044       C  
ATOM   1382  C   THR A 200     -10.288   2.831  57.229  1.00 43.67           C  
ANISOU 1382  C   THR A 200     5934   7025   3632   -367    234    934       C  
ATOM   1383  O   THR A 200     -11.381   2.911  57.786  1.00 42.06           O  
ANISOU 1383  O   THR A 200     5710   6856   3414   -400    268    938       O  
ATOM   1384  N   VAL A 201      -9.812   3.787  56.435  1.00 43.07           N  
ANISOU 1384  N   VAL A 201     5836   6962   3565   -324    212    900       N  
ATOM   1385  CA  VAL A 201     -10.559   5.014  56.165  1.00 36.70           C  
ANISOU 1385  CA  VAL A 201     4980   6214   2751   -310    227    865       C  
ATOM   1386  CB  VAL A 201      -9.673   6.055  55.472  1.00 42.48           C  
ANISOU 1386  CB  VAL A 201     5701   6952   3487   -254    198    835       C  
ATOM   1387  CG1 VAL A 201     -10.458   7.312  55.169  1.00 42.48           C  
ANISOU 1387  CG1 VAL A 201     5649   7012   3480   -241    213    799       C  
ATOM   1388  CG2 VAL A 201      -8.481   6.375  56.340  1.00 41.96           C  
ANISOU 1388  CG2 VAL A 201     5676   6877   3391   -220    182    859       C  
ATOM   1389  C   VAL A 201     -11.784   4.746  55.297  1.00 40.28           C  
ANISOU 1389  C   VAL A 201     5390   6680   3235   -344    243    841       C  
ATOM   1390  O   VAL A 201     -11.682   4.088  54.265  1.00 34.92           O  
ANISOU 1390  O   VAL A 201     4708   5966   2593   -349    225    829       O  
ATOM   1391  N   ARG A 202     -12.937   5.256  55.720  1.00 34.28           N  
ANISOU 1391  N   ARG A 202     4597   5970   2459   -365    277    833       N  
ATOM   1392  CA  ARG A 202     -14.170   5.067  54.964  1.00 36.97           C  
ANISOU 1392  CA  ARG A 202     4894   6327   2826   -398    295    811       C  
ATOM   1393  CB  ARG A 202     -15.338   4.746  55.902  1.00 44.35           C  
ANISOU 1393  CB  ARG A 202     5821   7289   3742   -446    335    831       C  
ATOM   1394  CG  ARG A 202     -15.450   3.252  56.206  1.00 52.99           C  
ANISOU 1394  CG  ARG A 202     6948   8337   4848   -490    341    867       C  
ATOM   1395  CD  ARG A 202     -16.357   2.925  57.392  1.00 64.30           C  
ANISOU 1395  CD  ARG A 202     8385   9793   6255   -532    379    896       C  
ATOM   1396  NE  ARG A 202     -17.316   3.983  57.723  1.00 74.18           N  
ANISOU 1396  NE  ARG A 202     9595  11107   7484   -534    409    878       N  
ATOM   1397  CZ  ARG A 202     -18.483   4.165  57.104  1.00 74.93           C  
ANISOU 1397  CZ  ARG A 202     9642  11231   7598   -556    427    852       C  
ATOM   1398  NH1 ARG A 202     -18.834   3.389  56.084  1.00 74.86           N  
ANISOU 1398  NH1 ARG A 202     9619  11193   7630   -578    418    840       N  
ATOM   1399  NH2 ARG A 202     -19.291   5.146  57.486  1.00 72.90           N  
ANISOU 1399  NH2 ARG A 202     9349  11031   7318   -555    453    838       N  
ATOM   1400  C   ARG A 202     -14.468   6.296  54.122  1.00 31.83           C  
ANISOU 1400  C   ARG A 202     4195   5717   2182   -368    291    765       C  
ATOM   1401  O   ARG A 202     -14.628   7.398  54.641  1.00 38.61           O  
ANISOU 1401  O   ARG A 202     5036   6622   3011   -348    304    755       O  
ATOM   1402  N   ILE A 203     -14.529   6.097  52.811  1.00 34.60           N  
ANISOU 1402  N   ILE A 203     4524   6050   2573   -364    273    737       N  
ATOM   1403  CA  ILE A 203     -14.609   7.205  51.871  1.00 30.38           C  
ANISOU 1403  CA  ILE A 203     3948   5546   2049   -330    262    693       C  
ATOM   1404  CB  ILE A 203     -13.429   7.159  50.879  1.00 32.29           C  
ANISOU 1404  CB  ILE A 203     4205   5748   2317   -290    221    678       C  
ATOM   1405  CG1 ILE A 203     -12.104   7.170  51.642  1.00 34.31           C  
ANISOU 1405  CG1 ILE A 203     4509   5980   2549   -260    202    706       C  
ATOM   1406  CD1 ILE A 203     -10.892   7.040  50.744  1.00 30.66           C  
ANISOU 1406  CD1 ILE A 203     4065   5474   2110   -222    161    696       C  
ATOM   1407  CG2 ILE A 203     -13.487   8.320  49.905  1.00 29.17           C  
ANISOU 1407  CG2 ILE A 203     3766   5384   1933   -254    210    633       C  
ATOM   1408  C   ILE A 203     -15.928   7.186  51.113  1.00 34.92           C  
ANISOU 1408  C   ILE A 203     4474   6145   2649   -360    281    666       C  
ATOM   1409  O   ILE A 203     -16.390   6.134  50.670  1.00 34.61           O  
ANISOU 1409  O   ILE A 203     4436   6077   2638   -396    284    672       O  
ATOM   1410  N   VAL A 204     -16.542   8.353  50.978  1.00 32.03           N  
ANISOU 1410  N   VAL A 204     4064   5833   2271   -345    295    636       N  
ATOM   1411  CA  VAL A 204     -17.763   8.465  50.197  1.00 36.03           C  
ANISOU 1411  CA  VAL A 204     4522   6366   2803   -369    311    607       C  
ATOM   1412  CB  VAL A 204     -18.965   8.845  51.065  1.00 33.35           C  
ANISOU 1412  CB  VAL A 204     4157   6077   2436   -400    352    613       C  
ATOM   1413  CG1 VAL A 204     -20.165   9.159  50.180  1.00 39.27           C  
ANISOU 1413  CG1 VAL A 204     4852   6858   3210   -417    367    577       C  
ATOM   1414  CG2 VAL A 204     -19.282   7.721  52.050  1.00 37.70           C  
ANISOU 1414  CG2 VAL A 204     4740   6607   2977   -445    373    656       C  
ATOM   1415  C   VAL A 204     -17.584   9.505  49.103  1.00 34.80           C  
ANISOU 1415  C   VAL A 204     4330   6230   2661   -328    292    562       C  
ATOM   1416  O   VAL A 204     -17.326  10.681  49.384  1.00 33.97           O  
ANISOU 1416  O   VAL A 204     4214   6162   2532   -293    292    548       O  
ATOM   1417  N   VAL A 205     -17.702   9.062  47.857  1.00 37.62           N  
ANISOU 1417  N   VAL A 205     4672   6562   3059   -332    276    539       N  
ATOM   1418  CA  VAL A 205     -17.566   9.946  46.713  1.00 35.69           C  
ANISOU 1418  CA  VAL A 205     4394   6333   2834   -296    257    496       C  
ATOM   1419  CB  VAL A 205     -16.708   9.297  45.605  1.00 34.31           C  
ANISOU 1419  CB  VAL A 205     4236   6104   2696   -279    220    488       C  
ATOM   1420  CG1 VAL A 205     -16.518  10.260  44.441  1.00 36.31           C  
ANISOU 1420  CG1 VAL A 205     4456   6374   2967   -239    201    443       C  
ATOM   1421  CG2 VAL A 205     -15.363   8.861  46.175  1.00 32.40           C  
ANISOU 1421  CG2 VAL A 205     4049   5820   2440   -258    198    519       C  
ATOM   1422  C   VAL A 205     -18.946  10.308  46.167  1.00 38.09           C  
ANISOU 1422  C   VAL A 205     4644   6678   3152   -320    280    466       C  
ATOM   1423  O   VAL A 205     -19.768   9.430  45.900  1.00 37.70           O  
ANISOU 1423  O   VAL A 205     4585   6615   3124   -363    292    471       O  
ATOM   1424  N   ASN A 206     -19.208  11.604  46.033  1.00 39.81           N  
ANISOU 1424  N   ASN A 206     4826   6946   3356   -292    286    437       N  
ATOM   1425  CA  ASN A 206     -20.500  12.066  45.538  1.00 42.25           C  
ANISOU 1425  CA  ASN A 206     5081   7296   3675   -312    308    407       C  
ATOM   1426  CB  ASN A 206     -21.159  13.029  46.530  1.00 43.81           C  
ANISOU 1426  CB  ASN A 206     5258   7553   3835   -313    339    408       C  
ATOM   1427  CG  ASN A 206     -22.643  13.235  46.249  1.00 48.53           C  
ANISOU 1427  CG  ASN A 206     5805   8191   4442   -346    368    387       C  
ATOM   1428  OD1 ASN A 206     -23.362  12.290  45.927  1.00 48.61           O  
ANISOU 1428  OD1 ASN A 206     5809   8183   4477   -387    378    393       O  
ATOM   1429  ND2 ASN A 206     -23.102  14.476  46.364  1.00 43.51           N  
ANISOU 1429  ND2 ASN A 206     5134   7610   3786   -327    382    364       N  
ATOM   1430  C   ASN A 206     -20.349  12.735  44.186  1.00 39.32           C  
ANISOU 1430  C   ASN A 206     4678   6930   3332   -278    285    363       C  
ATOM   1431  O   ASN A 206     -19.751  13.804  44.074  1.00 40.03           O  
ANISOU 1431  O   ASN A 206     4761   7042   3408   -233    272    344       O  
ATOM   1432  N   GLY A 207     -20.902  12.094  43.162  1.00 39.15           N  
ANISOU 1432  N   GLY A 207     4637   6889   3349   -301    280    346       N  
ATOM   1433  CA  GLY A 207     -20.767  12.550  41.795  1.00 39.37           C  
ANISOU 1433  CA  GLY A 207     4638   6916   3407   -273    257    305       C  
ATOM   1434  C   GLY A 207     -20.158  11.438  40.967  1.00 41.56           C  
ANISOU 1434  C   GLY A 207     4941   7130   3720   -277    229    310       C  
ATOM   1435  O   GLY A 207     -19.326  10.676  41.458  1.00 44.34           O  
ANISOU 1435  O   GLY A 207     5339   7442   4067   -278    217    342       O  
ATOM   1436  N   ALA A 208     -20.584  11.325  39.716  1.00 45.64           N  
ANISOU 1436  N   ALA A 208     5428   7640   4272   -280    219    279       N  
ATOM   1437  CA  ALA A 208     -20.065  10.288  38.834  1.00 48.15           C  
ANISOU 1437  CA  ALA A 208     5768   7900   4627   -284    192    281       C  
ATOM   1438  CB  ALA A 208     -21.141   9.257  38.530  1.00 45.33           C  
ANISOU 1438  CB  ALA A 208     5398   7529   4295   -337    208    285       C  
ATOM   1439  C   ALA A 208     -19.533  10.904  37.549  1.00 52.05           C  
ANISOU 1439  C   ALA A 208     6244   8388   5144   -241    163    242       C  
ATOM   1440  O   ALA A 208     -19.649  10.319  36.474  1.00 63.74           O  
ANISOU 1440  O   ALA A 208     7717   9840   6661   -248    148    226       O  
ATOM   1441  N   GLY A 209     -18.949  12.090  37.665  1.00 45.42           N  
ANISOU 1441  N   GLY A 209     5397   7577   4283   -196    155    227       N  
ATOM   1442  CA  GLY A 209     -18.400  12.784  36.516  1.00 45.11           C  
ANISOU 1442  CA  GLY A 209     5341   7537   4263   -151    128    191       C  
ATOM   1443  C   GLY A 209     -17.054  12.232  36.086  1.00 44.82           C  
ANISOU 1443  C   GLY A 209     5344   7444   4241   -124     93    201       C  
ATOM   1444  O   GLY A 209     -16.661  11.136  36.494  1.00 41.50           O  
ANISOU 1444  O   GLY A 209     4965   6981   3824   -144     88    234       O  
ATOM   1445  N   ALA A 210     -16.341  13.006  35.274  1.00 42.19           N  
ANISOU 1445  N   ALA A 210     5002   7112   3917    -76     68    173       N  
ATOM   1446  CA  ALA A 210     -15.074  12.565  34.697  1.00 31.20           C  
ANISOU 1446  CA  ALA A 210     3644   5668   2542    -46     33    178       C  
ATOM   1447  CB  ALA A 210     -14.555  13.612  33.698  1.00 31.26           C  
ANISOU 1447  CB  ALA A 210     3628   5689   2560      5     10    139       C  
ATOM   1448  C   ALA A 210     -13.989  12.256  35.728  1.00 33.25           C  
ANISOU 1448  C   ALA A 210     3954   5903   2777    -34     25    217       C  
ATOM   1449  O   ALA A 210     -13.091  11.466  35.456  1.00 32.42           O  
ANISOU 1449  O   ALA A 210     3885   5746   2687    -26      1    233       O  
ATOM   1450  N   SER A 211     -14.055  12.862  36.909  1.00 31.53           N  
ANISOU 1450  N   SER A 211     3740   5720   2521    -33     44    234       N  
ATOM   1451  CA  SER A 211     -12.954  12.698  37.858  1.00 31.03           C  
ANISOU 1451  CA  SER A 211     3723   5634   2432    -16     34    268       C  
ATOM   1452  CB  SER A 211     -12.547  14.058  38.430  1.00 37.76           C  
ANISOU 1452  CB  SER A 211     4567   6530   3251     24     36    260       C  
ATOM   1453  OG  SER A 211     -13.652  14.711  39.025  1.00 45.30           O  
ANISOU 1453  OG  SER A 211     5488   7539   4183      4     68    253       O  
ATOM   1454  C   SER A 211     -13.255  11.729  38.994  1.00 32.92           C  
ANISOU 1454  C   SER A 211     3994   5860   2656    -60     55    311       C  
ATOM   1455  O   SER A 211     -12.375  11.435  39.809  1.00 34.88           O  
ANISOU 1455  O   SER A 211     4283   6085   2884    -51     47    343       O  
ATOM   1456  N   ALA A 212     -14.484  11.216  39.032  1.00 31.71           N  
ANISOU 1456  N   ALA A 212     3820   5719   2511   -107     80    311       N  
ATOM   1457  CA  ALA A 212     -14.948  10.384  40.140  1.00 31.55           C  
ANISOU 1457  CA  ALA A 212     3822   5693   2474   -152    104    349       C  
ATOM   1458  CB  ALA A 212     -16.437  10.077  39.968  1.00 39.88           C  
ANISOU 1458  CB  ALA A 212     4841   6771   3541   -199    133    339       C  
ATOM   1459  C   ALA A 212     -14.159   9.081  40.306  1.00 32.34           C  
ANISOU 1459  C   ALA A 212     3974   5731   2585   -164     87    383       C  
ATOM   1460  O   ALA A 212     -13.545   8.851  41.345  1.00 33.22           O  
ANISOU 1460  O   ALA A 212     4122   5830   2670   -163     89    417       O  
ATOM   1461  N   ASN A 213     -14.194   8.228  39.289  1.00 35.02           N  
ANISOU 1461  N   ASN A 213     4314   6030   2962   -177     72    375       N  
ATOM   1462  CA  ASN A 213     -13.501   6.943  39.324  1.00 38.61           C  
ANISOU 1462  CA  ASN A 213     4814   6424   3431   -190     55    405       C  
ATOM   1463  CB  ASN A 213     -13.704   6.197  38.005  1.00 41.85           C  
ANISOU 1463  CB  ASN A 213     5216   6800   3887   -201     38    385       C  
ATOM   1464  CG  ASN A 213     -14.985   5.407  37.979  1.00 49.87           C  
ANISOU 1464  CG  ASN A 213     6213   7817   4916   -257     62    389       C  
ATOM   1465  OD1 ASN A 213     -15.854   5.578  38.837  1.00 48.90           O  
ANISOU 1465  OD1 ASN A 213     6077   7731   4772   -286     94    400       O  
ATOM   1466  ND2 ASN A 213     -15.114   4.532  36.993  1.00 53.20           N  
ANISOU 1466  ND2 ASN A 213     6637   8201   5376   -272     48    380       N  
ATOM   1467  C   ASN A 213     -12.010   7.054  39.589  1.00 34.87           C  
ANISOU 1467  C   ASN A 213     4381   5921   2945   -148     28    421       C  
ATOM   1468  O   ASN A 213     -11.420   6.209  40.262  1.00 32.71           O  
ANISOU 1468  O   ASN A 213     4153   5612   2664   -159     23    457       O  
ATOM   1469  N   SER A 214     -11.388   8.083  39.031  1.00 28.34           N  
ANISOU 1469  N   SER A 214     3540   5110   2118    -99      9    394       N  
ATOM   1470  CA  SER A 214      -9.959   8.257  39.223  1.00 30.29           C  
ANISOU 1470  CA  SER A 214     3823   5330   2355    -57    -18    407       C  
ATOM   1471  CB  SER A 214      -9.436   9.377  38.339  1.00 36.72           C  
ANISOU 1471  CB  SER A 214     4614   6162   3177     -5    -39    370       C  
ATOM   1472  OG  SER A 214      -8.037   9.467  38.458  1.00 36.61           O  
ANISOU 1472  OG  SER A 214     4635   6119   3157     35    -66    383       O  
ATOM   1473  C   SER A 214      -9.628   8.537  40.688  1.00 32.00           C  
ANISOU 1473  C   SER A 214     4066   5564   2529    -55     -4    439       C  
ATOM   1474  O   SER A 214      -8.589   8.104  41.189  1.00 31.48           O  
ANISOU 1474  O   SER A 214     4045   5464   2455    -42    -20    468       O  
ATOM   1475  N   CYS A 215     -10.517   9.241  41.384  1.00 27.97           N  
ANISOU 1475  N   CYS A 215     3529   5107   1993    -70     26    435       N  
ATOM   1476  CA  CYS A 215     -10.300   9.480  42.809  1.00 27.39           C  
ANISOU 1476  CA  CYS A 215     3479   5050   1878    -71     41    467       C  
ATOM   1477  CB  CYS A 215     -11.389  10.380  43.408  1.00 28.35           C  
ANISOU 1477  CB  CYS A 215     3563   5235   1973    -85     74    455       C  
ATOM   1478  SG  CYS A 215     -11.283  12.122  42.933  1.00 32.11           S  
ANISOU 1478  SG  CYS A 215     3998   5764   2440    -34     68    413       S  
ATOM   1479  C   CYS A 215     -10.257   8.148  43.544  1.00 34.30           C  
ANISOU 1479  C   CYS A 215     4395   5886   2750   -111     48    509       C  
ATOM   1480  O   CYS A 215      -9.369   7.906  44.361  1.00 35.67           O  
ANISOU 1480  O   CYS A 215     4611   6038   2904   -100     40    540       O  
ATOM   1481  N   ALA A 216     -11.207   7.273  43.234  1.00 32.99           N  
ANISOU 1481  N   ALA A 216     4219   5710   2607   -156     63    510       N  
ATOM   1482  CA  ALA A 216     -11.269   5.986  43.916  1.00 28.01           C  
ANISOU 1482  CA  ALA A 216     3624   5042   1974   -197     72    550       C  
ATOM   1483  CB  ALA A 216     -12.528   5.241  43.524  1.00 32.45           C  
ANISOU 1483  CB  ALA A 216     4164   5606   2561   -247     92    544       C  
ATOM   1484  C   ALA A 216     -10.031   5.141  43.619  1.00 34.31           C  
ANISOU 1484  C   ALA A 216     4468   5779   2789   -181     39    568       C  
ATOM   1485  O   ALA A 216      -9.487   4.480  44.506  1.00 31.65           O  
ANISOU 1485  O   ALA A 216     4174   5415   2436   -191     39    605       O  
ATOM   1486  N   LYS A 217      -9.578   5.179  42.369  1.00 32.19           N  
ANISOU 1486  N   LYS A 217     4190   5488   2552   -155     12    541       N  
ATOM   1487  CA  LYS A 217      -8.429   4.386  41.960  1.00 32.65           C  
ANISOU 1487  CA  LYS A 217     4289   5487   2630   -138    -19    555       C  
ATOM   1488  CB  LYS A 217      -8.269   4.428  40.436  1.00 39.78           C  
ANISOU 1488  CB  LYS A 217     5171   6373   3572   -117    -44    519       C  
ATOM   1489  CG  LYS A 217      -8.766   3.164  39.746  1.00 54.20           C  
ANISOU 1489  CG  LYS A 217     7001   8159   5433   -155    -46    522       C  
ATOM   1490  CD  LYS A 217      -9.187   3.416  38.300  1.00 64.48           C  
ANISOU 1490  CD  LYS A 217     8265   9465   6770   -146    -57    479       C  
ATOM   1491  CE  LYS A 217      -8.140   4.203  37.527  1.00 73.44           C  
ANISOU 1491  CE  LYS A 217     9397  10593   7912    -88    -87    456       C  
ATOM   1492  NZ  LYS A 217      -8.763   5.178  36.580  1.00 77.10           N  
ANISOU 1492  NZ  LYS A 217     9810  11097   8390    -72    -85    410       N  
ATOM   1493  C   LYS A 217      -7.154   4.861  42.647  1.00 34.50           C  
ANISOU 1493  C   LYS A 217     4556   5714   2837    -97    -36    573       C  
ATOM   1494  O   LYS A 217      -6.358   4.043  43.108  1.00 30.75           O  
ANISOU 1494  O   LYS A 217     4128   5197   2360   -100    -48    606       O  
ATOM   1495  N   ILE A 218      -6.975   6.178  42.733  1.00 32.88           N  
ANISOU 1495  N   ILE A 218     4329   5551   2613    -61    -37    553       N  
ATOM   1496  CA  ILE A 218      -5.810   6.748  43.411  1.00 33.05           C  
ANISOU 1496  CA  ILE A 218     4378   5570   2607    -21    -52    568       C  
ATOM   1497  CB  ILE A 218      -5.693   8.272  43.175  1.00 32.32           C  
ANISOU 1497  CB  ILE A 218     4253   5525   2502     23    -55    536       C  
ATOM   1498  CG1 ILE A 218      -5.241   8.559  41.748  1.00 41.15           C  
ANISOU 1498  CG1 ILE A 218     5353   6629   3654     57    -83    501       C  
ATOM   1499  CD1 ILE A 218      -3.775   8.227  41.490  1.00 38.31           C  
ANISOU 1499  CD1 ILE A 218     5033   6219   3304     92   -118    514       C  
ATOM   1500  CG2 ILE A 218      -4.690   8.899  44.143  1.00 35.63           C  
ANISOU 1500  CG2 ILE A 218     4700   5951   2886     56    -63    556       C  
ATOM   1501  C   ILE A 218      -5.863   6.468  44.919  1.00 33.23           C  
ANISOU 1501  C   ILE A 218     4432   5600   2594    -44    -31    608       C  
ATOM   1502  O   ILE A 218      -4.854   6.108  45.522  1.00 33.75           O  
ANISOU 1502  O   ILE A 218     4540   5635   2647    -31    -45    637       O  
ATOM   1503  N   PHE A 219      -7.034   6.624  45.528  1.00 28.88           N  
ANISOU 1503  N   PHE A 219     3858   5090   2027    -79      3    610       N  
ATOM   1504  CA  PHE A 219      -7.156   6.373  46.964  1.00 32.45           C  
ANISOU 1504  CA  PHE A 219     4337   5550   2443   -102     25    647       C  
ATOM   1505  CB  PHE A 219      -8.568   6.704  47.466  1.00 30.49           C  
ANISOU 1505  CB  PHE A 219     4054   5353   2180   -137     63    642       C  
ATOM   1506  CG  PHE A 219      -8.942   8.162  47.341  1.00 30.97           C  
ANISOU 1506  CG  PHE A 219     4072   5471   2225   -110     72    609       C  
ATOM   1507  CD1 PHE A 219      -7.983   9.128  47.076  1.00 35.96           C  
ANISOU 1507  CD1 PHE A 219     4704   6110   2850    -57     48    593       C  
ATOM   1508  CE1 PHE A 219      -8.336  10.465  46.949  1.00 36.90           C  
ANISOU 1508  CE1 PHE A 219     4783   6281   2955    -32     56    562       C  
ATOM   1509  CZ  PHE A 219      -9.658  10.846  47.086  1.00 42.98           C  
ANISOU 1509  CZ  PHE A 219     5514   7098   3718    -60     87    548       C  
ATOM   1510  CE2 PHE A 219     -10.623   9.895  47.345  1.00 44.78           C  
ANISOU 1510  CE2 PHE A 219     5741   7320   3953   -112    111    564       C  
ATOM   1511  CD2 PHE A 219     -10.265   8.560  47.473  1.00 38.28           C  
ANISOU 1511  CD2 PHE A 219     4958   6444   3144   -137    103    594       C  
ATOM   1512  C   PHE A 219      -6.796   4.909  47.273  1.00 31.80           C  
ANISOU 1512  C   PHE A 219     4300   5411   2371   -131     19    684       C  
ATOM   1513  O   PHE A 219      -6.069   4.632  48.219  1.00 32.31           O  
ANISOU 1513  O   PHE A 219     4405   5458   2413   -127     15    718       O  
ATOM   1514  N   ILE A 220      -7.278   3.983  46.451  1.00 33.30           N  
ANISOU 1514  N   ILE A 220     4483   5573   2596   -160     17    678       N  
ATOM   1515  CA  ILE A 220      -6.915   2.576  46.604  1.00 35.04           C  
ANISOU 1515  CA  ILE A 220     4746   5738   2830   -186      9    711       C  
ATOM   1516  CB  ILE A 220      -7.683   1.682  45.612  1.00 40.64           C  
ANISOU 1516  CB  ILE A 220     5438   6425   3578   -221     10    697       C  
ATOM   1517  CG1 ILE A 220      -9.154   1.582  46.022  1.00 37.42           C  
ANISOU 1517  CG1 ILE A 220     5001   6054   3164   -268     47    697       C  
ATOM   1518  CD1 ILE A 220      -9.997   0.759  45.080  1.00 41.07           C  
ANISOU 1518  CD1 ILE A 220     5444   6498   3664   -304     51    684       C  
ATOM   1519  CG2 ILE A 220      -7.068   0.288  45.555  1.00 41.02           C  
ANISOU 1519  CG2 ILE A 220     5532   6410   3645   -238     -7    726       C  
ATOM   1520  C   ILE A 220      -5.407   2.382  46.414  1.00 37.28           C  
ANISOU 1520  C   ILE A 220     5069   5977   3119   -147    -27    722       C  
ATOM   1521  O   ILE A 220      -4.761   1.662  47.173  1.00 36.40           O  
ANISOU 1521  O   ILE A 220     5003   5833   2996   -154    -32    758       O  
ATOM   1522  N   ALA A 221      -4.845   3.048  45.412  1.00 35.17           N  
ANISOU 1522  N   ALA A 221     4785   5709   2869   -105    -52    691       N  
ATOM   1523  CA  ALA A 221      -3.402   3.022  45.197  1.00 37.24           C  
ANISOU 1523  CA  ALA A 221     5081   5933   3136    -63    -86    698       C  
ATOM   1524  CB  ALA A 221      -3.043   3.806  43.936  1.00 40.81           C  
ANISOU 1524  CB  ALA A 221     5503   6391   3610    -21   -109    657       C  
ATOM   1525  C   ALA A 221      -2.633   3.571  46.399  1.00 40.27           C  
ANISOU 1525  C   ALA A 221     5492   6329   3479    -40    -86    723       C  
ATOM   1526  O   ALA A 221      -1.475   3.208  46.622  1.00 40.14           O  
ANISOU 1526  O   ALA A 221     5516   6274   3461    -19   -109    744       O  
ATOM   1527  N   LEU A 222      -3.278   4.444  47.171  1.00 39.45           N  
ANISOU 1527  N   LEU A 222     5366   6278   3344    -44    -61    719       N  
ATOM   1528  CA  LEU A 222      -2.675   4.987  48.386  1.00 40.98           C  
ANISOU 1528  CA  LEU A 222     5584   6487   3498    -26    -58    743       C  
ATOM   1529  CB  LEU A 222      -3.207   6.394  48.663  1.00 39.66           C  
ANISOU 1529  CB  LEU A 222     5379   6383   3306     -8    -41    719       C  
ATOM   1530  CG  LEU A 222      -2.788   7.459  47.644  1.00 45.01           C  
ANISOU 1530  CG  LEU A 222     6027   7078   3998     39    -62    680       C  
ATOM   1531  CD1 LEU A 222      -3.326   8.837  48.016  1.00 46.73           C  
ANISOU 1531  CD1 LEU A 222     6209   7359   4189     55    -44    659       C  
ATOM   1532  CD2 LEU A 222      -1.272   7.503  47.490  1.00 49.43           C  
ANISOU 1532  CD2 LEU A 222     6620   7600   4561     84    -98    688       C  
ATOM   1533  C   LEU A 222      -2.915   4.079  49.597  1.00 42.16           C  
ANISOU 1533  C   LEU A 222     5768   6623   3627    -66    -38    786       C  
ATOM   1534  O   LEU A 222      -2.435   4.356  50.696  1.00 46.06           O  
ANISOU 1534  O   LEU A 222     6288   7125   4087    -56    -34    810       O  
ATOM   1535  N   GLY A 223      -3.653   2.993  49.395  1.00 42.68           N  
ANISOU 1535  N   GLY A 223     5836   6668   3713   -112    -25    795       N  
ATOM   1536  CA  GLY A 223      -3.828   1.997  50.439  1.00 42.28           C  
ANISOU 1536  CA  GLY A 223     5820   6597   3646   -151     -9    836       C  
ATOM   1537  C   GLY A 223      -5.229   1.881  51.012  1.00 44.44           C  
ANISOU 1537  C   GLY A 223     6070   6907   3908   -198     30    841       C  
ATOM   1538  O   GLY A 223      -5.472   1.054  51.887  1.00 45.71           O  
ANISOU 1538  O   GLY A 223     6258   7054   4056   -234     46    875       O  
ATOM   1539  N   ALA A 224      -6.151   2.713  50.538  1.00 36.45           N  
ANISOU 1539  N   ALA A 224     5009   5941   2899   -199     46    807       N  
ATOM   1540  CA  ALA A 224      -7.550   2.570  50.924  1.00 37.03           C  
ANISOU 1540  CA  ALA A 224     5056   6048   2966   -245     82    808       C  
ATOM   1541  CB  ALA A 224      -8.384   3.736  50.402  1.00 40.85           C  
ANISOU 1541  CB  ALA A 224     5484   6587   3450   -234     95    768       C  
ATOM   1542  C   ALA A 224      -8.073   1.246  50.384  1.00 36.09           C  
ANISOU 1542  C   ALA A 224     4942   5891   2880   -288     84    816       C  
ATOM   1543  O   ALA A 224      -7.534   0.705  49.424  1.00 36.96           O  
ANISOU 1543  O   ALA A 224     5061   5959   3022   -277     58    807       O  
ATOM   1544  N   ARG A 225      -9.115   0.710  51.004  1.00 37.80           N  
ANISOU 1544  N   ARG A 225     5153   6120   3089   -336    115    833       N  
ATOM   1545  CA  ARG A 225      -9.665  -0.547  50.536  1.00 34.68           C  
ANISOU 1545  CA  ARG A 225     4762   5690   2724   -379    119    841       C  
ATOM   1546  CB  ARG A 225      -9.946  -1.489  51.707  1.00 41.21           C  
ANISOU 1546  CB  ARG A 225     5622   6503   3532   -421    140    885       C  
ATOM   1547  CG  ARG A 225      -8.692  -1.990  52.386  1.00 46.26           C  
ANISOU 1547  CG  ARG A 225     6317   7101   4157   -405    121    919       C  
ATOM   1548  CD  ARG A 225      -8.981  -3.200  53.260  1.00 65.15           C  
ANISOU 1548  CD  ARG A 225     8744   9468   6543   -451    138    961       C  
ATOM   1549  NE  ARG A 225      -7.877  -3.492  54.170  1.00 79.00           N  
ANISOU 1549  NE  ARG A 225    10549  11194   8273   -436    125    996       N  
ATOM   1550  CZ  ARG A 225      -7.111  -4.574  54.090  1.00 87.40           C  
ANISOU 1550  CZ  ARG A 225    11655  12200   9351   -441    105   1020       C  
ATOM   1551  NH1 ARG A 225      -7.324  -5.467  53.132  1.00 90.17           N  
ANISOU 1551  NH1 ARG A 225    12003  12516   9741   -461     94   1012       N  
ATOM   1552  NH2 ARG A 225      -6.130  -4.761  54.962  1.00 88.43           N  
ANISOU 1552  NH2 ARG A 225    11832  12310   9459   -426     95   1051       N  
ATOM   1553  C   ARG A 225     -10.927  -0.300  49.730  1.00 40.20           C  
ANISOU 1553  C   ARG A 225     5409   6421   3446   -400    136    808       C  
ATOM   1554  O   ARG A 225     -11.755   0.537  50.091  1.00 37.14           O  
ANISOU 1554  O   ARG A 225     4987   6085   3038   -406    161    795       O  
ATOM   1555  N   ARG A 226     -11.053  -1.033  48.631  1.00 37.99           N  
ANISOU 1555  N   ARG A 226     5123   6107   3205   -412    121    794       N  
ATOM   1556  CA  ARG A 226     -12.198  -0.927  47.743  1.00 40.80           C  
ANISOU 1556  CA  ARG A 226     5431   6485   3587   -434    133    763       C  
ATOM   1557  CB  ARG A 226     -12.129  -2.023  46.677  1.00 44.93           C  
ANISOU 1557  CB  ARG A 226     5961   6957   4152   -449    114    758       C  
ATOM   1558  CG  ARG A 226     -13.445  -2.726  46.424  1.00 55.41           C  
ANISOU 1558  CG  ARG A 226     7265   8289   5501   -502    136    755       C  
ATOM   1559  CD  ARG A 226     -13.359  -3.632  45.221  1.00 66.58           C  
ANISOU 1559  CD  ARG A 226     8682   9656   6959   -511    114    743       C  
ATOM   1560  NE  ARG A 226     -13.322  -2.866  43.984  1.00 74.04           N  
ANISOU 1560  NE  ARG A 226     9591  10614   7926   -479     97    699       N  
ATOM   1561  CZ  ARG A 226     -14.407  -2.462  43.333  1.00 80.34           C  
ANISOU 1561  CZ  ARG A 226    10342  11445   8740   -493    111    668       C  
ATOM   1562  NH1 ARG A 226     -15.616  -2.743  43.810  1.00 78.68           N  
ANISOU 1562  NH1 ARG A 226    10112  11259   8525   -539    143    677       N  
ATOM   1563  NH2 ARG A 226     -14.283  -1.770  42.211  1.00 83.72           N  
ANISOU 1563  NH2 ARG A 226    10740  11882   9187   -461     93    629       N  
ATOM   1564  C   ARG A 226     -13.520  -1.003  48.504  1.00 39.01           C  
ANISOU 1564  C   ARG A 226     5183   6295   3345   -480    173    773       C  
ATOM   1565  O   ARG A 226     -14.459  -0.269  48.204  1.00 43.03           O  
ANISOU 1565  O   ARG A 226     5646   6849   3854   -485    191    746       O  
ATOM   1566  N   GLU A 227     -13.573  -1.865  49.515  1.00 45.00           N  
ANISOU 1566  N   GLU A 227     5976   7036   4088   -513    188    813       N  
ATOM   1567  CA  GLU A 227     -14.792  -2.078  50.288  1.00 46.24           C  
ANISOU 1567  CA  GLU A 227     6117   7222   4230   -559    226    828       C  
ATOM   1568  CB  GLU A 227     -14.677  -3.345  51.142  1.00 55.15           C  
ANISOU 1568  CB  GLU A 227     7290   8312   5352   -596    234    873       C  
ATOM   1569  CG  GLU A 227     -14.442  -4.627  50.357  1.00 64.34           C  
ANISOU 1569  CG  GLU A 227     8474   9417   6554   -615    213    880       C  
ATOM   1570  CD  GLU A 227     -13.014  -4.760  49.856  1.00 72.80           C  
ANISOU 1570  CD  GLU A 227     9579  10445   7637   -574    174    880       C  
ATOM   1571  OE1 GLU A 227     -12.154  -3.963  50.288  1.00 71.26           O  
ANISOU 1571  OE1 GLU A 227     9397  10261   7416   -533    163    881       O  
ATOM   1572  OE2 GLU A 227     -12.756  -5.655  49.023  1.00 79.25           O  
ANISOU 1572  OE2 GLU A 227    10408  11215   8487   -582    154    878       O  
ATOM   1573  C   GLU A 227     -15.120  -0.892  51.186  1.00 46.16           C  
ANISOU 1573  C   GLU A 227     6089   7271   4180   -546    250    825       C  
ATOM   1574  O   GLU A 227     -16.237  -0.779  51.689  1.00 44.46           O  
ANISOU 1574  O   GLU A 227     5848   7091   3952   -579    283    828       O  
ATOM   1575  N   ASN A 228     -14.146  -0.011  51.398  1.00 40.45           N  
ANISOU 1575  N   ASN A 228     5377   6557   3436   -498    233    820       N  
ATOM   1576  CA  ASN A 228     -14.363   1.152  52.254  1.00 43.15           C  
ANISOU 1576  CA  ASN A 228     5703   6952   3738   -482    253    818       C  
ATOM   1577  CB  ASN A 228     -13.112   1.445  53.082  1.00 41.36           C  
ANISOU 1577  CB  ASN A 228     5520   6715   3482   -446    237    841       C  
ATOM   1578  CG  ASN A 228     -12.902   0.435  54.193  1.00 43.86           C  
ANISOU 1578  CG  ASN A 228     5883   7002   3781   -476    247    888       C  
ATOM   1579  OD1 ASN A 228     -13.830  -0.284  54.569  1.00 43.73           O  
ANISOU 1579  OD1 ASN A 228     5863   6987   3766   -523    273    905       O  
ATOM   1580  ND2 ASN A 228     -11.690   0.386  54.737  1.00 39.14           N  
ANISOU 1580  ND2 ASN A 228     5328   6378   3165   -448    227    910       N  
ATOM   1581  C   ASN A 228     -14.768   2.394  51.467  1.00 43.92           C  
ANISOU 1581  C   ASN A 228     5750   7095   3842   -454    252    773       C  
ATOM   1582  O   ASN A 228     -14.937   3.479  52.030  1.00 40.08           O  
ANISOU 1582  O   ASN A 228     5247   6657   3326   -436    266    765       O  
ATOM   1583  N   ILE A 229     -14.931   2.227  50.161  1.00 39.71           N  
ANISOU 1583  N   ILE A 229     5193   6547   3348   -452    236    743       N  
ATOM   1584  CA  ILE A 229     -15.315   3.335  49.305  1.00 36.46           C  
ANISOU 1584  CA  ILE A 229     4734   6175   2946   -426    234    699       C  
ATOM   1585  CB  ILE A 229     -14.326   3.495  48.141  1.00 34.68           C  
ANISOU 1585  CB  ILE A 229     4512   5919   2747   -384    195    674       C  
ATOM   1586  CG1 ILE A 229     -12.917   3.727  48.685  1.00 33.82           C  
ANISOU 1586  CG1 ILE A 229     4445   5790   2617   -344    172    693       C  
ATOM   1587  CD1 ILE A 229     -11.834   3.560  47.658  1.00 39.69           C  
ANISOU 1587  CD1 ILE A 229     5204   6491   3388   -309    133    680       C  
ATOM   1588  CG2 ILE A 229     -14.758   4.641  47.222  1.00 33.62           C  
ANISOU 1588  CG2 ILE A 229     4326   5825   2623   -359    193    628       C  
ATOM   1589  C   ILE A 229     -16.723   3.170  48.743  1.00 40.41           C  
ANISOU 1589  C   ILE A 229     5189   6697   3467   -465    256    679       C  
ATOM   1590  O   ILE A 229     -17.050   2.146  48.145  1.00 39.74           O  
ANISOU 1590  O   ILE A 229     5107   6579   3415   -495    252    681       O  
ATOM   1591  N   ILE A 230     -17.550   4.193  48.930  1.00 39.17           N  
ANISOU 1591  N   ILE A 230     4992   6598   3294   -463    280    658       N  
ATOM   1592  CA  ILE A 230     -18.891   4.202  48.359  1.00 40.75           C  
ANISOU 1592  CA  ILE A 230     5145   6824   3514   -495    301    635       C  
ATOM   1593  CB  ILE A 230     -19.978   4.318  49.440  1.00 34.18           C  
ANISOU 1593  CB  ILE A 230     4299   6034   2655   -532    342    652       C  
ATOM   1594  CG1 ILE A 230     -19.989   3.081  50.342  1.00 34.01           C  
ANISOU 1594  CG1 ILE A 230     4317   5978   2625   -572    354    698       C  
ATOM   1595  CD1 ILE A 230     -20.839   3.255  51.579  1.00 40.54           C  
ANISOU 1595  CD1 ILE A 230     5139   6845   3419   -601    393    720       C  
ATOM   1596  CG2 ILE A 230     -21.349   4.516  48.793  1.00 32.34           C  
ANISOU 1596  CG2 ILE A 230     4013   5834   2442   -559    363    624       C  
ATOM   1597  C   ILE A 230     -19.042   5.361  47.388  1.00 36.58           C  
ANISOU 1597  C   ILE A 230     4572   6330   2996   -461    291    589       C  
ATOM   1598  O   ILE A 230     -18.787   6.510  47.742  1.00 36.28           O  
ANISOU 1598  O   ILE A 230     4523   6330   2932   -427    293    577       O  
ATOM   1599  N   MET A 231     -19.455   5.048  46.162  1.00 37.88           N  
ANISOU 1599  N   MET A 231     4712   6481   3201   -470    281    562       N  
ATOM   1600  CA  MET A 231     -19.692   6.056  45.137  1.00 35.87           C  
ANISOU 1600  CA  MET A 231     4412   6256   2960   -441    272    516       C  
ATOM   1601  CB  MET A 231     -19.174   5.581  43.782  1.00 40.48           C  
ANISOU 1601  CB  MET A 231     4999   6797   3586   -426    239    496       C  
ATOM   1602  CG  MET A 231     -17.844   4.852  43.849  1.00 48.63           C  
ANISOU 1602  CG  MET A 231     6083   7773   4622   -409    210    520       C  
ATOM   1603  SD  MET A 231     -16.428   5.966  43.854  1.00 54.26           S  
ANISOU 1603  SD  MET A 231     6812   8491   5315   -341    182    510       S  
ATOM   1604  CE  MET A 231     -16.562   6.711  42.228  1.00 33.40           C  
ANISOU 1604  CE  MET A 231     4124   5861   2707   -310    162    455       C  
ATOM   1605  C   MET A 231     -21.178   6.362  45.033  1.00 41.52           C  
ANISOU 1605  C   MET A 231     5078   7017   3680   -473    304    498       C  
ATOM   1606  O   MET A 231     -22.011   5.455  45.084  1.00 42.41           O  
ANISOU 1606  O   MET A 231     5188   7118   3807   -521    320    511       O  
ATOM   1607  N   CYS A 232     -21.506   7.639  44.878  1.00 44.52           N  
ANISOU 1607  N   CYS A 232     5421   7448   4047   -448    311    468       N  
ATOM   1608  CA  CYS A 232     -22.895   8.062  44.747  1.00 40.09           C  
ANISOU 1608  CA  CYS A 232     4810   6933   3489   -474    340    447       C  
ATOM   1609  CB  CYS A 232     -23.370   8.802  46.000  1.00 40.63           C  
ANISOU 1609  CB  CYS A 232     4870   7052   3514   -479    372    461       C  
ATOM   1610  SG  CYS A 232     -23.181   7.916  47.546  1.00 47.55           S  
ANISOU 1610  SG  CYS A 232     5796   7909   4360   -510    391    517       S  
ATOM   1611  C   CYS A 232     -23.057   8.960  43.545  1.00 44.90           C  
ANISOU 1611  C   CYS A 232     5377   7565   4119   -445    327    400       C  
ATOM   1612  O   CYS A 232     -22.124   9.661  43.157  1.00 42.91           O  
ANISOU 1612  O   CYS A 232     5130   7311   3864   -398    302    383       O  
ATOM   1613  N   ASP A 233     -24.247   8.935  42.955  1.00 45.61           N  
ANISOU 1613  N   ASP A 233     5647   6708   4974   -857   -450    -23       N  
ATOM   1614  CA  ASP A 233     -24.591   9.877  41.905  1.00 48.10           C  
ANISOU 1614  CA  ASP A 233     5971   7036   5270   -835   -438    -67       C  
ATOM   1615  CB  ASP A 233     -24.698   9.175  40.547  1.00 52.18           C  
ANISOU 1615  CB  ASP A 233     6525   7486   5814   -840   -487    -99       C  
ATOM   1616  CG  ASP A 233     -25.657   7.997  40.564  1.00 50.83           C  
ANISOU 1616  CG  ASP A 233     6341   7285   5686   -889   -538    -54       C  
ATOM   1617  OD1 ASP A 233     -26.468   7.887  41.505  1.00 53.99           O  
ANISOU 1617  OD1 ASP A 233     6698   7723   6092   -920   -534      1       O  
ATOM   1618  OD2 ASP A 233     -25.604   7.180  39.622  1.00 55.36           O  
ANISOU 1618  OD2 ASP A 233     6948   7799   6288   -896   -582    -74       O  
ATOM   1619  C   ASP A 233     -25.899  10.573  42.259  1.00 52.32           C  
ANISOU 1619  C   ASP A 233     6456   7631   5794   -856   -422    -34       C  
ATOM   1620  O   ASP A 233     -26.352  10.508  43.402  1.00 48.92           O  
ANISOU 1620  O   ASP A 233     5984   7239   5363   -880   -409     18       O  
ATOM   1621  N   SER A 234     -26.505  11.220  41.269  1.00 55.29           N  
ANISOU 1621  N   SER A 234     6834   8013   6160   -847   -423    -63       N  
ATOM   1622  CA  SER A 234     -27.737  11.970  41.469  1.00 58.47           C  
ANISOU 1622  CA  SER A 234     7193   8472   6551   -863   -406    -38       C  
ATOM   1623  CB  SER A 234     -28.135  12.674  40.168  1.00 63.21           C  
ANISOU 1623  CB  SER A 234     7809   9069   7140   -845   -408    -85       C  
ATOM   1624  OG  SER A 234     -28.289  11.747  39.106  1.00 71.07           O  
ANISOU 1624  OG  SER A 234     8837   9999   8168   -859   -461   -102       O  
ATOM   1625  C   SER A 234     -28.881  11.087  41.967  1.00 58.59           C  
ANISOU 1625  C   SER A 234     7174   8487   6600   -915   -440     22       C  
ATOM   1626  O   SER A 234     -29.777  11.559  42.666  1.00 58.22           O  
ANISOU 1626  O   SER A 234     7081   8495   6544   -934   -421     61       O  
ATOM   1627  N   GLN A 235     -28.838   9.803  41.624  1.00 55.94           N  
ANISOU 1627  N   GLN A 235     6861   8090   6303   -939   -490     31       N  
ATOM   1628  CA  GLN A 235     -29.898   8.876  42.012  1.00 56.57           C  
ANISOU 1628  CA  GLN A 235     6913   8164   6419   -989   -526     87       C  
ATOM   1629  CB  GLN A 235     -30.088   7.818  40.931  1.00 61.77           C  
ANISOU 1629  CB  GLN A 235     7605   8752   7115  -1006   -584     72       C  
ATOM   1630  CG  GLN A 235     -30.595   8.371  39.622  1.00 69.09           C  
ANISOU 1630  CG  GLN A 235     8545   9670   8035   -994   -593     30       C  
ATOM   1631  CD  GLN A 235     -30.696   7.302  38.569  1.00 79.61           C  
ANISOU 1631  CD  GLN A 235     9912  10931   9404  -1009   -650     15       C  
ATOM   1632  OE1 GLN A 235     -30.758   6.113  38.884  1.00 83.98           O  
ANISOU 1632  OE1 GLN A 235    10468  11448   9992  -1040   -686     47       O  
ATOM   1633  NE2 GLN A 235     -30.694   7.711  37.306  1.00 85.77           N  
ANISOU 1633  NE2 GLN A 235    10721  11691  10178   -988   -658    -36       N  
ATOM   1634  C   GLN A 235     -29.636   8.185  43.349  1.00 57.31           C  
ANISOU 1634  C   GLN A 235     6987   8265   6524  -1010   -524    138       C  
ATOM   1635  O   GLN A 235     -30.478   7.438  43.840  1.00 58.54           O  
ANISOU 1635  O   GLN A 235     7115   8419   6707  -1052   -550    189       O  
ATOM   1636  N   GLY A 236     -28.464   8.422  43.930  1.00 56.98           N  
ANISOU 1636  N   GLY A 236     6958   8229   6462   -982   -494    125       N  
ATOM   1637  CA  GLY A 236     -28.115   7.814  45.202  1.00 52.82           C  
ANISOU 1637  CA  GLY A 236     6415   7710   5944   -999   -489    171       C  
ATOM   1638  C   GLY A 236     -26.922   6.881  45.121  1.00 51.56           C  
ANISOU 1638  C   GLY A 236     6298   7491   5802   -988   -511    154       C  
ATOM   1639  O   GLY A 236     -26.119   6.963  44.190  1.00 45.52           O  
ANISOU 1639  O   GLY A 236     5576   6688   5032   -958   -516    100       O  
ATOM   1640  N   VAL A 237     -26.812   5.989  46.101  1.00 52.43           N  
ANISOU 1640  N   VAL A 237     6396   7592   5932  -1015   -524    201       N  
ATOM   1641  CA  VAL A 237     -25.690   5.056  46.192  1.00 48.86           C  
ANISOU 1641  CA  VAL A 237     5980   7087   5498  -1007   -544    192       C  
ATOM   1642  CB  VAL A 237     -25.764   4.212  47.490  1.00 43.57           C  
ANISOU 1642  CB  VAL A 237     5286   6423   4847  -1040   -552    254       C  
ATOM   1643  CG1 VAL A 237     -24.834   3.007  47.417  1.00 44.69           C  
ANISOU 1643  CG1 VAL A 237     5465   6499   5017  -1042   -586    249       C  
ATOM   1644  CG2 VAL A 237     -25.447   5.068  48.705  1.00 42.50           C  
ANISOU 1644  CG2 VAL A 237     5119   6352   4677  -1026   -498    273       C  
ATOM   1645  C   VAL A 237     -25.634   4.116  44.996  1.00 53.71           C  
ANISOU 1645  C   VAL A 237     6635   7627   6145  -1014   -597    165       C  
ATOM   1646  O   VAL A 237     -26.650   3.551  44.587  1.00 60.84           O  
ANISOU 1646  O   VAL A 237     7527   8513   7075  -1048   -633    186       O  
ATOM   1647  N   ILE A 238     -24.442   3.960  44.432  1.00 47.54           N  
ANISOU 1647  N   ILE A 238     5900   6803   5361   -982   -600    118       N  
ATOM   1648  CA  ILE A 238     -24.220   2.988  43.373  1.00 49.58           C  
ANISOU 1648  CA  ILE A 238     6199   6986   5651   -987   -649     93       C  
ATOM   1649  CB  ILE A 238     -23.118   3.459  42.412  1.00 46.57           C  
ANISOU 1649  CB  ILE A 238     5866   6577   5252   -941   -638     23       C  
ATOM   1650  CG1 ILE A 238     -23.505   4.812  41.812  1.00 39.14           C  
ANISOU 1650  CG1 ILE A 238     4916   5678   4276   -916   -605    -11       C  
ATOM   1651  CD1 ILE A 238     -22.388   5.495  41.076  1.00 38.67           C  
ANISOU 1651  CD1 ILE A 238     4897   5606   4191   -866   -582    -76       C  
ATOM   1652  CG2 ILE A 238     -22.888   2.433  41.315  1.00 48.21           C  
ANISOU 1652  CG2 ILE A 238     6117   6707   5493   -946   -690     -3       C  
ATOM   1653  C   ILE A 238     -23.864   1.635  43.989  1.00 56.43           C  
ANISOU 1653  C   ILE A 238     7075   7813   6554  -1013   -682    129       C  
ATOM   1654  O   ILE A 238     -22.720   1.392  44.376  1.00 49.82           O  
ANISOU 1654  O   ILE A 238     6260   6958   5713   -993   -673    118       O  
ATOM   1655  N   TYR A 239     -24.867   0.769  44.099  1.00 59.81           N  
ANISOU 1655  N   TYR A 239     7484   8226   7015  -1058   -720    172       N  
ATOM   1656  CA  TYR A 239     -24.700  -0.551  44.699  1.00 64.28           C  
ANISOU 1656  CA  TYR A 239     8053   8754   7616  -1088   -754    212       C  
ATOM   1657  CB  TYR A 239     -25.780  -0.799  45.757  1.00 68.91           C  
ANISOU 1657  CB  TYR A 239     8589   9381   8214  -1131   -755    280       C  
ATOM   1658  CG  TYR A 239     -27.194  -0.828  45.206  1.00 72.32           C  
ANISOU 1658  CG  TYR A 239     8998   9820   8661  -1162   -779    296       C  
ATOM   1659  CD1 TYR A 239     -27.903   0.348  44.994  1.00 74.20           C  
ANISOU 1659  CD1 TYR A 239     9210  10110   8871  -1152   -749    286       C  
ATOM   1660  CE1 TYR A 239     -29.196   0.327  44.497  1.00 73.41           C  
ANISOU 1660  CE1 TYR A 239     9090  10018   8786  -1180   -771    301       C  
ATOM   1661  CZ  TYR A 239     -29.798  -0.880  44.209  1.00 70.46           C  
ANISOU 1661  CZ  TYR A 239     8720   9597   8454  -1219   -823    327       C  
ATOM   1662  OH  TYR A 239     -31.083  -0.900  43.715  1.00 69.71           O  
ANISOU 1662  OH  TYR A 239     8603   9509   8373  -1247   -845    341       O  
ATOM   1663  CE2 TYR A 239     -29.118  -2.063  44.413  1.00 70.33           C  
ANISOU 1663  CE2 TYR A 239     8728   9527   8466  -1229   -854    337       C  
ATOM   1664  CD2 TYR A 239     -27.824  -2.033  44.910  1.00 71.20           C  
ANISOU 1664  CD2 TYR A 239     8860   9632   8562  -1201   -832    322       C  
ATOM   1665  C   TYR A 239     -24.757  -1.628  43.628  1.00 65.40           C  
ANISOU 1665  C   TYR A 239     8230   8822   7796  -1102   -810    194       C  
ATOM   1666  O   TYR A 239     -25.403  -1.440  42.599  1.00 71.24           O  
ANISOU 1666  O   TYR A 239     8977   9550   8540  -1104   -827    171       O  
ATOM   1667  N   LYS A 240     -24.087  -2.753  43.858  1.00 63.99           N  
ANISOU 1667  N   LYS A 240     8075   8594   7645  -1111   -838    205       N  
ATOM   1668  CA  LYS A 240     -24.149  -3.846  42.891  1.00 68.42           C  
ANISOU 1668  CA  LYS A 240     8670   9083   8244  -1127   -893    191       C  
ATOM   1669  CB  LYS A 240     -23.165  -4.964  43.233  1.00 69.22           C  
ANISOU 1669  CB  LYS A 240     8799   9132   8369  -1129   -916    198       C  
ATOM   1670  CG  LYS A 240     -21.716  -4.588  43.008  1.00 74.12           C  
ANISOU 1670  CG  LYS A 240     9458   9736   8968  -1082   -893    147       C  
ATOM   1671  CD  LYS A 240     -20.810  -5.799  43.080  1.00 76.91           C  
ANISOU 1671  CD  LYS A 240     9844  10027   9351  -1086   -924    148       C  
ATOM   1672  CE  LYS A 240     -20.822  -6.393  44.464  1.00 80.60           C  
ANISOU 1672  CE  LYS A 240    10284  10511   9829  -1111   -922    207       C  
ATOM   1673  NZ  LYS A 240     -19.847  -7.509  44.607  1.00 85.20           N  
ANISOU 1673  NZ  LYS A 240    10900  11036  10438  -1111   -949    207       N  
ATOM   1674  C   LYS A 240     -25.561  -4.399  42.810  1.00 64.35           C  
ANISOU 1674  C   LYS A 240     8126   8567   7757  -1174   -927    233       C  
ATOM   1675  O   LYS A 240     -26.205  -4.652  43.830  1.00 64.59           O  
ANISOU 1675  O   LYS A 240     8118   8629   7795  -1205   -924    289       O  
ATOM   1676  N   GLY A 241     -26.036  -4.576  41.585  1.00 62.78           N  
ANISOU 1676  N   GLY A 241     7946   8333   7573  -1178   -958    205       N  
ATOM   1677  CA  GLY A 241     -27.394  -5.025  41.354  1.00 67.36           C  
ANISOU 1677  CA  GLY A 241     8502   8912   8179  -1220   -991    238       C  
ATOM   1678  C   GLY A 241     -28.253  -3.892  40.831  1.00 72.72           C  
ANISOU 1678  C   GLY A 241     9161   9637   8834  -1213   -969    222       C  
ATOM   1679  O   GLY A 241     -29.234  -4.126  40.121  1.00 77.30           O  
ANISOU 1679  O   GLY A 241     9735  10204   9432  -1236   -999    225       O  
ATOM   1680  N   ARG A 242     -27.888  -2.661  41.184  1.00 69.26           N  
ANISOU 1680  N   ARG A 242     8710   9253   8354  -1180   -918    204       N  
ATOM   1681  CA  ARG A 242     -28.596  -1.489  40.685  1.00 66.71           C  
ANISOU 1681  CA  ARG A 242     8369   8974   8004  -1168   -893    184       C  
ATOM   1682  CB  ARG A 242     -28.022  -0.201  41.278  1.00 64.62           C  
ANISOU 1682  CB  ARG A 242     8092   8769   7694  -1131   -833    169       C  
ATOM   1683  CG  ARG A 242     -28.879   1.028  41.029  1.00 59.55           C  
ANISOU 1683  CG  ARG A 242     7420   8182   7023  -1124   -804    161       C  
ATOM   1684  CD  ARG A 242     -28.202   2.288  41.535  1.00 54.91           C  
ANISOU 1684  CD  ARG A 242     6825   7648   6389  -1084   -745    140       C  
ATOM   1685  NE  ARG A 242     -27.996   3.260  40.468  1.00 52.73           N  
ANISOU 1685  NE  ARG A 242     6571   7376   6088  -1048   -728     81       N  
ATOM   1686  CZ  ARG A 242     -27.497   4.477  40.656  1.00 56.11           C  
ANISOU 1686  CZ  ARG A 242     6995   7849   6474  -1011   -677     55       C  
ATOM   1687  NH1 ARG A 242     -27.152   4.872  41.873  1.00 58.68           N  
ANISOU 1687  NH1 ARG A 242     7295   8221   6780  -1006   -639     82       N  
ATOM   1688  NH2 ARG A 242     -27.342   5.300  39.630  1.00 51.10           N  
ANISOU 1688  NH2 ARG A 242     6382   7215   5819   -980   -665      2       N  
ATOM   1689  C   ARG A 242     -28.510  -1.463  39.165  1.00 67.42           C  
ANISOU 1689  C   ARG A 242     8498   9019   8099  -1151   -918    129       C  
ATOM   1690  O   ARG A 242     -27.494  -1.851  38.586  1.00 65.02           O  
ANISOU 1690  O   ARG A 242     8239   8665   7801  -1128   -930     90       O  
ATOM   1691  N   THR A 243     -29.587  -1.024  38.524  1.00 68.40           N  
ANISOU 1691  N   THR A 243     8607   9161   8223  -1162   -925    126       N  
ATOM   1692  CA  THR A 243     -29.661  -1.018  37.070  1.00 67.46           C  
ANISOU 1692  CA  THR A 243     8521   9000   8109  -1150   -950     77       C  
ATOM   1693  CB  THR A 243     -30.780  -1.946  36.560  1.00 72.66           C  
ANISOU 1693  CB  THR A 243     9172   9626   8807  -1194  -1002    102       C  
ATOM   1694  OG1 THR A 243     -32.021  -1.229  36.523  1.00 78.81           O  
ANISOU 1694  OG1 THR A 243     9913  10455   9576  -1209   -992    119       O  
ATOM   1695  CG2 THR A 243     -30.921  -3.169  37.462  1.00 67.36           C  
ANISOU 1695  CG2 THR A 243     8487   8935   8170  -1232  -1030    157       C  
ATOM   1696  C   THR A 243     -29.908   0.390  36.550  1.00 67.05           C  
ANISOU 1696  C   THR A 243     8462   8994   8020  -1121   -914     41       C  
ATOM   1697  O   THR A 243     -29.370   0.787  35.516  1.00 63.62           O  
ANISOU 1697  O   THR A 243     8064   8535   7573  -1089   -913    -15       O  
ATOM   1698  N   ALA A 244     -30.727   1.139  37.280  1.00 69.77           N  
ANISOU 1698  N   ALA A 244     8759   9403   8346  -1132   -884     74       N  
ATOM   1699  CA  ALA A 244     -31.110   2.483  36.873  1.00 71.39           C  
ANISOU 1699  CA  ALA A 244     8951   9657   8517  -1108   -849     47       C  
ATOM   1700  CB  ALA A 244     -32.194   3.023  37.790  1.00 74.34           C  
ANISOU 1700  CB  ALA A 244     9267  10097   8880  -1132   -826     96       C  
ATOM   1701  C   ALA A 244     -29.913   3.420  36.862  1.00 72.83           C  
ANISOU 1701  C   ALA A 244     9156   9856   8661  -1058   -805      1       C  
ATOM   1702  O   ALA A 244     -29.166   3.503  37.838  1.00 75.98           O  
ANISOU 1702  O   ALA A 244     9549  10273   9047  -1047   -777     15       O  
ATOM   1703  N   GLY A 245     -29.731   4.115  35.744  1.00 68.33           N  
ANISOU 1703  N   GLY A 245     8612   9277   8073  -1028   -799    -54       N  
ATOM   1704  CA  GLY A 245     -28.662   5.084  35.611  1.00 66.36           C  
ANISOU 1704  CA  GLY A 245     8384   9043   7785   -979   -756   -101       C  
ATOM   1705  C   GLY A 245     -27.279   4.470  35.631  1.00 64.49           C  
ANISOU 1705  C   GLY A 245     8189   8759   7555   -959   -762   -125       C  
ATOM   1706  O   GLY A 245     -26.284   5.183  35.727  1.00 61.20           O  
ANISOU 1706  O   GLY A 245     7789   8356   7109   -919   -725   -158       O  
ATOM   1707  N   MET A 246     -27.219   3.145  35.534  1.00 63.73           N  
ANISOU 1707  N   MET A 246     8110   8606   7498   -985   -809   -107       N  
ATOM   1708  CA  MET A 246     -25.947   2.436  35.574  1.00 60.76           C  
ANISOU 1708  CA  MET A 246     7772   8180   7132   -969   -819   -126       C  
ATOM   1709  CB  MET A 246     -26.154   0.991  36.029  1.00 61.69           C  
ANISOU 1709  CB  MET A 246     7887   8258   7293  -1010   -863    -81       C  
ATOM   1710  CG  MET A 246     -26.423   0.848  37.508  1.00 62.64           C  
ANISOU 1710  CG  MET A 246     7965   8421   7414  -1033   -845    -20       C  
ATOM   1711  SD  MET A 246     -25.068   1.515  38.492  1.00 62.17           S  
ANISOU 1711  SD  MET A 246     7909   8393   7319   -994   -791    -31       S  
ATOM   1712  CE  MET A 246     -23.809   0.269  38.223  1.00 64.79           C  
ANISOU 1712  CE  MET A 246     8292   8645   7679   -987   -826    -51       C  
ATOM   1713  C   MET A 246     -25.227   2.447  34.232  1.00 61.53           C  
ANISOU 1713  C   MET A 246     7923   8227   7230   -939   -833   -191       C  
ATOM   1714  O   MET A 246     -25.796   2.786  33.199  1.00 66.36           O  
ANISOU 1714  O   MET A 246     8543   8832   7840   -936   -845   -219       O  
ATOM   1715  N   ASN A 247     -23.954   2.078  34.281  1.00 58.96           N  
ANISOU 1715  N   ASN A 247     7632   7866   6904   -916   -831   -216       N  
ATOM   1716  CA  ASN A 247     -23.118   1.870  33.106  1.00 51.43           C  
ANISOU 1716  CA  ASN A 247     6732   6855   5955   -889   -849   -274       C  
ATOM   1717  CB  ASN A 247     -22.753   3.191  32.430  1.00 50.16           C  
ANISOU 1717  CB  ASN A 247     6585   6720   5754   -846   -811   -329       C  
ATOM   1718  CG  ASN A 247     -22.014   4.154  33.351  1.00 63.74           C  
ANISOU 1718  CG  ASN A 247     8291   8493   7436   -815   -754   -332       C  
ATOM   1719  OD1 ASN A 247     -21.024   3.807  33.996  1.00 61.81           O  
ANISOU 1719  OD1 ASN A 247     8058   8235   7190   -804   -745   -329       O  
ATOM   1720  ND2 ASN A 247     -22.499   5.388  33.402  1.00 71.57           N  
ANISOU 1720  ND2 ASN A 247     9257   9543   8394   -801   -716   -339       N  
ATOM   1721  C   ASN A 247     -21.860   1.114  33.508  1.00 53.33           C  
ANISOU 1721  C   ASN A 247     7001   7055   6207   -878   -855   -280       C  
ATOM   1722  O   ASN A 247     -21.685   0.765  34.674  1.00 52.55           O  
ANISOU 1722  O   ASN A 247     6881   6973   6112   -891   -846   -238       O  
ATOM   1723  N   LYS A 248     -20.989   0.875  32.536  1.00 52.63           N  
ANISOU 1723  N   LYS A 248     6962   6913   6122   -853   -870   -332       N  
ATOM   1724  CA  LYS A 248     -19.769   0.109  32.747  1.00 54.38           C  
ANISOU 1724  CA  LYS A 248     7216   7088   6357   -841   -879   -343       C  
ATOM   1725  CB  LYS A 248     -18.991   0.033  31.436  1.00 57.27           C  
ANISOU 1725  CB  LYS A 248     7636   7399   6724   -812   -895   -408       C  
ATOM   1726  CG  LYS A 248     -17.697  -0.734  31.515  1.00 58.49           C  
ANISOU 1726  CG  LYS A 248     7829   7503   6892   -797   -906   -426       C  
ATOM   1727  CD  LYS A 248     -16.784  -0.356  30.364  1.00 60.71           C  
ANISOU 1727  CD  LYS A 248     8159   7749   7160   -757   -902   -497       C  
ATOM   1728  CE  LYS A 248     -17.530  -0.409  29.041  1.00 62.86           C  
ANISOU 1728  CE  LYS A 248     8448   7993   7444   -765   -933   -523       C  
ATOM   1729  NZ  LYS A 248     -16.773  -1.173  28.010  1.00 69.51           N  
ANISOU 1729  NZ  LYS A 248     9343   8761   8308   -754   -967   -566       N  
ATOM   1730  C   LYS A 248     -18.873   0.684  33.851  1.00 53.10           C  
ANISOU 1730  C   LYS A 248     7043   6966   6165   -816   -832   -337       C  
ATOM   1731  O   LYS A 248     -18.256  -0.057  34.618  1.00 55.81           O  
ANISOU 1731  O   LYS A 248     7390   7292   6524   -823   -838   -314       O  
ATOM   1732  N   TYR A 249     -18.827   2.007  33.946  1.00 48.46           N  
ANISOU 1732  N   TYR A 249     6442   6434   5538   -788   -784   -357       N  
ATOM   1733  CA  TYR A 249     -17.870   2.680  34.822  1.00 47.57           C  
ANISOU 1733  CA  TYR A 249     6324   6357   5394   -757   -736   -363       C  
ATOM   1734  CB  TYR A 249     -17.567   4.071  34.272  1.00 51.40           C  
ANISOU 1734  CB  TYR A 249     6818   6876   5837   -716   -694   -413       C  
ATOM   1735  CG  TYR A 249     -17.259   4.020  32.798  1.00 54.07           C  
ANISOU 1735  CG  TYR A 249     7202   7163   6180   -696   -716   -472       C  
ATOM   1736  CD1 TYR A 249     -15.978   3.741  32.342  1.00 43.79           C  
ANISOU 1736  CD1 TYR A 249     5946   5813   4878   -667   -719   -517       C  
ATOM   1737  CE1 TYR A 249     -15.712   3.665  30.988  1.00 37.59           C  
ANISOU 1737  CE1 TYR A 249     5204   4980   4098   -650   -740   -570       C  
ATOM   1738  CZ  TYR A 249     -16.736   3.856  30.080  1.00 46.47           C  
ANISOU 1738  CZ  TYR A 249     6324   6103   5228   -663   -760   -578       C  
ATOM   1739  OH  TYR A 249     -16.498   3.791  28.728  1.00 51.93           O  
ANISOU 1739  OH  TYR A 249     7058   6748   5924   -648   -782   -631       O  
ATOM   1740  CE2 TYR A 249     -18.012   4.118  30.511  1.00 50.78           C  
ANISOU 1740  CE2 TYR A 249     6824   6694   5774   -693   -758   -534       C  
ATOM   1741  CD2 TYR A 249     -18.270   4.191  31.858  1.00 56.77           C  
ANISOU 1741  CD2 TYR A 249     7541   7501   6528   -709   -737   -482       C  
ATOM   1742  C   TYR A 249     -18.357   2.771  36.260  1.00 50.09           C  
ANISOU 1742  C   TYR A 249     6593   6731   5708   -780   -715   -301       C  
ATOM   1743  O   TYR A 249     -17.593   2.525  37.193  1.00 55.61           O  
ANISOU 1743  O   TYR A 249     7290   7434   6404   -775   -700   -284       O  
ATOM   1744  N   LYS A 250     -19.626   3.120  36.439  1.00 43.55           N  
ANISOU 1744  N   LYS A 250     5725   5943   4878   -806   -713   -268       N  
ATOM   1745  CA  LYS A 250     -20.227   3.115  37.767  1.00 50.71           C  
ANISOU 1745  CA  LYS A 250     6583   6900   5784   -833   -698   -206       C  
ATOM   1746  CB  LYS A 250     -21.673   3.614  37.713  1.00 44.17           C  
ANISOU 1746  CB  LYS A 250     5715   6115   4952   -858   -697   -180       C  
ATOM   1747  CG  LYS A 250     -21.836   5.037  37.207  1.00 46.35           C  
ANISOU 1747  CG  LYS A 250     5986   6436   5190   -827   -657   -217       C  
ATOM   1748  CD  LYS A 250     -23.304   5.431  37.225  1.00 48.48           C  
ANISOU 1748  CD  LYS A 250     6214   6747   5460   -855   -659   -186       C  
ATOM   1749  CE  LYS A 250     -23.494   6.908  36.932  1.00 48.76           C  
ANISOU 1749  CE  LYS A 250     6237   6835   5453   -825   -615   -216       C  
ATOM   1750  NZ  LYS A 250     -24.899   7.327  37.187  1.00 48.56           N  
ANISOU 1750  NZ  LYS A 250     6165   6858   5426   -853   -611   -179       N  
ATOM   1751  C   LYS A 250     -20.190   1.713  38.364  1.00 57.56           C  
ANISOU 1751  C   LYS A 250     7451   7729   6692   -867   -736   -163       C  
ATOM   1752  O   LYS A 250     -20.133   1.545  39.584  1.00 60.06           O  
ANISOU 1752  O   LYS A 250     7740   8074   7007   -880   -721   -118       O  
ATOM   1753  N   GLU A 251     -20.219   0.708  37.495  1.00 52.37           N  
ANISOU 1753  N   GLU A 251     6824   7006   6068   -881   -785   -175       N  
ATOM   1754  CA  GLU A 251     -20.327  -0.670  37.942  1.00 63.56           C  
ANISOU 1754  CA  GLU A 251     8241   8383   7526   -918   -827   -133       C  
ATOM   1755  CB  GLU A 251     -20.703  -1.581  36.773  1.00 70.60           C  
ANISOU 1755  CB  GLU A 251     9162   9211   8453   -936   -881   -149       C  
ATOM   1756  CG  GLU A 251     -21.119  -2.977  37.203  1.00 78.36           C  
ANISOU 1756  CG  GLU A 251    10136  10157   9479   -980   -927   -100       C  
ATOM   1757  CD  GLU A 251     -22.212  -3.552  36.327  1.00 91.41           C  
ANISOU 1757  CD  GLU A 251    11790  11780  11162  -1012   -972    -94       C  
ATOM   1758  OE1 GLU A 251     -21.926  -4.498  35.562  1.00 97.13           O  
ANISOU 1758  OE1 GLU A 251    12550  12438  11915  -1018  -1014   -112       O  
ATOM   1759  OE2 GLU A 251     -23.359  -3.059  36.409  1.00 93.33           O  
ANISOU 1759  OE2 GLU A 251    11996  12065  11398  -1031   -966    -70       O  
ATOM   1760  C   GLU A 251     -19.053  -1.176  38.601  1.00 66.52           C  
ANISOU 1760  C   GLU A 251     8636   8735   7903   -902   -820   -134       C  
ATOM   1761  O   GLU A 251     -19.111  -2.032  39.485  1.00 66.04           O  
ANISOU 1761  O   GLU A 251     8561   8667   7865   -930   -836    -87       O  
ATOM   1762  N   TYR A 252     -17.905  -0.651  38.185  1.00 64.52           N  
ANISOU 1762  N   TYR A 252     8417   8471   7628   -859   -797   -187       N  
ATOM   1763  CA  TYR A 252     -16.650  -1.154  38.720  1.00 68.35           C  
ANISOU 1763  CA  TYR A 252     8925   8930   8116   -843   -793   -192       C  
ATOM   1764  CB  TYR A 252     -15.446  -0.513  38.037  1.00 72.04           C  
ANISOU 1764  CB  TYR A 252     9432   9381   8557   -793   -769   -258       C  
ATOM   1765  CG  TYR A 252     -14.162  -1.161  38.498  1.00 77.75           C  
ANISOU 1765  CG  TYR A 252    10182  10069   9289   -779   -771   -264       C  
ATOM   1766  CD1 TYR A 252     -13.829  -2.444  38.086  1.00 82.72           C  
ANISOU 1766  CD1 TYR A 252    10843  10629   9957   -794   -819   -265       C  
ATOM   1767  CE1 TYR A 252     -12.668  -3.057  38.515  1.00 82.84           C  
ANISOU 1767  CE1 TYR A 252    10882  10613   9982   -781   -822   -270       C  
ATOM   1768  CZ  TYR A 252     -11.825  -2.392  39.378  1.00 81.21           C  
ANISOU 1768  CZ  TYR A 252    10668  10444   9745   -753   -777   -273       C  
ATOM   1769  OH  TYR A 252     -10.670  -3.008  39.805  1.00 81.25           O  
ANISOU 1769  OH  TYR A 252    10697  10417   9759   -741   -780   -277       O  
ATOM   1770  CE2 TYR A 252     -12.137  -1.120  39.814  1.00 77.79           C  
ANISOU 1770  CE2 TYR A 252    10204  10081   9273   -738   -728   -271       C  
ATOM   1771  CD2 TYR A 252     -13.305  -0.514  39.379  1.00 76.76           C  
ANISOU 1771  CD2 TYR A 252    10050   9982   9134   -751   -726   -267       C  
ATOM   1772  C   TYR A 252     -16.545  -0.937  40.226  1.00 67.55           C  
ANISOU 1772  C   TYR A 252     8786   8880   8000   -849   -760   -145       C  
ATOM   1773  O   TYR A 252     -16.191  -1.855  40.962  1.00 71.60           O  
ANISOU 1773  O   TYR A 252     9299   9372   8535   -866   -777   -113       O  
ATOM   1774  N   PHE A 253     -16.861   0.269  40.685  1.00 60.68           N  
ANISOU 1774  N   PHE A 253     7885   8077   7094   -836   -714   -142       N  
ATOM   1775  CA  PHE A 253     -16.724   0.592  42.101  1.00 51.51           C  
ANISOU 1775  CA  PHE A 253     6688   6968   5914   -838   -679   -101       C  
ATOM   1776  CB  PHE A 253     -16.131   1.994  42.266  1.00 45.75           C  
ANISOU 1776  CB  PHE A 253     5955   6289   5137   -795   -621   -135       C  
ATOM   1777  CG  PHE A 253     -14.672   2.077  41.908  1.00 49.33           C  
ANISOU 1777  CG  PHE A 253     6453   6711   5579   -754   -609   -186       C  
ATOM   1778  CD1 PHE A 253     -13.725   1.383  42.644  1.00 51.22           C  
ANISOU 1778  CD1 PHE A 253     6704   6927   5829   -751   -612   -173       C  
ATOM   1779  CE1 PHE A 253     -12.378   1.450  42.315  1.00 51.73           C  
ANISOU 1779  CE1 PHE A 253     6809   6962   5884   -713   -602   -221       C  
ATOM   1780  CZ  PHE A 253     -11.969   2.217  41.241  1.00 51.85           C  
ANISOU 1780  CZ  PHE A 253     6854   6969   5878   -677   -588   -283       C  
ATOM   1781  CE2 PHE A 253     -12.904   2.912  40.499  1.00 49.93           C  
ANISOU 1781  CE2 PHE A 253     6599   6747   5623   -680   -584   -297       C  
ATOM   1782  CD2 PHE A 253     -14.246   2.840  40.832  1.00 50.28           C  
ANISOU 1782  CD2 PHE A 253     6604   6823   5679   -718   -595   -249       C  
ATOM   1783  C   PHE A 253     -18.045   0.482  42.863  1.00 51.75           C  
ANISOU 1783  C   PHE A 253     6668   7040   5955   -881   -683    -38       C  
ATOM   1784  O   PHE A 253     -18.182   1.021  43.960  1.00 50.07           O  
ANISOU 1784  O   PHE A 253     6419   6883   5721   -883   -648     -6       O  
ATOM   1785  N   ALA A 254     -19.009  -0.228  42.284  1.00 52.58           N  
ANISOU 1785  N   ALA A 254     6771   7116   6092   -915   -727    -22       N  
ATOM   1786  CA  ALA A 254     -20.287  -0.463  42.952  1.00 54.56           C  
ANISOU 1786  CA  ALA A 254     6975   7399   6355   -958   -737     38       C  
ATOM   1787  CB  ALA A 254     -21.220  -1.254  42.051  1.00 52.00           C  
ANISOU 1787  CB  ALA A 254     6658   7032   6067   -990   -788     44       C  
ATOM   1788  C   ALA A 254     -20.069  -1.186  44.281  1.00 51.81           C  
ANISOU 1788  C   ALA A 254     6607   7057   6021   -980   -738     92       C  
ATOM   1789  O   ALA A 254     -19.206  -2.054  44.392  1.00 51.34           O  
ANISOU 1789  O   ALA A 254     6576   6951   5980   -978   -758     89       O  
ATOM   1790  N   SER A 255     -20.854  -0.821  45.289  1.00 55.75           N  
ANISOU 1790  N   SER A 255     7058   7614   6510  -1002   -716    141       N  
ATOM   1791  CA  SER A 255     -20.593  -1.262  46.659  1.00 57.19           C  
ANISOU 1791  CA  SER A 255     7219   7815   6697  -1018   -707    190       C  
ATOM   1792  CB  SER A 255     -20.643  -0.056  47.603  1.00 52.08           C  
ANISOU 1792  CB  SER A 255     6535   7245   6009  -1002   -650    203       C  
ATOM   1793  OG  SER A 255     -20.513  -0.455  48.953  1.00 56.20           O  
ANISOU 1793  OG  SER A 255     7031   7789   6534  -1020   -640    255       O  
ATOM   1794  C   SER A 255     -21.558  -2.342  47.153  1.00 58.44           C  
ANISOU 1794  C   SER A 255     7351   7960   6892  -1070   -745    250       C  
ATOM   1795  O   SER A 255     -22.651  -2.510  46.615  1.00 55.97           O  
ANISOU 1795  O   SER A 255     7026   7644   6596  -1096   -770    262       O  
ATOM   1796  N   GLU A 256     -21.133  -3.068  48.183  1.00 62.56           N  
ANISOU 1796  N   GLU A 256     7866   8476   7426  -1084   -749    289       N  
ATOM   1797  CA  GLU A 256     -21.967  -4.068  48.844  1.00 67.74           C  
ANISOU 1797  CA  GLU A 256     8497   9125   8116  -1133   -781    350       C  
ATOM   1798  CB  GLU A 256     -21.106  -5.107  49.563  1.00 79.63           C  
ANISOU 1798  CB  GLU A 256    10018  10595   9641  -1140   -797    372       C  
ATOM   1799  CG  GLU A 256     -19.745  -5.318  48.954  1.00 90.80           C  
ANISOU 1799  CG  GLU A 256    11483  11960  11056  -1103   -802    321       C  
ATOM   1800  CD  GLU A 256     -19.820  -6.128  47.685  1.00102.01           C  
ANISOU 1800  CD  GLU A 256    12941  13311  12508  -1110   -851    292       C  
ATOM   1801  OE1 GLU A 256     -20.815  -6.865  47.516  1.00103.38           O  
ANISOU 1801  OE1 GLU A 256    13101  13466  12711  -1150   -889    324       O  
ATOM   1802  OE2 GLU A 256     -18.890  -6.025  46.858  1.00107.89           O  
ANISOU 1802  OE2 GLU A 256    13727  14019  13246  -1076   -853    237       O  
ATOM   1803  C   GLU A 256     -22.896  -3.425  49.854  1.00 63.50           C  
ANISOU 1803  C   GLU A 256     7906   8661   7562  -1153   -750    398       C  
ATOM   1804  O   GLU A 256     -23.836  -4.059  50.331  1.00 65.53           O  
ANISOU 1804  O   GLU A 256     8135   8922   7843  -1195   -773    449       O  
ATOM   1805  N   THR A 257     -22.608  -2.170  50.187  1.00 60.11           N  
ANISOU 1805  N   THR A 257     7462   8286   7090  -1122   -699    381       N  
ATOM   1806  CA  THR A 257     -23.287  -1.477  51.275  1.00 62.80           C  
ANISOU 1806  CA  THR A 257     7752   8699   7410  -1135   -663    423       C  
ATOM   1807  CB  THR A 257     -22.887   0.009  51.326  1.00 58.80           C  
ANISOU 1807  CB  THR A 257     7238   8247   6855  -1094   -606    389       C  
ATOM   1808  OG1 THR A 257     -23.508   0.631  52.456  1.00 58.04           O  
ANISOU 1808  OG1 THR A 257     7094   8220   6740  -1108   -571    433       O  
ATOM   1809  CG2 THR A 257     -23.317   0.730  50.054  1.00 58.66           C  
ANISOU 1809  CG2 THR A 257     7233   8228   6827  -1077   -606    343       C  
ATOM   1810  C   THR A 257     -24.806  -1.578  51.178  1.00 65.33           C  
ANISOU 1810  C   THR A 257     8038   9038   7746  -1176   -681    460       C  
ATOM   1811  O   THR A 257     -25.376  -1.663  50.087  1.00 64.68           O  
ANISOU 1811  O   THR A 257     7968   8930   7677  -1181   -708    437       O  
ATOM   1812  N   GLU A 258     -25.455  -1.596  52.334  1.00 65.83           N  
ANISOU 1812  N   GLU A 258     8057   9146   7808  -1204   -668    516       N  
ATOM   1813  CA  GLU A 258     -26.904  -1.654  52.382  1.00 70.93           C  
ANISOU 1813  CA  GLU A 258     8666   9816   8468  -1243   -683    555       C  
ATOM   1814  CB  GLU A 258     -27.371  -2.292  53.692  1.00 76.37           C  
ANISOU 1814  CB  GLU A 258     9318  10525   9172  -1282   -687    623       C  
ATOM   1815  CG  GLU A 258     -28.315  -3.470  53.506  1.00 84.16           C  
ANISOU 1815  CG  GLU A 258    10299  11475  10203  -1329   -739    661       C  
ATOM   1816  CD  GLU A 258     -28.116  -4.552  54.554  1.00 89.63           C  
ANISOU 1816  CD  GLU A 258    10983  12151  10920  -1358   -756    712       C  
ATOM   1817  OE1 GLU A 258     -28.623  -4.394  55.687  1.00 92.17           O  
ANISOU 1817  OE1 GLU A 258    11264  12521  11234  -1379   -736    761       O  
ATOM   1818  OE2 GLU A 258     -27.450  -5.562  54.242  1.00 90.86           O  
ANISOU 1818  OE2 GLU A 258    11176  12246  11103  -1359   -791    702       O  
ATOM   1819  C   GLU A 258     -27.461  -0.242  52.221  1.00 69.12           C  
ANISOU 1819  C   GLU A 258     8411   9648   8203  -1225   -641    538       C  
ATOM   1820  O   GLU A 258     -28.670  -0.047  52.080  1.00 66.59           O  
ANISOU 1820  O   GLU A 258     8060   9352   7888  -1251   -648    559       O  
ATOM   1821  N   ALA A 259     -26.559   0.737  52.230  1.00 65.63           N  
ANISOU 1821  N   ALA A 259     7982   9231   7725  -1182   -599    499       N  
ATOM   1822  CA  ALA A 259     -26.925   2.139  52.064  1.00 60.38           C  
ANISOU 1822  CA  ALA A 259     7295   8623   7022  -1159   -557    478       C  
ATOM   1823  CB  ALA A 259     -25.739   3.034  52.382  1.00 61.58           C  
ANISOU 1823  CB  ALA A 259     7461   8801   7136  -1113   -509    444       C  
ATOM   1824  C   ALA A 259     -27.435   2.420  50.657  1.00 61.39           C  
ANISOU 1824  C   ALA A 259     7441   8730   7154  -1152   -576    436       C  
ATOM   1825  O   ALA A 259     -26.975   1.818  49.686  1.00 62.79           O  
ANISOU 1825  O   ALA A 259     7660   8847   7350  -1144   -609    402       O  
ATOM   1826  N   ARG A 260     -28.383   3.343  50.551  1.00 55.19           N  
ANISOU 1826  N   ARG A 260     6625   7995   6351  -1155   -554    440       N  
ATOM   1827  CA  ARG A 260     -28.970   3.680  49.264  1.00 54.73           C  
ANISOU 1827  CA  ARG A 260     6578   7922   6294  -1150   -570    404       C  
ATOM   1828  CB  ARG A 260     -30.396   3.139  49.179  1.00 53.20           C  
ANISOU 1828  CB  ARG A 260     6355   7728   6129  -1197   -604    445       C  
ATOM   1829  CG  ARG A 260     -30.469   1.620  49.112  1.00 54.48           C  
ANISOU 1829  CG  ARG A 260     6533   7829   6338  -1231   -659    471       C  
ATOM   1830  CD  ARG A 260     -29.976   1.119  47.765  1.00 54.14           C  
ANISOU 1830  CD  ARG A 260     6541   7718   6312  -1215   -695    421       C  
ATOM   1831  NE  ARG A 260     -29.846  -0.334  47.715  1.00 56.89           N  
ANISOU 1831  NE  ARG A 260     6909   8004   6702  -1243   -744    441       N  
ATOM   1832  CZ  ARG A 260     -28.776  -1.007  48.126  1.00 57.56           C  
ANISOU 1832  CZ  ARG A 260     7019   8056   6796  -1234   -750    441       C  
ATOM   1833  NH1 ARG A 260     -27.731  -0.359  48.623  1.00 61.67           N  
ANISOU 1833  NH1 ARG A 260     7548   8599   7286  -1199   -710    421       N  
ATOM   1834  NH2 ARG A 260     -28.750  -2.330  48.040  1.00 55.59           N  
ANISOU 1834  NH2 ARG A 260     6786   7750   6585  -1261   -797    460       N  
ATOM   1835  C   ARG A 260     -28.958   5.185  49.002  1.00 51.44           C  
ANISOU 1835  C   ARG A 260     6153   7558   5835  -1115   -523    368       C  
ATOM   1836  O   ARG A 260     -29.020   5.619  47.851  1.00 55.38           O  
ANISOU 1836  O   ARG A 260     6673   8041   6327  -1095   -528    322       O  
ATOM   1837  N   THR A 261     -28.892   5.977  50.067  1.00 47.69           N  
ANISOU 1837  N   THR A 261     5645   7144   5330  -1107   -476    390       N  
ATOM   1838  CA  THR A 261     -28.765   7.422  49.916  1.00 54.70           C  
ANISOU 1838  CA  THR A 261     6524   8083   6175  -1071   -427    356       C  
ATOM   1839  CB  THR A 261     -29.863   8.191  50.673  1.00 53.08           C  
ANISOU 1839  CB  THR A 261     6264   7949   5954  -1090   -397    396       C  
ATOM   1840  OG1 THR A 261     -29.653   8.063  52.085  1.00 50.27           O  
ANISOU 1840  OG1 THR A 261     5882   7627   5593  -1102   -375    442       O  
ATOM   1841  CG2 THR A 261     -31.240   7.657  50.307  1.00 55.92           C  
ANISOU 1841  CG2 THR A 261     6603   8301   6344  -1132   -436    426       C  
ATOM   1842  C   THR A 261     -27.413   7.893  50.431  1.00 51.99           C  
ANISOU 1842  C   THR A 261     6199   7751   5804  -1032   -389    332       C  
ATOM   1843  O   THR A 261     -26.758   7.199  51.213  1.00 45.85           O  
ANISOU 1843  O   THR A 261     5426   6957   5036  -1039   -393    355       O  
ATOM   1844  N   LEU A 262     -27.013   9.081  49.994  1.00 52.27           N  
ANISOU 1844  N   LEU A 262     5593   9230   5036   -286   1090    133       N  
ATOM   1845  CA  LEU A 262     -25.775   9.703  50.448  1.00 53.00           C  
ANISOU 1845  CA  LEU A 262     5806   9278   5053   -282   1112     84       C  
ATOM   1846  CB  LEU A 262     -25.590  11.054  49.761  1.00 50.47           C  
ANISOU 1846  CB  LEU A 262     5512   8920   4746   -193   1125     49       C  
ATOM   1847  CG  LEU A 262     -24.439  11.928  50.252  1.00 49.81           C  
ANISOU 1847  CG  LEU A 262     5546   8790   4592   -175   1160     -3       C  
ATOM   1848  CD1 LEU A 262     -23.103  11.290  49.902  1.00 47.99           C  
ANISOU 1848  CD1 LEU A 262     5397   8517   4322   -227   1073    -15       C  
ATOM   1849  CD2 LEU A 262     -24.559  13.320  49.658  1.00 51.12           C  
ANISOU 1849  CD2 LEU A 262     5716   8928   4779    -82   1189    -32       C  
ATOM   1850  C   LEU A 262     -25.763   9.880  51.966  1.00 53.75           C  
ANISOU 1850  C   LEU A 262     5941   9393   5090   -304   1213     71       C  
ATOM   1851  O   LEU A 262     -24.732   9.716  52.619  1.00 46.67           O  
ANISOU 1851  O   LEU A 262     5138   8471   4124   -345   1213     46       O  
ATOM   1852  N   THR A 263     -26.923  10.217  52.520  1.00 52.56           N  
ANISOU 1852  N   THR A 263     5718   9285   4969   -275   1300     87       N  
ATOM   1853  CA  THR A 263     -27.057  10.417  53.955  1.00 53.96           C  
ANISOU 1853  CA  THR A 263     5925   9482   5093   -290   1404     77       C  
ATOM   1854  CB  THR A 263     -28.487  10.825  54.321  1.00 55.73           C  
ANISOU 1854  CB  THR A 263     6052   9756   5368   -247   1496     99       C  
ATOM   1855  OG1 THR A 263     -28.900  11.904  53.475  1.00 59.07           O  
ANISOU 1855  OG1 THR A 263     6439  10164   5840   -160   1502     85       O  
ATOM   1856  CG2 THR A 263     -28.567  11.259  55.785  1.00 59.57           C  
ANISOU 1856  CG2 THR A 263     6585  10257   5794   -247   1614     82       C  
ATOM   1857  C   THR A 263     -26.681   9.163  54.728  1.00 51.27           C  
ANISOU 1857  C   THR A 263     5613   9158   4709   -384   1384     97       C  
ATOM   1858  O   THR A 263     -25.969   9.233  55.734  1.00 53.71           O  
ANISOU 1858  O   THR A 263     6012   9453   4944   -412   1425     71       O  
ATOM   1859  N   GLU A 264     -27.155   8.017  54.252  1.00 49.58           N  
ANISOU 1859  N   GLU A 264     5325   8972   4542   -434   1319    142       N  
ATOM   1860  CA  GLU A 264     -26.856   6.750  54.908  1.00 61.66           C  
ANISOU 1860  CA  GLU A 264     6873  10518   6036   -526   1293    166       C  
ATOM   1861  CB  GLU A 264     -27.804   5.660  54.415  1.00 69.81           C  
ANISOU 1861  CB  GLU A 264     7793  11593   7139   -564   1244    222       C  
ATOM   1862  CG  GLU A 264     -29.265   6.065  54.475  1.00 80.62           C  
ANISOU 1862  CG  GLU A 264     9049  13006   8576   -517   1317    250       C  
ATOM   1863  CD  GLU A 264     -30.168   5.117  53.712  1.00 88.87           C  
ANISOU 1863  CD  GLU A 264     9979  14084   9705   -544   1251    304       C  
ATOM   1864  OE1 GLU A 264     -30.843   4.287  54.359  1.00 93.04           O  
ANISOU 1864  OE1 GLU A 264    10451  14654  10247   -596   1279    343       O  
ATOM   1865  OE2 GLU A 264     -30.198   5.201  52.466  1.00 91.32           O  
ANISOU 1865  OE2 GLU A 264    10257  14374  10066   -513   1169    307       O  
ATOM   1866  C   GLU A 264     -25.405   6.324  54.694  1.00 60.43           C  
ANISOU 1866  C   GLU A 264     6821  10315   5825   -570   1209    141       C  
ATOM   1867  O   GLU A 264     -24.765   5.805  55.606  1.00 57.93           O  
ANISOU 1867  O   GLU A 264     6572   9994   5444   -629   1219    133       O  
ATOM   1868  N   ALA A 265     -24.886   6.555  53.492  1.00 57.43           N  
ANISOU 1868  N   ALA A 265     6452   9898   5469   -540   1128    128       N  
ATOM   1869  CA  ALA A 265     -23.502   6.202  53.181  1.00 49.15           C  
ANISOU 1869  CA  ALA A 265     5498   8802   4376   -576   1047    105       C  
ATOM   1870  CB  ALA A 265     -23.226   6.407  51.697  1.00 47.74           C  
ANISOU 1870  CB  ALA A 265     5307   8590   4242   -537    960    102       C  
ATOM   1871  C   ALA A 265     -22.515   7.010  54.024  1.00 44.83           C  
ANISOU 1871  C   ALA A 265     5064   8217   3754   -565   1100     55       C  
ATOM   1872  O   ALA A 265     -21.429   6.534  54.362  1.00 44.87           O  
ANISOU 1872  O   ALA A 265     5152   8193   3705   -617   1061     39       O  
ATOM   1873  N   LEU A 266     -22.906   8.232  54.372  1.00 45.88           N  
ANISOU 1873  N   LEU A 266     5199   8349   3884   -496   1189     30       N  
ATOM   1874  CA  LEU A 266     -22.039   9.134  55.122  1.00 44.71           C  
ANISOU 1874  CA  LEU A 266     5156   8163   3669   -476   1240    -19       C  
ATOM   1875  CB  LEU A 266     -22.455  10.580  54.852  1.00 42.30           C  
ANISOU 1875  CB  LEU A 266     4839   7846   3386   -381   1303    -45       C  
ATOM   1876  CG  LEU A 266     -21.813  11.142  53.585  1.00 45.58           C  
ANISOU 1876  CG  LEU A 266     5277   8214   3827   -336   1234    -65       C  
ATOM   1877  CD1 LEU A 266     -22.211  12.587  53.388  1.00 52.58           C  
ANISOU 1877  CD1 LEU A 266     6157   9089   4733   -243   1298    -92       C  
ATOM   1878  CD2 LEU A 266     -20.308  11.021  53.701  1.00 42.54           C  
ANISOU 1878  CD2 LEU A 266     5003   7775   3385   -372   1183    -97       C  
ATOM   1879  C   LEU A 266     -22.007   8.885  56.630  1.00 46.17           C  
ANISOU 1879  C   LEU A 266     5387   8365   3790   -520   1313    -23       C  
ATOM   1880  O   LEU A 266     -21.120   9.389  57.319  1.00 48.22           O  
ANISOU 1880  O   LEU A 266     5747   8588   3986   -520   1339    -62       O  
ATOM   1881  N   ARG A 267     -22.966   8.125  57.151  1.00 51.78           N  
ANISOU 1881  N   ARG A 267     6027   9129   4516   -556   1347     17       N  
ATOM   1882  CA  ARG A 267     -22.998   7.850  58.586  1.00 51.32           C  
ANISOU 1882  CA  ARG A 267     6013   9089   4397   -599   1420     17       C  
ATOM   1883  CB  ARG A 267     -24.223   7.011  58.953  1.00 58.02           C  
ANISOU 1883  CB  ARG A 267     6764  10001   5282   -633   1455     68       C  
ATOM   1884  CG  ARG A 267     -25.514   7.806  59.026  1.00 69.92           C  
ANISOU 1884  CG  ARG A 267     8186  11545   6837   -565   1548     80       C  
ATOM   1885  CD  ARG A 267     -26.147   7.668  60.400  1.00 80.50           C  
ANISOU 1885  CD  ARG A 267     9525  12921   8140   -585   1655     93       C  
ATOM   1886  NE  ARG A 267     -26.487   6.282  60.718  1.00 88.48           N  
ANISOU 1886  NE  ARG A 267    10492  13968   9157   -667   1629    139       N  
ATOM   1887  CZ  ARG A 267     -27.344   5.918  61.667  1.00 92.47           C  
ANISOU 1887  CZ  ARG A 267    10957  14518   9658   -690   1712    168       C  
ATOM   1888  NH1 ARG A 267     -27.949   6.840  62.408  1.00 96.83           N  
ANISOU 1888  NH1 ARG A 267    11509  15084  10197   -636   1829    156       N  
ATOM   1889  NH2 ARG A 267     -27.591   4.632  61.883  1.00 91.72           N  
ANISOU 1889  NH2 ARG A 267    10825  14452   9570   -767   1679    211       N  
ATOM   1890  C   ARG A 267     -21.727   7.147  59.052  1.00 48.70           C  
ANISOU 1890  C   ARG A 267     5782   8723   3998   -670   1363      1       C  
ATOM   1891  O   ARG A 267     -21.427   6.036  58.620  1.00 43.04           O  
ANISOU 1891  O   ARG A 267     5051   8009   3293   -731   1277     25       O  
ATOM   1892  N   GLY A 268     -20.985   7.818  59.930  1.00 49.43           N  
ANISOU 1892  N   GLY A 268     5978   8783   4022   -661   1410    -42       N  
ATOM   1893  CA  GLY A 268     -19.718   7.317  60.434  1.00 45.52           C  
ANISOU 1893  CA  GLY A 268     5590   8218   3486   -712   1347    -62       C  
ATOM   1894  C   GLY A 268     -18.570   7.397  59.440  1.00 47.03           C  
ANISOU 1894  C   GLY A 268     5825   8363   3679   -712   1253    -85       C  
ATOM   1895  O   GLY A 268     -17.466   6.936  59.724  1.00 51.73           O  
ANISOU 1895  O   GLY A 268     6504   8895   4257   -752   1188   -100       O  
ATOM   1896  N   ALA A 269     -18.820   7.969  58.267  1.00 43.28           N  
ANISOU 1896  N   ALA A 269     5297   7904   3245   -660   1237    -87       N  
ATOM   1897  CA  ALA A 269     -17.772   8.062  57.245  1.00 40.25           C  
ANISOU 1897  CA  ALA A 269     4953   7469   2873   -653   1147   -106       C  
ATOM   1898  CB  ALA A 269     -18.364   8.512  55.912  1.00 40.20           C  
ANISOU 1898  CB  ALA A 269     4866   7466   2940   -591   1121    -94       C  
ATOM   1899  C   ALA A 269     -16.649   9.004  57.671  1.00 43.44           C  
ANISOU 1899  C   ALA A 269     5469   7798   3240   -625   1156   -157       C  
ATOM   1900  O   ALA A 269     -16.867   9.939  58.447  1.00 45.18           O  
ANISOU 1900  O   ALA A 269     5723   7994   3449   -578   1233   -179       O  
ATOM   1901  N   ASP A 270     -15.455   8.751  57.143  1.00 40.46           N  
ANISOU 1901  N   ASP A 270     5149   7361   2863   -646   1069   -172       N  
ATOM   1902  CA  ASP A 270     -14.279   9.561  57.448  1.00 41.81           C  
ANISOU 1902  CA  ASP A 270     5425   7435   3027   -617   1056   -215       C  
ATOM   1903  CB  ASP A 270     -13.029   8.683  57.521  1.00 40.91           C  
ANISOU 1903  CB  ASP A 270     5375   7257   2911   -676    964   -218       C  
ATOM   1904  CG  ASP A 270     -13.130   7.616  58.590  1.00 49.11           C  
ANISOU 1904  CG  ASP A 270     6426   8303   3931   -742    959   -198       C  
ATOM   1905  OD1 ASP A 270     -13.046   7.972  59.786  1.00 48.13           O  
ANISOU 1905  OD1 ASP A 270     6360   8146   3784   -734   1009   -213       O  
ATOM   1906  OD2 ASP A 270     -13.276   6.426  58.237  1.00 50.10           O  
ANISOU 1906  OD2 ASP A 270     6508   8465   4064   -801    905   -166       O  
ATOM   1907  C   ASP A 270     -14.061  10.666  56.423  1.00 36.67           C  
ANISOU 1907  C   ASP A 270     4772   6767   2394   -548   1056   -240       C  
ATOM   1908  O   ASP A 270     -13.661  11.782  56.767  1.00 38.38           O  
ANISOU 1908  O   ASP A 270     5049   6928   2606   -497   1093   -274       O  
ATOM   1909  N   VAL A 271     -14.310  10.346  55.158  1.00 43.02           N  
ANISOU 1909  N   VAL A 271     5509   7617   3218   -547   1012   -221       N  
ATOM   1910  CA  VAL A 271     -14.011  11.272  54.076  1.00 40.26           C  
ANISOU 1910  CA  VAL A 271     5162   7234   2900   -481    994   -240       C  
ATOM   1911  CB  VAL A 271     -12.784  10.800  53.255  1.00 34.52           C  
ANISOU 1911  CB  VAL A 271     4481   6458   2179   -510    897   -246       C  
ATOM   1912  CG1 VAL A 271     -12.409  11.833  52.202  1.00 32.29           C  
ANISOU 1912  CG1 VAL A 271     4210   6131   1928   -440    884   -268       C  
ATOM   1913  CG2 VAL A 271     -11.597  10.535  54.163  1.00 33.86           C  
ANISOU 1913  CG2 VAL A 271     4493   6293   2079   -552    867   -266       C  
ATOM   1914  C   VAL A 271     -15.193  11.448  53.129  1.00 39.49           C  
ANISOU 1914  C   VAL A 271     4963   7174   2869   -430   1000   -212       C  
ATOM   1915  O   VAL A 271     -15.778  10.470  52.667  1.00 42.39           O  
ANISOU 1915  O   VAL A 271     5260   7577   3269   -461    956   -173       O  
ATOM   1916  N   PHE A 272     -15.538  12.703  52.856  1.00 37.88           N  
ANISOU 1916  N   PHE A 272     4752   6958   2683   -351   1051   -233       N  
ATOM   1917  CA  PHE A 272     -16.503  13.045  51.817  1.00 34.69           C  
ANISOU 1917  CA  PHE A 272     4261   6576   2343   -292   1048   -213       C  
ATOM   1918  CB  PHE A 272     -17.568  13.987  52.363  1.00 39.35           C  
ANISOU 1918  CB  PHE A 272     4813   7198   2942   -233   1148   -219       C  
ATOM   1919  CG  PHE A 272     -18.498  14.521  51.317  1.00 40.74           C  
ANISOU 1919  CG  PHE A 272     4907   7388   3183   -164   1148   -204       C  
ATOM   1920  CD1 PHE A 272     -19.512  13.729  50.807  1.00 38.25           C  
ANISOU 1920  CD1 PHE A 272     4493   7121   2920   -177   1121   -160       C  
ATOM   1921  CE1 PHE A 272     -20.375  14.220  49.849  1.00 40.95           C  
ANISOU 1921  CE1 PHE A 272     4760   7474   3324   -114   1117   -146       C  
ATOM   1922  CZ  PHE A 272     -20.231  15.514  49.390  1.00 39.82           C  
ANISOU 1922  CZ  PHE A 272     4644   7297   3191    -36   1144   -177       C  
ATOM   1923  CE2 PHE A 272     -19.227  16.315  49.892  1.00 39.31           C  
ANISOU 1923  CE2 PHE A 272     4678   7186   3074    -23   1173   -221       C  
ATOM   1924  CD2 PHE A 272     -18.365  15.818  50.846  1.00 37.72           C  
ANISOU 1924  CD2 PHE A 272     4548   6971   2812    -87   1174   -234       C  
ATOM   1925  C   PHE A 272     -15.802  13.695  50.631  1.00 36.40           C  
ANISOU 1925  C   PHE A 272     4506   6739   2583   -245    998   -232       C  
ATOM   1926  O   PHE A 272     -15.203  14.758  50.764  1.00 34.57           O  
ANISOU 1926  O   PHE A 272     4338   6466   2332   -203   1030   -270       O  
ATOM   1927  N   VAL A 273     -15.872  13.051  49.474  1.00 36.16           N  
ANISOU 1927  N   VAL A 273     4432   6710   2596   -251    920   -205       N  
ATOM   1928  CA  VAL A 273     -15.324  13.624  48.256  1.00 33.36           C  
ANISOU 1928  CA  VAL A 273     4099   6308   2269   -203    874   -218       C  
ATOM   1929  CB  VAL A 273     -14.498  12.595  47.463  1.00 35.75           C  
ANISOU 1929  CB  VAL A 273     4421   6586   2577   -253    773   -203       C  
ATOM   1930  CG1 VAL A 273     -13.969  13.209  46.171  1.00 35.74           C  
ANISOU 1930  CG1 VAL A 273     4442   6535   2604   -199    730   -215       C  
ATOM   1931  CG2 VAL A 273     -13.346  12.084  48.321  1.00 36.46           C  
ANISOU 1931  CG2 VAL A 273     4592   6651   2611   -320    759   -220       C  
ATOM   1932  C   VAL A 273     -16.472  14.147  47.405  1.00 36.07           C  
ANISOU 1932  C   VAL A 273     4360   6674   2670   -135    886   -201       C  
ATOM   1933  O   VAL A 273     -17.192  13.376  46.779  1.00 36.91           O  
ANISOU 1933  O   VAL A 273     4393   6813   2817   -148    842   -164       O  
ATOM   1934  N   GLY A 274     -16.644  15.462  47.401  1.00 33.41           N  
ANISOU 1934  N   GLY A 274     4037   6320   2337    -63    946   -229       N  
ATOM   1935  CA  GLY A 274     -17.774  16.072  46.728  1.00 36.21           C  
ANISOU 1935  CA  GLY A 274     4316   6698   2745      6    967   -216       C  
ATOM   1936  C   GLY A 274     -17.442  16.560  45.332  1.00 37.91           C  
ANISOU 1936  C   GLY A 274     4540   6870   2995     58    913   -221       C  
ATOM   1937  O   GLY A 274     -16.707  17.530  45.162  1.00 38.29           O  
ANISOU 1937  O   GLY A 274     4652   6868   3026     99    928   -255       O  
ATOM   1938  N   LEU A 275     -17.996  15.883  44.334  1.00 36.88           N  
ANISOU 1938  N   LEU A 275     4346   6757   2911     57    848   -187       N  
ATOM   1939  CA  LEU A 275     -17.864  16.301  42.947  1.00 37.86           C  
ANISOU 1939  CA  LEU A 275     4471   6844   3071    110    796   -187       C  
ATOM   1940  CB  LEU A 275     -17.111  15.248  42.132  1.00 35.98           C  
ANISOU 1940  CB  LEU A 275     4255   6582   2833     63    698   -169       C  
ATOM   1941  CG  LEU A 275     -15.767  14.781  42.707  1.00 42.04           C  
ANISOU 1941  CG  LEU A 275     5108   7318   3547      0    680   -187       C  
ATOM   1942  CD1 LEU A 275     -15.402  13.385  42.214  1.00 38.36           C  
ANISOU 1942  CD1 LEU A 275     4636   6854   3084    -64    591   -158       C  
ATOM   1943  CD2 LEU A 275     -14.661  15.768  42.367  1.00 45.15           C  
ANISOU 1943  CD2 LEU A 275     5586   7646   3922     39    687   -224       C  
ATOM   1944  C   LEU A 275     -19.268  16.525  42.393  1.00 42.06           C  
ANISOU 1944  C   LEU A 275     4906   7413   3662    161    804   -162       C  
ATOM   1945  O   LEU A 275     -19.610  16.038  41.316  1.00 43.46           O  
ANISOU 1945  O   LEU A 275     5042   7590   3880    169    735   -136       O  
ATOM   1946  N   SER A 276     -20.080  17.261  43.147  1.00 47.92           N  
ANISOU 1946  N   SER A 276     5614   8185   4408    197    890   -171       N  
ATOM   1947  CA  SER A 276     -21.505  17.387  42.849  1.00 49.44           C  
ANISOU 1947  CA  SER A 276     5705   8420   4658    237    907   -145       C  
ATOM   1948  CB  SER A 276     -22.329  16.683  43.929  1.00 50.11           C  
ANISOU 1948  CB  SER A 276     5729   8567   4744    189    952   -121       C  
ATOM   1949  OG  SER A 276     -21.990  17.165  45.219  1.00 51.06           O  
ANISOU 1949  OG  SER A 276     5899   8690   4811    179   1036   -150       O  
ATOM   1950  C   SER A 276     -21.955  18.841  42.729  1.00 43.59           C  
ANISOU 1950  C   SER A 276     4960   7667   3935    326    971   -170       C  
ATOM   1951  O   SER A 276     -21.498  19.568  41.848  1.00 46.77           O  
ANISOU 1951  O   SER A 276     5403   8023   4345    377    945   -189       O  
ATOM   1952  N   VAL A 277     -22.853  19.256  43.619  1.00 47.24           N  
ANISOU 1952  N   VAL A 277     5376   8170   4404    345   1054   -171       N  
ATOM   1953  CA  VAL A 277     -23.410  20.606  43.579  1.00 50.02           C  
ANISOU 1953  CA  VAL A 277     5716   8516   4775    430   1120   -193       C  
ATOM   1954  CB  VAL A 277     -24.834  20.607  43.000  1.00 51.83           C  
ANISOU 1954  CB  VAL A 277     5833   8783   5077    472   1116   -162       C  
ATOM   1955  CG1 VAL A 277     -24.803  20.310  41.508  1.00 58.28           C  
ANISOU 1955  CG1 VAL A 277     6632   9575   5937    490   1017   -143       C  
ATOM   1956  CG2 VAL A 277     -25.713  19.611  43.748  1.00 46.53           C  
ANISOU 1956  CG2 VAL A 277     5082   8175   4423    418   1136   -126       C  
ATOM   1957  C   VAL A 277     -23.452  21.257  44.958  1.00 49.88           C  
ANISOU 1957  C   VAL A 277     5726   8512   4714    436   1224   -220       C  
ATOM   1958  O   VAL A 277     -23.432  20.574  45.981  1.00 46.54           O  
ANISOU 1958  O   VAL A 277     5305   8119   4259    377   1253   -211       O  
ATOM   1959  N   ALA A 278     -23.520  22.584  44.976  1.00 56.61           N  
ANISOU 1959  N   ALA A 278     6603   9341   5565    510   1280   -251       N  
ATOM   1960  CA  ALA A 278     -23.575  23.336  46.224  1.00 57.23           C  
ANISOU 1960  CA  ALA A 278     6715   9428   5602    526   1380   -279       C  
ATOM   1961  CB  ALA A 278     -23.720  24.821  45.939  1.00 59.33           C  
ANISOU 1961  CB  ALA A 278     7000   9663   5878    617   1426   -311       C  
ATOM   1962  C   ALA A 278     -24.719  22.853  47.103  1.00 60.33           C  
ANISOU 1962  C   ALA A 278     7027   9885   6010    506   1440   -253       C  
ATOM   1963  O   ALA A 278     -25.811  22.574  46.609  1.00 62.30           O  
ANISOU 1963  O   ALA A 278     7179  10172   6322    524   1429   -220       O  
ATOM   1964  N   GLY A 279     -24.456  22.732  48.402  1.00 60.96           N  
ANISOU 1964  N   GLY A 279     7149   9979   6035    468   1502   -266       N  
ATOM   1965  CA  GLY A 279     -25.480  22.341  49.353  1.00 56.80           C  
ANISOU 1965  CA  GLY A 279     6556   9510   5514    450   1571   -243       C  
ATOM   1966  C   GLY A 279     -25.725  20.845  49.444  1.00 55.43           C  
ANISOU 1966  C   GLY A 279     6330   9376   5353    369   1524   -200       C  
ATOM   1967  O   GLY A 279     -26.566  20.398  50.227  1.00 53.06           O  
ANISOU 1967  O   GLY A 279     5972   9127   5061    347   1579   -176       O  
ATOM   1968  N   ALA A 280     -24.990  20.068  48.653  1.00 52.12           N  
ANISOU 1968  N   ALA A 280     5932   8933   4936    326   1426   -189       N  
ATOM   1969  CA  ALA A 280     -25.146  18.615  48.643  1.00 51.37           C  
ANISOU 1969  CA  ALA A 280     5793   8872   4853    248   1370   -148       C  
ATOM   1970  CB  ALA A 280     -24.348  17.998  47.508  1.00 50.11           C  
ANISOU 1970  CB  ALA A 280     5659   8677   4703    221   1257   -141       C  
ATOM   1971  C   ALA A 280     -24.723  18.004  49.970  1.00 54.91           C  
ANISOU 1971  C   ALA A 280     6289   9336   5239    178   1410   -151       C  
ATOM   1972  O   ALA A 280     -25.108  16.882  50.291  1.00 53.46           O  
ANISOU 1972  O   ALA A 280     6058   9191   5062    116   1394   -116       O  
ATOM   1973  N   LEU A 281     -23.913  18.737  50.727  1.00 56.07           N  
ANISOU 1973  N   LEU A 281     6532   9450   5323    188   1459   -193       N  
ATOM   1974  CA  LEU A 281     -23.533  18.314  52.067  1.00 59.50           C  
ANISOU 1974  CA  LEU A 281     7019   9895   5692    130   1506   -201       C  
ATOM   1975  CB  LEU A 281     -22.017  18.399  52.263  1.00 53.97           C  
ANISOU 1975  CB  LEU A 281     6440   9139   4929    100   1469   -236       C  
ATOM   1976  CG  LEU A 281     -21.464  17.712  53.516  1.00 54.39           C  
ANISOU 1976  CG  LEU A 281     6553   9198   4915     26   1490   -241       C  
ATOM   1977  CD1 LEU A 281     -21.661  16.199  53.460  1.00 47.34           C  
ANISOU 1977  CD1 LEU A 281     5611   8340   4035    -53   1433   -197       C  
ATOM   1978  CD2 LEU A 281     -20.002  18.056  53.721  1.00 54.60           C  
ANISOU 1978  CD2 LEU A 281     6698   9162   4884     11   1463   -281       C  
ATOM   1979  C   LEU A 281     -24.260  19.177  53.093  1.00 65.68           C  
ANISOU 1979  C   LEU A 281     7796  10702   6459    176   1623   -215       C  
ATOM   1980  O   LEU A 281     -24.151  20.403  53.079  1.00 68.09           O  
ANISOU 1980  O   LEU A 281     8138  10979   6756    243   1667   -250       O  
ATOM   1981  N   THR A 282     -25.015  18.527  53.969  1.00 68.34           N  
ANISOU 1981  N   THR A 282     8085  11089   6791    139   1675   -188       N  
ATOM   1982  CA  THR A 282     -25.810  19.216  54.977  1.00 73.72           C  
ANISOU 1982  CA  THR A 282     8753  11799   7460    178   1791   -196       C  
ATOM   1983  CB  THR A 282     -27.277  18.748  54.948  1.00 66.51           C  
ANISOU 1983  CB  THR A 282     7711  10948   6612    183   1826   -150       C  
ATOM   1984  OG1 THR A 282     -27.341  17.361  55.295  1.00 65.05           O  
ANISOU 1984  OG1 THR A 282     7500  10796   6422     97   1794   -113       O  
ATOM   1985  CG2 THR A 282     -27.881  18.958  53.571  1.00 64.65           C  
ANISOU 1985  CG2 THR A 282     7390  10714   6460    231   1770   -132       C  
ATOM   1986  C   THR A 282     -25.241  18.976  56.370  1.00 78.23           C  
ANISOU 1986  C   THR A 282     9409  12366   7947    128   1842   -213       C  
ATOM   1987  O   THR A 282     -24.506  18.009  56.580  1.00 76.72           O  
ANISOU 1987  O   THR A 282     9260  12168   7723     53   1787   -206       O  
ATOM   1988  N   PRO A 283     -25.570  19.864  57.325  1.00 80.08           N  
ANISOU 1988  N   PRO A 283     9674  12605   8149    172   1946   -237       N  
ATOM   1989  CA  PRO A 283     -25.191  19.664  58.727  1.00 77.48           C  
ANISOU 1989  CA  PRO A 283     9424  12274   7742    130   2004   -251       C  
ATOM   1990  CB  PRO A 283     -25.974  20.759  59.449  1.00 81.64           C  
ANISOU 1990  CB  PRO A 283     9955  12783   8280    199   2108   -265       C  
ATOM   1991  CG  PRO A 283     -26.018  21.869  58.455  1.00 81.75           C  
ANISOU 1991  CG  PRO A 283     9949  12784   8327    280   2100   -289       C  
ATOM   1992  CD  PRO A 283     -26.150  21.203  57.105  1.00 79.38           C  
ANISOU 1992  CD  PRO A 283     9565  12510   8086    267   2008   -259       C  
ATOM   1993  C   PRO A 283     -25.560  18.281  59.266  1.00 71.34           C  
ANISOU 1993  C   PRO A 283     8603  11544   6957     49   1999   -208       C  
ATOM   1994  O   PRO A 283     -24.786  17.720  60.038  1.00 71.10           O  
ANISOU 1994  O   PRO A 283     8660  11476   6881    -12   1977   -215       O  
ATOM   1995  N   GLU A 284     -26.705  17.738  58.856  1.00 67.44           N  
ANISOU 1995  N   GLU A 284     7989  11101   6533     48   2003   -163       N  
ATOM   1996  CA  GLU A 284     -27.133  16.417  59.318  1.00 69.65           C  
ANISOU 1996  CA  GLU A 284     8221  11427   6817    -28   1998   -119       C  
ATOM   1997  CB  GLU A 284     -28.546  16.107  58.832  1.00 79.47           C  
ANISOU 1997  CB  GLU A 284     9322  12725   8148    -10   2016    -72       C  
ATOM   1998  CG  GLU A 284     -29.627  16.890  59.546  1.00 91.66           C  
ANISOU 1998  CG  GLU A 284    10823  14301   9704     50   2141    -71       C  
ATOM   1999  CD  GLU A 284     -30.994  16.260  59.375  1.00101.53           C  
ANISOU 1999  CD  GLU A 284    11935  15611  11033     43   2164    -17       C  
ATOM   2000  OE1 GLU A 284     -31.055  15.022  59.215  1.00101.88           O  
ANISOU 2000  OE1 GLU A 284    11937  15676  11095    -29   2105     21       O  
ATOM   2001  OE2 GLU A 284     -32.004  16.996  59.408  1.00107.99           O  
ANISOU 2001  OE2 GLU A 284    12684  16452  11896    109   2240    -12       O  
ATOM   2002  C   GLU A 284     -26.196  15.298  58.877  1.00 66.00           C  
ANISOU 2002  C   GLU A 284     7791  10946   6341   -107   1885   -108       C  
ATOM   2003  O   GLU A 284     -25.822  14.440  59.675  1.00 64.48           O  
ANISOU 2003  O   GLU A 284     7640  10761   6099   -179   1883    -99       O  
ATOM   2004  N   MET A 285     -25.839  15.295  57.598  1.00 58.76           N  
ANISOU 2004  N   MET A 285     6854  10004   5468    -94   1792   -108       N  
ATOM   2005  CA  MET A 285     -24.849  14.356  57.097  1.00 56.20           C  
ANISOU 2005  CA  MET A 285     6569   9655   5130   -160   1684   -103       C  
ATOM   2006  CB  MET A 285     -24.672  14.514  55.587  1.00 54.30           C  
ANISOU 2006  CB  MET A 285     6294   9390   4947   -128   1594   -101       C  
ATOM   2007  CG  MET A 285     -25.737  13.793  54.777  1.00 56.26           C  
ANISOU 2007  CG  MET A 285     6417   9681   5277   -134   1555    -51       C  
ATOM   2008  SD  MET A 285     -25.587  14.072  53.006  1.00 70.31           S  
ANISOU 2008  SD  MET A 285     8163  11428   7122    -88   1454    -51       S  
ATOM   2009  CE  MET A 285     -26.128  15.764  52.908  1.00 46.70           C  
ANISOU 2009  CE  MET A 285     5165   8428   4152     22   1537    -82       C  
ATOM   2010  C   MET A 285     -23.534  14.582  57.829  1.00 52.46           C  
ANISOU 2010  C   MET A 285     6228   9133   4571   -186   1682   -145       C  
ATOM   2011  O   MET A 285     -22.863  13.636  58.238  1.00 51.74           O  
ANISOU 2011  O   MET A 285     6184   9037   4440   -261   1639   -139       O  
ATOM   2012  N   LEU A 286     -23.193  15.850  58.019  1.00 52.20           N  
ANISOU 2012  N   LEU A 286     6257   9064   4511   -123   1730   -189       N  
ATOM   2013  CA  LEU A 286     -21.978  16.227  58.723  1.00 59.19           C  
ANISOU 2013  CA  LEU A 286     7271   9898   5321   -139   1732   -232       C  
ATOM   2014  CB  LEU A 286     -21.752  17.731  58.613  1.00 67.95           C  
ANISOU 2014  CB  LEU A 286     8431  10953   6434    -55   1768   -274       C  
ATOM   2015  CG  LEU A 286     -20.487  18.122  57.856  1.00 70.74           C  
ANISOU 2015  CG  LEU A 286     8856  11243   6779    -47   1691   -306       C  
ATOM   2016  CD1 LEU A 286     -20.259  19.621  57.938  1.00 73.00           C  
ANISOU 2016  CD1 LEU A 286     9202  11469   7066     31   1733   -347       C  
ATOM   2017  CD2 LEU A 286     -19.302  17.358  58.419  1.00 71.54           C  
ANISOU 2017  CD2 LEU A 286     9051  11288   6842   -121   1628   -312       C  
ATOM   2018  C   LEU A 286     -22.027  15.813  60.193  1.00 61.33           C  
ANISOU 2018  C   LEU A 286     7598  10147   5558   -180   1779   -226       C  
ATOM   2019  O   LEU A 286     -21.021  15.363  60.750  1.00 61.04           O  
ANISOU 2019  O   LEU A 286     7654  10055   5484   -230   1734   -238       O  
ATOM   2020  N   LYS A 287     -23.198  15.989  60.804  1.00 59.11           N  
ANISOU 2020  N   LYS A 287     7260   9908   5292   -155   1870   -208       N  
ATOM   2021  CA  LYS A 287     -23.476  15.553  62.170  1.00 60.89           C  
ANISOU 2021  CA  LYS A 287     7523  10124   5488   -189   1927   -195       C  
ATOM   2022  CB  LYS A 287     -24.990  15.638  62.436  1.00 62.86           C  
ANISOU 2022  CB  LYS A 287     7669  10442   5775   -158   2021   -164       C  
ATOM   2023  CG  LYS A 287     -25.550  14.569  63.369  1.00 75.54           C  
ANISOU 2023  CG  LYS A 287     9252  12080   7370   -219   2055   -126       C  
ATOM   2024  CD  LYS A 287     -26.562  15.090  64.370  1.00 79.00           C  
ANISOU 2024  CD  LYS A 287     9678  12525   7814   -178   2174   -119       C  
ATOM   2025  CE  LYS A 287     -26.876  14.044  65.423  1.00 84.52           C  
ANISOU 2025  CE  LYS A 287    10383  13238   8491   -242   2203    -86       C  
ATOM   2026  NZ  LYS A 287     -27.243  12.741  64.790  1.00 86.73           N  
ANISOU 2026  NZ  LYS A 287    10561  13589   8802   -309   2147    -40       N  
ATOM   2027  C   LYS A 287     -22.987  14.135  62.452  1.00 56.53           C  
ANISOU 2027  C   LYS A 287     6987   9578   4913   -283   1862   -170       C  
ATOM   2028  O   LYS A 287     -22.372  13.872  63.483  1.00 58.30           O  
ANISOU 2028  O   LYS A 287     7306   9750   5094   -316   1862   -180       O  
ATOM   2029  N   ASP A 288     -23.262  13.230  61.519  1.00 51.47           N  
ANISOU 2029  N   ASP A 288     6254   9001   4301   -323   1805   -138       N  
ATOM   2030  CA  ASP A 288     -23.034  11.801  61.726  1.00 52.42           C  
ANISOU 2030  CA  ASP A 288     6368   9142   4409   -413   1749   -106       C  
ATOM   2031  CB  ASP A 288     -24.239  11.021  61.185  1.00 45.06           C  
ANISOU 2031  CB  ASP A 288     5293   8308   3521   -435   1760    -54       C  
ATOM   2032  CG  ASP A 288     -25.449  11.097  62.108  1.00 66.24           C  
ANISOU 2032  CG  ASP A 288     7925  11025   6219   -419   1866    -30       C  
ATOM   2033  OD1 ASP A 288     -25.263  11.356  63.317  1.00 61.49           O  
ANISOU 2033  OD1 ASP A 288     7410  10373   5580   -416   1920    -47       O  
ATOM   2034  OD2 ASP A 288     -26.587  10.938  61.616  1.00 69.73           O  
ANISOU 2034  OD2 ASP A 288     8244  11529   6720   -402   1892      6       O  
ATOM   2035  C   ASP A 288     -21.748  11.221  61.123  1.00 52.96           C  
ANISOU 2035  C   ASP A 288     6494   9170   4459   -463   1634   -118       C  
ATOM   2036  O   ASP A 288     -21.536  10.012  61.191  1.00 49.32           O  
ANISOU 2036  O   ASP A 288     6025   8725   3990   -537   1579    -92       O  
ATOM   2037  N   MET A 289     -20.886  12.054  60.547  1.00 50.66           N  
ANISOU 2037  N   MET A 289     6260   8825   4164   -422   1598   -157       N  
ATOM   2038  CA  MET A 289     -19.577  11.557  60.121  1.00 48.32           C  
ANISOU 2038  CA  MET A 289     6031   8477   3852   -466   1495   -171       C  
ATOM   2039  CB  MET A 289     -18.882  12.534  59.161  1.00 44.78           C  
ANISOU 2039  CB  MET A 289     5613   7987   3414   -411   1460   -205       C  
ATOM   2040  CG  MET A 289     -19.653  12.805  57.882  1.00 44.83           C  
ANISOU 2040  CG  MET A 289     5515   8046   3473   -366   1453   -189       C  
ATOM   2041  SD  MET A 289     -18.730  13.778  56.674  1.00 47.52           S  
ANISOU 2041  SD  MET A 289     5898   8323   3836   -307   1394   -225       S  
ATOM   2042  CE  MET A 289     -17.374  12.666  56.285  1.00 38.95           C  
ANISOU 2042  CE  MET A 289     4870   7199   2729   -388   1277   -223       C  
ATOM   2043  C   MET A 289     -18.703  11.308  61.350  1.00 45.61           C  
ANISOU 2043  C   MET A 289     5803   8060   3467   -503   1486   -188       C  
ATOM   2044  O   MET A 289     -18.981  11.825  62.439  1.00 46.74           O  
ANISOU 2044  O   MET A 289     5989   8180   3588   -477   1561   -198       O  
ATOM   2045  N   ALA A 290     -17.655  10.508  61.172  1.00 46.67           N  
ANISOU 2045  N   ALA A 290     5985   8156   3591   -560   1393   -189       N  
ATOM   2046  CA  ALA A 290     -16.716  10.204  62.249  1.00 54.92           C  
ANISOU 2046  CA  ALA A 290     7136   9130   4602   -595   1370   -205       C  
ATOM   2047  CB  ALA A 290     -15.683   9.187  61.783  1.00 53.14           C  
ANISOU 2047  CB  ALA A 290     6936   8876   4380   -660   1259   -200       C  
ATOM   2048  C   ALA A 290     -16.026  11.467  62.746  1.00 51.94           C  
ANISOU 2048  C   ALA A 290     6854   8675   4206   -536   1398   -249       C  
ATOM   2049  O   ALA A 290     -16.084  12.511  62.093  1.00 51.18           O  
ANISOU 2049  O   ALA A 290     6748   8572   4127   -474   1418   -269       O  
ATOM   2050  N   LYS A 291     -15.379  11.372  63.903  1.00 48.30           N  
ANISOU 2050  N   LYS A 291     6484   8156   3711   -553   1397   -262       N  
ATOM   2051  CA  LYS A 291     -14.666  12.514  64.464  1.00 54.30           C  
ANISOU 2051  CA  LYS A 291     7339   8841   4450   -499   1417   -301       C  
ATOM   2052  CB  LYS A 291     -14.119  12.181  65.858  1.00 62.47           C  
ANISOU 2052  CB  LYS A 291     8462   9829   5444   -526   1416   -307       C  
ATOM   2053  CG  LYS A 291     -12.954  13.048  66.303  1.00 70.33           C  
ANISOU 2053  CG  LYS A 291     9562  10739   6422   -491   1391   -346       C  
ATOM   2054  CD  LYS A 291     -12.527  12.765  67.729  1.00 73.78           C  
ANISOU 2054  CD  LYS A 291    10078  11138   6816   -510   1395   -350       C  
ATOM   2055  CE  LYS A 291     -12.315  14.077  68.469  1.00 76.29           C  
ANISOU 2055  CE  LYS A 291    10469  11412   7105   -440   1445   -382       C  
ATOM   2056  NZ  LYS A 291     -11.211  14.866  67.836  1.00 76.68           N  
ANISOU 2056  NZ  LYS A 291    10560  11402   7172   -410   1388   -415       N  
ATOM   2057  C   LYS A 291     -13.547  12.937  63.512  1.00 44.42           C  
ANISOU 2057  C   LYS A 291     6120   7538   3220   -485   1341   -326       C  
ATOM   2058  O   LYS A 291     -13.002  12.107  62.787  1.00 43.54           O  
ANISOU 2058  O   LYS A 291     5989   7426   3127   -533   1259   -316       O  
ATOM   2059  N   ASP A 292     -13.240  14.234  63.509  1.00 46.63           N  
ANISOU 2059  N   ASP A 292     6447   7773   3497   -419   1371   -359       N  
ATOM   2060  CA  ASP A 292     -12.284  14.838  62.575  1.00 44.51           C  
ANISOU 2060  CA  ASP A 292     6205   7455   3251   -394   1314   -384       C  
ATOM   2061  CB  ASP A 292     -10.855  14.357  62.855  1.00 52.73           C  
ANISOU 2061  CB  ASP A 292     7323   8426   4287   -436   1227   -396       C  
ATOM   2062  CG  ASP A 292     -10.434  14.560  64.302  1.00 59.32           C  
ANISOU 2062  CG  ASP A 292     8242   9214   5082   -433   1248   -411       C  
ATOM   2063  OD1 ASP A 292     -10.850  15.569  64.913  1.00 60.39           O  
ANISOU 2063  OD1 ASP A 292     8405   9344   5196   -376   1320   -426       O  
ATOM   2064  OD2 ASP A 292      -9.670  13.712  64.818  1.00 57.45           O  
ANISOU 2064  OD2 ASP A 292     8044   8948   4837   -487   1188   -407       O  
ATOM   2065  C   ASP A 292     -12.632  14.540  61.117  1.00 46.15           C  
ANISOU 2065  C   ASP A 292     6325   7713   3497   -399   1280   -368       C  
ATOM   2066  O   ASP A 292     -11.794  14.031  60.378  1.00 35.47           O  
ANISOU 2066  O   ASP A 292     4978   6336   2162   -431   1197   -367       O  
ATOM   2067  N   PRO A 293     -13.863  14.867  60.694  1.00 45.90           N  
ANISOU 2067  N   PRO A 293     6211   7751   3479   -364   1343   -355       N  
ATOM   2068  CA  PRO A 293     -14.228  14.480  59.327  1.00 44.56           C  
ANISOU 2068  CA  PRO A 293     5953   7636   3342   -370   1305   -336       C  
ATOM   2069  CB  PRO A 293     -15.710  14.837  59.247  1.00 45.41           C  
ANISOU 2069  CB  PRO A 293     5970   7823   3462   -330   1390   -319       C  
ATOM   2070  CG  PRO A 293     -15.874  15.949  60.220  1.00 43.50           C  
ANISOU 2070  CG  PRO A 293     5784   7542   3200   -275   1471   -345       C  
ATOM   2071  CD  PRO A 293     -14.917  15.664  61.344  1.00 41.34           C  
ANISOU 2071  CD  PRO A 293     5615   7200   2891   -312   1447   -357       C  
ATOM   2072  C   PRO A 293     -13.420  15.238  58.282  1.00 43.12           C  
ANISOU 2072  C   PRO A 293     5795   7408   3180   -331   1261   -362       C  
ATOM   2073  O   PRO A 293     -13.081  16.408  58.479  1.00 39.27           O  
ANISOU 2073  O   PRO A 293     5362   6868   2689   -275   1293   -393       O  
ATOM   2074  N   ILE A 294     -13.108  14.558  57.186  1.00 38.04           N  
ANISOU 2074  N   ILE A 294     5113   6781   2558   -360   1187   -347       N  
ATOM   2075  CA  ILE A 294     -12.327  15.144  56.108  1.00 38.19           C  
ANISOU 2075  CA  ILE A 294     5154   6759   2599   -328   1140   -367       C  
ATOM   2076  CB  ILE A 294     -11.163  14.237  55.725  1.00 32.89           C  
ANISOU 2076  CB  ILE A 294     4520   6043   1935   -385   1042   -362       C  
ATOM   2077  CG1 ILE A 294     -10.309  13.952  56.965  1.00 38.47           C  
ANISOU 2077  CG1 ILE A 294     5311   6685   2620   -423   1027   -373       C  
ATOM   2078  CD1 ILE A 294      -9.330  12.816  56.785  1.00 35.04           C  
ANISOU 2078  CD1 ILE A 294     4901   6218   2196   -488    934   -361       C  
ATOM   2079  CG2 ILE A 294     -10.340  14.867  54.607  1.00 33.05           C  
ANISOU 2079  CG2 ILE A 294     4564   6017   1979   -349    998   -381       C  
ATOM   2080  C   ILE A 294     -13.217  15.404  54.900  1.00 38.81           C  
ANISOU 2080  C   ILE A 294     5138   6906   2700   -286   1153   -354       C  
ATOM   2081  O   ILE A 294     -13.773  14.479  54.306  1.00 37.08           O  
ANISOU 2081  O   ILE A 294     4844   6755   2490   -318   1123   -322       O  
ATOM   2082  N   ILE A 295     -13.337  16.675  54.542  1.00 37.33           N  
ANISOU 2082  N   ILE A 295     4958   6701   2523   -211   1194   -379       N  
ATOM   2083  CA  ILE A 295     -14.310  17.107  53.553  1.00 38.43           C  
ANISOU 2083  CA  ILE A 295     5010   6899   2693   -155   1217   -369       C  
ATOM   2084  CB  ILE A 295     -15.313  18.091  54.194  1.00 45.66           C  
ANISOU 2084  CB  ILE A 295     5901   7842   3604    -94   1319   -379       C  
ATOM   2085  CG1 ILE A 295     -15.997  17.446  55.400  1.00 49.15           C  
ANISOU 2085  CG1 ILE A 295     6327   8323   4025   -136   1368   -360       C  
ATOM   2086  CD1 ILE A 295     -16.777  18.423  56.214  1.00 61.36           C  
ANISOU 2086  CD1 ILE A 295     7875   9872   5569    -80   1466   -373       C  
ATOM   2087  CG2 ILE A 295     -16.347  18.553  53.188  1.00 40.30           C  
ANISOU 2087  CG2 ILE A 295     5133   7188   2990    -28   1328   -361       C  
ATOM   2088  C   ILE A 295     -13.662  17.776  52.340  1.00 38.01           C  
ANISOU 2088  C   ILE A 295     4975   6794   2672   -108   1169   -384       C  
ATOM   2089  O   ILE A 295     -13.112  18.869  52.454  1.00 41.32           O  
ANISOU 2089  O   ILE A 295     5455   7169   3076    -64   1197   -421       O  
ATOM   2090  N   PHE A 296     -13.720  17.115  51.182  1.00 37.60           N  
ANISOU 2090  N   PHE A 296     4874   6747   2665   -117   1097   -356       N  
ATOM   2091  CA  PHE A 296     -13.356  17.744  49.913  1.00 36.81           C  
ANISOU 2091  CA  PHE A 296     4776   6606   2602    -64   1057   -365       C  
ATOM   2092  CB  PHE A 296     -12.616  16.770  48.990  1.00 43.44           C  
ANISOU 2092  CB  PHE A 296     5621   7424   3459   -109    960   -346       C  
ATOM   2093  CG  PHE A 296     -11.270  16.351  49.498  1.00 46.04           C  
ANISOU 2093  CG  PHE A 296     6036   7711   3746   -168    925   -365       C  
ATOM   2094  CD1 PHE A 296     -10.137  17.090  49.191  1.00 49.69           C  
ANISOU 2094  CD1 PHE A 296     6571   8107   4201   -146    910   -397       C  
ATOM   2095  CE1 PHE A 296      -8.890  16.703  49.655  1.00 46.09           C  
ANISOU 2095  CE1 PHE A 296     6191   7603   3717   -199    872   -412       C  
ATOM   2096  CZ  PHE A 296      -8.767  15.566  50.435  1.00 41.54           C  
ANISOU 2096  CZ  PHE A 296     5620   7034   3129   -272    845   -393       C  
ATOM   2097  CE2 PHE A 296      -9.888  14.821  50.740  1.00 43.99           C  
ANISOU 2097  CE2 PHE A 296     5859   7428   3425   -299    867   -365       C  
ATOM   2098  CD2 PHE A 296     -11.131  15.212  50.273  1.00 42.85           C  
ANISOU 2098  CD2 PHE A 296     5637   7332   3312   -246    905   -349       C  
ATOM   2099  C   PHE A 296     -14.618  18.250  49.224  1.00 48.65           C  
ANISOU 2099  C   PHE A 296     6191   8139   4153      3   1085   -347       C  
ATOM   2100  O   PHE A 296     -15.415  17.463  48.714  1.00 52.86           O  
ANISOU 2100  O   PHE A 296     6646   8714   4723    -11   1054   -310       O  
ATOM   2101  N   ALA A 297     -14.814  19.563  49.226  1.00 46.61           N  
ANISOU 2101  N   ALA A 297     5948   7863   3899     75   1142   -374       N  
ATOM   2102  CA  ALA A 297     -15.981  20.144  48.578  1.00 41.96           C  
ANISOU 2102  CA  ALA A 297     5282   7302   3361    144   1170   -361       C  
ATOM   2103  CB  ALA A 297     -16.649  21.178  49.489  1.00 45.99           C  
ANISOU 2103  CB  ALA A 297     5792   7829   3855    193   1270   -383       C  
ATOM   2104  C   ALA A 297     -15.564  20.767  47.260  1.00 40.83           C  
ANISOU 2104  C   ALA A 297     5150   7112   3251    196   1124   -370       C  
ATOM   2105  O   ALA A 297     -15.275  21.962  47.197  1.00 44.22           O  
ANISOU 2105  O   ALA A 297     5623   7504   3675    254   1160   -401       O  
ATOM   2106  N   MET A 298     -15.533  19.943  46.212  1.00 40.81           N  
ANISOU 2106  N   MET A 298     5113   7111   3282    176   1045   -341       N  
ATOM   2107  CA  MET A 298     -14.952  20.326  44.922  1.00 43.71           C  
ANISOU 2107  CA  MET A 298     5504   7429   3675    214    990   -346       C  
ATOM   2108  CB  MET A 298     -14.250  19.137  44.268  1.00 45.12           C  
ANISOU 2108  CB  MET A 298     5693   7593   3856    155    899   -324       C  
ATOM   2109  CG  MET A 298     -13.424  18.317  45.194  1.00 53.62           C  
ANISOU 2109  CG  MET A 298     6819   8667   4888     75    887   -329       C  
ATOM   2110  SD  MET A 298     -11.903  19.145  45.611  1.00 63.53           S  
ANISOU 2110  SD  MET A 298     8188   9850   6100     76    901   -375       S  
ATOM   2111  CE  MET A 298     -10.890  17.695  45.849  1.00 66.37           C  
ANISOU 2111  CE  MET A 298     8584  10200   6434    -22    829   -362       C  
ATOM   2112  C   MET A 298     -15.950  20.862  43.914  1.00 45.81           C  
ANISOU 2112  C   MET A 298     5703   7707   3995    285    989   -332       C  
ATOM   2113  O   MET A 298     -15.564  21.203  42.791  1.00 47.86           O  
ANISOU 2113  O   MET A 298     5981   7927   4278    322    945   -335       O  
ATOM   2114  N   ALA A 299     -17.228  20.893  44.274  1.00 35.34           N  
ANISOU 2114  N   ALA A 299     4300   6436   2692    304   1035   -315       N  
ATOM   2115  CA  ALA A 299     -18.208  21.454  43.358  1.00 42.76           C  
ANISOU 2115  CA  ALA A 299     5174   7386   3685    375   1035   -303       C  
ATOM   2116  CB  ALA A 299     -19.599  21.365  43.933  1.00 40.90           C  
ANISOU 2116  CB  ALA A 299     4850   7214   3475    386   1089   -283       C  
ATOM   2117  C   ALA A 299     -17.826  22.901  43.081  1.00 48.13           C  
ANISOU 2117  C   ALA A 299     5907   8017   4361    449   1071   -340       C  
ATOM   2118  O   ALA A 299     -17.266  23.570  43.946  1.00 50.82           O  
ANISOU 2118  O   ALA A 299     6310   8337   4661    452   1125   -373       O  
ATOM   2119  N   ASN A 300     -18.172  23.432  41.938  1.00 59.01           N  
ANISOU 2119  N   ASN A 300     7265   9374   5781    507   1038   -335       N  
ATOM   2120  CA  ASN A 300     -17.866  24.821  41.668  1.00 68.53           C  
ANISOU 2120  CA  ASN A 300     8516  10536   6987    581   1074   -368       C  
ATOM   2121  CB  ASN A 300     -16.463  24.911  41.126  1.00 78.31           C  
ANISOU 2121  CB  ASN A 300     9848  11707   8199    570   1035   -389       C  
ATOM   2122  CG  ASN A 300     -16.381  24.411  39.723  1.00 89.29           C  
ANISOU 2122  CG  ASN A 300    11317  13070   9538    556   1089   -427       C  
ATOM   2123  OD1 ASN A 300     -16.766  25.125  38.810  1.00 90.19           O  
ANISOU 2123  OD1 ASN A 300    11489  13135   9644    602   1112   -458       O  
ATOM   2124  ND2 ASN A 300     -16.025  23.160  39.553  1.00 94.28           N  
ANISOU 2124  ND2 ASN A 300    11954  13732  10136    492   1109   -425       N  
ATOM   2125  C   ASN A 300     -18.869  25.349  40.668  1.00 67.08           C  
ANISOU 2125  C   ASN A 300     8271  10358   6858    655   1063   -355       C  
ATOM   2126  O   ASN A 300     -19.442  24.574  39.962  1.00 68.45           O  
ANISOU 2126  O   ASN A 300     8391  10548   7069    646   1001   -322       O  
ATOM   2127  N   PRO A 301     -19.079  26.645  40.570  1.00 66.45           N  
ANISOU 2127  N   PRO A 301     8203  10262   6785    728   1121   -381       N  
ATOM   2128  CA  PRO A 301     -18.465  27.728  41.357  1.00 66.24           C  
ANISOU 2128  CA  PRO A 301     8247  10202   6717    752   1188   -423       C  
ATOM   2129  CB  PRO A 301     -19.208  28.971  40.860  1.00 68.08           C  
ANISOU 2129  CB  PRO A 301     8456  10427   6984    845   1224   -435       C  
ATOM   2130  CG  PRO A 301     -20.540  28.457  40.454  1.00 67.54           C  
ANISOU 2130  CG  PRO A 301     8283  10413   6968    857   1209   -400       C  
ATOM   2131  CD  PRO A 301     -20.258  27.122  39.827  1.00 65.56           C  
ANISOU 2131  CD  PRO A 301     8016  10168   6726    796   1123   -367       C  
ATOM   2132  C   PRO A 301     -18.601  27.607  42.878  1.00 69.50           C  
ANISOU 2132  C   PRO A 301     8666  10650   7091    715   1257   -434       C  
ATOM   2133  O   PRO A 301     -17.686  28.018  43.590  1.00 70.26           O  
ANISOU 2133  O   PRO A 301     8841  10713   7141    700   1285   -465       O  
ATOM   2134  N   GLU A 302     -19.702  27.049  43.369  1.00 67.52           N  
ANISOU 2134  N   GLU A 302     8335  10462   6858    700   1283   -409       N  
ATOM   2135  CA  GLU A 302     -19.912  26.969  44.813  1.00 69.22           C  
ANISOU 2135  CA  GLU A 302     8556  10711   7036    670   1355   -418       C  
ATOM   2136  CB  GLU A 302     -21.322  27.452  45.170  1.00 76.50           C  
ANISOU 2136  CB  GLU A 302     9397  11681   7988    721   1425   -410       C  
ATOM   2137  CG  GLU A 302     -21.558  28.932  44.875  1.00 84.95           C  
ANISOU 2137  CG  GLU A 302    10482  12722   9072    812   1470   -439       C  
ATOM   2138  CD  GLU A 302     -20.894  29.860  45.885  1.00 92.19           C  
ANISOU 2138  CD  GLU A 302    11487  13609   9933    826   1538   -483       C  
ATOM   2139  OE1 GLU A 302     -20.278  29.362  46.852  1.00 94.56           O  
ANISOU 2139  OE1 GLU A 302    11835  13911  10183    765   1552   -491       O  
ATOM   2140  OE2 GLU A 302     -20.977  31.094  45.703  1.00 94.79           O  
ANISOU 2140  OE2 GLU A 302    11839  13910  10268    898   1575   -509       O  
ATOM   2141  C   GLU A 302     -19.682  25.564  45.369  1.00 58.11           C  
ANISOU 2141  C   GLU A 302     7140   9334   5607    578   1325   -394       C  
ATOM   2142  O   GLU A 302     -20.184  24.581  44.825  1.00 56.21           O  
ANISOU 2142  O   GLU A 302     6832   9124   5399    549   1272   -357       O  
ATOM   2143  N   PRO A 303     -18.909  25.473  46.463  1.00 53.63           N  
ANISOU 2143  N   PRO A 303     6641   8755   4981    533   1355   -416       N  
ATOM   2144  CA  PRO A 303     -18.609  24.218  47.161  1.00 51.77           C  
ANISOU 2144  CA  PRO A 303     6411   8545   4716    445   1333   -398       C  
ATOM   2145  CB  PRO A 303     -17.665  24.655  48.289  1.00 50.58           C  
ANISOU 2145  CB  PRO A 303     6356   8362   4499    424   1376   -436       C  
ATOM   2146  CG  PRO A 303     -17.139  25.976  47.869  1.00 54.84           C  
ANISOU 2146  CG  PRO A 303     6953   8846   5039    491   1391   -471       C  
ATOM   2147  CD  PRO A 303     -18.233  26.620  47.090  1.00 56.18           C  
ANISOU 2147  CD  PRO A 303     7049   9034   5262    566   1409   -461       C  
ATOM   2148  C   PRO A 303     -19.865  23.575  47.737  1.00 50.34           C  
ANISOU 2148  C   PRO A 303     6140   8433   4552    427   1371   -367       C  
ATOM   2149  O   PRO A 303     -20.846  24.284  47.964  1.00 57.79           O  
ANISOU 2149  O   PRO A 303     7037   9403   5517    483   1436   -368       O  
ATOM   2150  N   GLU A 304     -19.830  22.265  47.980  1.00 45.58           N  
ANISOU 2150  N   GLU A 304     5516   7861   3943    351   1332   -338       N  
ATOM   2151  CA  GLU A 304     -20.948  21.569  48.620  1.00 49.68           C  
ANISOU 2151  CA  GLU A 304     5954   8445   4476    324   1369   -306       C  
ATOM   2152  CB  GLU A 304     -20.613  20.091  48.839  1.00 45.91           C  
ANISOU 2152  CB  GLU A 304     5472   7988   3984    232   1312   -278       C  
ATOM   2153  CG  GLU A 304     -20.811  19.211  47.618  1.00 45.63           C  
ANISOU 2153  CG  GLU A 304     5379   7959   3999    214   1219   -242       C  
ATOM   2154  CD  GLU A 304     -19.625  19.233  46.675  1.00 44.41           C  
ANISOU 2154  CD  GLU A 304     5290   7746   3838    211   1141   -256       C  
ATOM   2155  OE1 GLU A 304     -18.679  20.010  46.923  1.00 39.73           O  
ANISOU 2155  OE1 GLU A 304     4783   7105   3206    228   1160   -295       O  
ATOM   2156  OE2 GLU A 304     -19.644  18.476  45.678  1.00 42.23           O  
ANISOU 2156  OE2 GLU A 304     4981   7470   3596    194   1060   -229       O  
ATOM   2157  C   GLU A 304     -21.314  22.222  49.952  1.00 52.09           C  
ANISOU 2157  C   GLU A 304     6279   8769   4744    341   1474   -327       C  
ATOM   2158  O   GLU A 304     -22.480  22.229  50.364  1.00 50.58           O  
ANISOU 2158  O   GLU A 304     6014   8627   4577    359   1532   -308       O  
ATOM   2159  N   ILE A 305     -20.302  22.766  50.617  1.00 52.99           N  
ANISOU 2159  N   ILE A 305     6494   8841   4800    336   1497   -366       N  
ATOM   2160  CA  ILE A 305     -20.488  23.535  51.839  1.00 53.82           C  
ANISOU 2160  CA  ILE A 305     6637   8950   4861    359   1594   -393       C  
ATOM   2161  CB  ILE A 305     -20.760  22.621  53.058  1.00 52.87           C  
ANISOU 2161  CB  ILE A 305     6511   8873   4703    293   1631   -376       C  
ATOM   2162  CG1 ILE A 305     -21.121  23.455  54.296  1.00 44.46           C  
ANISOU 2162  CG1 ILE A 305     5480   7817   3596    326   1739   -401       C  
ATOM   2163  CD1 ILE A 305     -21.587  22.638  55.483  1.00 52.65           C  
ANISOU 2163  CD1 ILE A 305     6503   8901   4600    271   1789   -382       C  
ATOM   2164  CG2 ILE A 305     -19.568  21.703  53.319  1.00 56.60           C  
ANISOU 2164  CG2 ILE A 305     7054   9320   5131    211   1568   -378       C  
ATOM   2165  C   ILE A 305     -19.234  24.378  52.055  1.00 56.29           C  
ANISOU 2165  C   ILE A 305     7064   9197   5126    373   1593   -439       C  
ATOM   2166  O   ILE A 305     -18.131  23.966  51.681  1.00 49.76           O  
ANISOU 2166  O   ILE A 305     6292   8331   4285    332   1523   -445       O  
ATOM   2167  N   THR A 306     -19.405  25.569  52.621  1.00 48.41           N  
ANISOU 2167  N   THR A 306     6100   8186   4108    432   1670   -471       N  
ATOM   2168  CA  THR A 306     -18.277  26.453  52.893  1.00 48.40           C  
ANISOU 2168  CA  THR A 306     6209   8106   4075    445   1668   -514       C  
ATOM   2169  CB  THR A 306     -18.739  27.914  53.084  1.00 57.82           C  
ANISOU 2169  CB  THR A 306     7419   9263   5287    524   1734   -540       C  
ATOM   2170  OG1 THR A 306     -19.425  28.044  54.335  1.00 56.58           O  
ANISOU 2170  OG1 THR A 306     7265   9117   5116    520   1812   -540       O  
ATOM   2171  CG2 THR A 306     -19.667  28.329  51.952  1.00 59.29           C  
ANISOU 2171  CG2 THR A 306     7512   9497   5518    599   1741   -527       C  
ATOM   2172  C   THR A 306     -17.534  25.971  54.133  1.00 46.48           C  
ANISOU 2172  C   THR A 306     6051   7821   3789    373   1668   -522       C  
ATOM   2173  O   THR A 306     -18.124  25.300  54.982  1.00 51.05           O  
ANISOU 2173  O   THR A 306     6604   8441   4352    337   1704   -502       O  
ATOM   2174  N   PRO A 307     -16.230  26.285  54.230  1.00 43.41           N  
ANISOU 2174  N   PRO A 307     5763   7350   3383    354   1626   -548       N  
ATOM   2175  CA  PRO A 307     -15.433  25.942  55.416  1.00 47.90           C  
ANISOU 2175  CA  PRO A 307     6421   7867   3910    295   1623   -558       C  
ATOM   2176  CB  PRO A 307     -14.112  26.663  55.164  1.00 47.28           C  
ANISOU 2176  CB  PRO A 307     6438   7698   3830    302   1580   -590       C  
ATOM   2177  CG  PRO A 307     -13.991  26.690  53.669  1.00 45.71           C  
ANISOU 2177  CG  PRO A 307     6188   7514   3665    328   1528   -584       C  
ATOM   2178  CD  PRO A 307     -15.396  26.833  53.141  1.00 43.06           C  
ANISOU 2178  CD  PRO A 307     5747   7257   3357    382   1572   -565       C  
ATOM   2179  C   PRO A 307     -16.065  26.416  56.727  1.00 49.13           C  
ANISOU 2179  C   PRO A 307     6604   8018   4045    309   1709   -566       C  
ATOM   2180  O   PRO A 307     -16.058  25.679  57.712  1.00 51.40           O  
ANISOU 2180  O   PRO A 307     6915   8312   4301    259   1720   -554       O  
ATOM   2181  N   ASP A 308     -16.605  27.630  56.730  1.00 55.65           N  
ANISOU 2181  N   ASP A 308     7428   8830   4888    376   1767   -588       N  
ATOM   2182  CA  ASP A 308     -17.227  28.190  57.929  1.00 57.34           C  
ANISOU 2182  CA  ASP A 308     7668   9035   5084    393   1853   -600       C  
ATOM   2183  CB  ASP A 308     -17.534  29.670  57.725  1.00 66.77           C  
ANISOU 2183  CB  ASP A 308     8870  10198   6303    464   1897   -632       C  
ATOM   2184  CG  ASP A 308     -16.313  30.541  57.903  1.00 73.74           C  
ANISOU 2184  CG  ASP A 308     9858  10988   7169    459   1870   -674       C  
ATOM   2185  OD1 ASP A 308     -15.224  29.988  58.161  1.00 76.65           O  
ANISOU 2185  OD1 ASP A 308    10297  11316   7510    405   1819   -676       O  
ATOM   2186  OD2 ASP A 308     -16.437  31.775  57.771  1.00 78.25           O  
ANISOU 2186  OD2 ASP A 308    10440  11532   7759    508   1897   -705       O  
ATOM   2187  C   ASP A 308     -18.496  27.447  58.316  1.00 55.56           C  
ANISOU 2187  C   ASP A 308     7354   8893   4863    385   1904   -565       C  
ATOM   2188  O   ASP A 308     -18.684  27.097  59.480  1.00 55.77           O  
ANISOU 2188  O   ASP A 308     7414   8919   4858    354   1946   -559       O  
ATOM   2189  N   LYS A 309     -19.367  27.209  57.340  1.00 51.38           N  
ANISOU 2189  N   LYS A 309     6713   8434   4374    414   1900   -540       N  
ATOM   2190  CA  LYS A 309     -20.592  26.466  57.601  1.00 58.83           C  
ANISOU 2190  CA  LYS A 309     7561   9463   5330    405   1945   -504       C  
ATOM   2191  CB  LYS A 309     -21.510  26.493  56.382  1.00 62.62           C  
ANISOU 2191  CB  LYS A 309     7920  10011   5861    455   1939   -482       C  
ATOM   2192  CG  LYS A 309     -22.196  27.830  56.192  1.00 67.42           C  
ANISOU 2192  CG  LYS A 309     8510  10606   6503    543   1997   -501       C  
ATOM   2193  CD  LYS A 309     -23.188  27.796  55.050  1.00 74.30           C  
ANISOU 2193  CD  LYS A 309     9257  11548   7426    595   1993   -475       C  
ATOM   2194  CE  LYS A 309     -24.226  28.896  55.208  1.00 82.04           C  
ANISOU 2194  CE  LYS A 309    10199  12530   8441    673   2072   -485       C  
ATOM   2195  NZ  LYS A 309     -23.596  30.238  55.351  1.00 85.21           N  
ANISOU 2195  NZ  LYS A 309    10696  12845   8836    714   2083   -530       N  
ATOM   2196  C   LYS A 309     -20.282  25.030  58.010  1.00 60.23           C  
ANISOU 2196  C   LYS A 309     7737   9668   5479    319   1906   -476       C  
ATOM   2197  O   LYS A 309     -21.036  24.415  58.764  1.00 58.82           O  
ANISOU 2197  O   LYS A 309     7521   9534   5292    293   1952   -452       O  
ATOM   2198  N   ALA A 310     -19.161  24.504  57.528  1.00 52.04           N  
ANISOU 2198  N   ALA A 310     6743   8601   4428    275   1820   -480       N  
ATOM   2199  CA  ALA A 310     -18.739  23.167  57.916  1.00 44.17           C  
ANISOU 2199  CA  ALA A 310     5757   7621   3407    190   1774   -457       C  
ATOM   2200  CB  ALA A 310     -17.634  22.663  56.992  1.00 46.94           C  
ANISOU 2200  CB  ALA A 310     6129   7947   3758    154   1673   -459       C  
ATOM   2201  C   ALA A 310     -18.276  23.139  59.371  1.00 48.54           C  
ANISOU 2201  C   ALA A 310     6409   8120   3914    159   1804   -469       C  
ATOM   2202  O   ALA A 310     -18.681  22.268  60.142  1.00 53.13           O  
ANISOU 2202  O   ALA A 310     6976   8735   4478    113   1825   -444       O  
ATOM   2203  N   ARG A 311     -17.437  24.099  59.748  1.00 46.54           N  
ANISOU 2203  N   ARG A 311     6259   7783   3641    186   1807   -505       N  
ATOM   2204  CA  ARG A 311     -16.849  24.100  61.084  1.00 48.71           C  
ANISOU 2204  CA  ARG A 311     6638   8001   3869    163   1824   -516       C  
ATOM   2205  CB  ARG A 311     -15.600  24.983  61.128  1.00 54.23           C  
ANISOU 2205  CB  ARG A 311     7445   8607   4552    185   1789   -552       C  
ATOM   2206  CG  ARG A 311     -14.295  24.215  60.866  1.00 52.31           C  
ANISOU 2206  CG  ARG A 311     7246   8329   4299    131   1689   -550       C  
ATOM   2207  CD  ARG A 311     -13.102  25.155  60.836  1.00 50.87           C  
ANISOU 2207  CD  ARG A 311     7159   8062   4110    162   1655   -583       C  
ATOM   2208  NE  ARG A 311     -13.390  26.337  60.032  1.00 56.74           N  
ANISOU 2208  NE  ARG A 311     7885   8789   4883    220   1687   -606       N  
ATOM   2209  CZ  ARG A 311     -12.772  26.637  58.893  1.00 65.40           C  
ANISOU 2209  CZ  ARG A 311     8975   9862   6010    229   1634   -617       C  
ATOM   2210  NH1 ARG A 311     -11.813  25.846  58.423  1.00 58.52           N  
ANISOU 2210  NH1 ARG A 311     8115   8977   5142    184   1549   -608       N  
ATOM   2211  NH2 ARG A 311     -13.110  27.733  58.225  1.00 68.27           N  
ANISOU 2211  NH2 ARG A 311     9319  10217   6404    282   1665   -639       N  
ATOM   2212  C   ARG A 311     -17.860  24.555  62.130  1.00 57.83           C  
ANISOU 2212  C   ARG A 311     7793   9171   5009    194   1927   -515       C  
ATOM   2213  O   ARG A 311     -17.737  24.227  63.313  1.00 52.10           O  
ANISOU 2213  O   ARG A 311     7126   8427   4242    172   1951   -509       O  
ATOM   2214  N   ALA A 312     -18.864  25.304  61.687  1.00 60.22           N  
ANISOU 2214  N   ALA A 312     8027   9507   5347    250   1986   -519       N  
ATOM   2215  CA  ALA A 312     -19.957  25.698  62.566  1.00 57.01           C  
ANISOU 2215  CA  ALA A 312     7603   9123   4937    279   2087   -516       C  
ATOM   2216  CB  ALA A 312     -20.867  26.692  61.870  1.00 57.01           C  
ANISOU 2216  CB  ALA A 312     7528   9149   4985    348   2133   -528       C  
ATOM   2217  C   ALA A 312     -20.744  24.468  63.014  1.00 58.20           C  
ANISOU 2217  C   ALA A 312     7685   9344   5084    233   2108   -473       C  
ATOM   2218  O   ALA A 312     -21.206  24.400  64.151  1.00 63.45           O  
ANISOU 2218  O   ALA A 312     8379  10008   5722    229   2176   -467       O  
ATOM   2219  N   ALA A 313     -20.889  23.494  62.116  1.00 57.37           N  
ANISOU 2219  N   ALA A 313     7492   9300   5006    198   2050   -444       N  
ATOM   2220  CA  ALA A 313     -21.592  22.254  62.437  1.00 64.35           C  
ANISOU 2220  CA  ALA A 313     8305  10253   5891    145   2061   -401       C  
ATOM   2221  CB  ALA A 313     -22.232  21.662  61.186  1.00 61.49           C  
ANISOU 2221  CB  ALA A 313     7812   9972   5578    141   2025   -372       C  
ATOM   2222  C   ALA A 313     -20.648  21.245  63.083  1.00 62.85           C  
ANISOU 2222  C   ALA A 313     8189  10034   5658     70   2004   -394       C  
ATOM   2223  O   ALA A 313     -21.015  20.555  64.037  1.00 52.71           O  
ANISOU 2223  O   ALA A 313     6910   8768   4350     33   2039   -372       O  
ATOM   2224  N   ARG A 314     -19.432  21.167  62.551  1.00 58.65           N  
ANISOU 2224  N   ARG A 314     7712   9455   5117     48   1917   -411       N  
ATOM   2225  CA  ARG A 314     -18.400  20.277  63.068  1.00 56.62           C  
ANISOU 2225  CA  ARG A 314     7526   9161   4824    -19   1850   -408       C  
ATOM   2226  CB  ARG A 314     -18.237  19.049  62.170  1.00 60.83           C  
ANISOU 2226  CB  ARG A 314     7992   9741   5379    -83   1769   -381       C  
ATOM   2227  CG  ARG A 314     -19.461  18.158  62.070  1.00 61.26           C  
ANISOU 2227  CG  ARG A 314     7933   9889   5455   -111   1800   -339       C  
ATOM   2228  CD  ARG A 314     -19.688  17.396  63.356  1.00 61.66           C  
ANISOU 2228  CD  ARG A 314     8013   9943   5472   -158   1834   -319       C  
ATOM   2229  NE  ARG A 314     -18.517  16.618  63.747  1.00 58.27           N  
ANISOU 2229  NE  ARG A 314     7664   9466   5011   -221   1756   -323       N  
ATOM   2230  CZ  ARG A 314     -18.330  15.340  63.436  1.00 51.29           C  
ANISOU 2230  CZ  ARG A 314     6744   8611   4132   -294   1690   -296       C  
ATOM   2231  NH1 ARG A 314     -19.237  14.695  62.716  1.00 51.62           N  
ANISOU 2231  NH1 ARG A 314     6672   8736   4207   -313   1690   -263       N  
ATOM   2232  NH2 ARG A 314     -17.234  14.710  63.841  1.00 41.93           N  
ANISOU 2232  NH2 ARG A 314     5636   7375   2922   -345   1620   -302       N  
ATOM   2233  C   ARG A 314     -17.077  21.024  63.166  1.00 59.91           C  
ANISOU 2233  C   ARG A 314     8056   9488   5220      0   1805   -445       C  
ATOM   2234  O   ARG A 314     -16.378  21.170  62.169  1.00 49.91           O  
ANISOU 2234  O   ARG A 314     6789   8200   3974      1   1740   -457       O  
ATOM   2235  N   PRO A 315     -16.732  21.513  64.365  1.00 60.31           N  
ANISOU 2235  N   PRO A 315     8201   9485   5227     20   1840   -461       N  
ATOM   2236  CA  PRO A 315     -15.480  22.257  64.559  1.00 63.32           C  
ANISOU 2236  CA  PRO A 315     8686   9785   5587     44   1797   -494       C  
ATOM   2237  CB  PRO A 315     -15.573  22.719  66.018  1.00 62.99           C  
ANISOU 2237  CB  PRO A 315     8719   9720   5496     77   1855   -501       C  
ATOM   2238  CG  PRO A 315     -17.031  22.729  66.315  1.00 63.18           C  
ANISOU 2238  CG  PRO A 315     8678   9800   5528     95   1955   -481       C  
ATOM   2239  CD  PRO A 315     -17.592  21.566  65.557  1.00 64.35           C  
ANISOU 2239  CD  PRO A 315     8722  10017   5713     35   1930   -449       C  
ATOM   2240  C   PRO A 315     -14.219  21.413  64.338  1.00 61.12           C  
ANISOU 2240  C   PRO A 315     8444   9476   5305    -17   1690   -494       C  
ATOM   2241  O   PRO A 315     -13.134  21.978  64.203  1.00 63.51           O  
ANISOU 2241  O   PRO A 315     8811   9717   5603      0   1640   -519       O  
ATOM   2242  N   ASP A 316     -14.366  20.090  64.307  1.00 52.11           N  
ANISOU 2242  N   ASP A 316     7257   8375   4166    -88   1655   -464       N  
ATOM   2243  CA  ASP A 316     -13.243  19.187  64.079  1.00 46.76           C  
ANISOU 2243  CA  ASP A 316     6607   7668   3490   -151   1555   -462       C  
ATOM   2244  CB  ASP A 316     -13.417  17.899  64.895  1.00 46.79           C  
ANISOU 2244  CB  ASP A 316     6606   7700   3472   -219   1545   -434       C  
ATOM   2245  CG  ASP A 316     -14.768  17.225  64.660  1.00 51.72           C  
ANISOU 2245  CG  ASP A 316     7128   8410   4113   -240   1594   -399       C  
ATOM   2246  OD1 ASP A 316     -15.724  17.917  64.240  1.00 53.78           O  
ANISOU 2246  OD1 ASP A 316     7331   8709   4393   -189   1660   -399       O  
ATOM   2247  OD2 ASP A 316     -14.879  16.004  64.923  1.00 44.01           O  
ANISOU 2247  OD2 ASP A 316     6127   7463   3130   -306   1567   -372       O  
ATOM   2248  C   ASP A 316     -13.081  18.855  62.591  1.00 42.41           C  
ANISOU 2248  C   ASP A 316     5992   7138   2983   -169   1496   -455       C  
ATOM   2249  O   ASP A 316     -12.234  18.052  62.211  1.00 45.49           O  
ANISOU 2249  O   ASP A 316     6393   7511   3382   -222   1412   -450       O  
ATOM   2250  N   ALA A 317     -13.899  19.487  61.757  1.00 39.72           N  
ANISOU 2250  N   ALA A 317     5585   6837   2670   -122   1538   -456       N  
ATOM   2251  CA  ALA A 317     -13.903  19.188  60.333  1.00 46.58           C  
ANISOU 2251  CA  ALA A 317     6384   7738   3578   -131   1487   -446       C  
ATOM   2252  CB  ALA A 317     -15.185  19.693  59.685  1.00 47.97           C  
ANISOU 2252  CB  ALA A 317     6464   7981   3781    -80   1549   -438       C  
ATOM   2253  C   ALA A 317     -12.695  19.783  59.638  1.00 45.71           C  
ANISOU 2253  C   ALA A 317     6330   7558   3479   -113   1425   -473       C  
ATOM   2254  O   ALA A 317     -12.337  20.942  59.862  1.00 46.37           O  
ANISOU 2254  O   ALA A 317     6473   7589   3557    -59   1453   -503       O  
ATOM   2255  N   ILE A 318     -12.070  18.967  58.795  1.00 44.01           N  
ANISOU 2255  N   ILE A 318     6096   7344   3282   -158   1343   -462       N  
ATOM   2256  CA  ILE A 318     -11.008  19.407  57.902  1.00 41.09           C  
ANISOU 2256  CA  ILE A 318     5762   6918   2932   -143   1283   -482       C  
ATOM   2257  CB  ILE A 318      -9.847  18.417  57.881  1.00 36.73           C  
ANISOU 2257  CB  ILE A 318     5249   6326   2381   -209   1192   -475       C  
ATOM   2258  CG1 ILE A 318      -9.231  18.300  59.276  1.00 44.78           C  
ANISOU 2258  CG1 ILE A 318     6348   7297   3369   -232   1192   -485       C  
ATOM   2259  CD1 ILE A 318      -8.458  17.023  59.480  1.00 41.76           C  
ANISOU 2259  CD1 ILE A 318     5981   6898   2986   -307   1114   -470       C  
ATOM   2260  CG2 ILE A 318      -8.809  18.841  56.863  1.00 35.40           C  
ANISOU 2260  CG2 ILE A 318     5108   6104   2239   -192   1134   -492       C  
ATOM   2261  C   ILE A 318     -11.570  19.551  56.496  1.00 39.88           C  
ANISOU 2261  C   ILE A 318     5527   6814   2813   -114   1276   -473       C  
ATOM   2262  O   ILE A 318     -12.232  18.643  55.994  1.00 43.00           O  
ANISOU 2262  O   ILE A 318     5843   7279   3218   -145   1260   -444       O  
ATOM   2263  N   ILE A 319     -11.317  20.685  55.855  1.00 35.14           N  
ANISOU 2263  N   ILE A 319     4944   6179   2229    -53   1286   -498       N  
ATOM   2264  CA  ILE A 319     -11.981  20.939  54.595  1.00 34.03           C  
ANISOU 2264  CA  ILE A 319     4724   6089   2117    -13   1288   -490       C  
ATOM   2265  CB  ILE A 319     -13.176  21.909  54.782  1.00 56.75           C  
ANISOU 2265  CB  ILE A 319     7558   9004   5000     56   1378   -497       C  
ATOM   2266  CG1 ILE A 319     -13.962  22.036  53.474  1.00 58.59           C  
ANISOU 2266  CG1 ILE A 319     7695   9300   5265    101   1374   -484       C  
ATOM   2267  CD1 ILE A 319     -15.168  22.920  53.567  1.00 67.20           C  
ANISOU 2267  CD1 ILE A 319     8732  10430   6370    172   1456   -487       C  
ATOM   2268  CG2 ILE A 319     -12.711  23.262  55.301  1.00 56.08           C  
ANISOU 2268  CG2 ILE A 319     7555   8843   4908    108   1418   -534       C  
ATOM   2269  C   ILE A 319     -11.043  21.481  53.520  1.00 38.74           C  
ANISOU 2269  C   ILE A 319     5352   6633   2736     13   1237   -508       C  
ATOM   2270  O   ILE A 319     -10.177  22.326  53.775  1.00 39.25           O  
ANISOU 2270  O   ILE A 319     5496   6620   2798     36   1237   -537       O  
ATOM   2271  N   ALA A 320     -11.222  20.946  52.318  1.00 36.00           N  
ANISOU 2271  N   ALA A 320     4941   6328   2409      9   1191   -489       N  
ATOM   2272  CA  ALA A 320     -10.509  21.394  51.138  1.00 32.37           C  
ANISOU 2272  CA  ALA A 320     4497   5830   1972     39   1146   -501       C  
ATOM   2273  CB  ALA A 320      -9.538  20.319  50.650  1.00 31.60           C  
ANISOU 2273  CB  ALA A 320     4419   5710   1879    -25   1058   -487       C  
ATOM   2274  C   ALA A 320     -11.537  21.738  50.064  1.00 41.10           C  
ANISOU 2274  C   ALA A 320     5518   6991   3109    100   1161   -488       C  
ATOM   2275  O   ALA A 320     -12.601  21.124  49.997  1.00 45.29           O  
ANISOU 2275  O   ALA A 320     5970   7579   3660     93   1168   -456       O  
ATOM   2276  N   THR A 321     -11.279  22.758  49.269  1.00 37.01           N  
ANISOU 2276  N   THR A 321     5018   6428   2615    161   1156   -505       N  
ATOM   2277  CA  THR A 321     -12.191  23.096  48.192  1.00 37.02           C  
ANISOU 2277  CA  THR A 321     4953   6447   2664    230   1168   -492       C  
ATOM   2278  CB  THR A 321     -13.200  24.211  48.534  1.00 41.17           C  
ANISOU 2278  CB  THR A 321     5488   6973   3181    299   1254   -520       C  
ATOM   2279  OG1 THR A 321     -12.762  25.457  48.042  1.00 37.30           O  
ANISOU 2279  OG1 THR A 321     4978   6533   2662    277   1314   -516       O  
ATOM   2280  CG2 THR A 321     -13.472  24.280  50.010  1.00 42.72           C  
ANISOU 2280  CG2 THR A 321     5623   7182   3428    376   1267   -511       C  
ATOM   2281  C   THR A 321     -11.489  23.410  46.881  1.00 37.20           C  
ANISOU 2281  C   THR A 321     4991   6422   2721    255   1106   -491       C  
ATOM   2282  O   THR A 321     -10.311  23.384  46.807  1.00 39.43           O  
ANISOU 2282  O   THR A 321     5341   6652   2988    229   1069   -507       O  
ATOM   2283  N   GLY A 322     -12.263  23.638  45.852  1.00 32.09           N  
ANISOU 2283  N   GLY A 322     4483   5080   2630   -154    280   -518       N  
ATOM   2284  CA  GLY A 322     -11.691  24.001  44.570  1.00 31.34           C  
ANISOU 2284  CA  GLY A 322     4396   4932   2582   -156    285   -529       C  
ATOM   2285  C   GLY A 322     -11.420  25.494  44.457  1.00 39.38           C  
ANISOU 2285  C   GLY A 322     5429   5936   3597   -225    306   -609       C  
ATOM   2286  O   GLY A 322     -10.969  25.962  43.417  1.00 39.79           O  
ANISOU 2286  O   GLY A 322     5488   5942   3687   -234    313   -625       O  
ATOM   2287  N   ARG A 323     -11.687  26.242  45.529  1.00 37.64           N  
ANISOU 2287  N   ARG A 323     5209   5742   3348   -269    310   -650       N  
ATOM   2288  CA  ARG A 323     -11.629  27.705  45.487  1.00 42.97           C  
ANISOU 2288  CA  ARG A 323     5900   6376   4052   -324    325   -713       C  
ATOM   2289  CB  ARG A 323     -12.888  28.308  46.127  1.00 50.27           C  
ANISOU 2289  CB  ARG A 323     6858   7243   4997   -331    341   -739       C  
ATOM   2290  CG  ARG A 323     -14.184  27.995  45.379  1.00 63.66           C  
ANISOU 2290  CG  ARG A 323     8606   8837   6745   -286    362   -723       C  
ATOM   2291  CD  ARG A 323     -14.856  29.268  44.872  1.00 76.65           C  
ANISOU 2291  CD  ARG A 323    10287  10382   8455   -310    383   -770       C  
ATOM   2292  NE  ARG A 323     -15.546  29.990  45.941  1.00 86.74           N  
ANISOU 2292  NE  ARG A 323    11569  11659   9727   -334    385   -799       N  
ATOM   2293  CZ  ARG A 323     -16.856  30.224  45.968  1.00 94.17           C  
ANISOU 2293  CZ  ARG A 323    12546  12527  10709   -315    399   -803       C  
ATOM   2294  NH1 ARG A 323     -17.630  29.810  44.974  1.00 97.41           N  
ANISOU 2294  NH1 ARG A 323    12988  12853  11170   -272    411   -779       N  
ATOM   2295  NH2 ARG A 323     -17.393  30.887  46.985  1.00 94.30           N  
ANISOU 2295  NH2 ARG A 323    12562  12552  10716   -338    400   -829       N  
ATOM   2296  C   ARG A 323     -10.388  28.279  46.172  1.00 41.15           C  
ANISOU 2296  C   ARG A 323     5622   6233   3781   -375    306   -739       C  
ATOM   2297  O   ARG A 323      -9.983  27.814  47.234  1.00 40.06           O  
ANISOU 2297  O   ARG A 323     5446   6184   3591   -378    286   -720       O  
ATOM   2298  N   SER A 324      -9.792  29.298  45.555  1.00 40.53           N  
ANISOU 2298  N   SER A 324     5543   6128   3728   -416    314   -781       N  
ATOM   2299  CA  SER A 324      -8.602  29.930  46.106  1.00 45.53           C  
ANISOU 2299  CA  SER A 324     6134   6838   4328   -467    298   -809       C  
ATOM   2300  CB  SER A 324      -7.833  30.658  45.001  1.00 52.30           C  
ANISOU 2300  CB  SER A 324     6991   7665   5216   -495    305   -836       C  
ATOM   2301  OG  SER A 324      -8.694  31.503  44.260  1.00 55.28           O  
ANISOU 2301  OG  SER A 324     7416   7931   5657   -501    331   -867       O  
ATOM   2302  C   SER A 324      -8.914  30.898  47.250  1.00 59.01           C  
ANISOU 2302  C   SER A 324     7840   8557   6025   -511    300   -853       C  
ATOM   2303  O   SER A 324      -7.996  31.432  47.872  1.00 64.24           O  
ANISOU 2303  O   SER A 324     8466   9286   6657   -555    287   -878       O  
ATOM   2304  N   ASP A 325     -10.198  31.124  47.529  1.00 62.80           N  
ANISOU 2304  N   ASP A 325     8357   8972   6530   -498    316   -863       N  
ATOM   2305  CA  ASP A 325     -10.592  31.947  48.675  1.00 63.24           C  
ANISOU 2305  CA  ASP A 325     8412   9042   6575   -532    318   -900       C  
ATOM   2306  CB  ASP A 325     -12.094  32.248  48.667  1.00 67.64           C  
ANISOU 2306  CB  ASP A 325     9018   9509   7175   -512    338   -909       C  
ATOM   2307  CG  ASP A 325     -12.650  32.424  47.279  1.00 76.55           C  
ANISOU 2307  CG  ASP A 325    10186  10529   8369   -491    357   -907       C  
ATOM   2308  OD1 ASP A 325     -12.411  33.489  46.673  1.00 84.30           O  
ANISOU 2308  OD1 ASP A 325    11176  11465   9391   -524    367   -944       O  
ATOM   2309  OD2 ASP A 325     -13.339  31.501  46.800  1.00 79.34           O  
ANISOU 2309  OD2 ASP A 325    10563  10846   8736   -440    363   -868       O  
ATOM   2310  C   ASP A 325     -10.241  31.250  49.982  1.00 63.15           C  
ANISOU 2310  C   ASP A 325     8361   9136   6498   -529    296   -877       C  
ATOM   2311  O   ASP A 325      -9.809  31.878  50.947  1.00 67.42           O  
ANISOU 2311  O   ASP A 325     8876   9731   7010   -569    287   -908       O  
ATOM   2312  N   TYR A 326     -10.446  29.940  50.003  1.00 55.38           N  
ANISOU 2312  N   TYR A 326     7372   8177   5493   -479    287   -820       N  
ATOM   2313  CA  TYR A 326     -10.323  29.164  51.225  1.00 51.55           C  
ANISOU 2313  CA  TYR A 326     6853   7782   4952   -466    268   -789       C  
ATOM   2314  CB  TYR A 326     -11.493  28.183  51.336  1.00 52.68           C  
ANISOU 2314  CB  TYR A 326     7023   7895   5099   -412    274   -744       C  
ATOM   2315  CG  TYR A 326     -12.846  28.821  51.090  1.00 56.90           C  
ANISOU 2315  CG  TYR A 326     7611   8327   5680   -407    300   -772       C  
ATOM   2316  CD1 TYR A 326     -13.332  29.817  51.933  1.00 58.94           C  
ANISOU 2316  CD1 TYR A 326     7878   8577   5940   -441    307   -817       C  
ATOM   2317  CE1 TYR A 326     -14.570  30.400  51.711  1.00 58.68           C  
ANISOU 2317  CE1 TYR A 326     7891   8452   5953   -435    329   -840       C  
ATOM   2318  CZ  TYR A 326     -15.334  29.985  50.641  1.00 61.38           C  
ANISOU 2318  CZ  TYR A 326     8273   8709   6341   -394    344   -817       C  
ATOM   2319  OH  TYR A 326     -16.564  30.555  50.407  1.00 62.01           O  
ANISOU 2319  OH  TYR A 326     8394   8696   6469   -385    364   -836       O  
ATOM   2320  CE2 TYR A 326     -14.873  29.000  49.795  1.00 62.82           C  
ANISOU 2320  CE2 TYR A 326     8450   8898   6522   -361    339   -774       C  
ATOM   2321  CD2 TYR A 326     -13.637  28.425  50.022  1.00 59.44           C  
ANISOU 2321  CD2 TYR A 326     7974   8563   6047   -367    316   -751       C  
ATOM   2322  C   TYR A 326      -8.997  28.420  51.274  1.00 51.51           C  
ANISOU 2322  C   TYR A 326     6796   7870   4907   -463    242   -754       C  
ATOM   2323  O   TYR A 326      -8.367  28.203  50.238  1.00 49.20           O  
ANISOU 2323  O   TYR A 326     6499   7567   4629   -455    240   -741       O  
ATOM   2324  N   PRO A 327      -8.559  28.040  52.483  1.00 44.73           N  
ANISOU 2324  N   PRO A 327     5895   7104   3996   -470    221   -738       N  
ATOM   2325  CA  PRO A 327      -7.368  27.196  52.613  1.00 40.48           C  
ANISOU 2325  CA  PRO A 327     5304   6656   3420   -459    194   -696       C  
ATOM   2326  CB  PRO A 327      -7.274  26.944  54.117  1.00 41.81           C  
ANISOU 2326  CB  PRO A 327     5438   6909   3541   -468    178   -686       C  
ATOM   2327  CG  PRO A 327      -7.992  28.100  54.744  1.00 43.58           C  
ANISOU 2327  CG  PRO A 327     5687   7099   3773   -505    196   -745       C  
ATOM   2328  CD  PRO A 327      -9.089  28.464  53.793  1.00 42.92           C  
ANISOU 2328  CD  PRO A 327     5663   6902   3744   -490    222   -762       C  
ATOM   2329  C   PRO A 327      -7.506  25.876  51.854  1.00 36.93           C  
ANISOU 2329  C   PRO A 327     4857   6195   2978   -398    187   -630       C  
ATOM   2330  O   PRO A 327      -8.620  25.479  51.504  1.00 36.15           O  
ANISOU 2330  O   PRO A 327     4797   6031   2905   -361    202   -611       O  
ATOM   2331  N   ASN A 328      -6.371  25.225  51.602  1.00 36.20           N  
ANISOU 2331  N   ASN A 328     4723   6167   2867   -387    165   -594       N  
ATOM   2332  CA  ASN A 328      -6.320  23.903  50.978  1.00 36.48           C  
ANISOU 2332  CA  ASN A 328     4749   6206   2906   -328    152   -526       C  
ATOM   2333  CB  ASN A 328      -6.924  22.847  51.907  1.00 33.64           C  
ANISOU 2333  CB  ASN A 328     4377   5882   2523   -288    139   -473       C  
ATOM   2334  CG  ASN A 328      -6.264  22.812  53.261  1.00 39.27           C  
ANISOU 2334  CG  ASN A 328     5042   6692   3189   -313    119   -471       C  
ATOM   2335  OD1 ASN A 328      -5.039  22.904  53.376  1.00 38.90           O  
ANISOU 2335  OD1 ASN A 328     4952   6709   3120   -336    102   -473       O  
ATOM   2336  ND2 ASN A 328      -7.076  22.663  54.304  1.00 35.12           N  
ANISOU 2336  ND2 ASN A 328     4520   6177   2646   -309    122   -466       N  
ATOM   2337  C   ASN A 328      -7.021  23.814  49.621  1.00 33.76           C  
ANISOU 2337  C   ASN A 328     4453   5766   2611   -296    172   -522       C  
ATOM   2338  O   ASN A 328      -7.853  22.933  49.407  1.00 34.22           O  
ANISOU 2338  O   ASN A 328     4530   5792   2681   -244    175   -479       O  
ATOM   2339  N   GLN A 329      -6.688  24.714  48.703  1.00 34.63           N  
ANISOU 2339  N   GLN A 329     4580   5829   2749   -326    187   -566       N  
ATOM   2340  CA  GLN A 329      -7.300  24.654  47.390  1.00 29.76           C  
ANISOU 2340  CA  GLN A 329     4007   5121   2179   -297    207   -564       C  
ATOM   2341  CB  GLN A 329      -7.072  25.941  46.603  1.00 33.14           C  
ANISOU 2341  CB  GLN A 329     4458   5491   2641   -343    227   -626       C  
ATOM   2342  CG  GLN A 329      -7.878  25.965  45.310  1.00 35.55           C  
ANISOU 2342  CG  GLN A 329     4815   5692   3002   -315    252   -629       C  
ATOM   2343  CD  GLN A 329      -7.399  27.001  44.316  1.00 39.13           C  
ANISOU 2343  CD  GLN A 329     5281   6096   3490   -352    268   -675       C  
ATOM   2344  OE1 GLN A 329      -6.366  27.635  44.510  1.00 46.24           O  
ANISOU 2344  OE1 GLN A 329     6150   7047   4372   -396    258   -701       O  
ATOM   2345  NE2 GLN A 329      -8.157  27.177  43.239  1.00 36.66           N  
ANISOU 2345  NE2 GLN A 329     5014   5675   3240   -329    290   -679       N  
ATOM   2346  C   GLN A 329      -6.774  23.475  46.590  1.00 32.99           C  
ANISOU 2346  C   GLN A 329     4394   5551   2591   -243    189   -502       C  
ATOM   2347  O   GLN A 329      -5.568  23.334  46.384  1.00 34.06           O  
ANISOU 2347  O   GLN A 329     4488   5743   2709   -251    170   -490       O  
ATOM   2348  N   VAL A 330      -7.692  22.627  46.144  1.00 27.51           N  
ANISOU 2348  N   VAL A 330     3726   4789   1939   -182    192   -455       N  
ATOM   2349  CA  VAL A 330      -7.354  21.539  45.253  1.00 30.38           C  
ANISOU 2349  CA  VAL A 330     4074   5131   2338   -121    175   -391       C  
ATOM   2350  CB  VAL A 330      -8.308  20.352  45.433  1.00 32.81           C  
ANISOU 2350  CB  VAL A 330     4393   5411   2663    -56    168   -330       C  
ATOM   2351  CG1 VAL A 330      -7.969  19.233  44.473  1.00 35.31           C  
ANISOU 2351  CG1 VAL A 330     4695   5701   3021      9    149   -265       C  
ATOM   2352  CG2 VAL A 330      -8.232  19.854  46.875  1.00 35.96           C  
ANISOU 2352  CG2 VAL A 330     4757   5911   2996    -62    150   -308       C  
ATOM   2353  C   VAL A 330      -7.396  22.082  43.835  1.00 36.08           C  
ANISOU 2353  C   VAL A 330     4828   5756   3124   -118    194   -412       C  
ATOM   2354  O   VAL A 330      -8.460  22.180  43.229  1.00 37.69           O  
ANISOU 2354  O   VAL A 330     5081   5862   3380    -95    215   -417       O  
ATOM   2355  N   ASN A 331      -6.219  22.445  43.327  1.00 26.50           N  
ANISOU 2355  N   ASN A 331     3587   4574   1907   -142    185   -425       N  
ATOM   2356  CA  ASN A 331      -6.064  23.103  42.039  1.00 22.71           C  
ANISOU 2356  CA  ASN A 331     3131   4018   1480   -149    202   -450       C  
ATOM   2357  CB  ASN A 331      -5.309  24.427  42.236  1.00 25.70           C  
ANISOU 2357  CB  ASN A 331     3500   4433   1833   -226    211   -517       C  
ATOM   2358  CG  ASN A 331      -5.303  25.311  40.999  1.00 36.08           C  
ANISOU 2358  CG  ASN A 331     4844   5663   3202   -243    233   -553       C  
ATOM   2359  OD1 ASN A 331      -5.182  24.842  39.858  1.00 34.22           O  
ANISOU 2359  OD1 ASN A 331     4612   5375   3012   -199    232   -520       O  
ATOM   2360  ND2 ASN A 331      -5.420  26.618  41.228  1.00 40.87           N  
ANISOU 2360  ND2 ASN A 331     5470   6255   3802   -306    254   -622       N  
ATOM   2361  C   ASN A 331      -5.302  22.169  41.103  1.00 24.40           C  
ANISOU 2361  C   ASN A 331     3318   4235   1720    -98    181   -394       C  
ATOM   2362  O   ASN A 331      -4.244  21.668  41.480  1.00 26.48           O  
ANISOU 2362  O   ASN A 331     3531   4588   1944    -97    155   -368       O  
ATOM   2363  N   ASN A 332      -5.839  21.897  39.916  1.00 23.58           N  
ANISOU 2363  N   ASN A 332     3245   4035   1679    -53    192   -376       N  
ATOM   2364  CA  ASN A 332      -5.167  20.977  39.000  1.00 22.94           C  
ANISOU 2364  CA  ASN A 332     3138   3953   1624      0    172   -323       C  
ATOM   2365  CB  ASN A 332      -6.022  20.700  37.760  1.00 38.77           C  
ANISOU 2365  CB  ASN A 332     5186   5843   3702     51    187   -306       C  
ATOM   2366  CG  ASN A 332      -7.219  19.827  38.063  1.00 53.19           C  
ANISOU 2366  CG  ASN A 332     7037   7627   5547    102    187   -269       C  
ATOM   2367  OD1 ASN A 332      -7.589  19.643  39.219  1.00 57.91           O  
ANISOU 2367  OD1 ASN A 332     7630   8270   6105     91    182   -265       O  
ATOM   2368  ND2 ASN A 332      -7.786  19.225  37.027  1.00 50.77           N  
ANISOU 2368  ND2 ASN A 332     6755   7236   5299    161    190   -237       N  
ATOM   2369  C   ASN A 332      -3.800  21.442  38.553  1.00 27.23           C  
ANISOU 2369  C   ASN A 332     3646   4547   2154    -32    163   -338       C  
ATOM   2370  O   ASN A 332      -2.989  20.627  38.118  1.00 26.34           O  
ANISOU 2370  O   ASN A 332     3497   4468   2042      5    140   -293       O  
ATOM   2371  N   VAL A 333      -3.518  22.734  38.668  1.00 25.79           N  
ANISOU 2371  N   VAL A 333     3470   4369   1958    -99    180   -400       N  
ATOM   2372  CA  VAL A 333      -2.216  23.233  38.234  1.00 24.62           C  
ANISOU 2372  CA  VAL A 333     3288   4267   1799   -132    172   -416       C  
ATOM   2373  CB  VAL A 333      -2.184  24.772  38.222  1.00 24.94           C  
ANISOU 2373  CB  VAL A 333     3349   4286   1840   -206    197   -490       C  
ATOM   2374  CG1 VAL A 333      -1.894  25.304  39.607  1.00 24.91           C  
ANISOU 2374  CG1 VAL A 333     3324   4367   1771   -264    192   -526       C  
ATOM   2375  CG2 VAL A 333      -1.142  25.271  37.232  1.00 26.43           C  
ANISOU 2375  CG2 VAL A 333     3519   4476   2048   -224    197   -500       C  
ATOM   2376  C   VAL A 333      -1.077  22.689  39.109  1.00 24.55           C  
ANISOU 2376  C   VAL A 333     3220   4381   1728   -141    141   -390       C  
ATOM   2377  O   VAL A 333       0.096  22.787  38.750  1.00 25.20           O  
ANISOU 2377  O   VAL A 333     3266   4512   1799   -155    127   -387       O  
ATOM   2378  N   LEU A 334      -1.417  22.086  40.244  1.00 26.60           N  
ANISOU 2378  N   LEU A 334     3468   4693   1947   -132    128   -370       N  
ATOM   2379  CA  LEU A 334      -0.411  21.444  41.081  1.00 25.61           C  
ANISOU 2379  CA  LEU A 334     3285   4682   1763   -133     97   -339       C  
ATOM   2380  CB  LEU A 334      -0.949  21.213  42.492  1.00 25.78           C  
ANISOU 2380  CB  LEU A 334     3304   4756   1737   -144     92   -338       C  
ATOM   2381  CG  LEU A 334      -1.090  22.470  43.347  1.00 31.98           C  
ANISOU 2381  CG  LEU A 334     4100   5566   2486   -218    109   -409       C  
ATOM   2382  CD1 LEU A 334      -1.902  22.169  44.609  1.00 31.28           C  
ANISOU 2382  CD1 LEU A 334     4018   5509   2359   -217    108   -404       C  
ATOM   2383  CD2 LEU A 334       0.283  23.024  43.719  1.00 31.65           C  
ANISOU 2383  CD2 LEU A 334     4011   5617   2396   -272     95   -434       C  
ATOM   2384  C   LEU A 334       0.072  20.115  40.500  1.00 28.50           C  
ANISOU 2384  C   LEU A 334     3622   5061   2145    -65     71   -268       C  
ATOM   2385  O   LEU A 334       1.130  19.611  40.893  1.00 29.79           O  
ANISOU 2385  O   LEU A 334     3735   5316   2269    -64     45   -241       O  
ATOM   2386  N   GLY A 335      -0.692  19.562  39.562  1.00 26.76           N  
ANISOU 2386  N   GLY A 335     3433   4750   1984     -8     79   -239       N  
ATOM   2387  CA  GLY A 335      -0.404  18.244  39.029  1.00 24.18           C  
ANISOU 2387  CA  GLY A 335     3083   4427   1677     63     54   -171       C  
ATOM   2388  C   GLY A 335       0.209  18.212  37.639  1.00 26.77           C  
ANISOU 2388  C   GLY A 335     3407   4717   2048     87     53   -162       C  
ATOM   2389  O   GLY A 335       1.410  17.948  37.497  1.00 27.53           O  
ANISOU 2389  O   GLY A 335     3457   4880   2122     87     32   -143       O  
ATOM   2390  N   PHE A 336      -0.603  18.469  36.611  1.00 25.32           N  
ANISOU 2390  N   PHE A 336     3269   4426   1925    109     76   -173       N  
ATOM   2391  CA  PHE A 336      -0.157  18.239  35.239  1.00 26.78           C  
ANISOU 2391  CA  PHE A 336     3451   4568   2155    146     74   -154       C  
ATOM   2392  CB  PHE A 336      -1.286  18.586  34.228  1.00 24.60           C  
ANISOU 2392  CB  PHE A 336     3233   4169   1946    167    102   -171       C  
ATOM   2393  CG  PHE A 336      -1.636  20.053  34.138  1.00 22.04           C  
ANISOU 2393  CG  PHE A 336     2944   3801   1630    103    135   -239       C  
ATOM   2394  CD1 PHE A 336      -0.966  20.889  33.261  1.00 25.82           C  
ANISOU 2394  CD1 PHE A 336     3420   4265   2126     74    146   -269       C  
ATOM   2395  CE1 PHE A 336      -1.295  22.232  33.170  1.00 27.05           C  
ANISOU 2395  CE1 PHE A 336     3608   4379   2292     15    176   -330       C  
ATOM   2396  CZ  PHE A 336      -2.309  22.753  33.957  1.00 23.50           C  
ANISOU 2396  CZ  PHE A 336     3194   3901   1835    -14    194   -364       C  
ATOM   2397  CE2 PHE A 336      -2.996  21.926  34.825  1.00 26.71           C  
ANISOU 2397  CE2 PHE A 336     3604   4322   2223     15    184   -335       C  
ATOM   2398  CD2 PHE A 336      -2.665  20.584  34.910  1.00 25.22           C  
ANISOU 2398  CD2 PHE A 336     3383   4175   2025     74    154   -272       C  
ATOM   2399  C   PHE A 336       1.169  18.926  34.800  1.00 23.94           C  
ANISOU 2399  C   PHE A 336     3058   4259   1779    105     70   -178       C  
ATOM   2400  O   PHE A 336       1.907  18.332  34.021  1.00 25.89           O  
ANISOU 2400  O   PHE A 336     3278   4518   2041    142     54   -144       O  
ATOM   2401  N   PRO A 337       1.481  20.149  35.282  1.00 24.54           N  
ANISOU 2401  N   PRO A 337     3135   4363   1826     30     85   -234       N  
ATOM   2402  CA  PRO A 337       2.752  20.708  34.794  1.00 24.32           C  
ANISOU 2402  CA  PRO A 337     3074   4380   1787     -3     80   -250       C  
ATOM   2403  CB  PRO A 337       2.820  22.078  35.474  1.00 25.50           C  
ANISOU 2403  CB  PRO A 337     3232   4550   1907    -87     98   -316       C  
ATOM   2404  CG  PRO A 337       1.382  22.408  35.795  1.00 26.19           C  
ANISOU 2404  CG  PRO A 337     3374   4563   2016    -90    122   -342       C  
ATOM   2405  CD  PRO A 337       0.804  21.092  36.190  1.00 26.25           C  
ANISOU 2405  CD  PRO A 337     3379   4574   2021    -27    105   -286       C  
ATOM   2406  C   PRO A 337       3.959  19.858  35.183  1.00 24.76           C  
ANISOU 2406  C   PRO A 337     3069   4541   1800     13     45   -207       C  
ATOM   2407  O   PRO A 337       4.799  19.595  34.319  1.00 25.78           O  
ANISOU 2407  O   PRO A 337     3172   4681   1943     35     34   -186       O  
ATOM   2408  N   SER A 338       4.020  19.399  36.431  1.00 26.56           N  
ANISOU 2408  N   SER A 338     3273   4842   1977      6     28   -193       N  
ATOM   2409  CA  SER A 338       5.146  18.564  36.867  1.00 29.18           C  
ANISOU 2409  CA  SER A 338     3546   5275   2265     21     -6   -151       C  
ATOM   2410  CB  SER A 338       5.164  18.441  38.385  1.00 31.64           C  
ANISOU 2410  CB  SER A 338     3837   5669   2515     -8    -18   -153       C  
ATOM   2411  OG  SER A 338       5.485  19.682  38.987  1.00 32.57           O  
ANISOU 2411  OG  SER A 338     3953   5822   2598    -86     -5   -213       O  
ATOM   2412  C   SER A 338       5.125  17.169  36.259  1.00 25.99           C  
ANISOU 2412  C   SER A 338     3129   4855   1890    104    -27    -84       C  
ATOM   2413  O   SER A 338       6.178  16.600  35.929  1.00 26.80           O  
ANISOU 2413  O   SER A 338     3189   5012   1982    126    -50    -52       O  
ATOM   2414  N   ILE A 339       3.932  16.602  36.142  1.00 25.36           N  
ANISOU 2414  N   ILE A 339     3086   4703   1846    150    -20    -64       N  
ATOM   2415  CA  ILE A 339       3.780  15.285  35.542  1.00 23.00           C  
ANISOU 2415  CA  ILE A 339     2780   4377   1580    231    -39     -3       C  
ATOM   2416  CB  ILE A 339       2.316  14.822  35.635  1.00 25.31           C  
ANISOU 2416  CB  ILE A 339     3118   4591   1909    270    -29     12       C  
ATOM   2417  CG1 ILE A 339       1.944  14.674  37.109  1.00 25.87           C  
ANISOU 2417  CG1 ILE A 339     3182   4718   1930    247    -35     14       C  
ATOM   2418  CD1 ILE A 339       0.507  14.299  37.342  1.00 26.60           C  
ANISOU 2418  CD1 ILE A 339     3317   4739   2051    278    -23     26       C  
ATOM   2419  CG2 ILE A 339       2.123  13.508  34.887  1.00 27.34           C  
ANISOU 2419  CG2 ILE A 339     3370   4810   2208    354    -48     72       C  
ATOM   2420  C   ILE A 339       4.276  15.273  34.097  1.00 24.05           C  
ANISOU 2420  C   ILE A 339     2912   4469   1758    260    -38      4       C  
ATOM   2421  O   ILE A 339       5.069  14.416  33.717  1.00 24.56           O  
ANISOU 2421  O   ILE A 339     2938   4572   1822    301    -63     47       O  
ATOM   2422  N   PHE A 340       3.860  16.243  33.290  1.00 19.93           N  
ANISOU 2422  N   PHE A 340     2428   3870   1273    237     -8    -38       N  
ATOM   2423  CA  PHE A 340       4.372  16.299  31.933  1.00 19.30           C  
ANISOU 2423  CA  PHE A 340     2345   3755   1232    261     -6    -33       C  
ATOM   2424  CB  PHE A 340       3.537  17.258  31.087  1.00 18.88           C  
ANISOU 2424  CB  PHE A 340     2346   3600   1229    245     29    -76       C  
ATOM   2425  CG  PHE A 340       2.326  16.614  30.479  1.00 24.38           C  
ANISOU 2425  CG  PHE A 340     3084   4199   1980    308     37    -53       C  
ATOM   2426  CD1 PHE A 340       2.422  15.926  29.278  1.00 22.61           C  
ANISOU 2426  CD1 PHE A 340     2858   3932   1802    371     29    -19       C  
ATOM   2427  CE1 PHE A 340       1.314  15.334  28.695  1.00 21.26           C  
ANISOU 2427  CE1 PHE A 340     2725   3671   1682    429     35      1       C  
ATOM   2428  CZ  PHE A 340       0.081  15.412  29.338  1.00 18.01           C  
ANISOU 2428  CZ  PHE A 340     2354   3212   1279    424     50    -10       C  
ATOM   2429  CE2 PHE A 340      -0.032  16.099  30.542  1.00 18.04           C  
ANISOU 2429  CE2 PHE A 340     2360   3258   1237    361     58    -43       C  
ATOM   2430  CD2 PHE A 340       1.097  16.686  31.115  1.00 22.34           C  
ANISOU 2430  CD2 PHE A 340     2865   3894   1729    304     51    -64       C  
ATOM   2431  C   PHE A 340       5.857  16.686  31.885  1.00 23.95           C  
ANISOU 2431  C   PHE A 340     2885   4431   1785    224    -19    -41       C  
ATOM   2432  O   PHE A 340       6.591  16.180  31.051  1.00 21.40           O  
ANISOU 2432  O   PHE A 340     2535   4119   1476    261    -34    -12       O  
ATOM   2433  N   ARG A 341       6.299  17.565  32.782  1.00 22.38           N  
ANISOU 2433  N   ARG A 341     2673   4292   1539    153    -14    -80       N  
ATOM   2434  CA  ARG A 341       7.713  17.941  32.818  1.00 22.63           C  
ANISOU 2434  CA  ARG A 341     2656   4408   1533    115    -27    -88       C  
ATOM   2435  CB  ARG A 341       7.956  19.002  33.903  1.00 22.20           C  
ANISOU 2435  CB  ARG A 341     2597   4409   1430     32    -18   -138       C  
ATOM   2436  CG  ARG A 341       9.397  19.516  34.022  1.00 23.56           C  
ANISOU 2436  CG  ARG A 341     2720   4669   1562    -16    -30   -152       C  
ATOM   2437  CD  ARG A 341       9.731  20.534  32.941  1.00 25.39           C  
ANISOU 2437  CD  ARG A 341     2963   4856   1827    -45    -10   -187       C  
ATOM   2438  NE  ARG A 341      10.140  19.904  31.686  1.00 25.63           N  
ANISOU 2438  NE  ARG A 341     2981   4862   1894     12    -18   -148       N  
ATOM   2439  CZ  ARG A 341      10.059  20.473  30.483  1.00 26.85           C  
ANISOU 2439  CZ  ARG A 341     3157   4948   2095     15      2   -164       C  
ATOM   2440  NH1 ARG A 341       9.597  21.714  30.343  1.00 23.98           N  
ANISOU 2440  NH1 ARG A 341     2829   4533   1750    -39     31   -217       N  
ATOM   2441  NH2 ARG A 341      10.463  19.804  29.413  1.00 26.82           N  
ANISOU 2441  NH2 ARG A 341     3138   4931   2120     70     -8   -127       N  
ATOM   2442  C   ARG A 341       8.602  16.712  33.050  1.00 23.48           C  
ANISOU 2442  C   ARG A 341     2711   4598   1613    159    -64    -31       C  
ATOM   2443  O   ARG A 341       9.594  16.521  32.350  1.00 26.39           O  
ANISOU 2443  O   ARG A 341     3047   4997   1984    173    -76    -13       O  
ATOM   2444  N   GLY A 342       8.235  15.877  34.018  1.00 24.48           N  
ANISOU 2444  N   GLY A 342     2829   4757   1714    181    -80     -1       N  
ATOM   2445  CA  GLY A 342       8.990  14.670  34.320  1.00 27.70           C  
ANISOU 2445  CA  GLY A 342     3188   5240   2096    224   -116     55       C  
ATOM   2446  C   GLY A 342       8.936  13.662  33.187  1.00 28.42           C  
ANISOU 2446  C   GLY A 342     3278   5283   2237    304   -128    102       C  
ATOM   2447  O   GLY A 342       9.940  13.033  32.854  1.00 27.60           O  
ANISOU 2447  O   GLY A 342     3130   5232   2123    331   -152    135       O  
ATOM   2448  N   ALA A 343       7.756  13.516  32.589  1.00 21.70           N  
ANISOU 2448  N   ALA A 343     2475   4331   1439    341   -111    103       N  
ATOM   2449  CA  ALA A 343       7.565  12.614  31.451  1.00 22.74           C  
ANISOU 2449  CA  ALA A 343     2612   4405   1624    418   -120    142       C  
ATOM   2450  CB  ALA A 343       6.085  12.543  31.066  1.00 22.73           C  
ANISOU 2450  CB  ALA A 343     2668   4293   1675    449   -100    138       C  
ATOM   2451  C   ALA A 343       8.387  13.046  30.255  1.00 23.19           C  
ANISOU 2451  C   ALA A 343     2657   4455   1701    417   -115    131       C  
ATOM   2452  O   ALA A 343       9.017  12.217  29.599  1.00 24.81           O  
ANISOU 2452  O   ALA A 343     2832   4676   1917    469   -137    170       O  
ATOM   2453  N   LEU A 344       8.371  14.344  29.962  1.00 22.34           N  
ANISOU 2453  N   LEU A 344     2571   4320   1597    359    -87     78       N  
ATOM   2454  CA  LEU A 344       9.131  14.873  28.821  1.00 22.79           C  
ANISOU 2454  CA  LEU A 344     2617   4368   1673    353    -80     65       C  
ATOM   2455  CB  LEU A 344       8.765  16.336  28.552  1.00 24.18           C  
ANISOU 2455  CB  LEU A 344     2830   4493   1864    291    -44      5       C  
ATOM   2456  CG  LEU A 344       7.346  16.602  28.028  1.00 21.50           C  
ANISOU 2456  CG  LEU A 344     2553   4038   1579    308    -17    -13       C  
ATOM   2457  CD1 LEU A 344       7.048  18.102  27.955  1.00 22.69           C  
ANISOU 2457  CD1 LEU A 344     2736   4149   1736    238     17    -74       C  
ATOM   2458  CD2 LEU A 344       7.105  15.954  26.671  1.00 24.09           C  
ANISOU 2458  CD2 LEU A 344     2892   4298   1962    380    -18     16       C  
ATOM   2459  C   LEU A 344      10.638  14.758  29.030  1.00 22.88           C  
ANISOU 2459  C   LEU A 344     2568   4485   1639    335   -104     79       C  
ATOM   2460  O   LEU A 344      11.365  14.377  28.113  1.00 26.06           O  
ANISOU 2460  O   LEU A 344     2946   4899   2058    370   -115    102       O  
ATOM   2461  N   ASP A 345      11.094  15.098  30.231  1.00 24.95           N  
ANISOU 2461  N   ASP A 345     2807   4827   1846    281   -111     64       N  
ATOM   2462  CA  ASP A 345      12.525  15.091  30.546  1.00 29.19           C  
ANISOU 2462  CA  ASP A 345     3286   5470   2335    255   -132     73       C  
ATOM   2463  CB  ASP A 345      12.771  15.614  31.966  1.00 33.31           C  
ANISOU 2463  CB  ASP A 345     3793   6066   2796    188   -135     47       C  
ATOM   2464  CG  ASP A 345      12.475  17.104  32.106  1.00 35.87           C  
ANISOU 2464  CG  ASP A 345     4147   6360   3120    113   -104    -18       C  
ATOM   2465  OD1 ASP A 345      12.321  17.789  31.068  1.00 38.52           O  
ANISOU 2465  OD1 ASP A 345     4508   6631   3497    107    -82    -41       O  
ATOM   2466  OD2 ASP A 345      12.409  17.580  33.260  1.00 41.26           O  
ANISOU 2466  OD2 ASP A 345     4828   7087   3761     61   -102    -44       O  
ATOM   2467  C   ASP A 345      13.121  13.697  30.389  1.00 33.38           C  
ANISOU 2467  C   ASP A 345     3776   6046   2861    323   -167    134       C  
ATOM   2468  O   ASP A 345      14.287  13.561  30.011  1.00 32.68           O  
ANISOU 2468  O   ASP A 345     3645   6017   2756    326   -183    148       O  
ATOM   2469  N   THR A 346      12.322  12.666  30.666  1.00 26.92           N  
ANISOU 2469  N   THR A 346     2971   5200   2058    378   -178    170       N  
ATOM   2470  CA  THR A 346      12.775  11.284  30.477  1.00 30.01           C  
ANISOU 2470  CA  THR A 346     3327   5624   2452    448   -211    229       C  
ATOM   2471  CB  THR A 346      12.240  10.365  31.584  1.00 27.03           C  
ANISOU 2471  CB  THR A 346     2944   5270   2054    471   -230    262       C  
ATOM   2472  OG1 THR A 346      10.806  10.441  31.631  1.00 27.50           O  
ANISOU 2472  OG1 THR A 346     3059   5241   2150    483   -209    251       O  
ATOM   2473  CG2 THR A 346      12.800  10.779  32.926  1.00 30.47           C  
ANISOU 2473  CG2 THR A 346     3353   5802   2424    408   -236    247       C  
ATOM   2474  C   THR A 346      12.374  10.679  29.131  1.00 30.37           C  
ANISOU 2474  C   THR A 346     3391   5589   2560    520   -211    252       C  
ATOM   2475  O   THR A 346      12.564   9.484  28.906  1.00 30.24           O  
ANISOU 2475  O   THR A 346     3351   5584   2554    585   -238    301       O  
ATOM   2476  N   ARG A 347      11.831  11.506  28.242  1.00 26.91           N  
ANISOU 2476  N   ARG A 347     2993   5069   2162    508   -181    217       N  
ATOM   2477  CA  ARG A 347      11.319  11.056  26.954  1.00 21.80           C  
ANISOU 2477  CA  ARG A 347     2369   4337   1575    573   -177    233       C  
ATOM   2478  CB  ARG A 347      12.473  10.853  25.957  1.00 24.02           C  
ANISOU 2478  CB  ARG A 347     2611   4653   1861    598   -190    249       C  
ATOM   2479  CG  ARG A 347      13.248  12.136  25.672  1.00 27.02           C  
ANISOU 2479  CG  ARG A 347     2983   5061   2223    531   -171    207       C  
ATOM   2480  CD  ARG A 347      14.380  11.910  24.688  1.00 30.42           C  
ANISOU 2480  CD  ARG A 347     3373   5528   2656    558   -185    226       C  
ATOM   2481  NE  ARG A 347      15.209  13.107  24.545  1.00 32.00           N  
ANISOU 2481  NE  ARG A 347     3558   5765   2834    490   -170    189       N  
ATOM   2482  CZ  ARG A 347      16.287  13.169  23.767  1.00 30.81           C  
ANISOU 2482  CZ  ARG A 347     3371   5654   2679    496   -178    198       C  
ATOM   2483  NH1 ARG A 347      16.650  12.107  23.059  1.00 29.62           N  
ANISOU 2483  NH1 ARG A 347     3197   5511   2546    569   -200    240       N  
ATOM   2484  NH2 ARG A 347      16.989  14.290  23.683  1.00 37.33           N  
ANISOU 2484  NH2 ARG A 347     4184   6512   3486    431   -163    165       N  
ATOM   2485  C   ARG A 347      10.482   9.780  27.100  1.00 31.54           C  
ANISOU 2485  C   ARG A 347     3615   5533   2835    644   -194    277       C  
ATOM   2486  O   ARG A 347      10.619   8.827  26.323  1.00 28.66           O  
ANISOU 2486  O   ARG A 347     3237   5152   2501    714   -213    314       O  
ATOM   2487  N   SER A 348       9.598   9.791  28.096  1.00 28.88           N  
ANISOU 2487  N   SER A 348     3303   5183   2488    626   -188    271       N  
ATOM   2488  CA  SER A 348       8.763   8.639  28.423  1.00 25.10           C  
ANISOU 2488  CA  SER A 348     2834   4673   2029    685   -204    312       C  
ATOM   2489  CB  SER A 348       8.040   8.852  29.757  1.00 27.99           C  
ANISOU 2489  CB  SER A 348     3218   5052   2366    646   -197    301       C  
ATOM   2490  OG  SER A 348       8.962   8.834  30.824  1.00 42.38           O  
ANISOU 2490  OG  SER A 348     4995   6982   4125    608   -215    308       O  
ATOM   2491  C   SER A 348       7.746   8.351  27.343  1.00 29.45           C  
ANISOU 2491  C   SER A 348     3429   5113   2648    741   -192    317       C  
ATOM   2492  O   SER A 348       7.325   9.245  26.610  1.00 31.21           O  
ANISOU 2492  O   SER A 348     3688   5271   2900    721   -163    279       O  
ATOM   2493  N   THR A 349       7.353   7.089  27.241  1.00 23.82           N  
ANISOU 2493  N   THR A 349     2711   4377   1961    813   -215    365       N  
ATOM   2494  CA  THR A 349       6.350   6.712  26.271  1.00 20.99           C  
ANISOU 2494  CA  THR A 349     2392   3914   1668    870   -207    372       C  
ATOM   2495  CB  THR A 349       6.621   5.315  25.694  1.00 25.91           C  
ANISOU 2495  CB  THR A 349     2992   4504   2348    930   -224    409       C  
ATOM   2496  OG1 THR A 349       6.644   4.365  26.764  1.00 28.68           O  
ANISOU 2496  OG1 THR A 349     3322   4874   2701    923   -235    433       O  
ATOM   2497  CG2 THR A 349       7.962   5.284  24.979  1.00 33.17           C  
ANISOU 2497  CG2 THR A 349     3871   5467   3266    929   -231    408       C  
ATOM   2498  C   THR A 349       4.961   6.716  26.893  1.00 27.56           C  
ANISOU 2498  C   THR A 349     3271   4684   2517    868   -192    367       C  
ATOM   2499  O   THR A 349       3.981   6.623  26.168  1.00 25.07           O  
ANISOU 2499  O   THR A 349     2996   4274   2254    904   -179    364       O  
ATOM   2500  N   GLN A 350       4.891   6.810  28.223  1.00 26.84           N  
ANISOU 2500  N   GLN A 350     3171   4647   2380    827   -195    366       N  
ATOM   2501  CA  GLN A 350       3.612   6.864  28.965  1.00 27.02           C  
ANISOU 2501  CA  GLN A 350     3233   4622   2410    818   -181    361       C  
ATOM   2502  CB  GLN A 350       3.207   5.482  29.502  1.00 33.45           C  
ANISOU 2502  CB  GLN A 350     4034   5444   3233    877   -211    418       C  
ATOM   2503  CG  GLN A 350       3.153   4.329  28.527  1.00 40.00           C  
ANISOU 2503  CG  GLN A 350     4857   6190   4150    931   -215    440       C  
ATOM   2504  CD  GLN A 350       3.094   2.992  29.263  1.00 44.25           C  
ANISOU 2504  CD  GLN A 350     5372   6719   4720    938   -226    471       C  
ATOM   2505  OE1 GLN A 350       2.785   2.943  30.455  1.00 42.10           O  
ANISOU 2505  OE1 GLN A 350     5095   6485   4414    917   -231    481       O  
ATOM   2506  NE2 GLN A 350       3.395   1.908  28.558  1.00 41.44           N  
ANISOU 2506  NE2 GLN A 350     5006   6313   4429    962   -229    482       N  
ATOM   2507  C   GLN A 350       3.664   7.795  30.178  1.00 27.38           C  
ANISOU 2507  C   GLN A 350     3280   4723   2401    738   -166    325       C  
ATOM   2508  O   GLN A 350       4.743   8.076  30.705  1.00 26.81           O  
ANISOU 2508  O   GLN A 350     3168   4742   2278    698   -177    319       O  
ATOM   2509  N   ILE A 351       2.490   8.245  30.624  1.00 24.70           N  
ANISOU 2509  N   ILE A 351     2986   4328   2072    717   -143    303       N  
ATOM   2510  CA  ILE A 351       2.300   8.669  32.010  1.00 23.61           C  
ANISOU 2510  CA  ILE A 351     2846   4243   1883    662   -138    287       C  
ATOM   2511  CB  ILE A 351       1.574  10.028  32.125  1.00 21.62           C  
ANISOU 2511  CB  ILE A 351     2642   3942   1632    601    -99    225       C  
ATOM   2512  CG1 ILE A 351       2.494  11.160  31.671  1.00 27.35           C  
ANISOU 2512  CG1 ILE A 351     3357   4693   2340    546    -84    179       C  
ATOM   2513  CD1 ILE A 351       1.747  12.428  31.303  1.00 23.07           C  
ANISOU 2513  CD1 ILE A 351     2867   4077   1822    501    -45    122       C  
ATOM   2514  CG2 ILE A 351       1.103  10.282  33.577  1.00 23.48           C  
ANISOU 2514  CG2 ILE A 351     2881   4218   1821    557    -94    213       C  
ATOM   2515  C   ILE A 351       1.492   7.549  32.665  1.00 25.97           C  
ANISOU 2515  C   ILE A 351     3148   4530   2190    709   -156    334       C  
ATOM   2516  O   ILE A 351       0.299   7.374  32.379  1.00 29.68           O  
ANISOU 2516  O   ILE A 351     3660   4912   2704    739   -143    337       O  
ATOM   2517  N   ASN A 352       2.149   6.760  33.512  1.00 28.74           N  
ANISOU 2517  N   ASN A 352     3450   4968   2500    719   -186    374       N  
ATOM   2518  CA  ASN A 352       1.478   5.598  34.089  1.00 29.93           C  
ANISOU 2518  CA  ASN A 352     3597   5113   2661    768   -206    426       C  
ATOM   2519  CB  ASN A 352       2.373   4.347  33.994  1.00 27.77           C  
ANISOU 2519  CB  ASN A 352     3271   4859   2420    801   -232    467       C  
ATOM   2520  CG  ASN A 352       3.747   4.552  34.608  1.00 29.99           C  
ANISOU 2520  CG  ASN A 352     3501   5246   2646    757   -245    462       C  
ATOM   2521  OD1 ASN A 352       3.953   5.445  35.432  1.00 30.46           O  
ANISOU 2521  OD1 ASN A 352     3558   5377   2639    701   -239    435       O  
ATOM   2522  ND2 ASN A 352       4.699   3.713  34.214  1.00 33.31           N  
ANISOU 2522  ND2 ASN A 352     3881   5675   3098    779   -260    484       N  
ATOM   2523  C   ASN A 352       1.070   5.857  35.535  1.00 34.12           C  
ANISOU 2523  C   ASN A 352     4129   5692   3143    723   -201    418       C  
ATOM   2524  O   ASN A 352       1.324   6.932  36.075  1.00 32.69           O  
ANISOU 2524  O   ASN A 352     3951   5550   2921    655   -183    371       O  
ATOM   2525  N   GLU A 353       0.454   4.865  36.166  1.00 34.43           N  
ANISOU 2525  N   GLU A 353     4162   5716   3203    755   -214    459       N  
ATOM   2526  CA  GLU A 353      -0.043   5.041  37.526  1.00 39.22           C  
ANISOU 2526  CA  GLU A 353     4770   6364   3766    719   -209    456       C  
ATOM   2527  CB  GLU A 353      -0.880   3.832  37.942  1.00 46.45           C  
ANISOU 2527  CB  GLU A 353     5687   7227   4735    759   -218    500       C  
ATOM   2528  CG  GLU A 353      -2.082   3.572  37.031  1.00 51.45           C  
ANISOU 2528  CG  GLU A 353     6369   7744   5435    808   -206    506       C  
ATOM   2529  CD  GLU A 353      -3.039   4.756  36.945  1.00 61.19           C  
ANISOU 2529  CD  GLU A 353     7660   8949   6639    789   -179    468       C  
ATOM   2530  OE1 GLU A 353      -3.506   5.228  38.007  1.00 64.09           O  
ANISOU 2530  OE1 GLU A 353     8037   9345   6969    745   -166    450       O  
ATOM   2531  OE2 GLU A 353      -3.323   5.217  35.815  1.00 58.00           O  
ANISOU 2531  OE2 GLU A 353     7291   8465   6282    798   -160    440       O  
ATOM   2532  C   GLU A 353       1.095   5.281  38.521  1.00 32.95           C  
ANISOU 2532  C   GLU A 353     3927   5680   2911    665   -220    447       C  
ATOM   2533  O   GLU A 353       0.921   6.006  39.504  1.00 32.71           O  
ANISOU 2533  O   GLU A 353     3903   5701   2826    613   -209    420       O  
ATOM   2534  N   GLU A 354       2.261   4.694  38.253  1.00 29.61           N  
ANISOU 2534  N   GLU A 354     3459   5292   2502    676   -239    467       N  
ATOM   2535  CA  GLU A 354       3.437   4.891  39.090  1.00 29.97           C  
ANISOU 2535  CA  GLU A 354     3456   5437   2495    628   -249    460       C  
ATOM   2536  CB  GLU A 354       4.590   3.994  38.620  1.00 40.64           C  
ANISOU 2536  CB  GLU A 354     4761   6804   3877    656   -268    489       C  
ATOM   2537  CG  GLU A 354       4.353   2.503  38.828  1.00 48.44           C  
ANISOU 2537  CG  GLU A 354     5733   7752   4920    703   -281    537       C  
ATOM   2538  CD  GLU A 354       3.902   1.787  37.564  1.00 53.31           C  
ANISOU 2538  CD  GLU A 354     6372   8268   5615    761   -280    553       C  
ATOM   2539  OE1 GLU A 354       3.162   2.389  36.749  1.00 38.83           O  
ANISOU 2539  OE1 GLU A 354     4581   6375   3796    774   -267    533       O  
ATOM   2540  OE2 GLU A 354       4.294   0.612  37.387  1.00 57.51           O  
ANISOU 2540  OE2 GLU A 354     6882   8777   6193    790   -291    582       O  
ATOM   2541  C   GLU A 354       3.898   6.344  39.103  1.00 31.11           C  
ANISOU 2541  C   GLU A 354     3608   5634   2578    565   -233    404       C  
ATOM   2542  O   GLU A 354       4.321   6.870  40.133  1.00 32.82           O  
ANISOU 2542  O   GLU A 354     3805   5923   2741    510   -231    382       O  
ATOM   2543  N   MET A 355       3.830   6.985  37.945  1.00 32.75           N  
ANISOU 2543  N   MET A 355     3845   5801   2797    573   -221    379       N  
ATOM   2544  CA  MET A 355       4.199   8.385  37.841  1.00 25.34           C  
ANISOU 2544  CA  MET A 355     2920   4880   1828    506   -198    317       C  
ATOM   2545  CB  MET A 355       4.412   8.759  36.370  1.00 26.20           C  
ANISOU 2545  CB  MET A 355     3046   4922   1986    522   -185    298       C  
ATOM   2546  CG  MET A 355       5.632   8.057  35.785  1.00 28.56           C  
ANISOU 2546  CG  MET A 355     3297   5271   2283    556   -214    333       C  
ATOM   2547  SD  MET A 355       5.598   7.950  33.982  1.00 46.14           S  
ANISOU 2547  SD  MET A 355     5545   7404   4581    608   -207    334       S  
ATOM   2548  CE  MET A 355       5.937   9.640  33.536  1.00 26.87           C  
ANISOU 2548  CE  MET A 355     3125   4951   2132    532   -172    261       C  
ATOM   2549  C   MET A 355       3.150   9.278  38.504  1.00 29.16           C  
ANISOU 2549  C   MET A 355     3447   5329   2303    460   -168    272       C  
ATOM   2550  O   MET A 355       3.498  10.270  39.134  1.00 27.08           O  
ANISOU 2550  O   MET A 355     3180   5114   1995    392   -155    227       O  
ATOM   2551  N   LYS A 356       1.874   8.915  38.387  1.00 26.89           N  
ANISOU 2551  N   LYS A 356     3200   4960   2056    496   -158    286       N  
ATOM   2552  CA  LYS A 356       0.820   9.672  39.065  1.00 24.82           C  
ANISOU 2552  CA  LYS A 356     2979   4665   1785    456   -131    247       C  
ATOM   2553  CB  LYS A 356      -0.564   9.175  38.660  1.00 22.55           C  
ANISOU 2553  CB  LYS A 356     2737   4276   1555    506   -121    267       C  
ATOM   2554  CG  LYS A 356      -0.891   9.271  37.170  1.00 23.47           C  
ANISOU 2554  CG  LYS A 356     2888   4291   1740    541   -107    259       C  
ATOM   2555  CD  LYS A 356      -2.247   8.631  36.906  1.00 29.97           C  
ANISOU 2555  CD  LYS A 356     3751   5021   2616    595   -102    285       C  
ATOM   2556  CE  LYS A 356      -2.580   8.579  35.437  1.00 36.32           C  
ANISOU 2556  CE  LYS A 356     4586   5727   3489    637    -92    283       C  
ATOM   2557  NZ  LYS A 356      -3.942   8.001  35.251  1.00 38.49           N  
ANISOU 2557  NZ  LYS A 356     4900   5911   3813    686    -86    307       N  
ATOM   2558  C   LYS A 356       0.976   9.575  40.582  1.00 28.39           C  
ANISOU 2558  C   LYS A 356     3402   5213   2172    423   -142    255       C  
ATOM   2559  O   LYS A 356       0.842  10.566  41.285  1.00 31.91           O  
ANISOU 2559  O   LYS A 356     3860   5683   2581    362   -124    206       O  
ATOM   2560  N   LEU A 357       1.267   8.375  41.069  1.00 28.94           N  
ANISOU 2560  N   LEU A 357     3433   5336   2226    465   -174    316       N  
ATOM   2561  CA  LEU A 357       1.434   8.145  42.496  1.00 34.28           C  
ANISOU 2561  CA  LEU A 357     4078   6085   2861    437   -184    326       C  
ATOM   2562  CB  LEU A 357       1.573   6.652  42.790  1.00 29.41           C  
ANISOU 2562  CB  LEU A 357     3424   5469   2280    489   -211    393       C  
ATOM   2563  CG  LEU A 357       0.275   5.861  42.893  1.00 40.75           C  
ANISOU 2563  CG  LEU A 357     4889   6836   3759    537   -210    429       C  
ATOM   2564  CD1 LEU A 357       0.585   4.419  43.275  1.00 46.35           C  
ANISOU 2564  CD1 LEU A 357     5556   7552   4504    578   -235    488       C  
ATOM   2565  CD2 LEU A 357      -0.640   6.510  43.922  1.00 47.12           C  
ANISOU 2565  CD2 LEU A 357     5721   7653   4527    498   -191    402       C  
ATOM   2566  C   LEU A 357       2.652   8.891  43.022  1.00 37.02           C  
ANISOU 2566  C   LEU A 357     4388   6519   3158    373   -186    291       C  
ATOM   2567  O   LEU A 357       2.643   9.382  44.152  1.00 35.79           O  
ANISOU 2567  O   LEU A 357     4224   6414   2961    323   -180    266       O  
ATOM   2568  N   ALA A 358       3.700   8.972  42.200  1.00 30.81           N  
ANISOU 2568  N   ALA A 358     3579   5751   2378    375   -195    288       N  
ATOM   2569  CA  ALA A 358       4.909   9.689  42.585  1.00 29.26           C  
ANISOU 2569  CA  ALA A 358     3347   5632   2137    316   -197    255       C  
ATOM   2570  CB  ALA A 358       6.018   9.498  41.530  1.00 28.78           C  
ANISOU 2570  CB  ALA A 358     3259   5581   2094    335   -210    267       C  
ATOM   2571  C   ALA A 358       4.604  11.172  42.786  1.00 33.08           C  
ANISOU 2571  C   ALA A 358     3864   6119   2587    248   -169    185       C  
ATOM   2572  O   ALA A 358       5.132  11.808  43.702  1.00 34.73           O  
ANISOU 2572  O   ALA A 358     4052   6390   2755    189   -167    153       O  
ATOM   2573  N   ALA A 359       3.744  11.718  41.927  1.00 27.23           N  
ANISOU 2573  N   ALA A 359     3176   5292   1880    255   -144    157       N  
ATOM   2574  CA  ALA A 359       3.315  13.102  42.043  1.00 26.04           C  
ANISOU 2574  CA  ALA A 359     3062   5109   1724    192   -112     87       C  
ATOM   2575  CB  ALA A 359       2.473  13.505  40.823  1.00 27.78           C  
ANISOU 2575  CB  ALA A 359     3336   5206   2014    211    -86     66       C  
ATOM   2576  C   ALA A 359       2.526  13.326  43.345  1.00 29.25           C  
ANISOU 2576  C   ALA A 359     3480   5541   2091    163   -104     71       C  
ATOM   2577  O   ALA A 359       2.723  14.331  44.026  1.00 31.51           O  
ANISOU 2577  O   ALA A 359     3766   5869   2336     98    -92     20       O  
ATOM   2578  N   VAL A 360       1.645  12.380  43.681  1.00 28.09           N  
ANISOU 2578  N   VAL A 360     3343   5371   1959    212   -111    117       N  
ATOM   2579  CA  VAL A 360       0.840  12.464  44.905  1.00 24.98           C  
ANISOU 2579  CA  VAL A 360     2960   4999   1532    192   -105    110       C  
ATOM   2580  CB  VAL A 360      -0.094  11.243  45.062  1.00 26.08           C  
ANISOU 2580  CB  VAL A 360     3108   5100   1702    257   -116    171       C  
ATOM   2581  CG1 VAL A 360      -0.773  11.266  46.437  1.00 23.50           C  
ANISOU 2581  CG1 VAL A 360     2781   4797   1349    234   -111    168       C  
ATOM   2582  CG2 VAL A 360      -1.135  11.214  43.945  1.00 29.68           C  
ANISOU 2582  CG2 VAL A 360     3617   5434   2227    297    -96    171       C  
ATOM   2583  C   VAL A 360       1.720  12.561  46.145  1.00 31.42           C  
ANISOU 2583  C   VAL A 360     3727   5906   2305    147   -119    104       C  
ATOM   2584  O   VAL A 360       1.541  13.447  46.984  1.00 29.83           O  
ANISOU 2584  O   VAL A 360     3534   5728   2073     91   -104     57       O  
ATOM   2585  N   HIS A 361       2.683  11.652  46.251  1.00 32.35           N  
ANISOU 2585  N   HIS A 361     3794   6074   2424    172   -147    152       N  
ATOM   2586  CA  HIS A 361       3.543  11.599  47.428  1.00 34.80           C  
ANISOU 2586  CA  HIS A 361     4055   6472   2697    137   -162    153       C  
ATOM   2587  CB  HIS A 361       4.364  10.313  47.416  1.00 33.73           C  
ANISOU 2587  CB  HIS A 361     3869   6371   2577    183   -192    217       C  
ATOM   2588  CG  HIS A 361       3.547   9.089  47.687  1.00 36.77           C  
ANISOU 2588  CG  HIS A 361     4256   6724   2991    241   -202    276       C  
ATOM   2589  ND1 HIS A 361       2.979   8.832  48.915  1.00 43.04           N  
ANISOU 2589  ND1 HIS A 361     5044   7543   3767    233   -202    287       N  
ATOM   2590  CE1 HIS A 361       2.308   7.695  48.859  1.00 43.22           C  
ANISOU 2590  CE1 HIS A 361     5070   7526   3827    291   -212    342       C  
ATOM   2591  NE2 HIS A 361       2.414   7.209  47.636  1.00 36.00           N  
ANISOU 2591  NE2 HIS A 361     4163   6559   2956    337   -219    365       N  
ATOM   2592  CD2 HIS A 361       3.182   8.063  46.881  1.00 42.52           C  
ANISOU 2592  CD2 HIS A 361     4991   7395   3770    308   -213    325       C  
ATOM   2593  C   HIS A 361       4.454  12.814  47.517  1.00 32.48           C  
ANISOU 2593  C   HIS A 361     3748   6223   2369     69   -153     94       C  
ATOM   2594  O   HIS A 361       4.706  13.324  48.607  1.00 37.79           O  
ANISOU 2594  O   HIS A 361     4404   6950   3005     21   -152     66       O  
ATOM   2595  N   ALA A 362       4.940  13.283  46.369  1.00 30.06           N  
ANISOU 2595  N   ALA A 362     3452   5894   2077     65   -148     74       N  
ATOM   2596  CA  ALA A 362       5.823  14.448  46.347  1.00 33.46           C  
ANISOU 2596  CA  ALA A 362     3871   6362   2481      0   -140     18       C  
ATOM   2597  CB  ALA A 362       6.447  14.625  44.960  1.00 27.24           C  
ANISOU 2597  CB  ALA A 362     3085   5551   1716     13   -140     14       C  
ATOM   2598  C   ALA A 362       5.071  15.712  46.763  1.00 34.86           C  
ANISOU 2598  C   ALA A 362     4088   6513   2643    -56   -112    -50       C  
ATOM   2599  O   ALA A 362       5.600  16.533  47.512  1.00 31.36           O  
ANISOU 2599  O   ALA A 362     3628   6119   2168   -115   -109    -92       O  
ATOM   2600  N   LEU A 363       3.837  15.856  46.280  1.00 32.35           N  
ANISOU 2600  N   LEU A 363     3824   6117   2350    -36    -91    -60       N  
ATOM   2601  CA  LEU A 363       2.990  16.986  46.651  1.00 26.17           C  
ANISOU 2601  CA  LEU A 363     3084   5299   1561    -85    -62   -123       C  
ATOM   2602  CB  LEU A 363       1.657  16.958  45.893  1.00 26.98           C  
ANISOU 2602  CB  LEU A 363     3245   5307   1699    -50    -40   -125       C  
ATOM   2603  CG  LEU A 363       1.675  17.463  44.451  1.00 31.28           C  
ANISOU 2603  CG  LEU A 363     3819   5768   2297    -45    -23   -146       C  
ATOM   2604  CD1 LEU A 363       0.321  17.183  43.795  1.00 30.67           C  
ANISOU 2604  CD1 LEU A 363     3795   5576   2281      1     -4   -134       C  
ATOM   2605  CD2 LEU A 363       2.017  18.949  44.399  1.00 29.30           C  
ANISOU 2605  CD2 LEU A 363     3581   5517   2036   -118     -2   -221       C  
ATOM   2606  C   LEU A 363       2.728  16.975  48.143  1.00 32.55           C  
ANISOU 2606  C   LEU A 363     3877   6153   2338   -108    -66   -127       C  
ATOM   2607  O   LEU A 363       2.798  18.008  48.802  1.00 33.33           O  
ANISOU 2607  O   LEU A 363     3979   6271   2414   -168    -54   -182       O  
ATOM   2608  N   ALA A 364       2.425  15.794  48.665  1.00 31.59           N  
ANISOU 2608  N   ALA A 364     3738   6048   2217    -61    -84    -67       N  
ATOM   2609  CA  ALA A 364       2.111  15.641  50.080  1.00 34.69           C  
ANISOU 2609  CA  ALA A 364     4115   6484   2582    -76    -88    -62       C  
ATOM   2610  CB  ALA A 364       1.668  14.221  50.377  1.00 33.91           C  
ANISOU 2610  CB  ALA A 364     4001   6386   2496    -13   -106     11       C  
ATOM   2611  C   ALA A 364       3.327  16.011  50.922  1.00 31.80           C  
ANISOU 2611  C   ALA A 364     3699   6208   2177   -123   -102    -80       C  
ATOM   2612  O   ALA A 364       3.218  16.733  51.914  1.00 41.68           O  
ANISOU 2612  O   ALA A 364     4948   7489   3400   -170    -93   -121       O  
ATOM   2613  N   LYS A 365       4.487  15.525  50.507  1.00 30.73           N  
ANISOU 2613  N   LYS A 365     3522   6113   2042   -110   -122    -51       N  
ATOM   2614  CA  LYS A 365       5.710  15.776  51.258  1.00 39.26           C  
ANISOU 2614  CA  LYS A 365     4550   7279   3086   -150   -136    -63       C  
ATOM   2615  CB  LYS A 365       6.851  14.911  50.726  1.00 38.35           C  
ANISOU 2615  CB  LYS A 365     4391   7200   2980   -117   -160    -14       C  
ATOM   2616  CG  LYS A 365       7.406  13.949  51.765  1.00 56.42           C  
ANISOU 2616  CG  LYS A 365     6627   9560   5249   -101   -183     34       C  
ATOM   2617  CD  LYS A 365       8.721  13.344  51.313  1.00 64.04           C  
ANISOU 2617  CD  LYS A 365     7545  10569   6219    -84   -204     68       C  
ATOM   2618  CE  LYS A 365       9.828  14.387  51.304  1.00 69.03           C  
ANISOU 2618  CE  LYS A 365     8156  11248   6824   -143   -202     19       C  
ATOM   2619  NZ  LYS A 365      10.023  15.000  52.652  1.00 68.32           N  
ANISOU 2619  NZ  LYS A 365     8046  11220   6692   -196   -200    -14       N  
ATOM   2620  C   LYS A 365       6.104  17.253  51.227  1.00 40.19           C  
ANISOU 2620  C   LYS A 365     4680   7404   3188   -219   -120   -137       C  
ATOM   2621  O   LYS A 365       6.652  17.774  52.203  1.00 36.96           O  
ANISOU 2621  O   LYS A 365     4242   7055   2745   -265   -123   -165       O  
ATOM   2622  N   LEU A 366       5.814  17.933  50.120  1.00 33.62           N  
ANISOU 2622  N   LEU A 366     3887   6507   2381   -227   -101   -170       N  
ATOM   2623  CA  LEU A 366       6.177  19.341  50.002  1.00 34.26           C  
ANISOU 2623  CA  LEU A 366     3978   6586   2452   -293    -85   -241       C  
ATOM   2624  CB  LEU A 366       5.933  19.853  48.576  1.00 32.32           C  
ANISOU 2624  CB  LEU A 366     3773   6267   2241   -289    -68   -264       C  
ATOM   2625  CG  LEU A 366       6.183  21.347  48.344  1.00 32.03           C  
ANISOU 2625  CG  LEU A 366     3753   6215   2203   -357    -48   -338       C  
ATOM   2626  CD1 LEU A 366       7.564  21.763  48.842  1.00 36.99           C  
ANISOU 2626  CD1 LEU A 366     4329   6925   2799   -402    -64   -354       C  
ATOM   2627  CD2 LEU A 366       6.017  21.723  46.874  1.00 36.81           C  
ANISOU 2627  CD2 LEU A 366     4392   6749   2843   -348    -32   -354       C  
ATOM   2628  C   LEU A 366       5.415  20.205  51.012  1.00 36.08           C  
ANISOU 2628  C   LEU A 366     4232   6811   2666   -337    -68   -292       C  
ATOM   2629  O   LEU A 366       5.971  21.159  51.559  1.00 39.60           O  
ANISOU 2629  O   LEU A 366     4663   7293   3089   -394    -65   -340       O  
ATOM   2630  N   ALA A 367       4.154  19.862  51.266  1.00 30.82           N  
ANISOU 2630  N   ALA A 367     3600   6097   2011   -308    -57   -280       N  
ATOM   2631  CA  ALA A 367       3.322  20.629  52.189  1.00 37.07           C  
ANISOU 2631  CA  ALA A 367     4418   6877   2791   -344    -40   -325       C  
ATOM   2632  CB  ALA A 367       1.884  20.133  52.135  1.00 30.49           C  
ANISOU 2632  CB  ALA A 367     3628   5979   1980   -302    -27   -304       C  
ATOM   2633  C   ALA A 367       3.843  20.569  53.626  1.00 39.41           C  
ANISOU 2633  C   ALA A 367     4669   7260   3045   -369    -55   -324       C  
ATOM   2634  O   ALA A 367       3.586  21.474  54.427  1.00 40.40           O  
ANISOU 2634  O   ALA A 367     4802   7395   3153   -414    -44   -375       O  
ATOM   2635  N   ARG A 368       4.570  19.505  53.954  1.00 35.92           N  
ANISOU 2635  N   ARG A 368     4179   6880   2588   -338    -81   -267       N  
ATOM   2636  CA  ARG A 368       5.116  19.356  55.308  1.00 41.27           C  
ANISOU 2636  CA  ARG A 368     4810   7643   3226   -358    -95   -261       C  
ATOM   2637  CB  ARG A 368       5.518  17.905  55.567  1.00 40.82           C  
ANISOU 2637  CB  ARG A 368     4712   7632   3166   -307   -120   -184       C  
ATOM   2638  CG  ARG A 368       4.349  16.953  55.575  1.00 44.61           C  
ANISOU 2638  CG  ARG A 368     5217   8067   3667   -251   -119   -137       C  
ATOM   2639  CD  ARG A 368       4.791  15.546  55.912  1.00 52.19           C  
ANISOU 2639  CD  ARG A 368     6132   9073   4624   -203   -144    -63       C  
ATOM   2640  NE  ARG A 368       3.642  14.659  56.054  1.00 64.70           N  
ANISOU 2640  NE  ARG A 368     7737  10617   6227   -154   -143    -19       N  
ATOM   2641  CZ  ARG A 368       3.728  13.368  56.349  1.00 79.59           C  
ANISOU 2641  CZ  ARG A 368     9593  12527   8120   -106   -162     48       C  
ATOM   2642  NH1 ARG A 368       4.916  12.806  56.533  1.00 84.34           N  
ANISOU 2642  NH1 ARG A 368    10142  13193   8712   -101   -183     78       N  
ATOM   2643  NH2 ARG A 368       2.626  12.638  56.456  1.00 83.58           N  
ANISOU 2643  NH2 ARG A 368    10120  12991   8645    -63   -160     85       N  
ATOM   2644  C   ARG A 368       6.308  20.267  55.577  1.00 46.98           C  
ANISOU 2644  C   ARG A 368     5501   8425   3925   -417   -100   -305       C  
ATOM   2645  O   ARG A 368       6.576  20.621  56.723  1.00 49.67           O  
ANISOU 2645  O   ARG A 368     5816   8823   4233   -450   -103   -327       O  
ATOM   2646  N   GLU A 369       7.027  20.637  54.522  1.00 48.53           N  
ANISOU 2646  N   GLU A 369     5697   8606   4137   -428    -99   -319       N  
ATOM   2647  CA  GLU A 369       8.173  21.535  54.640  1.00 53.82           C  
ANISOU 2647  CA  GLU A 369     6337   9324   4787   -484   -103   -361       C  
ATOM   2648  CB  GLU A 369       8.891  21.644  53.296  1.00 56.51           C  
ANISOU 2648  CB  GLU A 369     6678   9643   5151   -480   -104   -358       C  
ATOM   2649  CG  GLU A 369       9.383  20.324  52.756  1.00 57.88           C  
ANISOU 2649  CG  GLU A 369     6824   9833   5334   -421   -125   -286       C  
ATOM   2650  CD  GLU A 369      10.681  19.899  53.403  1.00 61.94           C  
ANISOU 2650  CD  GLU A 369     7276  10441   5819   -430   -148   -261       C  
ATOM   2651  OE1 GLU A 369      11.546  20.775  53.614  1.00 59.63           O  
ANISOU 2651  OE1 GLU A 369     6962  10189   5507   -483   -148   -303       O  
ATOM   2652  OE2 GLU A 369      10.830  18.697  53.709  1.00 65.60           O  
ANISOU 2652  OE2 GLU A 369     7711  10934   6280   -384   -165   -201       O  
ATOM   2653  C   GLU A 369       7.780  22.932  55.113  1.00 53.28           C  
ANISOU 2653  C   GLU A 369     6295   9239   4712   -544    -83   -436       C  
ATOM   2654  O   GLU A 369       6.628  23.341  54.963  1.00 45.53           O  
ANISOU 2654  O   GLU A 369     5362   8188   3749   -543    -63   -462       O  
ATOM   2655  N   ASP A 370       8.749  23.656  55.672  1.00 53.25           N  
ANISOU 2655  N   ASP A 370     6256   9296   4681   -595    -89   -472       N  
ATOM   2656  CA  ASP A 370       8.565  25.062  56.023  1.00 57.24           C  
ANISOU 2656  CA  ASP A 370     6781   9786   5182   -656    -72   -546       C  
ATOM   2657  CB  ASP A 370       9.843  25.652  56.625  1.00 62.22           C  
ANISOU 2657  CB  ASP A 370     7363  10496   5782   -706    -84   -573       C  
ATOM   2658  CG  ASP A 370      10.144  25.112  58.007  1.00 75.74           C  
ANISOU 2658  CG  ASP A 370     9033  12291   7455   -703    -99   -551       C  
ATOM   2659  OD1 ASP A 370       9.237  24.517  58.629  1.00 79.23           O  
ANISOU 2659  OD1 ASP A 370     9487  12725   7892   -672    -98   -527       O  
ATOM   2660  OD2 ASP A 370      11.291  25.290  58.475  1.00 80.45           O  
ANISOU 2660  OD2 ASP A 370     9582  12960   8024   -732   -113   -557       O  
ATOM   2661  C   ASP A 370       8.166  25.868  54.796  1.00 58.44           C  
ANISOU 2661  C   ASP A 370     6980   9853   5373   -670    -51   -584       C  
ATOM   2662  O   ASP A 370       8.688  25.647  53.703  1.00 56.90           O  
ANISOU 2662  O   ASP A 370     6782   9641   5196   -655    -55   -566       O  
ATOM   2663  N   VAL A 371       7.244  26.805  54.978  1.00 57.19           N  
ANISOU 2663  N   VAL A 371     6863   9640   5228   -697    -30   -637       N  
ATOM   2664  CA  VAL A 371       6.818  27.669  53.888  1.00 61.45           C  
ANISOU 2664  CA  VAL A 371     7447  10095   5806   -715     -8   -678       C  
ATOM   2665  CB  VAL A 371       5.348  28.085  54.046  1.00 59.68           C  
ANISOU 2665  CB  VAL A 371     7278   9793   5604   -712     16   -707       C  
ATOM   2666  CG1 VAL A 371       4.982  29.139  53.018  1.00 55.60           C  
ANISOU 2666  CG1 VAL A 371     6805   9192   5128   -739     39   -757       C  
ATOM   2667  CG2 VAL A 371       4.444  26.868  53.926  1.00 55.89           C  
ANISOU 2667  CG2 VAL A 371     6816   9286   5132   -646     14   -649       C  
ATOM   2668  C   VAL A 371       7.696  28.913  53.809  1.00 65.92           C  
ANISOU 2668  C   VAL A 371     7998  10678   6369   -780     -5   -736       C  
ATOM   2669  O   VAL A 371       7.747  29.697  54.755  1.00 68.86           O  
ANISOU 2669  O   VAL A 371     8362  11079   6724   -823     -3   -780       O  
ATOM   2670  N   PRO A 372       8.390  29.094  52.672  1.00 66.79           N  
ANISOU 2670  N   PRO A 372     8106  10774   6498   -787     -5   -736       N  
ATOM   2671  CA  PRO A 372       9.341  30.185  52.433  1.00 67.66           C  
ANISOU 2671  CA  PRO A 372     8198  10902   6608   -846     -5   -784       C  
ATOM   2672  CB  PRO A 372       9.808  29.941  50.990  1.00 63.50           C  
ANISOU 2672  CB  PRO A 372     7675  10346   6105   -827     -5   -762       C  
ATOM   2673  CG  PRO A 372       9.496  28.515  50.716  1.00 64.29           C  
ANISOU 2673  CG  PRO A 372     7775  10447   6207   -757    -15   -691       C  
ATOM   2674  CD  PRO A 372       8.248  28.230  51.490  1.00 68.27           C  
ANISOU 2674  CD  PRO A 372     8308  10922   6710   -734     -6   -688       C  
ATOM   2675  C   PRO A 372       8.705  31.564  52.559  1.00 70.70           C  
ANISOU 2675  C   PRO A 372     8620  11230   7014   -895     18   -856       C  
ATOM   2676  O   PRO A 372       7.481  31.684  52.507  1.00 69.13           O  
ANISOU 2676  O   PRO A 372     8466  10960   6839   -880     37   -868       O  
ATOM   2677  N   ASP A 373       9.541  32.587  52.709  1.00 74.70           N  
ANISOU 2677  N   ASP A 373     9104  11764   7514   -953     17   -902       N  
ATOM   2678  CA  ASP A 373       9.069  33.958  52.878  1.00 78.99           C  
ANISOU 2678  CA  ASP A 373     9676  12258   8079  -1005     37   -972       C  
ATOM   2679  CB  ASP A 373      10.263  34.913  53.049  1.00 82.56           C  
ANISOU 2679  CB  ASP A 373    10092  12759   8518  -1066     29  -1013       C  
ATOM   2680  CG  ASP A 373      10.940  34.773  54.407  1.00 86.14           C  
ANISOU 2680  CG  ASP A 373    10497  13309   8924  -1082     10  -1011       C  
ATOM   2681  OD1 ASP A 373      10.328  34.181  55.318  1.00 84.79           O  
ANISOU 2681  OD1 ASP A 373    10327  13158   8732  -1055      7   -992       O  
ATOM   2682  OD2 ASP A 373      12.081  35.263  54.564  1.00 87.88           O  
ANISOU 2682  OD2 ASP A 373    10678  13585   9126  -1123     -1  -1030       O  
ATOM   2683  C   ASP A 373       8.189  34.441  51.726  1.00 76.76           C  
ANISOU 2683  C   ASP A 373     9449  11867   7848  -1000     61   -993       C  
ATOM   2684  O   ASP A 373       7.115  34.994  51.948  1.00 73.04           O  
ANISOU 2684  O   ASP A 373     9018  11333   7400  -1006     80  -1025       O  
ATOM   2685  N   LYS A 374       8.639  34.221  50.495  1.00 79.97           N  
ANISOU 2685  N   LYS A 374     9857  12252   8274   -987     62   -973       N  
ATOM   2686  CA  LYS A 374       7.971  34.833  49.346  1.00 80.16           C  
ANISOU 2686  CA  LYS A 374     9930  12177   8349   -991     86   -998       C  
ATOM   2687  CB  LYS A 374       8.887  34.814  48.118  1.00 83.46           C  
ANISOU 2687  CB  LYS A 374    10334  12597   8779   -994     82   -985       C  
ATOM   2688  CG  LYS A 374       8.165  34.898  46.778  1.00 85.52           C  
ANISOU 2688  CG  LYS A 374    10642  12761   9089   -973    104   -985       C  
ATOM   2689  CD  LYS A 374       8.929  35.761  45.777  1.00 89.26           C  
ANISOU 2689  CD  LYS A 374    11112  13218   9586  -1014    110  -1014       C  
ATOM   2690  CE  LYS A 374       8.696  35.308  44.346  1.00 89.05           C  
ANISOU 2690  CE  LYS A 374    11111  13134   9591   -975    121   -986       C  
ATOM   2691  NZ  LYS A 374       7.463  35.930  43.780  1.00 88.57           N  
ANISOU 2691  NZ  LYS A 374    11109  12960   9582   -975    151  -1017       N  
ATOM   2692  C   LYS A 374       6.620  34.172  49.045  1.00 75.22           C  
ANISOU 2692  C   LYS A 374     9352  11479   7748   -937    100   -972       C  
ATOM   2693  O   LYS A 374       5.726  34.820  48.485  1.00 74.34           O  
ANISOU 2693  O   LYS A 374     9288  11277   7679   -943    125  -1003       O  
ATOM   2694  N   VAL A 375       6.446  32.912  49.443  1.00 72.37           N  
ANISOU 2694  N   VAL A 375     8979  11158   7362   -885     86   -916       N  
ATOM   2695  CA  VAL A 375       5.125  32.290  49.358  1.00 69.85           C  
ANISOU 2695  CA  VAL A 375     8703  10777   7062   -835     99   -892       C  
ATOM   2696  CB  VAL A 375       5.127  30.826  49.824  1.00 68.78           C  
ANISOU 2696  CB  VAL A 375     8544  10696   6895   -778     79   -825       C  
ATOM   2697  CG1 VAL A 375       3.714  30.247  49.756  1.00 66.20           C  
ANISOU 2697  CG1 VAL A 375     8262  10302   6588   -730     93   -803       C  
ATOM   2698  CG2 VAL A 375       6.077  29.994  48.987  1.00 67.95           C  
ANISOU 2698  CG2 VAL A 375     8408  10626   6783   -749     62   -775       C  
ATOM   2699  C   VAL A 375       4.138  33.081  50.208  1.00 65.89           C  
ANISOU 2699  C   VAL A 375     8231  10237   6569   -860    115   -938       C  
ATOM   2700  O   VAL A 375       3.037  33.407  49.755  1.00 64.29           O  
ANISOU 2700  O   VAL A 375     8078   9945   6405   -850    138   -955       O  
ATOM   2701  N   SER A 376       4.545  33.381  51.440  1.00 66.86           N  
ANISOU 2701  N   SER A 376     8320  10428   6656   -891    103   -957       N  
ATOM   2702  CA  SER A 376       3.774  34.255  52.312  1.00 65.18           C  
ANISOU 2702  CA  SER A 376     8129  10190   6448   -920    116  -1005       C  
ATOM   2703  CB  SER A 376       4.481  34.454  53.655  1.00 65.78           C  
ANISOU 2703  CB  SER A 376     8158  10358   6477   -952     98  -1020       C  
ATOM   2704  OG  SER A 376       4.620  33.229  54.353  1.00 71.29           O  
ANISOU 2704  OG  SER A 376     8827  11126   7136   -912     79   -965       O  
ATOM   2705  C   SER A 376       3.553  35.597  51.626  1.00 63.45           C  
ANISOU 2705  C   SER A 376     7942   9892   6275   -964    138  -1064       C  
ATOM   2706  O   SER A 376       2.437  36.118  51.608  1.00 57.05           O  
ANISOU 2706  O   SER A 376     7175   9005   5497   -963    158  -1090       O  
ATOM   2707  N   ALA A 377       4.624  36.141  51.052  1.00 69.43           N  
ANISOU 2707  N   ALA A 377     8676  10669   7036  -1000    133  -1082       N  
ATOM   2708  CA  ALA A 377       4.560  37.415  50.342  1.00 72.33           C  
ANISOU 2708  CA  ALA A 377     9068  10966   7447  -1043    152  -1135       C  
ATOM   2709  CB  ALA A 377       5.942  37.812  49.838  1.00 67.87           C  
ANISOU 2709  CB  ALA A 377     8466  10447   6875  -1081    141  -1145       C  
ATOM   2710  C   ALA A 377       3.564  37.359  49.184  1.00 72.71           C  
ANISOU 2710  C   ALA A 377     9170  10909   7548  -1012    175  -1127       C  
ATOM   2711  O   ALA A 377       2.781  38.288  48.985  1.00 68.78           O  
ANISOU 2711  O   ALA A 377     8710  10331   7093  -1032    196  -1167       O  
ATOM   2712  N   THR A 378       3.591  36.262  48.432  1.00 73.38           N  
ANISOU 2712  N   THR A 378     9257  10992   7631   -963    170  -1075       N  
ATOM   2713  CA  THR A 378       2.677  36.077  47.309  1.00 71.94           C  
ANISOU 2713  CA  THR A 378     9124  10714   7497   -928    191  -1063       C  
ATOM   2714  CB  THR A 378       2.972  34.760  46.555  1.00 69.39           C  
ANISOU 2714  CB  THR A 378     8792  10413   7162   -873    180  -1000       C  
ATOM   2715  OG1 THR A 378       4.342  34.745  46.133  1.00 69.16           O  
ANISOU 2715  OG1 THR A 378     8719  10445   7112   -892    164   -992       O  
ATOM   2716  CG2 THR A 378       2.072  34.616  45.337  1.00 68.95           C  
ANISOU 2716  CG2 THR A 378     8785  10255   7156   -838    203   -990       C  
ATOM   2717  C   THR A 378       1.220  36.086  47.773  1.00 73.50           C  
ANISOU 2717  C   THR A 378     9365  10847   7714   -905    207  -1069       C  
ATOM   2718  O   THR A 378       0.342  36.601  47.079  1.00 77.77           O  
ANISOU 2718  O   THR A 378     9951  11291   8305   -902    231  -1088       O  
ATOM   2719  N   TYR A 379       0.969  35.538  48.957  1.00 68.80           N  
ANISOU 2719  N   TYR A 379     8754  10306   7080   -890    195  -1052       N  
ATOM   2720  CA  TYR A 379      -0.394  35.433  49.469  1.00 66.94           C  
ANISOU 2720  CA  TYR A 379     8557  10020   6858   -865    208  -1053       C  
ATOM   2721  CB  TYR A 379      -0.671  33.998  49.924  1.00 61.57           C  
ANISOU 2721  CB  TYR A 379     7866   9385   6144   -808    194   -993       C  
ATOM   2722  CG  TYR A 379      -0.758  33.017  48.777  1.00 58.06           C  
ANISOU 2722  CG  TYR A 379     7435   8909   5715   -757    195   -944       C  
ATOM   2723  CD1 TYR A 379      -1.982  32.705  48.199  1.00 54.31           C  
ANISOU 2723  CD1 TYR A 379     7010   8347   5278   -717    214   -930       C  
ATOM   2724  CE1 TYR A 379      -2.069  31.814  47.143  1.00 54.69           C  
ANISOU 2724  CE1 TYR A 379     7071   8367   5342   -669    216   -886       C  
ATOM   2725  CZ  TYR A 379      -0.920  31.224  46.648  1.00 51.42           C  
ANISOU 2725  CZ  TYR A 379     6618   8012   4906   -659    198   -854       C  
ATOM   2726  OH  TYR A 379      -1.005  30.333  45.595  1.00 46.96           O  
ANISOU 2726  OH  TYR A 379     6065   7420   4358   -609    199   -810       O  
ATOM   2727  CE2 TYR A 379       0.308  31.520  47.204  1.00 52.18           C  
ANISOU 2727  CE2 TYR A 379     6665   8195   4966   -699    178   -866       C  
ATOM   2728  CD2 TYR A 379       0.384  32.413  48.262  1.00 58.96           C  
ANISOU 2728  CD2 TYR A 379     7512   9081   5809   -748    177   -911       C  
ATOM   2729  C   TYR A 379      -0.687  36.419  50.607  1.00 73.93           C  
ANISOU 2729  C   TYR A 379     9440  10914   7736   -906    212  -1102       C  
ATOM   2730  O   TYR A 379      -1.342  36.073  51.591  1.00 71.08           O  
ANISOU 2730  O   TYR A 379     9082  10573   7353   -889    209  -1094       O  
ATOM   2731  N   GLY A 380      -0.196  37.646  50.461  1.00 79.37           N  
ANISOU 2731  N   GLY A 380    10125  11590   8444   -961    218  -1153       N  
ATOM   2732  CA  GLY A 380      -0.552  38.736  51.355  1.00 78.58           C  
ANISOU 2732  CA  GLY A 380    10029  11480   8348  -1000    224  -1204       C  
ATOM   2733  C   GLY A 380      -0.017  38.665  52.773  1.00 77.82           C  
ANISOU 2733  C   GLY A 380     9889  11483   8195  -1020    205  -1211       C  
ATOM   2734  O   GLY A 380      -0.657  39.155  53.703  1.00 80.85           O  
ANISOU 2734  O   GLY A 380    10281  11862   8575  -1031    210  -1239       O  
ATOM   2735  N   GLY A 381       1.156  38.063  52.945  1.00 75.38           N  
ANISOU 2735  N   GLY A 381     9533  11263   7844  -1022    183  -1186       N  
ATOM   2736  CA  GLY A 381       1.793  38.010  54.251  1.00 76.10           C  
ANISOU 2736  CA  GLY A 381     9580  11453   7883  -1042    164  -1192       C  
ATOM   2737  C   GLY A 381       1.196  36.969  55.180  1.00 76.48           C  
ANISOU 2737  C   GLY A 381     9622  11541   7895   -999    155  -1153       C  
ATOM   2738  O   GLY A 381       1.528  36.918  56.366  1.00 75.98           O  
ANISOU 2738  O   GLY A 381     9526  11554   7790  -1012    141  -1158       O  
ATOM   2739  N   LYS A 382       0.311  36.141  54.635  1.00 75.01           N  
ANISOU 2739  N   LYS A 382     9469  11303   7727   -948    163  -1113       N  
ATOM   2740  CA  LYS A 382      -0.312  35.049  55.378  1.00 71.89           C  
ANISOU 2740  CA  LYS A 382     9072  10939   7302   -902    155  -1069       C  
ATOM   2741  CB  LYS A 382      -1.447  34.437  54.555  1.00 71.52           C  
ANISOU 2741  CB  LYS A 382     9074  10809   7292   -852    171  -1037       C  
ATOM   2742  CG  LYS A 382      -2.433  33.596  55.344  1.00 74.67           C  
ANISOU 2742  CG  LYS A 382     9483  11216   7672   -809    170  -1004       C  
ATOM   2743  CD  LYS A 382      -3.735  33.432  54.567  1.00 75.28           C  
ANISOU 2743  CD  LYS A 382     9617  11190   7795   -773    191   -994       C  
ATOM   2744  CE  LYS A 382      -4.852  32.878  55.438  1.00 75.72           C  
ANISOU 2744  CE  LYS A 382     9689  11245   7837   -740    194   -973       C  
ATOM   2745  NZ  LYS A 382      -6.194  33.218  54.888  1.00 75.96           N  
ANISOU 2745  NZ  LYS A 382     9778  11168   7916   -722    219   -986       N  
ATOM   2746  C   LYS A 382       0.718  33.978  55.728  1.00 69.46           C  
ANISOU 2746  C   LYS A 382     8712  10731   6947   -884    129  -1019       C  
ATOM   2747  O   LYS A 382       1.483  33.545  54.865  1.00 71.87           O  
ANISOU 2747  O   LYS A 382     9003  11047   7256   -874    121   -992       O  
ATOM   2748  N   SER A 383       0.746  33.547  56.985  1.00 65.33           N  
ANISOU 2748  N   SER A 383     8161  10281   6382   -878    115  -1005       N  
ATOM   2749  CA  SER A 383       1.697  32.517  57.388  1.00 64.27           C  
ANISOU 2749  CA  SER A 383     7976  10240   6204   -859     90   -955       C  
ATOM   2750  CB  SER A 383       2.226  32.781  58.798  1.00 66.58           C  
ANISOU 2750  CB  SER A 383     8225  10620   6451   -890     76   -974       C  
ATOM   2751  OG  SER A 383       1.216  32.586  59.765  1.00 68.05           O  
ANISOU 2751  OG  SER A 383     8425  10807   6624   -872     81   -972       O  
ATOM   2752  C   SER A 383       1.066  31.131  57.311  1.00 68.00           C  
ANISOU 2752  C   SER A 383     8456  10709   6672   -795     85   -888       C  
ATOM   2753  O   SER A 383      -0.039  30.907  57.802  1.00 73.19           O  
ANISOU 2753  O   SER A 383     9139  11338   7331   -772     94   -882       O  
ATOM   2754  N   PHE A 384       1.779  30.207  56.676  1.00 64.50           N  
ANISOU 2754  N   PHE A 384     7991  10294   6224   -766     70   -838       N  
ATOM   2755  CA  PHE A 384       1.311  28.838  56.540  1.00 60.20           C  
ANISOU 2755  CA  PHE A 384     7448   9749   5676   -704     62   -770       C  
ATOM   2756  CB  PHE A 384       1.214  28.433  55.066  1.00 60.15           C  
ANISOU 2756  CB  PHE A 384     7469   9679   5708   -672     69   -744       C  
ATOM   2757  CG  PHE A 384       0.400  29.370  54.228  1.00 63.24           C  
ANISOU 2757  CG  PHE A 384     7915   9969   6145   -687     96   -790       C  
ATOM   2758  CD1 PHE A 384      -0.985  29.294  54.220  1.00 65.07           C  
ANISOU 2758  CD1 PHE A 384     8194  10129   6400   -662    115   -790       C  
ATOM   2759  CE1 PHE A 384      -1.738  30.158  53.444  1.00 64.85           C  
ANISOU 2759  CE1 PHE A 384     8217  10005   6419   -675    141   -832       C  
ATOM   2760  CZ  PHE A 384      -1.109  31.104  52.661  1.00 66.81           C  
ANISOU 2760  CZ  PHE A 384     8467  10226   6690   -715    148   -873       C  
ATOM   2761  CE2 PHE A 384       0.273  31.186  52.655  1.00 68.02           C  
ANISOU 2761  CE2 PHE A 384     8575  10452   6819   -741    130   -873       C  
ATOM   2762  CD2 PHE A 384       1.019  30.321  53.434  1.00 64.92           C  
ANISOU 2762  CD2 PHE A 384     8132  10155   6380   -727    104   -832       C  
ATOM   2763  C   PHE A 384       2.236  27.877  57.261  1.00 57.32           C  
ANISOU 2763  C   PHE A 384     7025   9485   5268   -688     35   -721       C  
ATOM   2764  O   PHE A 384       3.458  27.974  57.166  1.00 60.91           O  
ANISOU 2764  O   PHE A 384     7441   9994   5707   -710     20   -722       O  
ATOM   2765  N   LYS A 385       1.645  26.938  57.978  1.00 56.50           N  
ANISOU 2765  N   LYS A 385     6916   9404   5147   -649     28   -677       N  
ATOM   2766  CA  LYS A 385       2.409  25.836  58.526  1.00 52.27           C  
ANISOU 2766  CA  LYS A 385     6329   8952   4579   -622      2   -620       C  
ATOM   2767  CB  LYS A 385       2.778  26.083  59.987  1.00 58.81           C  
ANISOU 2767  CB  LYS A 385     7119   9863   5365   -652     -8   -637       C  
ATOM   2768  CG  LYS A 385       3.869  25.150  60.469  1.00 69.63           C  
ANISOU 2768  CG  LYS A 385     8429  11325   6703   -637    -34   -586       C  
ATOM   2769  CD  LYS A 385       5.240  25.687  60.080  1.00 77.11           C  
ANISOU 2769  CD  LYS A 385     9344  12311   7643   -675    -43   -609       C  
ATOM   2770  CE  LYS A 385       6.161  25.821  61.278  1.00 78.35           C  
ANISOU 2770  CE  LYS A 385     9447  12565   7756   -706    -59   -617       C  
ATOM   2771  NZ  LYS A 385       7.310  26.737  61.017  1.00 79.27           N  
ANISOU 2771  NZ  LYS A 385     9542  12710   7868   -757    -62   -660       N  
ATOM   2772  C   LYS A 385       1.584  24.574  58.383  1.00 41.98           C  
ANISOU 2772  C   LYS A 385     5039   7625   3285   -559     -1   -555       C  
ATOM   2773  O   LYS A 385       0.355  24.629  58.442  1.00 43.76           O  
ANISOU 2773  O   LYS A 385     5307   7793   3527   -543     16   -562       O  
ATOM   2774  N   PHE A 386       2.262  23.448  58.189  1.00 42.48           N  
ANISOU 2774  N   PHE A 386     5067   7731   3341   -522    -22   -494       N  
ATOM   2775  CA  PHE A 386       1.586  22.182  57.942  1.00 37.81           C  
ANISOU 2775  CA  PHE A 386     4486   7117   2763   -459    -27   -428       C  
ATOM   2776  CB  PHE A 386       2.595  21.043  57.826  1.00 39.05           C  
ANISOU 2776  CB  PHE A 386     4593   7333   2910   -426    -53   -364       C  
ATOM   2777  CG  PHE A 386       1.957  19.709  57.582  1.00 40.62           C  
ANISOU 2777  CG  PHE A 386     4799   7510   3126   -360    -61   -294       C  
ATOM   2778  CD1 PHE A 386       1.294  19.454  56.391  1.00 41.39           C  
ANISOU 2778  CD1 PHE A 386     4938   7525   3263   -325    -50   -279       C  
ATOM   2779  CE1 PHE A 386       0.695  18.232  56.165  1.00 45.25           C  
ANISOU 2779  CE1 PHE A 386     5431   7991   3769   -264    -58   -215       C  
ATOM   2780  CZ  PHE A 386       0.751  17.249  57.133  1.00 46.91           C  
ANISOU 2780  CZ  PHE A 386     5605   8259   3960   -238    -77   -164       C  
ATOM   2781  CE2 PHE A 386       1.404  17.495  58.326  1.00 46.87           C  
ANISOU 2781  CE2 PHE A 386     5558   8335   3915   -273    -86   -178       C  
ATOM   2782  CD2 PHE A 386       1.998  18.719  58.547  1.00 41.88           C  
ANISOU 2782  CD2 PHE A 386     4921   7727   3264   -333    -78   -243       C  
ATOM   2783  C   PHE A 386       0.570  21.850  59.031  1.00 45.38           C  
ANISOU 2783  C   PHE A 386     5452   8083   3707   -444    -23   -415       C  
ATOM   2784  O   PHE A 386       0.906  21.775  60.213  1.00 45.84           O  
ANISOU 2784  O   PHE A 386     5473   8214   3730   -459    -34   -413       O  
ATOM   2785  N   GLY A 387      -0.678  21.661  58.618  1.00 39.88           N  
ANISOU 2785  N   GLY A 387     4804   7311   3038   -413     -7   -407       N  
ATOM   2786  CA  GLY A 387      -1.742  21.332  59.546  1.00 41.58           C  
ANISOU 2786  CA  GLY A 387     5030   7525   3242   -396     -2   -393       C  
ATOM   2787  C   GLY A 387      -3.082  21.287  58.847  1.00 45.45           C  
ANISOU 2787  C   GLY A 387     5580   7920   3770   -367     19   -391       C  
ATOM   2788  O   GLY A 387      -3.156  21.152  57.620  1.00 42.55           O  
ANISOU 2788  O   GLY A 387     5238   7492   3435   -346     25   -382       O  
ATOM   2789  N   ARG A 388      -4.148  21.408  59.630  1.00 37.22           N  
ANISOU 2789  N   ARG A 388     4559   6863   2721   -365     30   -400       N  
ATOM   2790  CA  ARG A 388      -5.502  21.357  59.099  1.00 39.39           C  
ANISOU 2790  CA  ARG A 388     4890   7049   3029   -338     51   -398       C  
ATOM   2791  CB  ARG A 388      -6.508  21.381  60.250  1.00 41.45           C  
ANISOU 2791  CB  ARG A 388     5159   7318   3272   -337     59   -402       C  
ATOM   2792  CG  ARG A 388      -6.480  20.115  61.065  1.00 49.46           C  
ANISOU 2792  CG  ARG A 388     6134   8396   4263   -299     37   -333       C  
ATOM   2793  CD  ARG A 388      -7.187  20.266  62.399  1.00 55.05           C  
ANISOU 2793  CD  ARG A 388     6838   9137   4943   -309     42   -343       C  
ATOM   2794  NE  ARG A 388      -7.257  18.972  63.067  1.00 54.06           N  
ANISOU 2794  NE  ARG A 388     6678   9062   4802   -267     23   -272       N  
ATOM   2795  CZ  ARG A 388      -8.382  18.300  63.281  1.00 54.07           C  
ANISOU 2795  CZ  ARG A 388     6698   9033   4812   -229     28   -234       C  
ATOM   2796  NH1 ARG A 388      -9.552  18.819  62.910  1.00 46.02           N  
ANISOU 2796  NH1 ARG A 388     5734   7934   3817   -228     52   -262       N  
ATOM   2797  NH2 ARG A 388      -8.336  17.117  63.881  1.00 51.97           N  
ANISOU 2797  NH2 ARG A 388     6395   8816   4534   -193      9   -167       N  
ATOM   2798  C   ARG A 388      -5.813  22.484  58.119  1.00 37.62           C  
ANISOU 2798  C   ARG A 388     4714   6741   2839   -365     76   -458       C  
ATOM   2799  O   ARG A 388      -6.749  22.374  57.334  1.00 42.30           O  
ANISOU 2799  O   ARG A 388     5353   7253   3466   -338     92   -453       O  
ATOM   2800  N   ASP A 389      -5.037  23.564  58.166  1.00 35.44           N  
ANISOU 2800  N   ASP A 389     4427   6484   2554   -418     78   -515       N  
ATOM   2801  CA  ASP A 389      -5.299  24.709  57.305  1.00 36.40           C  
ANISOU 2801  CA  ASP A 389     4592   6528   2711   -448    101   -575       C  
ATOM   2802  CB  ASP A 389      -5.284  26.011  58.111  1.00 45.43           C  
ANISOU 2802  CB  ASP A 389     5736   7684   3841   -506    110   -644       C  
ATOM   2803  CG  ASP A 389      -6.453  26.114  59.089  1.00 55.74           C  
ANISOU 2803  CG  ASP A 389     7062   8979   5138   -501    121   -653       C  
ATOM   2804  OD1 ASP A 389      -7.511  25.496  58.840  1.00 56.70           O  
ANISOU 2804  OD1 ASP A 389     7216   9050   5278   -459    130   -621       O  
ATOM   2805  OD2 ASP A 389      -6.311  26.826  60.106  1.00 60.53           O  
ANISOU 2805  OD2 ASP A 389     7651   9628   5719   -538    120   -692       O  
ATOM   2806  C   ASP A 389      -4.286  24.779  56.167  1.00 42.24           C  
ANISOU 2806  C   ASP A 389     5322   7262   3467   -454     95   -574       C  
ATOM   2807  O   ASP A 389      -4.379  25.642  55.298  1.00 41.34           O  
ANISOU 2807  O   ASP A 389     5240   7084   3385   -477    113   -617       O  
ATOM   2808  N   TYR A 390      -3.329  23.859  56.174  1.00 39.90           N  
ANISOU 2808  N   TYR A 390     4979   7032   3151   -433     71   -524       N  
ATOM   2809  CA  TYR A 390      -2.319  23.804  55.125  1.00 37.95           C  
ANISOU 2809  CA  TYR A 390     4717   6786   2915   -434     63   -517       C  
ATOM   2810  CB  TYR A 390      -1.112  24.667  55.507  1.00 37.66           C  
ANISOU 2810  CB  TYR A 390     4643   6810   2855   -491     54   -560       C  
ATOM   2811  CG  TYR A 390      -0.021  24.722  54.462  1.00 36.51           C  
ANISOU 2811  CG  TYR A 390     4481   6671   2720   -497     46   -557       C  
ATOM   2812  CD1 TYR A 390      -0.206  25.409  53.265  1.00 39.31           C  
ANISOU 2812  CD1 TYR A 390     4874   6949   3114   -508     65   -589       C  
ATOM   2813  CE1 TYR A 390       0.795  25.462  52.308  1.00 36.56           C  
ANISOU 2813  CE1 TYR A 390     4509   6608   2774   -514     59   -586       C  
ATOM   2814  CZ  TYR A 390       2.002  24.838  52.550  1.00 35.17           C  
ANISOU 2814  CZ  TYR A 390     4277   6517   2569   -509     32   -550       C  
ATOM   2815  OH  TYR A 390       3.009  24.884  51.608  1.00 41.62           O  
ANISOU 2815  OH  TYR A 390     5076   7344   3394   -514     25   -545       O  
ATOM   2816  CE2 TYR A 390       2.213  24.163  53.733  1.00 38.62           C  
ANISOU 2816  CE2 TYR A 390     4676   7028   2970   -498     13   -518       C  
ATOM   2817  CD2 TYR A 390       1.204  24.111  54.681  1.00 40.15           C  
ANISOU 2817  CD2 TYR A 390     4886   7214   3154   -493     20   -521       C  
ATOM   2818  C   TYR A 390      -1.901  22.361  54.853  1.00 32.33           C  
ANISOU 2818  C   TYR A 390     3975   6110   2199   -379     40   -439       C  
ATOM   2819  O   TYR A 390      -0.917  21.874  55.406  1.00 39.67           O  
ANISOU 2819  O   TYR A 390     4853   7121   3099   -380     16   -412       O  
ATOM   2820  N   LEU A 391      -2.657  21.698  53.978  1.00 35.12           N  
ANISOU 2820  N   LEU A 391     4362   6399   2585   -330     47   -404       N  
ATOM   2821  CA  LEU A 391      -2.491  20.273  53.674  1.00 35.67           C  
ANISOU 2821  CA  LEU A 391     4408   6486   2657   -269     27   -327       C  
ATOM   2822  CB  LEU A 391      -3.857  19.590  53.590  1.00 33.46           C  
ANISOU 2822  CB  LEU A 391     4166   6147   2399   -221     37   -293       C  
ATOM   2823  CG  LEU A 391      -4.708  19.467  54.853  1.00 30.90           C  
ANISOU 2823  CG  LEU A 391     3844   5842   2054   -221     39   -290       C  
ATOM   2824  CD1 LEU A 391      -6.064  18.922  54.466  1.00 38.17           C  
ANISOU 2824  CD1 LEU A 391     4809   6689   3005   -175     53   -262       C  
ATOM   2825  CD2 LEU A 391      -4.026  18.531  55.811  1.00 40.48           C  
ANISOU 2825  CD2 LEU A 391     4999   7145   3235   -206     11   -238       C  
ATOM   2826  C   LEU A 391      -1.749  19.991  52.369  1.00 35.36           C  
ANISOU 2826  C   LEU A 391     4364   6430   2641   -249     20   -308       C  
ATOM   2827  O   LEU A 391      -1.268  18.879  52.157  1.00 35.56           O  
ANISOU 2827  O   LEU A 391     4359   6486   2667   -205     -2   -247       O  
ATOM   2828  N   ILE A 392      -1.707  20.980  51.482  1.00 32.02           N  
ANISOU 2828  N   ILE A 392     3971   5954   2240   -279     39   -359       N  
ATOM   2829  CA  ILE A 392      -1.028  20.837  50.198  1.00 36.63           C  
ANISOU 2829  CA  ILE A 392     4553   6520   2846   -263     36   -348       C  
ATOM   2830  CB  ILE A 392      -2.006  20.420  49.078  1.00 37.12           C  
ANISOU 2830  CB  ILE A 392     4662   6493   2951   -214     51   -327       C  
ATOM   2831  CG1 ILE A 392      -3.392  21.028  49.317  1.00 38.29           C  
ANISOU 2831  CG1 ILE A 392     4863   6570   3114   -225     79   -365       C  
ATOM   2832  CD1 ILE A 392      -4.346  20.801  48.162  1.00 42.04           C  
ANISOU 2832  CD1 ILE A 392     5387   6952   3633   -184     99   -355       C  
ATOM   2833  CG2 ILE A 392      -2.063  18.899  48.955  1.00 37.71           C  
ANISOU 2833  CG2 ILE A 392     4715   6583   3029   -144     29   -246       C  
ATOM   2834  C   ILE A 392      -0.355  22.148  49.831  1.00 33.57           C  
ANISOU 2834  C   ILE A 392     4168   6128   2460   -324     47   -413       C  
ATOM   2835  O   ILE A 392      -0.715  23.193  50.369  1.00 34.34           O  
ANISOU 2835  O   ILE A 392     4284   6210   2554   -372     64   -470       O  
ATOM   2836  N   PRO A 393       0.628  22.109  48.913  1.00 33.34           N  
ANISOU 2836  N   PRO A 393     4119   6111   2438   -323     39   -405       N  
ATOM   2837  CA  PRO A 393       1.271  23.374  48.545  1.00 36.28           C  
ANISOU 2837  CA  PRO A 393     4492   6478   2813   -382     50   -467       C  
ATOM   2838  CB  PRO A 393       2.333  22.946  47.516  1.00 35.51           C  
ANISOU 2838  CB  PRO A 393     4369   6402   2723   -363     36   -438       C  
ATOM   2839  CG  PRO A 393       2.540  21.493  47.755  1.00 35.90           C  
ANISOU 2839  CG  PRO A 393     4385   6496   2760   -304      9   -362       C  
ATOM   2840  CD  PRO A 393       1.212  20.967  48.182  1.00 33.88           C  
ANISOU 2840  CD  PRO A 393     4161   6198   2513   -269     18   -342       C  
ATOM   2841  C   PRO A 393       0.285  24.358  47.926  1.00 33.46           C  
ANISOU 2841  C   PRO A 393     4196   6025   2494   -403     83   -521       C  
ATOM   2842  O   PRO A 393      -0.758  23.946  47.408  1.00 35.13           O  
ANISOU 2842  O   PRO A 393     4447   6169   2734   -362     97   -503       O  
ATOM   2843  N   LYS A 394       0.605  25.645  47.993  1.00 33.15           N  
ANISOU 2843  N   LYS A 394     4162   5978   2457   -464     95   -584       N  
ATOM   2844  CA  LYS A 394      -0.156  26.659  47.272  1.00 37.16           C  
ANISOU 2844  CA  LYS A 394     4722   6392   3006   -487    126   -637       C  
ATOM   2845  CB  LYS A 394       0.159  28.061  47.806  1.00 41.48           C  
ANISOU 2845  CB  LYS A 394     5266   6945   3549   -559    135   -705       C  
ATOM   2846  CG  LYS A 394       0.059  28.188  49.317  1.00 42.45           C  
ANISOU 2846  CG  LYS A 394     5368   7125   3635   -581    125   -716       C  
ATOM   2847  CD  LYS A 394      -1.358  27.969  49.812  1.00 51.70           C  
ANISOU 2847  CD  LYS A 394     6579   8247   4818   -555    139   -712       C  
ATOM   2848  CE  LYS A 394      -2.309  29.008  49.250  1.00 56.00           C  
ANISOU 2848  CE  LYS A 394     7179   8689   5410   -576    170   -764       C  
ATOM   2849  NZ  LYS A 394      -3.691  28.803  49.762  1.00 66.46           N  
ANISOU 2849  NZ  LYS A 394     8541   9967   6745   -550    183   -760       N  
ATOM   2850  C   LYS A 394       0.163  26.573  45.779  1.00 35.25           C  
ANISOU 2850  C   LYS A 394     4492   6107   2796   -469    133   -627       C  
ATOM   2851  O   LYS A 394       1.278  26.208  45.402  1.00 37.07           O  
ANISOU 2851  O   LYS A 394     4683   6392   3011   -464    114   -602       O  
ATOM   2852  N   PRO A 395      -0.815  26.905  44.925  1.00 32.97           N  
ANISOU 2852  N   PRO A 395     4256   5720   2552   -457    160   -646       N  
ATOM   2853  CA  PRO A 395      -0.607  26.824  43.474  1.00 37.30           C  
ANISOU 2853  CA  PRO A 395     4817   6207   3147   -432    167   -632       C  
ATOM   2854  CB  PRO A 395      -1.946  27.301  42.905  1.00 35.47           C  
ANISOU 2854  CB  PRO A 395     4648   5857   2971   -423    199   -657       C  
ATOM   2855  CG  PRO A 395      -2.937  26.945  43.958  1.00 36.74           C  
ANISOU 2855  CG  PRO A 395     4825   6030   3106   -411    201   -653       C  
ATOM   2856  CD  PRO A 395      -2.226  27.154  45.268  1.00 33.23           C  
ANISOU 2856  CD  PRO A 395     4338   5682   2607   -451    182   -665       C  
ATOM   2857  C   PRO A 395       0.535  27.695  42.959  1.00 43.05           C  
ANISOU 2857  C   PRO A 395     5523   6958   3878   -480    166   -665       C  
ATOM   2858  O   PRO A 395       1.187  27.311  41.992  1.00 41.10           O  
ANISOU 2858  O   PRO A 395     5260   6699   3657   -453    158   -632       O  
ATOM   2859  N   PHE A 396       0.784  28.842  43.583  1.00 35.96           N  
ANISOU 2859  N   PHE A 396     4622   6085   2957   -549    173   -727       N  
ATOM   2860  CA  PHE A 396       1.830  29.731  43.087  1.00 39.85           C  
ANISOU 2860  CA  PHE A 396     5095   6595   3452   -598    173   -762       C  
ATOM   2861  CB  PHE A 396       1.348  31.184  43.099  1.00 39.19           C  
ANISOU 2861  CB  PHE A 396     5044   6443   3401   -654    198   -831       C  
ATOM   2862  CG  PHE A 396       0.363  31.499  42.008  1.00 41.18           C  
ANISOU 2862  CG  PHE A 396     5352   6582   3711   -637    227   -845       C  
ATOM   2863  CD1 PHE A 396      -0.979  31.171  42.144  1.00 45.86           C  
ANISOU 2863  CD1 PHE A 396     5988   7109   4327   -602    242   -836       C  
ATOM   2864  CE1 PHE A 396      -1.891  31.451  41.130  1.00 48.18           C  
ANISOU 2864  CE1 PHE A 396     6333   7294   4677   -585    270   -847       C  
ATOM   2865  CZ  PHE A 396      -1.461  32.058  39.965  1.00 44.78           C  
ANISOU 2865  CZ  PHE A 396     5909   6812   4293   -598    280   -860       C  
ATOM   2866  CE2 PHE A 396      -0.121  32.384  39.816  1.00 42.56           C  
ANISOU 2866  CE2 PHE A 396     5584   6594   3993   -632    265   -866       C  
ATOM   2867  CD2 PHE A 396       0.781  32.102  40.833  1.00 44.54           C  
ANISOU 2867  CD2 PHE A 396     5785   6959   4178   -652    239   -860       C  
ATOM   2868  C   PHE A 396       3.127  29.582  43.879  1.00 43.02           C  
ANISOU 2868  C   PHE A 396     5435   7108   3804   -622    143   -750       C  
ATOM   2869  O   PHE A 396       3.977  30.470  43.870  1.00 53.72           O  
ANISOU 2869  O   PHE A 396     6768   8489   5153   -675    142   -787       O  
ATOM   2870  N   ASP A 397       3.268  28.449  44.560  1.00 41.67           N  
ANISOU 2870  N   ASP A 397     5234   7000   3599   -582    121   -698       N  
ATOM   2871  CA  ASP A 397       4.526  28.068  45.196  1.00 44.77           C  
ANISOU 2871  CA  ASP A 397     5566   7497   3948   -593     91   -674       C  
ATOM   2872  CB  ASP A 397       4.288  27.018  46.291  1.00 44.44           C  
ANISOU 2872  CB  ASP A 397     5503   7507   3874   -557     72   -628       C  
ATOM   2873  CG  ASP A 397       5.555  26.661  47.066  1.00 46.59           C  
ANISOU 2873  CG  ASP A 397     5713   7887   4103   -570     43   -606       C  
ATOM   2874  OD1 ASP A 397       6.661  27.084  46.665  1.00 45.97           O  
ANISOU 2874  OD1 ASP A 397     5605   7844   4018   -600     35   -619       O  
ATOM   2875  OD2 ASP A 397       5.442  25.939  48.083  1.00 41.87           O  
ANISOU 2875  OD2 ASP A 397     5093   7337   3478   -549     27   -575       O  
ATOM   2876  C   ASP A 397       5.464  27.525  44.122  1.00 39.88           C  
ANISOU 2876  C   ASP A 397     4922   6901   3331   -567     79   -638       C  
ATOM   2877  O   ASP A 397       5.208  26.478  43.532  1.00 42.48           O  
ANISOU 2877  O   ASP A 397     5256   7211   3675   -505     73   -584       O  
ATOM   2878  N   THR A 398       6.561  28.229  43.876  1.00 44.96           N  
ANISOU 2878  N   THR A 398     5537   7581   3966   -613     73   -664       N  
ATOM   2879  CA  THR A 398       7.446  27.856  42.779  1.00 41.18           C  
ANISOU 2879  CA  THR A 398     5035   7111   3501   -590     64   -632       C  
ATOM   2880  CB  THR A 398       8.366  29.021  42.408  1.00 49.72           C  
ANISOU 2880  CB  THR A 398     6101   8205   4586   -653     68   -679       C  
ATOM   2881  OG1 THR A 398       9.193  29.359  43.527  1.00 55.97           O  
ANISOU 2881  OG1 THR A 398     6851   9087   5329   -700     50   -698       O  
ATOM   2882  CG2 THR A 398       7.530  30.227  42.021  1.00 46.77           C  
ANISOU 2882  CG2 THR A 398     5778   7737   4254   -691    100   -739       C  
ATOM   2883  C   THR A 398       8.288  26.616  43.079  1.00 37.08           C  
ANISOU 2883  C   THR A 398     4465   6680   2944   -549     31   -568       C  
ATOM   2884  O   THR A 398       8.998  26.118  42.208  1.00 39.96           O  
ANISOU 2884  O   THR A 398     4808   7047   3329   -518     20   -530       O  
ATOM   2885  N   ARG A 399       8.199  26.103  44.300  1.00 32.68           N  
ANISOU 2885  N   ARG A 399     3777   5943   2696    -19   -433   -650       N  
ATOM   2886  CA  ARG A 399       8.921  24.884  44.651  1.00 31.27           C  
ANISOU 2886  CA  ARG A 399     3559   5844   2481     27   -465   -586       C  
ATOM   2887  CB  ARG A 399       8.991  24.719  46.168  1.00 40.42           C  
ANISOU 2887  CB  ARG A 399     4679   7065   3614    -24   -482   -553       C  
ATOM   2888  CG  ARG A 399       9.762  25.822  46.887  1.00 38.32           C  
ANISOU 2888  CG  ARG A 399     4365   6861   3334    -97   -472   -564       C  
ATOM   2889  CD  ARG A 399       9.674  25.637  48.399  1.00 43.39           C  
ANISOU 2889  CD  ARG A 399     4979   7554   3955   -146   -486   -535       C  
ATOM   2890  NE  ARG A 399       8.295  25.771  48.869  1.00 42.20           N  
ANISOU 2890  NE  ARG A 399     4878   7329   3826   -175   -477   -564       N  
ATOM   2891  CZ  ARG A 399       7.841  25.304  50.031  1.00 46.51           C  
ANISOU 2891  CZ  ARG A 399     5419   7893   4359   -199   -492   -540       C  
ATOM   2892  NH1 ARG A 399       8.651  24.671  50.870  1.00 47.08           N  
ANISOU 2892  NH1 ARG A 399     5438   8055   4397   -200   -515   -486       N  
ATOM   2893  NH2 ARG A 399       6.572  25.479  50.360  1.00 42.75           N  
ANISOU 2893  NH2 ARG A 399     4991   7345   3906   -222   -482   -568       N  
ATOM   2894  C   ARG A 399       8.298  23.634  44.045  1.00 37.84           C  
ANISOU 2894  C   ARG A 399     4431   6627   3319    106   -480   -563       C  
ATOM   2895  O   ARG A 399       8.972  22.615  43.917  1.00 36.22           O  
ANISOU 2895  O   ARG A 399     4198   6472   3091    165   -502   -509       O  
ATOM   2896  N   VAL A 400       7.016  23.705  43.680  1.00 33.29           N  
ANISOU 2896  N   VAL A 400     3920   5952   2777    107   -466   -601       N  
ATOM   2897  CA  VAL A 400       6.281  22.511  43.252  1.00 28.50           C  
ANISOU 2897  CA  VAL A 400     3356   5294   2178    176   -479   -581       C  
ATOM   2898  CB  VAL A 400       4.829  22.849  42.852  1.00 28.18           C  
ANISOU 2898  CB  VAL A 400     3389   5138   2181    163   -458   -631       C  
ATOM   2899  CG1 VAL A 400       4.115  21.618  42.310  1.00 29.93           C  
ANISOU 2899  CG1 VAL A 400     3656   5304   2411    239   -470   -612       C  
ATOM   2900  CG2 VAL A 400       4.070  23.387  44.058  1.00 32.72           C  
ANISOU 2900  CG2 VAL A 400     3967   5705   2761     85   -454   -645       C  
ATOM   2901  C   VAL A 400       6.978  21.792  42.098  1.00 27.59           C  
ANISOU 2901  C   VAL A 400     3241   5186   2058    266   -486   -557       C  
ATOM   2902  O   VAL A 400       7.204  20.587  42.174  1.00 32.47           O  
ANISOU 2902  O   VAL A 400     3851   5807   2681    323   -501   -494       O  
ATOM   2903  N   LEU A 401       7.339  22.533  41.052  1.00 31.05           N  
ANISOU 2903  N   LEU A 401     3690   5590   2519    274   -461   -593       N  
ATOM   2904  CA  LEU A 401       7.945  21.932  39.858  1.00 28.74           C  
ANISOU 2904  CA  LEU A 401     3406   5249   2265    355   -449   -561       C  
ATOM   2905  CB  LEU A 401       8.194  22.987  38.776  1.00 27.10           C  
ANISOU 2905  CB  LEU A 401     3214   5002   2080    349   -420   -615       C  
ATOM   2906  CG  LEU A 401       8.557  22.424  37.395  1.00 29.92           C  
ANISOU 2906  CG  LEU A 401     3597   5287   2484    432   -403   -594       C  
ATOM   2907  CD1 LEU A 401       7.342  21.758  36.773  1.00 27.86           C  
ANISOU 2907  CD1 LEU A 401     3409   4918   2261    477   -397   -604       C  
ATOM   2908  CD2 LEU A 401       9.096  23.502  36.476  1.00 32.76           C  
ANISOU 2908  CD2 LEU A 401     3956   5633   2859    420   -377   -639       C  
ATOM   2909  C   LEU A 401       9.249  21.233  40.218  1.00 31.57           C  
ANISOU 2909  C   LEU A 401     3700   5689   2607    384   -466   -487       C  
ATOM   2910  O   LEU A 401       9.483  20.096  39.813  1.00 30.45           O  
ANISOU 2910  O   LEU A 401     3563   5520   2487    457   -470   -431       O  
ATOM   2911  N   LEU A 402      10.072  21.922  41.009  1.00 34.22           N  
ANISOU 2911  N   LEU A 402     3975   6126   2902    326   -474   -486       N  
ATOM   2912  CA  LEU A 402      11.364  21.413  41.461  1.00 45.85           C  
ANISOU 2912  CA  LEU A 402     5379   7688   4354    343   -491   -418       C  
ATOM   2913  CB  LEU A 402      12.108  22.504  42.240  1.00 52.35           C  
ANISOU 2913  CB  LEU A 402     6145   8612   5132    264   -496   -439       C  
ATOM   2914  CG  LEU A 402      12.482  23.767  41.460  1.00 61.23           C  
ANISOU 2914  CG  LEU A 402     7273   9725   6267    236   -470   -497       C  
ATOM   2915  CD1 LEU A 402      13.081  24.819  42.396  1.00 57.44           C  
ANISOU 2915  CD1 LEU A 402     6738   9344   5742    150   -476   -518       C  
ATOM   2916  CD2 LEU A 402      13.429  23.440  40.313  1.00 61.18           C  
ANISOU 2916  CD2 LEU A 402     7257   9694   6295    306   -455   -466       C  
ATOM   2917  C   LEU A 402      11.238  20.168  42.338  1.00 37.90           C  
ANISOU 2917  C   LEU A 402     4356   6712   3331    368   -519   -353       C  
ATOM   2918  O   LEU A 402      12.141  19.336  42.381  1.00 41.39           O  
ANISOU 2918  O   LEU A 402     4758   7194   3774    414   -530   -285       O  
ATOM   2919  N   TRP A 403      10.123  20.064  43.050  1.00 36.96           N  
ANISOU 2919  N   TRP A 403     4267   6576   3199    335   -530   -373       N  
ATOM   2920  CA  TRP A 403       9.888  18.968  43.982  1.00 38.75           C  
ANISOU 2920  CA  TRP A 403     4481   6834   3408    350   -557   -317       C  
ATOM   2921  CB  TRP A 403       9.004  19.441  45.139  1.00 45.08           C  
ANISOU 2921  CB  TRP A 403     5289   7665   4176    273   -569   -352       C  
ATOM   2922  CG  TRP A 403       9.788  19.763  46.348  1.00 52.42           C  
ANISOU 2922  CG  TRP A 403     6155   8685   5079    211   -579   -325       C  
ATOM   2923  CD1 TRP A 403      10.583  20.853  46.542  1.00 58.77           C  
ANISOU 2923  CD1 TRP A 403     6918   9538   5873    155   -567   -347       C  
ATOM   2924  NE1 TRP A 403      11.164  20.800  47.787  1.00 57.83           N  
ANISOU 2924  NE1 TRP A 403     6745   9498   5729    110   -580   -309       N  
ATOM   2925  CE2 TRP A 403      10.748  19.658  48.420  1.00 58.80           C  
ANISOU 2925  CE2 TRP A 403     6871   9622   5847    136   -602   -261       C  
ATOM   2926  CD2 TRP A 403       9.879  18.979  47.540  1.00 55.25           C  
ANISOU 2926  CD2 TRP A 403     6481   9093   5419    200   -602   -269       C  
ATOM   2927  CE3 TRP A 403       9.307  17.772  47.952  1.00 54.72           C  
ANISOU 2927  CE3 TRP A 403     6430   9009   5353    238   -621   -225       C  
ATOM   2928  CZ3 TRP A 403       9.617  17.288  49.207  1.00 57.18           C  
ANISOU 2928  CZ3 TRP A 403     6699   9382   5645    211   -639   -176       C  
ATOM   2929  CH2 TRP A 403      10.483  17.985  50.062  1.00 56.15           C  
ANISOU 2929  CH2 TRP A 403     6511   9330   5493    147   -638   -171       C  
ATOM   2930  CZ2 TRP A 403      11.057  19.170  49.688  1.00 55.29           C  
ANISOU 2930  CZ2 TRP A 403     6385   9240   5382    109   -620   -212       C  
ATOM   2931  C   TRP A 403       9.245  17.755  43.328  1.00 38.83           C  
ANISOU 2931  C   TRP A 403     4541   6753   3458    430   -555   -286       C  
ATOM   2932  O   TRP A 403       9.634  16.617  43.602  1.00 36.81           O  
ANISOU 2932  O   TRP A 403     4263   6520   3202    478   -572   -217       O  
ATOM   2933  N   VAL A 404       8.264  18.007  42.464  1.00 30.28           N  
ANISOU 2933  N   VAL A 404     3525   5569   2410    444   -535   -338       N  
ATOM   2934  CA  VAL A 404       7.424  16.945  41.926  1.00 31.97           C  
ANISOU 2934  CA  VAL A 404     3795   5692   2660    509   -534   -319       C  
ATOM   2935  CB  VAL A 404       5.988  17.443  41.675  1.00 31.18           C  
ANISOU 2935  CB  VAL A 404     3763   5508   2575    483   -522   -387       C  
ATOM   2936  CG1 VAL A 404       5.108  16.305  41.173  1.00 30.23           C  
ANISOU 2936  CG1 VAL A 404     3700   5297   2490    549   -522   -365       C  
ATOM   2937  CG2 VAL A 404       5.386  18.045  42.955  1.00 32.13           C  
ANISOU 2937  CG2 VAL A 404     3872   5683   2653    400   -536   -418       C  
ATOM   2938  C   VAL A 404       7.966  16.346  40.625  1.00 30.09           C  
ANISOU 2938  C   VAL A 404     3572   5394   2465    593   -517   -290       C  
ATOM   2939  O   VAL A 404       7.969  15.129  40.466  1.00 28.14           O  
ANISOU 2939  O   VAL A 404     3335   5121   2236    658   -524   -235       O  
ATOM   2940  N   ALA A 405       8.401  17.190  39.691  1.00 28.37           N  
ANISOU 2940  N   ALA A 405     3360   5153   2266    592   -493   -328       N  
ATOM   2941  CA  ALA A 405       8.880  16.687  38.400  1.00 28.72           C  
ANISOU 2941  CA  ALA A 405     3424   5137   2353    670   -475   -306       C  
ATOM   2942  CB  ALA A 405       9.329  17.853  37.494  1.00 27.24           C  
ANISOU 2942  CB  ALA A 405     3238   4933   2179    652   -449   -358       C  
ATOM   2943  C   ALA A 405      10.007  15.640  38.531  1.00 27.31           C  
ANISOU 2943  C   ALA A 405     3195   5010   2173    725   -487   -222       C  
ATOM   2944  O   ALA A 405       9.961  14.610  37.853  1.00 28.40           O  
ANISOU 2944  O   ALA A 405     3360   5088   2343    800   -482   -183       O  
ATOM   2945  N   PRO A 406      11.013  15.876  39.408  1.00 30.08           N  
ANISOU 2945  N   PRO A 406     3474   5470   2486    689   -503   -192       N  
ATOM   2946  CA  PRO A 406      12.037  14.829  39.507  1.00 32.23           C  
ANISOU 2946  CA  PRO A 406     3701   5787   2759    746   -514   -109       C  
ATOM   2947  CB  PRO A 406      13.060  15.426  40.488  1.00 36.25           C  
ANISOU 2947  CB  PRO A 406     4133   6419   3222    688   -530    -93       C  
ATOM   2948  CG  PRO A 406      12.878  16.885  40.386  1.00 39.81           C  
ANISOU 2948  CG  PRO A 406     4590   6875   3662    619   -516   -170       C  
ATOM   2949  CD  PRO A 406      11.406  17.094  40.140  1.00 32.36           C  
ANISOU 2949  CD  PRO A 406     3719   5842   2734    606   -507   -228       C  
ATOM   2950  C   PRO A 406      11.510  13.487  40.036  1.00 31.20           C  
ANISOU 2950  C   PRO A 406     3584   5642   2630    786   -534    -55       C  
ATOM   2951  O   PRO A 406      12.041  12.447  39.651  1.00 28.51           O  
ANISOU 2951  O   PRO A 406     3234   5289   2309    856   -534      5       O  
ATOM   2952  N   GLU A 407      10.500  13.501  40.903  1.00 27.42           N  
ANISOU 2952  N   GLU A 407     3124   5165   2129    742   -549    -76       N  
ATOM   2953  CA  GLU A 407       9.928  12.249  41.412  1.00 29.41           C  
ANISOU 2953  CA  GLU A 407     3391   5400   2382    778   -567    -28       C  
ATOM   2954  CB  GLU A 407       8.996  12.517  42.600  1.00 34.82           C  
ANISOU 2954  CB  GLU A 407     4082   6115   3032    711   -586    -54       C  
ATOM   2955  CG  GLU A 407       9.691  13.155  43.806  1.00 39.34           C  
ANISOU 2955  CG  GLU A 407     4586   6808   3554    639   -605    -48       C  
ATOM   2956  CD  GLU A 407      10.952  12.410  44.231  1.00 54.41           C  
ANISOU 2956  CD  GLU A 407     6427   8799   5447    670   -622     33       C  
ATOM   2957  OE1 GLU A 407      10.914  11.162  44.317  1.00 50.59           O  
ANISOU 2957  OE1 GLU A 407     5947   8300   4975    728   -633     93       O  
ATOM   2958  OE2 GLU A 407      11.981  13.079  44.480  1.00 61.84           O  
ANISOU 2958  OE2 GLU A 407     7311   9819   6365    636   -623     37       O  
ATOM   2959  C   GLU A 407       9.181  11.491  40.305  1.00 30.33           C  
ANISOU 2959  C   GLU A 407     3579   5399   2548    850   -551    -30       C  
ATOM   2960  O   GLU A 407       9.282  10.271  40.204  1.00 30.72           O  
ANISOU 2960  O   GLU A 407     3632   5428   2613    913   -557     30       O  
ATOM   2961  N   VAL A 408       8.436  12.221  39.480  1.00 26.08           N  
ANISOU 2961  N   VAL A 408     3095   4781   2033    838   -529    -97       N  
ATOM   2962  CA  VAL A 408       7.785  11.643  38.309  1.00 24.77           C  
ANISOU 2962  CA  VAL A 408     2996   4501   1914    903   -511   -104       C  
ATOM   2963  CB  VAL A 408       6.964  12.703  37.547  1.00 26.52           C  
ANISOU 2963  CB  VAL A 408     3271   4649   2154    873   -489   -187       C  
ATOM   2964  CG1 VAL A 408       6.407  12.133  36.256  1.00 24.78           C  
ANISOU 2964  CG1 VAL A 408     3118   4313   1983    941   -470   -193       C  
ATOM   2965  CG2 VAL A 408       5.823  13.225  38.420  1.00 28.46           C  
ANISOU 2965  CG2 VAL A 408     3538   4898   2376    805   -501   -234       C  
ATOM   2966  C   VAL A 408       8.831  11.024  37.377  1.00 23.22           C  
ANISOU 2966  C   VAL A 408     2786   4291   1747    977   -498    -56       C  
ATOM   2967  O   VAL A 408       8.669   9.903  36.892  1.00 27.56           O  
ANISOU 2967  O   VAL A 408     3363   4785   2323   1047   -496    -15       O  
ATOM   2968  N   ALA A 409       9.908  11.764  37.138  1.00 28.73           N  
ANISOU 2968  N   ALA A 409     3439   5040   2437    962   -489    -61       N  
ATOM   2969  CA  ALA A 409      10.986  11.289  36.281  1.00 31.54           C  
ANISOU 2969  CA  ALA A 409     3776   5391   2819   1027   -475    -17       C  
ATOM   2970  CB  ALA A 409      12.053  12.357  36.136  1.00 26.74           C  
ANISOU 2970  CB  ALA A 409     3119   4845   2197    992   -466    -36       C  
ATOM   2971  C   ALA A 409      11.590  10.002  36.831  1.00 28.28           C  
ANISOU 2971  C   ALA A 409     3324   5022   2398   1075   -493     69       C  
ATOM   2972  O   ALA A 409      11.813   9.045  36.094  1.00 30.72           O  
ANISOU 2972  O   ALA A 409     3652   5281   2740   1150   -484    111       O  
ATOM   2973  N   LYS A 410      11.839   9.987  38.136  1.00 30.77           N  
ANISOU 2973  N   LYS A 410     3588   5432   2672   1030   -519     95       N  
ATOM   2974  CA  LYS A 410      12.377   8.809  38.801  1.00 32.12           C  
ANISOU 2974  CA  LYS A 410     3718   5653   2832   1068   -539    177       C  
ATOM   2975  CB  LYS A 410      12.649   9.118  40.278  1.00 35.63           C  
ANISOU 2975  CB  LYS A 410     4103   6210   3225   1000   -567    191       C  
ATOM   2976  CG  LYS A 410      13.369   8.018  41.026  1.00 52.49           C  
ANISOU 2976  CG  LYS A 410     6186   8412   5345   1033   -589    278       C  
ATOM   2977  CD  LYS A 410      13.569   8.374  42.496  1.00 65.23           C  
ANISOU 2977  CD  LYS A 410     7743  10135   6905    961   -617    288       C  
ATOM   2978  CE  LYS A 410      14.361   9.663  42.669  1.00 69.64           C  
ANISOU 2978  CE  LYS A 410     8255  10766   7439    898   -614    254       C  
ATOM   2979  NZ  LYS A 410      14.514  10.026  44.113  1.00 71.70           N  
ANISOU 2979  NZ  LYS A 410     8464  11133   7647    825   -642    262       N  
ATOM   2980  C   LYS A 410      11.414   7.626  38.643  1.00 33.05           C  
ANISOU 2980  C   LYS A 410     3891   5692   2973   1121   -542    200       C  
ATOM   2981  O   LYS A 410      11.837   6.515  38.333  1.00 36.24           O  
ANISOU 2981  O   LYS A 410     4291   6080   3397   1191   -541    262       O  
ATOM   2982  N   ALA A 411      10.116   7.874  38.820  1.00 33.27           N  
ANISOU 2982  N   ALA A 411     3971   5670   3000   1089   -545    150       N  
ATOM   2983  CA  ALA A 411       9.118   6.817  38.677  1.00 30.90           C  
ANISOU 2983  CA  ALA A 411     3726   5292   2721   1134   -547    166       C  
ATOM   2984  CB  ALA A 411       7.735   7.320  39.096  1.00 29.25           C  
ANISOU 2984  CB  ALA A 411     3564   5048   2502   1080   -553    105       C  
ATOM   2985  C   ALA A 411       9.063   6.276  37.255  1.00 33.09           C  
ANISOU 2985  C   ALA A 411     4055   5470   3049   1210   -522    170       C  
ATOM   2986  O   ALA A 411       8.822   5.087  37.053  1.00 35.24           O  
ANISOU 2986  O   ALA A 411     4351   5697   3341   1272   -524    215       O  
ATOM   2987  N   ALA A 412       9.263   7.153  36.272  1.00 28.51           N  
ANISOU 2987  N   ALA A 412     3492   4852   2488   1206   -498    122       N  
ATOM   2988  CA  ALA A 412       9.255   6.743  34.870  1.00 23.69           C  
ANISOU 2988  CA  ALA A 412     2929   4147   1925   1275   -472    122       C  
ATOM   2989  CB  ALA A 412       9.285   7.949  33.960  1.00 25.26           C  
ANISOU 2989  CB  ALA A 412     3148   4310   2138   1251   -449     55       C  
ATOM   2990  C   ALA A 412      10.436   5.830  34.564  1.00 28.02           C  
ANISOU 2990  C   ALA A 412     3440   4720   2486   1343   -469    197       C  
ATOM   2991  O   ALA A 412      10.302   4.842  33.846  1.00 29.84           O  
ANISOU 2991  O   ALA A 412     3707   4882   2750   1413   -458    228       O  
ATOM   2992  N   MET A 413      11.594   6.185  35.103  1.00 31.70           N  
ANISOU 2992  N   MET A 413     3834   5284   2927   1320   -477    224       N  
ATOM   2993  CA  MET A 413      12.799   5.388  34.896  1.00 35.24           C  
ANISOU 2993  CA  MET A 413     4238   5765   3385   1380   -474    296       C  
ATOM   2994  CB  MET A 413      14.027   6.140  35.404  1.00 31.07           C  
ANISOU 2994  CB  MET A 413     3633   5345   2828   1339   -480    308       C  
ATOM   2995  CG  MET A 413      14.538   7.161  34.401  1.00 39.95           C  
ANISOU 2995  CG  MET A 413     4761   6448   3969   1332   -455    262       C  
ATOM   2996  SD  MET A 413      15.878   8.198  35.008  1.00 49.40           S  
ANISOU 2996  SD  MET A 413     5871   7769   5130   1275   -462    265       S  
ATOM   2997  CE  MET A 413      14.962   9.445  35.903  1.00 49.21           C  
ANISOU 2997  CE  MET A 413     5854   7777   5067   1172   -476    189       C  
ATOM   2998  C   MET A 413      12.669   4.034  35.578  1.00 38.20           C  
ANISOU 2998  C   MET A 413     4605   6154   3756   1419   -493    366       C  
ATOM   2999  O   MET A 413      12.997   3.001  34.994  1.00 36.52           O  
ANISOU 2999  O   MET A 413     4403   5901   3571   1493   -483    416       O  
ATOM   3000  N   LYS A 414      12.159   4.047  36.807  1.00 38.03           N  
ANISOU 3000  N   LYS A 414     4567   6185   3699   1368   -519    366       N  
ATOM   3001  CA  LYS A 414      12.026   2.835  37.598  1.00 41.66           C  
ANISOU 3001  CA  LYS A 414     5014   6667   4149   1397   -540    431       C  
ATOM   3002  CB  LYS A 414      11.594   3.176  39.021  1.00 41.57           C  
ANISOU 3002  CB  LYS A 414     4973   6729   4091   1324   -569    421       C  
ATOM   3003  CG  LYS A 414      11.612   2.001  39.977  1.00 48.36           C  
ANISOU 3003  CG  LYS A 414     5807   7631   4935   1347   -593    491       C  
ATOM   3004  CD  LYS A 414      11.093   2.416  41.344  1.00 59.55           C  
ANISOU 3004  CD  LYS A 414     7202   9116   6307   1271   -621    474       C  
ATOM   3005  CE  LYS A 414      11.688   3.750  41.775  1.00 63.30           C  
ANISOU 3005  CE  LYS A 414     7630   9672   6751   1196   -624    437       C  
ATOM   3006  NZ  LYS A 414      13.178   3.731  41.749  1.00 68.66           N  
ANISOU 3006  NZ  LYS A 414     8240  10425   7423   1214   -624    487       N  
ATOM   3007  C   LYS A 414      11.034   1.860  36.984  1.00 40.36           C  
ANISOU 3007  C   LYS A 414     4920   6396   4018   1454   -531    435       C  
ATOM   3008  O   LYS A 414      11.214   0.649  37.083  1.00 43.26           O  
ANISOU 3008  O   LYS A 414     5284   6757   4396   1511   -536    499       O  
ATOM   3009  N   SER A 415       9.987   2.386  36.352  1.00 35.61           N  
ANISOU 3009  N   SER A 415     4384   5712   3434   1439   -518    368       N  
ATOM   3010  CA  SER A 415       8.946   1.530  35.786  1.00 36.48           C  
ANISOU 3010  CA  SER A 415     4567   5720   3575   1486   -511    366       C  
ATOM   3011  CB  SER A 415       7.574   2.204  35.893  1.00 37.61           C  
ANISOU 3011  CB  SER A 415     4764   5814   3714   1434   -513    294       C  
ATOM   3012  OG  SER A 415       7.499   3.353  35.069  1.00 39.02           O  
ANISOU 3012  OG  SER A 415     4965   5957   3905   1407   -493    227       O  
ATOM   3013  C   SER A 415       9.245   1.156  34.336  1.00 34.01           C  
ANISOU 3013  C   SER A 415     4291   5323   3307   1557   -481    372       C  
ATOM   3014  O   SER A 415       8.497   0.408  33.715  1.00 42.90           O  
ANISOU 3014  O   SER A 415     5477   6360   4462   1604   -472    374       O  
ATOM   3015  N   GLY A 416      10.339   1.687  33.804  1.00 33.43           N  
ANISOU 3015  N   GLY A 416     4183   5280   3240   1564   -466    374       N  
ATOM   3016  CA  GLY A 416      10.812   1.298  32.488  1.00 34.87           C  
ANISOU 3016  CA  GLY A 416     4391   5396   3463   1633   -439    388       C  
ATOM   3017  C   GLY A 416      10.140   1.960  31.299  1.00 43.64           C  
ANISOU 3017  C   GLY A 416     5568   6411   4604   1633   -414    319       C  
ATOM   3018  O   GLY A 416      10.268   1.475  30.175  1.00 42.98           O  
ANISOU 3018  O   GLY A 416     5520   6253   4556   1695   -391    329       O  
ATOM   3019  N   VAL A 417       9.427   3.062  31.516  1.00 36.52           N  
ANISOU 3019  N   VAL A 417     4682   5507   3686   1565   -418    250       N  
ATOM   3020  CA  VAL A 417       8.821   3.760  30.380  1.00 31.97           C  
ANISOU 3020  CA  VAL A 417     4167   4843   3138   1563   -394    184       C  
ATOM   3021  CB  VAL A 417       7.397   4.267  30.705  1.00 34.22           C  
ANISOU 3021  CB  VAL A 417     4499   5088   3414   1511   -403    122       C  
ATOM   3022  CG1 VAL A 417       6.474   3.095  31.033  1.00 34.47           C  
ANISOU 3022  CG1 VAL A 417     4570   5075   3452   1543   -416    152       C  
ATOM   3023  CG2 VAL A 417       7.418   5.274  31.842  1.00 32.24           C  
ANISOU 3023  CG2 VAL A 417     4202   4926   3121   1427   -422     93       C  
ATOM   3024  C   VAL A 417       9.680   4.934  29.896  1.00 32.71           C  
ANISOU 3024  C   VAL A 417     4230   4969   3230   1536   -379    149       C  
ATOM   3025  O   VAL A 417       9.410   5.508  28.837  1.00 33.37           O  
ANISOU 3025  O   VAL A 417     4356   4983   3338   1541   -357    101       O  
ATOM   3026  N   ALA A 418      10.715   5.282  30.660  1.00 32.49           N  
ANISOU 3026  N   ALA A 418     4128   5046   3172   1506   -391    176       N  
ATOM   3027  CA  ALA A 418      11.678   6.300  30.236  1.00 33.02           C  
ANISOU 3027  CA  ALA A 418     4158   5151   3237   1485   -377    153       C  
ATOM   3028  CB  ALA A 418      12.602   6.670  31.381  1.00 32.54           C  
ANISOU 3028  CB  ALA A 418     4015   5214   3135   1439   -397    181       C  
ATOM   3029  C   ALA A 418      12.495   5.802  29.050  1.00 35.93           C  
ANISOU 3029  C   ALA A 418     4534   5476   3642   1559   -352    184       C  
ATOM   3030  O   ALA A 418      12.857   4.630  29.001  1.00 39.17           O  
ANISOU 3030  O   ALA A 418     4939   5881   4065   1620   -352    248       O  
ATOM   3031  N   THR A 419      12.788   6.676  28.091  1.00 27.13           N  
ANISOU 3031  N   THR A 419     3433   4332   2545   1553   -328    139       N  
ATOM   3032  CA  THR A 419      13.695   6.281  27.009  1.00 35.05           C  
ANISOU 3032  CA  THR A 419     4435   5303   3579   1620   -304    170       C  
ATOM   3033  CB  THR A 419      13.040   6.365  25.621  1.00 35.13           C  
ANISOU 3033  CB  THR A 419     4522   5196   3630   1653   -277    126       C  
ATOM   3034  OG1 THR A 419      12.760   7.733  25.302  1.00 38.17           O  
ANISOU 3034  OG1 THR A 419     4920   5572   4011   1597   -268     51       O  
ATOM   3035  CG2 THR A 419      11.764   5.528  25.574  1.00 32.02           C  
ANISOU 3035  CG2 THR A 419     4193   4723   3250   1677   -283    125       C  
ATOM   3036  C   THR A 419      14.948   7.140  27.007  1.00 37.21           C  
ANISOU 3036  C   THR A 419     4646   5653   3840   1595   -298    170       C  
ATOM   3037  O   THR A 419      15.772   7.044  26.097  1.00 40.10           O  
ANISOU 3037  O   THR A 419     5007   6000   4230   1641   -277    186       O  
ATOM   3038  N   ARG A 420      15.086   7.970  28.035  1.00 38.63           N  
ANISOU 3038  N   ARG A 420     4778   5920   3981   1523   -317    150       N  
ATOM   3039  CA  ARG A 420      16.279   8.786  28.239  1.00 46.43           C  
ANISOU 3039  CA  ARG A 420     5699   6993   4949   1492   -316    153       C  
ATOM   3040  CB  ARG A 420      16.044  10.193  27.704  1.00 38.90           C  
ANISOU 3040  CB  ARG A 420     4765   6019   3996   1441   -301     73       C  
ATOM   3041  CG  ARG A 420      17.151  11.190  27.986  1.00 42.93           C  
ANISOU 3041  CG  ARG A 420     5210   6619   4484   1397   -301     65       C  
ATOM   3042  CD  ARG A 420      16.563  12.585  27.984  1.00 47.85           C  
ANISOU 3042  CD  ARG A 420     5851   7237   5094   1324   -297    -18       C  
ATOM   3043  NE  ARG A 420      17.526  13.628  27.651  1.00 52.83           N  
ANISOU 3043  NE  ARG A 420     6442   7911   5718   1297   -284    -41       N  
ATOM   3044  CZ  ARG A 420      17.288  14.926  27.812  1.00 58.06           C  
ANISOU 3044  CZ  ARG A 420     7104   8594   6363   1227   -281   -107       C  
ATOM   3045  NH1 ARG A 420      16.123  15.328  28.308  1.00 48.37           N  
ANISOU 3045  NH1 ARG A 420     5910   7345   5122   1177   -291   -154       N  
ATOM   3046  NH2 ARG A 420      18.209  15.822  27.485  1.00 64.20           N  
ANISOU 3046  NH2 ARG A 420     7845   9411   7137   1206   -269   -124       N  
ATOM   3047  C   ARG A 420      16.662   8.843  29.723  1.00 58.84           C  
ANISOU 3047  C   ARG A 420     7202   8679   6475   1442   -347    184       C  
ATOM   3048  O   ARG A 420      15.849   9.234  30.569  1.00 58.69           O  
ANISOU 3048  O   ARG A 420     7190   8681   6430   1384   -365    152       O  
ATOM   3049  N   ALA A 421      17.898   8.463  30.036  1.00 67.31           N  
ANISOU 3049  N   ALA A 421     8210   9827   7539   1464   -352    246       N  
ATOM   3050  CA  ALA A 421      18.371   8.454  31.424  1.00 76.48           C  
ANISOU 3050  CA  ALA A 421     9302  11100   8657   1421   -381    282       C  
ATOM   3051  CB  ALA A 421      19.569   7.524  31.568  1.00 75.78           C  
ANISOU 3051  CB  ALA A 421     9158  11064   8571   1475   -385    368       C  
ATOM   3052  C   ALA A 421      18.729   9.858  31.920  1.00 78.88           C  
ANISOU 3052  C   ALA A 421     9565  11479   8928   1339   -387    235       C  
ATOM   3053  O   ALA A 421      19.614  10.513  31.366  1.00 80.38           O  
ANISOU 3053  O   ALA A 421     9729  11689   9123   1337   -371    225       O  
ATOM   3062  N   THR B  15      29.221  19.649   0.890  1.00 73.91           N  
ANISOU 3062  N   THR B  15     8406   9962   9717    309     24   -545       N  
ATOM   3063  CA  THR B  15      29.846  20.299   2.036  1.00 68.77           C  
ANISOU 3063  CA  THR B  15     7734   9329   9065    292     10   -535       C  
ATOM   3064  CB  THR B  15      29.747  21.848   1.934  1.00 76.74           C  
ANISOU 3064  CB  THR B  15     8744  10345  10070    259     18   -543       C  
ATOM   3065  OG1 THR B  15      30.062  22.440   3.202  1.00 72.94           O  
ANISOU 3065  OG1 THR B  15     8248   9880   9586    239      1   -539       O  
ATOM   3066  CG2 THR B  15      28.350  22.292   1.473  1.00 71.66           C  
ANISOU 3066  CG2 THR B  15     8127   9684   9417    248     22   -552       C  
ATOM   3067  C   THR B  15      29.225  19.813   3.347  1.00 54.45           C  
ANISOU 3067  C   THR B  15     5924   7516   7247    292    -18   -526       C  
ATOM   3068  O   THR B  15      28.270  20.394   3.865  1.00 49.55           O  
ANISOU 3068  O   THR B  15     5317   6893   6616    273    -28   -530       O  
ATOM   3069  N   THR B  16      29.776  18.738   3.891  1.00 46.72           N  
ANISOU 3069  N   THR B  16     4931   6542   6277    314    -28   -511       N  
ATOM   3070  CA  THR B  16      29.188  18.156   5.086  1.00 56.07           C  
ANISOU 3070  CA  THR B  16     6118   7728   7457    317    -53   -498       C  
ATOM   3071  CB  THR B  16      29.571  16.660   5.248  1.00 72.74           C  
ANISOU 3071  CB  THR B  16     8221   9834   9585    351    -57   -480       C  
ATOM   3072  OG1 THR B  16      28.580  15.980   6.037  1.00 75.92           O  
ANISOU 3072  OG1 THR B  16     8635  10227   9984    357    -77   -469       O  
ATOM   3073  CG2 THR B  16      30.904  16.519   5.910  1.00 74.23           C  
ANISOU 3073  CG2 THR B  16     8376  10047   9781    355    -61   -460       C  
ATOM   3074  C   THR B  16      29.582  18.961   6.334  1.00 47.26           C  
ANISOU 3074  C   THR B  16     4986   6640   6331    292    -69   -491       C  
ATOM   3075  O   THR B  16      29.051  18.713   7.416  1.00 48.14           O  
ANISOU 3075  O   THR B  16     5100   6758   6434    289    -90   -481       O  
ATOM   3076  N   ASN B  17      30.488  19.933   6.199  1.00 40.23           N  
ANISOU 3076  N   ASN B  17     4079   5767   5442    274    -60   -497       N  
ATOM   3077  CA  ASN B  17      30.706  20.844   7.322  1.00 25.76           C  
ANISOU 3077  CA  ASN B  17     2232   3957   3597    246    -75   -499       C  
ATOM   3078  CB  ASN B  17      32.094  21.484   7.271  1.00 23.48           C  
ANISOU 3078  CB  ASN B  17     1916   3692   3316    233    -68   -498       C  
ATOM   3079  CG  ASN B  17      33.170  20.575   7.848  1.00 25.93           C  
ANISOU 3079  CG  ASN B  17     2196   4022   3633    251    -79   -473       C  
ATOM   3080  OD1 ASN B  17      32.896  19.429   8.202  1.00 33.08           O  
ANISOU 3080  OD1 ASN B  17     3104   4923   4541    275    -89   -455       O  
ATOM   3081  ND2 ASN B  17      34.400  21.087   7.950  1.00 19.96           N  
ANISOU 3081  ND2 ASN B  17     1412   3290   2883    240    -77   -468       N  
ATOM   3082  C   ASN B  17      29.614  21.915   7.362  1.00 27.72           C  
ANISOU 3082  C   ASN B  17     2503   4196   3834    220    -72   -519       C  
ATOM   3083  O   ASN B  17      29.297  22.455   8.427  1.00 27.10           O  
ANISOU 3083  O   ASN B  17     2423   4131   3743    200    -87   -524       O  
ATOM   3084  N   PHE B  18      29.019  22.222   6.214  1.00 26.02           N  
ANISOU 3084  N   PHE B  18     2306   3957   3622    221    -53   -530       N  
ATOM   3085  CA  PHE B  18      27.838  23.078   6.245  1.00 29.80           C  
ANISOU 3085  CA  PHE B  18     2806   4423   4094    201    -50   -543       C  
ATOM   3086  CB  PHE B  18      27.455  23.593   4.857  1.00 35.92           C  
ANISOU 3086  CB  PHE B  18     3595   5178   4875    199    -25   -551       C  
ATOM   3087  CG  PHE B  18      26.235  24.496   4.860  1.00 30.52           C  
ANISOU 3087  CG  PHE B  18     2931   4480   4187    179    -20   -560       C  
ATOM   3088  CD1 PHE B  18      26.342  25.834   5.215  1.00 37.30           C  
ANISOU 3088  CD1 PHE B  18     3782   5342   5047    150    -12   -571       C  
ATOM   3089  CE1 PHE B  18      25.223  26.666   5.213  1.00 40.91           C  
ANISOU 3089  CE1 PHE B  18     4255   5784   5504    133     -3   -576       C  
ATOM   3090  CZ  PHE B  18      23.979  26.157   4.850  1.00 36.62           C  
ANISOU 3090  CZ  PHE B  18     3733   5223   4956    145     -4   -568       C  
ATOM   3091  CE2 PHE B  18      23.856  24.832   4.506  1.00 33.63           C  
ANISOU 3091  CE2 PHE B  18     3362   4842   4573    172    -15   -559       C  
ATOM   3092  CD2 PHE B  18      24.984  24.004   4.504  1.00 43.62           C  
ANISOU 3092  CD2 PHE B  18     4613   6121   5841    189    -21   -556       C  
ATOM   3093  C   PHE B  18      26.693  22.285   6.865  1.00 28.58           C  
ANISOU 3093  C   PHE B  18     2669   4259   3930    212    -67   -535       C  
ATOM   3094  O   PHE B  18      25.856  22.846   7.577  1.00 22.74           O  
ANISOU 3094  O   PHE B  18     1939   3520   3181    196    -75   -540       O  
ATOM   3095  N   ASP B  19      26.670  20.977   6.614  1.00 24.26           N  
ANISOU 3095  N   ASP B  19     2125   3704   3388    241    -73   -522       N  
ATOM   3096  CA  ASP B  19      25.717  20.098   7.301  1.00 28.28           C  
ANISOU 3096  CA  ASP B  19     2647   4205   3892    254    -92   -510       C  
ATOM   3097  CB  ASP B  19      25.883  18.640   6.886  1.00 33.94           C  
ANISOU 3097  CB  ASP B  19     3364   4910   4622    287    -94   -498       C  
ATOM   3098  CG  ASP B  19      25.304  18.346   5.517  1.00 46.57           C  
ANISOU 3098  CG  ASP B  19     4983   6485   6228    298    -77   -510       C  
ATOM   3099  OD1 ASP B  19      24.548  19.185   4.986  1.00 41.81           O  
ANISOU 3099  OD1 ASP B  19     4394   5873   5618    281    -68   -522       O  
ATOM   3100  OD2 ASP B  19      25.602  17.258   4.976  1.00 57.84           O  
ANISOU 3100  OD2 ASP B  19     6407   7900   7667    324    -73   -507       O  
ATOM   3101  C   ASP B  19      25.908  20.217   8.803  1.00 26.87           C  
ANISOU 3101  C   ASP B  19     2455   4051   3702    243   -113   -501       C  
ATOM   3102  O   ASP B  19      24.930  20.286   9.560  1.00 23.66           O  
ANISOU 3102  O   ASP B  19     2061   3644   3284    237   -125   -498       O  
ATOM   3103  N   GLN B  20      27.172  20.244   9.219  1.00 24.97           N  
ANISOU 3103  N   GLN B  20     2189   3835   3463    241   -116   -495       N  
ATOM   3104  CA  GLN B  20      27.525  20.401  10.627  1.00 27.63           C  
ANISOU 3104  CA  GLN B  20     2509   4202   3787    228   -136   -487       C  
ATOM   3105  CB  GLN B  20      29.044  20.370  10.809  1.00 36.11           C  
ANISOU 3105  CB  GLN B  20     3551   5302   4867    228   -137   -478       C  
ATOM   3106  CG  GLN B  20      29.655  18.983  10.736  1.00 52.52           C  
ANISOU 3106  CG  GLN B  20     5615   7379   6959    260   -141   -450       C  
ATOM   3107  CD  GLN B  20      29.092  18.048  11.784  1.00 61.01           C  
ANISOU 3107  CD  GLN B  20     6692   8460   8028    273   -163   -426       C  
ATOM   3108  OE1 GLN B  20      28.651  18.481  12.851  1.00 61.48           O  
ANISOU 3108  OE1 GLN B  20     6754   8539   8068    255   -178   -426       O  
ATOM   3109  NE2 GLN B  20      29.108  16.755  11.490  1.00 71.74           N  
ANISOU 3109  NE2 GLN B  20     8051   9802   9405    304   -162   -404       N  
ATOM   3110  C   GLN B  20      26.979  21.690  11.227  1.00 20.86           C  
ANISOU 3110  C   GLN B  20     1658   3354   2914    196   -137   -508       C  
ATOM   3111  O   GLN B  20      26.460  21.676  12.342  1.00 21.73           O  
ANISOU 3111  O   GLN B  20     1770   3479   3008    189   -153   -504       O  
ATOM   3112  N   GLU B  21      27.129  22.801  10.501  1.00 22.85           N  
ANISOU 3112  N   GLU B  21     1912   3599   3172    177   -117   -530       N  
ATOM   3113  CA  GLU B  21      26.598  24.088  10.939  1.00 18.12           C  
ANISOU 3113  CA  GLU B  21     1319   3002   2564    147   -113   -552       C  
ATOM   3114  CB  GLU B  21      26.888  25.179   9.911  1.00 27.31           C  
ANISOU 3114  CB  GLU B  21     2483   4153   3743    130    -87   -570       C  
ATOM   3115  CG  GLU B  21      28.360  25.535   9.778  1.00 38.94           C  
ANISOU 3115  CG  GLU B  21     3929   5644   5223    122    -83   -573       C  
ATOM   3116  CD  GLU B  21      28.584  26.763   8.914  1.00 48.97           C  
ANISOU 3116  CD  GLU B  21     5198   6901   6507    101    -58   -590       C  
ATOM   3117  OE1 GLU B  21      27.772  27.710   8.998  1.00 40.75           O  
ANISOU 3117  OE1 GLU B  21     4169   5847   5467     81    -48   -606       O  
ATOM   3118  OE2 GLU B  21      29.573  26.779   8.147  1.00 59.21           O  
ANISOU 3118  OE2 GLU B  21     6480   8200   7816    106    -48   -585       O  
ATOM   3119  C   GLU B  21      25.087  24.015  11.173  1.00 18.38           C  
ANISOU 3119  C   GLU B  21     1377   3018   2590    149   -116   -552       C  
ATOM   3120  O   GLU B  21      24.564  24.614  12.105  1.00 21.51           O  
ANISOU 3120  O   GLU B  21     1774   3424   2973    131   -122   -563       O  
ATOM   3121  N   ALA B  22      24.389  23.283  10.306  1.00 19.26           N  
ANISOU 3121  N   ALA B  22     1506   3102   2709    171   -111   -540       N  
ATOM   3122  CA  ALA B  22      22.930  23.192  10.404  1.00 18.90           C  
ANISOU 3122  CA  ALA B  22     1484   3038   2659    173   -113   -537       C  
ATOM   3123  CB  ALA B  22      22.358  22.650   9.114  1.00 19.15           C  
ANISOU 3123  CB  ALA B  22     1532   3041   2702    191   -102   -530       C  
ATOM   3124  C   ALA B  22      22.515  22.321  11.588  1.00 18.70           C  
ANISOU 3124  C   ALA B  22     1459   3025   2620    185   -137   -519       C  
ATOM   3125  O   ALA B  22      21.580  22.652  12.325  1.00 17.02           O  
ANISOU 3125  O   ALA B  22     1255   2815   2396    176   -143   -520       O  
ATOM   3126  N   LEU B  23      23.216  21.216  11.793  1.00 19.69           N  
ANISOU 3126  N   LEU B  23     1573   3161   2748    205   -150   -499       N  
ATOM   3127  CA  LEU B  23      22.913  20.366  12.940  1.00 18.11           C  
ANISOU 3127  CA  LEU B  23     1370   2974   2536    216   -173   -477       C  
ATOM   3128  CB  LEU B  23      23.781  19.098  12.949  1.00 18.28           C  
ANISOU 3128  CB  LEU B  23     1377   3001   2569    242   -182   -452       C  
ATOM   3129  CG  LEU B  23      23.564  18.096  11.821  1.00 18.26           C  
ANISOU 3129  CG  LEU B  23     1386   2967   2587    268   -174   -444       C  
ATOM   3130  CD1 LEU B  23      24.575  16.927  11.919  1.00 23.89           C  
ANISOU 3130  CD1 LEU B  23     2078   3686   3315    293   -180   -421       C  
ATOM   3131  CD2 LEU B  23      22.160  17.575  11.802  1.00 19.26           C  
ANISOU 3131  CD2 LEU B  23     1536   3069   2713    278   -181   -435       C  
ATOM   3132  C   LEU B  23      23.113  21.138  14.239  1.00 25.26           C  
ANISOU 3132  C   LEU B  23     2263   3913   3420    193   -183   -486       C  
ATOM   3133  O   LEU B  23      22.287  21.061  15.155  1.00 17.86           O  
ANISOU 3133  O   LEU B  23     1333   2984   2468    191   -195   -479       O  
ATOM   3134  N   LEU B  24      24.199  21.901  14.315  1.00 19.78           N  
ANISOU 3134  N   LEU B  24     1550   3241   2725    174   -178   -503       N  
ATOM   3135  CA  LEU B  24      24.479  22.679  15.522  1.00 20.38           C  
ANISOU 3135  CA  LEU B  24     1613   3352   2780    148   -187   -517       C  
ATOM   3136  CB  LEU B  24      25.843  23.378  15.397  1.00 18.53           C  
ANISOU 3136  CB  LEU B  24     1354   3138   2549    130   -182   -533       C  
ATOM   3137  CG  LEU B  24      26.254  24.166  16.638  1.00 28.51           C  
ANISOU 3137  CG  LEU B  24     2602   4441   3790    100   -192   -551       C  
ATOM   3138  CD1 LEU B  24      26.576  23.217  17.780  1.00 29.93           C  
ANISOU 3138  CD1 LEU B  24     2767   4654   3950    111   -218   -522       C  
ATOM   3139  CD2 LEU B  24      27.457  25.041  16.315  1.00 26.03           C  
ANISOU 3139  CD2 LEU B  24     2267   4139   3484     78   -183   -571       C  
ATOM   3140  C   LEU B  24      23.386  23.719  15.799  1.00 21.06           C  
ANISOU 3140  C   LEU B  24     1713   3431   2857    127   -178   -542       C  
ATOM   3141  O   LEU B  24      22.898  23.864  16.920  1.00 19.10           O  
ANISOU 3141  O   LEU B  24     1465   3204   2588    118   -190   -544       O  
ATOM   3142  N   TYR B  25      23.024  24.446  14.752  1.00 14.30           N  
ANISOU 3142  N   TYR B  25      869   2545   2018    120   -156   -559       N  
ATOM   3143  CA  TYR B  25      21.949  25.413  14.775  1.00 15.45           C  
ANISOU 3143  CA  TYR B  25     1030   2677   2164    104   -142   -578       C  
ATOM   3144  CB  TYR B  25      21.716  25.898  13.350  1.00 15.98           C  
ANISOU 3144  CB  TYR B  25     1107   2708   2254    104   -117   -584       C  
ATOM   3145  CG  TYR B  25      20.601  26.885  13.181  1.00 19.38           C  
ANISOU 3145  CG  TYR B  25     1552   3119   2693     89    -97   -599       C  
ATOM   3146  CD1 TYR B  25      19.292  26.459  12.941  1.00 16.33           C  
ANISOU 3146  CD1 TYR B  25     1186   2711   2308    104    -97   -581       C  
ATOM   3147  CE1 TYR B  25      18.259  27.381  12.778  1.00 17.74           C  
ANISOU 3147  CE1 TYR B  25     1374   2870   2496     90    -76   -590       C  
ATOM   3148  CZ  TYR B  25      18.535  28.739  12.843  1.00 16.39           C  
ANISOU 3148  CZ  TYR B  25     1194   2699   2336     62    -54   -619       C  
ATOM   3149  OH  TYR B  25      17.530  29.666  12.670  1.00 18.63           O  
ANISOU 3149  OH  TYR B  25     1499   2952   2628     49    -29   -619       O  
ATOM   3150  CE2 TYR B  25      19.835  29.174  13.062  1.00 16.42           C  
ANISOU 3150  CE2 TYR B  25     1179   2722   2338     46    -55   -639       C  
ATOM   3151  CD2 TYR B  25      20.851  28.248  13.233  1.00 17.74           C  
ANISOU 3151  CD2 TYR B  25     1335   2911   2493     59    -77   -628       C  
ATOM   3152  C   TYR B  25      20.663  24.811  15.363  1.00 18.95           C  
ANISOU 3152  C   TYR B  25     1489   3116   2596    118   -153   -561       C  
ATOM   3153  O   TYR B  25      20.007  25.447  16.179  1.00 17.79           O  
ANISOU 3153  O   TYR B  25     1343   2979   2436    102   -152   -575       O  
ATOM   3154  N   HIS B  26      20.331  23.581  14.962  1.00 15.34           N  
ANISOU 3154  N   HIS B  26     1042   2642   2143    146   -163   -531       N  
ATOM   3155  CA  HIS B  26      19.082  22.959  15.405  1.00 15.46           C  
ANISOU 3155  CA  HIS B  26     1074   2648   2152    161   -174   -510       C  
ATOM   3156  CB  HIS B  26      18.691  21.796  14.483  1.00 19.03           C  
ANISOU 3156  CB  HIS B  26     1541   3071   2621    188   -177   -485       C  
ATOM   3157  CG  HIS B  26      18.077  22.254  13.197  1.00 17.99           C  
ANISOU 3157  CG  HIS B  26     1424   2907   2505    186   -157   -494       C  
ATOM   3158  ND1 HIS B  26      18.826  22.800  12.179  1.00 16.23           N  
ANISOU 3158  ND1 HIS B  26     1196   2676   2295    178   -139   -510       N  
ATOM   3159  CE1 HIS B  26      18.024  23.151  11.187  1.00 14.33           C  
ANISOU 3159  CE1 HIS B  26      970   2410   2066    177   -123   -512       C  
ATOM   3160  NE2 HIS B  26      16.777  22.884  11.546  1.00 15.20           N  
ANISOU 3160  NE2 HIS B  26     1094   2510   2172    183   -130   -498       N  
ATOM   3161  CD2 HIS B  26      16.783  22.336  12.806  1.00 16.62           C  
ANISOU 3161  CD2 HIS B  26     1269   2710   2337    189   -151   -486       C  
ATOM   3162  C   HIS B  26      19.137  22.484  16.846  1.00 16.05           C  
ANISOU 3162  C   HIS B  26     1138   2756   2203    163   -196   -497       C  
ATOM   3163  O   HIS B  26      18.108  22.348  17.486  1.00 17.38           O  
ANISOU 3163  O   HIS B  26     1316   2926   2361    166   -203   -487       O  
ATOM   3164  N   GLN B  27      20.329  22.237  17.372  1.00 23.97           N  
ANISOU 3164  N   GLN B  27     2121   3789   3198    160   -207   -494       N  
ATOM   3165  CA  GLN B  27      20.407  21.708  18.730  1.00 26.94           C  
ANISOU 3165  CA  GLN B  27     2487   4200   3551    163   -229   -476       C  
ATOM   3166  CB  GLN B  27      21.328  20.485  18.773  1.00 28.51           C  
ANISOU 3166  CB  GLN B  27     2670   4406   3756    184   -243   -443       C  
ATOM   3167  CG  GLN B  27      22.781  20.838  18.581  1.00 36.46           C  
ANISOU 3167  CG  GLN B  27     3655   5432   4766    172   -240   -456       C  
ATOM   3168  CD  GLN B  27      23.706  19.715  18.995  1.00 64.97           C  
ANISOU 3168  CD  GLN B  27     7246   9062   8380    190   -256   -421       C  
ATOM   3169  OE1 GLN B  27      23.267  18.585  19.209  1.00 71.40           O  
ANISOU 3169  OE1 GLN B  27     8063   9865   9199    214   -267   -387       O  
ATOM   3170  NE2 GLN B  27      24.993  20.021  19.121  1.00 73.99           N  
ANISOU 3170  NE2 GLN B  27     8363  10229   9520    178   -258   -428       N  
ATOM   3171  C   GLN B  27      20.877  22.731  19.752  1.00 27.93           C  
ANISOU 3171  C   GLN B  27     2596   4366   3651    133   -231   -505       C  
ATOM   3172  O   GLN B  27      20.777  22.482  20.950  1.00 33.61           O  
ANISOU 3172  O   GLN B  27     3307   5118   4344    130   -247   -494       O  
ATOM   3173  N   GLN B  28      21.381  23.878  19.295  1.00 21.86           N  
ANISOU 3173  N   GLN B  28     1821   3596   2889    108   -214   -541       N  
ATOM   3174  CA  GLN B  28      21.918  24.881  20.215  1.00 27.04           C  
ANISOU 3174  CA  GLN B  28     2460   4289   3523     76   -215   -573       C  
ATOM   3175  CB  GLN B  28      22.627  25.993  19.436  1.00 31.37           C  
ANISOU 3175  CB  GLN B  28     3002   4826   4090     52   -195   -607       C  
ATOM   3176  CG  GLN B  28      21.697  27.011  18.804  1.00 38.84           C  
ANISOU 3176  CG  GLN B  28     3963   5739   5054     40   -169   -634       C  
ATOM   3177  CD  GLN B  28      22.434  28.051  17.979  1.00 60.55           C  
ANISOU 3177  CD  GLN B  28     6705   8475   7826     18   -147   -662       C  
ATOM   3178  OE1 GLN B  28      23.604  27.875  17.636  1.00 70.90           O  
ANISOU 3178  OE1 GLN B  28     8002   9794   9143     18   -151   -656       O  
ATOM   3179  NE2 GLN B  28      21.759  29.153  17.676  1.00 62.99           N  
ANISOU 3179  NE2 GLN B  28     7022   8761   8150     -1   -122   -689       N  
ATOM   3180  C   GLN B  28      20.827  25.471  21.118  1.00 32.15           C  
ANISOU 3180  C   GLN B  28     3115   4949   4150     62   -214   -592       C  
ATOM   3181  O   GLN B  28      19.681  25.608  20.700  1.00 35.53           O  
ANISOU 3181  O   GLN B  28     3561   5347   4590     70   -201   -591       O  
ATOM   3182  N   GLY B  29      21.186  25.797  22.361  1.00 26.18           N  
ANISOU 3182  N   GLY B  29     2345   4239   3363     42   -226   -606       N  
ATOM   3183  CA  GLY B  29      20.224  26.327  23.321  1.00 18.84           C  
ANISOU 3183  CA  GLY B  29     1420   3329   2410     28   -224   -626       C  
ATOM   3184  C   GLY B  29      19.060  25.358  23.503  1.00 24.13           C  
ANISOU 3184  C   GLY B  29     2105   3987   3076     59   -233   -588       C  
ATOM   3185  O   GLY B  29      19.202  24.308  24.117  1.00 45.11           O  
ANISOU 3185  O   GLY B  29     4758   6664   5718     77   -255   -550       O  
ATOM   3186  N   LYS B  30      17.907  25.715  22.971  1.00 31.27           N  
ANISOU 3186  N   LYS B  30     3026   4857   3998     64   -216   -594       N  
ATOM   3187  CA  LYS B  30      16.736  24.844  23.065  1.00 31.86           C  
ANISOU 3187  CA  LYS B  30     3117   4917   4073     92   -223   -556       C  
ATOM   3188  CB  LYS B  30      15.429  25.625  23.157  1.00 41.02           C  
ANISOU 3188  CB  LYS B  30     4302   6052   5233     84   -201   -568       C  
ATOM   3189  CG  LYS B  30      15.430  26.881  23.995  1.00 52.77           C  
ANISOU 3189  CG  LYS B  30     5793   7557   6699     51   -184   -611       C  
ATOM   3190  CD  LYS B  30      14.092  27.594  23.817  1.00 62.29           C  
ANISOU 3190  CD  LYS B  30     7035   8718   7915     48   -154   -613       C  
ATOM   3191  CE  LYS B  30      14.186  29.089  24.100  1.00 67.27           C  
ANISOU 3191  CE  LYS B  30     7673   9343   8544     12   -125   -663       C  
ATOM   3192  NZ  LYS B  30      13.694  29.439  25.465  1.00 69.82           N  
ANISOU 3192  NZ  LYS B  30     8001   9697   8830      0   -123   -679       N  
ATOM   3193  C   LYS B  30      16.718  23.991  21.814  1.00 27.40           C  
ANISOU 3193  C   LYS B  30     2565   4307   3539    118   -222   -525       C  
ATOM   3194  O   LYS B  30      16.943  24.506  20.726  1.00 31.20           O  
ANISOU 3194  O   LYS B  30     3050   4758   4045    112   -205   -541       O  
ATOM   3195  N   PRO B  31      16.434  22.695  21.956  1.00 23.55           N  
ANISOU 3195  N   PRO B  31     2083   3813   3050    146   -240   -480       N  
ATOM   3196  CA  PRO B  31      16.225  21.911  20.738  1.00 16.70           C  
ANISOU 3196  CA  PRO B  31     1231   2901   2213    169   -237   -455       C  
ATOM   3197  CB  PRO B  31      15.802  20.539  21.277  1.00 23.52           C  
ANISOU 3197  CB  PRO B  31     2100   3765   3073    195   -257   -408       C  
ATOM   3198  CG  PRO B  31      16.389  20.487  22.658  1.00 27.06           C  
ANISOU 3198  CG  PRO B  31     2529   4263   3490    187   -273   -404       C  
ATOM   3199  CD  PRO B  31      16.260  21.883  23.173  1.00 27.10           C  
ANISOU 3199  CD  PRO B  31     2528   4294   3474    157   -262   -449       C  
ATOM   3200  C   PRO B  31      15.145  22.493  19.827  1.00 12.95           C  
ANISOU 3200  C   PRO B  31      775   2388   1758    168   -217   -466       C  
ATOM   3201  O   PRO B  31      14.095  22.992  20.288  1.00 18.14           O  
ANISOU 3201  O   PRO B  31     1439   3047   2408    163   -211   -470       O  
ATOM   3202  N   GLY B  32      15.400  22.415  18.525  1.00 16.07           N  
ANISOU 3202  N   GLY B  32     1177   2750   2179    173   -206   -467       N  
ATOM   3203  CA  GLY B  32      14.410  22.847  17.553  1.00 13.59           C  
ANISOU 3203  CA  GLY B  32      880   2400   1884    173   -188   -470       C  
ATOM   3204  C   GLY B  32      14.440  24.343  17.311  1.00 16.75           C  
ANISOU 3204  C   GLY B  32     1286   2790   2287    145   -160   -503       C  
ATOM   3205  O   GLY B  32      15.374  25.037  17.737  1.00 20.94           O  
ANISOU 3205  O   GLY B  32     1798   3347   2810    125   -157   -533       O  
ATOM   3206  N   LYS B  33      13.425  24.848  16.620  1.00 14.90           N  
ANISOU 3206  N   LYS B  33     1078   2518   2066    142   -139   -496       N  
ATOM   3207  CA  LYS B  33      13.470  26.216  16.147  1.00 15.03           C  
ANISOU 3207  CA  LYS B  33     1100   2516   2094    117   -109   -522       C  
ATOM   3208  CB  LYS B  33      13.541  26.241  14.617  1.00 11.49           C  
ANISOU 3208  CB  LYS B  33      659   2037   1670    121    -95   -516       C  
ATOM   3209  CG  LYS B  33      14.882  25.704  14.075  1.00 12.41           C  
ANISOU 3209  CG  LYS B  33      753   2169   1792    128   -106   -525       C  
ATOM   3210  CD  LYS B  33      14.833  25.655  12.552  1.00 15.47           C  
ANISOU 3210  CD  LYS B  33     1150   2528   2199    134    -92   -517       C  
ATOM   3211  CE  LYS B  33      13.802  24.626  12.068  1.00 16.77           C  
ANISOU 3211  CE  LYS B  33     1336   2671   2365    155   -103   -485       C  
ATOM   3212  NZ  LYS B  33      14.194  24.053  10.763  1.00 18.63           N  
ANISOU 3212  NZ  LYS B  33     1573   2894   2613    166   -101   -481       N  
ATOM   3213  C   LYS B  33      12.291  27.055  16.614  1.00 18.47           C  
ANISOU 3213  C   LYS B  33     1557   2934   2527    106    -89   -521       C  
ATOM   3214  O   LYS B  33      12.233  28.235  16.310  1.00 18.50           O  
ANISOU 3214  O   LYS B  33     1565   2920   2542     87    -61   -540       O  
ATOM   3215  N   ILE B  34      11.350  26.461  17.337  1.00 14.77           N  
ANISOU 3215  N   ILE B  34     1099   2469   2044    120   -101   -496       N  
ATOM   3216  CA  ILE B  34      10.145  27.207  17.703  1.00 15.46           C  
ANISOU 3216  CA  ILE B  34     1208   2537   2131    112    -80   -491       C  
ATOM   3217  CB  ILE B  34       8.894  26.692  16.929  1.00 18.45           C  
ANISOU 3217  CB  ILE B  34     1607   2880   2522    129    -78   -449       C  
ATOM   3218  CG1 ILE B  34       8.565  25.241  17.284  1.00 20.58           C  
ANISOU 3218  CG1 ILE B  34     1877   3162   2782    154   -111   -417       C  
ATOM   3219  CD1 ILE B  34       7.340  25.077  18.127  1.00 27.39           C  
ANISOU 3219  CD1 ILE B  34     2752   4023   3633    162   -112   -391       C  
ATOM   3220  CG2 ILE B  34       9.121  26.852  15.433  1.00 22.64           C  
ANISOU 3220  CG2 ILE B  34     2141   3385   3078    128    -66   -447       C  
ATOM   3221  C   ILE B  34       9.874  27.186  19.193  1.00 18.65           C  
ANISOU 3221  C   ILE B  34     1609   2970   2506    111    -89   -495       C  
ATOM   3222  O   ILE B  34      10.364  26.315  19.922  1.00 19.71           O  
ANISOU 3222  O   ILE B  34     1727   3140   2621    121   -117   -490       O  
ATOM   3223  N   GLU B  35       9.116  28.192  19.625  1.00 17.11           N  
ANISOU 3223  N   GLU B  35     1429   2762   2311     97    -62   -506       N  
ATOM   3224  CA  GLU B  35       8.679  28.354  20.999  1.00 19.69           C  
ANISOU 3224  CA  GLU B  35     1757   3113   2610     94    -62   -512       C  
ATOM   3225  CB  GLU B  35       9.633  29.285  21.758  1.00 20.93           C  
ANISOU 3225  CB  GLU B  35     1901   3299   2753     66    -53   -563       C  
ATOM   3226  CG  GLU B  35       9.339  29.440  23.222  1.00 44.45           C  
ANISOU 3226  CG  GLU B  35     4880   6312   5697     60    -55   -576       C  
ATOM   3227  CD  GLU B  35      10.434  30.213  23.941  1.00 57.05           C  
ANISOU 3227  CD  GLU B  35     6459   7942   7275     30    -53   -628       C  
ATOM   3228  OE1 GLU B  35      11.405  30.642  23.267  1.00 53.24           O  
ANISOU 3228  OE1 GLU B  35     5964   7453   6810     14    -49   -652       O  
ATOM   3229  OE2 GLU B  35      10.325  30.378  25.177  1.00 56.53           O  
ANISOU 3229  OE2 GLU B  35     6392   7911   7176     20    -55   -645       O  
ATOM   3230  C   GLU B  35       7.283  28.941  20.948  1.00 21.37           C  
ANISOU 3230  C   GLU B  35     1994   3290   2833     96    -34   -494       C  
ATOM   3231  O   GLU B  35       6.978  29.712  20.029  1.00 19.08           O  
ANISOU 3231  O   GLU B  35     1715   2963   2572     88     -6   -495       O  
ATOM   3232  N   VAL B  36       6.417  28.558  21.887  1.00 15.28           N  
ANISOU 3232  N   VAL B  36     1231   2533   2043    107    -40   -474       N  
ATOM   3233  CA  VAL B  36       5.089  29.158  21.965  1.00 15.44           C  
ANISOU 3233  CA  VAL B  36     1273   2522   2073    109    -11   -457       C  
ATOM   3234  CB  VAL B  36       3.966  28.107  22.070  1.00 19.66           C  
ANISOU 3234  CB  VAL B  36     1816   3052   2603    136    -29   -403       C  
ATOM   3235  CG1 VAL B  36       2.610  28.792  22.281  1.00 22.79           C  
ANISOU 3235  CG1 VAL B  36     2232   3421   3008    138      3   -385       C  
ATOM   3236  CG2 VAL B  36       3.947  27.217  20.827  1.00 21.04           C  
ANISOU 3236  CG2 VAL B  36     1991   3205   2800    150    -48   -371       C  
ATOM   3237  C   VAL B  36       5.050  30.058  23.187  1.00 22.84           C  
ANISOU 3237  C   VAL B  36     2212   3478   2988     93      9   -492       C  
ATOM   3238  O   VAL B  36       5.329  29.605  24.304  1.00 24.83           O  
ANISOU 3238  O   VAL B  36     2454   3774   3206     94    -11   -500       O  
ATOM   3239  N   ILE B  37       4.709  31.327  22.980  1.00 18.08           N  
ANISOU 3239  N   ILE B  37     1621   2843   2405     76     50   -513       N  
ATOM   3240  CA  ILE B  37       4.678  32.278  24.087  1.00 17.74           C  
ANISOU 3240  CA  ILE B  37     1583   2813   2344     57     75   -554       C  
ATOM   3241  CB  ILE B  37       5.745  33.373  23.933  1.00 22.33           C  
ANISOU 3241  CB  ILE B  37     2156   3391   2937     26     95   -610       C  
ATOM   3242  CG1 ILE B  37       5.526  34.157  22.634  1.00 21.79           C  
ANISOU 3242  CG1 ILE B  37     2095   3269   2916     21    127   -602       C  
ATOM   3243  CD1 ILE B  37       6.344  35.453  22.563  1.00 28.14           C  
ANISOU 3243  CD1 ILE B  37     2894   4060   3738    -11    157   -656       C  
ATOM   3244  CG2 ILE B  37       7.143  32.762  23.944  1.00 24.36           C  
ANISOU 3244  CG2 ILE B  37     2390   3690   3178     20     58   -628       C  
ATOM   3245  C   ILE B  37       3.333  32.946  24.207  1.00 21.00           C  
ANISOU 3245  C   ILE B  37     2017   3191   2773     63    113   -536       C  
ATOM   3246  O   ILE B  37       2.521  32.891  23.287  1.00 21.76           O  
ANISOU 3246  O   ILE B  37     2122   3248   2898     76    124   -496       O  
ATOM   3247  N   SER B  38       3.118  33.597  25.343  1.00 22.50           N  
ANISOU 3247  N   SER B  38     2676   2877   2995   -214     54   -654       N  
ATOM   3248  CA  SER B  38       1.875  34.318  25.564  1.00 25.82           C  
ANISOU 3248  CA  SER B  38     3099   3268   3442   -207     87   -677       C  
ATOM   3249  CB  SER B  38       1.558  34.425  27.053  1.00 27.90           C  
ANISOU 3249  CB  SER B  38     3374   3550   3677   -235    109   -709       C  
ATOM   3250  OG  SER B  38       0.366  35.173  27.239  1.00 29.16           O  
ANISOU 3250  OG  SER B  38     3536   3677   3867   -226    147   -731       O  
ATOM   3251  C   SER B  38       1.965  35.696  24.948  1.00 30.00           C  
ANISOU 3251  C   SER B  38     3634   3757   4009   -204    106   -692       C  
ATOM   3252  O   SER B  38       2.994  36.363  25.034  1.00 31.66           O  
ANISOU 3252  O   SER B  38     3851   3968   4210   -226    105   -706       O  
ATOM   3253  N   SER B  39       0.885  36.127  24.315  1.00 27.20           N  
ANISOU 3253  N   SER B  39     3274   3366   3695   -177    122   -688       N  
ATOM   3254  CA  SER B  39       0.844  37.475  23.769  1.00 26.96           C  
ANISOU 3254  CA  SER B  39     3250   3293   3702   -170    144   -702       C  
ATOM   3255  CB  SER B  39       0.040  37.488  22.469  1.00 30.03           C  
ANISOU 3255  CB  SER B  39     3627   3651   4132   -131    137   -672       C  
ATOM   3256  OG  SER B  39      -1.299  37.061  22.720  1.00 26.12           O  
ANISOU 3256  OG  SER B  39     3118   3155   3652   -114    146   -667       O  
ATOM   3257  C   SER B  39       0.238  38.460  24.779  1.00 30.55           C  
ANISOU 3257  C   SER B  39     3714   3728   4165   -185    188   -742       C  
ATOM   3258  O   SER B  39       0.079  39.637  24.474  1.00 34.91           O  
ANISOU 3258  O   SER B  39     4274   4240   4749   -179    214   -757       O  
ATOM   3259  N   LYS B  40      -0.081  37.969  25.976  1.00 26.82           N  
ANISOU 3259  N   LYS B  40     3246   3283   3662   -204    198   -760       N  
ATOM   3260  CA  LYS B  40      -0.771  38.760  27.015  1.00 28.53           C  
ANISOU 3260  CA  LYS B  40     3475   3482   3884   -217    245   -799       C  
ATOM   3261  CB  LYS B  40      -2.271  38.405  27.045  1.00 29.21           C  
ANISOU 3261  CB  LYS B  40     3544   3556   3998   -189    265   -791       C  
ATOM   3262  CG  LYS B  40      -3.020  38.420  25.693  1.00 34.72           C  
ANISOU 3262  CG  LYS B  40     4219   4226   4748   -145    253   -756       C  
ATOM   3263  CD  LYS B  40      -3.299  39.837  25.232  1.00 30.50           C  
ANISOU 3263  CD  LYS B  40     3689   3641   4260   -129    284   -768       C  
ATOM   3264  CE  LYS B  40      -3.614  39.913  23.754  1.00 25.59           C  
ANISOU 3264  CE  LYS B  40     3049   2994   3679    -91    261   -730       C  
ATOM   3265  NZ  LYS B  40      -5.002  39.486  23.454  1.00 19.51           N  
ANISOU 3265  NZ  LYS B  40     2251   2219   2943    -60    262   -708       N  
ATOM   3266  C   LYS B  40      -0.160  38.524  28.414  1.00 26.15           C  
ANISOU 3266  C   LYS B  40     3192   3217   3525   -262    249   -828       C  
ATOM   3267  O   LYS B  40       0.498  37.515  28.652  1.00 25.30           O  
ANISOU 3267  O   LYS B  40     3082   3153   3379   -274    214   -811       O  
ATOM   3268  N   PRO B  41      -0.406  39.438  29.370  1.00 28.42           N  
ANISOU 3268  N   PRO B  41     3502   3488   3808   -286    292   -871       N  
ATOM   3269  CA  PRO B  41       0.082  39.180  30.737  1.00 28.33           C  
ANISOU 3269  CA  PRO B  41     3512   3513   3738   -330    294   -898       C  
ATOM   3270  CB  PRO B  41      -0.450  40.384  31.532  1.00 31.85           C  
ANISOU 3270  CB  PRO B  41     3984   3923   4193   -349    352   -945       C  
ATOM   3271  CG  PRO B  41      -0.615  41.463  30.501  1.00 31.56           C  
ANISOU 3271  CG  PRO B  41     3942   3834   4214   -323    371   -944       C  
ATOM   3272  CD  PRO B  41      -1.009  40.776  29.230  1.00 32.63           C  
ANISOU 3272  CD  PRO B  41     4045   3967   4386   -276    339   -895       C  
ATOM   3273  C   PRO B  41      -0.434  37.874  31.356  1.00 27.83           C  
ANISOU 3273  C   PRO B  41     3443   3488   3645   -327    282   -882       C  
ATOM   3274  O   PRO B  41      -1.642  37.620  31.345  1.00 27.50           O  
ANISOU 3274  O   PRO B  41     3391   3431   3629   -302    306   -877       O  
ATOM   3275  N   CYS B  42       0.465  37.059  31.909  1.00 25.39           N  
ANISOU 3275  N   CYS B  42     3139   3227   3281   -353    247   -873       N  
ATOM   3276  CA  CYS B  42       0.061  35.778  32.491  1.00 27.04           C  
ANISOU 3276  CA  CYS B  42     3344   3470   3458   -350    235   -855       C  
ATOM   3277  CB  CYS B  42       0.142  34.680  31.422  1.00 23.81           C  
ANISOU 3277  CB  CYS B  42     2909   3074   3065   -316    194   -806       C  
ATOM   3278  SG  CYS B  42       1.801  34.506  30.741  1.00 34.64           S  
ANISOU 3278  SG  CYS B  42     4272   4469   4421   -324    144   -782       S  
ATOM   3279  C   CYS B  42       0.890  35.362  33.711  1.00 31.76           C  
ANISOU 3279  C   CYS B  42     3964   4115   3988   -393    218   -867       C  
ATOM   3280  O   CYS B  42       1.133  34.176  33.929  1.00 32.02           O  
ANISOU 3280  O   CYS B  42     3992   4186   3989   -391    187   -839       O  
ATOM   3281  N   ALA B  43       1.306  36.331  34.519  1.00 34.23           N  
ANISOU 3281  N   ALA B  43     4303   4425   4277   -433    238   -908       N  
ATOM   3282  CA  ALA B  43       2.167  36.044  35.668  1.00 43.58           C  
ANISOU 3282  CA  ALA B  43     5510   5656   5393   -478    217   -920       C  
ATOM   3283  CB  ALA B  43       3.236  37.122  35.791  1.00 39.31           C  
ANISOU 3283  CB  ALA B  43     4982   5115   4841   -517    211   -948       C  
ATOM   3284  C   ALA B  43       1.395  35.913  36.991  1.00 46.36           C  
ANISOU 3284  C   ALA B  43     5893   6016   5707   -502    253   -947       C  
ATOM   3285  O   ALA B  43       1.645  34.999  37.781  1.00 47.81           O  
ANISOU 3285  O   ALA B  43     6086   6243   5838   -518    231   -935       O  
ATOM   3286  N   THR B  44       0.457  36.824  37.221  1.00 38.24           N  
ANISOU 3286  N   THR B  44     4880   4944   4705   -501    311   -983       N  
ATOM   3287  CA  THR B  44      -0.253  36.890  38.495  1.00 42.25           C  
ANISOU 3287  CA  THR B  44     5421   5453   5179   -526    354  -1013       C  
ATOM   3288  CB  THR B  44      -0.617  38.331  38.836  1.00 44.10           C  
ANISOU 3288  CB  THR B  44     5677   5641   5436   -535    406  -1041       C  
ATOM   3289  OG1 THR B  44      -1.669  38.770  37.968  1.00 42.79           O  
ANISOU 3289  OG1 THR B  44     5491   5425   5343   -493    444  -1044       O  
ATOM   3290  CG2 THR B  44       0.600  39.241  38.672  1.00 41.71           C  
ANISOU 3290  CG2 THR B  44     5381   5339   5125   -561    382  -1045       C  
ATOM   3291  C   THR B  44      -1.534  36.061  38.515  1.00 42.84           C  
ANISOU 3291  C   THR B  44     5484   5521   5273   -494    379   -999       C  
ATOM   3292  O   THR B  44      -2.008  35.596  37.477  1.00 32.06           O  
ANISOU 3292  O   THR B  44     4083   4142   3956   -450    367   -965       O  
ATOM   3293  N   GLU B  45      -2.111  35.883  39.697  1.00 41.07           N  
ANISOU 3293  N   GLU B  45     5290   5303   5010   -517    414  -1022       N  
ATOM   3294  CA  GLU B  45      -3.368  35.155  39.786  1.00 42.91           C  
ANISOU 3294  CA  GLU B  45     5511   5528   5264   -489    444  -1008       C  
ATOM   3295  CB  GLU B  45      -3.741  34.878  41.245  1.00 55.48           C  
ANISOU 3295  CB  GLU B  45     7145   7138   6798   -525    478  -1033       C  
ATOM   3296  CG  GLU B  45      -5.209  34.540  41.451  1.00 69.64           C  
ANISOU 3296  CG  GLU B  45     8930   8909   8623   -502    532  -1035       C  
ATOM   3297  CD  GLU B  45      -5.459  33.747  42.718  1.00 83.35           C  
ANISOU 3297  CD  GLU B  45    10700  10674  10294   -530    547  -1039       C  
ATOM   3298  OE1 GLU B  45      -4.474  33.307  43.350  1.00 87.39           O  
ANISOU 3298  OE1 GLU B  45    11236  11228  10738   -561    505  -1029       O  
ATOM   3299  OE2 GLU B  45      -6.641  33.567  43.082  1.00 88.41           O  
ANISOU 3299  OE2 GLU B  45    11340  11296  10955   -519    599  -1046       O  
ATOM   3300  C   GLU B  45      -4.474  35.941  39.077  1.00 37.88           C  
ANISOU 3300  C   GLU B  45     4852   4836   4706   -453    492  -1018       C  
ATOM   3301  O   GLU B  45      -5.383  35.353  38.479  1.00 35.76           O  
ANISOU 3301  O   GLU B  45     4550   4557   4481   -415    497   -991       O  
ATOM   3302  N   LYS B  46      -4.386  37.267  39.133  1.00 35.02           N  
ANISOU 3302  N   LYS B  46     4506   4438   4363   -464    525  -1051       N  
ATOM   3303  CA  LYS B  46      -5.345  38.122  38.437  1.00 31.36           C  
ANISOU 3303  CA  LYS B  46     4020   3919   3976   -427    570  -1058       C  
ATOM   3304  CB  LYS B  46      -5.142  39.592  38.814  1.00 36.24           C  
ANISOU 3304  CB  LYS B  46     4666   4503   4603   -444    604  -1078       C  
ATOM   3305  CG  LYS B  46      -6.022  40.548  38.017  1.00 34.34           C  
ANISOU 3305  CG  LYS B  46     4402   4204   4443   -404    645  -1079       C  
ATOM   3306  CD  LYS B  46      -7.496  40.254  38.243  1.00 40.23           C  
ANISOU 3306  CD  LYS B  46     5130   4930   5226   -376    695  -1080       C  
ATOM   3307  CE  LYS B  46      -8.379  40.949  37.211  1.00 47.47           C  
ANISOU 3307  CE  LYS B  46     6010   5796   6229   -326    722  -1069       C  
ATOM   3308  NZ  LYS B  46      -8.060  42.397  37.083  1.00 50.27           N  
ANISOU 3308  NZ  LYS B  46     6384   6111   6607   -329    745  -1079       N  
ATOM   3309  C   LYS B  46      -5.242  37.951  36.922  1.00 32.42           C  
ANISOU 3309  C   LYS B  46     4111   4044   4165   -385    529  -1021       C  
ATOM   3310  O   LYS B  46      -6.263  37.827  36.243  1.00 29.40           O  
ANISOU 3310  O   LYS B  46     3694   3637   3839   -343    544  -1000       O  
ATOM   3311  N   ASP B  47      -4.014  37.950  36.400  1.00 31.35           N  
ANISOU 3311  N   ASP B  47     3974   3928   4010   -395    477  -1007       N  
ATOM   3312  CA  ASP B  47      -3.777  37.716  34.972  1.00 29.61           C  
ANISOU 3312  CA  ASP B  47     3717   3702   3832   -358    434   -966       C  
ATOM   3313  CB  ASP B  47      -2.278  37.682  34.640  1.00 29.63           C  
ANISOU 3313  CB  ASP B  47     3724   3731   3803   -379    381   -956       C  
ATOM   3314  CG  ASP B  47      -1.585  39.016  34.863  1.00 45.48           C  
ANISOU 3314  CG  ASP B  47     5757   5716   5807   -409    401   -994       C  
ATOM   3315  OD1 ASP B  47      -2.264  40.065  34.796  1.00 45.28           O  
ANISOU 3315  OD1 ASP B  47     5739   5642   5822   -399    451  -1020       O  
ATOM   3316  OD2 ASP B  47      -0.349  39.009  35.084  1.00 45.93           O  
ANISOU 3316  OD2 ASP B  47     5826   5803   5822   -442    366   -998       O  
ATOM   3317  C   ASP B  47      -4.404  36.390  34.556  1.00 28.80           C  
ANISOU 3317  C   ASP B  47     3584   3620   3738   -329    409   -925       C  
ATOM   3318  O   ASP B  47      -5.086  36.290  33.531  1.00 24.49           O  
ANISOU 3318  O   ASP B  47     3005   3052   3247   -289    405   -899       O  
ATOM   3319  N   LEU B  48      -4.164  35.368  35.368  1.00 24.01           N  
ANISOU 3319  N   LEU B  48     2991   3056   3076   -350    392   -918       N  
ATOM   3320  CA  LEU B  48      -4.578  34.023  35.010  1.00 25.56           C  
ANISOU 3320  CA  LEU B  48     3164   3275   3274   -328    365   -879       C  
ATOM   3321  CB  LEU B  48      -3.740  32.985  35.765  1.00 28.44           C  
ANISOU 3321  CB  LEU B  48     3548   3689   3568   -356    331   -866       C  
ATOM   3322  CG  LEU B  48      -2.271  32.862  35.338  1.00 36.54           C  
ANISOU 3322  CG  LEU B  48     4573   4741   4568   -365    277   -848       C  
ATOM   3323  CD1 LEU B  48      -1.571  31.742  36.101  1.00 34.12           C  
ANISOU 3323  CD1 LEU B  48     4281   4485   4197   -386    244   -830       C  
ATOM   3324  CD2 LEU B  48      -2.139  32.627  33.838  1.00 34.13           C  
ANISOU 3324  CD2 LEU B  48     4236   4423   4310   -328    245   -813       C  
ATOM   3325  C   LEU B  48      -6.058  33.797  35.255  1.00 28.79           C  
ANISOU 3325  C   LEU B  48     3560   3665   3714   -311    409   -882       C  
ATOM   3326  O   LEU B  48      -6.614  32.825  34.765  1.00 25.30           O  
ANISOU 3326  O   LEU B  48     3093   3232   3288   -288    393   -850       O  
ATOM   3327  N   SER B  49      -6.696  34.695  36.007  1.00 25.39           N  
ANISOU 3327  N   SER B  49     3145   3208   3293   -321    468   -920       N  
ATOM   3328  CA  SER B  49      -8.146  34.657  36.164  1.00 28.47           C  
ANISOU 3328  CA  SER B  49     3516   3574   3725   -301    516   -924       C  
ATOM   3329  CB  SER B  49      -8.583  35.454  37.408  1.00 30.15           C  
ANISOU 3329  CB  SER B  49     3763   3769   3923   -327    584   -973       C  
ATOM   3330  OG  SER B  49      -8.714  36.840  37.131  1.00 30.22           O  
ANISOU 3330  OG  SER B  49     3774   3732   3976   -317    620   -998       O  
ATOM   3331  C   SER B  49      -8.829  35.199  34.898  1.00 26.80           C  
ANISOU 3331  C   SER B  49     3264   3325   3593   -257    518   -906       C  
ATOM   3332  O   SER B  49     -10.042  35.049  34.716  1.00 31.11           O  
ANISOU 3332  O   SER B  49     3780   3855   4186   -232    545   -897       O  
ATOM   3333  N   LEU B  50      -8.044  35.838  34.034  1.00 23.51           N  
ANISOU 3333  N   LEU B  50     2844   2896   3192   -248    489   -899       N  
ATOM   3334  CA  LEU B  50      -8.543  36.309  32.749  1.00 23.78           C  
ANISOU 3334  CA  LEU B  50     2842   2897   3294   -207    481   -877       C  
ATOM   3335  CB  LEU B  50      -7.974  37.686  32.417  1.00 25.70           C  
ANISOU 3335  CB  LEU B  50     3100   3106   3558   -207    494   -897       C  
ATOM   3336  CG  LEU B  50      -8.421  38.839  33.329  1.00 25.64           C  
ANISOU 3336  CG  LEU B  50     3117   3064   3562   -219    564   -943       C  
ATOM   3337  CD1 LEU B  50      -7.855  40.145  32.810  1.00 31.98           C  
ANISOU 3337  CD1 LEU B  50     3932   3828   4389   -216    573   -957       C  
ATOM   3338  CD2 LEU B  50      -9.927  38.905  33.401  1.00 28.36           C  
ANISOU 3338  CD2 LEU B  50     3433   3383   3961   -189    611   -941       C  
ATOM   3339  C   LEU B  50      -8.186  35.327  31.631  1.00 21.49           C  
ANISOU 3339  C   LEU B  50     2529   2630   3005   -189    417   -831       C  
ATOM   3340  O   LEU B  50      -9.009  35.031  30.769  1.00 24.84           O  
ANISOU 3340  O   LEU B  50     2918   3043   3475   -158    407   -803       O  
ATOM   3341  N   ALA B  51      -6.960  34.827  31.654  1.00 20.25           N  
ANISOU 3341  N   ALA B  51     2391   2504   2797   -211    376   -823       N  
ATOM   3342  CA  ALA B  51      -6.503  33.900  30.604  1.00 18.25           C  
ANISOU 3342  CA  ALA B  51     2121   2269   2542   -195    319   -781       C  
ATOM   3343  CB  ALA B  51      -4.998  33.831  30.584  1.00 20.17           C  
ANISOU 3343  CB  ALA B  51     2386   2536   2741   -216    283   -779       C  
ATOM   3344  C   ALA B  51      -7.087  32.504  30.792  1.00 23.80           C  
ANISOU 3344  C   ALA B  51     2813   3000   3229   -193    307   -758       C  
ATOM   3345  O   ALA B  51      -7.150  31.707  29.843  1.00 22.60           O  
ANISOU 3345  O   ALA B  51     2644   2855   3090   -175    271   -724       O  
ATOM   3346  N   TYR B  52      -7.472  32.181  32.024  1.00 21.83           N  
ANISOU 3346  N   TYR B  52     2579   2765   2950   -214    338   -778       N  
ATOM   3347  CA  TYR B  52      -8.073  30.884  32.301  1.00 19.96           C  
ANISOU 3347  CA  TYR B  52     2334   2551   2697   -215    334   -759       C  
ATOM   3348  CB  TYR B  52      -7.050  29.923  32.935  1.00 22.58           C  
ANISOU 3348  CB  TYR B  52     2695   2924   2961   -240    305   -750       C  
ATOM   3349  CG  TYR B  52      -7.409  28.454  32.735  1.00 22.68           C  
ANISOU 3349  CG  TYR B  52     2698   2957   2963   -234    284   -717       C  
ATOM   3350  CD1 TYR B  52      -7.525  27.914  31.456  1.00 25.42           C  
ANISOU 3350  CD1 TYR B  52     3021   3297   3340   -209    250   -683       C  
ATOM   3351  CE1 TYR B  52      -7.864  26.578  31.265  1.00 23.81           C  
ANISOU 3351  CE1 TYR B  52     2812   3109   3126   -206    233   -655       C  
ATOM   3352  CZ  TYR B  52      -8.090  25.771  32.366  1.00 32.49           C  
ANISOU 3352  CZ  TYR B  52     3930   4230   4186   -226    252   -659       C  
ATOM   3353  OH  TYR B  52      -8.435  24.445  32.188  1.00 35.33           O  
ANISOU 3353  OH  TYR B  52     4286   4600   4535   -224    239   -632       O  
ATOM   3354  CE2 TYR B  52      -7.980  26.291  33.644  1.00 25.41           C  
ANISOU 3354  CE2 TYR B  52     3057   3341   3258   -249    285   -690       C  
ATOM   3355  CD2 TYR B  52      -7.636  27.616  33.820  1.00 25.56           C  
ANISOU 3355  CD2 TYR B  52     3082   3345   3285   -254    300   -720       C  
ATOM   3356  C   TYR B  52      -9.296  31.106  33.199  1.00 24.39           C  
ANISOU 3356  C   TYR B  52     2893   3100   3276   -219    392   -783       C  
ATOM   3357  O   TYR B  52      -9.859  32.191  33.208  1.00 26.60           O  
ANISOU 3357  O   TYR B  52     3163   3347   3595   -209    429   -805       O  
ATOM   3358  N   SER B  53      -9.711  30.074  33.920  1.00 26.77           N  
ANISOU 3358  N   SER B  53     3201   3424   3548   -233    401   -778       N  
ATOM   3359  CA  SER B  53     -10.909  30.147  34.766  1.00 26.27           C  
ANISOU 3359  CA  SER B  53     3133   3350   3500   -237    458   -798       C  
ATOM   3360  CB  SER B  53     -11.132  28.786  35.425  1.00 30.99           C  
ANISOU 3360  CB  SER B  53     3741   3978   4056   -254    456   -785       C  
ATOM   3361  OG  SER B  53     -12.377  28.741  36.099  1.00 44.86           O  
ANISOU 3361  OG  SER B  53     5487   5723   5834   -256    512   -799       O  
ATOM   3362  C   SER B  53     -10.818  31.251  35.830  1.00 27.25           C  
ANISOU 3362  C   SER B  53     3287   3460   3609   -258    509   -844       C  
ATOM   3363  O   SER B  53      -9.788  31.384  36.499  1.00 30.92           O  
ANISOU 3363  O   SER B  53     3791   3943   4016   -286    499   -860       O  
ATOM   3364  N   PRO B  54     -11.903  32.034  36.014  1.00 30.19           N  
ANISOU 3364  N   PRO B  54     3642   3797   4030   -245    565   -864       N  
ATOM   3365  CA  PRO B  54     -13.221  31.944  35.374  1.00 22.41           C  
ANISOU 3365  CA  PRO B  54     2607   2793   3116   -213    583   -847       C  
ATOM   3366  CB  PRO B  54     -14.166  32.352  36.508  1.00 28.05           C  
ANISOU 3366  CB  PRO B  54     3329   3490   3839   -223    659   -880       C  
ATOM   3367  CG  PRO B  54     -13.379  33.424  37.210  1.00 31.02           C  
ANISOU 3367  CG  PRO B  54     3751   3853   4182   -245    685   -920       C  
ATOM   3368  CD  PRO B  54     -11.918  33.003  37.128  1.00 35.23           C  
ANISOU 3368  CD  PRO B  54     4315   4419   4651   -267    623   -910       C  
ATOM   3369  C   PRO B  54     -13.440  32.877  34.185  1.00 26.81           C  
ANISOU 3369  C   PRO B  54     3130   3317   3739   -178    572   -836       C  
ATOM   3370  O   PRO B  54     -14.440  32.722  33.481  1.00 30.32           O  
ANISOU 3370  O   PRO B  54     3529   3750   4242   -150    572   -813       O  
ATOM   3371  N   GLY B  55     -12.546  33.840  33.981  1.00 25.85           N  
ANISOU 3371  N   GLY B  55     3031   3181   3611   -180    564   -851       N  
ATOM   3372  CA  GLY B  55     -12.714  34.836  32.935  1.00 30.74           C  
ANISOU 3372  CA  GLY B  55     3624   3765   4291   -147    560   -842       C  
ATOM   3373  C   GLY B  55     -12.773  34.275  31.521  1.00 27.80           C  
ANISOU 3373  C   GLY B  55     3215   3398   3948   -120    501   -797       C  
ATOM   3374  O   GLY B  55     -13.472  34.816  30.651  1.00 21.88           O  
ANISOU 3374  O   GLY B  55     2430   2622   3261    -87    502   -780       O  
ATOM   3375  N   VAL B  56     -12.038  33.191  31.293  1.00 24.53           N  
ANISOU 3375  N   VAL B  56     2812   3019   3487   -134    450   -776       N  
ATOM   3376  CA  VAL B  56     -11.946  32.602  29.958  1.00 21.43           C  
ANISOU 3376  CA  VAL B  56     2396   2634   3113   -114    394   -735       C  
ATOM   3377  CB  VAL B  56     -10.877  31.481  29.916  1.00 22.78           C  
ANISOU 3377  CB  VAL B  56     2592   2841   3223   -134    346   -719       C  
ATOM   3378  CG1 VAL B  56     -11.354  30.254  30.662  1.00 21.21           C  
ANISOU 3378  CG1 VAL B  56     2395   2670   2995   -151    354   -714       C  
ATOM   3379  CG2 VAL B  56     -10.503  31.129  28.464  1.00 22.63           C  
ANISOU 3379  CG2 VAL B  56     2559   2822   3219   -115    291   -682       C  
ATOM   3380  C   VAL B  56     -13.308  32.074  29.501  1.00 21.20           C  
ANISOU 3380  C   VAL B  56     2321   2602   3132    -94    396   -712       C  
ATOM   3381  O   VAL B  56     -13.528  31.901  28.314  1.00 21.79           O  
ANISOU 3381  O   VAL B  56     2370   2672   3238    -73    358   -681       O  
ATOM   3382  N   ALA B  57     -14.255  31.896  30.430  1.00 20.68           N  
ANISOU 3382  N   ALA B  57     2245   2536   3076   -101    443   -728       N  
ATOM   3383  CA  ALA B  57     -15.602  31.454  30.044  1.00 27.55           C  
ANISOU 3383  CA  ALA B  57     3066   3404   3997    -83    449   -707       C  
ATOM   3384  CB  ALA B  57     -16.454  31.180  31.281  1.00 28.01           C  
ANISOU 3384  CB  ALA B  57     3122   3467   4054    -99    508   -729       C  
ATOM   3385  C   ALA B  57     -16.315  32.467  29.139  1.00 24.88           C  
ANISOU 3385  C   ALA B  57     2686   3033   3733    -47    453   -695       C  
ATOM   3386  O   ALA B  57     -17.133  32.083  28.299  1.00 23.87           O  
ANISOU 3386  O   ALA B  57     2515   2907   3647    -29    428   -664       O  
ATOM   3387  N   ALA B  58     -15.990  33.745  29.299  1.00 23.39           N  
ANISOU 3387  N   ALA B  58     2513   2815   3560    -36    482   -717       N  
ATOM   3388  CA  ALA B  58     -16.680  34.812  28.571  1.00 25.68           C  
ANISOU 3388  CA  ALA B  58     2767   3069   3922      1    494   -706       C  
ATOM   3389  CB  ALA B  58     -16.262  36.190  29.094  1.00 27.97           C  
ANISOU 3389  CB  ALA B  58     3086   3324   4219      4    542   -740       C  
ATOM   3390  C   ALA B  58     -16.474  34.718  27.056  1.00 22.47           C  
ANISOU 3390  C   ALA B  58     2342   2663   3535     23    429   -666       C  
ATOM   3391  O   ALA B  58     -17.462  34.696  26.319  1.00 23.77           O  
ANISOU 3391  O   ALA B  58     2458   2822   3753     48    416   -637       O  
ATOM   3392  N   PRO B  59     -15.210  34.627  26.575  1.00 21.87           N  
ANISOU 3392  N   PRO B  59     2302   2595   3414     11    387   -662       N  
ATOM   3393  CA  PRO B  59     -15.112  34.459  25.116  1.00 21.32           C  
ANISOU 3393  CA  PRO B  59     2215   2525   3361     31    329   -623       C  
ATOM   3394  CB  PRO B  59     -13.599  34.543  24.839  1.00 17.17           C  
ANISOU 3394  CB  PRO B  59     1736   2004   2785     16    299   -627       C  
ATOM   3395  CG  PRO B  59     -12.924  34.260  26.177  1.00 18.54           C  
ANISOU 3395  CG  PRO B  59     1946   2196   2903    -19    328   -662       C  
ATOM   3396  CD  PRO B  59     -13.892  34.791  27.213  1.00 22.47           C  
ANISOU 3396  CD  PRO B  59     2430   2678   3430    -16    391   -689       C  
ATOM   3397  C   PRO B  59     -15.672  33.127  24.625  1.00 20.81           C  
ANISOU 3397  C   PRO B  59     2125   2490   3291     25    289   -593       C  
ATOM   3398  O   PRO B  59     -16.157  33.037  23.497  1.00 20.60           O  
ANISOU 3398  O   PRO B  59     2069   2460   3296     44    251   -560       O  
ATOM   3399  N   CYS B  60     -15.606  32.095  25.457  1.00 18.57           N  
ANISOU 3399  N   CYS B  60     1855   2234   2966     -4    297   -604       N  
ATOM   3400  CA  CYS B  60     -16.159  30.804  25.066  1.00 19.72           C  
ANISOU 3400  CA  CYS B  60     1980   2405   3106    -13    265   -579       C  
ATOM   3401  CB  CYS B  60     -15.900  29.763  26.140  1.00 19.73           C  
ANISOU 3401  CB  CYS B  60     2008   2434   3055    -45    281   -595       C  
ATOM   3402  SG  CYS B  60     -14.127  29.335  26.258  1.00 22.79           S  
ANISOU 3402  SG  CYS B  60     2456   2839   3365    -66    252   -601       S  
ATOM   3403  C   CYS B  60     -17.661  30.929  24.792  1.00 24.00           C  
ANISOU 3403  C   CYS B  60     2464   2940   3715      6    276   -564       C  
ATOM   3404  O   CYS B  60     -18.165  30.486  23.755  1.00 21.93           O  
ANISOU 3404  O   CYS B  60     2173   2684   3474     15    233   -532       O  
ATOM   3405  N   LYS B  61     -18.367  31.557  25.719  1.00 24.78           N  
ANISOU 3405  N   LYS B  61     2546   3025   3846     13    335   -586       N  
ATOM   3406  CA  LYS B  61     -19.802  31.745  25.557  1.00 25.32           C  
ANISOU 3406  CA  LYS B  61     2553   3085   3982     33    353   -572       C  
ATOM   3407  CB  LYS B  61     -20.404  32.387  26.792  1.00 23.18           C  
ANISOU 3407  CB  LYS B  61     2274   2798   3737     37    430   -604       C  
ATOM   3408  CG  LYS B  61     -20.374  31.547  28.040  1.00 29.92           C  
ANISOU 3408  CG  LYS B  61     3151   3671   4544      2    465   -629       C  
ATOM   3409  CD  LYS B  61     -20.958  32.371  29.186  1.00 41.10           C  
ANISOU 3409  CD  LYS B  61     4564   5065   5989      8    546   -662       C  
ATOM   3410  CE  LYS B  61     -20.556  31.831  30.538  1.00 49.17           C  
ANISOU 3410  CE  LYS B  61     5632   6102   6948    -29    585   -695       C  
ATOM   3411  NZ  LYS B  61     -20.958  32.751  31.639  1.00 50.54           N  
ANISOU 3411  NZ  LYS B  61     5814   6249   7141    -26    665   -732       N  
ATOM   3412  C   LYS B  61     -20.108  32.598  24.336  1.00 27.63           C  
ANISOU 3412  C   LYS B  61     2813   3356   4328     69    323   -543       C  
ATOM   3413  O   LYS B  61     -21.080  32.342  23.631  1.00 27.33           O  
ANISOU 3413  O   LYS B  61     2725   3324   4334     82    298   -513       O  
ATOM   3414  N   ALA B  62     -19.279  33.603  24.071  1.00 23.53           N  
ANISOU 3414  N   ALA B  62     2324   2813   3804     84    323   -551       N  
ATOM   3415  CA  ALA B  62     -19.523  34.465  22.919  1.00 23.51           C  
ANISOU 3415  CA  ALA B  62     2297   2787   3850    119    297   -522       C  
ATOM   3416  CB  ALA B  62     -18.590  35.671  22.936  1.00 23.74           C  
ANISOU 3416  CB  ALA B  62     2365   2783   3873    131    316   -540       C  
ATOM   3417  C   ALA B  62     -19.386  33.708  21.599  1.00 24.47           C  
ANISOU 3417  C   ALA B  62     2413   2927   3957    116    221   -484       C  
ATOM   3418  O   ALA B  62     -20.187  33.912  20.677  1.00 22.72           O  
ANISOU 3418  O   ALA B  62     2148   2702   3783    140    192   -450       O  
ATOM   3419  N   ILE B  63     -18.384  32.834  21.514  1.00 23.32           N  
ANISOU 3419  N   ILE B  63     2311   2803   3746     88    191   -488       N  
ATOM   3420  CA  ILE B  63     -18.145  32.040  20.311  1.00 18.40           C  
ANISOU 3420  CA  ILE B  63     1693   2196   3101     80    124   -456       C  
ATOM   3421  CB  ILE B  63     -16.756  31.336  20.357  1.00 16.77           C  
ANISOU 3421  CB  ILE B  63     1545   2004   2821     53    105   -466       C  
ATOM   3422  CG1 ILE B  63     -15.626  32.385  20.393  1.00 16.65           C  
ANISOU 3422  CG1 ILE B  63     1568   1966   2792     63    118   -483       C  
ATOM   3423  CD1 ILE B  63     -14.250  31.805  20.754  1.00 18.12           C  
ANISOU 3423  CD1 ILE B  63     1806   2167   2911     36    111   -499       C  
ATOM   3424  CG2 ILE B  63     -16.567  30.401  19.146  1.00 17.64           C  
ANISOU 3424  CG2 ILE B  63     1664   2131   2908     44     42   -435       C  
ATOM   3425  C   ILE B  63     -19.260  31.001  20.133  1.00 20.76           C  
ANISOU 3425  C   ILE B  63     1950   2521   3417     69    104   -436       C  
ATOM   3426  O   ILE B  63     -19.692  30.730  19.019  1.00 22.22           O  
ANISOU 3426  O   ILE B  63     2113   2712   3617     74     55   -403       O  
ATOM   3427  N   ALA B  64     -19.715  30.415  21.231  1.00 19.57           N  
ANISOU 3427  N   ALA B  64     1790   2385   3261     50    143   -457       N  
ATOM   3428  CA  ALA B  64     -20.828  29.461  21.152  1.00 22.43           C  
ANISOU 3428  CA  ALA B  64     2109   2769   3643     36    130   -441       C  
ATOM   3429  CB  ALA B  64     -21.132  28.875  22.515  1.00 19.54           C  
ANISOU 3429  CB  ALA B  64     1745   2416   3264     14    182   -468       C  
ATOM   3430  C   ALA B  64     -22.086  30.117  20.562  1.00 26.67           C  
ANISOU 3430  C   ALA B  64     2580   3298   4258     65    123   -415       C  
ATOM   3431  O   ALA B  64     -22.794  29.494  19.768  1.00 28.55           O  
ANISOU 3431  O   ALA B  64     2783   3553   4511     59     79   -386       O  
ATOM   3432  N   LYS B  65     -22.357  31.364  20.948  1.00 22.84           N  
ANISOU 3432  N   LYS B  65     2076   2785   3818     97    166   -425       N  
ATOM   3433  CA  LYS B  65     -23.486  32.108  20.384  1.00 35.52           C  
ANISOU 3433  CA  LYS B  65     3616   4379   5501    131    162   -397       C  
ATOM   3434  CB  LYS B  65     -23.774  33.371  21.192  1.00 35.01           C  
ANISOU 3434  CB  LYS B  65     3537   4280   5483    162    231   -418       C  
ATOM   3435  CG  LYS B  65     -24.488  33.159  22.503  1.00 49.67           C  
ANISOU 3435  CG  LYS B  65     5373   6141   7359    152    298   -445       C  
ATOM   3436  CD  LYS B  65     -24.828  34.519  23.108  1.00 58.59           C  
ANISOU 3436  CD  LYS B  65     6487   7232   8542    187    365   -461       C  
ATOM   3437  CE  LYS B  65     -25.406  34.400  24.509  1.00 66.93           C  
ANISOU 3437  CE  LYS B  65     7533   8286   9610    175    443   -494       C  
ATOM   3438  NZ  LYS B  65     -25.787  35.734  25.059  1.00 71.92           N  
ANISOU 3438  NZ  LYS B  65     8152   8876  10297    211    513   -510       N  
ATOM   3439  C   LYS B  65     -23.243  32.503  18.935  1.00 41.02           C  
ANISOU 3439  C   LYS B  65     4314   5068   6204    151     99   -361       C  
ATOM   3440  O   LYS B  65     -24.147  32.427  18.107  1.00 38.21           O  
ANISOU 3440  O   LYS B  65     3907   4722   5889    162     59   -325       O  
ATOM   3441  N   ASP B  66     -22.021  32.946  18.637  1.00 30.21           N  
ANISOU 3441  N   ASP B  66     3002   3682   4794    153     89   -369       N  
ATOM   3442  CA  ASP B  66     -21.672  33.406  17.298  1.00 25.36           C  
ANISOU 3442  CA  ASP B  66     2397   3057   4180    172     35   -337       C  
ATOM   3443  CB  ASP B  66     -21.657  34.934  17.241  1.00 36.07           C  
ANISOU 3443  CB  ASP B  66     3748   4374   5583    213     65   -335       C  
ATOM   3444  CG  ASP B  66     -21.252  35.481  15.870  1.00 51.99           C  
ANISOU 3444  CG  ASP B  66     5779   6375   7598    233     13   -301       C  
ATOM   3445  OD1 ASP B  66     -21.043  34.688  14.915  1.00 49.20           O  
ANISOU 3445  OD1 ASP B  66     5440   6043   7211    215    -48   -278       O  
ATOM   3446  OD2 ASP B  66     -21.167  36.726  15.745  1.00 51.37           O  
ANISOU 3446  OD2 ASP B  66     5702   6261   7554    268     36   -298       O  
ATOM   3447  C   ASP B  66     -20.311  32.861  16.903  1.00 22.28           C  
ANISOU 3447  C   ASP B  66     2075   2674   3717    147      4   -345       C  
ATOM   3448  O   ASP B  66     -19.294  33.441  17.302  1.00 22.88           O  
ANISOU 3448  O   ASP B  66     2194   2731   3767    148     31   -369       O  
ATOM   3449  N   PRO B  67     -20.290  31.767  16.119  1.00 21.45           N  
ANISOU 3449  N   PRO B  67     1977   2594   3579    122    -50   -324       N  
ATOM   3450  CA  PRO B  67     -19.038  31.090  15.749  1.00 21.55           C  
ANISOU 3450  CA  PRO B  67     2051   2613   3522     98    -76   -330       C  
ATOM   3451  CB  PRO B  67     -19.492  30.056  14.717  1.00 26.09           C  
ANISOU 3451  CB  PRO B  67     2617   3211   4083     78   -137   -300       C  
ATOM   3452  CG  PRO B  67     -20.906  29.718  15.142  1.00 27.86           C  
ANISOU 3452  CG  PRO B  67     2779   3454   4355     75   -128   -294       C  
ATOM   3453  CD  PRO B  67     -21.478  31.031  15.629  1.00 28.41           C  
ANISOU 3453  CD  PRO B  67     2808   3500   4487    113    -86   -297       C  
ATOM   3454  C   PRO B  67     -17.950  31.997  15.153  1.00 22.10           C  
ANISOU 3454  C   PRO B  67     2164   2657   3576    115    -84   -328       C  
ATOM   3455  O   PRO B  67     -16.772  31.718  15.407  1.00 21.97           O  
ANISOU 3455  O   PRO B  67     2197   2642   3509     99    -76   -347       O  
ATOM   3456  N   ALA B  68     -18.320  33.036  14.401  1.00 24.80           N  
ANISOU 3456  N   ALA B  68     2485   2976   3960    148    -97   -304       N  
ATOM   3457  CA  ALA B  68     -17.338  33.917  13.764  1.00 20.54           C  
ANISOU 3457  CA  ALA B  68     1987   2410   3408    164   -103   -300       C  
ATOM   3458  CB  ALA B  68     -18.035  34.944  12.875  1.00 24.66           C  
ANISOU 3458  CB  ALA B  68     2477   2909   3983    201   -123   -265       C  
ATOM   3459  C   ALA B  68     -16.459  34.638  14.771  1.00 28.41           C  
ANISOU 3459  C   ALA B  68     3014   3387   4395    165    -48   -338       C  
ATOM   3460  O   ALA B  68     -15.364  35.090  14.426  1.00 25.70           O  
ANISOU 3460  O   ALA B  68     2714   3027   4025    166    -50   -343       O  
ATOM   3461  N   LYS B  69     -16.928  34.762  16.008  1.00 20.84           N  
ANISOU 3461  N   LYS B  69     2033   2430   3457    164      3   -365       N  
ATOM   3462  CA  LYS B  69     -16.136  35.460  17.010  1.00 23.47           C  
ANISOU 3462  CA  LYS B  69     2395   2744   3777    161     55   -404       C  
ATOM   3463  CB  LYS B  69     -16.990  35.776  18.227  1.00 26.47           C  
ANISOU 3463  CB  LYS B  69     2743   3120   4194    167    112   -428       C  
ATOM   3464  CG  LYS B  69     -18.018  36.861  17.943  1.00 28.86           C  
ANISOU 3464  CG  LYS B  69     3001   3393   4570    207    130   -409       C  
ATOM   3465  CD  LYS B  69     -18.758  37.225  19.191  1.00 29.35           C  
ANISOU 3465  CD  LYS B  69     3038   3447   4668    213    196   -437       C  
ATOM   3466  CE  LYS B  69     -19.918  38.177  18.861  1.00 34.52           C  
ANISOU 3466  CE  LYS B  69     3639   4075   5403    257    212   -413       C  
ATOM   3467  NZ  LYS B  69     -20.485  38.797  20.083  1.00 36.83           N  
ANISOU 3467  NZ  LYS B  69     3914   4346   5732    267    289   -443       N  
ATOM   3468  C   LYS B  69     -14.885  34.677  17.432  1.00 20.01           C  
ANISOU 3468  C   LYS B  69     2007   2326   3270    126     52   -426       C  
ATOM   3469  O   LYS B  69     -14.053  35.195  18.189  1.00 21.44           O  
ANISOU 3469  O   LYS B  69     2218   2496   3432    118     87   -457       O  
ATOM   3470  N   VAL B  70     -14.739  33.442  16.947  1.00 18.94           N  
ANISOU 3470  N   VAL B  70     1880   2218   3099    106     11   -411       N  
ATOM   3471  CA  VAL B  70     -13.499  32.716  17.204  1.00 16.02           C  
ANISOU 3471  CA  VAL B  70     1557   1864   2667     78      5   -426       C  
ATOM   3472  CB  VAL B  70     -13.528  31.287  16.592  1.00 18.58           C  
ANISOU 3472  CB  VAL B  70     1887   2215   2957     58    -39   -405       C  
ATOM   3473  CG1 VAL B  70     -13.536  31.339  15.062  1.00 18.36           C  
ANISOU 3473  CG1 VAL B  70     1864   2178   2933     70    -88   -370       C  
ATOM   3474  CG2 VAL B  70     -12.328  30.440  17.095  1.00 18.91           C  
ANISOU 3474  CG2 VAL B  70     1972   2275   2939     32    -36   -421       C  
ATOM   3475  C   VAL B  70     -12.325  33.524  16.649  1.00 18.79           C  
ANISOU 3475  C   VAL B  70     1944   2193   3003     86      0   -427       C  
ATOM   3476  O   VAL B  70     -11.228  33.461  17.190  1.00 18.75           O  
ANISOU 3476  O   VAL B  70     1972   2192   2960     69     14   -448       O  
ATOM   3477  N   TYR B  71     -12.553  34.302  15.590  1.00 17.30           N  
ANISOU 3477  N   TYR B  71     1749   1980   2844    110    -20   -402       N  
ATOM   3478  CA  TYR B  71     -11.486  35.130  15.023  1.00 19.75           C  
ANISOU 3478  CA  TYR B  71     2094   2266   3144    118    -22   -402       C  
ATOM   3479  CB  TYR B  71     -11.858  35.605  13.619  1.00 18.24           C  
ANISOU 3479  CB  TYR B  71     1897   2054   2977    142    -58   -364       C  
ATOM   3480  CG  TYR B  71     -11.777  34.559  12.539  1.00 21.48           C  
ANISOU 3480  CG  TYR B  71     2321   2484   3357    130   -111   -335       C  
ATOM   3481  CD1 TYR B  71     -10.581  34.313  11.882  1.00 23.76           C  
ANISOU 3481  CD1 TYR B  71     2655   2769   3603    118   -128   -331       C  
ATOM   3482  CE1 TYR B  71     -10.487  33.360  10.885  1.00 27.55           C  
ANISOU 3482  CE1 TYR B  71     3153   3263   4053    106   -171   -306       C  
ATOM   3483  CZ  TYR B  71     -11.609  32.630  10.531  1.00 23.72           C  
ANISOU 3483  CZ  TYR B  71     2640   2796   3577    103   -202   -286       C  
ATOM   3484  OH  TYR B  71     -11.505  31.704   9.528  1.00 24.47           O  
ANISOU 3484  OH  TYR B  71     2758   2902   3639     88   -243   -264       O  
ATOM   3485  CE2 TYR B  71     -12.815  32.853  11.168  1.00 21.45           C  
ANISOU 3485  CE2 TYR B  71     2303   2514   3334    114   -189   -289       C  
ATOM   3486  CD2 TYR B  71     -12.897  33.821  12.166  1.00 23.47           C  
ANISOU 3486  CD2 TYR B  71     2541   2755   3622    129   -141   -312       C  
ATOM   3487  C   TYR B  71     -11.151  36.355  15.881  1.00 27.39           C  
ANISOU 3487  C   TYR B  71     3068   3208   4131    125     29   -432       C  
ATOM   3488  O   TYR B  71     -10.093  36.969  15.711  1.00 22.32           O  
ANISOU 3488  O   TYR B  71     2459   2549   3473    121     36   -442       O  
ATOM   3489  N   ASP B  72     -12.064  36.726  16.772  1.00 23.55           N  
ANISOU 3489  N   ASP B  72     2552   2717   3680    133     66   -448       N  
ATOM   3490  CA  ASP B  72     -11.864  37.893  17.626  1.00 21.49           C  
ANISOU 3490  CA  ASP B  72     2299   2428   3438    138    120   -480       C  
ATOM   3491  CB  ASP B  72     -13.206  38.520  17.987  1.00 24.93           C  
ANISOU 3491  CB  ASP B  72     2692   2845   3934    165    152   -478       C  
ATOM   3492  CG  ASP B  72     -13.950  39.048  16.772  1.00 36.75           C  
ANISOU 3492  CG  ASP B  72     4163   4321   5479    202    124   -437       C  
ATOM   3493  OD1 ASP B  72     -13.297  39.601  15.855  1.00 37.62           O  
ANISOU 3493  OD1 ASP B  72     4298   4411   5585    212    104   -420       O  
ATOM   3494  OD2 ASP B  72     -15.188  38.889  16.728  1.00 36.13           O  
ANISOU 3494  OD2 ASP B  72     4038   4248   5443    220    122   -418       O  
ATOM   3495  C   ASP B  72     -11.112  37.579  18.916  1.00 21.20           C  
ANISOU 3495  C   ASP B  72     2287   2409   3358    106    150   -520       C  
ATOM   3496  O   ASP B  72     -10.416  38.431  19.450  1.00 21.69           O  
ANISOU 3496  O   ASP B  72     2374   2453   3415     98    183   -548       O  
ATOM   3497  N   TYR B  73     -11.257  36.358  19.413  1.00 19.97           N  
ANISOU 3497  N   TYR B  73     2126   2290   3173     85    139   -523       N  
ATOM   3498  CA  TYR B  73     -10.836  36.042  20.783  1.00 18.46           C  
ANISOU 3498  CA  TYR B  73     1952   2118   2946     56    172   -559       C  
ATOM   3499  CB  TYR B  73     -12.033  35.563  21.592  1.00 15.80           C  
ANISOU 3499  CB  TYR B  73     1583   1794   2627     55    197   -566       C  
ATOM   3500  CG  TYR B  73     -13.117  36.606  21.737  1.00 16.36           C  
ANISOU 3500  CG  TYR B  73     1623   1833   2761     83    235   -570       C  
ATOM   3501  CD1 TYR B  73     -12.813  37.890  22.157  1.00 18.79           C  
ANISOU 3501  CD1 TYR B  73     1947   2106   3085     90    278   -595       C  
ATOM   3502  CE1 TYR B  73     -13.803  38.860  22.289  1.00 23.02           C  
ANISOU 3502  CE1 TYR B  73     2457   2609   3682    119    319   -597       C  
ATOM   3503  CZ  TYR B  73     -15.109  38.533  21.966  1.00 24.79           C  
ANISOU 3503  CZ  TYR B  73     2630   2838   3953    142    312   -571       C  
ATOM   3504  OH  TYR B  73     -16.106  39.482  22.092  1.00 28.64           O  
ANISOU 3504  OH  TYR B  73     3085   3291   4504    174    354   -570       O  
ATOM   3505  CE2 TYR B  73     -15.429  37.259  21.532  1.00 23.03           C  
ANISOU 3505  CE2 TYR B  73     2388   2651   3713    132    266   -546       C  
ATOM   3506  CD2 TYR B  73     -14.429  36.307  21.401  1.00 20.50           C  
ANISOU 3506  CD2 TYR B  73     2100   2360   3329    103    229   -546       C  
ATOM   3507  C   TYR B  73      -9.751  34.979  20.861  1.00 15.68           C  
ANISOU 3507  C   TYR B  73     1627   1798   2532     28    143   -559       C  
ATOM   3508  O   TYR B  73      -9.314  34.632  21.955  1.00 18.04           O  
ANISOU 3508  O   TYR B  73     1942   2116   2796      3    162   -585       O  
ATOM   3509  N   THR B  74      -9.357  34.443  19.712  1.00 13.79           N  
ANISOU 3509  N   THR B  74     1395   1564   2281     33     97   -529       N  
ATOM   3510  CA  THR B  74      -8.315  33.413  19.659  1.00 11.78           C  
ANISOU 3510  CA  THR B  74     1166   1337   1974     11     71   -524       C  
ATOM   3511  CB  THR B  74      -8.873  32.015  19.322  1.00 15.93           C  
ANISOU 3511  CB  THR B  74     1680   1887   2485      6     42   -501       C  
ATOM   3512  OG1 THR B  74      -9.153  31.919  17.909  1.00 15.69           O  
ANISOU 3512  OG1 THR B  74     1645   1845   2472     22      4   -468       O  
ATOM   3513  CG2 THR B  74     -10.150  31.717  20.134  1.00 16.24           C  
ANISOU 3513  CG2 THR B  74     1689   1936   2547      5     65   -509       C  
ATOM   3514  C   THR B  74      -7.291  33.774  18.592  1.00 15.38           C  
ANISOU 3514  C   THR B  74     1645   1778   2420     16     46   -509       C  
ATOM   3515  O   THR B  74      -7.481  34.729  17.837  1.00 16.73           O  
ANISOU 3515  O   THR B  74     1813   1920   2625     36     46   -500       O  
ATOM   3516  N   ALA B  75      -6.230  32.975  18.496  1.00 13.97           N  
ANISOU 3516  N   ALA B  75     1490   1621   2199      0     27   -504       N  
ATOM   3517  CA  ALA B  75      -5.223  33.187  17.454  1.00 16.26           C  
ANISOU 3517  CA  ALA B  75     1802   1899   2479      3      5   -489       C  
ATOM   3518  CB  ALA B  75      -3.908  32.526  17.872  1.00 19.31           C  
ANISOU 3518  CB  ALA B  75     2210   2309   2819    -18      0   -495       C  
ATOM   3519  C   ALA B  75      -5.618  32.695  16.051  1.00 13.11           C  
ANISOU 3519  C   ALA B  75     1402   1491   2086     18    -31   -453       C  
ATOM   3520  O   ALA B  75      -4.817  32.825  15.115  1.00 15.26           O  
ANISOU 3520  O   ALA B  75     1697   1752   2349     21    -47   -438       O  
ATOM   3521  N   LYS B  76      -6.841  32.173  15.881  1.00 14.11           N  
ANISOU 3521  N   LYS B  76     1506   1624   2230     25    -43   -439       N  
ATOM   3522  CA  LYS B  76      -7.207  31.492  14.631  1.00 15.82           C  
ANISOU 3522  CA  LYS B  76     1727   1841   2445     31    -82   -407       C  
ATOM   3523  CB  LYS B  76      -8.683  31.082  14.663  1.00 16.74           C  
ANISOU 3523  CB  LYS B  76     1809   1966   2587     36    -91   -396       C  
ATOM   3524  CG  LYS B  76      -9.150  30.379  13.390  1.00 19.06           C  
ANISOU 3524  CG  LYS B  76     2105   2260   2875     37   -134   -364       C  
ATOM   3525  CD  LYS B  76     -10.650  30.162  13.408  1.00 24.68           C  
ANISOU 3525  CD  LYS B  76     2777   2980   3621     41   -143   -353       C  
ATOM   3526  CE  LYS B  76     -11.142  29.498  12.115  1.00 24.49           C  
ANISOU 3526  CE  LYS B  76     2756   2959   3589     37   -190   -321       C  
ATOM   3527  NZ  LYS B  76     -11.132  28.019  12.191  1.00 20.71           N  
ANISOU 3527  NZ  LYS B  76     2291   2503   3074     11   -203   -320       N  
ATOM   3528  C   LYS B  76      -6.927  32.337  13.379  1.00 16.91           C  
ANISOU 3528  C   LYS B  76     1878   1949   2596     48    -98   -387       C  
ATOM   3529  O   LYS B  76      -6.430  31.825  12.372  1.00 14.48           O  
ANISOU 3529  O   LYS B  76     1596   1641   2267     45   -124   -366       O  
ATOM   3530  N   GLY B  77      -7.201  33.633  13.464  1.00 18.07           N  
ANISOU 3530  N   GLY B  77     2014   2072   2781     65    -79   -394       N  
ATOM   3531  CA  GLY B  77      -7.066  34.504  12.314  1.00 16.05           C  
ANISOU 3531  CA  GLY B  77     1770   1785   2542     84    -92   -374       C  
ATOM   3532  C   GLY B  77      -5.644  34.821  11.885  1.00 17.65           C  
ANISOU 3532  C   GLY B  77     2010   1975   2719     77    -88   -376       C  
ATOM   3533  O   GLY B  77      -5.436  35.527  10.889  1.00 19.44           O  
ANISOU 3533  O   GLY B  77     2254   2176   2958     90    -97   -359       O  
ATOM   3534  N   ASN B  78      -4.667  34.326  12.636  1.00 12.36           N  
ANISOU 3534  N   ASN B  78     1353   1325   2018     56    -74   -397       N  
ATOM   3535  CA  ASN B  78      -3.272  34.494  12.267  1.00 11.83           C  
ANISOU 3535  CA  ASN B  78     1316   1252   1928     47    -71   -399       C  
ATOM   3536  CB  ASN B  78      -2.590  35.521  13.180  1.00 13.82           C  
ANISOU 3536  CB  ASN B  78     1568   1494   2188     38    -36   -430       C  
ATOM   3537  CG  ASN B  78      -1.283  36.060  12.579  1.00 16.13           C  
ANISOU 3537  CG  ASN B  78     1888   1770   2471     33    -31   -429       C  
ATOM   3538  OD1 ASN B  78      -1.262  36.463  11.413  1.00 17.95           O  
ANISOU 3538  OD1 ASN B  78     2134   1975   2711     47    -43   -406       O  
ATOM   3539  ND2 ASN B  78      -0.189  35.998  13.342  1.00 14.14           N  
ANISOU 3539  ND2 ASN B  78     1641   1534   2197     11    -17   -451       N  
ATOM   3540  C   ASN B  78      -2.542  33.165  12.340  1.00 15.49           C  
ANISOU 3540  C   ASN B  78     1792   1743   2349     29    -84   -395       C  
ATOM   3541  O   ASN B  78      -1.326  33.139  12.409  1.00 15.48           O  
ANISOU 3541  O   ASN B  78     1809   1746   2328     18    -76   -401       O  
ATOM   3542  N   LEU B  79      -3.279  32.060  12.327  1.00 11.99           N  
ANISOU 3542  N   LEU B  79     1341   1319   1895     27   -102   -384       N  
ATOM   3543  CA  LEU B  79      -2.670  30.764  12.602  1.00 13.30           C  
ANISOU 3543  CA  LEU B  79     1519   1511   2024     11   -108   -382       C  
ATOM   3544  CB  LEU B  79      -3.294  30.145  13.867  1.00 14.06           C  
ANISOU 3544  CB  LEU B  79     1593   1634   2116      1    -98   -398       C  
ATOM   3545  CG  LEU B  79      -2.678  28.823  14.346  1.00 13.76           C  
ANISOU 3545  CG  LEU B  79     1565   1622   2039    -14   -100   -397       C  
ATOM   3546  CD1 LEU B  79      -1.220  29.038  14.771  1.00 20.08           C  
ANISOU 3546  CD1 LEU B  79     2378   2430   2820    -22    -87   -407       C  
ATOM   3547  CD2 LEU B  79      -3.471  28.264  15.513  1.00 13.69           C  
ANISOU 3547  CD2 LEU B  79     1537   1636   2028    -24    -89   -410       C  
ATOM   3548  C   LEU B  79      -2.831  29.822  11.424  1.00 12.71           C  
ANISOU 3548  C   LEU B  79     1464   1434   1932     12   -137   -354       C  
ATOM   3549  O   LEU B  79      -3.962  29.445  11.064  1.00 13.87           O  
ANISOU 3549  O   LEU B  79     1600   1582   2088     15   -156   -341       O  
ATOM   3550  N   VAL B  80      -1.706  29.407  10.832  1.00 13.37           N  
ANISOU 3550  N   VAL B  80     1577   1514   1990      8   -139   -344       N  
ATOM   3551  CA  VAL B  80      -1.722  28.467   9.720  1.00 13.59           C  
ANISOU 3551  CA  VAL B  80     1631   1537   1996      6   -160   -320       C  
ATOM   3552  CB  VAL B  80      -0.975  29.060   8.486  1.00 15.49           C  
ANISOU 3552  CB  VAL B  80     1902   1751   2234     13   -163   -305       C  
ATOM   3553  CG1 VAL B  80      -0.681  28.005   7.404  1.00 14.11           C  
ANISOU 3553  CG1 VAL B  80     1764   1570   2028      7   -177   -284       C  
ATOM   3554  CG2 VAL B  80      -1.793  30.219   7.895  1.00 15.78           C  
ANISOU 3554  CG2 VAL B  80     1930   1764   2300     27   -174   -298       C  
ATOM   3555  C   VAL B  80      -1.090  27.152  10.178  1.00 10.56           C  
ANISOU 3555  C   VAL B  80     1258   1174   1580     -6   -154   -320       C  
ATOM   3556  O   VAL B  80      -0.110  27.153  10.936  1.00 12.02           O  
ANISOU 3556  O   VAL B  80     1440   1371   1756    -10   -136   -332       O  
ATOM   3557  N   ALA B  81      -1.644  26.038   9.739  1.00 10.88           N  
ANISOU 3557  N   ALA B  81     1311   1219   1603    -13   -170   -306       N  
ATOM   3558  CA  ALA B  81      -1.007  24.742   9.976  1.00 12.47           C  
ANISOU 3558  CA  ALA B  81     1530   1433   1774    -22   -163   -302       C  
ATOM   3559  CB  ALA B  81      -2.052  23.641  10.185  1.00 10.61           C  
ANISOU 3559  CB  ALA B  81     1292   1210   1529    -33   -174   -298       C  
ATOM   3560  C   ALA B  81      -0.136  24.411   8.786  1.00 11.84           C  
ANISOU 3560  C   ALA B  81     1490   1333   1675    -20   -163   -284       C  
ATOM   3561  O   ALA B  81      -0.597  24.454   7.647  1.00 12.93           O  
ANISOU 3561  O   ALA B  81     1649   1453   1810    -21   -181   -271       O  
ATOM   3562  N   VAL B  82       1.131  24.087   9.025  1.00 10.79           N  
ANISOU 3562  N   VAL B  82     1367   1204   1528    -18   -144   -284       N  
ATOM   3563  CA  VAL B  82       1.943  23.487   7.971  1.00 11.03           C  
ANISOU 3563  CA  VAL B  82     1437   1217   1539    -16   -138   -267       C  
ATOM   3564  CB  VAL B  82       3.387  24.033   7.984  1.00 12.79           C  
ANISOU 3564  CB  VAL B  82     1660   1435   1765     -8   -116   -267       C  
ATOM   3565  CG1 VAL B  82       4.285  23.206   7.085  1.00 14.25           C  
ANISOU 3565  CG1 VAL B  82     1882   1602   1929     -5   -102   -250       C  
ATOM   3566  CG2 VAL B  82       3.369  25.476   7.505  1.00 13.14           C  
ANISOU 3566  CG2 VAL B  82     1700   1462   1831     -4   -119   -272       C  
ATOM   3567  C   VAL B  82       1.915  21.990   8.201  1.00 13.06           C  
ANISOU 3567  C   VAL B  82     1709   1483   1772    -23   -133   -259       C  
ATOM   3568  O   VAL B  82       2.445  21.515   9.218  1.00 14.20           O  
ANISOU 3568  O   VAL B  82     1838   1647   1911    -21   -119   -263       O  
ATOM   3569  N   ILE B  83       1.266  21.257   7.287  1.00  8.37           N  
ANISOU 3569  N   ILE B  83     1145    874   1160    -32   -146   -248       N  
ATOM   3570  CA  ILE B  83       0.953  19.856   7.535  1.00 11.03           C  
ANISOU 3570  CA  ILE B  83     1497   1218   1477    -42   -143   -243       C  
ATOM   3571  CB  ILE B  83      -0.586  19.604   7.556  1.00 12.72           C  
ANISOU 3571  CB  ILE B  83     1701   1438   1694    -58   -168   -247       C  
ATOM   3572  CG1 ILE B  83      -1.289  20.572   8.524  1.00 14.88           C  
ANISOU 3572  CG1 ILE B  83     1925   1732   1997    -54   -176   -262       C  
ATOM   3573  CD1 ILE B  83      -2.782  20.182   8.793  1.00 14.32           C  
ANISOU 3573  CD1 ILE B  83     1835   1672   1933    -69   -195   -266       C  
ATOM   3574  CG2 ILE B  83      -0.869  18.165   7.931  1.00 14.93           C  
ANISOU 3574  CG2 ILE B  83     1995   1724   1953    -71   -161   -244       C  
ATOM   3575  C   ILE B  83       1.599  18.970   6.491  1.00 11.88           C  
ANISOU 3575  C   ILE B  83     1654   1300   1558    -44   -131   -228       C  
ATOM   3576  O   ILE B  83       1.471  19.196   5.295  1.00 12.73           O  
ANISOU 3576  O   ILE B  83     1793   1387   1658    -49   -140   -221       O  
ATOM   3577  N   SER B  84       2.278  17.942   6.960  1.00 11.35           N  
ANISOU 3577  N   SER B  84     1597   1237   1477    -40   -108   -222       N  
ATOM   3578  CA  SER B  84       2.978  17.017   6.068  1.00 12.26           C  
ANISOU 3578  CA  SER B  84     1761   1327   1571    -39    -87   -208       C  
ATOM   3579  CB  SER B  84       4.450  17.411   5.937  1.00 11.58           C  
ANISOU 3579  CB  SER B  84     1675   1234   1492    -20    -61   -201       C  
ATOM   3580  OG  SER B  84       5.104  16.583   4.975  1.00 14.01           O  
ANISOU 3580  OG  SER B  84     2031   1512   1780    -18    -36   -187       O  
ATOM   3581  C   SER B  84       2.924  15.599   6.588  1.00 13.84           C  
ANISOU 3581  C   SER B  84     1975   1529   1753    -43    -72   -203       C  
ATOM   3582  O   SER B  84       2.902  15.398   7.802  1.00 14.37           O  
ANISOU 3582  O   SER B  84     2011   1622   1828    -39    -69   -206       O  
ATOM   3583  N   ASN B  85       2.978  14.619   5.687  1.00 12.94           N  
ANISOU 3583  N   ASN B  85     1912   1388   1615    -52    -59   -193       N  
ATOM   3584  CA  ASN B  85       3.254  13.260   6.140  1.00 10.83           C  
ANISOU 3584  CA  ASN B  85     1664   1117   1334    -50    -34   -185       C  
ATOM   3585  CB  ASN B  85       2.235  12.263   5.570  1.00 12.88           C  
ANISOU 3585  CB  ASN B  85     1964   1359   1570    -77    -41   -187       C  
ATOM   3586  CG  ASN B  85       2.223  12.196   4.047  1.00 13.06           C  
ANISOU 3586  CG  ASN B  85     2041   1349   1572    -91    -41   -184       C  
ATOM   3587  OD1 ASN B  85       3.022  12.818   3.360  1.00 15.14           O  
ANISOU 3587  OD1 ASN B  85     2316   1598   1837    -79    -31   -179       O  
ATOM   3588  ND2 ASN B  85       1.321  11.371   3.516  1.00 14.23           N  
ANISOU 3588  ND2 ASN B  85     2226   1484   1697   -120    -51   -187       N  
ATOM   3589  C   ASN B  85       4.673  12.817   5.808  1.00 15.08           C  
ANISOU 3589  C   ASN B  85     2226   1636   1869    -28      5   -169       C  
ATOM   3590  O   ASN B  85       5.009  11.635   5.980  1.00 15.76           O  
ANISOU 3590  O   ASN B  85     2335   1710   1943    -23     31   -159       O  
ATOM   3591  N   GLY B  86       5.498  13.761   5.355  1.00 16.47           N  
ANISOU 3591  N   GLY B  86     2393   1806   2057    -15     10   -168       N  
ATOM   3592  CA  GLY B  86       6.903  13.476   5.095  1.00 12.44           C  
ANISOU 3592  CA  GLY B  86     1895   1281   1551      7     47   -152       C  
ATOM   3593  C   GLY B  86       7.189  12.498   3.979  1.00 16.11           C  
ANISOU 3593  C   GLY B  86     2423   1705   1993      4     78   -142       C  
ATOM   3594  O   GLY B  86       8.244  11.841   4.006  1.00 16.01           O  
ANISOU 3594  O   GLY B  86     2421   1679   1984     25    116   -127       O  
ATOM   3595  N   THR B  87       6.282  12.390   3.006  1.00 12.82           N  
ANISOU 3595  N   THR B  87     2050   1268   1554    -21     63   -150       N  
ATOM   3596  CA  THR B  87       6.498  11.473   1.891  1.00 18.04           C  
ANISOU 3596  CA  THR B  87     2779   1887   2188    -30     92   -144       C  
ATOM   3597  CB  THR B  87       5.158  10.895   1.376  1.00 17.33           C  
ANISOU 3597  CB  THR B  87     2729   1788   2069    -66     67   -154       C  
ATOM   3598  OG1 THR B  87       4.220  11.952   1.098  1.00 13.59           O  
ANISOU 3598  OG1 THR B  87     2235   1330   1597    -83     20   -165       O  
ATOM   3599  CG2 THR B  87       4.565   9.938   2.428  1.00 18.10           C  
ANISOU 3599  CG2 THR B  87     2810   1900   2166    -71     66   -156       C  
ATOM   3600  C   THR B  87       7.282  12.070   0.712  1.00 14.87           C  
ANISOU 3600  C   THR B  87     2409   1458   1782    -24    111   -140       C  
ATOM   3601  O   THR B  87       7.696  11.328  -0.178  1.00 16.34           O  
ANISOU 3601  O   THR B  87     2653   1608   1948    -27    146   -134       O  
ATOM   3602  N   ALA B  88       7.504  13.385   0.715  1.00 14.91           N  
ANISOU 3602  N   ALA B  88     2379   1480   1808    -17     93   -143       N  
ATOM   3603  CA  ALA B  88       8.374  14.030  -0.275  1.00 15.28           C  
ANISOU 3603  CA  ALA B  88     2449   1502   1856    -10    116   -138       C  
ATOM   3604  CB  ALA B  88       7.573  14.422  -1.534  1.00 17.78           C  
ANISOU 3604  CB  ALA B  88     2814   1797   2143    -36     92   -144       C  
ATOM   3605  C   ALA B  88       9.041  15.250   0.338  1.00 19.19           C  
ANISOU 3605  C   ALA B  88     2885   2022   2385      9    110   -138       C  
ATOM   3606  O   ALA B  88       8.683  16.386   0.032  1.00 15.38           O  
ANISOU 3606  O   ALA B  88     2391   1544   1908      1     84   -145       O  
ATOM   3607  N   VAL B  89      10.003  15.014   1.222  1.00 16.93           N  
ANISOU 3607  N   VAL B  89     2560   1751   2122     32    134   -130       N  
ATOM   3608  CA  VAL B  89      10.606  16.108   1.967  1.00 14.38           C  
ANISOU 3608  CA  VAL B  89     2177   1456   1830     45    125   -132       C  
ATOM   3609  CB  VAL B  89      11.115  15.660   3.348  1.00 15.73           C  
ANISOU 3609  CB  VAL B  89     2297   1659   2020     62    130   -126       C  
ATOM   3610  CG1 VAL B  89      11.807  16.811   4.052  1.00 17.14           C  
ANISOU 3610  CG1 VAL B  89     2419   1867   2228     70    121   -130       C  
ATOM   3611  CG2 VAL B  89       9.975  15.111   4.206  1.00 15.58           C  
ANISOU 3611  CG2 VAL B  89     2268   1662   1989     51    101   -134       C  
ATOM   3612  C   VAL B  89      11.763  16.661   1.161  1.00 16.62           C  
ANISOU 3612  C   VAL B  89     2471   1718   2125     56    158   -124       C  
ATOM   3613  O   VAL B  89      12.726  15.933   0.884  1.00 21.11           O  
ANISOU 3613  O   VAL B  89     3056   2269   2696     71    201   -110       O  
ATOM   3614  N   LEU B  90      11.651  17.942   0.808  1.00 20.16           N  
ANISOU 3614  N   LEU B  90     2910   2167   2582     48    140   -133       N  
ATOM   3615  CA  LEU B  90      12.637  18.639  -0.026  1.00 21.58           C  
ANISOU 3615  CA  LEU B  90     3102   2325   2773     54    170   -128       C  
ATOM   3616  CB  LEU B  90      13.875  19.028   0.803  1.00 20.46           C  
ANISOU 3616  CB  LEU B  90     2903   2206   2667     71    189   -123       C  
ATOM   3617  CG  LEU B  90      13.607  20.073   1.906  1.00 20.12           C  
ANISOU 3617  CG  LEU B  90     2798   2201   2645     66    153   -137       C  
ATOM   3618  CD1 LEU B  90      14.838  20.234   2.780  1.00 27.51           C  
ANISOU 3618  CD1 LEU B  90     3679   3162   3610     80    169   -130       C  
ATOM   3619  CD2 LEU B  90      13.179  21.401   1.341  1.00 21.94           C  
ANISOU 3619  CD2 LEU B  90     3037   2421   2879     53    135   -149       C  
ATOM   3620  C   LEU B  90      12.981  17.734  -1.204  1.00 28.77           C  
ANISOU 3620  C   LEU B  90     4079   3194   3659     54    209   -117       C  
ATOM   3621  O   LEU B  90      12.077  17.318  -1.943  1.00 22.46           O  
ANISOU 3621  O   LEU B  90     3332   2374   2826     37    196   -120       O  
ATOM   3622  N   GLY B  91      14.259  17.397  -1.354  1.00 25.61           N  
ANISOU 3622  N   GLY B  91     3677   2781   3274     73    257   -103       N  
ATOM   3623  CA  GLY B  91      14.695  16.447  -2.374  1.00 27.60           C  
ANISOU 3623  CA  GLY B  91     3991   2990   3505     76    304    -93       C  
ATOM   3624  C   GLY B  91      15.135  15.106  -1.801  1.00 28.43           C  
ANISOU 3624  C   GLY B  91     4091   3096   3616     95    334    -79       C  
ATOM   3625  O   GLY B  91      15.831  14.315  -2.462  1.00 28.52           O  
ANISOU 3625  O   GLY B  91     4142   3073   3622    107    386    -67       O  
ATOM   3626  N   LEU B  92      14.710  14.834  -0.568  1.00 22.16           N  
ANISOU 3626  N   LEU B  92     3251   2338   2831    100    303    -81       N  
ATOM   3627  CA  LEU B  92      15.113  13.637   0.178  1.00 17.76           C  
ANISOU 3627  CA  LEU B  92     2680   1787   2281    120    325    -66       C  
ATOM   3628  CB  LEU B  92      15.209  13.974   1.669  1.00 21.76           C  
ANISOU 3628  CB  LEU B  92     3110   2345   2814    130    293    -64       C  
ATOM   3629  CG  LEU B  92      16.215  15.057   2.034  1.00 22.49           C  
ANISOU 3629  CG  LEU B  92     3145   2461   2941    140    294    -61       C  
ATOM   3630  CD1 LEU B  92      16.166  15.354   3.516  1.00 26.43           C  
ANISOU 3630  CD1 LEU B  92     3576   3011   3457    143    258    -63       C  
ATOM   3631  CD2 LEU B  92      17.632  14.596   1.614  1.00 22.83           C  
ANISOU 3631  CD2 LEU B  92     3186   2483   3005    166    351    -38       C  
ATOM   3632  C   LEU B  92      14.158  12.448  -0.014  1.00 20.81           C  
ANISOU 3632  C   LEU B  92     3119   2153   2633    107    324    -69       C  
ATOM   3633  O   LEU B  92      14.460  11.306   0.371  1.00 21.68           O  
ANISOU 3633  O   LEU B  92     3236   2256   2745    124    352    -55       O  
ATOM   3634  N   GLY B  93      12.997  12.728  -0.594  1.00 22.94           N  
ANISOU 3634  N   GLY B  93     3426   2416   2874     77    291    -86       N  
ATOM   3635  CA  GLY B  93      11.999  11.703  -0.826  1.00 20.49           C  
ANISOU 3635  CA  GLY B  93     3165   2089   2531     58    284    -92       C  
ATOM   3636  C   GLY B  93      11.198  11.333   0.403  1.00 21.57           C  
ANISOU 3636  C   GLY B  93     3264   2261   2671     54    250    -96       C  
ATOM   3637  O   GLY B  93      10.877  12.179   1.254  1.00 22.45           O  
ANISOU 3637  O   GLY B  93     3319   2411   2800     54    211   -103       O  
ATOM   3638  N   ASN B  94      10.850  10.057   0.481  1.00 20.94           N  
ANISOU 3638  N   ASN B  94     3220   2164   2573     50    266    -92       N  
ATOM   3639  CA  ASN B  94       9.902   9.592   1.480  1.00 15.63           C  
ANISOU 3639  CA  ASN B  94     2525   1518   1896     40    235    -98       C  
ATOM   3640  CB  ASN B  94       9.091   8.429   0.904  1.00 18.58           C  
ANISOU 3640  CB  ASN B  94     2964   1859   2235     14    245   -103       C  
ATOM   3641  CG  ASN B  94       7.951   8.012   1.792  1.00 24.76           C  
ANISOU 3641  CG  ASN B  94     3729   2667   3011     -4    211   -112       C  
ATOM   3642  OD1 ASN B  94       7.822   8.470   2.924  1.00 19.92           O  
ANISOU 3642  OD1 ASN B  94     3056   2094   2420      6    186   -112       O  
ATOM   3643  ND2 ASN B  94       7.115   7.107   1.288  1.00 29.32           N  
ANISOU 3643  ND2 ASN B  94     4361   3220   3558    -33    213   -120       N  
ATOM   3644  C   ASN B  94      10.621   9.186   2.749  1.00 21.58           C  
ANISOU 3644  C   ASN B  94     3228   2296   2676     70    249    -81       C  
ATOM   3645  O   ASN B  94      10.923   8.000   2.950  1.00 24.03           O  
ANISOU 3645  O   ASN B  94     3561   2588   2982     83    283    -67       O  
ATOM   3646  N   ILE B  95      10.901  10.162   3.611  1.00 16.30           N  
ANISOU 3646  N   ILE B  95     2493   1667   2032     81    223    -82       N  
ATOM   3647  CA  ILE B  95      11.641   9.871   4.834  1.00 17.66           C  
ANISOU 3647  CA  ILE B  95     2615   1868   2226    108    231    -64       C  
ATOM   3648  CB  ILE B  95      12.722  10.936   5.075  1.00 16.48           C  
ANISOU 3648  CB  ILE B  95     2414   1741   2107    126    230    -59       C  
ATOM   3649  CG1 ILE B  95      12.101  12.334   5.187  1.00 19.36           C  
ANISOU 3649  CG1 ILE B  95     2749   2131   2476    105    186    -82       C  
ATOM   3650  CD1 ILE B  95      13.088  13.467   5.496  1.00 21.05           C  
ANISOU 3650  CD1 ILE B  95     2911   2368   2719    117    183    -80       C  
ATOM   3651  CG2 ILE B  95      13.755  10.867   3.941  1.00 20.95           C  
ANISOU 3651  CG2 ILE B  95     3010   2269   2680    141    276    -47       C  
ATOM   3652  C   ILE B  95      10.742   9.743   6.060  1.00 18.95           C  
ANISOU 3652  C   ILE B  95     2747   2067   2385     98    195    -72       C  
ATOM   3653  O   ILE B  95      11.209   9.354   7.138  1.00 18.38           O  
ANISOU 3653  O   ILE B  95     2640   2019   2324    117    199    -56       O  
ATOM   3654  N   GLY B  96       9.451  10.035   5.887  1.00 17.91           N  
ANISOU 3654  N   GLY B  96     2628   1938   2238     68    162    -93       N  
ATOM   3655  CA  GLY B  96       8.485   9.914   6.971  1.00 17.28           C  
ANISOU 3655  CA  GLY B  96     2523   1890   2154     55    132   -102       C  
ATOM   3656  C   GLY B  96       8.294  11.174   7.798  1.00 19.49           C  
ANISOU 3656  C   GLY B  96     2744   2211   2452     52     96   -116       C  
ATOM   3657  O   GLY B  96       9.075  12.118   7.699  1.00 18.86           O  
ANISOU 3657  O   GLY B  96     2637   2139   2389     63     95   -115       O  
ATOM   3658  N   PRO B  97       7.253  11.189   8.646  1.00 16.05           N  
ANISOU 3658  N   PRO B  97     2288   1798   2011     36     69   -128       N  
ATOM   3659  CA  PRO B  97       6.811  12.450   9.276  1.00 16.60           C  
ANISOU 3659  CA  PRO B  97     2311   1901   2094     28     36   -146       C  
ATOM   3660  CB  PRO B  97       5.461  12.077   9.916  1.00 19.70           C  
ANISOU 3660  CB  PRO B  97     2700   2306   2477      7     17   -158       C  
ATOM   3661  CG  PRO B  97       5.438  10.587   9.976  1.00 16.93           C  
ANISOU 3661  CG  PRO B  97     2385   1939   2109      9     41   -143       C  
ATOM   3662  CD  PRO B  97       6.292  10.090   8.832  1.00 18.99           C  
ANISOU 3662  CD  PRO B  97     2689   2163   2364     20     70   -129       C  
ATOM   3663  C   PRO B  97       7.761  12.998  10.326  1.00 16.15           C  
ANISOU 3663  C   PRO B  97     2205   1876   2054     46     36   -141       C  
ATOM   3664  O   PRO B  97       8.003  14.200  10.339  1.00 16.37           O  
ANISOU 3664  O   PRO B  97     2205   1917   2097     45     22   -152       O  
ATOM   3665  N   ALA B  98       8.296  12.152  11.206  1.00 16.73           N  
ANISOU 3665  N   ALA B  98     2269   1963   2124     61     49   -123       N  
ATOM   3666  CA  ALA B  98       9.256  12.661  12.184  1.00 18.53           C  
ANISOU 3666  CA  ALA B  98     2451   2226   2365     75     45   -116       C  
ATOM   3667  CB  ALA B  98       9.719  11.550  13.116  1.00 22.95           C  
ANISOU 3667  CB  ALA B  98     3006   2799   2916     92     57    -92       C  
ATOM   3668  C   ALA B  98      10.466  13.315  11.503  1.00 14.96           C  
ANISOU 3668  C   ALA B  98     1987   1765   1931     89     57   -108       C  
ATOM   3669  O   ALA B  98      10.887  14.415  11.888  1.00 14.30           O  
ANISOU 3669  O   ALA B  98     1866   1705   1862     87     43   -119       O  
ATOM   3670  N   ALA B  99      11.021  12.650  10.489  1.00 17.40           N  
ANISOU 3670  N   ALA B  99     2332   2040   2241    103     88    -92       N  
ATOM   3671  CA  ALA B  99      12.208  13.175   9.818  1.00 18.24           C  
ANISOU 3671  CA  ALA B  99     2429   2136   2366    117    107    -83       C  
ATOM   3672  CB  ALA B  99      12.800  12.119   8.866  1.00 14.63           C  
ANISOU 3672  CB  ALA B  99     2015   1638   1906    135    149    -61       C  
ATOM   3673  C   ALA B  99      11.909  14.473   9.075  1.00 16.15           C  
ANISOU 3673  C   ALA B  99     2164   1863   2108    100     92   -105       C  
ATOM   3674  O   ALA B  99      12.814  15.284   8.837  1.00 19.70           O  
ANISOU 3674  O   ALA B  99     2592   2315   2576    106     98   -104       O  
ATOM   3675  N   GLY B 100      10.649  14.693   8.720  1.00 15.48           N  
ANISOU 3675  N   GLY B 100     2104   1769   2010     79     72   -125       N  
ATOM   3676  CA  GLY B 100      10.276  15.947   8.083  1.00 18.01           C  
ANISOU 3676  CA  GLY B 100     2424   2083   2338     65     55   -144       C  
ATOM   3677  C   GLY B 100      10.031  17.122   9.026  1.00 15.84           C  
ANISOU 3677  C   GLY B 100     2100   1840   2077     56     28   -162       C  
ATOM   3678  O   GLY B 100       9.903  18.258   8.568  1.00 14.13           O  
ANISOU 3678  O   GLY B 100     1880   1618   1872     48     18   -176       O  
ATOM   3679  N   LYS B 101       9.984  16.869  10.333  1.00 12.27           N  
ANISOU 3679  N   LYS B 101     1617   1422   1624     57     17   -163       N  
ATOM   3680  CA  LYS B 101       9.623  17.916  11.284  1.00 16.18           C  
ANISOU 3680  CA  LYS B 101     2073   1947   2127     44     -6   -184       C  
ATOM   3681  CB  LYS B 101       9.595  17.342  12.700  1.00 13.89           C  
ANISOU 3681  CB  LYS B 101     1759   1692   1828     45    -14   -180       C  
ATOM   3682  CG  LYS B 101       9.117  18.332  13.759  1.00 16.50           C  
ANISOU 3682  CG  LYS B 101     2055   2052   2162     30    -35   -204       C  
ATOM   3683  CD  LYS B 101       8.767  17.604  15.078  1.00 15.10           C  
ANISOU 3683  CD  LYS B 101     1866   1904   1968     27    -42   -202       C  
ATOM   3684  CE  LYS B 101       8.253  18.549  16.185  1.00 14.25           C  
ANISOU 3684  CE  LYS B 101     1730   1824   1860      9    -58   -228       C  
ATOM   3685  NZ  LYS B 101       6.861  19.073  15.908  1.00 14.77           N  
ANISOU 3685  NZ  LYS B 101     1804   1875   1932     -4    -66   -250       N  
ATOM   3686  C   LYS B 101      10.528  19.161  11.226  1.00 15.60           C  
ANISOU 3686  C   LYS B 101     1972   1880   2074     44     -6   -191       C  
ATOM   3687  O   LYS B 101      10.028  20.276  11.324  1.00 13.78           O  
ANISOU 3687  O   LYS B 101     1730   1653   1854     31    -21   -212       O  
ATOM   3688  N   PRO B 102      11.860  18.992  11.069  1.00 14.12           N  
ANISOU 3688  N   PRO B 102     1774   1694   1897     58     13   -173       N  
ATOM   3689  CA  PRO B 102      12.665  20.221  10.955  1.00 12.44           C  
ANISOU 3689  CA  PRO B 102     1536   1486   1705     53     14   -182       C  
ATOM   3690  CB  PRO B 102      14.104  19.689  10.777  1.00 17.35           C  
ANISOU 3690  CB  PRO B 102     2146   2110   2337     71     38   -156       C  
ATOM   3691  CG  PRO B 102      14.071  18.361  11.475  1.00 14.66           C  
ANISOU 3691  CG  PRO B 102     1806   1784   1982     84     40   -137       C  
ATOM   3692  CD  PRO B 102      12.714  17.787  11.101  1.00 14.48           C  
ANISOU 3692  CD  PRO B 102     1824   1739   1938     78     35   -144       C  
ATOM   3693  C   PRO B 102      12.279  21.095   9.773  1.00 13.01           C  
ANISOU 3693  C   PRO B 102     1634   1524   1784     46     17   -194       C  
ATOM   3694  O   PRO B 102      12.345  22.329   9.857  1.00 13.03           O  
ANISOU 3694  O   PRO B 102     1619   1531   1801     35     10   -211       O  
ATOM   3695  N   VAL B 103      11.915  20.446   8.672  1.00 11.61           N  
ANISOU 3695  N   VAL B 103     1501   1314   1595     52     29   -183       N  
ATOM   3696  CA  VAL B 103      11.498  21.188   7.485  1.00 11.68           C  
ANISOU 3696  CA  VAL B 103     1541   1291   1606     45     29   -191       C  
ATOM   3697  CB  VAL B 103      11.331  20.271   6.244  1.00 14.07           C  
ANISOU 3697  CB  VAL B 103     1898   1558   1891     50     47   -176       C  
ATOM   3698  CG1 VAL B 103      10.504  20.963   5.150  1.00 17.85           C  
ANISOU 3698  CG1 VAL B 103     2411   2009   2363     39     35   -184       C  
ATOM   3699  CG2 VAL B 103      12.705  19.923   5.697  1.00 16.42           C  
ANISOU 3699  CG2 VAL B 103     2202   1840   2196     65     83   -157       C  
ATOM   3700  C   VAL B 103      10.197  21.922   7.782  1.00 13.93           C  
ANISOU 3700  C   VAL B 103     1821   1582   1891     31      0   -212       C  
ATOM   3701  O   VAL B 103      10.062  23.064   7.399  1.00 12.75           O  
ANISOU 3701  O   VAL B 103     1669   1421   1753     25     -5   -223       O  
ATOM   3702  N   MET B 104       9.237  21.284   8.447  1.00 12.92           N  
ANISOU 3702  N   MET B 104     1690   1469   1751     26    -16   -216       N  
ATOM   3703  CA  MET B 104       7.969  21.988   8.733  1.00 11.07           C  
ANISOU 3703  CA  MET B 104     1446   1240   1521     15    -41   -235       C  
ATOM   3704  CB  MET B 104       6.892  20.998   9.192  1.00 14.62           C  
ANISOU 3704  CB  MET B 104     1901   1698   1954     10    -53   -235       C  
ATOM   3705  CG  MET B 104       6.719  19.807   8.249  1.00 16.94           C  
ANISOU 3705  CG  MET B 104     2239   1968   2227     11    -45   -218       C  
ATOM   3706  SD  MET B 104       6.711  20.216   6.479  1.00 18.58           S  
ANISOU 3706  SD  MET B 104     2493   2136   2431      9    -43   -211       S  
ATOM   3707  CE  MET B 104       7.742  18.883   5.801  1.00 15.59           C  
ANISOU 3707  CE  MET B 104     2154   1735   2033     19     -8   -189       C  
ATOM   3708  C   MET B 104       8.114  23.104   9.764  1.00 10.90           C  
ANISOU 3708  C   MET B 104     1383   1241   1517      9    -48   -254       C  
ATOM   3709  O   MET B 104       7.499  24.162   9.616  1.00 12.50           O  
ANISOU 3709  O   MET B 104     1581   1436   1733      3    -58   -268       O  
ATOM   3710  N   GLU B 105       8.939  22.898  10.798  1.00 11.01           N  
ANISOU 3710  N   GLU B 105     1368   1283   1530     10    -42   -254       N  
ATOM   3711  CA  GLU B 105       9.281  24.007  11.699  1.00 11.50           C  
ANISOU 3711  CA  GLU B 105     1396   1367   1606     -1    -46   -273       C  
ATOM   3712  CB  GLU B 105      10.247  23.546  12.805  1.00 15.10           C  
ANISOU 3712  CB  GLU B 105     1824   1858   2056     -1    -44   -268       C  
ATOM   3713  CG  GLU B 105       9.583  22.729  13.913  1.00 16.22           C  
ANISOU 3713  CG  GLU B 105     1958   2026   2179     -4    -55   -269       C  
ATOM   3714  CD  GLU B 105      10.503  22.464  15.121  1.00 21.98           C  
ANISOU 3714  CD  GLU B 105     2657   2793   2900     -6    -58   -264       C  
ATOM   3715  OE1 GLU B 105      11.626  23.034  15.198  1.00 19.77           O  
ANISOU 3715  OE1 GLU B 105     2356   2524   2631     -9    -55   -263       O  
ATOM   3716  OE2 GLU B 105      10.069  21.704  16.008  1.00 16.75           O  
ANISOU 3716  OE2 GLU B 105     1992   2152   2219     -7    -65   -261       O  
ATOM   3717  C   GLU B 105       9.909  25.186  10.925  1.00 11.28           C  
ANISOU 3717  C   GLU B 105     1370   1318   1598     -3    -37   -278       C  
ATOM   3718  O   GLU B 105       9.557  26.337  11.151  1.00 13.26           O  
ANISOU 3718  O   GLU B 105     1610   1566   1863    -12    -42   -298       O  
ATOM   3719  N   GLY B 106      10.799  24.872   9.996  1.00 12.45           N  
ANISOU 3719  N   GLY B 106     1534   1447   1747      7    -20   -260       N  
ATOM   3720  CA  GLY B 106      11.455  25.882   9.182  1.00 13.29           C  
ANISOU 3720  CA  GLY B 106     1647   1531   1871      4     -7   -262       C  
ATOM   3721  C   GLY B 106      10.488  26.615   8.274  1.00 12.35           C  
ANISOU 3721  C   GLY B 106     1556   1381   1756      3    -13   -268       C  
ATOM   3722  O   GLY B 106      10.558  27.836   8.163  1.00 14.13           O  
ANISOU 3722  O   GLY B 106     1775   1596   1999     -4    -11   -281       O  
ATOM   3723  N   LYS B 107       9.579  25.872   7.634  1.00 11.99           N  
ANISOU 3723  N   LYS B 107     1541   1321   1694      9    -23   -258       N  
ATOM   3724  CA  LYS B 107       8.535  26.508   6.824  1.00 13.90           C  
ANISOU 3724  CA  LYS B 107     1805   1537   1939      7    -36   -261       C  
ATOM   3725  CB  LYS B 107       7.610  25.449   6.209  1.00 14.85           C  
ANISOU 3725  CB  LYS B 107     1957   1648   2037      9    -49   -248       C  
ATOM   3726  CG  LYS B 107       6.652  25.993   5.146  1.00 20.07           C  
ANISOU 3726  CG  LYS B 107     2645   2282   2697      8    -66   -244       C  
ATOM   3727  CD  LYS B 107       7.305  25.992   3.789  1.00 22.65           C  
ANISOU 3727  CD  LYS B 107     3015   2578   3013     11    -51   -228       C  
ATOM   3728  CE  LYS B 107       6.330  26.456   2.707  1.00 30.27           C  
ANISOU 3728  CE  LYS B 107     4011   3519   3972      9    -72   -220       C  
ATOM   3729  NZ  LYS B 107       6.878  26.114   1.365  1.00 27.82           N  
ANISOU 3729  NZ  LYS B 107     3752   3178   3639      8    -57   -203       N  
ATOM   3730  C   LYS B 107       7.735  27.492   7.691  1.00 12.27           C  
ANISOU 3730  C   LYS B 107     1570   1343   1749      1    -51   -282       C  
ATOM   3731  O   LYS B 107       7.408  28.606   7.266  1.00 13.40           O  
ANISOU 3731  O   LYS B 107     1717   1466   1907      1    -53   -288       O  
ATOM   3732  N   GLY B 108       7.435  27.105   8.930  1.00 12.28           N  
ANISOU 3732  N   GLY B 108     1543   1374   1747     -3    -57   -294       N  
ATOM   3733  CA  GLY B 108       6.705  27.996   9.821  1.00 12.98           C  
ANISOU 3733  CA  GLY B 108     1607   1474   1852    -10    -65   -316       C  
ATOM   3734  C   GLY B 108       7.478  29.264  10.153  1.00 15.38           C  
ANISOU 3734  C   GLY B 108     1895   1776   2174    -18    -52   -332       C  
ATOM   3735  O   GLY B 108       6.875  30.326  10.289  1.00 14.77           O  
ANISOU 3735  O   GLY B 108     1811   1687   2115    -20    -53   -348       O  
ATOM   3736  N   ILE B 109       8.804  29.151  10.291  1.00 11.90           N  
ANISOU 3736  N   ILE B 109     1446   1346   1731    -22    -39   -329       N  
ATOM   3737  CA  ILE B 109       9.674  30.297  10.507  1.00 15.64           C  
ANISOU 3737  CA  ILE B 109     1905   1816   2222    -34    -26   -343       C  
ATOM   3738  CB  ILE B 109      11.151  29.880  10.687  1.00 18.23           C  
ANISOU 3738  CB  ILE B 109     2218   2163   2546    -38    -14   -334       C  
ATOM   3739  CG1 ILE B 109      11.325  29.092  11.985  1.00 24.57           C  
ANISOU 3739  CG1 ILE B 109     2994   3008   3334    -44    -25   -337       C  
ATOM   3740  CD1 ILE B 109      10.826  29.781  13.172  1.00 30.50           C  
ANISOU 3740  CD1 ILE B 109     3726   3778   4086    -60    -32   -365       C  
ATOM   3741  CG2 ILE B 109      12.075  31.116  10.705  1.00 18.30           C  
ANISOU 3741  CG2 ILE B 109     2214   2165   2575    -54      0   -348       C  
ATOM   3742  C   ILE B 109       9.563  31.272   9.333  1.00 17.00           C  
ANISOU 3742  C   ILE B 109     2101   1948   2410    -29    -17   -340       C  
ATOM   3743  O   ILE B 109       9.479  32.468   9.550  1.00 17.15           O  
ANISOU 3743  O   ILE B 109     2114   1955   2447    -37    -10   -358       O  
ATOM   3744  N   LEU B 110       9.531  30.751   8.106  1.00 12.81           N  
ANISOU 3744  N   LEU B 110     1603   1395   1871    -17    -16   -317       N  
ATOM   3745  CA  LEU B 110       9.334  31.603   6.918  1.00 12.51           C  
ANISOU 3745  CA  LEU B 110     1593   1317   1843    -12    -11   -310       C  
ATOM   3746  CB  LEU B 110       9.480  30.781   5.650  1.00 13.14           C  
ANISOU 3746  CB  LEU B 110     1711   1378   1905     -2     -8   -284       C  
ATOM   3747  CG  LEU B 110      10.841  30.082   5.429  1.00 13.30           C  
ANISOU 3747  CG  LEU B 110     1733   1403   1917     -2     14   -272       C  
ATOM   3748  CD1 LEU B 110      10.814  29.481   4.050  1.00 17.43           C  
ANISOU 3748  CD1 LEU B 110     2303   1898   2423      6     20   -250       C  
ATOM   3749  CD2 LEU B 110      11.985  31.084   5.569  1.00 18.51           C  
ANISOU 3749  CD2 LEU B 110     2375   2059   2598    -12     36   -282       C  
ATOM   3750  C   LEU B 110       7.979  32.325   6.917  1.00 11.40           C  
ANISOU 3750  C   LEU B 110     1455   1163   1714     -7    -26   -317       C  
ATOM   3751  O   LEU B 110       7.915  33.522   6.599  1.00 15.31           O  
ANISOU 3751  O   LEU B 110     1956   1633   2228     -7    -18   -323       O  
ATOM   3752  N   PHE B 111       6.890  31.615   7.263  1.00 11.27           N  
ANISOU 3752  N   PHE B 111     1433   1161   1688     -2    -47   -316       N  
ATOM   3753  CA  PHE B 111       5.595  32.293   7.448  1.00 11.00           C  
ANISOU 3753  CA  PHE B 111     1391   1119   1671      4    -60   -324       C  
ATOM   3754  CB  PHE B 111       4.523  31.311   7.953  1.00 11.87           C  
ANISOU 3754  CB  PHE B 111     1488   1251   1770      6    -80   -322       C  
ATOM   3755  CG  PHE B 111       3.800  30.559   6.865  1.00 12.27           C  
ANISOU 3755  CG  PHE B 111     1566   1290   1806     13   -100   -299       C  
ATOM   3756  CD1 PHE B 111       2.660  31.089   6.286  1.00 15.26           C  
ANISOU 3756  CD1 PHE B 111     1949   1652   2198     21   -119   -290       C  
ATOM   3757  CE1 PHE B 111       1.947  30.374   5.288  1.00 13.06           C  
ANISOU 3757  CE1 PHE B 111     1694   1365   1902     23   -143   -268       C  
ATOM   3758  CZ  PHE B 111       2.396  29.155   4.867  1.00 15.61           C  
ANISOU 3758  CZ  PHE B 111     2041   1694   2195     16   -144   -258       C  
ATOM   3759  CE2 PHE B 111       3.543  28.605   5.448  1.00 16.15           C  
ANISOU 3759  CE2 PHE B 111     2106   1776   2252     11   -121   -265       C  
ATOM   3760  CD2 PHE B 111       4.236  29.312   6.443  1.00 11.13           C  
ANISOU 3760  CD2 PHE B 111     1442   1152   1634     10   -102   -284       C  
ATOM   3761  C   PHE B 111       5.685  33.470   8.432  1.00 14.76           C  
ANISOU 3761  C   PHE B 111     1841   1596   2170     -4    -45   -351       C  
ATOM   3762  O   PHE B 111       5.136  34.550   8.192  1.00 14.00           O  
ANISOU 3762  O   PHE B 111     1748   1476   2097      3    -42   -355       O  
ATOM   3763  N   LYS B 112       6.358  33.263   9.555  1.00 12.67           N  
ANISOU 3763  N   LYS B 112     1553   1360   1899    -18    -36   -368       N  
ATOM   3764  CA  LYS B 112       6.384  34.296  10.576  1.00 13.28           C  
ANISOU 3764  CA  LYS B 112     1611   1441   1994    -30    -23   -397       C  
ATOM   3765  CB  LYS B 112       6.869  33.698  11.913  1.00 16.86           C  
ANISOU 3765  CB  LYS B 112     2039   1936   2430    -46    -23   -413       C  
ATOM   3766  CG  LYS B 112       6.778  34.665  13.116  1.00 18.96           C  
ANISOU 3766  CG  LYS B 112     2288   2210   2708    -64     -9   -447       C  
ATOM   3767  CD  LYS B 112       5.299  34.802  13.534  1.00 22.75           C  
ANISOU 3767  CD  LYS B 112     2763   2685   3198    -54    -12   -456       C  
ATOM   3768  CE  LYS B 112       5.049  35.860  14.584  1.00 36.03           C  
ANISOU 3768  CE  LYS B 112     4433   4364   4893    -68      7   -489       C  
ATOM   3769  NZ  LYS B 112       5.498  35.430  15.922  1.00 40.31           N  
ANISOU 3769  NZ  LYS B 112     4960   4945   5411    -91      8   -509       N  
ATOM   3770  C   LYS B 112       7.270  35.470  10.132  1.00 12.77           C  
ANISOU 3770  C   LYS B 112     1555   1350   1945    -37     -3   -403       C  
ATOM   3771  O   LYS B 112       6.892  36.649  10.265  1.00 15.12           O  
ANISOU 3771  O   LYS B 112     1854   1626   2266    -38      9   -419       O  
ATOM   3772  N   GLN B 113       8.446  35.152   9.606  1.00 14.57           N  
ANISOU 3772  N   GLN B 113     1791   1580   2164    -43      4   -392       N  
ATOM   3773  CA  GLN B 113       9.408  36.210   9.257  1.00 14.85           C  
ANISOU 3773  CA  GLN B 113     1833   1594   2216    -54     26   -399       C  
ATOM   3774  CB  GLN B 113      10.791  35.611   9.018  1.00 19.68           C  
ANISOU 3774  CB  GLN B 113     2440   2220   2817    -63     34   -388       C  
ATOM   3775  CG  GLN B 113      11.344  34.999  10.291  1.00 25.01           C  
ANISOU 3775  CG  GLN B 113     3082   2942   3480    -78     27   -400       C  
ATOM   3776  CD  GLN B 113      11.334  35.987  11.437  1.00 36.80           C  
ANISOU 3776  CD  GLN B 113     4556   4444   4983   -101     33   -433       C  
ATOM   3777  OE1 GLN B 113      10.674  35.777  12.467  1.00 41.51           O  
ANISOU 3777  OE1 GLN B 113     5139   5063   5571   -105     23   -449       O  
ATOM   3778  NE2 GLN B 113      12.061  37.082  11.264  1.00 27.03           N  
ANISOU 3778  NE2 GLN B 113     3319   3188   3763   -117     53   -446       N  
ATOM   3779  C   GLN B 113       8.943  37.019   8.048  1.00 16.95           C  
ANISOU 3779  C   GLN B 113     2130   1814   2497    -40     32   -385       C  
ATOM   3780  O   GLN B 113       9.179  38.219   7.984  1.00 19.37           O  
ANISOU 3780  O   GLN B 113     2441   2095   2824    -47     50   -397       O  
ATOM   3781  N   PHE B 114       8.225  36.401   7.118  1.00 15.43           N  
ANISOU 3781  N   PHE B 114     1958   1610   2294    -20     15   -360       N  
ATOM   3782  CA  PHE B 114       7.883  37.111   5.896  1.00 14.97           C  
ANISOU 3782  CA  PHE B 114     1932   1509   2245     -7     17   -342       C  
ATOM   3783  CB  PHE B 114       8.125  36.219   4.688  1.00 15.05           C  
ANISOU 3783  CB  PHE B 114     1973   1512   2232      1      9   -313       C  
ATOM   3784  CG  PHE B 114       9.583  36.052   4.367  1.00 16.98           C  
ANISOU 3784  CG  PHE B 114     2225   1756   2471    -10     33   -310       C  
ATOM   3785  CD1 PHE B 114      10.353  35.116   5.051  1.00 16.45           C  
ANISOU 3785  CD1 PHE B 114     2135   1724   2393    -19     36   -315       C  
ATOM   3786  CE1 PHE B 114      11.707  34.969   4.781  1.00 19.39           C  
ANISOU 3786  CE1 PHE B 114     2506   2096   2764    -28     59   -311       C  
ATOM   3787  CZ  PHE B 114      12.306  35.752   3.801  1.00 18.85           C  
ANISOU 3787  CZ  PHE B 114     2464   1993   2705    -30     82   -303       C  
ATOM   3788  CE2 PHE B 114      11.546  36.704   3.123  1.00 18.10           C  
ANISOU 3788  CE2 PHE B 114     2396   1862   2618    -23     80   -298       C  
ATOM   3789  CD2 PHE B 114      10.190  36.844   3.409  1.00 19.68           C  
ANISOU 3789  CD2 PHE B 114     2594   2063   2820    -12     54   -301       C  
ATOM   3790  C   PHE B 114       6.455  37.650   5.882  1.00 17.52           C  
ANISOU 3790  C   PHE B 114     2255   1818   2585      9      3   -340       C  
ATOM   3791  O   PHE B 114       6.192  38.603   5.170  1.00 21.57           O  
ANISOU 3791  O   PHE B 114     2787   2295   3113     19      9   -331       O  
ATOM   3792  N   ALA B 115       5.554  37.078   6.682  1.00 14.71           N  
ANISOU 3792  N   ALA B 115     1876   1488   2227     12    -14   -348       N  
ATOM   3793  CA  ALA B 115       4.179  37.583   6.699  1.00 15.78           C  
ANISOU 3793  CA  ALA B 115     2004   1609   2382     29    -26   -345       C  
ATOM   3794  CB  ALA B 115       3.261  36.618   5.926  1.00 16.46           C  
ANISOU 3794  CB  ALA B 115     2100   1702   2453     43    -58   -317       C  
ATOM   3795  C   ALA B 115       3.613  37.820   8.099  1.00 16.66           C  
ANISOU 3795  C   ALA B 115     2082   1740   2508     24    -18   -373       C  
ATOM   3796  O   ALA B 115       2.469  38.230   8.234  1.00 17.05           O  
ANISOU 3796  O   ALA B 115     2120   1779   2578     39    -23   -372       O  
ATOM   3797  N   GLY B 116       4.399  37.548   9.137  1.00 13.84           N  
ANISOU 3797  N   GLY B 116     1709   1410   2140      4     -6   -397       N  
ATOM   3798  CA  GLY B 116       3.912  37.684  10.498  1.00 14.08           C  
ANISOU 3798  CA  GLY B 116     1713   1461   2178     -5      2   -425       C  
ATOM   3799  C   GLY B 116       2.884  36.639  10.907  1.00 18.09           C  
ANISOU 3799  C   GLY B 116     2205   1994   2675      3    -18   -419       C  
ATOM   3800  O   GLY B 116       2.148  36.856  11.866  1.00 18.68           O  
ANISOU 3800  O   GLY B 116     2259   2077   2760      1    -10   -438       O  
ATOM   3801  N   ILE B 117       2.841  35.516  10.192  1.00 15.26           N  
ANISOU 3801  N   ILE B 117     1856   1647   2296      8    -41   -394       N  
ATOM   3802  CA  ILE B 117       1.864  34.467  10.464  1.00 12.98           C  
ANISOU 3802  CA  ILE B 117     1555   1380   1997     13    -60   -386       C  
ATOM   3803  CB  ILE B 117       1.444  33.791   9.159  1.00 11.91           C  
ANISOU 3803  CB  ILE B 117     1440   1235   1851     25    -85   -354       C  
ATOM   3804  CG1 ILE B 117       0.651  34.794   8.309  1.00 15.04           C  
ANISOU 3804  CG1 ILE B 117     1842   1597   2274     43    -92   -341       C  
ATOM   3805  CD1 ILE B 117       0.478  34.380   6.853  1.00 15.09           C  
ANISOU 3805  CD1 ILE B 117     1878   1589   2267     51   -117   -308       C  
ATOM   3806  CG2 ILE B 117       0.580  32.524   9.445  1.00 13.69           C  
ANISOU 3806  CG2 ILE B 117     1654   1486   2061     23   -105   -348       C  
ATOM   3807  C   ILE B 117       2.423  33.426  11.449  1.00 13.26           C  
ANISOU 3807  C   ILE B 117     1580   1454   2006     -3    -59   -397       C  
ATOM   3808  O   ILE B 117       3.545  32.940  11.281  1.00 13.25           O  
ANISOU 3808  O   ILE B 117     1587   1462   1984    -11    -57   -392       O  
ATOM   3809  N   ASP B 118       1.637  33.090  12.475  1.00 12.87           N  
ANISOU 3809  N   ASP B 118     1508   1425   1956     -7    -58   -411       N  
ATOM   3810  CA  ASP B 118       1.987  32.013  13.409  1.00 15.23           C  
ANISOU 3810  CA  ASP B 118     1799   1760   2228    -20    -60   -417       C  
ATOM   3811  CB  ASP B 118       1.199  32.177  14.719  1.00 16.79           C  
ANISOU 3811  CB  ASP B 118     1974   1974   2431    -27    -49   -442       C  
ATOM   3812  CG  ASP B 118       1.494  33.491  15.410  1.00 25.28           C  
ANISOU 3812  CG  ASP B 118     3043   3038   3522    -37    -25   -470       C  
ATOM   3813  OD1 ASP B 118       2.636  33.667  15.889  1.00 21.10           O  
ANISOU 3813  OD1 ASP B 118     2516   2522   2978    -54    -17   -482       O  
ATOM   3814  OD2 ASP B 118       0.583  34.352  15.473  1.00 26.33           O  
ANISOU 3814  OD2 ASP B 118     3169   3150   3684    -27    -13   -480       O  
ATOM   3815  C   ASP B 118       1.677  30.650  12.796  1.00 14.03           C  
ANISOU 3815  C   ASP B 118     1657   1618   2056    -15    -80   -392       C  
ATOM   3816  O   ASP B 118       0.659  30.487  12.108  1.00 13.76           O  
ANISOU 3816  O   ASP B 118     1626   1571   2032     -5    -95   -378       O  
ATOM   3817  N   VAL B 119       2.551  29.673  13.036  1.00 13.49           N  
ANISOU 3817  N   VAL B 119     1595   1571   1961    -22    -81   -386       N  
ATOM   3818  CA  VAL B 119       2.345  28.355  12.456  1.00 10.56           C  
ANISOU 3818  CA  VAL B 119     1238   1204   1570    -18    -95   -363       C  
ATOM   3819  CB  VAL B 119       3.363  28.099  11.308  1.00 12.60           C  
ANISOU 3819  CB  VAL B 119     1524   1446   1818    -13    -95   -343       C  
ATOM   3820  CG1 VAL B 119       3.484  26.594  10.962  1.00 11.51           C  
ANISOU 3820  CG1 VAL B 119     1404   1315   1653    -13   -101   -324       C  
ATOM   3821  CG2 VAL B 119       2.999  28.925  10.071  1.00 14.74           C  
ANISOU 3821  CG2 VAL B 119     1812   1683   2105     -4   -102   -334       C  
ATOM   3822  C   VAL B 119       2.484  27.262  13.510  1.00 13.47           C  
ANISOU 3822  C   VAL B 119     1599   1605   1916    -27    -93   -366       C  
ATOM   3823  O   VAL B 119       3.418  27.275  14.307  1.00 14.06           O  
ANISOU 3823  O   VAL B 119     1665   1698   1980    -34    -84   -374       O  
ATOM   3824  N   PHE B 120       1.544  26.322  13.500  1.00 10.63           N  
ANISOU 3824  N   PHE B 120     1241   1250   1548    -27   -103   -358       N  
ATOM   3825  CA  PHE B 120       1.730  25.055  14.157  1.00 10.73           C  
ANISOU 3825  CA  PHE B 120     1256   1287   1535    -32   -102   -352       C  
ATOM   3826  CB  PHE B 120       0.441  24.546  14.815  1.00 13.11           C  
ANISOU 3826  CB  PHE B 120     1546   1600   1837    -38   -105   -358       C  
ATOM   3827  CG  PHE B 120      -0.028  25.323  16.024  1.00 12.59           C  
ANISOU 3827  CG  PHE B 120     1453   1547   1782    -45    -93   -383       C  
ATOM   3828  CD1 PHE B 120       0.759  26.300  16.636  1.00 14.46           C  
ANISOU 3828  CD1 PHE B 120     1682   1790   2024    -49    -81   -401       C  
ATOM   3829  CE1 PHE B 120       0.287  26.994  17.752  1.00 17.88           C  
ANISOU 3829  CE1 PHE B 120     2098   2233   2465    -58    -67   -427       C  
ATOM   3830  CZ  PHE B 120      -0.971  26.712  18.275  1.00 15.38           C  
ANISOU 3830  CZ  PHE B 120     1768   1920   2154    -60    -62   -434       C  
ATOM   3831  CE2 PHE B 120      -1.755  25.723  17.682  1.00 14.37           C  
ANISOU 3831  CE2 PHE B 120     1644   1789   2025    -56    -75   -415       C  
ATOM   3832  CD2 PHE B 120      -1.283  25.050  16.553  1.00 12.83           C  
ANISOU 3832  CD2 PHE B 120     1470   1584   1820    -50    -92   -391       C  
ATOM   3833  C   PHE B 120       2.156  24.081  13.057  1.00 15.09           C  
ANISOU 3833  C   PHE B 120     1837   1824   2071    -27   -107   -327       C  
ATOM   3834  O   PHE B 120       1.410  23.863  12.085  1.00 13.27           O  
ANISOU 3834  O   PHE B 120     1623   1577   1844    -25   -120   -316       O  
ATOM   3835  N   ASP B 121       3.344  23.500  13.177  1.00 13.33           N  
ANISOU 3835  N   ASP B 121     1622   1611   1832    -24    -98   -316       N  
ATOM   3836  CA  ASP B 121       3.738  22.446  12.240  1.00 14.22           C  
ANISOU 3836  CA  ASP B 121     1765   1709   1928    -18    -97   -294       C  
ATOM   3837  CB  ASP B 121       5.262  22.336  12.122  1.00 13.38           C  
ANISOU 3837  CB  ASP B 121     1662   1604   1816    -11    -82   -282       C  
ATOM   3838  CG  ASP B 121       5.929  22.027  13.450  1.00 19.99           C  
ANISOU 3838  CG  ASP B 121     2476   2474   2645    -12    -77   -285       C  
ATOM   3839  OD1 ASP B 121       5.943  22.893  14.356  1.00 18.19           O  
ANISOU 3839  OD1 ASP B 121     2222   2264   2425    -21    -79   -304       O  
ATOM   3840  OD2 ASP B 121       6.449  20.907  13.588  1.00 18.87           O  
ANISOU 3840  OD2 ASP B 121     2344   2339   2488     -6    -70   -267       O  
ATOM   3841  C   ASP B 121       3.155  21.121  12.700  1.00 16.30           C  
ANISOU 3841  C   ASP B 121     2037   1984   2173    -23    -98   -286       C  
ATOM   3842  O   ASP B 121       3.277  20.743  13.866  1.00 16.98           O  
ANISOU 3842  O   ASP B 121     2106   2095   2250    -26    -93   -291       O  
ATOM   3843  N   ILE B 122       2.520  20.418  11.778  1.00 11.59           N  
ANISOU 3843  N   ILE B 122     1466   1368   1568    -25   -104   -275       N  
ATOM   3844  CA  ILE B 122       1.832  19.183  12.135  1.00 14.30           C  
ANISOU 3844  CA  ILE B 122     1819   1718   1895    -33   -105   -270       C  
ATOM   3845  CB  ILE B 122       0.304  19.337  12.011  1.00 14.22           C  
ANISOU 3845  CB  ILE B 122     1801   1707   1896    -46   -122   -279       C  
ATOM   3846  CG1 ILE B 122      -0.210  20.557  12.811  1.00 15.14           C  
ANISOU 3846  CG1 ILE B 122     1879   1838   2037    -46   -125   -299       C  
ATOM   3847  CD1 ILE B 122      -0.115  20.411  14.332  1.00 18.39           C  
ANISOU 3847  CD1 ILE B 122     2267   2276   2442    -49   -113   -311       C  
ATOM   3848  CG2 ILE B 122      -0.409  18.028  12.406  1.00 16.03           C  
ANISOU 3848  CG2 ILE B 122     2040   1943   2108    -58   -120   -274       C  
ATOM   3849  C   ILE B 122       2.314  18.069  11.225  1.00 18.79           C  
ANISOU 3849  C   ILE B 122     2428   2266   2444    -31    -96   -250       C  
ATOM   3850  O   ILE B 122       2.072  18.099  10.022  1.00 16.12           O  
ANISOU 3850  O   ILE B 122     2117   1905   2104    -34   -103   -244       O  
ATOM   3851  N   GLU B 123       3.008  17.093  11.801  1.00 13.10           N  
ANISOU 3851  N   GLU B 123     1714   1555   1709    -25    -79   -239       N  
ATOM   3852  CA  GLU B 123       3.529  15.973  11.046  1.00 12.23           C  
ANISOU 3852  CA  GLU B 123     1643   1422   1581    -20    -63   -219       C  
ATOM   3853  CB  GLU B 123       4.971  15.654  11.489  1.00 15.84           C  
ANISOU 3853  CB  GLU B 123     2095   1888   2036     -1    -42   -205       C  
ATOM   3854  CG  GLU B 123       5.993  16.796  11.214  1.00 17.42           C  
ANISOU 3854  CG  GLU B 123     2277   2089   2254     10    -40   -207       C  
ATOM   3855  CD  GLU B 123       5.950  17.912  12.235  1.00 19.74           C  
ANISOU 3855  CD  GLU B 123     2528   2412   2562      5    -53   -225       C  
ATOM   3856  OE1 GLU B 123       5.827  17.627  13.449  1.00 16.40           O  
ANISOU 3856  OE1 GLU B 123     2084   2015   2132      3    -56   -228       O  
ATOM   3857  OE2 GLU B 123       6.078  19.082  11.816  1.00 18.86           O  
ANISOU 3857  OE2 GLU B 123     2406   2294   2466      4    -59   -236       O  
ATOM   3858  C   GLU B 123       2.593  14.800  11.294  1.00 18.02           C  
ANISOU 3858  C   GLU B 123     2393   2155   2299    -33    -63   -217       C  
ATOM   3859  O   GLU B 123       2.323  14.454  12.465  1.00 19.45           O  
ANISOU 3859  O   GLU B 123     2555   2359   2477    -36    -61   -220       O  
ATOM   3860  N   VAL B 124       2.082  14.219  10.208  1.00 13.50           N  
ANISOU 3860  N   VAL B 124     1858   1556   1714    -45    -65   -213       N  
ATOM   3861  CA  VAL B 124       0.986  13.241  10.268  1.00 14.73           C  
ANISOU 3861  CA  VAL B 124     2031   1708   1857    -65    -69   -214       C  
ATOM   3862  CB  VAL B 124      -0.193  13.701   9.378  1.00 15.78           C  
ANISOU 3862  CB  VAL B 124     2169   1832   1995    -86    -97   -224       C  
ATOM   3863  CG1 VAL B 124      -1.359  12.702   9.430  1.00 17.62           C  
ANISOU 3863  CG1 VAL B 124     2415   2064   2216   -112   -103   -226       C  
ATOM   3864  CG2 VAL B 124      -0.638  15.118   9.811  1.00 18.19           C  
ANISOU 3864  CG2 VAL B 124     2427   2158   2327    -82   -117   -238       C  
ATOM   3865  C   VAL B 124       1.465  11.866   9.817  1.00 16.85           C  
ANISOU 3865  C   VAL B 124     2347   1952   2103    -65    -44   -198       C  
ATOM   3866  O   VAL B 124       1.942  11.713   8.695  1.00 13.66           O  
ANISOU 3866  O   VAL B 124     1979   1520   1690    -63    -35   -191       O  
ATOM   3867  N   ALA B 125       1.354  10.867  10.691  1.00 13.75           N  
ANISOU 3867  N   ALA B 125     1956   1566   1700    -66    -29   -192       N  
ATOM   3868  CA  ALA B 125       1.749   9.507  10.324  1.00 16.23           C  
ANISOU 3868  CA  ALA B 125     2318   1854   1995    -65     -1   -177       C  
ATOM   3869  CB  ALA B 125       2.123   8.700  11.570  1.00 18.60           C  
ANISOU 3869  CB  ALA B 125     2609   2168   2290    -52     19   -164       C  
ATOM   3870  C   ALA B 125       0.624   8.812   9.551  1.00 20.64           C  
ANISOU 3870  C   ALA B 125     2913   2391   2538    -97     -8   -184       C  
ATOM   3871  O   ALA B 125      -0.032   7.897  10.070  1.00 17.15           O  
ANISOU 3871  O   ALA B 125     2480   1949   2086   -112     -1   -184       O  
ATOM   3872  N   ALA B 126       0.388   9.256   8.320  1.00 16.07           N  
ANISOU 3872  N   ALA B 126     2356   1795   1956   -109    -23   -190       N  
ATOM   3873  CA  ALA B 126      -0.614   8.623   7.469  1.00 18.23           C  
ANISOU 3873  CA  ALA B 126     2667   2049   2211   -144    -34   -196       C  
ATOM   3874  CB  ALA B 126      -2.013   9.206   7.739  1.00 18.78           C  
ANISOU 3874  CB  ALA B 126     2698   2143   2295   -167    -72   -211       C  
ATOM   3875  C   ALA B 126      -0.251   8.797   6.011  1.00 19.49           C  
ANISOU 3875  C   ALA B 126     2870   2179   2357   -149    -35   -193       C  
ATOM   3876  O   ALA B 126      -0.071   9.919   5.547  1.00 18.78           O  
ANISOU 3876  O   ALA B 126     2764   2095   2278   -140    -53   -196       O  
ATOM   3877  N   THR B 127      -0.162   7.678   5.299  1.00 18.43           N  
ANISOU 3877  N   THR B 127     2796   2012   2196   -164    -12   -189       N  
ATOM   3878  CA  THR B 127       0.120   7.670   3.867  1.00 20.83           C  
ANISOU 3878  CA  THR B 127     3153   2283   2479   -174     -9   -188       C  
ATOM   3879  CB  THR B 127       1.190   6.637   3.546  1.00 25.55           C  
ANISOU 3879  CB  THR B 127     3803   2844   3060   -160     43   -176       C  
ATOM   3880  OG1 THR B 127       0.777   5.382   4.094  1.00 22.96           O  
ANISOU 3880  OG1 THR B 127     3494   2507   2721   -174     62   -176       O  
ATOM   3881  CG2 THR B 127       2.531   7.040   4.184  1.00 25.87           C  
ANISOU 3881  CG2 THR B 127     3812   2893   3124   -115     69   -162       C  
ATOM   3882  C   THR B 127      -1.148   7.357   3.059  1.00 23.52           C  
ANISOU 3882  C   THR B 127     3523   2617   2799   -220    -39   -199       C  
ATOM   3883  O   THR B 127      -1.216   7.606   1.858  1.00 21.81           O  
ANISOU 3883  O   THR B 127     3344   2382   2563   -236    -52   -201       O  
ATOM   3884  N   ASP B 128      -2.149   6.794   3.728  1.00 17.73           N  
ANISOU 3884  N   ASP B 128     2772   1897   2066   -243    -51   -206       N  
ATOM   3885  CA  ASP B 128      -3.434   6.523   3.101  1.00 17.73           C  
ANISOU 3885  CA  ASP B 128     2788   1898   2051   -289    -84   -216       C  
ATOM   3886  CB  ASP B 128      -4.223   5.491   3.936  1.00 17.42           C  
ANISOU 3886  CB  ASP B 128     2743   1865   2011   -312    -76   -222       C  
ATOM   3887  CG  ASP B 128      -5.595   5.176   3.360  1.00 29.11           C  
ANISOU 3887  CG  ASP B 128     4233   3348   3478   -364   -112   -233       C  
ATOM   3888  OD1 ASP B 128      -6.539   5.959   3.609  1.00 19.75           O  
ANISOU 3888  OD1 ASP B 128     2994   2196   2316   -373   -153   -237       O  
ATOM   3889  OD2 ASP B 128      -5.750   4.117   2.699  1.00 31.89           O  
ANISOU 3889  OD2 ASP B 128     4647   3671   3799   -397    -98   -237       O  
ATOM   3890  C   ASP B 128      -4.190   7.836   2.964  1.00 19.00           C  
ANISOU 3890  C   ASP B 128     2898   2089   2233   -292   -135   -220       C  
ATOM   3891  O   ASP B 128      -4.294   8.601   3.918  1.00 19.97           O  
ANISOU 3891  O   ASP B 128     2959   2240   2386   -270   -144   -221       O  
ATOM   3892  N   VAL B 129      -4.682   8.107   1.766  1.00 19.30           N  
ANISOU 3892  N   VAL B 129     2963   2118   2252   -318   -166   -221       N  
ATOM   3893  CA  VAL B 129      -5.347   9.372   1.466  1.00 18.37           C  
ANISOU 3893  CA  VAL B 129     2802   2024   2153   -318   -214   -220       C  
ATOM   3894  CB  VAL B 129      -5.780   9.430  -0.022  1.00 21.47           C  
ANISOU 3894  CB  VAL B 129     3242   2400   2514   -350   -246   -218       C  
ATOM   3895  CG1 VAL B 129      -6.777  10.558  -0.276  1.00 19.63           C  
ANISOU 3895  CG1 VAL B 129     2960   2196   2302   -356   -303   -214       C  
ATOM   3896  CG2 VAL B 129      -4.555   9.548  -0.932  1.00 27.59           C  
ANISOU 3896  CG2 VAL B 129     4074   3143   3265   -334   -219   -212       C  
ATOM   3897  C   VAL B 129      -6.564   9.604   2.367  1.00 21.06           C  
ANISOU 3897  C   VAL B 129     3078   2400   2524   -328   -242   -226       C  
ATOM   3898  O   VAL B 129      -6.762  10.705   2.872  1.00 18.06           O  
ANISOU 3898  O   VAL B 129     2642   2045   2178   -306   -260   -226       O  
ATOM   3899  N   ASP B 130      -7.368   8.564   2.567  1.00 17.25           N  
ANISOU 3899  N   ASP B 130     2605   1918   2031   -363   -243   -233       N  
ATOM   3900  CA  ASP B 130      -8.542   8.686   3.430  1.00 17.06           C  
ANISOU 3900  CA  ASP B 130     2520   1926   2036   -376   -265   -239       C  
ATOM   3901  CB  ASP B 130      -9.416   7.430   3.309  1.00 25.50           C  
ANISOU 3901  CB  ASP B 130     3615   2990   3086   -425   -267   -246       C  
ATOM   3902  CG  ASP B 130     -10.012   7.278   1.920  1.00 34.09           C  
ANISOU 3902  CG  ASP B 130     4741   4067   4144   -466   -306   -245       C  
ATOM   3903  OD1 ASP B 130     -11.084   7.863   1.672  1.00 35.39           O  
ANISOU 3903  OD1 ASP B 130     4864   4257   4326   -485   -354   -243       O  
ATOM   3904  OD2 ASP B 130      -9.396   6.594   1.074  1.00 38.06           O  
ANISOU 3904  OD2 ASP B 130     5317   4537   4608   -481   -287   -245       O  
ATOM   3905  C   ASP B 130      -8.168   8.939   4.893  1.00 19.02           C  
ANISOU 3905  C   ASP B 130     2721   2192   2313   -342   -236   -241       C  
ATOM   3906  O   ASP B 130      -8.775   9.798   5.551  1.00 19.26           O  
ANISOU 3906  O   ASP B 130     2689   2250   2377   -330   -254   -244       O  
ATOM   3907  N   VAL B 131      -7.177   8.213   5.403  1.00 16.51           N  
ANISOU 3907  N   VAL B 131     2432   1858   1982   -324   -192   -239       N  
ATOM   3908  CA  VAL B 131      -6.745   8.423   6.785  1.00 15.64           C  
ANISOU 3908  CA  VAL B 131     2282   1766   1894   -293   -166   -240       C  
ATOM   3909  CB  VAL B 131      -5.633   7.446   7.213  1.00 15.63           C  
ANISOU 3909  CB  VAL B 131     2320   1744   1875   -276   -119   -233       C  
ATOM   3910  CG1 VAL B 131      -5.129   7.776   8.656  1.00 17.07           C  
ANISOU 3910  CG1 VAL B 131     2459   1950   2077   -244    -99   -231       C  
ATOM   3911  CG2 VAL B 131      -6.137   5.982   7.118  1.00 17.83           C  
ANISOU 3911  CG2 VAL B 131     2642   2003   2129   -311   -102   -235       C  
ATOM   3912  C   VAL B 131      -6.240   9.857   6.948  1.00 16.25           C  
ANISOU 3912  C   VAL B 131     2319   1859   1996   -258   -178   -239       C  
ATOM   3913  O   VAL B 131      -6.616  10.555   7.901  1.00 15.64           O  
ANISOU 3913  O   VAL B 131     2188   1808   1947   -246   -183   -245       O  
ATOM   3914  N   PHE B 132      -5.409  10.284   6.005  1.00 15.98           N  
ANISOU 3914  N   PHE B 132     2315   1806   1951   -245   -178   -232       N  
ATOM   3915  CA  PHE B 132      -4.817  11.624   6.075  1.00 12.89           C  
ANISOU 3915  CA  PHE B 132     1893   1424   1581   -213   -185   -230       C  
ATOM   3916  CB  PHE B 132      -3.796  11.812   4.949  1.00 13.46           C  
ANISOU 3916  CB  PHE B 132     2011   1469   1635   -203   -176   -222       C  
ATOM   3917  CG  PHE B 132      -3.081  13.144   5.008  1.00 14.64           C  
ANISOU 3917  CG  PHE B 132     2133   1625   1805   -172   -178   -220       C  
ATOM   3918  CD1 PHE B 132      -3.650  14.278   4.428  1.00 16.68           C  
ANISOU 3918  CD1 PHE B 132     2371   1889   2079   -173   -212   -220       C  
ATOM   3919  CE1 PHE B 132      -3.012  15.537   4.494  1.00 15.45           C  
ANISOU 3919  CE1 PHE B 132     2191   1736   1944   -146   -211   -219       C  
ATOM   3920  CZ  PHE B 132      -1.797  15.653   5.125  1.00 17.51           C  
ANISOU 3920  CZ  PHE B 132     2447   1998   2210   -121   -179   -220       C  
ATOM   3921  CE2 PHE B 132      -1.195  14.495   5.698  1.00 16.61           C  
ANISOU 3921  CE2 PHE B 132     2350   1881   2081   -119   -148   -217       C  
ATOM   3922  CD2 PHE B 132      -1.858  13.266   5.656  1.00 16.18           C  
ANISOU 3922  CD2 PHE B 132     2320   1821   2007   -143   -147   -217       C  
ATOM   3923  C   PHE B 132      -5.886  12.722   6.017  1.00 17.79           C  
ANISOU 3923  C   PHE B 132     2465   2065   2229   -218   -224   -235       C  
ATOM   3924  O   PHE B 132      -5.914  13.622   6.870  1.00 15.06           O  
ANISOU 3924  O   PHE B 132     2071   1740   1913   -198   -224   -240       O  
ATOM   3925  N   CYS B 133      -6.778  12.634   5.036  1.00 14.84           N  
ANISOU 3925  N   CYS B 133     2105   1687   1847   -246   -257   -232       N  
ATOM   3926  CA  CYS B 133      -7.814  13.651   4.889  1.00 16.89           C  
ANISOU 3926  CA  CYS B 133     2318   1965   2134   -249   -296   -232       C  
ATOM   3927  CB  CYS B 133      -8.552  13.470   3.576  1.00 16.90           C  
ANISOU 3927  CB  CYS B 133     2347   1958   2116   -280   -335   -224       C  
ATOM   3928  SG  CYS B 133      -7.551  13.923   2.162  1.00 20.43           S  
ANISOU 3928  SG  CYS B 133     2852   2377   2535   -271   -339   -212       S  
ATOM   3929  C   CYS B 133      -8.803  13.662   6.046  1.00 18.60           C  
ANISOU 3929  C   CYS B 133     2477   2209   2381   -254   -298   -241       C  
ATOM   3930  O   CYS B 133      -9.211  14.744   6.483  1.00 17.76           O  
ANISOU 3930  O   CYS B 133     2320   2119   2309   -236   -309   -243       O  
ATOM   3931  N   ASN B 134      -9.170  12.483   6.558  1.00 17.59           N  
ANISOU 3931  N   ASN B 134     2359   2083   2241   -277   -282   -246       N  
ATOM   3932  CA  ASN B 134     -10.091  12.427   7.693  1.00 16.69           C  
ANISOU 3932  CA  ASN B 134     2193   1994   2154   -283   -278   -255       C  
ATOM   3933  CB  ASN B 134     -10.479  10.983   8.011  1.00 19.73           C  
ANISOU 3933  CB  ASN B 134     2602   2375   2519   -314   -262   -259       C  
ATOM   3934  CG  ASN B 134     -11.471  10.431   7.025  1.00 28.88           C  
ANISOU 3934  CG  ASN B 134     3776   3530   3667   -357   -294   -257       C  
ATOM   3935  OD1 ASN B 134     -12.201  11.186   6.383  1.00 25.07           O  
ANISOU 3935  OD1 ASN B 134     3266   3058   3201   -363   -334   -252       O  
ATOM   3936  ND2 ASN B 134     -11.495   9.107   6.878  1.00 30.28           N  
ANISOU 3936  ND2 ASN B 134     3999   3692   3814   -387   -279   -259       N  
ATOM   3937  C   ASN B 134      -9.474  13.107   8.910  1.00 19.92           C  
ANISOU 3937  C   ASN B 134     2570   2415   2583   -248   -250   -262       C  
ATOM   3938  O   ASN B 134     -10.150  13.833   9.629  1.00 22.09           O  
ANISOU 3938  O   ASN B 134     2792   2709   2891   -241   -254   -269       O  
ATOM   3939  N   ALA B 135      -8.169  12.924   9.100  1.00 15.69           N  
ANISOU 3939  N   ALA B 135     2066   1868   2029   -228   -223   -260       N  
ATOM   3940  CA  ALA B 135      -7.463  13.514  10.230  1.00 18.89           C  
ANISOU 3940  CA  ALA B 135     2445   2285   2447   -199   -199   -266       C  
ATOM   3941  CB  ALA B 135      -6.074  12.919  10.349  1.00 18.90           C  
ANISOU 3941  CB  ALA B 135     2485   2273   2422   -184   -170   -259       C  
ATOM   3942  C   ALA B 135      -7.376  15.030  10.117  1.00 17.51           C  
ANISOU 3942  C   ALA B 135     2237   2117   2300   -177   -213   -269       C  
ATOM   3943  O   ALA B 135      -7.614  15.743  11.082  1.00 19.97           O  
ANISOU 3943  O   ALA B 135     2508   2446   2636   -165   -205   -279       O  
ATOM   3944  N   VAL B 136      -7.023  15.526   8.935  1.00 14.58           N  
ANISOU 3944  N   VAL B 136     1888   1729   1923   -172   -231   -260       N  
ATOM   3945  CA  VAL B 136      -6.808  16.954   8.757  1.00 14.86           C  
ANISOU 3945  CA  VAL B 136     1899   1765   1983   -149   -242   -261       C  
ATOM   3946  CB  VAL B 136      -5.965  17.207   7.494  1.00 17.23           C  
ANISOU 3946  CB  VAL B 136     2241   2041   2265   -143   -249   -249       C  
ATOM   3947  CG1 VAL B 136      -5.882  18.690   7.181  1.00 18.70           C  
ANISOU 3947  CG1 VAL B 136     2405   2224   2476   -122   -262   -248       C  
ATOM   3948  CG2 VAL B 136      -4.551  16.588   7.669  1.00 15.49           C  
ANISOU 3948  CG2 VAL B 136     2055   1809   2019   -132   -216   -247       C  
ATOM   3949  C   VAL B 136      -8.133  17.731   8.705  1.00 12.67           C  
ANISOU 3949  C   VAL B 136     1577   1499   1740   -153   -269   -262       C  
ATOM   3950  O   VAL B 136      -8.225  18.843   9.217  1.00 13.93           O  
ANISOU 3950  O   VAL B 136     1698   1665   1928   -134   -265   -269       O  
ATOM   3951  N   ARG B 137      -9.173  17.136   8.125  1.00 14.28           N  
ANISOU 3951  N   ARG B 137     1781   1705   1940   -179   -294   -256       N  
ATOM   3952  CA  ARG B 137     -10.441  17.846   7.961  1.00 16.32           C  
ANISOU 3952  CA  ARG B 137     1994   1976   2234   -182   -323   -253       C  
ATOM   3953  CB  ARG B 137     -11.465  16.947   7.260  1.00 20.19           C  
ANISOU 3953  CB  ARG B 137     2490   2468   2711   -217   -353   -244       C  
ATOM   3954  CG  ARG B 137     -12.855  17.529   7.233  1.00 26.48           C  
ANISOU 3954  CG  ARG B 137     3230   3283   3548   -222   -383   -239       C  
ATOM   3955  CD  ARG B 137     -13.817  16.612   6.486  1.00 30.05           C  
ANISOU 3955  CD  ARG B 137     3690   3741   3987   -262   -416   -230       C  
ATOM   3956  NE  ARG B 137     -14.171  15.418   7.250  1.00 42.56           N  
ANISOU 3956  NE  ARG B 137     5275   5334   5562   -289   -395   -242       N  
ATOM   3957  CZ  ARG B 137     -13.712  14.198   6.988  1.00 55.23           C  
ANISOU 3957  CZ  ARG B 137     6935   6926   7125   -314   -383   -245       C  
ATOM   3958  NH1 ARG B 137     -12.878  14.004   5.972  1.00 57.99           N  
ANISOU 3958  NH1 ARG B 137     7342   7254   7438   -316   -390   -238       N  
ATOM   3959  NH2 ARG B 137     -14.088  13.169   7.739  1.00 58.77           N  
ANISOU 3959  NH2 ARG B 137     7381   7380   7568   -336   -361   -255       N  
ATOM   3960  C   ARG B 137     -11.006  18.332   9.298  1.00 14.96           C  
ANISOU 3960  C   ARG B 137     1766   1822   2097   -171   -303   -266       C  
ATOM   3961  O   ARG B 137     -11.493  19.467   9.414  1.00 17.43           O  
ANISOU 3961  O   ARG B 137     2038   2139   2446   -153   -311   -266       O  
ATOM   3962  N   VAL B 138     -10.911  17.485  10.317  1.00 16.40           N  
ANISOU 3962  N   VAL B 138     1949   2013   2268   -180   -274   -278       N  
ATOM   3963  CA  VAL B 138     -11.529  17.806  11.599  1.00 15.62           C  
ANISOU 3963  CA  VAL B 138     1804   1932   2198   -175   -253   -292       C  
ATOM   3964  CB  VAL B 138     -11.836  16.532  12.409  1.00 15.39           C  
ANISOU 3964  CB  VAL B 138     1781   1914   2153   -198   -232   -299       C  
ATOM   3965  CG1 VAL B 138     -12.885  15.668  11.676  1.00 17.66           C  
ANISOU 3965  CG1 VAL B 138     2070   2203   2438   -232   -258   -290       C  
ATOM   3966  CG2 VAL B 138     -10.570  15.725  12.665  1.00 19.33           C  
ANISOU 3966  CG2 VAL B 138     2328   2404   2611   -196   -208   -299       C  
ATOM   3967  C   VAL B 138     -10.676  18.768  12.430  1.00 20.45           C  
ANISOU 3967  C   VAL B 138     2406   2544   2818   -147   -226   -304       C  
ATOM   3968  O   VAL B 138     -11.062  19.162  13.524  1.00 15.75           O  
ANISOU 3968  O   VAL B 138     1777   1962   2244   -141   -204   -318       O  
ATOM   3969  N   LEU B 139      -9.535  19.193  11.899  1.00 15.47           N  
ANISOU 3969  N   LEU B 139     1806   1901   2173   -131   -227   -300       N  
ATOM   3970  CA  LEU B 139      -8.745  20.230  12.578  1.00 15.00           C  
ANISOU 3970  CA  LEU B 139     1736   1841   2124   -108   -206   -311       C  
ATOM   3971  CB  LEU B 139      -7.237  20.047  12.279  1.00 12.18           C  
ANISOU 3971  CB  LEU B 139     1420   1473   1736   -100   -197   -307       C  
ATOM   3972  CG  LEU B 139      -6.674  18.683  12.662  1.00 20.10           C  
ANISOU 3972  CG  LEU B 139     2454   2481   2704   -112   -182   -304       C  
ATOM   3973  CD1 LEU B 139      -5.158  18.684  12.446  1.00 20.69           C  
ANISOU 3973  CD1 LEU B 139     2558   2546   2756    -98   -170   -299       C  
ATOM   3974  CD2 LEU B 139      -7.046  18.346  14.109  1.00 26.78           C  
ANISOU 3974  CD2 LEU B 139     3277   3348   3552   -118   -159   -318       C  
ATOM   3975  C   LEU B 139      -9.131  21.658  12.218  1.00 14.75           C  
ANISOU 3975  C   LEU B 139     1675   1801   2128    -90   -217   -311       C  
ATOM   3976  O   LEU B 139      -8.569  22.620  12.793  1.00 16.28           O  
ANISOU 3976  O   LEU B 139     1860   1993   2334    -73   -198   -324       O  
ATOM   3977  N   GLU B 140     -10.079  21.819  11.294  1.00 15.53           N  
ANISOU 3977  N   GLU B 140     1760   1895   2244    -94   -248   -297       N  
ATOM   3978  CA  GLU B 140     -10.520  23.166  10.899  1.00 18.49           C  
ANISOU 3978  CA  GLU B 140     2108   2260   2657    -73   -260   -292       C  
ATOM   3979  CB  GLU B 140     -11.779  23.102  10.014  1.00 22.15           C  
ANISOU 3979  CB  GLU B 140     2549   2726   3140    -81   -298   -273       C  
ATOM   3980  CG  GLU B 140     -12.288  24.509   9.679  1.00 22.74           C  
ANISOU 3980  CG  GLU B 140     2591   2790   3258    -55   -309   -264       C  
ATOM   3981  CD  GLU B 140     -13.204  24.588   8.465  1.00 27.53           C  
ANISOU 3981  CD  GLU B 140     3187   3397   3878    -59   -356   -237       C  
ATOM   3982  OE1 GLU B 140     -13.208  23.659   7.635  1.00 23.98           O  
ANISOU 3982  OE1 GLU B 140     2767   2949   3394    -83   -384   -225       O  
ATOM   3983  OE2 GLU B 140     -13.915  25.618   8.337  1.00 27.41           O  
ANISOU 3983  OE2 GLU B 140     3133   3377   3905    -38   -365   -227       O  
ATOM   3984  C   GLU B 140     -10.784  24.141  12.070  1.00 16.36           C  
ANISOU 3984  C   GLU B 140     1799   1995   2422    -56   -230   -311       C  
ATOM   3985  O   GLU B 140     -10.368  25.306  11.984  1.00 18.96           O  
ANISOU 3985  O   GLU B 140     2125   2309   2769    -36   -222   -314       O  
ATOM   3986  N   PRO B 141     -11.434  23.696  13.175  1.00 15.23           N  
ANISOU 3986  N   PRO B 141     1630   1869   2289    -66   -208   -325       N  
ATOM   3987  CA  PRO B 141     -11.719  24.690  14.227  1.00 17.12           C  
ANISOU 3987  CA  PRO B 141     1836   2109   2560    -51   -176   -345       C  
ATOM   3988  CB  PRO B 141     -12.387  23.859  15.332  1.00 18.04           C  
ANISOU 3988  CB  PRO B 141     1934   2245   2675    -69   -154   -358       C  
ATOM   3989  CG  PRO B 141     -12.933  22.653  14.645  1.00 16.59           C  
ANISOU 3989  CG  PRO B 141     1757   2070   2477    -91   -182   -341       C  
ATOM   3990  CD  PRO B 141     -11.971  22.362  13.526  1.00 14.54           C  
ANISOU 3990  CD  PRO B 141     1542   1798   2183    -92   -208   -326       C  
ATOM   3991  C   PRO B 141     -10.467  25.377  14.795  1.00 17.27           C  
ANISOU 3991  C   PRO B 141     1876   2120   2564    -41   -150   -362       C  
ATOM   3992  O   PRO B 141     -10.562  26.487  15.294  1.00 18.44           O  
ANISOU 3992  O   PRO B 141     2005   2260   2741    -26   -129   -375       O  
ATOM   3993  N   THR B 142      -9.321  24.703  14.704  1.00 14.71           N  
ANISOU 3993  N   THR B 142     1591   1799   2199    -49   -152   -361       N  
ATOM   3994  CA  THR B 142      -8.062  25.208  15.244  1.00 14.52           C  
ANISOU 3994  CA  THR B 142     1586   1773   2158    -44   -131   -375       C  
ATOM   3995  CB  THR B 142      -7.015  24.071  15.315  1.00 15.93           C  
ANISOU 3995  CB  THR B 142     1800   1962   2292    -56   -132   -370       C  
ATOM   3996  OG1 THR B 142      -7.543  22.947  16.044  1.00 17.56           O  
ANISOU 3996  OG1 THR B 142     2003   2186   2483    -72   -123   -372       O  
ATOM   3997  CG2 THR B 142      -5.709  24.557  15.981  1.00 17.78           C  
ANISOU 3997  CG2 THR B 142     2047   2200   2510    -52   -112   -384       C  
ATOM   3998  C   THR B 142      -7.437  26.346  14.419  1.00 14.38           C  
ANISOU 3998  C   THR B 142     1578   1733   2153    -27   -139   -370       C  
ATOM   3999  O   THR B 142      -6.798  27.245  14.969  1.00 14.89           O  
ANISOU 3999  O   THR B 142     1643   1793   2223    -20   -118   -387       O  
ATOM   4000  N   PHE B 143      -7.618  26.287  13.104  1.00 12.66           N  
ANISOU 4000  N   PHE B 143     1372   1502   1937    -22   -169   -347       N  
ATOM   4001  CA  PHE B 143      -6.725  27.013  12.183  1.00 11.92           C  
ANISOU 4001  CA  PHE B 143     1303   1387   1841    -11   -177   -338       C  
ATOM   4002  CB  PHE B 143      -5.977  26.017  11.288  1.00 13.33           C  
ANISOU 4002  CB  PHE B 143     1521   1563   1981    -20   -193   -321       C  
ATOM   4003  CG  PHE B 143      -5.031  25.129  12.044  1.00 12.95           C  
ANISOU 4003  CG  PHE B 143     1490   1530   1901    -31   -175   -331       C  
ATOM   4004  CD1 PHE B 143      -3.917  25.691  12.650  1.00 12.84           C  
ANISOU 4004  CD1 PHE B 143     1479   1517   1881    -26   -153   -344       C  
ATOM   4005  CE1 PHE B 143      -3.028  24.910  13.379  1.00 16.52           C  
ANISOU 4005  CE1 PHE B 143     1957   2001   2320    -34   -139   -349       C  
ATOM   4006  CZ  PHE B 143      -3.254  23.558  13.528  1.00 12.87           C  
ANISOU 4006  CZ  PHE B 143     1505   1551   1835    -45   -143   -341       C  
ATOM   4007  CE2 PHE B 143      -4.368  22.951  12.929  1.00 12.06           C  
ANISOU 4007  CE2 PHE B 143     1402   1445   1736    -52   -161   -330       C  
ATOM   4008  CD2 PHE B 143      -5.275  23.762  12.193  1.00 12.95           C  
ANISOU 4008  CD2 PHE B 143     1499   1543   1876    -46   -179   -325       C  
ATOM   4009  C   PHE B 143      -7.440  28.005  11.297  1.00 13.52           C  
ANISOU 4009  C   PHE B 143     1492   1569   2076      6   -194   -324       C  
ATOM   4010  O   PHE B 143      -8.599  27.798  10.937  1.00 16.42           O  
ANISOU 4010  O   PHE B 143     1837   1940   2461      6   -215   -311       O  
ATOM   4011  N   GLY B 144      -6.732  29.068  10.909  1.00 14.44           N  
ANISOU 4011  N   GLY B 144     1621   1664   2201     20   -187   -324       N  
ATOM   4012  CA  GLY B 144      -7.240  29.983   9.897  1.00 15.09           C  
ANISOU 4012  CA  GLY B 144     1700   1724   2310     37   -206   -305       C  
ATOM   4013  C   GLY B 144      -6.925  29.566   8.471  1.00 12.55           C  
ANISOU 4013  C   GLY B 144     1413   1391   1963     34   -238   -279       C  
ATOM   4014  O   GLY B 144      -7.572  30.030   7.524  1.00 15.04           O  
ANISOU 4014  O   GLY B 144     1726   1693   2294     44   -264   -257       O  
ATOM   4015  N   GLY B 145      -5.941  28.682   8.311  1.00 12.27           N  
ANISOU 4015  N   GLY B 145     1412   1361   1888     19   -235   -280       N  
ATOM   4016  CA  GLY B 145      -5.614  28.168   6.994  1.00 12.87           C  
ANISOU 4016  CA  GLY B 145     1529   1427   1936     13   -259   -258       C  
ATOM   4017  C   GLY B 145      -4.698  26.957   7.101  1.00 11.07           C  
ANISOU 4017  C   GLY B 145     1331   1208   1668     -4   -249   -262       C  
ATOM   4018  O   GLY B 145      -4.104  26.740   8.149  1.00 12.04           O  
ANISOU 4018  O   GLY B 145     1444   1344   1786     -6   -223   -281       O  
ATOM   4019  N   ILE B 146      -4.585  26.212   6.011  1.00 11.02           N  
ANISOU 4019  N   ILE B 146     1361   1193   1632    -14   -268   -245       N  
ATOM   4020  CA  ILE B 146      -3.770  24.983   5.950  1.00  9.76           C  
ANISOU 4020  CA  ILE B 146     1235   1038   1435    -28   -256   -245       C  
ATOM   4021  CB  ILE B 146      -4.642  23.710   5.753  1.00 14.01           C  
ANISOU 4021  CB  ILE B 146     1780   1588   1955    -49   -276   -238       C  
ATOM   4022  CG1 ILE B 146      -5.771  23.600   6.788  1.00 19.87           C  
ANISOU 4022  CG1 ILE B 146     2476   2353   2722    -53   -279   -249       C  
ATOM   4023  CD1 ILE B 146      -5.315  23.444   8.194  1.00 16.20           C  
ANISOU 4023  CD1 ILE B 146     1990   1904   2261    -50   -248   -269       C  
ATOM   4024  CG2 ILE B 146      -3.757  22.451   5.758  1.00 16.00           C  
ANISOU 4024  CG2 ILE B 146     2069   1839   2170    -60   -257   -239       C  
ATOM   4025  C   ILE B 146      -2.790  25.047   4.781  1.00 14.66           C  
ANISOU 4025  C   ILE B 146     1903   1635   2033    -26   -254   -232       C  
ATOM   4026  O   ILE B 146      -3.201  25.190   3.622  1.00 12.60           O  
ANISOU 4026  O   ILE B 146     1666   1358   1763    -29   -279   -214       O  
ATOM   4027  N   ASN B 147      -1.500  24.969   5.075  1.00 12.25           N  
ANISOU 4027  N   ASN B 147     1612   1327   1718    -22   -225   -239       N  
ATOM   4028  CA  ASN B 147      -0.485  24.837   4.037  1.00 10.99           C  
ANISOU 4028  CA  ASN B 147     1498   1145   1535    -22   -215   -227       C  
ATOM   4029  CB  ASN B 147       0.680  25.808   4.303  1.00 13.20           C  
ANISOU 4029  CB  ASN B 147     1770   1415   1829     -8   -188   -234       C  
ATOM   4030  CG  ASN B 147       1.753  25.725   3.257  1.00 18.12           C  
ANISOU 4030  CG  ASN B 147     2438   2015   2432     -8   -173   -222       C  
ATOM   4031  OD1 ASN B 147       1.697  26.423   2.254  1.00 20.55           O  
ANISOU 4031  OD1 ASN B 147     2769   2300   2740     -4   -182   -211       O  
ATOM   4032  ND2 ASN B 147       2.739  24.859   3.475  1.00 16.38           N  
ANISOU 4032  ND2 ASN B 147     2230   1798   2196     -9   -149   -223       N  
ATOM   4033  C   ASN B 147       0.018  23.401   4.019  1.00 13.51           C  
ANISOU 4033  C   ASN B 147     1844   1466   1822    -33   -202   -224       C  
ATOM   4034  O   ASN B 147       0.750  22.996   4.922  1.00 13.08           O  
ANISOU 4034  O   ASN B 147     1777   1425   1768    -29   -178   -233       O  
ATOM   4035  N   LEU B 148      -0.416  22.623   3.032  1.00 11.74           N  
ANISOU 4035  N   LEU B 148     1658   1230   1572    -47   -218   -211       N  
ATOM   4036  CA  LEU B 148       0.089  21.273   2.844  1.00 14.29           C  
ANISOU 4036  CA  LEU B 148     2017   1549   1864    -57   -201   -208       C  
ATOM   4037  CB  LEU B 148      -0.785  20.498   1.856  1.00 12.83           C  
ANISOU 4037  CB  LEU B 148     1869   1354   1652    -79   -226   -198       C  
ATOM   4038  CG  LEU B 148      -2.246  20.362   2.317  1.00 12.55           C  
ANISOU 4038  CG  LEU B 148     1800   1340   1629    -92   -258   -202       C  
ATOM   4039  CD1 LEU B 148      -3.036  19.749   1.160  1.00 14.22           C  
ANISOU 4039  CD1 LEU B 148     2051   1541   1812   -118   -288   -190       C  
ATOM   4040  CD2 LEU B 148      -2.366  19.498   3.580  1.00 17.74           C  
ANISOU 4040  CD2 LEU B 148     2431   2019   2291    -96   -241   -214       C  
ATOM   4041  C   LEU B 148       1.498  21.382   2.319  1.00 14.57           C  
ANISOU 4041  C   LEU B 148     2083   1564   1890    -47   -170   -202       C  
ATOM   4042  O   LEU B 148       1.791  22.286   1.540  1.00 12.86           O  
ANISOU 4042  O   LEU B 148     1880   1328   1676    -41   -172   -196       O  
ATOM   4043  N   GLU B 149       2.379  20.485   2.749  1.00 12.27           N  
ANISOU 4043  N   GLU B 149     1800   1273   1587    -43   -140   -203       N  
ATOM   4044  CA  GLU B 149       3.767  20.584   2.353  1.00 14.29           C  
ANISOU 4044  CA  GLU B 149     2077   1513   1841    -31   -107   -197       C  
ATOM   4045  CB  GLU B 149       4.541  21.463   3.344  1.00 14.45           C  
ANISOU 4045  CB  GLU B 149     2050   1551   1890    -16    -94   -206       C  
ATOM   4046  CG  GLU B 149       5.964  21.746   2.916  1.00 15.53           C  
ANISOU 4046  CG  GLU B 149     2200   1671   2029     -4    -62   -199       C  
ATOM   4047  CD  GLU B 149       6.045  22.840   1.863  1.00 22.94           C  
ANISOU 4047  CD  GLU B 149     3159   2585   2971     -4    -65   -195       C  
ATOM   4048  OE1 GLU B 149       5.085  23.645   1.788  1.00 23.16           O  
ANISOU 4048  OE1 GLU B 149     3175   2615   3009     -8    -94   -199       O  
ATOM   4049  OE2 GLU B 149       7.059  22.886   1.119  1.00 23.54           O  
ANISOU 4049  OE2 GLU B 149     3263   2640   3042      0    -38   -186       O  
ATOM   4050  C   GLU B 149       4.395  19.197   2.272  1.00 14.29           C  
ANISOU 4050  C   GLU B 149     2108   1504   1818    -32    -79   -189       C  
ATOM   4051  O   GLU B 149       4.123  18.343   3.114  1.00 15.31           O  
ANISOU 4051  O   GLU B 149     2223   1650   1945    -34    -77   -193       O  
ATOM   4052  N   ASP B 150       5.212  18.978   1.242  1.00 11.52           N  
ANISOU 4052  N   ASP B 150     1803   1124   1451    -30    -55   -179       N  
ATOM   4053  CA  ASP B 150       6.068  17.798   1.166  1.00 15.35           C  
ANISOU 4053  CA  ASP B 150     2316   1596   1921    -24    -17   -171       C  
ATOM   4054  CB  ASP B 150       7.159  17.933   2.231  1.00 13.43           C  
ANISOU 4054  CB  ASP B 150     2028   1373   1704     -3      6   -170       C  
ATOM   4055  CG  ASP B 150       8.167  19.012   1.853  1.00 18.85           C  
ANISOU 4055  CG  ASP B 150     2704   2050   2407      9     22   -168       C  
ATOM   4056  OD1 ASP B 150       7.847  19.770   0.921  1.00 18.42           O  
ANISOU 4056  OD1 ASP B 150     2674   1978   2348      1     11   -169       O  
ATOM   4057  OD2 ASP B 150       9.257  19.121   2.459  1.00 19.26           O  
ANISOU 4057  OD2 ASP B 150     2726   2114   2479     24     45   -165       O  
ATOM   4058  C   ASP B 150       5.323  16.453   1.265  1.00 16.23           C  
ANISOU 4058  C   ASP B 150     2451   1705   2009    -39    -21   -171       C  
ATOM   4059  O   ASP B 150       5.718  15.546   2.010  1.00 16.05           O  
ANISOU 4059  O   ASP B 150     2420   1690   1987    -31      0   -168       O  
ATOM   4060  N   ILE B 151       4.259  16.352   0.467  1.00 13.84           N  
ANISOU 4060  N   ILE B 151     2181   1393   1685    -63    -49   -173       N  
ATOM   4061  CA  ILE B 151       3.441  15.156   0.294  1.00 17.47           C  
ANISOU 4061  CA  ILE B 151     2673   1847   2119    -86    -56   -174       C  
ATOM   4062  CB  ILE B 151       1.928  15.448   0.538  1.00 15.98           C  
ANISOU 4062  CB  ILE B 151     2457   1680   1933   -106   -105   -182       C  
ATOM   4063  CG1 ILE B 151       1.701  15.958   1.969  1.00 18.76           C  
ANISOU 4063  CG1 ILE B 151     2740   2067   2320    -92   -114   -190       C  
ATOM   4064  CD1 ILE B 151       0.329  16.555   2.163  1.00 18.34           C  
ANISOU 4064  CD1 ILE B 151     2654   2035   2280   -105   -158   -197       C  
ATOM   4065  CG2 ILE B 151       1.032  14.213   0.189  1.00 14.84           C  
ANISOU 4065  CG2 ILE B 151     2351   1527   1759   -137   -115   -184       C  
ATOM   4066  C   ILE B 151       3.694  14.714  -1.145  1.00 15.65           C  
ANISOU 4066  C   ILE B 151     2515   1577   1853   -100    -41   -168       C  
ATOM   4067  O   ILE B 151       3.613  15.529  -2.077  1.00 16.89           O  
ANISOU 4067  O   ILE B 151     2692   1722   2002   -106    -56   -165       O  
ATOM   4068  N   LYS B 152       4.030  13.445  -1.338  1.00 13.24           N  
ANISOU 4068  N   LYS B 152     2253   1251   1526   -106     -8   -165       N  
ATOM   4069  CA  LYS B 152       4.393  13.002  -2.675  1.00 19.20           C  
ANISOU 4069  CA  LYS B 152     3083   1966   2247   -119     15   -161       C  
ATOM   4070  CB  LYS B 152       5.046  11.619  -2.606  1.00 17.47           C  
ANISOU 4070  CB  LYS B 152     2902   1722   2014   -114     65   -157       C  
ATOM   4071  CG  LYS B 152       4.099  10.491  -2.231  1.00 17.07           C  
ANISOU 4071  CG  LYS B 152     2865   1675   1947   -139     54   -164       C  
ATOM   4072  CD  LYS B 152       4.814   9.142  -2.244  1.00 25.25           C  
ANISOU 4072  CD  LYS B 152     3946   2679   2970   -132    110   -158       C  
ATOM   4073  CE  LYS B 152       5.025   8.636  -3.655  1.00 29.04           C  
ANISOU 4073  CE  LYS B 152     4512   3113   3410   -153    137   -160       C  
ATOM   4074  NZ  LYS B 152       3.752   8.112  -4.245  1.00 34.67           N  
ANISOU 4074  NZ  LYS B 152     5268   3821   4086   -201    103   -172       N  
ATOM   4075  C   LYS B 152       3.193  12.973  -3.637  1.00 20.57           C  
ANISOU 4075  C   LYS B 152     3296   2132   2386   -157    -27   -165       C  
ATOM   4076  O   LYS B 152       2.030  12.868  -3.215  1.00 17.74           O  
ANISOU 4076  O   LYS B 152     2913   1798   2030   -176    -67   -171       O  
ATOM   4077  N   ALA B 153       3.498  13.077  -4.926  1.00 18.22           N  
ANISOU 4077  N   ALA B 153     3061   1804   2059   -169    -16   -161       N  
ATOM   4078  CA  ALA B 153       2.535  12.801  -5.994  1.00 22.37           C  
ANISOU 4078  CA  ALA B 153     3641   2316   2541   -209    -49   -164       C  
ATOM   4079  CB  ALA B 153       2.974  13.503  -7.273  1.00 28.00           C  
ANISOU 4079  CB  ALA B 153     4404   3004   3231   -213    -45   -156       C  
ATOM   4080  C   ALA B 153       2.395  11.282  -6.224  1.00 23.72           C  
ANISOU 4080  C   ALA B 153     3870   2464   2678   -235    -23   -170       C  
ATOM   4081  O   ALA B 153       3.334  10.535  -6.008  1.00 23.07           O  
ANISOU 4081  O   ALA B 153     3807   2359   2599   -218     32   -169       O  
ATOM   4082  N   PRO B 154       1.220  10.816  -6.668  1.00 23.22           N  
ANISOU 4082  N   PRO B 154     3834   2404   2585   -277    -62   -177       N  
ATOM   4083  CA  PRO B 154      -0.002  11.541  -7.008  1.00 23.45           C  
ANISOU 4083  CA  PRO B 154     3842   2458   2608   -302   -131   -176       C  
ATOM   4084  CB  PRO B 154      -0.709  10.582  -7.991  1.00 24.37           C  
ANISOU 4084  CB  PRO B 154     4033   2555   2671   -353   -145   -182       C  
ATOM   4085  CG  PRO B 154      -0.322   9.243  -7.492  1.00 28.73           C  
ANISOU 4085  CG  PRO B 154     4611   3088   3219   -356    -94   -191       C  
ATOM   4086  CD  PRO B 154       1.109   9.383  -7.012  1.00 28.15           C  
ANISOU 4086  CD  PRO B 154     4523   2999   3172   -307    -34   -185       C  
ATOM   4087  C   PRO B 154      -0.896  11.813  -5.805  1.00 19.68           C  
ANISOU 4087  C   PRO B 154     3283   2024   2171   -295   -167   -179       C  
ATOM   4088  O   PRO B 154      -1.861  12.558  -5.960  1.00 20.19           O  
ANISOU 4088  O   PRO B 154     3316   2113   2242   -307   -222   -175       O  
ATOM   4089  N   GLU B 155      -0.611  11.207  -4.650  1.00 18.97           N  
ANISOU 4089  N   GLU B 155     3159   1943   2105   -278   -138   -184       N  
ATOM   4090  CA  GLU B 155      -1.430  11.423  -3.447  1.00 19.08           C  
ANISOU 4090  CA  GLU B 155     3099   1997   2156   -273   -167   -188       C  
ATOM   4091  CB  GLU B 155      -0.789  10.759  -2.228  1.00 22.07           C  
ANISOU 4091  CB  GLU B 155     3451   2379   2556   -248   -123   -191       C  
ATOM   4092  CG  GLU B 155      -0.868   9.242  -2.257  1.00 25.14           C  
ANISOU 4092  CG  GLU B 155     3889   2745   2917   -271    -95   -196       C  
ATOM   4093  CD  GLU B 155       0.407   8.583  -2.762  1.00 36.28           C  
ANISOU 4093  CD  GLU B 155     5360   4116   4310   -257    -35   -191       C  
ATOM   4094  OE1 GLU B 155       1.122   9.197  -3.576  1.00 25.90           O  
ANISOU 4094  OE1 GLU B 155     4070   2784   2988   -245    -25   -185       O  
ATOM   4095  OE2 GLU B 155       0.694   7.445  -2.342  1.00 40.20           O  
ANISOU 4095  OE2 GLU B 155     5878   4596   4801   -256      3   -192       O  
ATOM   4096  C   GLU B 155      -1.684  12.891  -3.126  1.00 18.06           C  
ANISOU 4096  C   GLU B 155     2905   1894   2061   -251   -201   -183       C  
ATOM   4097  O   GLU B 155      -2.784  13.268  -2.718  1.00 17.58           O  
ANISOU 4097  O   GLU B 155     2797   1862   2019   -261   -243   -185       O  
ATOM   4098  N   CYS B 156      -0.672  13.731  -3.307  1.00 17.85           N  
ANISOU 4098  N   CYS B 156     2876   1858   2047   -221   -180   -177       N  
ATOM   4099  CA  CYS B 156      -0.848  15.145  -2.984  1.00 16.75           C  
ANISOU 4099  CA  CYS B 156     2680   1740   1942   -199   -207   -173       C  
ATOM   4100  CB  CYS B 156       0.474  15.897  -3.171  1.00 16.03           C  
ANISOU 4100  CB  CYS B 156     2595   1633   1862   -168   -173   -167       C  
ATOM   4101  SG  CYS B 156       1.122  15.917  -4.866  1.00 21.00           S  
ANISOU 4101  SG  CYS B 156     3310   2221   2447   -180   -157   -158       S  
ATOM   4102  C   CYS B 156      -1.957  15.798  -3.821  1.00 16.59           C  
ANISOU 4102  C   CYS B 156     2663   1727   1912   -220   -262   -166       C  
ATOM   4103  O   CYS B 156      -2.647  16.706  -3.343  1.00 17.18           O  
ANISOU 4103  O   CYS B 156     2681   1827   2019   -210   -295   -164       O  
ATOM   4104  N   PHE B 157      -2.157  15.327  -5.047  1.00 18.06           N  
ANISOU 4104  N   PHE B 157     2915   1892   2054   -250   -274   -161       N  
ATOM   4105  CA  PHE B 157      -3.210  15.894  -5.881  1.00 20.14           C  
ANISOU 4105  CA  PHE B 157     3183   2165   2305   -272   -331   -151       C  
ATOM   4106  CB  PHE B 157      -3.113  15.412  -7.326  1.00 22.18           C  
ANISOU 4106  CB  PHE B 157     3527   2393   2506   -304   -335   -145       C  
ATOM   4107  CG  PHE B 157      -1.806  15.729  -7.985  1.00 24.84           C  
ANISOU 4107  CG  PHE B 157     3914   2698   2828   -286   -291   -141       C  
ATOM   4108  CD1 PHE B 157      -1.273  17.003  -7.920  1.00 28.50           C  
ANISOU 4108  CD1 PHE B 157     4347   3161   3319   -252   -287   -132       C  
ATOM   4109  CE1 PHE B 157      -0.064  17.297  -8.535  1.00 24.16           C  
ANISOU 4109  CE1 PHE B 157     3841   2581   2757   -237   -245   -128       C  
ATOM   4110  CZ  PHE B 157       0.634  16.312  -9.211  1.00 25.54           C  
ANISOU 4110  CZ  PHE B 157     4089   2723   2892   -252   -202   -133       C  
ATOM   4111  CE2 PHE B 157       0.108  15.034  -9.292  1.00 24.96           C  
ANISOU 4111  CE2 PHE B 157     4049   2645   2788   -285   -204   -142       C  
ATOM   4112  CD2 PHE B 157      -1.105  14.744  -8.672  1.00 22.38           C  
ANISOU 4112  CD2 PHE B 157     3679   2351   2474   -302   -250   -146       C  
ATOM   4113  C   PHE B 157      -4.573  15.532  -5.314  1.00 19.04           C  
ANISOU 4113  C   PHE B 157     2998   2056   2179   -294   -373   -155       C  
ATOM   4114  O   PHE B 157      -5.433  16.402  -5.192  1.00 19.36           O  
ANISOU 4114  O   PHE B 157     2989   2120   2245   -289   -416   -146       O  
ATOM   4115  N   GLU B 158      -4.760  14.253  -4.975  1.00 20.05           N  
ANISOU 4115  N   GLU B 158     3144   2182   2291   -318   -356   -167       N  
ATOM   4116  CA  GLU B 158      -6.034  13.794  -4.414  1.00 19.51           C  
ANISOU 4116  CA  GLU B 158     3036   2143   2236   -343   -390   -172       C  
ATOM   4117  CB  GLU B 158      -6.021  12.267  -4.246  1.00 24.45           C  
ANISOU 4117  CB  GLU B 158     3702   2755   2834   -372   -362   -185       C  
ATOM   4118  CG  GLU B 158      -7.406  11.663  -4.020  1.00 38.27           C  
ANISOU 4118  CG  GLU B 158     5427   4528   4585   -412   -400   -190       C  
ATOM   4119  CD  GLU B 158      -7.399  10.137  -3.966  1.00 54.56           C  
ANISOU 4119  CD  GLU B 158     7540   6573   6618   -445   -371   -203       C  
ATOM   4120  OE1 GLU B 158      -6.330   9.528  -4.193  1.00 50.03           O  
ANISOU 4120  OE1 GLU B 158     7023   5966   6020   -437   -321   -207       O  
ATOM   4121  OE2 GLU B 158      -8.473   9.547  -3.704  1.00 59.90           O  
ANISOU 4121  OE2 GLU B 158     8197   7267   7295   -480   -396   -210       O  
ATOM   4122  C   GLU B 158      -6.319  14.480  -3.089  1.00 20.46           C  
ANISOU 4122  C   GLU B 158     3070   2292   2411   -312   -391   -175       C  
ATOM   4123  O   GLU B 158      -7.439  14.934  -2.844  1.00 19.51           O  
ANISOU 4123  O   GLU B 158     2898   2198   2315   -319   -433   -171       O  
ATOM   4124  N   ILE B 159      -5.297  14.579  -2.242  1.00 16.30           N  
ANISOU 4124  N   ILE B 159     2528   1761   1904   -278   -345   -181       N  
ATOM   4125  CA  ILE B 159      -5.451  15.161  -0.920  1.00 12.65           C  
ANISOU 4125  CA  ILE B 159     1993   1325   1488   -251   -340   -187       C  
ATOM   4126  CB  ILE B 159      -4.159  14.961  -0.093  1.00 13.40           C  
ANISOU 4126  CB  ILE B 159     2087   1412   1592   -221   -286   -193       C  
ATOM   4127  CG1 ILE B 159      -4.002  13.489   0.301  1.00 13.85           C  
ANISOU 4127  CG1 ILE B 159     2173   1461   1629   -237   -256   -200       C  
ATOM   4128  CD1 ILE B 159      -2.565  13.169   0.802  1.00 13.65           C  
ANISOU 4128  CD1 ILE B 159     2161   1421   1603   -209   -203   -200       C  
ATOM   4129  CG2 ILE B 159      -4.141  15.874   1.142  1.00 14.85           C  
ANISOU 4129  CG2 ILE B 159     2202   1621   1821   -192   -282   -198       C  
ATOM   4130  C   ILE B 159      -5.810  16.653  -1.010  1.00 15.46           C  
ANISOU 4130  C   ILE B 159     2304   1693   1876   -230   -371   -178       C  
ATOM   4131  O   ILE B 159      -6.755  17.093  -0.360  1.00 16.73           O  
ANISOU 4131  O   ILE B 159     2407   1880   2070   -227   -394   -179       O  
ATOM   4132  N   GLU B 160      -5.080  17.425  -1.817  1.00 16.26           N  
ANISOU 4132  N   GLU B 160     2434   1776   1968   -215   -367   -168       N  
ATOM   4133  CA  GLU B 160      -5.392  18.844  -1.892  1.00 16.47           C  
ANISOU 4133  CA  GLU B 160     2421   1810   2026   -193   -392   -159       C  
ATOM   4134  CB  GLU B 160      -4.348  19.619  -2.710  1.00 16.91           C  
ANISOU 4134  CB  GLU B 160     2516   1840   2071   -175   -377   -150       C  
ATOM   4135  CG  GLU B 160      -4.468  21.142  -2.449  1.00 16.37           C  
ANISOU 4135  CG  GLU B 160     2400   1778   2042   -146   -389   -144       C  
ATOM   4136  CD  GLU B 160      -3.830  22.016  -3.530  1.00 21.68           C  
ANISOU 4136  CD  GLU B 160     3111   2424   2701   -135   -388   -129       C  
ATOM   4137  OE1 GLU B 160      -3.795  21.588  -4.704  1.00 22.39           O  
ANISOU 4137  OE1 GLU B 160     3261   2497   2750   -156   -401   -118       O  
ATOM   4138  OE2 GLU B 160      -3.376  23.146  -3.207  1.00 16.25           O  
ANISOU 4138  OE2 GLU B 160     2398   1733   2045   -107   -375   -128       O  
ATOM   4139  C   GLU B 160      -6.801  19.087  -2.466  1.00 17.81           C  
ANISOU 4139  C   GLU B 160     2574   1995   2198   -213   -450   -146       C  
ATOM   4140  O   GLU B 160      -7.554  19.896  -1.939  1.00 17.19           O  
ANISOU 4140  O   GLU B 160     2436   1936   2160   -199   -471   -143       O  
ATOM   4141  N   GLU B 161      -7.176  18.374  -3.519  1.00 19.68           N  
ANISOU 4141  N   GLU B 161     2861   2223   2393   -248   -475   -139       N  
ATOM   4142  CA  GLU B 161      -8.490  18.596  -4.103  1.00 20.15           C  
ANISOU 4142  CA  GLU B 161     2902   2301   2453   -270   -535   -124       C  
ATOM   4143  CB  GLU B 161      -8.655  17.783  -5.393  1.00 29.51           C  
ANISOU 4143  CB  GLU B 161     4159   3472   3580   -312   -559   -118       C  
ATOM   4144  CG  GLU B 161      -7.628  18.111  -6.478  1.00 46.14           C  
ANISOU 4144  CG  GLU B 161     6336   5546   5650   -307   -543   -109       C  
ATOM   4145  CD  GLU B 161      -7.806  19.485  -7.123  1.00 72.29           C  
ANISOU 4145  CD  GLU B 161     9636   8857   8974   -286   -576    -86       C  
ATOM   4146  OE1 GLU B 161      -8.393  20.402  -6.501  1.00 72.92           O  
ANISOU 4146  OE1 GLU B 161     9647   8957   9103   -260   -595    -79       O  
ATOM   4147  OE2 GLU B 161      -7.340  19.649  -8.271  1.00 86.12           O  
ANISOU 4147  OE2 GLU B 161    11451  10585  10685   -294   -581    -74       O  
ATOM   4148  C   GLU B 161      -9.592  18.252  -3.097  1.00 17.15           C  
ANISOU 4148  C   GLU B 161     2457   1952   2107   -279   -550   -132       C  
ATOM   4149  O   GLU B 161     -10.550  19.002  -2.952  1.00 21.21           O  
ANISOU 4149  O   GLU B 161     2916   2487   2657   -271   -585   -121       O  
ATOM   4150  N   ARG B 162      -9.426  17.139  -2.393  1.00 18.15           N  
ANISOU 4150  N   ARG B 162     2591   2080   2226   -294   -518   -150       N  
ATOM   4151  CA  ARG B 162     -10.410  16.707  -1.408  1.00 18.69           C  
ANISOU 4151  CA  ARG B 162     2603   2176   2324   -305   -525   -159       C  
ATOM   4152  CB  ARG B 162     -10.066  15.307  -0.888  1.00 20.84           C  
ANISOU 4152  CB  ARG B 162     2905   2440   2572   -326   -488   -177       C  
ATOM   4153  CG  ARG B 162     -10.981  14.819   0.211  1.00 24.15           C  
ANISOU 4153  CG  ARG B 162     3270   2885   3020   -337   -487   -187       C  
ATOM   4154  CD  ARG B 162     -10.879  13.313   0.381  1.00 28.78           C  
ANISOU 4154  CD  ARG B 162     3898   3462   3575   -370   -462   -200       C  
ATOM   4155  NE  ARG B 162     -11.484  12.897   1.641  1.00 34.99           N  
ANISOU 4155  NE  ARG B 162     4635   4269   4391   -373   -446   -211       N  
ATOM   4156  CZ  ARG B 162     -11.493  11.641   2.073  1.00 39.60           C  
ANISOU 4156  CZ  ARG B 162     5243   4847   4956   -397   -420   -222       C  
ATOM   4157  NH1 ARG B 162     -10.935  10.695   1.333  1.00 26.37           N  
ANISOU 4157  NH1 ARG B 162     3640   3144   3235   -419   -405   -223       N  
ATOM   4158  NH2 ARG B 162     -12.055  11.336   3.238  1.00 41.21           N  
ANISOU 4158  NH2 ARG B 162     5401   5070   5187   -399   -405   -231       N  
ATOM   4159  C   ARG B 162     -10.496  17.701  -0.254  1.00 20.75           C  
ANISOU 4159  C   ARG B 162     2793   2453   2640   -266   -511   -163       C  
ATOM   4160  O   ARG B 162     -11.582  18.118   0.111  1.00 19.44           O  
ANISOU 4160  O   ARG B 162     2568   2310   2509   -266   -538   -158       O  
ATOM   4161  N   LEU B 163      -9.356  18.106   0.305  1.00 16.16           N  
ANISOU 4161  N   LEU B 163     2216   1859   2065   -234   -468   -171       N  
ATOM   4162  CA  LEU B 163      -9.411  19.006   1.452  1.00 16.28           C  
ANISOU 4162  CA  LEU B 163     2169   1888   2128   -202   -451   -179       C  
ATOM   4163  CB  LEU B 163      -8.053  19.102   2.149  1.00 14.56           C  
ANISOU 4163  CB  LEU B 163     1964   1660   1909   -177   -402   -191       C  
ATOM   4164  CG  LEU B 163      -7.699  17.829   2.917  1.00 16.78           C  
ANISOU 4164  CG  LEU B 163     2259   1943   2172   -190   -369   -205       C  
ATOM   4165  CD1 LEU B 163      -6.336  18.012   3.561  1.00 16.72           C  
ANISOU 4165  CD1 LEU B 163     2261   1928   2165   -163   -326   -213       C  
ATOM   4166  CD2 LEU B 163      -8.775  17.504   3.980  1.00 15.62           C  
ANISOU 4166  CD2 LEU B 163     2061   1823   2052   -200   -372   -214       C  
ATOM   4167  C   LEU B 163      -9.913  20.392   1.057  1.00 22.32           C  
ANISOU 4167  C   LEU B 163     2901   2656   2925   -180   -481   -163       C  
ATOM   4168  O   LEU B 163     -10.614  21.041   1.848  1.00 17.94           O  
ANISOU 4168  O   LEU B 163     2285   2118   2414   -165   -484   -166       O  
ATOM   4169  N   LYS B 164      -9.581  20.851  -0.150  1.00 18.60           N  
ANISOU 4169  N   LYS B 164     2469   2166   2431   -179   -502   -147       N  
ATOM   4170  CA  LYS B 164     -10.127  22.136  -0.612  1.00 23.72           C  
ANISOU 4170  CA  LYS B 164     3089   2816   3109   -159   -533   -128       C  
ATOM   4171  CB  LYS B 164      -9.549  22.512  -1.979  1.00 21.12           C  
ANISOU 4171  CB  LYS B 164     2818   2461   2744   -160   -549   -109       C  
ATOM   4172  CG  LYS B 164      -8.159  23.094  -1.864  1.00 14.90           C  
ANISOU 4172  CG  LYS B 164     2057   1651   1955   -133   -505   -117       C  
ATOM   4173  CD  LYS B 164      -7.497  23.280  -3.207  1.00 23.03           C  
ANISOU 4173  CD  LYS B 164     3152   2653   2945   -138   -512   -101       C  
ATOM   4174  CE  LYS B 164      -8.126  24.392  -4.013  1.00 32.36           C  
ANISOU 4174  CE  LYS B 164     4325   3832   4140   -126   -553    -75       C  
ATOM   4175  NZ  LYS B 164      -7.674  24.256  -5.431  1.00 34.79           N  
ANISOU 4175  NZ  LYS B 164     4706   4116   4396   -143   -567    -59       N  
ATOM   4176  C   LYS B 164     -11.654  22.116  -0.677  1.00 29.92           C  
ANISOU 4176  C   LYS B 164     3826   3625   3918   -173   -580   -115       C  
ATOM   4177  O   LYS B 164     -12.308  23.102  -0.336  1.00 28.83           O  
ANISOU 4177  O   LYS B 164     3633   3497   3826   -149   -592   -106       O  
ATOM   4178  N   LYS B 165     -12.208  20.985  -1.102  1.00 20.93           N  
ANISOU 4178  N   LYS B 165     2707   2496   2748   -213   -604   -114       N  
ATOM   4179  CA  LYS B 165     -13.650  20.817  -1.187  1.00 22.48           C  
ANISOU 4179  CA  LYS B 165     2857   2720   2966   -234   -650   -102       C  
ATOM   4180  CB  LYS B 165     -13.999  19.586  -2.034  1.00 27.61           C  
ANISOU 4180  CB  LYS B 165     3553   3372   3565   -285   -679   -100       C  
ATOM   4181  CG  LYS B 165     -15.491  19.344  -2.139  1.00 46.08           C  
ANISOU 4181  CG  LYS B 165     5842   5742   5925   -312   -730    -88       C  
ATOM   4182  CD  LYS B 165     -16.181  20.558  -2.763  1.00 61.77           C  
ANISOU 4182  CD  LYS B 165     7791   7738   7942   -291   -778    -57       C  
ATOM   4183  CE  LYS B 165     -17.667  20.325  -2.995  1.00 66.60           C  
ANISOU 4183  CE  LYS B 165     8350   8382   8573   -319   -835    -40       C  
ATOM   4184  NZ  LYS B 165     -18.340  21.583  -3.426  1.00 67.09           N  
ANISOU 4184  NZ  LYS B 165     8364   8454   8674   -289   -877     -7       N  
ATOM   4185  C   LYS B 165     -14.285  20.689   0.194  1.00 24.94           C  
ANISOU 4185  C   LYS B 165     3102   3053   3323   -227   -627   -118       C  
ATOM   4186  O   LYS B 165     -15.333  21.268   0.456  1.00 25.74           O  
ANISOU 4186  O   LYS B 165     3139   3172   3469   -217   -651   -107       O  
ATOM   4187  N   GLU B 166     -13.629  19.945   1.078  1.00 22.50           N  
ANISOU 4187  N   GLU B 166     2807   2740   3002   -231   -581   -143       N  
ATOM   4188  CA  GLU B 166     -14.220  19.566   2.366  1.00 21.95           C  
ANISOU 4188  CA  GLU B 166     2686   2690   2965   -233   -557   -159       C  
ATOM   4189  CB  GLU B 166     -13.588  18.269   2.866  1.00 22.96           C  
ANISOU 4189  CB  GLU B 166     2854   2812   3057   -255   -521   -179       C  
ATOM   4190  CG  GLU B 166     -13.985  17.062   2.042  1.00 29.63           C  
ANISOU 4190  CG  GLU B 166     3739   3656   3861   -302   -547   -176       C  
ATOM   4191  CD  GLU B 166     -13.361  15.772   2.563  1.00 37.14           C  
ANISOU 4191  CD  GLU B 166     4733   4599   4781   -320   -506   -194       C  
ATOM   4192  OE1 GLU B 166     -12.383  15.846   3.339  1.00 38.35           O  
ANISOU 4192  OE1 GLU B 166     4893   4742   4935   -294   -462   -205       O  
ATOM   4193  OE2 GLU B 166     -13.848  14.680   2.193  1.00 41.01           O  
ANISOU 4193  OE2 GLU B 166     5247   5090   5245   -362   -519   -196       O  
ATOM   4194  C   GLU B 166     -14.084  20.625   3.449  1.00 24.75           C  
ANISOU 4194  C   GLU B 166     2990   3047   3366   -192   -525   -168       C  
ATOM   4195  O   GLU B 166     -14.934  20.729   4.331  1.00 21.89           O  
ANISOU 4195  O   GLU B 166     2571   2703   3043   -189   -518   -174       O  
ATOM   4196  N   MET B 167     -13.020  21.415   3.394  1.00 18.36           N  
ANISOU 4196  N   MET B 167     2204   2218   2553   -163   -503   -170       N  
ATOM   4197  CA  MET B 167     -12.783  22.397   4.451  1.00 17.30           C  
ANISOU 4197  CA  MET B 167     2031   2084   2459   -128   -469   -182       C  
ATOM   4198  CB  MET B 167     -11.298  22.422   4.842  1.00 16.59           C  
ANISOU 4198  CB  MET B 167     1980   1977   2345   -115   -427   -198       C  
ATOM   4199  CG  MET B 167     -10.786  21.052   5.257  1.00 19.21           C  
ANISOU 4199  CG  MET B 167     2345   2313   2641   -138   -405   -211       C  
ATOM   4200  SD  MET B 167      -9.095  21.052   5.842  1.00 18.93           S  
ANISOU 4200  SD  MET B 167     2343   2264   2585   -121   -357   -226       S  
ATOM   4201  CE  MET B 167      -9.301  21.808   7.467  1.00 19.31           C  
ANISOU 4201  CE  MET B 167     2333   2328   2674   -100   -326   -247       C  
ATOM   4202  C   MET B 167     -13.229  23.789   4.045  1.00 21.98           C  
ANISOU 4202  C   MET B 167     2592   2670   3090   -100   -489   -165       C  
ATOM   4203  O   MET B 167     -13.238  24.121   2.855  1.00 23.23           O  
ANISOU 4203  O   MET B 167     2774   2818   3234   -100   -524   -142       O  
ATOM   4204  N   ASN B 168     -13.613  24.604   5.031  1.00 18.53           N  
ANISOU 4204  N   ASN B 168     2103   2238   2700    -75   -466   -174       N  
ATOM   4205  CA  ASN B 168     -14.071  25.968   4.744  1.00 18.25           C  
ANISOU 4205  CA  ASN B 168     2034   2193   2707    -44   -479   -157       C  
ATOM   4206  CB  ASN B 168     -15.432  26.202   5.369  1.00 23.60           C  
ANISOU 4206  CB  ASN B 168     2640   2889   3437    -38   -484   -154       C  
ATOM   4207  CG  ASN B 168     -16.510  25.456   4.626  1.00 44.03           C  
ANISOU 4207  CG  ASN B 168     5212   5497   6021    -65   -534   -133       C  
ATOM   4208  OD1 ASN B 168     -16.570  25.515   3.397  1.00 47.92           O  
ANISOU 4208  OD1 ASN B 168     5730   5986   6493    -72   -579   -108       O  
ATOM   4209  ND2 ASN B 168     -17.331  24.709   5.351  1.00 52.17           N  
ANISOU 4209  ND2 ASN B 168     6205   6550   7067    -85   -528   -143       N  
ATOM   4210  C   ASN B 168     -13.079  27.034   5.197  1.00 18.69           C  
ANISOU 4210  C   ASN B 168     2100   2227   2774    -13   -440   -170       C  
ATOM   4211  O   ASN B 168     -13.439  28.193   5.481  1.00 19.58           O  
ANISOU 4211  O   ASN B 168     2177   2330   2931     15   -430   -167       O  
ATOM   4212  N   ILE B 169     -11.823  26.616   5.263  1.00 17.69           N  
ANISOU 4212  N   ILE B 169     2023   2092   2608    -21   -416   -185       N  
ATOM   4213  CA  ILE B 169     -10.695  27.528   5.407  1.00 15.80           C  
ANISOU 4213  CA  ILE B 169     1804   1830   2368      0   -386   -194       C  
ATOM   4214  CB  ILE B 169      -9.934  27.348   6.750  1.00 15.52           C  
ANISOU 4214  CB  ILE B 169     1766   1801   2330      0   -339   -226       C  
ATOM   4215  CG1 ILE B 169      -9.490  25.896   6.962  1.00 14.75           C  
ANISOU 4215  CG1 ILE B 169     1696   1718   2191    -27   -334   -234       C  
ATOM   4216  CD1 ILE B 169      -8.625  25.708   8.228  1.00 14.68           C  
ANISOU 4216  CD1 ILE B 169     1688   1717   2174    -26   -291   -261       C  
ATOM   4217  CG2 ILE B 169     -10.767  27.870   7.921  1.00 16.50           C  
ANISOU 4217  CG2 ILE B 169     1835   1936   2499     12   -317   -240       C  
ATOM   4218  C   ILE B 169      -9.763  27.253   4.233  1.00 13.82           C  
ANISOU 4218  C   ILE B 169     1614   1563   2074     -8   -401   -181       C  
ATOM   4219  O   ILE B 169      -9.862  26.202   3.587  1.00 16.39           O  
ANISOU 4219  O   ILE B 169     1968   1895   2364    -33   -423   -173       O  
ATOM   4220  N   PRO B 170      -8.871  28.204   3.933  1.00 16.01           N  
ANISOU 4220  N   PRO B 170     1914   1817   2353     10   -385   -180       N  
ATOM   4221  CA  PRO B 170      -7.986  27.989   2.790  1.00 14.80           C  
ANISOU 4221  CA  PRO B 170     1819   1646   2159      3   -394   -167       C  
ATOM   4222  CB  PRO B 170      -7.168  29.276   2.743  1.00 18.07           C  
ANISOU 4222  CB  PRO B 170     2242   2035   2590     27   -370   -169       C  
ATOM   4223  CG  PRO B 170      -8.014  30.279   3.420  1.00 17.63           C  
ANISOU 4223  CG  PRO B 170     2133   1980   2585     48   -366   -171       C  
ATOM   4224  CD  PRO B 170      -8.696  29.546   4.509  1.00 16.18           C  
ANISOU 4224  CD  PRO B 170     1910   1824   2412     38   -359   -189       C  
ATOM   4225  C   PRO B 170      -7.086  26.782   2.987  1.00 17.14           C  
ANISOU 4225  C   PRO B 170     2151   1948   2415    -18   -374   -181       C  
ATOM   4226  O   PRO B 170      -6.589  26.542   4.094  1.00 16.84           O  
ANISOU 4226  O   PRO B 170     2098   1920   2381    -17   -341   -204       O  
ATOM   4227  N   VAL B 171      -6.921  26.030   1.907  1.00 15.39           N  
ANISOU 4227  N   VAL B 171     1975   1719   2153    -37   -394   -167       N  
ATOM   4228  CA  VAL B 171      -6.045  24.870   1.835  1.00 15.41           C  
ANISOU 4228  CA  VAL B 171     2020   1720   2115    -55   -375   -176       C  
ATOM   4229  CB  VAL B 171      -6.824  23.562   1.747  1.00 17.14           C  
ANISOU 4229  CB  VAL B 171     2245   1954   2313    -83   -395   -174       C  
ATOM   4230  CG1 VAL B 171      -5.872  22.383   1.503  1.00 19.32           C  
ANISOU 4230  CG1 VAL B 171     2573   2221   2545   -100   -372   -180       C  
ATOM   4231  CG2 VAL B 171      -7.677  23.363   3.020  1.00 15.16           C  
ANISOU 4231  CG2 VAL B 171     1937   1729   2093    -84   -390   -189       C  
ATOM   4232  C   VAL B 171      -5.181  25.048   0.590  1.00 17.08           C  
ANISOU 4232  C   VAL B 171     2290   1905   2297    -55   -375   -162       C  
ATOM   4233  O   VAL B 171      -5.694  25.339  -0.495  1.00 17.65           O  
ANISOU 4233  O   VAL B 171     2381   1966   2358    -60   -409   -141       O  
ATOM   4234  N   PHE B 172      -3.876  24.921   0.747  1.00 14.30           N  
ANISOU 4234  N   PHE B 172     1963   1541   1931    -50   -338   -171       N  
ATOM   4235  CA  PHE B 172      -2.950  25.271  -0.332  1.00 13.23           C  
ANISOU 4235  CA  PHE B 172     1877   1377   1772    -47   -328   -160       C  
ATOM   4236  CB  PHE B 172      -2.603  26.753  -0.220  1.00 10.94           C  
ANISOU 4236  CB  PHE B 172     1568   1075   1514    -22   -318   -159       C  
ATOM   4237  CG  PHE B 172      -1.599  27.274  -1.227  1.00 14.50           C  
ANISOU 4237  CG  PHE B 172     2066   1495   1947    -17   -303   -148       C  
ATOM   4238  CD1 PHE B 172      -2.010  27.726  -2.471  1.00 16.62           C  
ANISOU 4238  CD1 PHE B 172     2367   1745   2201    -19   -331   -125       C  
ATOM   4239  CE1 PHE B 172      -1.080  28.275  -3.380  1.00 20.24           C  
ANISOU 4239  CE1 PHE B 172     2872   2175   2645    -14   -313   -115       C  
ATOM   4240  CZ  PHE B 172       0.248  28.414  -3.019  1.00 19.14           C  
ANISOU 4240  CZ  PHE B 172     2738   2026   2510     -8   -267   -129       C  
ATOM   4241  CE2 PHE B 172       0.664  28.012  -1.758  1.00 17.77           C  
ANISOU 4241  CE2 PHE B 172     2527   1873   2353     -5   -242   -151       C  
ATOM   4242  CD2 PHE B 172      -0.268  27.453  -0.863  1.00 16.48           C  
ANISOU 4242  CD2 PHE B 172     2323   1737   2200    -10   -260   -160       C  
ATOM   4243  C   PHE B 172      -1.708  24.411  -0.226  1.00 18.40           C  
ANISOU 4243  C   PHE B 172     2565   2025   2402    -52   -291   -169       C  
ATOM   4244  O   PHE B 172      -1.069  24.418   0.822  1.00 16.11           O  
ANISOU 4244  O   PHE B 172     2247   1745   2128    -42   -261   -184       O  
ATOM   4245  N   HIS B 173      -1.383  23.654  -1.275  1.00 16.39           N  
ANISOU 4245  N   HIS B 173     2367   1753   2107    -67   -290   -159       N  
ATOM   4246  CA  HIS B 173      -0.170  22.821  -1.249  1.00 11.81           C  
ANISOU 4246  CA  HIS B 173     1819   1162   1505    -69   -250   -165       C  
ATOM   4247  CB  HIS B 173      -0.393  21.458  -1.934  1.00 14.76           C  
ANISOU 4247  CB  HIS B 173     2243   1528   1838    -94   -254   -160       C  
ATOM   4248  CG  HIS B 173       0.810  20.564  -1.887  1.00 17.01           C  
ANISOU 4248  CG  HIS B 173     2560   1799   2104    -92   -208   -164       C  
ATOM   4249  ND1 HIS B 173       0.896  19.388  -2.609  1.00 18.47           N  
ANISOU 4249  ND1 HIS B 173     2802   1967   2251   -112   -199   -161       N  
ATOM   4250  CE1 HIS B 173       2.063  18.813  -2.374  1.00 18.09           C  
ANISOU 4250  CE1 HIS B 173     2767   1907   2198   -101   -153   -164       C  
ATOM   4251  NE2 HIS B 173       2.742  19.575  -1.529  1.00 16.47           N  
ANISOU 4251  NE2 HIS B 173     2516   1714   2027    -77   -136   -168       N  
ATOM   4252  CD2 HIS B 173       1.981  20.678  -1.216  1.00 14.28           C  
ANISOU 4252  CD2 HIS B 173     2196   1453   1775    -73   -169   -170       C  
ATOM   4253  C   HIS B 173       0.945  23.586  -1.928  1.00 18.31           C  
ANISOU 4253  C   HIS B 173     2671   1960   2326    -56   -225   -158       C  
ATOM   4254  O   HIS B 173       0.979  23.689  -3.153  1.00 16.46           O  
ANISOU 4254  O   HIS B 173     2485   1702   2066    -65   -233   -144       O  
ATOM   4255  N   ASP B 174       1.845  24.159  -1.134  1.00 13.54           N  
ANISOU 4255  N   ASP B 174     2036   1359   1748    -39   -195   -168       N  
ATOM   4256  CA  ASP B 174       2.806  25.074  -1.707  1.00 15.45           C  
ANISOU 4256  CA  ASP B 174     2295   1578   1995    -28   -173   -163       C  
ATOM   4257  CB  ASP B 174       3.643  25.762  -0.615  1.00 19.78           C  
ANISOU 4257  CB  ASP B 174     2798   2138   2578    -12   -146   -178       C  
ATOM   4258  CG  ASP B 174       4.548  26.862  -1.192  1.00 26.32           C  
ANISOU 4258  CG  ASP B 174     3641   2942   3417     -4   -124   -173       C  
ATOM   4259  OD1 ASP B 174       4.019  27.784  -1.866  1.00 21.30           O  
ANISOU 4259  OD1 ASP B 174     3018   2291   2785     -1   -143   -164       O  
ATOM   4260  OD2 ASP B 174       5.784  26.799  -1.009  1.00 25.33           O  
ANISOU 4260  OD2 ASP B 174     3515   2812   3295      1    -88   -177       O  
ATOM   4261  C   ASP B 174       3.736  24.389  -2.706  1.00 18.93           C  
ANISOU 4261  C   ASP B 174     2797   1994   2403    -35   -145   -154       C  
ATOM   4262  O   ASP B 174       4.143  25.020  -3.683  1.00 16.62           O  
ANISOU 4262  O   ASP B 174     2539   1675   2100    -33   -138   -144       O  
ATOM   4263  N   ASP B 175       4.088  23.119  -2.494  1.00 16.44           N  
ANISOU 4263  N   ASP B 175     2496   1682   2070    -41   -125   -158       N  
ATOM   4264  CA  ASP B 175       4.975  22.466  -3.455  1.00 16.90           C  
ANISOU 4264  CA  ASP B 175     2612   1711   2097    -46    -93   -150       C  
ATOM   4265  CB  ASP B 175       5.378  21.077  -2.968  1.00 20.11           C  
ANISOU 4265  CB  ASP B 175     3025   2123   2493    -48    -67   -154       C  
ATOM   4266  CG  ASP B 175       5.997  21.130  -1.615  1.00 20.97           C  
ANISOU 4266  CG  ASP B 175     3076   2257   2635    -31    -49   -163       C  
ATOM   4267  OD1 ASP B 175       7.225  21.371  -1.545  1.00 20.95           O  
ANISOU 4267  OD1 ASP B 175     3068   2248   2646    -17    -13   -161       O  
ATOM   4268  OD2 ASP B 175       5.239  21.000  -0.625  1.00 22.57           O  
ANISOU 4268  OD2 ASP B 175     3238   2488   2851    -32    -72   -172       O  
ATOM   4269  C   ASP B 175       4.360  22.355  -4.840  1.00 23.53           C  
ANISOU 4269  C   ASP B 175     3513   2527   2899    -65   -114   -137       C  
ATOM   4270  O   ASP B 175       5.079  22.378  -5.847  1.00 23.00           O  
ANISOU 4270  O   ASP B 175     3498   2431   2809    -68    -89   -129       O  
ATOM   4271  N   GLN B 176       3.040  22.222  -4.901  1.00 17.53           N  
ANISOU 4271  N   GLN B 176     2748   1782   2131    -80   -161   -135       N  
ATOM   4272  CA  GLN B 176       2.373  22.169  -6.195  1.00 17.76           C  
ANISOU 4272  CA  GLN B 176     2832   1794   2122   -101   -190   -122       C  
ATOM   4273  CB  GLN B 176       0.936  21.697  -6.070  1.00 20.94           C  
ANISOU 4273  CB  GLN B 176     3221   2219   2517   -121   -240   -122       C  
ATOM   4274  CG  GLN B 176       0.785  20.221  -5.893  1.00 21.46           C  
ANISOU 4274  CG  GLN B 176     3308   2287   2558   -141   -231   -131       C  
ATOM   4275  CD  GLN B 176      -0.667  19.819  -5.870  1.00 24.09           C  
ANISOU 4275  CD  GLN B 176     3628   2642   2883   -165   -282   -130       C  
ATOM   4276  OE1 GLN B 176      -1.422  20.131  -6.798  1.00 26.32           O  
ANISOU 4276  OE1 GLN B 176     3935   2922   3145   -182   -323   -117       O  
ATOM   4277  NE2 GLN B 176      -1.080  19.145  -4.799  1.00 18.87           N  
ANISOU 4277  NE2 GLN B 176     2927   2004   2240   -167   -281   -142       N  
ATOM   4278  C   GLN B 176       2.355  23.505  -6.895  1.00 20.53           C  
ANISOU 4278  C   GLN B 176     3191   2132   2479    -92   -205   -109       C  
ATOM   4279  O   GLN B 176       2.511  23.550  -8.104  1.00 25.80           O  
ANISOU 4279  O   GLN B 176     3919   2773   3111   -104   -205    -96       O  
ATOM   4280  N   HIS B 177       2.148  24.580  -6.139  1.00 17.70           N  
ANISOU 4280  N   HIS B 177     2774   1787   2163    -72   -216   -111       N  
ATOM   4281  CA  HIS B 177       1.755  25.851  -6.752  1.00 17.97           C  
ANISOU 4281  CA  HIS B 177     2810   1811   2206    -64   -241    -96       C  
ATOM   4282  CB  HIS B 177       0.415  26.282  -6.154  1.00 19.03           C  
ANISOU 4282  CB  HIS B 177     2891   1972   2368    -60   -288    -94       C  
ATOM   4283  CG  HIS B 177      -0.642  25.231  -6.302  1.00 21.16           C  
ANISOU 4283  CG  HIS B 177     3167   2259   2614    -84   -325    -92       C  
ATOM   4284  ND1 HIS B 177      -1.023  24.732  -7.529  1.00 21.98           N  
ANISOU 4284  ND1 HIS B 177     3330   2350   2670   -108   -350    -77       N  
ATOM   4285  CE1 HIS B 177      -1.943  23.796  -7.359  1.00 24.26           C  
ANISOU 4285  CE1 HIS B 177     3611   2659   2946   -130   -379    -81       C  
ATOM   4286  NE2 HIS B 177      -2.171  23.673  -6.063  1.00 21.97           N  
ANISOU 4286  NE2 HIS B 177     3259   2394   2695   -119   -372    -96       N  
ATOM   4287  CD2 HIS B 177      -1.376  24.561  -5.378  1.00 20.03           C  
ANISOU 4287  CD2 HIS B 177     2981   2144   2485    -90   -339   -104       C  
ATOM   4288  C   HIS B 177       2.743  27.006  -6.641  1.00 22.32           C  
ANISOU 4288  C   HIS B 177     3351   2345   2784    -43   -208    -97       C  
ATOM   4289  O   HIS B 177       2.657  27.975  -7.417  1.00 18.93           O  
ANISOU 4289  O   HIS B 177     2943   1896   2353    -38   -218    -81       O  
ATOM   4290  N   GLY B 178       3.661  26.929  -5.684  1.00 18.35           N  
ANISOU 4290  N   GLY B 178     2815   1851   2307    -32   -169   -114       N  
ATOM   4291  CA  GLY B 178       4.572  28.035  -5.455  1.00 17.52           C  
ANISOU 4291  CA  GLY B 178     2693   1734   2231    -16   -139   -118       C  
ATOM   4292  C   GLY B 178       5.464  28.338  -6.644  1.00 19.18           C  
ANISOU 4292  C   GLY B 178     2961   1908   2418    -19   -110   -105       C  
ATOM   4293  O   GLY B 178       5.582  29.503  -7.042  1.00 20.17           O  
ANISOU 4293  O   GLY B 178     3091   2015   2556    -11   -109    -96       O  
ATOM   4294  N   THR B 179       6.106  27.306  -7.190  1.00 17.33           N  
ANISOU 4294  N   THR B 179     2772   1662   2153    -30    -83   -104       N  
ATOM   4295  CA  THR B 179       6.977  27.460  -8.351  1.00 18.30           C  
ANISOU 4295  CA  THR B 179     2955   1749   2250    -34    -50    -93       C  
ATOM   4296  CB  THR B 179       7.637  26.121  -8.755  1.00 23.23           C  
ANISOU 4296  CB  THR B 179     3622   2361   2842    -44    -15    -95       C  
ATOM   4297  OG1 THR B 179       8.554  25.734  -7.733  1.00 29.73           O  
ANISOU 4297  OG1 THR B 179     4401   3200   3696    -32     21   -108       O  
ATOM   4298  CG2 THR B 179       8.412  26.283 -10.073  1.00 25.84           C  
ANISOU 4298  CG2 THR B 179     4023   2652   3143    -51     20    -82       C  
ATOM   4299  C   THR B 179       6.202  28.009  -9.537  1.00 18.03           C  
ANISOU 4299  C   THR B 179     2970   1695   2187    -43    -84    -72       C  
ATOM   4300  O   THR B 179       6.689  28.864 -10.269  1.00 20.80           O  
ANISOU 4300  O   THR B 179     3351   2019   2534    -39    -67    -61       O  
ATOM   4301  N   ALA B 180       4.984  27.517  -9.705  1.00 16.02           N  
ANISOU 4301  N   ALA B 180     2721   1456   1911    -55   -133    -66       N  
ATOM   4302  CA  ALA B 180       4.121  27.950 -10.798  1.00 17.70           C  
ANISOU 4302  CA  ALA B 180     2976   1656   2093    -65   -175    -44       C  
ATOM   4303  CB  ALA B 180       2.829  27.126 -10.794  1.00 18.35           C  
ANISOU 4303  CB  ALA B 180     3056   1763   2155    -83   -228    -42       C  
ATOM   4304  C   ALA B 180       3.806  29.447 -10.723  1.00 17.66           C  
ANISOU 4304  C   ALA B 180     2942   1647   2122    -46   -194    -32       C  
ATOM   4305  O   ALA B 180       3.865  30.149 -11.726  1.00 19.19           O  
ANISOU 4305  O   ALA B 180     3181   1814   2296    -46   -197    -12       O  
ATOM   4306  N   ILE B 181       3.441  29.913  -9.535  1.00 16.48           N  
ANISOU 4306  N   ILE B 181     2720   1520   2020    -29   -203    -44       N  
ATOM   4307  CA  ILE B 181       3.096  31.313  -9.300  1.00 16.22           C  
ANISOU 4307  CA  ILE B 181     2655   1483   2025     -9   -216    -36       C  
ATOM   4308  CB  ILE B 181       2.548  31.491  -7.871  1.00 16.86           C  
ANISOU 4308  CB  ILE B 181     2658   1595   2154      4   -227    -54       C  
ATOM   4309  CG1 ILE B 181       1.152  30.859  -7.798  1.00 20.31           C  
ANISOU 4309  CG1 ILE B 181     3077   2058   2582     -4   -281    -47       C  
ATOM   4310  CD1 ILE B 181       0.608  30.767  -6.396  1.00 20.80           C  
ANISOU 4310  CD1 ILE B 181     3067   2151   2684      4   -287    -66       C  
ATOM   4311  CG2 ILE B 181       2.534  32.970  -7.446  1.00 16.42           C  
ANISOU 4311  CG2 ILE B 181     2568   1528   2143     26   -220    -53       C  
ATOM   4312  C   ILE B 181       4.304  32.207  -9.538  1.00 15.12           C  
ANISOU 4312  C   ILE B 181     2533   1313   1898      0   -168    -37       C  
ATOM   4313  O   ILE B 181       4.221  33.202 -10.256  1.00 16.55           O  
ANISOU 4313  O   ILE B 181     2740   1470   2079      7   -173    -18       O  
ATOM   4314  N   VAL B 182       5.438  31.839  -8.951  1.00 15.25           N  
ANISOU 4314  N   VAL B 182     2535   1332   1926     -1   -120    -58       N  
ATOM   4315  CA  VAL B 182       6.612  32.702  -9.033  1.00 15.56           C  
ANISOU 4315  CA  VAL B 182     2581   1347   1985      5    -73    -61       C  
ATOM   4316  CB  VAL B 182       7.634  32.343  -7.933  1.00 16.09           C  
ANISOU 4316  CB  VAL B 182     2603   1431   2080      7    -33    -87       C  
ATOM   4317  CG1 VAL B 182       8.886  33.208  -8.077  1.00 16.74           C  
ANISOU 4317  CG1 VAL B 182     2690   1490   2182      9     16    -90       C  
ATOM   4318  CG2 VAL B 182       7.005  32.562  -6.558  1.00 17.37           C  
ANISOU 4318  CG2 VAL B 182     2694   1626   2279     16    -55   -104       C  
ATOM   4319  C   VAL B 182       7.252  32.613 -10.437  1.00 15.20           C  
ANISOU 4319  C   VAL B 182     2612   1266   1898     -5    -49    -44       C  
ATOM   4320  O   VAL B 182       7.664  33.630 -10.999  1.00 16.77           O  
ANISOU 4320  O   VAL B 182     2835   1436   2102     -1    -31    -33       O  
ATOM   4321  N   SER B 183       7.305  31.416 -11.027  1.00 17.85           N  
ANISOU 4321  N   SER B 183     2991   1600   2190    -21    -47    -41       N  
ATOM   4322  CA  SER B 183       7.844  31.313 -12.384  1.00 17.91           C  
ANISOU 4322  CA  SER B 183     3077   1572   2154    -33    -23    -25       C  
ATOM   4323  CB  SER B 183       8.110  29.849 -12.792  1.00 23.51           C  
ANISOU 4323  CB  SER B 183     3830   2281   2823    -50     -6    -30       C  
ATOM   4324  OG  SER B 183       6.911  29.164 -13.109  1.00 26.30           O  
ANISOU 4324  OG  SER B 183     4202   2649   3141    -64    -59    -23       O  
ATOM   4325  C   SER B 183       6.900  31.971 -13.380  1.00 17.87           C  
ANISOU 4325  C   SER B 183     3116   1553   2122    -36    -67      1       C  
ATOM   4326  O   SER B 183       7.352  32.537 -14.366  1.00 19.37           O  
ANISOU 4326  O   SER B 183     3360   1709   2291    -39    -47     17       O  
ATOM   4327  N   GLY B 184       5.597  31.938 -13.104  1.00 17.10           N  
ANISOU 4327  N   GLY B 184     2991   1480   2028    -34   -127      8       N  
ATOM   4328  CA  GLY B 184       4.641  32.604 -13.969  1.00 20.56           C  
ANISOU 4328  CA  GLY B 184     3458   1908   2444    -34   -175     37       C  
ATOM   4329  C   GLY B 184       4.889  34.104 -14.010  1.00 17.93           C  
ANISOU 4329  C   GLY B 184     3116   1553   2145    -13   -162     49       C  
ATOM   4330  O   GLY B 184       4.824  34.737 -15.075  1.00 19.01           O  
ANISOU 4330  O   GLY B 184     3307   1661   2255    -14   -170     76       O  
ATOM   4331  N   ALA B 185       5.194  34.686 -12.853  1.00 17.54           N  
ANISOU 4331  N   ALA B 185     3001   1513   2151      4   -141     30       N  
ATOM   4332  CA  ALA B 185       5.494  36.107 -12.802  1.00 21.02           C  
ANISOU 4332  CA  ALA B 185     3431   1928   2626     21   -122     37       C  
ATOM   4333  CB  ALA B 185       5.655  36.579 -11.363  1.00 18.74           C  
ANISOU 4333  CB  ALA B 185     3065   1657   2396     35   -106     10       C  
ATOM   4334  C   ALA B 185       6.754  36.386 -13.609  1.00 19.46           C  
ANISOU 4334  C   ALA B 185     3290   1694   2410     13    -68     40       C  
ATOM   4335  O   ALA B 185       6.805  37.333 -14.391  1.00 19.35           O  
ANISOU 4335  O   ALA B 185     3314   1648   2389     18    -63     62       O  
ATOM   4336  N   ALA B 186       7.766  35.541 -13.427  1.00 16.98           N  
ANISOU 4336  N   ALA B 186     2980   1383   2088      1    -24     20       N  
ATOM   4337  CA  ALA B 186       9.039  35.735 -14.118  1.00 20.33           C  
ANISOU 4337  CA  ALA B 186     3450   1773   2500     -7     35     21       C  
ATOM   4338  CB  ALA B 186      10.066  34.729 -13.615  1.00 20.64           C  
ANISOU 4338  CB  ALA B 186     3472   1825   2544    -15     80     -3       C  
ATOM   4339  C   ALA B 186       8.862  35.610 -15.634  1.00 23.08           C  
ANISOU 4339  C   ALA B 186     3888   2093   2789    -20     27     49       C  
ATOM   4340  O   ALA B 186       9.448  36.379 -16.410  1.00 23.90           O  
ANISOU 4340  O   ALA B 186     4036   2160   2883    -21     59     62       O  
ATOM   4341  N   LEU B 187       8.030  34.661 -16.041  1.00 24.53           N  
ANISOU 4341  N   LEU B 187     4098   2292   2930    -32    -15     56       N  
ATOM   4342  CA  LEU B 187       7.764  34.413 -17.453  1.00 28.20           C  
ANISOU 4342  CA  LEU B 187     4651   2734   3331    -49    -29     81       C  
ATOM   4343  CB  LEU B 187       6.906  33.158 -17.644  1.00 24.93           C  
ANISOU 4343  CB  LEU B 187     4253   2344   2874    -67    -74     80       C  
ATOM   4344  CG  LEU B 187       6.522  32.818 -19.090  1.00 27.91           C  
ANISOU 4344  CG  LEU B 187     4723   2703   3178    -91    -97    105       C  
ATOM   4345  CD1 LEU B 187       7.761  32.641 -19.971  1.00 26.59           C  
ANISOU 4345  CD1 LEU B 187     4631   2496   2978   -104    -28    103       C  
ATOM   4346  CD2 LEU B 187       5.658  31.570 -19.137  1.00 33.65           C  
ANISOU 4346  CD2 LEU B 187     5459   3457   3869   -113   -141     99       C  
ATOM   4347  C   LEU B 187       7.076  35.594 -18.098  1.00 28.27           C  
ANISOU 4347  C   LEU B 187     4682   2726   3334    -39    -66    113       C  
ATOM   4348  O   LEU B 187       7.452  36.004 -19.199  1.00 24.79           O  
ANISOU 4348  O   LEU B 187     4312   2250   2858    -47    -47    133       O  
ATOM   4349  N   LEU B 188       6.063  36.132 -17.417  1.00 26.17           N  
ANISOU 4349  N   LEU B 188     4357   2482   3103    -21   -116    119       N  
ATOM   4350  CA  LEU B 188       5.357  37.312 -17.900  1.00 22.77           C  
ANISOU 4350  CA  LEU B 188     3938   2036   2678     -5   -151    152       C  
ATOM   4351  CB  LEU B 188       4.336  37.809 -16.874  1.00 31.38           C  
ANISOU 4351  CB  LEU B 188     4947   3154   3822     18   -194    151       C  
ATOM   4352  CG  LEU B 188       2.888  37.335 -16.938  1.00 41.04           C  
ANISOU 4352  CG  LEU B 188     6153   4409   5030     17   -270    168       C  
ATOM   4353  CD1 LEU B 188       2.132  37.923 -15.750  1.00 38.73           C  
ANISOU 4353  CD1 LEU B 188     5774   4140   4803     43   -292    162       C  
ATOM   4354  CD2 LEU B 188       2.246  37.768 -18.253  1.00 46.29           C  
ANISOU 4354  CD2 LEU B 188     6881   5057   5650     14   -314    213       C  
ATOM   4355  C   LEU B 188       6.341  38.429 -18.203  1.00 24.31           C  
ANISOU 4355  C   LEU B 188     4157   2188   2890      3    -96    157       C  
ATOM   4356  O   LEU B 188       6.271  39.072 -19.249  1.00 27.82           O  
ANISOU 4356  O   LEU B 188     4662   2603   3304      3   -101    188       O  
ATOM   4357  N   ASN B 189       7.255  38.660 -17.268  1.00 21.10           N  
ANISOU 4357  N   ASN B 189     3702   1782   2532      9    -44    127       N  
ATOM   4358  CA  ASN B 189       8.230  39.711 -17.420  1.00 21.52           C  
ANISOU 4358  CA  ASN B 189     3770   1798   2608     15     11    127       C  
ATOM   4359  CB  ASN B 189       8.890  40.016 -16.079  1.00 18.80           C  
ANISOU 4359  CB  ASN B 189     3349   1466   2326     22     48     93       C  
ATOM   4360  CG  ASN B 189       8.009  40.904 -15.202  1.00 21.22           C  
ANISOU 4360  CG  ASN B 189     3596   1784   2682     44     14     93       C  
ATOM   4361  OD1 ASN B 189       7.083  41.561 -15.698  1.00 24.75           O  
ANISOU 4361  OD1 ASN B 189     4060   2219   3123     59    -25    124       O  
ATOM   4362  ND2 ASN B 189       8.309  40.950 -13.913  1.00 18.58           N  
ANISOU 4362  ND2 ASN B 189     3192   1471   2396     48     32     61       N  
ATOM   4363  C   ASN B 189       9.279  39.375 -18.465  1.00 28.18           C  
ANISOU 4363  C   ASN B 189     4689   2610   3408     -5     62    132       C  
ATOM   4364  O   ASN B 189       9.715  40.254 -19.198  1.00 24.68           O  
ANISOU 4364  O   ASN B 189     4292   2128   2957     -5     90    150       O  
ATOM   4365  N   ALA B 190       9.660  38.106 -18.552  1.00 26.19           N  
ANISOU 4365  N   ALA B 190     4452   2373   3127    -23     77    116       N  
ATOM   4366  CA  ALA B 190      10.631  37.693 -19.565  1.00 29.22           C  
ANISOU 4366  CA  ALA B 190     4909   2725   3467    -42    129    119       C  
ATOM   4367  CB  ALA B 190      11.021  36.233 -19.375  1.00 24.33           C  
ANISOU 4367  CB  ALA B 190     4290   2126   2830    -56    148     97       C  
ATOM   4368  C   ALA B 190      10.063  37.915 -20.957  1.00 23.95           C  
ANISOU 4368  C   ALA B 190     4330   2031   2737    -51    101    155       C  
ATOM   4369  O   ALA B 190      10.779  38.323 -21.879  1.00 25.75           O  
ANISOU 4369  O   ALA B 190     4623   2220   2939    -60    145    168       O  
ATOM   4370  N   CYS B 191       8.773  37.642 -21.112  1.00 25.24           N  
ANISOU 4370  N   CYS B 191     4496   2219   2876    -51     27    172       N  
ATOM   4371  CA  CYS B 191       8.092  37.856 -22.389  1.00 31.55           C  
ANISOU 4371  CA  CYS B 191     5373   2999   3613    -60    -13    209       C  
ATOM   4372  CB  CYS B 191       6.702  37.221 -22.362  1.00 30.19           C  
ANISOU 4372  CB  CYS B 191     5188   2865   3417    -65    -96    220       C  
ATOM   4373  SG  CYS B 191       6.711  35.415 -22.448  1.00 36.62           S  
ANISOU 4373  SG  CYS B 191     6026   3703   4184    -97    -97    195       S  
ATOM   4374  C   CYS B 191       7.984  39.337 -22.752  1.00 35.93           C  
ANISOU 4374  C   CYS B 191     5942   3525   4185    -41    -16    239       C  
ATOM   4375  O   CYS B 191       8.146  39.711 -23.917  1.00 32.24           O  
ANISOU 4375  O   CYS B 191     5556   3023   3670    -51     -7    266       O  
ATOM   4376  N   SER B 192       7.685  40.165 -21.752  1.00 27.70           N  
ANISOU 4376  N   SER B 192     4823   2493   3209    -15    -27    234       N  
ATOM   4377  CA  SER B 192       7.642  41.610 -21.897  1.00 31.36           C  
ANISOU 4377  CA  SER B 192     5290   2925   3701      6    -21    258       C  
ATOM   4378  CB  SER B 192       7.322  42.267 -20.547  1.00 35.17           C  
ANISOU 4378  CB  SER B 192     5677   3426   4260     31    -28    240       C  
ATOM   4379  OG  SER B 192       7.190  43.671 -20.679  1.00 52.47           O  
ANISOU 4379  OG  SER B 192     7872   5584   6480     53    -23    264       O  
ATOM   4380  C   SER B 192       8.962  42.135 -22.448  1.00 34.80           C  
ANISOU 4380  C   SER B 192     5776   3315   4132     -4     57    255       C  
ATOM   4381  O   SER B 192       8.986  42.881 -23.423  1.00 35.39           O  
ANISOU 4381  O   SER B 192     5916   3353   4178     -3     62    287       O  
ATOM   4382  N   ILE B 193      10.052  41.721 -21.814  1.00 31.97           N  
ANISOU 4382  N   ILE B 193     5386   2961   3802    -13    117    218       N  
ATOM   4383  CA  ILE B 193      11.404  42.122 -22.181  1.00 36.40           C  
ANISOU 4383  CA  ILE B 193     5969   3495   4368    -24    196    207       C  
ATOM   4384  CB  ILE B 193      12.411  41.528 -21.179  1.00 38.62           C  
ANISOU 4384  CB  ILE B 193     6189   3794   4691    -30    247    165       C  
ATOM   4385  CG1 ILE B 193      12.163  42.129 -19.799  1.00 42.87           C  
ANISOU 4385  CG1 ILE B 193     6645   4346   5300    -12    234    147       C  
ATOM   4386  CD1 ILE B 193      12.997  41.503 -18.715  1.00 39.66           C  
ANISOU 4386  CD1 ILE B 193     6170   3966   4932    -18    269    107       C  
ATOM   4387  CG2 ILE B 193      13.848  41.757 -21.619  1.00 38.30           C  
ANISOU 4387  CG2 ILE B 193     6156   3744   4653    -43    325    152       C  
ATOM   4388  C   ILE B 193      11.800  41.709 -23.598  1.00 38.51           C  
ANISOU 4388  C   ILE B 193     6316   3751   4564    -44    218    221       C  
ATOM   4389  O   ILE B 193      12.502  42.444 -24.293  1.00 43.52           O  
ANISOU 4389  O   ILE B 193     6979   4366   5191    -48    262    228       O  
ATOM   4390  N   THR B 194      11.349  40.537 -24.026  1.00 33.78           N  
ANISOU 4390  N   THR B 194     6483   3477   2874     -5   1154   -343       N  
ATOM   4391  CA  THR B 194      11.722  40.018 -25.340  1.00 32.05           C  
ANISOU 4391  CA  THR B 194     6400   3217   2562      3   1243   -407       C  
ATOM   4392  CB  THR B 194      12.045  38.519 -25.271  1.00 37.35           C  
ANISOU 4392  CB  THR B 194     7118   3804   3271     28   1279   -480       C  
ATOM   4393  OG1 THR B 194      10.912  37.804 -24.761  1.00 35.77           O  
ANISOU 4393  OG1 THR B 194     6935   3592   3063    -17   1140   -492       O  
ATOM   4394  CG2 THR B 194      13.231  38.288 -24.364  1.00 37.37           C  
ANISOU 4394  CG2 THR B 194     6993   3776   3428     92   1371   -470       C  
ATOM   4395  C   THR B 194      10.636  40.252 -26.387  1.00 38.84           C  
ANISOU 4395  C   THR B 194     7347   4112   3300    -56   1147   -403       C  
ATOM   4396  O   THR B 194      10.685  39.681 -27.480  1.00 38.16           O  
ANISOU 4396  O   THR B 194     7352   3994   3154    -61   1173   -448       O  
ATOM   4397  N   ASN B 195       9.665  41.098 -26.041  1.00 44.29           N  
ANISOU 4397  N   ASN B 195     7998   4868   3961    -97   1034   -345       N  
ATOM   4398  CA  ASN B 195       8.593  41.493 -26.951  1.00 44.48           C  
ANISOU 4398  CA  ASN B 195     8072   4938   3889   -148    937   -327       C  
ATOM   4399  CB  ASN B 195       9.165  42.296 -28.125  1.00 49.17           C  
ANISOU 4399  CB  ASN B 195     8684   5554   4445   -133   1017   -318       C  
ATOM   4400  CG  ASN B 195       9.717  43.635 -27.686  1.00 52.84           C  
ANISOU 4400  CG  ASN B 195     9046   6066   4966   -109   1059   -254       C  
ATOM   4401  OD1 ASN B 195       9.053  44.385 -26.972  1.00 54.81           O  
ANISOU 4401  OD1 ASN B 195     9223   6368   5234   -129    972   -197       O  
ATOM   4402  ND2 ASN B 195      10.944  43.935 -28.095  1.00 59.00           N  
ANISOU 4402  ND2 ASN B 195     9813   6828   5778    -66   1190   -260       N  
ATOM   4403  C   ASN B 195       7.791  40.312 -27.474  1.00 48.78           C  
ANISOU 4403  C   ASN B 195     8717   5447   4371   -188    865   -380       C  
ATOM   4404  O   ASN B 195       7.513  40.215 -28.665  1.00 47.18           O  
ANISOU 4404  O   ASN B 195     8589   5246   4091   -208    861   -402       O  
ATOM   4405  N   ARG B 196       7.413  39.417 -26.573  1.00 44.79           N  
ANISOU 4405  N   ARG B 196     8210   4909   3901   -199    806   -401       N  
ATOM   4406  CA  ARG B 196       6.571  38.292 -26.945  1.00 44.96           C  
ANISOU 4406  CA  ARG B 196     8316   4896   3872   -243    722   -446       C  
ATOM   4407  CB  ARG B 196       7.151  36.980 -26.443  1.00 44.61           C  
ANISOU 4407  CB  ARG B 196     8300   4762   3886   -215    773   -513       C  
ATOM   4408  CG  ARG B 196       8.346  36.504 -27.193  1.00 47.69           C  
ANISOU 4408  CG  ARG B 196     8740   5093   4288   -165    919   -566       C  
ATOM   4409  CD  ARG B 196       8.835  35.209 -26.605  1.00 50.90           C  
ANISOU 4409  CD  ARG B 196     9155   5414   4771   -134    958   -624       C  
ATOM   4410  NE  ARG B 196      10.170  35.409 -26.071  1.00 53.54           N  
ANISOU 4410  NE  ARG B 196     9410   5726   5206    -59   1093   -621       N  
ATOM   4411  CZ  ARG B 196      11.247  34.731 -26.441  1.00 41.46           C  
ANISOU 4411  CZ  ARG B 196     7896   4136   3721     -5   1215   -661       C  
ATOM   4412  NH1 ARG B 196      11.164  33.763 -27.346  1.00 46.62           N  
ANISOU 4412  NH1 ARG B 196     8654   4741   4320    -16   1223   -713       N  
ATOM   4413  NH2 ARG B 196      12.414  35.024 -25.884  1.00 40.52           N  
ANISOU 4413  NH2 ARG B 196     7681   4011   3703     60   1328   -644       N  
ATOM   4414  C   ARG B 196       5.169  38.442 -26.403  1.00 50.10           C  
ANISOU 4414  C   ARG B 196     8929   5599   4506   -300    557   -398       C  
ATOM   4415  O   ARG B 196       4.939  39.138 -25.417  1.00 53.30           O  
ANISOU 4415  O   ARG B 196     9242   6052   4959   -296    509   -339       O  
ATOM   4416  N   LYS B 197       4.236  37.770 -27.062  1.00 44.56           N  
ANISOU 4416  N   LYS B 197     8296   4892   3742   -352    472   -420       N  
ATOM   4417  CA  LYS B 197       2.848  37.745 -26.628  1.00 50.59           C  
ANISOU 4417  CA  LYS B 197     9020   5703   4498   -408    314   -374       C  
ATOM   4418  CB  LYS B 197       1.871  38.140 -27.759  1.00 56.88           C  
ANISOU 4418  CB  LYS B 197     9842   6555   5215   -454    247   -352       C  
ATOM   4419  CG  LYS B 197       2.037  39.545 -28.418  1.00 66.49           C  
ANISOU 4419  CG  LYS B 197    11017   7838   6407   -434    289   -307       C  
ATOM   4420  CD  LYS B 197       3.469  39.915 -28.827  1.00 71.98           C  
ANISOU 4420  CD  LYS B 197    11740   8501   7107   -377    445   -336       C  
ATOM   4421  CE  LYS B 197       3.603  41.312 -29.411  1.00 72.54           C  
ANISOU 4421  CE  LYS B 197    11763   8637   7161   -361    478   -288       C  
ATOM   4422  NZ  LYS B 197       4.986  41.529 -29.938  1.00 72.46           N  
ANISOU 4422  NZ  LYS B 197    11787   8591   7154   -310    630   -319       N  
ATOM   4423  C   LYS B 197       2.598  36.319 -26.143  1.00 50.38           C  
ANISOU 4423  C   LYS B 197     9039   5608   4493   -430    266   -425       C  
ATOM   4424  O   LYS B 197       2.892  35.365 -26.859  1.00 53.17           O  
ANISOU 4424  O   LYS B 197     9489   5898   4817   -433    313   -493       O  
ATOM   4425  N   MET B 198       2.086  36.178 -24.924  1.00 47.77           N  
ANISOU 4425  N   MET B 198     8636   5292   4223   -441    175   -390       N  
ATOM   4426  CA  MET B 198       1.960  34.873 -24.271  1.00 44.60           C  
ANISOU 4426  CA  MET B 198     8261   4821   3864   -453    134   -436       C  
ATOM   4427  CB  MET B 198       1.220  35.038 -22.943  1.00 44.12           C  
ANISOU 4427  CB  MET B 198     8097   4802   3865   -469     12   -373       C  
ATOM   4428  CG  MET B 198       2.102  35.559 -21.809  1.00 42.45           C  
ANISOU 4428  CG  MET B 198     7758   4594   3777   -401     72   -339       C  
ATOM   4429  SD  MET B 198       3.392  34.382 -21.329  1.00 60.11           S  
ANISOU 4429  SD  MET B 198     9965   6722   6152   -338    188   -409       S  
ATOM   4430  CE  MET B 198       2.422  33.079 -20.582  1.00 52.11           C  
ANISOU 4430  CE  MET B 198     8939   5671   5191   -382     52   -416       C  
ATOM   4431  C   MET B 198       1.261  33.821 -25.142  1.00 46.06           C  
ANISOU 4431  C   MET B 198     8538   4971   3993   -508     80   -479       C  
ATOM   4432  O   MET B 198       1.598  32.636 -25.099  1.00 45.54           O  
ANISOU 4432  O   MET B 198     8530   4821   3950   -504    108   -545       O  
ATOM   4433  N   GLU B 199       0.318  34.271 -25.960  1.00 45.76           N  
ANISOU 4433  N   GLU B 199     8507   4995   3886   -554     10   -441       N  
ATOM   4434  CA  GLU B 199      -0.497  33.380 -26.777  1.00 52.56           C  
ANISOU 4434  CA  GLU B 199     9447   5835   4689   -613    -54   -471       C  
ATOM   4435  CB  GLU B 199      -1.629  34.178 -27.424  1.00 63.57           C  
ANISOU 4435  CB  GLU B 199    10805   7318   6030   -656   -139   -409       C  
ATOM   4436  CG  GLU B 199      -1.283  35.646 -27.653  1.00 77.00           C  
ANISOU 4436  CG  GLU B 199    12446   9087   7723   -618    -85   -362       C  
ATOM   4437  CD  GLU B 199      -2.313  36.371 -28.497  1.00 86.39           C  
ANISOU 4437  CD  GLU B 199    13609  10357   8860   -652   -149   -316       C  
ATOM   4438  OE1 GLU B 199      -3.218  35.705 -29.048  1.00 91.78           O  
ANISOU 4438  OE1 GLU B 199    14336  11039   9500   -706   -223   -327       O  
ATOM   4439  OE2 GLU B 199      -2.216  37.612 -28.608  1.00 85.73           O  
ANISOU 4439  OE2 GLU B 199    13457  10336   8779   -624   -123   -269       O  
ATOM   4440  C   GLU B 199       0.277  32.620 -27.858  1.00 49.61           C  
ANISOU 4440  C   GLU B 199     9201   5385   4264   -599     51   -556       C  
ATOM   4441  O   GLU B 199      -0.232  31.649 -28.409  1.00 48.97           O  
ANISOU 4441  O   GLU B 199     9196   5267   4144   -643      8   -594       O  
ATOM   4442  N   THR B 200       1.501  33.048 -28.157  1.00 44.50           N  
ANISOU 4442  N   THR B 200     8571   4716   3620   -538    189   -583       N  
ATOM   4443  CA  THR B 200       2.279  32.408 -29.216  1.00 42.49           C  
ANISOU 4443  CA  THR B 200     8426   4396   3322   -516    297   -656       C  
ATOM   4444  CB  THR B 200       2.569  33.399 -30.374  1.00 60.71           C  
ANISOU 4444  CB  THR B 200    10760   6750   5558   -501    363   -642       C  
ATOM   4445  OG1 THR B 200       3.557  34.355 -29.967  1.00 60.15           O  
ANISOU 4445  OG1 THR B 200    10620   6699   5535   -439    461   -617       O  
ATOM   4446  CG2 THR B 200       1.298  34.137 -30.776  1.00 51.35           C  
ANISOU 4446  CG2 THR B 200     9543   5652   4316   -558    245   -582       C  
ATOM   4447  C   THR B 200       3.603  31.830 -28.706  1.00 45.33           C  
ANISOU 4447  C   THR B 200     8788   4676   3760   -446    424   -707       C  
ATOM   4448  O   THR B 200       4.435  31.370 -29.487  1.00 48.64           O  
ANISOU 4448  O   THR B 200     9280   5041   4159   -411    532   -760       O  
ATOM   4449  N   VAL B 201       3.783  31.839 -27.390  1.00 43.05           N  
ANISOU 4449  N   VAL B 201     8413   4380   3564   -423    409   -688       N  
ATOM   4450  CA  VAL B 201       5.016  31.349 -26.781  1.00 39.75           C  
ANISOU 4450  CA  VAL B 201     7971   3891   3240   -351    528   -728       C  
ATOM   4451  CB  VAL B 201       5.201  31.925 -25.361  1.00 43.06           C  
ANISOU 4451  CB  VAL B 201     8272   4335   3755   -322    513   -686       C  
ATOM   4452  CG1 VAL B 201       6.483  31.410 -24.738  1.00 48.63           C  
ANISOU 4452  CG1 VAL B 201     8937   4967   4574   -243    640   -724       C  
ATOM   4453  CG2 VAL B 201       5.199  33.429 -25.413  1.00 44.71           C  
ANISOU 4453  CG2 VAL B 201     8424   4632   3931   -316    520   -621       C  
ATOM   4454  C   VAL B 201       5.045  29.830 -26.701  1.00 40.46           C  
ANISOU 4454  C   VAL B 201     8116   3891   3366   -355    524   -790       C  
ATOM   4455  O   VAL B 201       4.096  29.209 -26.227  1.00 42.16           O  
ANISOU 4455  O   VAL B 201     8328   4099   3590   -408    403   -785       O  
ATOM   4456  N   ARG B 202       6.140  29.236 -27.159  1.00 38.17           N  
ANISOU 4456  N   ARG B 202     7869   3536   3100   -298    656   -841       N  
ATOM   4457  CA  ARG B 202       6.295  27.793 -27.089  1.00 38.81           C  
ANISOU 4457  CA  ARG B 202     7995   3528   3221   -292    668   -897       C  
ATOM   4458  CB  ARG B 202       6.945  27.262 -28.362  1.00 51.26           C  
ANISOU 4458  CB  ARG B 202     9679   5060   4737   -268    770   -948       C  
ATOM   4459  CG  ARG B 202       6.191  27.653 -29.611  1.00 58.15           C  
ANISOU 4459  CG  ARG B 202    10643   5977   5475   -327    717   -945       C  
ATOM   4460  CD  ARG B 202       6.615  26.793 -30.782  1.00 73.29           C  
ANISOU 4460  CD  ARG B 202    12681   7832   7333   -315    790  -1006       C  
ATOM   4461  NE  ARG B 202       7.868  26.100 -30.505  1.00 84.61           N  
ANISOU 4461  NE  ARG B 202    14101   9195   8851   -234    920  -1040       N  
ATOM   4462  CZ  ARG B 202       8.535  25.378 -31.397  1.00 89.55           C  
ANISOU 4462  CZ  ARG B 202    14817   9763   9445   -201   1012  -1089       C  
ATOM   4463  NH1 ARG B 202       8.063  25.245 -32.626  1.00 90.71           N  
ANISOU 4463  NH1 ARG B 202    15079   9910   9475   -243    987  -1113       N  
ATOM   4464  NH2 ARG B 202       9.668  24.782 -31.057  1.00 91.84           N  
ANISOU 4464  NH2 ARG B 202    15078   9995   9821   -124   1127  -1109       N  
ATOM   4465  C   ARG B 202       7.110  27.405 -25.873  1.00 44.20           C  
ANISOU 4465  C   ARG B 202     8582   4164   4046   -226    728   -900       C  
ATOM   4466  O   ARG B 202       8.272  27.800 -25.730  1.00 39.11           O  
ANISOU 4466  O   ARG B 202     7885   3514   3460   -153    855   -896       O  
ATOM   4467  N   ILE B 203       6.485  26.616 -25.005  1.00 35.91           N  
ANISOU 4467  N   ILE B 203     7503   3084   3058   -254    633   -903       N  
ATOM   4468  CA  ILE B 203       7.028  26.303 -23.696  1.00 41.16           C  
ANISOU 4468  CA  ILE B 203     8057   3712   3868   -201    659   -894       C  
ATOM   4469  CB  ILE B 203       6.063  26.757 -22.571  1.00 36.35           C  
ANISOU 4469  CB  ILE B 203     7366   3147   3300   -244    519   -843       C  
ATOM   4470  CG1 ILE B 203       5.793  28.261 -22.653  1.00 41.15           C  
ANISOU 4470  CG1 ILE B 203     7945   3846   3845   -260    494   -791       C  
ATOM   4471  CD1 ILE B 203       4.615  28.717 -21.775  1.00 33.52           C  
ANISOU 4471  CD1 ILE B 203     6887   2950   2899   -314    330   -719       C  
ATOM   4472  CG2 ILE B 203       6.588  26.346 -21.190  1.00 36.09           C  
ANISOU 4472  CG2 ILE B 203     7214   3070   3429   -188    539   -832       C  
ATOM   4473  C   ILE B 203       7.267  24.812 -23.563  1.00 39.21           C  
ANISOU 4473  C   ILE B 203     7836   3379   3682   -184    680   -941       C  
ATOM   4474  O   ILE B 203       6.391  24.015 -23.873  1.00 41.17           O  
ANISOU 4474  O   ILE B 203     8157   3605   3882   -246    588   -962       O  
ATOM   4475  N   VAL B 204       8.447  24.436 -23.088  1.00 40.35           N  
ANISOU 4475  N   VAL B 204     7916   3479   3936   -100    799   -951       N  
ATOM   4476  CA  VAL B 204       8.695  23.040 -22.760  1.00 45.18           C  
ANISOU 4476  CA  VAL B 204     8530   4013   4623    -77    816   -986       C  
ATOM   4477  CB  VAL B 204       9.888  22.468 -23.532  1.00 47.12           C  
ANISOU 4477  CB  VAL B 204     8825   4212   4867    -10    967  -1025       C  
ATOM   4478  CG1 VAL B 204      10.048  20.991 -23.206  1.00 48.60           C  
ANISOU 4478  CG1 VAL B 204     9023   4321   5124     10    974  -1060       C  
ATOM   4479  CG2 VAL B 204       9.695  22.660 -25.026  1.00 46.35           C  
ANISOU 4479  CG2 VAL B 204     8868   4125   4619    -46    985  -1055       C  
ATOM   4480  C   VAL B 204       8.950  22.866 -21.274  1.00 42.25           C  
ANISOU 4480  C   VAL B 204     8014   3629   4408    -34    803   -953       C  
ATOM   4481  O   VAL B 204       9.858  23.478 -20.712  1.00 41.16           O  
ANISOU 4481  O   VAL B 204     7774   3512   4355     33    888   -923       O  
ATOM   4482  N   VAL B 205       8.143  22.019 -20.646  1.00 36.59           N  
ANISOU 4482  N   VAL B 205     7287   2883   3734    -74    696   -954       N  
ATOM   4483  CA  VAL B 205       8.308  21.697 -19.238  1.00 39.97           C  
ANISOU 4483  CA  VAL B 205     7578   3293   4314    -36    674   -922       C  
ATOM   4484  CB  VAL B 205       6.959  21.652 -18.519  1.00 39.07           C  
ANISOU 4484  CB  VAL B 205     7438   3199   4208   -111    502   -890       C  
ATOM   4485  CG1 VAL B 205       7.145  21.318 -17.035  1.00 31.96           C  
ANISOU 4485  CG1 VAL B 205     6389   2282   3472    -67    480   -850       C  
ATOM   4486  CG2 VAL B 205       6.223  22.983 -18.708  1.00 36.29           C  
ANISOU 4486  CG2 VAL B 205     7096   2924   3767   -164    423   -851       C  
ATOM   4487  C   VAL B 205       9.010  20.349 -19.108  1.00 38.88           C  
ANISOU 4487  C   VAL B 205     7437   3083   4254     16    748   -957       C  
ATOM   4488  O   VAL B 205       8.512  19.347 -19.600  1.00 43.85           O  
ANISOU 4488  O   VAL B 205     8160   3666   4835    -25    708   -997       O  
ATOM   4489  N   ASN B 206      10.170  20.336 -18.456  1.00 40.41           N  
ANISOU 4489  N   ASN B 206     7519   3270   4565    104    855   -938       N  
ATOM   4490  CA  ASN B 206      10.943  19.107 -18.304  1.00 46.10           C  
ANISOU 4490  CA  ASN B 206     8225   3929   5361    162    932   -964       C  
ATOM   4491  CB  ASN B 206      12.394  19.325 -18.745  1.00 44.73           C  
ANISOU 4491  CB  ASN B 206     8031   3760   5205    246   1097   -967       C  
ATOM   4492  CG  ASN B 206      13.163  18.020 -18.893  1.00 47.97           C  
ANISOU 4492  CG  ASN B 206     8463   4106   5658    299   1181   -999       C  
ATOM   4493  OD1 ASN B 206      12.620  17.015 -19.353  1.00 45.61           O  
ANISOU 4493  OD1 ASN B 206     8271   3752   5309    261   1140  -1044       O  
ATOM   4494  ND2 ASN B 206      14.427  18.029 -18.489  1.00 48.95           N  
ANISOU 4494  ND2 ASN B 206     8484   4240   5874    385   1295   -973       N  
ATOM   4495  C   ASN B 206      10.893  18.607 -16.865  1.00 38.01           C  
ANISOU 4495  C   ASN B 206     7061   2894   4487    189    884   -928       C  
ATOM   4496  O   ASN B 206      11.506  19.186 -15.963  1.00 43.74           O  
ANISOU 4496  O   ASN B 206     7646   3657   5318    244    919   -879       O  
ATOM   4497  N   GLY B 207      10.146  17.533 -16.653  1.00 39.53           N  
ANISOU 4497  N   GLY B 207     7290   3040   4691    149    800   -948       N  
ATOM   4498  CA  GLY B 207       9.964  16.986 -15.325  1.00 39.65           C  
ANISOU 4498  CA  GLY B 207     7179   3044   4842    167    741   -913       C  
ATOM   4499  C   GLY B 207       8.487  16.892 -15.022  1.00 45.80           C  
ANISOU 4499  C   GLY B 207     7982   3828   5592     76    577   -900       C  
ATOM   4500  O   GLY B 207       7.729  17.804 -15.356  1.00 51.02           O  
ANISOU 4500  O   GLY B 207     8683   4535   6166     15    502   -885       O  
ATOM   4501  N   ALA B 208       8.070  15.796 -14.394  1.00 43.45           N  
ANISOU 4501  N   ALA B 208     7656   3488   5364     65    517   -901       N  
ATOM   4502  CA  ALA B 208       6.648  15.544 -14.195  1.00 43.00           C  
ANISOU 4502  CA  ALA B 208     7629   3434   5275    -27    361   -889       C  
ATOM   4503  CB  ALA B 208       6.230  14.306 -14.966  1.00 46.78           C  
ANISOU 4503  CB  ALA B 208     8238   3848   5690    -73    345   -947       C  
ATOM   4504  C   ALA B 208       6.268  15.394 -12.727  1.00 41.53           C  
ANISOU 4504  C   ALA B 208     7292   3261   5225    -16    279   -828       C  
ATOM   4505  O   ALA B 208       5.329  14.673 -12.397  1.00 55.87           O  
ANISOU 4505  O   ALA B 208     9114   5059   7054    -71    174   -821       O  
ATOM   4506  N   GLY B 209       6.980  16.085 -11.847  1.00 46.16           N  
ANISOU 4506  N   GLY B 209     7741   3885   5913     54    325   -780       N  
ATOM   4507  CA  GLY B 209       6.693  16.015 -10.427  1.00 35.44           C  
ANISOU 4507  CA  GLY B 209     6231   2548   4687     73    252   -716       C  
ATOM   4508  C   GLY B 209       5.531  16.889  -9.980  1.00 42.60           C  
ANISOU 4508  C   GLY B 209     7104   3514   5568      8    108   -657       C  
ATOM   4509  O   GLY B 209       4.678  17.284 -10.780  1.00 42.71           O  
ANISOU 4509  O   GLY B 209     7225   3548   5455    -71     36   -669       O  
ATOM   4510  N   ALA B 210       5.510  17.201  -8.690  1.00 31.32           N  
ANISOU 4510  N   ALA B 210     5520   2121   4258     45     64   -588       N  
ATOM   4511  CA  ALA B 210       4.343  17.819  -8.077  1.00 36.84           C  
ANISOU 4511  CA  ALA B 210     6167   2879   4952    -11    -89   -519       C  
ATOM   4512  CB  ALA B 210       4.517  17.875  -6.569  1.00 37.96           C  
ANISOU 4512  CB  ALA B 210     6123   3054   5247     48   -117   -446       C  
ATOM   4513  C   ALA B 210       4.027  19.215  -8.609  1.00 33.66           C  
ANISOU 4513  C   ALA B 210     5788   2555   4446    -45   -124   -493       C  
ATOM   4514  O   ALA B 210       2.889  19.667  -8.494  1.00 25.27           O  
ANISOU 4514  O   ALA B 210     4710   1558   3335   -111   -258   -444       O  
ATOM   4515  N   SER B 211       5.006  19.914  -9.183  1.00 33.34           N  
ANISOU 4515  N   SER B 211     5763   2530   4374     -1     -4   -517       N  
ATOM   4516  CA  SER B 211       4.724  21.279  -9.625  1.00 33.72           C  
ANISOU 4516  CA  SER B 211     5805   2674   4334    -30    -33   -482       C  
ATOM   4517  CB  SER B 211       5.840  22.230  -9.159  1.00 31.01           C  
ANISOU 4517  CB  SER B 211     5336   2384   4062     50     65   -446       C  
ATOM   4518  OG  SER B 211       7.117  21.639  -9.321  1.00 50.81           O  
ANISOU 4518  OG  SER B 211     7860   4820   6625    122    216   -498       O  
ATOM   4519  C   SER B 211       4.504  21.420 -11.137  1.00 35.28           C  
ANISOU 4519  C   SER B 211     6185   2852   4367    -87    -10   -545       C  
ATOM   4520  O   SER B 211       4.143  22.493 -11.609  1.00 29.91           O  
ANISOU 4520  O   SER B 211     5517   2248   3599   -120    -42   -518       O  
ATOM   4521  N   ALA B 212       4.671  20.340 -11.891  1.00 33.33           N  
ANISOU 4521  N   ALA B 212     6084   2503   4077   -101     43   -627       N  
ATOM   4522  CA  ALA B 212       4.652  20.439 -13.351  1.00 36.79           C  
ANISOU 4522  CA  ALA B 212     6700   2916   4362   -143     87   -694       C  
ATOM   4523  CB  ALA B 212       5.066  19.106 -13.970  1.00 36.45           C  
ANISOU 4523  CB  ALA B 212     6740   2799   4311   -131    161   -764       C  
ATOM   4524  C   ALA B 212       3.305  20.895 -13.934  1.00 34.01           C  
ANISOU 4524  C   ALA B 212     6422   2621   3880   -245    -53   -676       C  
ATOM   4525  O   ALA B 212       3.258  21.874 -14.679  1.00 32.53           O  
ANISOU 4525  O   ALA B 212     6275   2493   3591   -264    -40   -671       O  
ATOM   4526  N   ASN B 213       2.222  20.190 -13.612  1.00 33.11           N  
ANISOU 4526  N   ASN B 213     6312   2499   3768   -310   -182   -660       N  
ATOM   4527  CA  ASN B 213       0.900  20.555 -14.119  1.00 33.86           C  
ANISOU 4527  CA  ASN B 213     6467   2655   3744   -408   -320   -635       C  
ATOM   4528  CB  ASN B 213      -0.145  19.539 -13.663  1.00 39.85           C  
ANISOU 4528  CB  ASN B 213     7201   3406   4533   -465   -441   -612       C  
ATOM   4529  CG  ASN B 213      -0.326  18.402 -14.655  1.00 50.15           C  
ANISOU 4529  CG  ASN B 213     8635   4655   5764   -506   -420   -680       C  
ATOM   4530  OD1 ASN B 213       0.540  18.150 -15.496  1.00 48.19           O  
ANISOU 4530  OD1 ASN B 213     8476   4357   5475   -473   -297   -748       O  
ATOM   4531  ND2 ASN B 213      -1.457  17.710 -14.561  1.00 52.93           N  
ANISOU 4531  ND2 ASN B 213     8994   5019   6100   -578   -540   -658       N  
ATOM   4532  C   ASN B 213       0.459  21.958 -13.697  1.00 30.03           C  
ANISOU 4532  C   ASN B 213     5875   2287   3248   -413   -389   -548       C  
ATOM   4533  O   ASN B 213      -0.177  22.678 -14.475  1.00 31.73           O  
ANISOU 4533  O   ASN B 213     6156   2562   3337   -470   -440   -538       O  
ATOM   4534  N   SER B 214       0.794  22.361 -12.478  1.00 26.64           N  
ANISOU 4534  N   SER B 214     5271   1901   2949   -351   -388   -481       N  
ATOM   4535  CA  SER B 214       0.363  23.668 -12.010  1.00 23.23           C  
ANISOU 4535  CA  SER B 214     4727   1587   2514   -350   -453   -393       C  
ATOM   4536  CB  SER B 214       0.640  23.836 -10.520  1.00 26.76           C  
ANISOU 4536  CB  SER B 214     4984   2066   3117   -284   -467   -324       C  
ATOM   4537  OG  SER B 214       0.089  25.054 -10.060  1.00 36.61           O  
ANISOU 4537  OG  SER B 214     6133   3423   4352   -289   -543   -237       O  
ATOM   4538  C   SER B 214       1.045  24.788 -12.805  1.00 27.42           C  
ANISOU 4538  C   SER B 214     5290   2159   2968   -325   -357   -405       C  
ATOM   4539  O   SER B 214       0.450  25.829 -13.050  1.00 27.08           O  
ANISOU 4539  O   SER B 214     5238   2203   2848   -357   -416   -356       O  
ATOM   4540  N   CYS B 215       2.284  24.549 -13.217  1.00 24.50           N  
ANISOU 4540  N   CYS B 215     4962   1728   2620   -267   -207   -467       N  
ATOM   4541  CA  CYS B 215       2.985  25.477 -14.099  1.00 24.22           C  
ANISOU 4541  CA  CYS B 215     4976   1719   2506   -245   -105   -487       C  
ATOM   4542  CB  CYS B 215       4.404  24.982 -14.405  1.00 30.38           C  
ANISOU 4542  CB  CYS B 215     5790   2420   3332   -173     64   -554       C  
ATOM   4543  SG  CYS B 215       5.590  25.223 -13.056  1.00 30.37           S  
ANISOU 4543  SG  CYS B 215     5590   2431   3517    -69    148   -507       S  
ATOM   4544  C   CYS B 215       2.201  25.657 -15.395  1.00 26.87           C  
ANISOU 4544  C   CYS B 215     5472   2068   2670   -325   -151   -520       C  
ATOM   4545  O   CYS B 215       1.911  26.784 -15.802  1.00 28.08           O  
ANISOU 4545  O   CYS B 215     5625   2301   2742   -345   -171   -482       O  
ATOM   4546  N   ALA B 216       1.850  24.545 -16.030  1.00 31.68           N  
ANISOU 4546  N   ALA B 216     6217   2598   3220   -372   -168   -588       N  
ATOM   4547  CA  ALA B 216       1.106  24.601 -17.279  1.00 33.74           C  
ANISOU 4547  CA  ALA B 216     6640   2866   3315   -452   -214   -624       C  
ATOM   4548  CB  ALA B 216       0.851  23.197 -17.800  1.00 35.84           C  
ANISOU 4548  CB  ALA B 216     7029   3039   3548   -493   -225   -696       C  
ATOM   4549  C   ALA B 216      -0.209  25.371 -17.101  1.00 31.91           C  
ANISOU 4549  C   ALA B 216     6363   2737   3023   -520   -369   -545       C  
ATOM   4550  O   ALA B 216      -0.537  26.238 -17.906  1.00 31.72           O  
ANISOU 4550  O   ALA B 216     6397   2774   2880   -552   -381   -533       O  
ATOM   4551  N   LYS B 217      -0.945  25.075 -16.034  1.00 30.76           N  
ANISOU 4551  N   LYS B 217     6111   2613   2961   -537   -483   -485       N  
ATOM   4552  CA  LYS B 217      -2.219  25.742 -15.793  1.00 34.17           C  
ANISOU 4552  CA  LYS B 217     6495   3145   3345   -596   -631   -402       C  
ATOM   4553  CB  LYS B 217      -2.937  25.099 -14.601  1.00 42.11           C  
ANISOU 4553  CB  LYS B 217     7393   4150   4455   -610   -745   -349       C  
ATOM   4554  CG  LYS B 217      -3.743  23.865 -14.985  1.00 49.31           C  
ANISOU 4554  CG  LYS B 217     8411   5003   5323   -690   -827   -390       C  
ATOM   4555  CD  LYS B 217      -4.171  23.039 -13.775  1.00 54.54           C  
ANISOU 4555  CD  LYS B 217     8966   5645   6113   -686   -905   -348       C  
ATOM   4556  CE  LYS B 217      -3.403  21.716 -13.710  1.00 58.82           C  
ANISOU 4556  CE  LYS B 217     9545   6072   6733   -652   -816   -423       C  
ATOM   4557  NZ  LYS B 217      -3.833  20.834 -12.579  1.00 53.80           N  
ANISOU 4557  NZ  LYS B 217     8805   5417   6218   -648   -887   -383       N  
ATOM   4558  C   LYS B 217      -2.066  27.243 -15.569  1.00 35.91           C  
ANISOU 4558  C   LYS B 217     6618   3466   3559   -558   -616   -331       C  
ATOM   4559  O   LYS B 217      -2.849  28.029 -16.089  1.00 32.31           O  
ANISOU 4559  O   LYS B 217     6196   3088   2995   -606   -684   -292       O  
ATOM   4560  N   ILE B 218      -1.062  27.645 -14.798  1.00 25.62           N  
ANISOU 4560  N   ILE B 218     5197   2164   2372   -473   -527   -312       N  
ATOM   4561  CA  ILE B 218      -0.812  29.059 -14.589  1.00 27.05           C  
ANISOU 4561  CA  ILE B 218     5294   2432   2553   -436   -502   -250       C  
ATOM   4562  CB  ILE B 218       0.268  29.275 -13.512  1.00 22.97           C  
ANISOU 4562  CB  ILE B 218     4631   1906   2189   -346   -420   -228       C  
ATOM   4563  CG1 ILE B 218      -0.298  28.901 -12.144  1.00 27.00           C  
ANISOU 4563  CG1 ILE B 218     5009   2433   2815   -338   -522   -166       C  
ATOM   4564  CD1 ILE B 218      -1.320  29.918 -11.638  1.00 29.41           C  
ANISOU 4564  CD1 ILE B 218     5234   2845   3095   -360   -641    -68       C  
ATOM   4565  CG2 ILE B 218       0.695  30.737 -13.477  1.00 28.05           C  
ANISOU 4565  CG2 ILE B 218     5211   2626   2821   -310   -373   -179       C  
ATOM   4566  C   ILE B 218      -0.405  29.763 -15.895  1.00 27.59           C  
ANISOU 4566  C   ILE B 218     5478   2513   2493   -445   -417   -290       C  
ATOM   4567  O   ILE B 218      -0.863  30.879 -16.178  1.00 29.05           O  
ANISOU 4567  O   ILE B 218     5656   2781   2602   -462   -453   -238       O  
ATOM   4568  N   PHE B 219       0.439  29.121 -16.694  1.00 24.83           N  
ANISOU 4568  N   PHE B 219     5235   2081   2117   -429   -303   -379       N  
ATOM   4569  CA  PHE B 219       0.873  29.743 -17.944  1.00 31.19           C  
ANISOU 4569  CA  PHE B 219     6153   2895   2802   -432   -215   -418       C  
ATOM   4570  CB  PHE B 219       1.934  28.895 -18.650  1.00 25.94           C  
ANISOU 4570  CB  PHE B 219     5593   2129   2134   -399    -77   -516       C  
ATOM   4571  CG  PHE B 219       3.201  28.699 -17.858  1.00 30.02           C  
ANISOU 4571  CG  PHE B 219     6004   2603   2799   -310     37   -521       C  
ATOM   4572  CD1 PHE B 219       3.543  29.558 -16.822  1.00 29.20           C  
ANISOU 4572  CD1 PHE B 219     5735   2561   2801   -262     39   -448       C  
ATOM   4573  CE1 PHE B 219       4.706  29.359 -16.092  1.00 32.64           C  
ANISOU 4573  CE1 PHE B 219     6070   2961   3371   -183    140   -451       C  
ATOM   4574  CZ  PHE B 219       5.537  28.287 -16.399  1.00 29.50           C  
ANISOU 4574  CZ  PHE B 219     5737   2466   3004   -148    245   -527       C  
ATOM   4575  CE2 PHE B 219       5.205  27.435 -17.427  1.00 35.86           C  
ANISOU 4575  CE2 PHE B 219     6713   3208   3706   -192    247   -601       C  
ATOM   4576  CD2 PHE B 219       4.043  27.640 -18.151  1.00 30.74           C  
ANISOU 4576  CD2 PHE B 219     6164   2594   2921   -275    142   -600       C  
ATOM   4577  C   PHE B 219      -0.325  29.969 -18.881  1.00 35.47           C  
ANISOU 4577  C   PHE B 219     6810   3483   3184   -520   -316   -413       C  
ATOM   4578  O   PHE B 219      -0.429  31.006 -19.548  1.00 30.16           O  
ANISOU 4578  O   PHE B 219     6170   2874   2415   -529   -302   -390       O  
ATOM   4579  N   ILE B 220      -1.233  29.002 -18.915  1.00 31.71           N  
ANISOU 4579  N   ILE B 220     6391   2976   2680   -584   -420   -430       N  
ATOM   4580  CA  ILE B 220      -2.458  29.124 -19.699  1.00 34.59           C  
ANISOU 4580  CA  ILE B 220     6826   3397   2920   -666   -526   -406       C  
ATOM   4581  CB  ILE B 220      -3.220  27.788 -19.741  1.00 40.94           C  
ANISOU 4581  CB  ILE B 220     7659   4154   3741   -720   -604   -423       C  
ATOM   4582  CG1 ILE B 220      -2.418  26.748 -20.525  1.00 33.18           C  
ANISOU 4582  CG1 ILE B 220     6798   3067   2741   -707   -497   -526       C  
ATOM   4583  CD1 ILE B 220      -2.958  25.338 -20.411  1.00 37.37           C  
ANISOU 4583  CD1 ILE B 220     7355   3537   3306   -749   -557   -550       C  
ATOM   4584  CG2 ILE B 220      -4.590  27.964 -20.373  1.00 43.94           C  
ANISOU 4584  CG2 ILE B 220     8033   4611   4050   -789   -708   -361       C  
ATOM   4585  C   ILE B 220      -3.359  30.226 -19.141  1.00 38.08           C  
ANISOU 4585  C   ILE B 220     7146   3955   3366   -677   -627   -293       C  
ATOM   4586  O   ILE B 220      -3.964  30.987 -19.897  1.00 36.00           O  
ANISOU 4586  O   ILE B 220     6878   3766   3036   -700   -644   -248       O  
ATOM   4587  N   ALA B 221      -3.429  30.333 -17.817  1.00 29.47           N  
ANISOU 4587  N   ALA B 221     5941   2882   2375   -652   -685   -244       N  
ATOM   4588  CA  ALA B 221      -4.168  31.424 -17.185  1.00 27.87           C  
ANISOU 4588  CA  ALA B 221     5606   2789   2196   -645   -763   -131       C  
ATOM   4589  CB  ALA B 221      -4.214  31.232 -15.676  1.00 32.68           C  
ANISOU 4589  CB  ALA B 221     6076   3403   2940   -610   -821    -79       C  
ATOM   4590  C   ALA B 221      -3.561  32.787 -17.524  1.00 37.33           C  
ANISOU 4590  C   ALA B 221     6792   4041   3351   -603   -681   -109       C  
ATOM   4591  O   ALA B 221      -4.243  33.812 -17.473  1.00 36.63           O  
ANISOU 4591  O   ALA B 221     6600   4042   3278   -597   -714    -25       O  
ATOM   4592  N   LEU B 222      -2.276  32.795 -17.857  1.00 31.34           N  
ANISOU 4592  N   LEU B 222     6074   3225   2607   -553   -542   -174       N  
ATOM   4593  CA  LEU B 222      -1.586  34.026 -18.208  1.00 35.04           C  
ANISOU 4593  CA  LEU B 222     6529   3735   3047   -511   -448   -157       C  
ATOM   4594  CB  LEU B 222      -0.118  33.944 -17.803  1.00 35.04           C  
ANISOU 4594  CB  LEU B 222     6470   3678   3164   -432   -307   -193       C  
ATOM   4595  CG  LEU B 222       0.093  33.942 -16.297  1.00 37.19           C  
ANISOU 4595  CG  LEU B 222     6576   3959   3598   -383   -334   -139       C  
ATOM   4596  CD1 LEU B 222       1.554  33.679 -15.982  1.00 38.45           C  
ANISOU 4596  CD1 LEU B 222     6687   4056   3868   -311   -194   -183       C  
ATOM   4597  CD2 LEU B 222      -0.359  35.278 -15.730  1.00 37.54           C  
ANISOU 4597  CD2 LEU B 222     6522   4100   3643   -373   -390    -44       C  
ATOM   4598  C   LEU B 222      -1.697  34.327 -19.694  1.00 38.72           C  
ANISOU 4598  C   LEU B 222     7141   4212   3359   -549   -410   -196       C  
ATOM   4599  O   LEU B 222      -1.259  35.385 -20.151  1.00 38.48           O  
ANISOU 4599  O   LEU B 222     7102   4222   3296   -522   -338   -177       O  
ATOM   4600  N   GLY B 223      -2.268  33.390 -20.448  1.00 35.06           N  
ANISOU 4600  N   GLY B 223     6752   3713   2855   -600   -444   -237       N  
ATOM   4601  CA  GLY B 223      -2.512  33.617 -21.858  1.00 41.88           C  
ANISOU 4601  CA  GLY B 223     7690   4594   3629   -627   -410   -254       C  
ATOM   4602  C   GLY B 223      -1.820  32.668 -22.813  1.00 41.44           C  
ANISOU 4602  C   GLY B 223     7777   4449   3520   -631   -321   -355       C  
ATOM   4603  O   GLY B 223      -1.966  32.806 -24.023  1.00 45.00           O  
ANISOU 4603  O   GLY B 223     8296   4910   3892   -652   -292   -373       O  
ATOM   4604  N   ALA B 224      -1.070  31.706 -22.289  1.00 39.16           N  
ANISOU 4604  N   ALA B 224     7524   4070   3284   -606   -273   -421       N  
ATOM   4605  CA  ALA B 224      -0.436  30.715 -23.151  1.00 32.91           C  
ANISOU 4605  CA  ALA B 224     6851   3188   2464   -602   -183   -513       C  
ATOM   4606  CB  ALA B 224       0.699  30.005 -22.425  1.00 37.22           C  
ANISOU 4606  CB  ALA B 224     7396   3640   3106   -542    -89   -576       C  
ATOM   4607  C   ALA B 224      -1.471  29.708 -23.632  1.00 32.79           C  
ANISOU 4607  C   ALA B 224     6888   3157   2415   -672   -279   -523       C  
ATOM   4608  O   ALA B 224      -2.546  29.585 -23.043  1.00 40.21           O  
ANISOU 4608  O   ALA B 224     7761   4137   3379   -716   -408   -466       O  
ATOM   4609  N   ARG B 225      -1.146  29.000 -24.707  1.00 40.75           N  
ANISOU 4609  N   ARG B 225     8011   4107   3366   -679   -214   -592       N  
ATOM   4610  CA  ARG B 225      -2.039  27.972 -25.245  1.00 47.68           C  
ANISOU 4610  CA  ARG B 225     8953   4960   4205   -746   -294   -610       C  
ATOM   4611  CB  ARG B 225      -2.294  28.233 -26.733  1.00 61.12           C  
ANISOU 4611  CB  ARG B 225    10744   6686   5792   -775   -273   -625       C  
ATOM   4612  CG  ARG B 225      -3.420  29.216 -26.991  1.00 69.74           C  
ANISOU 4612  CG  ARG B 225    11773   7884   6841   -818   -369   -543       C  
ATOM   4613  CD  ARG B 225      -3.168  30.067 -28.237  1.00 80.93           C  
ANISOU 4613  CD  ARG B 225    13241   9339   8170   -807   -301   -549       C  
ATOM   4614  NE  ARG B 225      -4.283  30.943 -28.624  1.00 88.86           N  
ANISOU 4614  NE  ARG B 225    14185  10440   9137   -846   -386   -477       N  
ATOM   4615  CZ  ARG B 225      -4.993  31.732 -27.811  1.00 94.60           C  
ANISOU 4615  CZ  ARG B 225    14782  11245   9917   -848   -464   -393       C  
ATOM   4616  NH1 ARG B 225      -4.721  31.830 -26.513  1.00 95.98           N  
ANISOU 4616  NH1 ARG B 225    14871  11418  10180   -817   -476   -365       N  
ATOM   4617  NH2 ARG B 225      -5.977  32.463 -28.316  1.00 95.41           N  
ANISOU 4617  NH2 ARG B 225    14833  11430   9987   -876   -524   -337       N  
ATOM   4618  C   ARG B 225      -1.509  26.550 -25.049  1.00 40.67           C  
ANISOU 4618  C   ARG B 225     8122   3963   3367   -732   -252   -685       C  
ATOM   4619  O   ARG B 225      -0.304  26.327 -25.121  1.00 41.99           O  
ANISOU 4619  O   ARG B 225     8323   4067   3566   -668   -122   -742       O  
ATOM   4620  N   ARG B 226      -2.413  25.594 -24.812  1.00 47.58           N  
ANISOU 4620  N   ARG B 226     9002   4819   4259   -789   -356   -680       N  
ATOM   4621  CA  ARG B 226      -2.031  24.182 -24.645  1.00 48.83           C  
ANISOU 4621  CA  ARG B 226     9210   4874   4467   -781   -325   -747       C  
ATOM   4622  CB  ARG B 226      -3.253  23.269 -24.517  1.00 50.61           C  
ANISOU 4622  CB  ARG B 226     9440   5097   4693   -859   -458   -727       C  
ATOM   4623  CG  ARG B 226      -4.475  23.880 -23.878  1.00 53.42           C  
ANISOU 4623  CG  ARG B 226     9690   5546   5061   -907   -598   -631       C  
ATOM   4624  CD  ARG B 226      -5.589  22.847 -23.776  1.00 59.04           C  
ANISOU 4624  CD  ARG B 226    10407   6245   5780   -978   -713   -615       C  
ATOM   4625  NE  ARG B 226      -5.463  22.018 -22.579  1.00 63.11           N  
ANISOU 4625  NE  ARG B 226    10860   6709   6411   -961   -739   -617       N  
ATOM   4626  CZ  ARG B 226      -4.978  20.779 -22.561  1.00 61.18           C  
ANISOU 4626  CZ  ARG B 226    10674   6366   6204   -950   -693   -686       C  
ATOM   4627  NH1 ARG B 226      -4.562  20.204 -23.681  1.00 61.85           N  
ANISOU 4627  NH1 ARG B 226    10890   6392   6218   -954   -619   -760       N  
ATOM   4628  NH2 ARG B 226      -4.911  20.114 -21.415  1.00 57.05           N  
ANISOU 4628  NH2 ARG B 226    10076   5804   5797   -930   -719   -678       N  
ATOM   4629  C   ARG B 226      -1.182  23.673 -25.800  1.00 51.72           C  
ANISOU 4629  C   ARG B 226     9702   5174   4776   -754   -202   -827       C  
ATOM   4630  O   ARG B 226      -0.185  22.988 -25.585  1.00 54.44           O  
ANISOU 4630  O   ARG B 226    10065   5437   5182   -697   -101   -882       O  
ATOM   4631  N   GLU B 227      -1.582  24.022 -27.022  1.00 54.21           N  
ANISOU 4631  N   GLU B 227    10096   5525   4978   -792   -209   -829       N  
ATOM   4632  CA  GLU B 227      -0.919  23.548 -28.239  1.00 60.74           C  
ANISOU 4632  CA  GLU B 227    11048   6295   5735   -774   -106   -901       C  
ATOM   4633  CB  GLU B 227      -1.633  24.068 -29.493  1.00 68.74           C  
ANISOU 4633  CB  GLU B 227    12128   7366   6626   -828   -147   -886       C  
ATOM   4634  CG  GLU B 227      -3.044  23.529 -29.719  1.00 81.37           C  
ANISOU 4634  CG  GLU B 227    13747   8987   8183   -921   -290   -862       C  
ATOM   4635  CD  GLU B 227      -4.056  24.069 -28.724  1.00 89.24           C  
ANISOU 4635  CD  GLU B 227    14617  10062   9229   -957   -416   -775       C  
ATOM   4636  OE1 GLU B 227      -3.775  25.110 -28.091  1.00 90.08           O  
ANISOU 4636  OE1 GLU B 227    14629  10222   9375   -917   -400   -727       O  
ATOM   4637  OE2 GLU B 227      -5.133  23.453 -28.576  1.00 93.07           O  
ANISOU 4637  OE2 GLU B 227    15094  10554   9715  -1025   -530   -750       O  
ATOM   4638  C   GLU B 227       0.540  23.984 -28.275  1.00 55.31           C  
ANISOU 4638  C   GLU B 227    10357   5579   5079   -682     53   -931       C  
ATOM   4639  O   GLU B 227       1.349  23.440 -29.027  1.00 55.85           O  
ANISOU 4639  O   GLU B 227    10513   5586   5124   -645    160   -992       O  
ATOM   4640  N   ASN B 228       0.857  24.973 -27.448  1.00 48.81           N  
ANISOU 4640  N   ASN B 228     9429   4805   4312   -643     67   -885       N  
ATOM   4641  CA  ASN B 228       2.172  25.588 -27.416  1.00 43.96           C  
ANISOU 4641  CA  ASN B 228     8791   4180   3731   -558    212   -898       C  
ATOM   4642  CB  ASN B 228       2.013  27.103 -27.298  1.00 48.40           C  
ANISOU 4642  CB  ASN B 228     9283   4839   4269   -556    195   -833       C  
ATOM   4643  CG  ASN B 228       1.575  27.749 -28.601  1.00 60.15           C  
ANISOU 4643  CG  ASN B 228    10836   6382   5635   -592    185   -821       C  
ATOM   4644  OD1 ASN B 228       2.271  28.606 -29.144  1.00 70.60           O  
ANISOU 4644  OD1 ASN B 228    12164   7732   6929   -550    278   -817       O  
ATOM   4645  ND2 ASN B 228       0.437  27.315 -29.127  1.00 63.86           N  
ANISOU 4645  ND2 ASN B 228    11355   6868   6042   -667     75   -816       N  
ATOM   4646  C   ASN B 228       3.030  25.059 -26.272  1.00 45.98           C  
ANISOU 4646  C   ASN B 228     8976   4375   4120   -493    275   -916       C  
ATOM   4647  O   ASN B 228       4.197  25.429 -26.136  1.00 44.25           O  
ANISOU 4647  O   ASN B 228     8724   4140   3950   -416    403   -926       O  
ATOM   4648  N   ILE B 229       2.437  24.204 -25.445  1.00 43.07           N  
ANISOU 4648  N   ILE B 229     8573   3974   3816   -523    185   -914       N  
ATOM   4649  CA  ILE B 229       3.122  23.656 -24.283  1.00 40.66           C  
ANISOU 4649  CA  ILE B 229     8187   3613   3649   -465    230   -923       C  
ATOM   4650  CB  ILE B 229       2.312  23.908 -22.989  1.00 39.44           C  
ANISOU 4650  CB  ILE B 229     7921   3498   3568   -495    101   -864       C  
ATOM   4651  CG1 ILE B 229       2.139  25.413 -22.750  1.00 40.73           C  
ANISOU 4651  CG1 ILE B 229     8019   3752   3703   -495     75   -803       C  
ATOM   4652  CD1 ILE B 229       1.263  25.753 -21.550  1.00 41.61           C  
ANISOU 4652  CD1 ILE B 229     8025   3912   3874   -527    -62   -736       C  
ATOM   4653  CG2 ILE B 229       2.994  23.283 -21.804  1.00 39.51           C  
ANISOU 4653  CG2 ILE B 229     7840   3444   3726   -433    144   -871       C  
ATOM   4654  C   ILE B 229       3.385  22.151 -24.445  1.00 45.81           C  
ANISOU 4654  C   ILE B 229     8900   4171   4335   -455    264   -983       C  
ATOM   4655  O   ILE B 229       2.476  21.374 -24.749  1.00 47.61           O  
ANISOU 4655  O   ILE B 229     9187   4383   4519   -523    170   -994       O  
ATOM   4656  N   ILE B 230       4.640  21.752 -24.258  1.00 44.00           N  
ANISOU 4656  N   ILE B 230     8652   3883   4184   -370    400  -1015       N  
ATOM   4657  CA  ILE B 230       5.018  20.343 -24.311  1.00 49.05           C  
ANISOU 4657  CA  ILE B 230     9335   4434   4868   -348    445  -1067       C  
ATOM   4658  CB  ILE B 230       5.986  20.058 -25.477  1.00 56.54           C  
ANISOU 4658  CB  ILE B 230    10384   5342   5758   -300    584  -1119       C  
ATOM   4659  CG1 ILE B 230       5.396  20.557 -26.799  1.00 58.45           C  
ANISOU 4659  CG1 ILE B 230    10739   5624   5847   -360    551  -1127       C  
ATOM   4660  CD1 ILE B 230       6.280  20.305 -27.995  1.00 58.07           C  
ANISOU 4660  CD1 ILE B 230    10793   5537   5734   -317    679  -1174       C  
ATOM   4661  CG2 ILE B 230       6.311  18.569 -25.550  1.00 58.77           C  
ANISOU 4661  CG2 ILE B 230    10720   5532   6079   -280    623  -1171       C  
ATOM   4662  C   ILE B 230       5.669  19.901 -23.002  1.00 50.01           C  
ANISOU 4662  C   ILE B 230     9336   4517   5149   -282    484  -1055       C  
ATOM   4663  O   ILE B 230       6.664  20.480 -22.569  1.00 49.82           O  
ANISOU 4663  O   ILE B 230     9232   4504   5196   -206    583  -1039       O  
ATOM   4664  N   MET B 231       5.101  18.871 -22.380  1.00 42.25           N  
ANISOU 4664  N   MET B 231     8337   3492   4226   -310    405  -1060       N  
ATOM   4665  CA  MET B 231       5.611  18.347 -21.119  1.00 43.18           C  
ANISOU 4665  CA  MET B 231     8335   3572   4497   -252    429  -1046       C  
ATOM   4666  CB  MET B 231       4.452  17.953 -20.207  1.00 41.79           C  
ANISOU 4666  CB  MET B 231     8103   3405   4371   -314    276  -1011       C  
ATOM   4667  CG  MET B 231       3.279  18.905 -20.281  1.00 47.47           C  
ANISOU 4667  CG  MET B 231     8822   4205   5008   -395    143   -964       C  
ATOM   4668  SD  MET B 231       3.594  20.428 -19.365  1.00 49.50           S  
ANISOU 4668  SD  MET B 231     8946   4534   5326   -353    147   -898       S  
ATOM   4669  CE  MET B 231       3.325  19.829 -17.692  1.00 37.19           C  
ANISOU 4669  CE  MET B 231     7240   2954   3935   -336     70   -854       C  
ATOM   4670  C   MET B 231       6.515  17.143 -21.343  1.00 49.13           C  
ANISOU 4670  C   MET B 231     9128   4243   5297   -193    539  -1097       C  
ATOM   4671  O   MET B 231       6.210  16.275 -22.156  1.00 53.31           O  
ANISOU 4671  O   MET B 231     9774   4726   5754   -229    529  -1143       O  
ATOM   4672  N   CYS B 232       7.624  17.085 -20.616  1.00 52.37           N  
ANISOU 4672  N   CYS B 232     9436   4635   5826   -101    642  -1085       N  
ATOM   4673  CA  CYS B 232       8.521  15.938 -20.714  1.00 53.45           C  
ANISOU 4673  CA  CYS B 232     9593   4700   6017    -38    745  -1124       C  
ATOM   4674  CB  CYS B 232       9.863  16.345 -21.327  1.00 43.80           C  
ANISOU 4674  CB  CYS B 232     8380   3481   4782     43    906  -1135       C  
ATOM   4675  SG  CYS B 232       9.751  17.055 -22.978  1.00 59.86           S  
ANISOU 4675  SG  CYS B 232    10565   5541   6637      4    938  -1164       S  
ATOM   4676  C   CYS B 232       8.753  15.311 -19.350  1.00 59.26           C  
ANISOU 4676  C   CYS B 232    10196   5410   6909      6    734  -1097       C  
ATOM   4677  O   CYS B 232       8.483  15.927 -18.319  1.00 51.43           O  
ANISOU 4677  O   CYS B 232     9083   4463   5997      7    675  -1045       O  
ATOM   4678  N   ASP B 233       9.259  14.083 -19.349  1.00 66.54           N  
ANISOU 4678  N   ASP B 233    11141   6262   7877     45    792  -1131       N  
ATOM   4679  CA  ASP B 233       9.666  13.438 -18.112  1.00 66.21           C  
ANISOU 4679  CA  ASP B 233    10971   6198   7988    100    802  -1105       C  
ATOM   4680  CB  ASP B 233       8.537  12.563 -17.549  1.00 68.35           C  
ANISOU 4680  CB  ASP B 233    11243   6436   8290     35    671  -1106       C  
ATOM   4681  CG  ASP B 233       8.119  11.427 -18.493  1.00 70.62           C  
ANISOU 4681  CG  ASP B 233    11687   6654   8490    -12    658  -1168       C  
ATOM   4682  OD1 ASP B 233       8.787  11.191 -19.524  1.00 62.01           O  
ANISOU 4682  OD1 ASP B 233    10703   5533   7327     15    758  -1212       O  
ATOM   4683  OD2 ASP B 233       7.112  10.751 -18.184  1.00 68.44           O  
ANISOU 4683  OD2 ASP B 233    11427   6354   8222    -78    545  -1170       O  
ATOM   4684  C   ASP B 233      10.919  12.604 -18.323  1.00 69.87           C  
ANISOU 4684  C   ASP B 233    11443   6609   8494    186    942  -1132       C  
ATOM   4685  O   ASP B 233      11.691  12.837 -19.258  1.00 63.53           O  
ANISOU 4685  O   ASP B 233    10710   5805   7624    221   1049  -1154       O  
ATOM   4686  N   SER B 234      11.114  11.647 -17.424  1.00 75.34           N  
ANISOU 4686  N   SER B 234    12061   7264   9300    222    939  -1123       N  
ATOM   4687  CA  SER B 234      12.093  10.578 -17.586  1.00 82.41           C  
ANISOU 4687  CA  SER B 234    12979   8099  10232    292   1048  -1150       C  
ATOM   4688  CB  SER B 234      11.791   9.467 -16.570  1.00 78.66           C  
ANISOU 4688  CB  SER B 234    12439   7581   9866    297    991  -1142       C  
ATOM   4689  OG  SER B 234      10.480   8.957 -16.767  1.00 76.63           O  
ANISOU 4689  OG  SER B 234    12269   7290   9555    202    866  -1168       O  
ATOM   4690  C   SER B 234      12.103  10.000 -19.001  1.00 87.31           C  
ANISOU 4690  C   SER B 234    13786   8664  10723    269   1095  -1215       C  
ATOM   4691  O   SER B 234      13.138   9.963 -19.675  1.00 88.74           O  
ANISOU 4691  O   SER B 234    14009   8833  10874    330   1222  -1231       O  
ATOM   4692  N   GLN B 235      10.934   9.546 -19.443  1.00 87.85           N  
ANISOU 4692  N   GLN B 235    13962   8701  10714    179    989  -1249       N  
ATOM   4693  CA  GLN B 235      10.795   8.819 -20.708  1.00 85.44           C  
ANISOU 4693  CA  GLN B 235    13837   8336  10292    147   1014  -1313       C  
ATOM   4694  CB  GLN B 235       9.522   7.987 -20.695  1.00 88.63           C  
ANISOU 4694  CB  GLN B 235    14311   8697  10667     56    883  -1338       C  
ATOM   4695  CG  GLN B 235       9.489   6.922 -19.630  1.00 90.42           C  
ANISOU 4695  CG  GLN B 235    14461   8877  11019     77    857  -1328       C  
ATOM   4696  CD  GLN B 235       8.511   5.828 -19.973  1.00 95.14           C  
ANISOU 4696  CD  GLN B 235    15170   9409  11569     -1    770  -1369       C  
ATOM   4697  OE1 GLN B 235       8.550   5.264 -21.072  1.00 97.14           O  
ANISOU 4697  OE1 GLN B 235    15576   9611  11723    -19    807  -1424       O  
ATOM   4698  NE2 GLN B 235       7.590   5.553 -19.053  1.00 97.01           N  
ANISOU 4698  NE2 GLN B 235    15333   9651  11875    -52    651  -1341       N  
ATOM   4699  C   GLN B 235      10.778   9.730 -21.935  1.00 83.70           C  
ANISOU 4699  C   GLN B 235    13718   8151   9932    120   1042  -1330       C  
ATOM   4700  O   GLN B 235      10.375   9.313 -23.024  1.00 80.73           O  
ANISOU 4700  O   GLN B 235    13495   7738   9440     72   1030  -1378       O  
ATOM   4701  N   GLY B 236      11.184  10.981 -21.765  1.00 82.15           N  
ANISOU 4701  N   GLY B 236    13439   8027   9747    148   1075  -1289       N  
ATOM   4702  CA  GLY B 236      11.144  11.917 -22.869  1.00 77.22           C  
ANISOU 4702  CA  GLY B 236    12900   7443   8996    122   1097  -1300       C  
ATOM   4703  C   GLY B 236       9.794  12.605 -22.963  1.00 69.62           C  
ANISOU 4703  C   GLY B 236    11963   6529   7960     20    952  -1287       C  
ATOM   4704  O   GLY B 236       9.098  12.765 -21.960  1.00 67.67           O  
ANISOU 4704  O   GLY B 236    11621   6308   7781    -13    850  -1251       O  
ATOM   4705  N   VAL B 237       9.413  12.998 -24.174  1.00 58.87           N  
ANISOU 4705  N   VAL B 237    10728   5183   6459    -29    941  -1313       N  
ATOM   4706  CA  VAL B 237       8.171  13.734 -24.388  1.00 54.05           C  
ANISOU 4706  CA  VAL B 237    10144   4629   5765   -125    809  -1296       C  
ATOM   4707  CB  VAL B 237       8.042  14.163 -25.864  1.00 51.76           C  
ANISOU 4707  CB  VAL B 237     9994   4354   5319   -160    830  -1325       C  
ATOM   4708  CG1 VAL B 237       6.676  14.790 -26.153  1.00 51.86           C  
ANISOU 4708  CG1 VAL B 237    10040   4426   5238   -265    685  -1306       C  
ATOM   4709  CG2 VAL B 237       9.157  15.128 -26.217  1.00 56.74           C  
ANISOU 4709  CG2 VAL B 237    10593   5022   5944    -85    959  -1309       C  
ATOM   4710  C   VAL B 237       6.925  12.943 -23.989  1.00 54.44           C  
ANISOU 4710  C   VAL B 237    10212   4655   5819   -209    664  -1300       C  
ATOM   4711  O   VAL B 237       6.815  11.752 -24.274  1.00 60.59           O  
ANISOU 4711  O   VAL B 237    11070   5362   6589   -222    664  -1342       O  
ATOM   4712  N   ILE B 238       5.993  13.616 -23.317  1.00 51.60           N  
ANISOU 4712  N   ILE B 238     9775   4356   5474   -266    543  -1252       N  
ATOM   4713  CA  ILE B 238       4.664  13.071 -23.067  1.00 52.69           C  
ANISOU 4713  CA  ILE B 238     9932   4491   5597   -359    391  -1245       C  
ATOM   4714  CB  ILE B 238       4.091  13.568 -21.730  1.00 50.36           C  
ANISOU 4714  CB  ILE B 238     9489   4248   5400   -374    293  -1180       C  
ATOM   4715  CG1 ILE B 238       5.010  13.138 -20.586  1.00 52.43           C  
ANISOU 4715  CG1 ILE B 238     9628   4472   5819   -284    367  -1168       C  
ATOM   4716  CD1 ILE B 238       4.571  13.613 -19.214  1.00 44.18           C  
ANISOU 4716  CD1 ILE B 238     8429   3473   4882   -287    282  -1102       C  
ATOM   4717  CG2 ILE B 238       2.675  13.050 -21.529  1.00 50.79           C  
ANISOU 4717  CG2 ILE B 238     9559   4308   5431   -474    133  -1163       C  
ATOM   4718  C   ILE B 238       3.735  13.462 -24.215  1.00 59.78           C  
ANISOU 4718  C   ILE B 238    10947   5427   6340   -448    315  -1254       C  
ATOM   4719  O   ILE B 238       3.164  14.554 -24.229  1.00 54.32           O  
ANISOU 4719  O   ILE B 238    10223   4815   5601   -488    247  -1211       O  
ATOM   4720  N   TYR B 239       3.607  12.571 -25.196  1.00 66.59           N  
ANISOU 4720  N   TYR B 239    11947   6232   7122   -478    327  -1309       N  
ATOM   4721  CA  TYR B 239       2.771  12.844 -26.366  1.00 70.29           C  
ANISOU 4721  CA  TYR B 239    12532   6730   7443   -560    261  -1320       C  
ATOM   4722  CB  TYR B 239       3.456  12.345 -27.645  1.00 77.78           C  
ANISOU 4722  CB  TYR B 239    13626   7622   8306   -532    368  -1385       C  
ATOM   4723  CG  TYR B 239       3.720  10.854 -27.693  1.00 82.28           C  
ANISOU 4723  CG  TYR B 239    14264   8089   8908   -517    404  -1438       C  
ATOM   4724  CD2 TYR B 239       4.924  10.331 -27.236  1.00 81.72           C  
ANISOU 4724  CD2 TYR B 239    14155   7961   8934   -418    530  -1457       C  
ATOM   4725  CE2 TYR B 239       5.176   8.975 -27.283  1.00 84.83           C  
ANISOU 4725  CE2 TYR B 239    14613   8263   9357   -401    565  -1503       C  
ATOM   4726  CZ  TYR B 239       4.221   8.122 -27.794  1.00 89.20           C  
ANISOU 4726  CZ  TYR B 239    15274   8776   9842   -487    474  -1534       C  
ATOM   4727  OH  TYR B 239       4.473   6.769 -27.838  1.00 94.06           O  
ANISOU 4727  OH  TYR B 239    15957   9295  10485   -471    510  -1581       O  
ATOM   4728  CE1 TYR B 239       3.018   8.615 -28.259  1.00 86.86           C  
ANISOU 4728  CE1 TYR B 239    15017   8537   9451   -588    347  -1516       C  
ATOM   4729  CD1 TYR B 239       2.775   9.973 -28.209  1.00 84.90           C  
ANISOU 4729  CD1 TYR B 239    14700   8384   9174   -602    313  -1467       C  
ATOM   4730  C   TYR B 239       1.389  12.211 -26.226  1.00 65.73           C  
ANISOU 4730  C   TYR B 239    11977   6153   6843   -662    106  -1308       C  
ATOM   4731  O   TYR B 239       1.247  11.184 -25.562  1.00 60.25           O  
ANISOU 4731  O   TYR B 239    11259   5403   6228   -665     79  -1318       O  
ATOM   4732  N   LYS B 240       0.371  12.816 -26.842  1.00 65.19           N  
ANISOU 4732  N   LYS B 240    11948   6150   6669   -746      5  -1283       N  
ATOM   4733  CA  LYS B 240      -0.971  12.237 -26.770  1.00 63.87           C  
ANISOU 4733  CA  LYS B 240    11799   5991   6477   -846   -143  -1264       C  
ATOM   4734  CB  LYS B 240      -2.042  13.149 -27.392  1.00 62.59           C  
ANISOU 4734  CB  LYS B 240    11654   5921   6205   -928   -249  -1220       C  
ATOM   4735  CG  LYS B 240      -3.457  12.654 -27.059  1.00 71.21           C  
ANISOU 4735  CG  LYS B 240    12725   7037   7295  -1026   -408  -1180       C  
ATOM   4736  CD  LYS B 240      -4.617  13.602 -27.418  1.00 74.42           C  
ANISOU 4736  CD  LYS B 240    13110   7548   7618  -1104   -526  -1114       C  
ATOM   4737  CE  LYS B 240      -4.256  15.083 -27.366  1.00 74.12           C  
ANISOU 4737  CE  LYS B 240    13004   7593   7567  -1062   -490  -1072       C  
ATOM   4738  NZ  LYS B 240      -4.771  15.812 -26.174  1.00 77.14           N  
ANISOU 4738  NZ  LYS B 240    13233   8050   8025  -1065   -573   -988       N  
ATOM   4739  C   LYS B 240      -0.972  10.878 -27.460  1.00 71.31           C  
ANISOU 4739  C   LYS B 240    12872   6839   7381   -868   -123  -1332       C  
ATOM   4740  O   LYS B 240      -0.437  10.735 -28.559  1.00 63.96           O  
ANISOU 4740  O   LYS B 240    12061   5874   6368   -849    -40  -1384       O  
ATOM   4741  N   GLY B 241      -1.554   9.882 -26.794  1.00 75.17           N  
ANISOU 4741  N   GLY B 241    13338   7288   7934   -906   -198  -1328       N  
ATOM   4742  CA  GLY B 241      -1.544   8.513 -27.278  1.00 79.10           C  
ANISOU 4742  CA  GLY B 241    13950   7690   8413   -925   -181  -1391       C  
ATOM   4743  C   GLY B 241      -0.419   7.665 -26.710  1.00 80.66           C  
ANISOU 4743  C   GLY B 241    14130   7800   8719   -833    -64  -1430       C  
ATOM   4744  O   GLY B 241      -0.246   6.501 -27.086  1.00 84.73           O  
ANISOU 4744  O   GLY B 241    14741   8227   9226   -834    -31  -1485       O  
ATOM   4745  N   ARG B 242       0.377   8.247 -25.827  1.00 75.79           N  
ANISOU 4745  N   ARG B 242    13388   7205   8202   -750      3  -1402       N  
ATOM   4746  CA  ARG B 242       1.388   7.467 -25.135  1.00 75.59           C  
ANISOU 4746  CA  ARG B 242    13320   7106   8295   -662    104  -1426       C  
ATOM   4747  CB  ARG B 242       2.544   8.387 -24.681  1.00 72.30           C  
ANISOU 4747  CB  ARG B 242    12803   6723   7944   -560    217  -1404       C  
ATOM   4748  CG  ARG B 242       3.842   7.672 -24.308  1.00 73.89           C  
ANISOU 4748  CG  ARG B 242    12981   6852   8243   -453    357  -1433       C  
ATOM   4749  CD  ARG B 242       4.875   8.654 -23.731  1.00 72.55           C  
ANISOU 4749  CD  ARG B 242    12691   6728   8148   -360    452  -1398       C  
ATOM   4750  NE  ARG B 242       4.939   8.592 -22.270  1.00 74.59           N  
ANISOU 4750  NE  ARG B 242    12789   6996   8555   -326    425  -1352       N  
ATOM   4751  CZ  ARG B 242       5.887   9.150 -21.516  1.00 78.68           C  
ANISOU 4751  CZ  ARG B 242    13184   7540   9172   -238    507  -1321       C  
ATOM   4752  NH1 ARG B 242       6.894   9.826 -22.057  1.00 80.20           N  
ANISOU 4752  NH1 ARG B 242    13388   7750   9333   -173    626  -1327       N  
ATOM   4753  NH2 ARG B 242       5.828   9.027 -20.200  1.00 77.81           N  
ANISOU 4753  NH2 ARG B 242    12932   7436   9194   -215    469  -1278       N  
ATOM   4754  C   ARG B 242       0.778   6.727 -23.937  1.00 75.21           C  
ANISOU 4754  C   ARG B 242    13177   7038   8360   -688     16  -1396       C  
ATOM   4755  O   ARG B 242      -0.021   7.312 -23.202  1.00 73.28           O  
ANISOU 4755  O   ARG B 242    12830   6863   8149   -731    -91  -1335       O  
ATOM   4756  N   THR B 243       1.084   5.434 -23.788  1.00 77.37           N  
ANISOU 4756  N   THR B 243    13491   7219   8686   -666     55  -1438       N  
ATOM   4757  CA  THR B 243       0.811   4.692 -22.534  1.00 73.94           C  
ANISOU 4757  CA  THR B 243    12952   6757   8386   -663      5  -1411       C  
ATOM   4758  CB  THR B 243       0.250   3.294 -22.799  1.00 74.61           C  
ANISOU 4758  CB  THR B 243    13134   6759   8455   -720    -40  -1451       C  
ATOM   4759  OG1 THR B 243       0.973   2.682 -23.870  1.00 73.67           O  
ANISOU 4759  OG1 THR B 243    13163   6566   8263   -688     65  -1523       O  
ATOM   4760  CG2 THR B 243      -1.194   3.366 -23.120  1.00 73.02           C  
ANISOU 4760  CG2 THR B 243    12971   6602   8171   -842   -192  -1427       C  
ATOM   4761  C   THR B 243       1.966   4.448 -21.564  1.00 73.35           C  
ANISOU 4761  C   THR B 243    12767   6647   8454   -551    113  -1405       C  
ATOM   4762  O   THR B 243       1.740   4.240 -20.365  1.00 73.55           O  
ANISOU 4762  O   THR B 243    12667   6680   8600   -542     66  -1363       O  
ATOM   4763  N   ALA B 244       3.184   4.395 -22.086  1.00 70.04           N  
ANISOU 4763  N   ALA B 244    12397   6190   8024   -465    258  -1445       N  
ATOM   4764  CA  ALA B 244       4.336   3.966 -21.298  1.00 70.21           C  
ANISOU 4764  CA  ALA B 244    12331   6170   8173   -357    369  -1444       C  
ATOM   4765  CB  ALA B 244       5.548   3.817 -22.196  1.00 66.04           C  
ANISOU 4765  CB  ALA B 244    11896   5600   7597   -279    522  -1491       C  
ATOM   4766  C   ALA B 244       4.637   4.931 -20.155  1.00 75.67           C  
ANISOU 4766  C   ALA B 244    12844   6934   8974   -307    368  -1378       C  
ATOM   4767  O   ALA B 244       5.166   6.023 -20.370  1.00 76.77           O  
ANISOU 4767  O   ALA B 244    12952   7130   9085   -270    422  -1361       O  
ATOM   4768  N   GLY B 245       4.287   4.524 -18.939  1.00 74.65           N  
ANISOU 4768  N   GLY B 245    12595   6801   8966   -307    306  -1340       N  
ATOM   4769  CA  GLY B 245       4.601   5.298 -17.752  1.00 65.45           C  
ANISOU 4769  CA  GLY B 245    11255   5695   7918   -254    306  -1277       C  
ATOM   4770  C   GLY B 245       3.716   6.513 -17.586  1.00 61.62           C  
ANISOU 4770  C   GLY B 245    10718   5303   7392   -318    198  -1226       C  
ATOM   4771  O   GLY B 245       4.114   7.519 -16.986  1.00 62.80           O  
ANISOU 4771  O   GLY B 245    10754   5512   7593   -273    218  -1181       O  
ATOM   4772  N   MET B 246       2.500   6.404 -18.111  1.00 59.24           N  
ANISOU 4772  N   MET B 246    10498   5014   6995   -424     81  -1230       N  
ATOM   4773  CA  MET B 246       1.531   7.491 -18.063  1.00 59.48           C  
ANISOU 4773  CA  MET B 246    10494   5136   6970   -494    -33  -1178       C  
ATOM   4774  CB  MET B 246       0.693   7.485 -19.342  1.00 60.93           C  
ANISOU 4774  CB  MET B 246    10829   5328   6993   -588    -96  -1208       C  
ATOM   4775  CG  MET B 246       1.523   7.686 -20.584  1.00 67.15           C  
ANISOU 4775  CG  MET B 246    11740   6093   7680   -553     19  -1266       C  
ATOM   4776  SD  MET B 246       2.165   9.356 -20.711  1.00 72.45           S  
ANISOU 4776  SD  MET B 246    12354   6850   8323   -503     80  -1234       S  
ATOM   4777  CE  MET B 246       0.620  10.229 -20.575  1.00 41.25           C  
ANISOU 4777  CE  MET B 246     8369   2996   4308   -612    -98  -1169       C  
ATOM   4778  C   MET B 246       0.627   7.402 -16.839  1.00 57.37           C  
ANISOU 4778  C   MET B 246    10099   4902   6796   -532   -155  -1113       C  
ATOM   4779  O   MET B 246       0.643   6.405 -16.121  1.00 57.81           O  
ANISOU 4779  O   MET B 246    10110   4905   6952   -515   -158  -1113       O  
ATOM   4780  N   ASN B 247      -0.178   8.441 -16.621  1.00 52.89           N  
ANISOU 4780  N   ASN B 247     9478   4425   6194   -582   -257  -1054       N  
ATOM   4781  CA  ASN B 247      -1.188   8.423 -15.554  1.00 49.75           C  
ANISOU 4781  CA  ASN B 247     8965   4070   5865   -627   -386   -983       C  
ATOM   4782  CB  ASN B 247      -0.547   8.579 -14.175  1.00 49.96           C  
ANISOU 4782  CB  ASN B 247     8828   4103   6052   -543   -348   -939       C  
ATOM   4783  CG  ASN B 247       0.098   9.943 -13.957  1.00 50.71           C  
ANISOU 4783  CG  ASN B 247     8851   4260   6158   -486   -300   -909       C  
ATOM   4784  OD1 ASN B 247      -0.576  10.970 -13.960  1.00 54.98           O  
ANISOU 4784  OD1 ASN B 247     9366   4882   6643   -530   -384   -860       O  
ATOM   4785  ND2 ASN B 247       1.411   9.950 -13.739  1.00 52.82           N  
ANISOU 4785  ND2 ASN B 247     9079   4491   6498   -387   -165   -932       N  
ATOM   4786  C   ASN B 247      -2.240   9.493 -15.808  1.00 49.41           C  
ANISOU 4786  C   ASN B 247     8917   4127   5728   -703   -506   -928       C  
ATOM   4787  O   ASN B 247      -2.216  10.199 -16.831  1.00 49.34           O  
ANISOU 4787  O   ASN B 247     8998   4150   5600   -725   -489   -949       O  
ATOM   4788  N   LYS B 248      -3.153   9.622 -14.858  1.00 53.10           N  
ANISOU 4788  N   LYS B 248     9275   4649   6251   -739   -624   -853       N  
ATOM   4789  CA  LYS B 248      -4.311  10.502 -14.979  1.00 50.49           C  
ANISOU 4789  CA  LYS B 248     8926   4418   5840   -814   -754   -786       C  
ATOM   4790  CB  LYS B 248      -5.299  10.193 -13.851  1.00 59.24           C  
ANISOU 4790  CB  LYS B 248     9915   5566   7029   -847   -877   -707       C  
ATOM   4791  CG  LYS B 248      -6.720  10.664 -14.120  1.00 64.26           C  
ANISOU 4791  CG  LYS B 248    10550   6291   7572   -939  -1023   -639       C  
ATOM   4792  CD  LYS B 248      -7.274  11.478 -12.962  1.00 58.14           C  
ANISOU 4792  CD  LYS B 248     9616   5610   6865   -927  -1112   -535       C  
ATOM   4793  CE  LYS B 248      -7.280  10.680 -11.677  1.00 60.19           C  
ANISOU 4793  CE  LYS B 248     9760   5842   7267   -892  -1128   -503       C  
ATOM   4794  NZ  LYS B 248      -7.836  11.468 -10.547  1.00 64.05           N  
ANISOU 4794  NZ  LYS B 248    10091   6425   7819   -875  -1216   -397       N  
ATOM   4795  C   LYS B 248      -3.937  11.985 -14.950  1.00 59.33           C  
ANISOU 4795  C   LYS B 248     9996   5611   6936   -778   -733   -754       C  
ATOM   4796  O   LYS B 248      -4.791  12.848 -15.143  1.00 64.33           O  
ANISOU 4796  O   LYS B 248    10617   6331   7495   -832   -828   -699       O  
ATOM   4797  N   TYR B 249      -2.664  12.276 -14.699  1.00 49.98           N  
ANISOU 4797  N   TYR B 249     8780   4393   5817   -686   -607   -783       N  
ATOM   4798  CA  TYR B 249      -2.224  13.664 -14.602  1.00 47.53           C  
ANISOU 4798  CA  TYR B 249     8419   4146   5496   -647   -578   -753       C  
ATOM   4799  CB  TYR B 249      -1.562  13.911 -13.247  1.00 48.41           C  
ANISOU 4799  CB  TYR B 249     8375   4258   5760   -564   -543   -711       C  
ATOM   4800  CG  TYR B 249      -2.469  13.567 -12.086  1.00 41.28           C  
ANISOU 4800  CG  TYR B 249     7353   3387   4944   -590   -663   -638       C  
ATOM   4801  CD1 TYR B 249      -3.436  14.459 -11.652  1.00 36.20           C  
ANISOU 4801  CD1 TYR B 249     6635   2841   4279   -632   -789   -554       C  
ATOM   4802  CE1 TYR B 249      -4.278  14.147 -10.588  1.00 37.29           C  
ANISOU 4802  CE1 TYR B 249     6658   3015   4494   -649   -897   -480       C  
ATOM   4803  CZ  TYR B 249      -4.155  12.928  -9.961  1.00 36.37           C  
ANISOU 4803  CZ  TYR B 249     6506   2837   4477   -629   -878   -493       C  
ATOM   4804  OH  TYR B 249      -4.984  12.602  -8.915  1.00 44.34           O  
ANISOU 4804  OH  TYR B 249     7401   3886   5559   -644   -980   -418       O  
ATOM   4805  CE2 TYR B 249      -3.205  12.022 -10.382  1.00 44.56           C  
ANISOU 4805  CE2 TYR B 249     7619   3773   5538   -591   -755   -579       C  
ATOM   4806  CD2 TYR B 249      -2.370  12.344 -11.440  1.00 42.45           C  
ANISOU 4806  CD2 TYR B 249     7462   3472   5193   -570   -649   -649       C  
ATOM   4807  C   TYR B 249      -1.287  14.024 -15.754  1.00 47.06           C  
ANISOU 4807  C   TYR B 249     8473   4059   5350   -614   -452   -821       C  
ATOM   4808  O   TYR B 249      -1.354  15.131 -16.296  1.00 52.80           O  
ANISOU 4808  O   TYR B 249     9227   4847   5990   -628   -457   -807       O  
ATOM   4809  N   LYS B 250      -0.429  13.082 -16.135  1.00 47.11           N  
ANISOU 4809  N   LYS B 250     8545   3978   5378   -570   -341   -892       N  
ATOM   4810  CA  LYS B 250       0.476  13.281 -17.265  1.00 51.65           C  
ANISOU 4810  CA  LYS B 250     9231   4525   5871   -535   -216   -955       C  
ATOM   4811  CB  LYS B 250       1.447  12.106 -17.402  1.00 52.08           C  
ANISOU 4811  CB  LYS B 250     9326   4481   5979   -473    -96  -1019       C  
ATOM   4812  CG  LYS B 250       2.495  11.997 -16.314  1.00 53.69           C  
ANISOU 4812  CG  LYS B 250     9403   4661   6338   -371     -8  -1004       C  
ATOM   4813  CD  LYS B 250       3.523  10.935 -16.677  1.00 50.08           C  
ANISOU 4813  CD  LYS B 250     9002   4115   5910   -307    121  -1067       C  
ATOM   4814  CE  LYS B 250       4.661  10.903 -15.676  1.00 54.10           C  
ANISOU 4814  CE  LYS B 250     9379   4611   6566   -200    218  -1046       C  
ATOM   4815  NZ  LYS B 250       5.769  10.023 -16.137  1.00 53.02           N  
ANISOU 4815  NZ  LYS B 250     9299   4403   6444   -129    354  -1101       N  
ATOM   4816  C   LYS B 250      -0.267  13.462 -18.587  1.00 58.17           C  
ANISOU 4816  C   LYS B 250    10195   5376   6532   -618   -266   -978       C  
ATOM   4817  O   LYS B 250       0.200  14.183 -19.470  1.00 59.85           O  
ANISOU 4817  O   LYS B 250    10474   5608   6657   -603   -198  -1001       O  
ATOM   4818  N   GLU B 251      -1.409  12.794 -18.735  1.00 60.15           N  
ANISOU 4818  N   GLU B 251    10484   5627   6743   -703   -382   -968       N  
ATOM   4819  CA  GLU B 251      -2.132  12.829 -20.005  1.00 66.66           C  
ANISOU 4819  CA  GLU B 251    11440   6471   7417   -783   -430   -988       C  
ATOM   4820  CB  GLU B 251      -3.133  11.671 -20.119  1.00 71.63           C  
ANISOU 4820  CB  GLU B 251    12119   7068   8030   -862   -527   -994       C  
ATOM   4821  CG  GLU B 251      -2.729  10.561 -21.103  1.00 84.14           C  
ANISOU 4821  CG  GLU B 251    13850   8559   9562   -865   -453  -1079       C  
ATOM   4822  CD  GLU B 251      -2.963  10.928 -22.569  1.00 91.79           C  
ANISOU 4822  CD  GLU B 251    14956   9547  10373   -912   -448  -1110       C  
ATOM   4823  OE1 GLU B 251      -4.049  11.456 -22.892  1.00 92.36           O  
ANISOU 4823  OE1 GLU B 251    15033   9693  10367   -991   -561  -1064       O  
ATOM   4824  OE2 GLU B 251      -2.060  10.686 -23.400  1.00 96.29           O  
ANISOU 4824  OE2 GLU B 251    15626  10061  10899   -868   -331  -1176       O  
ATOM   4825  C   GLU B 251      -2.862  14.144 -20.190  1.00 59.55           C  
ANISOU 4825  C   GLU B 251    10510   5678   6440   -828   -513   -927       C  
ATOM   4826  O   GLU B 251      -3.160  14.537 -21.311  1.00 63.18           O  
ANISOU 4826  O   GLU B 251    11066   6166   6773   -871   -519   -941       O  
ATOM   4827  N   TYR B 252      -3.141  14.833 -19.093  1.00 54.48           N  
ANISOU 4827  N   TYR B 252     9730   5095   5873   -816   -575   -855       N  
ATOM   4828  CA  TYR B 252      -3.957  16.033 -19.161  1.00 56.53           C  
ANISOU 4828  CA  TYR B 252     9951   5461   6068   -861   -668   -785       C  
ATOM   4829  CB  TYR B 252      -4.248  16.547 -17.752  1.00 61.47           C  
ANISOU 4829  CB  TYR B 252    10416   6139   6802   -840   -739   -705       C  
ATOM   4830  CG  TYR B 252      -5.054  17.822 -17.730  1.00 71.76           C  
ANISOU 4830  CG  TYR B 252    11666   7555   8045   -877   -832   -625       C  
ATOM   4831  CD1 TYR B 252      -6.433  17.806 -17.947  1.00 76.26           C  
ANISOU 4831  CD1 TYR B 252    12232   8189   8554   -960   -962   -565       C  
ATOM   4832  CE1 TYR B 252      -7.173  18.974 -17.923  1.00 76.14           C  
ANISOU 4832  CE1 TYR B 252    12157   8282   8492   -985  -1038   -484       C  
ATOM   4833  CZ  TYR B 252      -6.539  20.176 -17.677  1.00 72.28           C  
ANISOU 4833  CZ  TYR B 252    11618   7834   8010   -931   -990   -466       C  
ATOM   4834  OH  TYR B 252      -7.287  21.329 -17.657  1.00 71.94           O  
ANISOU 4834  OH  TYR B 252    11512   7899   7923   -952  -1060   -382       O  
ATOM   4835  CE2 TYR B 252      -5.173  20.220 -17.457  1.00 71.01           C  
ANISOU 4835  CE2 TYR B 252    11467   7608   7905   -855   -865   -528       C  
ATOM   4836  CD2 TYR B 252      -4.441  19.046 -17.482  1.00 72.39           C  
ANISOU 4836  CD2 TYR B 252    11693   7678   8134   -825   -784   -604       C  
ATOM   4837  C   TYR B 252      -3.310  17.132 -20.016  1.00 56.14           C  
ANISOU 4837  C   TYR B 252     9957   5444   5931   -832   -583   -806       C  
ATOM   4838  O   TYR B 252      -4.011  17.979 -20.564  1.00 53.83           O  
ANISOU 4838  O   TYR B 252     9680   5230   5544   -880   -645   -766       O  
ATOM   4839  N   PHE B 253      -1.983  17.103 -20.149  1.00 51.77           N  
ANISOU 4839  N   PHE B 253     9427   4832   5411   -750   -437   -863       N  
ATOM   4840  CA  PHE B 253      -1.288  18.056 -21.020  1.00 49.52           C  
ANISOU 4840  CA  PHE B 253     9199   4571   5043   -718   -342   -885       C  
ATOM   4841  CB  PHE B 253      -0.381  18.986 -20.200  1.00 53.29           C  
ANISOU 4841  CB  PHE B 253     9573   5070   5606   -638   -270   -861       C  
ATOM   4842  CG  PHE B 253      -1.122  20.040 -19.427  1.00 47.12           C  
ANISOU 4842  CG  PHE B 253     8685   4378   4839   -664   -379   -777       C  
ATOM   4843  CD1 PHE B 253      -1.846  21.025 -20.085  1.00 40.92           C  
ANISOU 4843  CD1 PHE B 253     7929   3680   3940   -716   -442   -739       C  
ATOM   4844  CE1 PHE B 253      -2.528  22.001 -19.373  1.00 44.57           C  
ANISOU 4844  CE1 PHE B 253     8290   4230   4416   -735   -541   -656       C  
ATOM   4845  CZ  PHE B 253      -2.470  22.011 -17.991  1.00 46.11           C  
ANISOU 4845  CZ  PHE B 253     8358   4423   4738   -702   -580   -614       C  
ATOM   4846  CE2 PHE B 253      -1.742  21.042 -17.326  1.00 46.26           C  
ANISOU 4846  CE2 PHE B 253     8346   4354   4875   -650   -517   -652       C  
ATOM   4847  CD2 PHE B 253      -1.066  20.069 -18.043  1.00 46.89           C  
ANISOU 4847  CD2 PHE B 253     8524   4351   4942   -630   -414   -732       C  
ATOM   4848  C   PHE B 253      -0.446  17.404 -22.131  1.00 54.44           C  
ANISOU 4848  C   PHE B 253     9952   5121   5611   -689   -217   -969       C  
ATOM   4849  O   PHE B 253       0.490  18.016 -22.616  1.00 58.47           O  
ANISOU 4849  O   PHE B 253    10488   5633   6095   -632   -103   -992       O  
ATOM   4850  N   ALA B 254      -0.769  16.175 -22.529  1.00 49.30           N  
ANISOU 4850  N   ALA B 254     9380   4408   4943   -725   -237  -1010       N  
ATOM   4851  CA  ALA B 254      -0.038  15.513 -23.612  1.00 48.43           C  
ANISOU 4851  CA  ALA B 254     9400   4227   4774   -700   -127  -1087       C  
ATOM   4852  CB  ALA B 254      -0.515  14.077 -23.767  1.00 54.29           C  
ANISOU 4852  CB  ALA B 254    10212   4898   5519   -744   -170  -1124       C  
ATOM   4853  C   ALA B 254      -0.200  16.293 -24.936  1.00 49.31           C  
ANISOU 4853  C   ALA B 254     9610   4386   4740   -732   -114  -1096       C  
ATOM   4854  O   ALA B 254      -1.273  16.787 -25.225  1.00 48.86           O  
ANISOU 4854  O   ALA B 254     9558   4397   4610   -807   -225  -1054       O  
ATOM   4855  N   SER B 255       0.864  16.414 -25.731  1.00 55.32           N  
ANISOU 4855  N   SER B 255    10442   5116   5463   -671     23  -1144       N  
ATOM   4856  CA  SER B 255       0.832  17.257 -26.939  1.00 59.47           C  
ANISOU 4856  CA  SER B 255    11047   5689   5861   -689     48  -1148       C  
ATOM   4857  CB  SER B 255       1.885  18.366 -26.843  1.00 73.97           C  
ANISOU 4857  CB  SER B 255    12827   7559   7719   -609    161  -1134       C  
ATOM   4858  OG  SER B 255       3.174  17.861 -27.153  1.00 78.60           O  
ANISOU 4858  OG  SER B 255    13454   8075   8336   -526    313  -1187       O  
ATOM   4859  C   SER B 255       1.015  16.485 -28.279  1.00 61.24           C  
ANISOU 4859  C   SER B 255    11427   5853   5987   -702    102  -1215       C  
ATOM   4860  O   SER B 255       1.654  15.440 -28.334  1.00 53.50           O  
ANISOU 4860  O   SER B 255    10496   4787   5044   -663    175  -1267       O  
ATOM   4861  N   GLU B 256       0.390  17.015 -29.337  1.00 61.63           N  
ANISOU 4861  N   GLU B 256    11551   5952   5914   -759     57  -1208       N  
ATOM   4862  CA  GLU B 256       0.406  16.417 -30.675  1.00 62.55           C  
ANISOU 4862  CA  GLU B 256    11819   6024   5925   -782     91  -1266       C  
ATOM   4863  CB  GLU B 256      -0.663  17.055 -31.566  1.00 64.88           C  
ANISOU 4863  CB  GLU B 256    12159   6391   6100   -865     -6  -1237       C  
ATOM   4864  CG  GLU B 256      -2.019  17.158 -30.915  1.00 71.74           C  
ANISOU 4864  CG  GLU B 256    12955   7319   6984   -948   -168  -1176       C  
ATOM   4865  CD  GLU B 256      -3.114  17.548 -31.876  1.00 79.61           C  
ANISOU 4865  CD  GLU B 256    14004   8377   7865  -1032   -263  -1151       C  
ATOM   4866  OE1 GLU B 256      -2.831  18.274 -32.852  1.00 76.19           O  
ANISOU 4866  OE1 GLU B 256    13624   7977   7350  -1018   -209  -1160       O  
ATOM   4867  OE2 GLU B 256      -4.264  17.111 -31.650  1.00 87.99           O  
ANISOU 4867  OE2 GLU B 256    15052   9456   8925  -1111   -390  -1122       O  
ATOM   4868  C   GLU B 256       1.748  16.506 -31.396  1.00 63.82           C  
ANISOU 4868  C   GLU B 256    12041   6144   6065   -696    255  -1312       C  
ATOM   4869  O   GLU B 256       1.834  16.166 -32.578  1.00 67.84           O  
ANISOU 4869  O   GLU B 256    12675   6622   6479   -708    292  -1357       O  
ATOM   4870  N   THR B 257       2.786  16.956 -30.700  1.00 58.51           N  
ANISOU 4870  N   THR B 257    11279   5471   5480   -609    355  -1300       N  
ATOM   4871  CA  THR B 257       4.108  17.112 -31.305  1.00 66.10           C  
ANISOU 4871  CA  THR B 257    12279   6403   6433   -522    516  -1332       C  
ATOM   4872  CB  THR B 257       5.139  17.629 -30.283  1.00 67.84           C  
ANISOU 4872  CB  THR B 257    12370   6633   6773   -433    607  -1304       C  
ATOM   4873  OG1 THR B 257       6.375  17.920 -30.948  1.00 67.25           O  
ANISOU 4873  OG1 THR B 257    12326   6544   6682   -352    760  -1324       O  
ATOM   4874  CG2 THR B 257       5.381  16.586 -29.203  1.00 67.54           C  
ANISOU 4874  CG2 THR B 257    12274   6531   6859   -403    610  -1316       C  
ATOM   4875  C   THR B 257       4.650  15.812 -31.906  1.00 67.53           C  
ANISOU 4875  C   THR B 257    12573   6485   6601   -495    591  -1400       C  
ATOM   4876  O   THR B 257       4.272  14.709 -31.500  1.00 64.00           O  
ANISOU 4876  O   THR B 257    12144   5979   6193   -521    541  -1423       O  
ATOM   4877  N   GLU B 258       5.539  15.961 -32.879  1.00 68.21           N  
ANISOU 4877  N   GLU B 258    12734   6552   6630   -441    712  -1430       N  
ATOM   4878  CA  GLU B 258       6.165  14.829 -33.541  1.00 75.60           C  
ANISOU 4878  CA  GLU B 258    13782   7397   7545   -405    798  -1491       C  
ATOM   4879  CB  GLU B 258       6.454  15.147 -35.013  1.00 84.88           C  
ANISOU 4879  CB  GLU B 258    15079   8576   8596   -398    861  -1519       C  
ATOM   4880  CG  GLU B 258       5.205  15.397 -35.860  1.00 88.72           C  
ANISOU 4880  CG  GLU B 258    15647   9103   8960   -501    739  -1519       C  
ATOM   4881  CD  GLU B 258       4.486  16.689 -35.491  1.00 93.17           C  
ANISOU 4881  CD  GLU B 258    16112   9772   9516   -545    650  -1455       C  
ATOM   4882  OE1 GLU B 258       5.163  17.669 -35.100  1.00 87.69           O  
ANISOU 4882  OE1 GLU B 258    15325   9126   8869   -487    717  -1418       O  
ATOM   4883  OE2 GLU B 258       3.238  16.712 -35.563  1.00 97.30           O  
ANISOU 4883  OE2 GLU B 258    16648  10331   9991   -637    513  -1437       O  
ATOM   4884  C   GLU B 258       7.444  14.500 -32.789  1.00 76.88           C  
ANISOU 4884  C   GLU B 258    13869   7516   7828   -300    925  -1493       C  
ATOM   4885  O   GLU B 258       8.041  13.441 -32.976  1.00 75.99           O  
ANISOU 4885  O   GLU B 258    13817   7322   7733   -258    998  -1536       O  
ATOM   4886  N   ALA B 259       7.851  15.427 -31.928  1.00 74.95           N  
ANISOU 4886  N   ALA B 259    13486   7328   7664   -259    949  -1443       N  
ATOM   4887  CA  ALA B 259       9.043  15.257 -31.109  1.00 71.78           C  
ANISOU 4887  CA  ALA B 259    12987   6900   7386   -161   1063  -1432       C  
ATOM   4888  CB  ALA B 259       9.417  16.567 -30.434  1.00 71.06           C  
ANISOU 4888  CB  ALA B 259    12760   6887   7353   -126   1086  -1373       C  
ATOM   4889  C   ALA B 259       8.820  14.167 -30.071  1.00 68.59           C  
ANISOU 4889  C   ALA B 259    12536   6440   7084   -163   1017  -1440       C  
ATOM   4890  O   ALA B 259       7.700  13.971 -29.593  1.00 72.02           O  
ANISOU 4890  O   ALA B 259    12955   6886   7523   -240    882  -1430       O  
ATOM   4891  N   ARG B 260       9.891  13.461 -29.725  1.00 59.25           N  
ANISOU 4891  N   ARG B 260    11325   5200   5986    -78   1129  -1454       N  
ATOM   4892  CA  ARG B 260       9.821  12.393 -28.740  1.00 64.94           C  
ANISOU 4892  CA  ARG B 260    11996   5866   6814    -68   1101  -1460       C  
ATOM   4893  CB  ARG B 260       9.957  11.016 -29.414  1.00 72.74           C  
ANISOU 4893  CB  ARG B 260    13117   6760   7762    -64   1137  -1521       C  
ATOM   4894  CG  ARG B 260       8.635  10.256 -29.624  1.00 72.35           C  
ANISOU 4894  CG  ARG B 260    13158   6678   7654   -168    998  -1550       C  
ATOM   4895  CD  ARG B 260       7.623  11.074 -30.415  1.00 69.41           C  
ANISOU 4895  CD  ARG B 260    12850   6368   7157   -258    901  -1544       C  
ATOM   4896  NE  ARG B 260       6.336  10.406 -30.585  1.00 71.20           N  
ANISOU 4896  NE  ARG B 260    13150   6574   7330   -361    763  -1563       N  
ATOM   4897  CZ  ARG B 260       5.213  11.033 -30.925  1.00 76.16           C  
ANISOU 4897  CZ  ARG B 260    13797   7264   7877   -452    642  -1542       C  
ATOM   4898  NH1 ARG B 260       5.216  12.349 -31.107  1.00 81.00           N  
ANISOU 4898  NH1 ARG B 260    14363   7960   8452   -452    643  -1504       N  
ATOM   4899  NH2 ARG B 260       4.083  10.353 -31.067  1.00 70.12           N  
ANISOU 4899  NH2 ARG B 260    13094   6479   7069   -545    521  -1556       N  
ATOM   4900  C   ARG B 260      10.899  12.572 -27.673  1.00 60.45           C  
ANISOU 4900  C   ARG B 260    11276   5306   6386     27   1192  -1423       C  
ATOM   4901  O   ARG B 260      10.741  12.105 -26.549  1.00 57.99           O  
ANISOU 4901  O   ARG B 260    10870   4979   6183     33   1149  -1406       O  
ATOM   4902  N   THR B 261      11.996  13.244 -28.013  1.00 58.84           N  
ANISOU 4902  N   THR B 261    11045   5129   6184    101   1318  -1407       N  
ATOM   4903  CA  THR B 261      13.009  13.536 -27.001  1.00 73.28           C  
ANISOU 4903  CA  THR B 261    12719   6978   8145    187   1400  -1363       C  
ATOM   4904  CB  THR B 261      14.433  13.181 -27.461  1.00 81.67           C  
ANISOU 4904  CB  THR B 261    13797   8007   9226    285   1564  -1371       C  
ATOM   4905  OG1 THR B 261      15.355  13.530 -26.421  1.00 84.56           O  
ANISOU 4905  OG1 THR B 261    14000   8406   9725    361   1632  -1320       O  
ATOM   4906  CG2 THR B 261      14.804  13.962 -28.702  1.00 83.94           C  
ANISOU 4906  CG2 THR B 261    14168   8324   9402    292   1633  -1377       C  
ATOM   4907  C   THR B 261      13.010  15.007 -26.591  1.00 70.19           C  
ANISOU 4907  C   THR B 261    12220   6677   7772    185   1386  -1309       C  
ATOM   4908  O   THR B 261      12.437  15.864 -27.268  1.00 64.49           O  
ANISOU 4908  O   THR B 261    11552   6002   6950    132   1340  -1307       O  
ATOM   4909  N   LEU B 262      13.679  15.279 -25.476  1.00 68.87           N  
ANISOU 4909  N   LEU B 262    11899   6534   7736    246   1426  -1265       N  
ATOM   4910  CA  LEU B 262      13.825  16.629 -24.960  1.00 68.26           C  
ANISOU 4910  CA  LEU B 262    11705   6536   7693    255   1425  -1211       C  
ATOM   4911  CB  LEU B 262      14.573  16.607 -23.630  1.00 60.91           C  
ANISOU 4911  CB  LEU B 262    10604   5618   6922    324   1466  -1166       C  
ATOM   4912  CG  LEU B 262      14.755  17.971 -22.977  1.00 52.78           C  
ANISOU 4912  CG  LEU B 262     9445   4668   5943    336   1464  -1108       C  
ATOM   4913  CD1 LEU B 262      13.390  18.566 -22.701  1.00 50.24           C  
ANISOU 4913  CD1 LEU B 262     9131   4382   5577    248   1316  -1099       C  
ATOM   4914  CD2 LEU B 262      15.572  17.839 -21.702  1.00 50.45           C  
ANISOU 4914  CD2 LEU B 262     8979   4382   5806    407   1510  -1063       C  
ATOM   4915  C   LEU B 262      14.559  17.516 -25.951  1.00 77.21           C  
ANISOU 4915  C   LEU B 262    12877   7706   8753    286   1527  -1204       C  
ATOM   4916  O   LEU B 262      14.223  18.690 -26.115  1.00 77.00           O  
ANISOU 4916  O   LEU B 262    12833   7743   8678    254   1495  -1179       O  
ATOM   4917  N   THR B 263      15.565  16.944 -26.607  1.00 77.19           N  
ANISOU 4917  N   THR B 263    12926   7663   8740    349   1650  -1225       N  
ATOM   4918  CA  THR B 263      16.336  17.658 -27.614  1.00 72.31           C  
ANISOU 4918  CA  THR B 263    12350   7072   8054    384   1754  -1218       C  
ATOM   4919  CB  THR B 263      17.456  16.782 -28.203  1.00 71.58           C  
ANISOU 4919  CB  THR B 263    12311   6922   7966    460   1886  -1240       C  
ATOM   4920  OG1 THR B 263      18.351  16.384 -27.159  1.00 71.24           O  
ANISOU 4920  OG1 THR B 263    12134   6871   8062    532   1949  -1207       O  
ATOM   4921  CG2 THR B 263      18.235  17.554 -29.259  1.00 72.68           C  
ANISOU 4921  CG2 THR B 263    12491   7091   8034    495   1991  -1229       C  
ATOM   4922  C   THR B 263      15.427  18.132 -28.737  1.00 65.36           C  
ANISOU 4922  C   THR B 263    11603   6209   7024    308   1689  -1246       C  
ATOM   4923  O   THR B 263      15.468  19.303 -29.127  1.00 59.87           O  
ANISOU 4923  O   THR B 263    10893   5576   6281    299   1701  -1219       O  
ATOM   4924  N   GLU B 264      14.601  17.223 -29.245  1.00 65.28           N  
ANISOU 4924  N   GLU B 264    11717   6146   6941    252   1617  -1296       N  
ATOM   4925  CA  GLU B 264      13.669  17.559 -30.310  1.00 67.01           C  
ANISOU 4925  CA  GLU B 264    12062   6381   7017    175   1544  -1321       C  
ATOM   4926  CB  GLU B 264      12.933  16.315 -30.803  1.00 74.59           C  
ANISOU 4926  CB  GLU B 264    13155   7271   7916    123   1479  -1378       C  
ATOM   4927  CG  GLU B 264      13.613  15.602 -31.958  1.00 82.71           C  
ANISOU 4927  CG  GLU B 264    14313   8239   8875    164   1582  -1423       C  
ATOM   4928  CD  GLU B 264      13.598  14.097 -31.807  1.00 87.74           C  
ANISOU 4928  CD  GLU B 264    15010   8785   9541    171   1581  -1467       C  
ATOM   4929  OE1 GLU B 264      12.544  13.550 -31.426  1.00 86.61           O  
ANISOU 4929  OE1 GLU B 264    14888   8623   9397     99   1459  -1484       O  
ATOM   4930  OE2 GLU B 264      14.643  13.462 -32.059  1.00 90.28           O  
ANISOU 4930  OE2 GLU B 264    15357   9056   9888    249   1702  -1482       O  
ATOM   4931  C   GLU B 264      12.662  18.604 -29.861  1.00 59.85           C  
ANISOU 4931  C   GLU B 264    11098   5548   6094    105   1424  -1286       C  
ATOM   4932  O   GLU B 264      12.361  19.538 -30.599  1.00 60.63           O  
ANISOU 4932  O   GLU B 264    11236   5699   6101     73   1408  -1275       O  
ATOM   4933  N   ALA B 265      12.149  18.450 -28.645  1.00 59.80           N  
ANISOU 4933  N   ALA B 265    10996   5548   6178     84   1339  -1265       N  
ATOM   4934  CA  ALA B 265      11.131  19.360 -28.120  1.00 54.47           C  
ANISOU 4934  CA  ALA B 265    10264   4939   5491     17   1216  -1228       C  
ATOM   4935  CB  ALA B 265      10.688  18.908 -26.754  1.00 40.75           C  
ANISOU 4935  CB  ALA B 265     8427   3190   3868      6   1135  -1210       C  
ATOM   4936  C   ALA B 265      11.621  20.802 -28.059  1.00 55.69           C  
ANISOU 4936  C   ALA B 265    10339   5170   5651     46   1267  -1180       C  
ATOM   4937  O   ALA B 265      10.843  21.742 -28.198  1.00 60.22           O  
ANISOU 4937  O   ALA B 265    10914   5805   6161    -10   1187  -1156       O  
ATOM   4938  N   LEU B 266      12.923  20.971 -27.875  1.00 55.95           N  
ANISOU 4938  N   LEU B 266    10301   5199   5757    135   1402  -1164       N  
ATOM   4939  CA  LEU B 266      13.484  22.284 -27.598  1.00 56.98           C  
ANISOU 4939  CA  LEU B 266    10332   5398   5920    168   1455  -1113       C  
ATOM   4940  CB  LEU B 266      14.692  22.143 -26.669  1.00 58.36           C  
ANISOU 4940  CB  LEU B 266    10373   5563   6239    257   1557  -1085       C  
ATOM   4941  CG  LEU B 266      14.381  22.267 -25.176  1.00 66.16           C  
ANISOU 4941  CG  LEU B 266    11223   6568   7346    255   1487  -1049       C  
ATOM   4942  CD1 LEU B 266      13.162  21.460 -24.797  1.00 72.24           C  
ANISOU 4942  CD1 LEU B 266    12038   7305   8106    187   1349  -1075       C  
ATOM   4943  CD2 LEU B 266      15.562  21.835 -24.348  1.00 61.72           C  
ANISOU 4943  CD2 LEU B 266    10540   5987   6925    341   1584  -1027       C  
ATOM   4944  C   LEU B 266      13.886  23.051 -28.854  1.00 65.30           C  
ANISOU 4944  C   LEU B 266    11457   6484   6870    176   1527  -1113       C  
ATOM   4945  O   LEU B 266      14.263  24.217 -28.771  1.00 61.94           O  
ANISOU 4945  O   LEU B 266    10961   6119   6454    194   1565  -1070       O  
ATOM   4946  N   ARG B 267      13.809  22.407 -30.015  1.00 67.24           N  
ANISOU 4946  N   ARG B 267    11841   6688   7018    163   1547  -1159       N  
ATOM   4947  CA  ARG B 267      14.191  23.081 -31.251  1.00 68.20           C  
ANISOU 4947  CA  ARG B 267    12033   6836   7042    173   1615  -1159       C  
ATOM   4948  CB  ARG B 267      14.352  22.079 -32.398  1.00 73.04           C  
ANISOU 4948  CB  ARG B 267    12792   7384   7575    179   1659  -1214       C  
ATOM   4949  CG  ARG B 267      15.799  21.918 -32.843  1.00 81.79           C  
ANISOU 4949  CG  ARG B 267    13895   8466   8713    272   1820  -1213       C  
ATOM   4950  CD  ARG B 267      15.916  21.326 -34.240  1.00 86.75           C  
ANISOU 4950  CD  ARG B 267    14682   9050   9231    275   1866  -1261       C  
ATOM   4951  NE  ARG B 267      15.326  22.193 -35.257  1.00 87.38           N  
ANISOU 4951  NE  ARG B 267    14833   9178   9189    225   1825  -1259       N  
ATOM   4952  CZ  ARG B 267      14.215  21.903 -35.926  1.00 85.15           C  
ANISOU 4952  CZ  ARG B 267    14665   8887   8801    148   1723  -1294       C  
ATOM   4953  NH1 ARG B 267      13.577  20.768 -35.681  1.00 84.18           N  
ANISOU 4953  NH1 ARG B 267    14599   8706   8679    110   1651  -1335       N  
ATOM   4954  NH2 ARG B 267      13.742  22.744 -36.834  1.00 83.50           N  
ANISOU 4954  NH2 ARG B 267    14509   8730   8489    107   1691  -1287       N  
ATOM   4955  C   ARG B 267      13.179  24.157 -31.631  1.00 60.00           C  
ANISOU 4955  C   ARG B 267    11017   5868   5911     99   1517  -1137       C  
ATOM   4956  O   ARG B 267      12.017  23.864 -31.910  1.00 55.55           O  
ANISOU 4956  O   ARG B 267    10530   5304   5273     22   1399  -1158       O  
ATOM   4957  N   GLY B 268      13.633  25.406 -31.635  1.00 56.58           N  
ANISOU 4957  N   GLY B 268    10513   5500   5485    122   1564  -1091       N  
ATOM   4958  CA  GLY B 268      12.781  26.533 -31.974  1.00 59.18           C  
ANISOU 4958  CA  GLY B 268    10851   5904   5733     61   1482  -1062       C  
ATOM   4959  C   GLY B 268      11.893  27.009 -30.836  1.00 59.81           C  
ANISOU 4959  C   GLY B 268    10844   6026   5856     14   1364  -1027       C  
ATOM   4960  O   GLY B 268      11.135  27.969 -31.000  1.00 59.57           O  
ANISOU 4960  O   GLY B 268    10809   6062   5764    -37   1288   -995       O  
ATOM   4961  N   ALA B 269      11.980  26.342 -29.688  1.00 55.94           N  
ANISOU 4961  N   ALA B 269    10282   5499   5473     32   1347  -1030       N  
ATOM   4962  CA  ALA B 269      11.147  26.679 -28.531  1.00 55.68           C  
ANISOU 4962  CA  ALA B 269    10166   5500   5490     -8   1233   -998       C  
ATOM   4963  CB  ALA B 269      11.149  25.540 -27.523  1.00 49.51           C  
ANISOU 4963  CB  ALA B 269     9342   4657   4813      7   1208  -1018       C  
ATOM   4964  C   ALA B 269      11.604  27.972 -27.862  1.00 51.44           C  
ANISOU 4964  C   ALA B 269     9508   5027   5010     23   1269   -940       C  
ATOM   4965  O   ALA B 269      12.772  28.349 -27.950  1.00 47.13           O  
ANISOU 4965  O   ALA B 269     8911   4485   4511     90   1395   -926       O  
ATOM   4966  N   ASP B 270      10.675  28.628 -27.173  1.00 47.55           N  
ANISOU 4966  N   ASP B 270     8968   4585   4515    -27   1155   -905       N  
ATOM   4967  CA  ASP B 270      10.941  29.913 -26.530  1.00 43.93           C  
ANISOU 4967  CA  ASP B 270     8402   4191   4097     -7   1173   -849       C  
ATOM   4968  CB  ASP B 270       9.712  30.826 -26.626  1.00 48.30           C  
ANISOU 4968  CB  ASP B 270     8972   4819   4562    -81   1044   -812       C  
ATOM   4969  CG  ASP B 270       9.308  31.114 -28.059  1.00 52.23           C  
ANISOU 4969  CG  ASP B 270     9575   5344   4925   -121   1033   -820       C  
ATOM   4970  OD1 ASP B 270      10.087  31.790 -28.767  1.00 49.84           O  
ANISOU 4970  OD1 ASP B 270     9275   5063   4597    -85   1134   -809       O  
ATOM   4971  OD2 ASP B 270       8.211  30.679 -28.473  1.00 50.40           O  
ANISOU 4971  OD2 ASP B 270     9417   5114   4617   -189    921   -834       O  
ATOM   4972  C   ASP B 270      11.339  29.759 -25.069  1.00 42.17           C  
ANISOU 4972  C   ASP B 270     8053   3950   4019     36   1181   -830       C  
ATOM   4973  O   ASP B 270      12.159  30.521 -24.552  1.00 39.87           O  
ANISOU 4973  O   ASP B 270     7661   3686   3801     87   1260   -794       O  
ATOM   4974  N   VAL B 271      10.740  28.784 -24.393  1.00 35.93           N  
ANISOU 4974  N   VAL B 271     7261   3114   3275     13   1097   -851       N  
ATOM   4975  CA  VAL B 271      10.906  28.667 -22.949  1.00 41.25           C  
ANISOU 4975  CA  VAL B 271     7811   3775   4088     45   1079   -828       C  
ATOM   4976  CB  VAL B 271       9.659  29.184 -22.192  1.00 41.35           C  
ANISOU 4976  CB  VAL B 271     7782   3836   4092    -19    920   -787       C  
ATOM   4977  CG1 VAL B 271       9.881  29.120 -20.686  1.00 37.74           C  
ANISOU 4977  CG1 VAL B 271     7139   3393   3806     17    885   -731       C  
ATOM   4978  CG2 VAL B 271       9.317  30.603 -22.616  1.00 40.81           C  
ANISOU 4978  CG2 VAL B 271     7702   3862   3940    -49    891   -735       C  
ATOM   4979  C   VAL B 271      11.184  27.230 -22.510  1.00 34.70           C  
ANISOU 4979  C   VAL B 271     6970   2867   3347     73   1092   -862       C  
ATOM   4980  O   VAL B 271      10.500  26.290 -22.923  1.00 39.33           O  
ANISOU 4980  O   VAL B 271     7648   3415   3882     28   1026   -899       O  
ATOM   4981  N   PHE B 272      12.203  27.071 -21.673  1.00 38.44           N  
ANISOU 4981  N   PHE B 272     7326   3322   3958    148   1178   -844       N  
ATOM   4982  CA  PHE B 272      12.482  25.794 -21.028  1.00 37.27           C  
ANISOU 4982  CA  PHE B 272     7137   3110   3913    181   1185   -862       C  
ATOM   4983  CB  PHE B 272      13.934  25.383 -21.239  1.00 40.93           C  
ANISOU 4983  CB  PHE B 272     7561   3550   4441    265   1340   -868       C  
ATOM   4984  CG  PHE B 272      14.351  24.187 -20.433  1.00 39.29           C  
ANISOU 4984  CG  PHE B 272     7285   3290   4355    309   1355   -874       C  
ATOM   4985  CD1 PHE B 272      14.028  22.908 -20.852  1.00 46.33           C  
ANISOU 4985  CD1 PHE B 272     8273   4118   5213    291   1332   -923       C  
ATOM   4986  CE1 PHE B 272      14.421  21.799 -20.123  1.00 40.95           C  
ANISOU 4986  CE1 PHE B 272     7530   3390   4640    333   1348   -927       C  
ATOM   4987  CZ  PHE B 272      15.146  21.963 -18.963  1.00 41.80           C  
ANISOU 4987  CZ  PHE B 272     7472   3519   4891    393   1384   -879       C  
ATOM   4988  CE2 PHE B 272      15.481  23.233 -18.532  1.00 47.47           C  
ANISOU 4988  CE2 PHE B 272     8088   4302   5646    410   1405   -828       C  
ATOM   4989  CD2 PHE B 272      15.088  24.339 -19.270  1.00 42.74           C  
ANISOU 4989  CD2 PHE B 272     7557   3744   4937    368   1394   -828       C  
ATOM   4990  C   PHE B 272      12.189  25.898 -19.542  1.00 36.28           C  
ANISOU 4990  C   PHE B 272     6878   2992   3913    189   1112   -821       C  
ATOM   4991  O   PHE B 272      12.788  26.728 -18.849  1.00 37.01           O  
ANISOU 4991  O   PHE B 272     6852   3122   4088    232   1158   -776       O  
ATOM   4992  N   VAL B 273      11.272  25.068 -19.058  1.00 31.88           N  
ANISOU 4992  N   VAL B 273     6338   2402   3375    146    998   -833       N  
ATOM   4993  CA  VAL B 273      10.976  25.029 -17.631  1.00 38.79           C  
ANISOU 4993  CA  VAL B 273     7079   3281   4378    155    921   -787       C  
ATOM   4994  CB  VAL B 273       9.464  25.121 -17.350  1.00 37.45           C  
ANISOU 4994  CB  VAL B 273     6914   3151   4163     66    737   -759       C  
ATOM   4995  CG1 VAL B 273       9.206  25.141 -15.850  1.00 37.77           C  
ANISOU 4995  CG1 VAL B 273     6777   3228   4345     79    651   -689       C  
ATOM   4996  CG2 VAL B 273       8.893  26.376 -17.984  1.00 39.09           C  
ANISOU 4996  CG2 VAL B 273     7151   3446   4256     14    686   -727       C  
ATOM   4997  C   VAL B 273      11.542  23.755 -17.020  1.00 35.32           C  
ANISOU 4997  C   VAL B 273     6580   2783   4055    206    961   -801       C  
ATOM   4998  O   VAL B 273      11.012  22.657 -17.218  1.00 36.46           O  
ANISOU 4998  O   VAL B 273     6796   2880   4177    174    909   -837       O  
ATOM   4999  N   GLY B 274      12.627  23.911 -16.274  1.00 34.22           N  
ANISOU 4999  N   GLY B 274     6303   2658   4040    284   1050   -766       N  
ATOM   5000  CA  GLY B 274      13.370  22.773 -15.770  1.00 42.06           C  
ANISOU 5000  CA  GLY B 274     7229   3612   5141    342   1106   -771       C  
ATOM   5001  C   GLY B 274      12.999  22.404 -14.356  1.00 38.43           C  
ANISOU 5001  C   GLY B 274     6640   3152   4811    350   1019   -731       C  
ATOM   5002  O   GLY B 274      13.343  23.109 -13.404  1.00 40.98           O  
ANISOU 5002  O   GLY B 274     6819   3521   5230    384   1021   -674       O  
ATOM   5003  N   LEU B 275      12.281  21.296 -14.229  1.00 36.20           N  
ANISOU 5003  N   LEU B 275     6406   2820   4528    317    942   -758       N  
ATOM   5004  CA  LEU B 275      11.910  20.738 -12.934  1.00 37.44           C  
ANISOU 5004  CA  LEU B 275     6449   2971   4808    325    859   -722       C  
ATOM   5005  CB  LEU B 275      10.387  20.674 -12.782  1.00 39.39           C  
ANISOU 5005  CB  LEU B 275     6754   3209   5004    238    700   -719       C  
ATOM   5006  CG  LEU B 275       9.592  21.952 -13.068  1.00 40.55           C  
ANISOU 5006  CG  LEU B 275     6939   3408   5059    178    623   -695       C  
ATOM   5007  CD1 LEU B 275       8.097  21.647 -13.209  1.00 36.64           C  
ANISOU 5007  CD1 LEU B 275     6520   2915   4488     82    463   -696       C  
ATOM   5008  CD2 LEU B 275       9.819  22.954 -11.967  1.00 33.67           C  
ANISOU 5008  CD2 LEU B 275     5874   2630   4288    211    595   -608       C  
ATOM   5009  C   LEU B 275      12.514  19.340 -12.820  1.00 46.94           C  
ANISOU 5009  C   LEU B 275     7642   4121   6071    369    914   -750       C  
ATOM   5010  O   LEU B 275      11.835  18.387 -12.434  1.00 52.93           O  
ANISOU 5010  O   LEU B 275     8414   4840   6858    342    834   -761       O  
ATOM   5011  N   SER B 276      13.788  19.214 -13.173  1.00 44.42           N  
ANISOU 5011  N   SER B 276     7304   3804   5770    435   1050   -758       N  
ATOM   5012  CA  SER B 276      14.380  17.886 -13.355  1.00 44.40           C  
ANISOU 5012  CA  SER B 276     7331   3747   5793    474   1113   -791       C  
ATOM   5013  CB  SER B 276      14.633  17.630 -14.844  1.00 47.34           C  
ANISOU 5013  CB  SER B 276     7872   4080   6037    463   1192   -852       C  
ATOM   5014  OG  SER B 276      15.320  18.713 -15.455  1.00 42.82           O  
ANISOU 5014  OG  SER B 276     7300   3553   5416    484   1279   -839       O  
ATOM   5015  C   SER B 276      15.674  17.686 -12.570  1.00 49.31           C  
ANISOU 5015  C   SER B 276     7802   4397   6535    560   1202   -749       C  
ATOM   5016  O   SER B 276      15.690  17.750 -11.338  1.00 47.09           O  
ANISOU 5016  O   SER B 276     7373   4152   6365    581   1152   -698       O  
ATOM   5017  N   VAL B 277      16.758  17.437 -13.295  1.00 51.55           N  
ANISOU 5017  N   VAL B 277     8124   4670   6794    608   1329   -767       N  
ATOM   5018  CA  VAL B 277      18.042  17.147 -12.674  1.00 50.82           C  
ANISOU 5018  CA  VAL B 277     7902   4605   6802    685   1417   -727       C  
ATOM   5019  CB  VAL B 277      18.354  15.645 -12.729  1.00 48.22           C  
ANISOU 5019  CB  VAL B 277     7618   4211   6494    715   1451   -758       C  
ATOM   5020  CG1 VAL B 277      17.535  14.896 -11.688  1.00 42.16           C  
ANISOU 5020  CG1 VAL B 277     6796   3423   5798    696   1336   -750       C  
ATOM   5021  CG2 VAL B 277      18.074  15.119 -14.120  1.00 52.30           C  
ANISOU 5021  CG2 VAL B 277     8330   4657   6883    688   1486   -830       C  
ATOM   5022  C   VAL B 277      19.162  17.915 -13.352  1.00 47.30           C  
ANISOU 5022  C   VAL B 277     7450   4197   6326    723   1542   -713       C  
ATOM   5023  O   VAL B 277      19.001  18.401 -14.469  1.00 51.05           O  
ANISOU 5023  O   VAL B 277     8045   4659   6691    696   1575   -746       O  
ATOM   5024  N   ALA B 278      20.299  18.018 -12.673  1.00 51.83           N  
ANISOU 5024  N   ALA B 278     7879   4819   6993    781   1606   -659       N  
ATOM   5025  CA  ALA B 278      21.448  18.742 -13.208  1.00 58.41           C  
ANISOU 5025  CA  ALA B 278     8686   5692   7813    817   1722   -634       C  
ATOM   5026  CB  ALA B 278      22.583  18.742 -12.200  1.00 58.53           C  
ANISOU 5026  CB  ALA B 278     8524   5766   7947    871   1763   -567       C  
ATOM   5027  C   ALA B 278      21.926  18.166 -14.538  1.00 59.34           C  
ANISOU 5027  C   ALA B 278     8954   5755   7839    836   1824   -683       C  
ATOM   5028  O   ALA B 278      21.933  16.953 -14.739  1.00 58.74           O  
ANISOU 5028  O   ALA B 278     8947   5616   7755    852   1838   -719       O  
ATOM   5029  N   GLY B 279      22.312  19.053 -15.448  1.00 59.70           N  
ANISOU 5029  N   GLY B 279     9049   5822   7813    834   1893   -683       N  
ATOM   5030  CA  GLY B 279      22.842  18.646 -16.736  1.00 60.15           C  
ANISOU 5030  CA  GLY B 279     9239   5835   7780    855   1993   -722       C  
ATOM   5031  C   GLY B 279      21.783  18.330 -17.773  1.00 59.67           C  
ANISOU 5031  C   GLY B 279     9368   5713   7590    800   1949   -794       C  
ATOM   5032  O   GLY B 279      22.104  18.139 -18.948  1.00 57.49           O  
ANISOU 5032  O   GLY B 279     9216   5405   7222    809   2024   -828       O  
ATOM   5033  N   ALA B 280      20.520  18.289 -17.349  1.00 55.44           N  
ANISOU 5033  N   ALA B 280     8855   5165   7044    741   1823   -814       N  
ATOM   5034  CA  ALA B 280      19.429  17.879 -18.233  1.00 55.49           C  
ANISOU 5034  CA  ALA B 280     9037   5116   6932    679   1761   -880       C  
ATOM   5035  CB  ALA B 280      18.115  17.839 -17.475  1.00 59.53           C  
ANISOU 5035  CB  ALA B 280     9532   5623   7462    617   1614   -884       C  
ATOM   5036  C   ALA B 280      19.315  18.797 -19.442  1.00 62.00           C  
ANISOU 5036  C   ALA B 280     9969   5958   7629    649   1793   -899       C  
ATOM   5037  O   ALA B 280      18.802  18.402 -20.488  1.00 63.47           O  
ANISOU 5037  O   ALA B 280    10314   6101   7701    612   1783   -953       O  
ATOM   5038  N   LEU B 281      19.795  20.026 -19.287  1.00 62.81           N  
ANISOU 5038  N   LEU B 281     9983   6130   7754    663   1829   -851       N  
ATOM   5039  CA  LEU B 281      19.833  20.982 -20.380  1.00 60.87           C  
ANISOU 5039  CA  LEU B 281     9820   5910   7398    642   1871   -859       C  
ATOM   5040  CB  LEU B 281      19.228  22.319 -19.942  1.00 53.83           C  
ANISOU 5040  CB  LEU B 281     8867   5082   6505    600   1801   -826       C  
ATOM   5041  CG  LEU B 281      19.175  23.378 -21.042  1.00 48.65           C  
ANISOU 5041  CG  LEU B 281     8295   4458   5730    573   1834   -831       C  
ATOM   5042  CD1 LEU B 281      18.201  22.950 -22.123  1.00 36.74           C  
ANISOU 5042  CD1 LEU B 281     6971   2908   4080    513   1778   -893       C  
ATOM   5043  CD2 LEU B 281      18.792  24.744 -20.473  1.00 50.36           C  
ANISOU 5043  CD2 LEU B 281     8427   4743   5964    546   1782   -787       C  
ATOM   5044  C   LEU B 281      21.268  21.177 -20.856  1.00 67.63           C  
ANISOU 5044  C   LEU B 281    10641   6784   8272    710   2014   -832       C  
ATOM   5045  O   LEU B 281      22.100  21.716 -20.128  1.00 67.08           O  
ANISOU 5045  O   LEU B 281    10423   6765   8301    751   2059   -774       O  
ATOM   5046  N   THR B 282      21.559  20.733 -22.073  1.00 74.37           N  
ANISOU 5046  N   THR B 282    11629   7598   9031    720   2083   -871       N  
ATOM   5047  CA  THR B 282      22.912  20.826 -22.610  1.00 77.56           C  
ANISOU 5047  CA  THR B 282    12012   8012   9445    786   2220   -846       C  
ATOM   5048  CB  THR B 282      23.370  19.471 -23.195  1.00 76.35           C  
ANISOU 5048  CB  THR B 282    11955   7786   9269    826   2285   -884       C  
ATOM   5049  OG1 THR B 282      22.673  19.214 -24.418  1.00 71.79           O  
ANISOU 5049  OG1 THR B 282    11561   7164   8551    784   2267   -946       O  
ATOM   5050  CG2 THR B 282      23.094  18.342 -22.207  1.00 75.55           C  
ANISOU 5050  CG2 THR B 282    11807   7644   9253    834   2231   -894       C  
ATOM   5051  C   THR B 282      22.993  21.920 -23.681  1.00 79.70           C  
ANISOU 5051  C   THR B 282    12349   8318   9615    767   2261   -843       C  
ATOM   5052  O   THR B 282      21.974  22.279 -24.277  1.00 78.99           O  
ANISOU 5052  O   THR B 282    12366   8226   9420    705   2190   -878       O  
ATOM   5053  N   PRO B 283      24.203  22.467 -23.914  1.00 80.41           N  
ANISOU 5053  N   PRO B 283    12372   8445   9737    820   2370   -797       N  
ATOM   5054  CA  PRO B 283      24.435  23.535 -24.898  1.00 77.05           C  
ANISOU 5054  CA  PRO B 283    11992   8056   9226    810   2419   -786       C  
ATOM   5055  CB  PRO B 283      25.971  23.631 -24.960  1.00 80.63           C  
ANISOU 5055  CB  PRO B 283    12358   8531   9748    884   2548   -735       C  
ATOM   5056  CG  PRO B 283      26.494  22.460 -24.151  1.00 84.19           C  
ANISOU 5056  CG  PRO B 283    12742   8947  10301    932   2567   -728       C  
ATOM   5057  CD  PRO B 283      25.428  22.173 -23.153  1.00 82.08           C  
ANISOU 5057  CD  PRO B 283    12441   8672  10074    888   2445   -746       C  
ATOM   5058  C   PRO B 283      23.863  23.259 -26.289  1.00 70.84           C  
ANISOU 5058  C   PRO B 283    11398   7228   8291    779   2417   -846       C  
ATOM   5059  O   PRO B 283      23.409  24.200 -26.942  1.00 66.78           O  
ANISOU 5059  O   PRO B 283    10937   6748   7690    738   2394   -848       O  
ATOM   5060  N   GLU B 284      23.876  22.004 -26.729  1.00 70.18           N  
ANISOU 5060  N   GLU B 284    11415   7074   8175    797   2437   -893       N  
ATOM   5061  CA  GLU B 284      23.393  21.673 -28.066  1.00 75.36           C  
ANISOU 5061  CA  GLU B 284    12255   7688   8691    770   2437   -950       C  
ATOM   5062  CB  GLU B 284      23.611  20.188 -28.370  1.00 84.89           C  
ANISOU 5062  CB  GLU B 284    13551   8813   9888    803   2473   -994       C  
ATOM   5063  CG  GLU B 284      22.645  19.636 -29.411  1.00 93.92           C  
ANISOU 5063  CG  GLU B 284    14884   9906  10897    749   2417  -1064       C  
ATOM   5064  CD  GLU B 284      22.726  18.130 -29.564  1.00102.12           C  
ANISOU 5064  CD  GLU B 284    16008  10860  11933    773   2437  -1110       C  
ATOM   5065  OE1 GLU B 284      23.637  17.514 -28.971  1.00104.81           O  
ANISOU 5065  OE1 GLU B 284    16269  11183  12372    840   2509  -1086       O  
ATOM   5066  OE2 GLU B 284      21.873  17.563 -30.280  1.00105.10           O  
ANISOU 5066  OE2 GLU B 284    16533  11189  12209    724   2379  -1168       O  
ATOM   5067  C   GLU B 284      21.917  22.032 -28.250  1.00 71.57           C  
ANISOU 5067  C   GLU B 284    11857   7216   8121    680   2306   -985       C  
ATOM   5068  O   GLU B 284      21.552  22.685 -29.225  1.00 72.73           O  
ANISOU 5068  O   GLU B 284    12093   7383   8158    645   2298   -998       O  
ATOM   5069  N   MET B 285      21.068  21.616 -27.316  1.00 74.78           N  
ANISOU 5069  N   MET B 285    12231   7609   8574    642   2202   -997       N  
ATOM   5070  CA  MET B 285      19.647  21.928 -27.415  1.00 74.80           C  
ANISOU 5070  CA  MET B 285    12303   7621   8495    554   2069  -1024       C  
ATOM   5071  CB  MET B 285      18.823  21.007 -26.497  1.00 78.01           C  
ANISOU 5071  CB  MET B 285    12697   7989   8956    523   1966  -1047       C  
ATOM   5072  CG  MET B 285      19.084  21.147 -25.007  1.00 79.23           C  
ANISOU 5072  CG  MET B 285    12676   8169   9257    551   1948  -1000       C  
ATOM   5073  SD  MET B 285      18.309  19.850 -24.003  1.00 97.04           S  
ANISOU 5073  SD  MET B 285    14918  10368  11585    528   1846  -1026       S  
ATOM   5074  CE  MET B 285      19.593  18.634 -23.882  1.00 68.68           C  
ANISOU 5074  CE  MET B 285    11297   6723   8075    619   1967  -1028       C  
ATOM   5075  C   MET B 285      19.408  23.413 -27.108  1.00 65.32           C  
ANISOU 5075  C   MET B 285    11021   6501   7296    526   2036   -978       C  
ATOM   5076  O   MET B 285      18.461  24.012 -27.615  1.00 57.51           O  
ANISOU 5076  O   MET B 285    10106   5538   6209    461   1958   -990       O  
ATOM   5077  N   LEU B 286      20.296  24.015 -26.323  1.00 61.40           N  
ANISOU 5077  N   LEU B 286    10374   6047   6910    576   2097   -921       N  
ATOM   5078  CA  LEU B 286      20.238  25.454 -26.087  1.00 63.37           C  
ANISOU 5078  CA  LEU B 286    10545   6371   7163    557   2083   -874       C  
ATOM   5079  CB  LEU B 286      21.217  25.861 -24.984  1.00 61.75           C  
ANISOU 5079  CB  LEU B 286    10156   6203   7102    612   2139   -813       C  
ATOM   5080  CG  LEU B 286      20.827  27.133 -24.231  1.00 65.44           C  
ANISOU 5080  CG  LEU B 286    10522   6738   7604    582   2082   -767       C  
ATOM   5081  CD1 LEU B 286      19.424  26.994 -23.661  1.00 67.41           C  
ANISOU 5081  CD1 LEU B 286    10801   6978   7832    518   1940   -791       C  
ATOM   5082  CD2 LEU B 286      21.834  27.446 -23.134  1.00 65.01           C  
ANISOU 5082  CD2 LEU B 286    10284   6719   7698    635   2135   -706       C  
ATOM   5083  C   LEU B 286      20.536  26.234 -27.370  1.00 67.71           C  
ANISOU 5083  C   LEU B 286    11173   6948   7606    555   2145   -872       C  
ATOM   5084  O   LEU B 286      19.942  27.283 -27.628  1.00 67.90           O  
ANISOU 5084  O   LEU B 286    11212   7022   7566    508   2096   -858       O  
ATOM   5085  N   LYS B 287      21.450  25.708 -28.179  1.00 70.41           N  
ANISOU 5085  N   LYS B 287    11567   7258   7930    606   2251   -884       N  
ATOM   5086  CA  LYS B 287      21.857  26.382 -29.409  1.00 70.23           C  
ANISOU 5086  CA  LYS B 287    11612   7256   7815    613   2319   -878       C  
ATOM   5087  CB  LYS B 287      23.048  25.660 -30.046  1.00 77.60           C  
ANISOU 5087  CB  LYS B 287    12576   8150   8760    685   2447   -884       C  
ATOM   5088  CG  LYS B 287      24.378  25.944 -29.363  1.00 81.64           C  
ANISOU 5088  CG  LYS B 287    12931   8689   9397    754   2544   -822       C  
ATOM   5089  CD  LYS B 287      25.148  27.052 -30.067  1.00 84.33           C  
ANISOU 5089  CD  LYS B 287    13248   9082   9713    775   2624   -779       C  
ATOM   5090  CE  LYS B 287      26.506  27.264 -29.418  1.00 84.52           C  
ANISOU 5090  CE  LYS B 287    13118   9133   9863    840   2718   -716       C  
ATOM   5091  NZ  LYS B 287      26.993  26.025 -28.745  1.00 84.68           N  
ANISOU 5091  NZ  LYS B 287    13098   9107   9971    887   2744   -722       N  
ATOM   5092  C   LYS B 287      20.718  26.492 -30.420  1.00 62.73           C  
ANISOU 5092  C   LYS B 287    10816   6302   6717    544   2240   -923       C  
ATOM   5093  O   LYS B 287      20.705  27.406 -31.244  1.00 60.68           O  
ANISOU 5093  O   LYS B 287    10593   6082   6380    528   2257   -909       O  
ATOM   5094  N   ASP B 288      19.756  25.577 -30.352  1.00 53.49           N  
ANISOU 5094  N   ASP B 288     7852   5764   6706    561   2470   -367       N  
ATOM   5095  CA  ASP B 288      18.672  25.580 -31.328  1.00 61.27           C  
ANISOU 5095  CA  ASP B 288     8944   6759   7576    537   2449   -359       C  
ATOM   5096  CB  ASP B 288      18.541  24.197 -31.974  1.00 72.53           C  
ANISOU 5096  CB  ASP B 288    10395   8182   8981    555   2453   -394       C  
ATOM   5097  CG  ASP B 288      19.747  23.838 -32.833  1.00 79.77           C  
ANISOU 5097  CG  ASP B 288    11278   9091   9940    555   2553   -429       C  
ATOM   5098  OD1 ASP B 288      20.060  24.613 -33.764  1.00 83.62           O  
ANISOU 5098  OD1 ASP B 288    11795   9582  10396    522   2615   -422       O  
ATOM   5099  OD2 ASP B 288      20.375  22.785 -32.586  1.00 75.36           O  
ANISOU 5099  OD2 ASP B 288    10664   8523   9448    588   2567   -462       O  
ATOM   5100  C   ASP B 288      17.329  26.018 -30.748  1.00 59.18           C  
ANISOU 5100  C   ASP B 288     8735   6505   7247    529   2353   -324       C  
ATOM   5101  O   ASP B 288      16.276  25.677 -31.284  1.00 61.06           O  
ANISOU 5101  O   ASP B 288     9052   6750   7399    520   2308   -319       O  
ATOM   5102  N   MET B 289      17.362  26.776 -29.655  1.00 57.25           N  
ANISOU 5102  N   MET B 289     8446   6261   7044    532   2320   -299       N  
ATOM   5103  CA  MET B 289      16.148  27.425 -29.165  1.00 54.26           C  
ANISOU 5103  CA  MET B 289     8120   5892   6603    518   2237   -263       C  
ATOM   5104  CB  MET B 289      16.207  27.646 -27.650  1.00 55.02           C  
ANISOU 5104  CB  MET B 289     8148   5988   6768    541   2184   -250       C  
ATOM   5105  CG  MET B 289      15.918  26.397 -26.826  1.00 56.04           C  
ANISOU 5105  CG  MET B 289     8248   6115   6930    581   2119   -270       C  
ATOM   5106  SD  MET B 289      16.012  26.674 -25.040  1.00 64.42           S  
ANISOU 5106  SD  MET B 289     9224   7176   8078    606   2052   -256       S  
ATOM   5107  CE  MET B 289      14.536  27.656 -24.753  1.00 59.51           C  
ANISOU 5107  CE  MET B 289     8684   6569   7358    579   1969   -213       C  
ATOM   5108  C   MET B 289      15.964  28.749 -29.897  1.00 51.32           C  
ANISOU 5108  C   MET B 289     7799   5526   6173    475   2266   -234       C  
ATOM   5109  O   MET B 289      16.901  29.241 -30.534  1.00 53.59           O  
ANISOU 5109  O   MET B 289     8064   5810   6486    458   2349   -240       O  
ATOM   5110  N   ALA B 290      14.768  29.326 -29.811  1.00 52.90           N  
ANISOU 5110  N   ALA B 290     8066   5736   6298    456   2194   -203       N  
ATOM   5111  CA  ALA B 290      14.485  30.594 -30.486  1.00 51.02           C  
ANISOU 5111  CA  ALA B 290     7877   5504   6005    414   2208   -174       C  
ATOM   5112  CB  ALA B 290      13.033  30.992 -30.282  1.00 41.27           C  
ANISOU 5112  CB  ALA B 290     6712   4278   4691    400   2109   -143       C  
ATOM   5113  C   ALA B 290      15.410  31.718 -30.015  1.00 51.27           C  
ANISOU 5113  C   ALA B 290     7846   5533   6100    403   2257   -159       C  
ATOM   5114  O   ALA B 290      16.133  31.568 -29.024  1.00 46.75           O  
ANISOU 5114  O   ALA B 290     7190   4956   5616    428   2268   -167       O  
ATOM   5115  N   LYS B 291      15.403  32.831 -30.749  1.00 49.19           N  
ANISOU 5115  N   LYS B 291     7617   5274   5797    365   2286   -139       N  
ATOM   5116  CA  LYS B 291      16.128  34.023 -30.323  1.00 48.62           C  
ANISOU 5116  CA  LYS B 291     7493   5204   5777    349   2323   -119       C  
ATOM   5117  CB  LYS B 291      15.960  35.168 -31.323  1.00 54.19           C  
ANISOU 5117  CB  LYS B 291     8251   5916   6421    305   2346    -97       C  
ATOM   5118  CG  LYS B 291      16.680  36.449 -30.907  1.00 58.41           C  
ANISOU 5118  CG  LYS B 291     8733   6453   7007    285   2381    -75       C  
ATOM   5119  CD  LYS B 291      16.493  37.572 -31.914  1.00 61.24           C  
ANISOU 5119  CD  LYS B 291     9144   6819   7305    242   2398    -54       C  
ATOM   5120  CE  LYS B 291      15.113  38.190 -31.797  1.00 61.53           C  
ANISOU 5120  CE  LYS B 291     9247   6864   7266    224   2304    -24       C  
ATOM   5121  NZ  LYS B 291      14.941  39.320 -32.750  1.00 65.90           N  
ANISOU 5121  NZ  LYS B 291     9845   7426   7768    183   2315     -4       N  
ATOM   5122  C   LYS B 291      15.615  34.444 -28.953  1.00 40.67           C  
ANISOU 5122  C   LYS B 291     6459   4200   4793    360   2250    -95       C  
ATOM   5123  O   LYS B 291      14.415  34.377 -28.699  1.00 44.81           O  
ANISOU 5123  O   LYS B 291     7040   4731   5257    360   2166    -80       O  
ATOM   5124  N   ASP B 292      16.531  34.876 -28.089  1.00 51.19           N  
ANISOU 5124  N   ASP B 292     7703   5530   6217    369   2282    -91       N  
ATOM   5125  CA  ASP B 292      16.212  35.248 -26.710  1.00 47.67           C  
ANISOU 5125  CA  ASP B 292     7215   5088   5809    382   2221    -71       C  
ATOM   5126  CB  ASP B 292      15.298  36.477 -26.672  1.00 49.76           C  
ANISOU 5126  CB  ASP B 292     7535   5363   6008    349   2170    -33       C  
ATOM   5127  CG  ASP B 292      15.925  37.688 -27.324  1.00 53.53           C  
ANISOU 5127  CG  ASP B 292     8007   5844   6489    312   2232    -16       C  
ATOM   5128  OD1 ASP B 292      17.145  37.889 -27.153  1.00 55.89           O  
ANISOU 5128  OD1 ASP B 292     8226   6139   6871    315   2301    -23       O  
ATOM   5129  OD2 ASP B 292      15.197  38.439 -28.007  1.00 54.72           O  
ANISOU 5129  OD2 ASP B 292     8228   6001   6561    280   2206      5       O  
ATOM   5130  C   ASP B 292      15.553  34.096 -25.964  1.00 45.05           C  
ANISOU 5130  C   ASP B 292     6886   4754   5477    419   2149    -86       C  
ATOM   5131  O   ASP B 292      14.394  34.199 -25.571  1.00 46.22           O  
ANISOU 5131  O   ASP B 292     7085   4909   5566    417   2066    -69       O  
ATOM   5132  N   PRO B 293      16.284  32.984 -25.776  1.00 47.78           N  
ANISOU 5132  N   PRO B 293     7174   5091   5890    453   2176   -120       N  
ATOM   5133  CA  PRO B 293      15.664  31.859 -25.073  1.00 45.51           C  
ANISOU 5133  CA  PRO B 293     6886   4803   5603    488   2102   -135       C  
ATOM   5134  CB  PRO B 293      16.669  30.724 -25.271  1.00 42.81           C  
ANISOU 5134  CB  PRO B 293     6485   4450   5331    516   2154   -173       C  
ATOM   5135  CG  PRO B 293      17.973  31.403 -25.434  1.00 42.35           C  
ANISOU 5135  CG  PRO B 293     6357   4387   5348    504   2241   -174       C  
ATOM   5136  CD  PRO B 293      17.672  32.684 -26.173  1.00 49.39           C  
ANISOU 5136  CD  PRO B 293     7310   5287   6171    460   2266   -145       C  
ATOM   5137  C   PRO B 293      15.459  32.159 -23.592  1.00 39.98           C  
ANISOU 5137  C   PRO B 293     6129   4105   4956    505   2037   -119       C  
ATOM   5138  O   PRO B 293      16.293  32.813 -22.968  1.00 40.52           O  
ANISOU 5138  O   PRO B 293     6117   4171   5107    505   2069   -111       O  
ATOM   5139  N   ILE B 294      14.350  31.679 -23.047  1.00 36.05           N  
ANISOU 5139  N   ILE B 294     5672   3612   4412    519   1945   -115       N  
ATOM   5140  CA  ILE B 294      14.039  31.876 -21.642  1.00 34.24           C  
ANISOU 5140  CA  ILE B 294     5397   3387   4228    537   1873   -103       C  
ATOM   5141  CB  ILE B 294      12.624  32.468 -21.480  1.00 29.73           C  
ANISOU 5141  CB  ILE B 294     4910   2828   3559    517   1790    -74       C  
ATOM   5142  CG1 ILE B 294      12.535  33.815 -22.202  1.00 31.14           C  
ANISOU 5142  CG1 ILE B 294     5135   3013   3685    473   1831    -45       C  
ATOM   5143  CD1 ILE B 294      11.113  34.278 -22.462  1.00 33.98           C  
ANISOU 5143  CD1 ILE B 294     5593   3383   3934    447   1754    -19       C  
ATOM   5144  CG2 ILE B 294      12.237  32.619 -20.007  1.00 27.42           C  
ANISOU 5144  CG2 ILE B 294     4572   2539   3308    536   1708    -64       C  
ATOM   5145  C   ILE B 294      14.180  30.541 -20.910  1.00 33.85           C  
ANISOU 5145  C   ILE B 294     5292   3331   4237    579   1827   -131       C  
ATOM   5146  O   ILE B 294      13.458  29.581 -21.184  1.00 39.76           O  
ANISOU 5146  O   ILE B 294     6095   4083   4931    590   1780   -144       O  
ATOM   5147  N   ILE B 295      15.130  30.475 -19.986  1.00 34.50           N  
ANISOU 5147  N   ILE B 295     5266   3406   4437    601   1835   -138       N  
ATOM   5148  CA  ILE B 295      15.422  29.218 -19.300  1.00 36.11           C  
ANISOU 5148  CA  ILE B 295     5406   3602   4711    639   1793   -164       C  
ATOM   5149  CB  ILE B 295      16.896  28.785 -19.521  1.00 43.81           C  
ANISOU 5149  CB  ILE B 295     6293   4566   5787    652   1873   -187       C  
ATOM   5150  CG1 ILE B 295      17.113  28.329 -20.963  1.00 48.57           C  
ANISOU 5150  CG1 ILE B 295     6956   5166   6334    642   1949   -208       C  
ATOM   5151  CD1 ILE B 295      17.427  29.448 -21.919  1.00 51.84           C  
ANISOU 5151  CD1 ILE B 295     7406   5583   6709    604   2032   -193       C  
ATOM   5152  CG2 ILE B 295      17.285  27.650 -18.572  1.00 45.64           C  
ANISOU 5152  CG2 ILE B 295     6441   4792   6110    690   1819   -208       C  
ATOM   5153  C   ILE B 295      15.154  29.288 -17.797  1.00 33.77           C  
ANISOU 5153  C   ILE B 295     5047   3307   4475    658   1700   -151       C  
ATOM   5154  O   ILE B 295      15.795  30.049 -17.079  1.00 40.54           O  
ANISOU 5154  O   ILE B 295     5825   4163   5413    655   1710   -136       O  
ATOM   5155  N   PHE B 296      14.213  28.474 -17.334  1.00 32.67           N  
ANISOU 5155  N   PHE B 296     4941   3174   4299    674   1606   -157       N  
ATOM   5156  CA  PHE B 296      13.988  28.263 -15.903  1.00 35.59           C  
ANISOU 5156  CA  PHE B 296     5246   3546   4732    694   1506   -150       C  
ATOM   5157  CB  PHE B 296      12.494  28.199 -15.596  1.00 36.51           C  
ANISOU 5157  CB  PHE B 296     5444   3674   4753    688   1403   -136       C  
ATOM   5158  CG  PHE B 296      11.781  29.505 -15.763  1.00 37.92           C  
ANISOU 5158  CG  PHE B 296     5689   3861   4858    658   1400   -107       C  
ATOM   5159  CD2 PHE B 296      11.663  30.378 -14.701  1.00 38.53           C  
ANISOU 5159  CD2 PHE B 296     5723   3938   4979    653   1349    -83       C  
ATOM   5160  CE2 PHE B 296      10.993  31.585 -14.846  1.00 32.96           C  
ANISOU 5160  CE2 PHE B 296     5079   3240   4205    623   1342    -56       C  
ATOM   5161  CZ  PHE B 296      10.435  31.927 -16.063  1.00 37.04           C  
ANISOU 5161  CZ  PHE B 296     5703   3763   4608    599   1389    -52       C  
ATOM   5162  CE1 PHE B 296      10.540  31.057 -17.131  1.00 45.68           C  
ANISOU 5162  CE1 PHE B 296     6838   4858   5660    601   1436    -72       C  
ATOM   5163  CD1 PHE B 296      11.206  29.849 -16.977  1.00 43.54           C  
ANISOU 5163  CD1 PHE B 296     6506   4579   5457    631   1443   -101       C  
ATOM   5164  C   PHE B 296      14.651  26.972 -15.429  1.00 36.21           C  
ANISOU 5164  C   PHE B 296     5244   3616   4896    727   1484   -176       C  
ATOM   5165  O   PHE B 296      14.102  25.891 -15.616  1.00 48.16           O  
ANISOU 5165  O   PHE B 296     6798   5133   6367    741   1442   -194       O  
ATOM   5166  N   ALA B 297      15.824  27.081 -14.813  1.00 33.56           N  
ANISOU 5166  N   ALA B 297     4796   3273   4680    736   1510   -177       N  
ATOM   5167  CA  ALA B 297      16.570  25.898 -14.383  1.00 36.34           C  
ANISOU 5167  CA  ALA B 297     5068   3619   5120    765   1493   -201       C  
ATOM   5168  CB  ALA B 297      18.055  26.024 -14.761  1.00 33.95           C  
ANISOU 5168  CB  ALA B 297     4687   3306   4905    765   1593   -212       C  
ATOM   5169  C   ALA B 297      16.398  25.706 -12.882  1.00 31.34           C  
ANISOU 5169  C   ALA B 297     4361   2992   4556    777   1382   -188       C  
ATOM   5170  O   ALA B 297      17.197  26.197 -12.085  1.00 37.09           O  
ANISOU 5170  O   ALA B 297     4990   3720   5381    775   1379   -174       O  
ATOM   5171  N   MET B 298      15.346  24.993 -12.499  1.00 34.02           N  
ANISOU 5171  N   MET B 298     4745   3339   4842    787   1286   -191       N  
ATOM   5172  CA  MET B 298      14.946  24.954 -11.097  1.00 34.64           C  
ANISOU 5172  CA  MET B 298     4770   3428   4964    791   1169   -174       C  
ATOM   5173  CB  MET B 298      13.475  25.382 -10.966  1.00 35.84           C  
ANISOU 5173  CB  MET B 298     5014   3593   5010    775   1093   -156       C  
ATOM   5174  CG  MET B 298      13.288  26.907 -11.161  1.00 25.29           C  
ANISOU 5174  CG  MET B 298     3710   2258   3642    748   1131   -128       C  
ATOM   5175  SD  MET B 298      11.613  27.443 -11.518  1.00 51.04           S  
ANISOU 5175  SD  MET B 298     7107   5533   6753    725   1074   -110       S  
ATOM   5176  CE  MET B 298      11.168  26.314 -12.840  1.00 67.06           C  
ANISOU 5176  CE  MET B 298     9232   7564   8685    732   1112   -140       C  
ATOM   5177  C   MET B 298      15.195  23.589 -10.460  1.00 41.15           C  
ANISOU 5177  C   MET B 298     5537   4253   5846    818   1106   -194       C  
ATOM   5178  O   MET B 298      14.571  23.241  -9.460  1.00 51.39           O  
ANISOU 5178  O   MET B 298     6817   5562   7148    822    995   -186       O  
ATOM   5179  N   ALA B 299      16.132  22.832 -11.027  1.00 36.10           N  
ANISOU 5179  N   ALA B 299     4865   3601   5251    835   1174   -221       N  
ATOM   5180  CA  ALA B 299      16.567  21.582 -10.416  1.00 41.87           C  
ANISOU 5180  CA  ALA B 299     5530   4329   6049    861   1123   -240       C  
ATOM   5181  CB  ALA B 299      17.480  20.798 -11.358  1.00 44.07           C  
ANISOU 5181  CB  ALA B 299     5800   4592   6353    878   1215   -271       C  
ATOM   5182  C   ALA B 299      17.278  21.859  -9.099  1.00 51.02           C  
ANISOU 5182  C   ALA B 299     6573   5496   7318    859   1070   -220       C  
ATOM   5183  O   ALA B 299      18.064  22.804  -8.987  1.00 53.20           O  
ANISOU 5183  O   ALA B 299     6793   5771   7650    844   1122   -203       O  
ATOM   5184  N   ASN B 300      16.986  21.029  -8.107  1.00 56.06           N  
ANISOU 5184  N   ASN B 300     7176   6144   7982    872    965   -220       N  
ATOM   5185  CA  ASN B 300      17.629  21.098  -6.804  1.00 66.54           C  
ANISOU 5185  CA  ASN B 300     8393   7482   9405    868    901   -202       C  
ATOM   5186  CB  ASN B 300      16.563  21.061  -5.704  1.00 68.01           C  
ANISOU 5186  CB  ASN B 300     8591   7691   9561    860    768   -184       C  
ATOM   5187  CG  ASN B 300      17.015  21.722  -4.417  1.00 74.14           C  
ANISOU 5187  CG  ASN B 300     9272   8487  10412    839    709   -153       C  
ATOM   5188  OD1 ASN B 300      18.084  21.420  -3.886  1.00 75.91           O  
ANISOU 5188  OD1 ASN B 300     9405   8713  10725    841    714   -151       O  
ATOM   5189  ND2 ASN B 300      16.193  22.631  -3.904  1.00 74.79           N  
ANISOU 5189  ND2 ASN B 300     9376   8585  10457    815    651   -128       N  
ATOM   5190  C   ASN B 300      18.624  19.940  -6.653  1.00 72.12           C  
ANISOU 5190  C   ASN B 300     9033   8181  10188    892    911   -223       C  
ATOM   5191  O   ASN B 300      18.287  18.792  -6.952  1.00 73.53           O  
ANISOU 5191  O   ASN B 300     9251   8354  10335    915    890   -248       O  
ATOM   5192  N   PRO B 301      19.857  20.228  -6.201  1.00 71.51           N  
ANISOU 5192  N   PRO B 301     8857   8105  10210    885    941   -213       N  
ATOM   5193  CA  PRO B 301      20.409  21.529  -5.806  1.00 71.84           C  
ANISOU 5193  CA  PRO B 301     8840   8154  10301    857    965   -184       C  
ATOM   5194  CB  PRO B 301      21.383  21.153  -4.690  1.00 75.14           C  
ANISOU 5194  CB  PRO B 301     9146   8583  10821    855    918   -174       C  
ATOM   5195  CG  PRO B 301      21.899  19.820  -5.112  1.00 74.81           C  
ANISOU 5195  CG  PRO B 301     9099   8525  10800    885    943   -205       C  
ATOM   5196  CD  PRO B 301      20.773  19.126  -5.850  1.00 73.07           C  
ANISOU 5196  CD  PRO B 301     8985   8296  10481    905    932   -228       C  
ATOM   5197  C   PRO B 301      21.140  22.264  -6.924  1.00 70.65           C  
ANISOU 5197  C   PRO B 301     8699   7988  10158    850   1097   -191       C  
ATOM   5198  O   PRO B 301      21.307  23.482  -6.841  1.00 73.07           O  
ANISOU 5198  O   PRO B 301     8986   8299  10476    825   1125   -168       O  
ATOM   5199  N   GLU B 302      21.583  21.543  -7.947  1.00 68.12           N  
ANISOU 5199  N   GLU B 302     8406   7649   9828    869   1176   -222       N  
ATOM   5200  CA  GLU B 302      22.234  22.197  -9.071  1.00 71.78           C  
ANISOU 5200  CA  GLU B 302     8886   8100  10286    860   1301   -229       C  
ATOM   5201  CB  GLU B 302      23.520  21.471  -9.468  1.00 74.48           C  
ANISOU 5201  CB  GLU B 302     9170   8427  10700    875   1367   -253       C  
ATOM   5202  CG  GLU B 302      23.993  21.822 -10.875  1.00 78.62           C  
ANISOU 5202  CG  GLU B 302     9740   8938  11195    869   1496   -271       C  
ATOM   5203  CD  GLU B 302      25.475  22.127 -10.933  1.00 85.67           C  
ANISOU 5203  CD  GLU B 302    10545   9825  12182    862   1567   -272       C  
ATOM   5204  OE1 GLU B 302      26.226  21.596 -10.085  1.00 90.58           O  
ANISOU 5204  OE1 GLU B 302    11078  10447  12891    871   1525   -270       O  
ATOM   5205  OE2 GLU B 302      25.887  22.910 -11.816  1.00 85.12           O  
ANISOU 5205  OE2 GLU B 302    10495   9750  12095    844   1663   -272       O  
ATOM   5206  C   GLU B 302      21.289  22.288 -10.260  1.00 67.77           C  
ANISOU 5206  C   GLU B 302     8501   7585   9662    860   1348   -243       C  
ATOM   5207  O   GLU B 302      20.684  21.292 -10.661  1.00 68.07           O  
ANISOU 5207  O   GLU B 302     8598   7618   9645    879   1326   -266       O  
ATOM   5208  N   PRO B 303      21.164  23.496 -10.825  1.00 61.45           N  
ANISOU 5208  N   PRO B 303     7739   6786   8823    836   1410   -228       N  
ATOM   5209  CA  PRO B 303      20.302  23.755 -11.980  1.00 56.93           C  
ANISOU 5209  CA  PRO B 303     7286   6210   8133    828   1459   -235       C  
ATOM   5210  CB  PRO B 303      20.565  25.233 -12.288  1.00 54.41           C  
ANISOU 5210  CB  PRO B 303     6970   5894   7810    798   1526   -211       C  
ATOM   5211  CG  PRO B 303      21.061  25.807 -11.014  1.00 56.69           C  
ANISOU 5211  CG  PRO B 303     7154   6192   8194    790   1472   -185       C  
ATOM   5212  CD  PRO B 303      21.846  24.717 -10.362  1.00 57.42           C  
ANISOU 5212  CD  PRO B 303     7159   6281   8375    811   1435   -200       C  
ATOM   5213  C   PRO B 303      20.655  22.893 -13.184  1.00 50.61           C  
ANISOU 5213  C   PRO B 303     6529   5397   7304    841   1538   -270       C  
ATOM   5214  O   PRO B 303      21.800  22.454 -13.322  1.00 53.21           O  
ANISOU 5214  O   PRO B 303     6791   5716   7709    851   1588   -286       O  
ATOM   5215  N   GLU B 304      19.669  22.665 -14.047  1.00 44.09           N  
ANISOU 5215  N   GLU B 304     5813   4571   6367    840   1546   -280       N  
ATOM   5216  CA  GLU B 304      19.878  21.984 -15.322  1.00 49.17           C  
ANISOU 5216  CA  GLU B 304     6511   5205   6967    846   1624   -311       C  
ATOM   5217  CB  GLU B 304      18.612  22.080 -16.178  1.00 44.50           C  
ANISOU 5217  CB  GLU B 304     6048   4620   6240    833   1621   -311       C  
ATOM   5218  CG  GLU B 304      17.462  21.182 -15.718  1.00 45.04           C  
ANISOU 5218  CG  GLU B 304     6160   4695   6256    848   1515   -316       C  
ATOM   5219  CD  GLU B 304      16.688  21.718 -14.517  1.00 47.83           C  
ANISOU 5219  CD  GLU B 304     6502   5061   6610    843   1412   -287       C  
ATOM   5220  OE1 GLU B 304      17.048  22.780 -13.964  1.00 42.19           O  
ANISOU 5220  OE1 GLU B 304     5739   4350   5941    828   1418   -261       O  
ATOM   5221  OE2 GLU B 304      15.709  21.056 -14.119  1.00 42.83           O  
ANISOU 5221  OE2 GLU B 304     5905   4436   5931    851   1322   -289       O  
ATOM   5222  C   GLU B 304      21.073  22.551 -16.093  1.00 57.47           C  
ANISOU 5222  C   GLU B 304     7528   6248   8058    832   1741   -317       C  
ATOM   5223  O   GLU B 304      21.756  21.826 -16.824  1.00 52.40           O  
ANISOU 5223  O   GLU B 304     6880   5596   7435    843   1802   -345       O  
ATOM   5224  N   ILE B 305      21.310  23.851 -15.929  1.00 52.66           N  
ANISOU 5224  N   ILE B 305     6899   5644   7464    807   1770   -289       N  
ATOM   5225  CA  ILE B 305      22.509  24.514 -16.438  1.00 52.70           C  
ANISOU 5225  CA  ILE B 305     6857   5644   7522    791   1869   -289       C  
ATOM   5226  CB  ILE B 305      22.388  24.850 -17.941  1.00 52.45           C  
ANISOU 5226  CB  ILE B 305     6918   5611   7400    771   1964   -300       C  
ATOM   5227  CG1 ILE B 305      23.757  25.217 -18.528  1.00 51.47           C  
ANISOU 5227  CG1 ILE B 305     6738   5479   7337    759   2066   -308       C  
ATOM   5228  CD1 ILE B 305      23.766  25.325 -20.036  1.00 49.38           C  
ANISOU 5228  CD1 ILE B 305     6557   5212   6993    740   2158   -324       C  
ATOM   5229  CG2 ILE B 305      21.364  25.962 -18.165  1.00 56.53           C  
ANISOU 5229  CG2 ILE B 305     7519   6139   7822    743   1955   -271       C  
ATOM   5230  C   ILE B 305      22.728  25.781 -15.612  1.00 55.81           C  
ANISOU 5230  C   ILE B 305     7194   6046   7964    771   1853   -254       C  
ATOM   5231  O   ILE B 305      21.772  26.320 -15.044  1.00 45.29           O  
ANISOU 5231  O   ILE B 305     5893   4724   6591    763   1788   -231       O  
ATOM   5232  N   THR B 306      23.970  26.246 -15.508  1.00 50.89           N  
ANISOU 5232  N   THR B 306     6487   5421   7430    761   1908   -250       N  
ATOM   5233  CA  THR B 306      24.227  27.472 -14.758  1.00 42.37           C  
ANISOU 5233  CA  THR B 306     5350   4352   6398    739   1896   -217       C  
ATOM   5234  CB  THR B 306      25.642  27.509 -14.138  1.00 52.46           C  
ANISOU 5234  CB  THR B 306     6502   5627   7802    739   1910   -214       C  
ATOM   5235  OG1 THR B 306      26.610  27.806 -15.149  1.00 53.01           O  
ANISOU 5235  OG1 THR B 306     6569   5690   7883    726   2020   -227       O  
ATOM   5236  CG2 THR B 306      25.981  26.179 -13.475  1.00 50.47           C  
ANISOU 5236  CG2 THR B 306     6192   5370   7615    771   1851   -234       C  
ATOM   5237  C   THR B 306      24.037  28.656 -15.693  1.00 43.44           C  
ANISOU 5237  C   THR B 306     5552   4490   6462    707   1973   -203       C  
ATOM   5238  O   THR B 306      24.090  28.498 -16.913  1.00 45.14           O  
ANISOU 5238  O   THR B 306     5834   4699   6616    701   2048   -221       O  
ATOM   5239  N   PRO B 307      23.758  29.841 -15.128  1.00 44.43           N  
ANISOU 5239  N   PRO B 307     5664   4625   6590    685   1950   -170       N  
ATOM   5240  CA  PRO B 307      23.642  31.036 -15.963  1.00 44.52           C  
ANISOU 5240  CA  PRO B 307     5734   4642   6540    652   2022   -154       C  
ATOM   5241  CB  PRO B 307      23.467  32.158 -14.938  1.00 49.39           C  
ANISOU 5241  CB  PRO B 307     6302   5269   7194    635   1974   -118       C  
ATOM   5242  CG  PRO B 307      22.759  31.487 -13.795  1.00 49.20           C  
ANISOU 5242  CG  PRO B 307     6256   5248   7190    660   1859   -116       C  
ATOM   5243  CD  PRO B 307      23.308  30.085 -13.744  1.00 48.18           C  
ANISOU 5243  CD  PRO B 307     6087   5109   7108    689   1848   -146       C  
ATOM   5244  C   PRO B 307      24.887  31.258 -16.821  1.00 46.99           C  
ANISOU 5244  C   PRO B 307     6017   4949   6889    638   2126   -166       C  
ATOM   5245  O   PRO B 307      24.763  31.642 -17.981  1.00 43.33           O  
ANISOU 5245  O   PRO B 307     5629   4484   6349    618   2197   -169       O  
ATOM   5246  N   ASP B 308      26.063  30.997 -16.264  1.00 47.44           N  
ANISOU 5246  N   ASP B 308     5965   5002   7058    646   2131   -171       N  
ATOM   5247  CA  ASP B 308      27.308  31.262 -16.990  1.00 58.14           C  
ANISOU 5247  CA  ASP B 308     7284   6351   8453    632   2225   -182       C  
ATOM   5248  CB  ASP B 308      28.511  31.126 -16.060  1.00 65.03           C  
ANISOU 5248  CB  ASP B 308     8029   7223   9456    639   2207   -179       C  
ATOM   5249  CG  ASP B 308      28.717  32.356 -15.203  1.00 72.73           C  
ANISOU 5249  CG  ASP B 308     8944   8211  10480    614   2180   -143       C  
ATOM   5250  OD1 ASP B 308      28.235  33.440 -15.599  1.00 71.11           O  
ANISOU 5250  OD1 ASP B 308     8792   8014  10215    587   2206   -122       O  
ATOM   5251  OD2 ASP B 308      29.355  32.241 -14.135  1.00 77.52           O  
ANISOU 5251  OD2 ASP B 308     9452   8821  11183    620   2129   -134       O  
ATOM   5252  C   ASP B 308      27.502  30.369 -18.212  1.00 59.00           C  
ANISOU 5252  C   ASP B 308     7450   6450   8518    643   2291   -217       C  
ATOM   5253  O   ASP B 308      27.887  30.857 -19.275  1.00 66.08           O  
ANISOU 5253  O   ASP B 308     8384   7345   9378    621   2375   -222       O  
ATOM   5254  N   LYS B 309      27.247  29.072 -18.076  1.00 49.27           N  
ANISOU 5254  N   LYS B 309     6223   5210   7288    675   2251   -243       N  
ATOM   5255  CA  LYS B 309      27.399  28.180 -19.218  1.00 51.15           C  
ANISOU 5255  CA  LYS B 309     6514   5438   7484    686   2310   -278       C  
ATOM   5256  CB  LYS B 309      27.490  26.718 -18.777  1.00 50.56           C  
ANISOU 5256  CB  LYS B 309     6405   5354   7453    724   2261   -305       C  
ATOM   5257  CG  LYS B 309      28.020  26.549 -17.373  1.00 55.56           C  
ANISOU 5257  CG  LYS B 309     6926   5988   8195    739   2191   -292       C  
ATOM   5258  CD  LYS B 309      28.665  25.199 -17.144  1.00 66.13           C  
ANISOU 5258  CD  LYS B 309     8209   7315   9601    771   2175   -322       C  
ATOM   5259  CE  LYS B 309      30.135  25.236 -17.531  1.00 71.17           C  
ANISOU 5259  CE  LYS B 309     8780   7945  10318    766   2255   -336       C  
ATOM   5260  NZ  LYS B 309      30.881  24.069 -16.986  1.00 73.72           N  
ANISOU 5260  NZ  LYS B 309     9026   8258  10727    796   2226   -356       N  
ATOM   5261  C   LYS B 309      26.251  28.372 -20.193  1.00 49.06           C  
ANISOU 5261  C   LYS B 309     6376   5177   7086    671   2325   -277       C  
ATOM   5262  O   LYS B 309      26.386  28.108 -21.386  1.00 54.43           O  
ANISOU 5262  O   LYS B 309     7113   5853   7714    664   2393   -298       O  
ATOM   5263  N   ALA B 310      25.120  28.850 -19.689  1.00 46.03           N  
ANISOU 5263  N   ALA B 310     6039   4803   6647    665   2259   -252       N  
ATOM   5264  CA  ALA B 310      24.005  29.162 -20.566  1.00 43.43           C  
ANISOU 5264  CA  ALA B 310     5833   4480   6190    647   2268   -246       C  
ATOM   5265  CB  ALA B 310      22.730  29.390 -19.759  1.00 41.80           C  
ANISOU 5265  CB  ALA B 310     5666   4282   5935    650   2173   -223       C  
ATOM   5266  C   ALA B 310      24.336  30.390 -21.410  1.00 47.63           C  
ANISOU 5266  C   ALA B 310     6394   5016   6685    608   2347   -230       C  
ATOM   5267  O   ALA B 310      23.969  30.462 -22.582  1.00 46.00           O  
ANISOU 5267  O   ALA B 310     6277   4811   6389    590   2392   -236       O  
ATOM   5268  N   ARG B 311      25.030  31.353 -20.808  1.00 46.94           N  
ANISOU 5268  N   ARG B 311     6231   4933   6670    593   2359   -207       N  
ATOM   5269  CA  ARG B 311      25.426  32.572 -21.512  1.00 45.42           C  
ANISOU 5269  CA  ARG B 311     6057   4747   6455    554   2429   -190       C  
ATOM   5270  CB  ARG B 311      25.871  33.653 -20.525  1.00 44.80           C  
ANISOU 5270  CB  ARG B 311     5897   4676   6451    540   2410   -158       C  
ATOM   5271  CG  ARG B 311      24.737  34.289 -19.709  1.00 48.14           C  
ANISOU 5271  CG  ARG B 311     6347   5109   6836    534   2333   -127       C  
ATOM   5272  CD  ARG B 311      23.889  35.217 -20.552  1.00 50.90           C  
ANISOU 5272  CD  ARG B 311     6803   5467   7071    500   2355   -107       C  
ATOM   5273  NE  ARG B 311      23.752  36.536 -19.942  1.00 63.20           N  
ANISOU 5273  NE  ARG B 311     8336   7035   8641    475   2336    -70       N  
ATOM   5274  CZ  ARG B 311      22.676  36.949 -19.277  1.00 66.96           C  
ANISOU 5274  CZ  ARG B 311     8845   7521   9078    473   2267    -47       C  
ATOM   5275  NH1 ARG B 311      21.633  36.145 -19.130  1.00 65.50           N  
ANISOU 5275  NH1 ARG B 311     8720   7333   8834    496   2206    -58       N  
ATOM   5276  NH2 ARG B 311      22.643  38.169 -18.758  1.00 63.09           N  
ANISOU 5276  NH2 ARG B 311     8325   7041   8604    447   2255    -14       N  
ATOM   5277  C   ARG B 311      26.548  32.283 -22.513  1.00 54.82           C  
ANISOU 5277  C   ARG B 311     7230   5928   7669    549   2521   -216       C  
ATOM   5278  O   ARG B 311      26.710  33.000 -23.501  1.00 57.20           O  
ANISOU 5278  O   ARG B 311     7579   6234   7920    518   2586   -210       O  
ATOM   5279  N   ALA B 312      27.315  31.232 -22.243  1.00 57.71           N  
ANISOU 5279  N   ALA B 312     7530   6285   8114    579   2523   -244       N  
ATOM   5280  CA  ALA B 312      28.391  30.806 -23.133  1.00 61.57           C  
ANISOU 5280  CA  ALA B 312     7997   6764   8631    578   2606   -273       C  
ATOM   5281  CB  ALA B 312      29.309  29.823 -22.428  1.00 59.66           C  
ANISOU 5281  CB  ALA B 312     7655   6513   8501    611   2591   -295       C  
ATOM   5282  C   ALA B 312      27.817  30.187 -24.399  1.00 62.47           C  
ANISOU 5282  C   ALA B 312     8214   6876   8644    576   2641   -297       C  
ATOM   5283  O   ALA B 312      28.136  30.607 -25.509  1.00 67.74           O  
ANISOU 5283  O   ALA B 312     8924   7546   9269    551   2715   -302       O  
ATOM   5284  N   ALA B 313      26.970  29.182 -24.223  1.00 61.41           N  
ANISOU 5284  N   ALA B 313     8121   6740   8474    602   2584   -310       N  
ATOM   5285  CA  ALA B 313      26.271  28.584 -25.345  1.00 56.90           C  
ANISOU 5285  CA  ALA B 313     7651   6168   7801    599   2603   -330       C  
ATOM   5286  CB  ALA B 313      25.451  27.393 -24.876  1.00 58.60           C  
ANISOU 5286  CB  ALA B 313     7887   6380   7998    633   2527   -345       C  
ATOM   5287  C   ALA B 313      25.379  29.610 -26.061  1.00 61.03           C  
ANISOU 5287  C   ALA B 313     8273   6702   8212    562   2611   -303       C  
ATOM   5288  O   ALA B 313      25.317  29.633 -27.284  1.00 58.39           O  
ANISOU 5288  O   ALA B 313     8008   6370   7809    542   2665   -314       O  
ATOM   5289  N   ARG B 314      24.708  30.461 -25.290  1.00 64.26           N  
ANISOU 5289  N   ARG B 314     8689   7120   8607    552   2556   -269       N  
ATOM   5290  CA  ARG B 314      23.755  31.416 -25.832  1.00 68.58           C  
ANISOU 5290  CA  ARG B 314     9331   7678   9049    518   2548   -241       C  
ATOM   5291  CB  ARG B 314      22.316  30.887 -25.760  1.00 67.72           C  
ANISOU 5291  CB  ARG B 314     9307   7573   8850    528   2471   -237       C  
ATOM   5292  CG  ARG B 314      22.021  29.764 -26.698  1.00 62.39           C  
ANISOU 5292  CG  ARG B 314     8693   6894   8118    538   2484   -268       C  
ATOM   5293  CD  ARG B 314      22.147  30.192 -28.143  1.00 59.70           C  
ANISOU 5293  CD  ARG B 314     8420   6556   7708    504   2556   -271       C  
ATOM   5294  NE  ARG B 314      21.197  31.227 -28.540  1.00 56.63           N  
ANISOU 5294  NE  ARG B 314     8115   6179   7224    469   2533   -238       N  
ATOM   5295  CZ  ARG B 314      19.965  30.985 -28.978  1.00 49.29           C  
ANISOU 5295  CZ  ARG B 314     7280   5254   6193    462   2482   -231       C  
ATOM   5296  NH1 ARG B 314      19.515  29.739 -29.058  1.00 44.60           N  
ANISOU 5296  NH1 ARG B 314     6710   4657   5578    487   2449   -255       N  
ATOM   5297  NH2 ARG B 314      19.181  31.992 -29.330  1.00 47.87           N  
ANISOU 5297  NH2 ARG B 314     7169   5084   5935    428   2459   -200       N  
ATOM   5298  C   ARG B 314      23.852  32.751 -25.088  1.00 75.50           C  
ANISOU 5298  C   ARG B 314    10167   8562   9958    497   2535   -204       C  
ATOM   5299  O   ARG B 314      23.282  32.911 -24.011  1.00 71.87           O  
ANISOU 5299  O   ARG B 314     9687   8107   9515    508   2463   -185       O  
ATOM   5300  N   PRO B 315      24.545  33.728 -25.688  1.00 70.48           N  
ANISOU 5300  N   PRO B 315     9523   7930   9327    465   2602   -193       N  
ATOM   5301  CA  PRO B 315      24.629  35.091 -25.157  1.00 66.43           C  
ANISOU 5301  CA  PRO B 315     8981   7426   8835    439   2595   -156       C  
ATOM   5302  CB  PRO B 315      25.460  35.808 -26.218  1.00 63.72           C  
ANISOU 5302  CB  PRO B 315     8644   7083   8483    406   2682   -157       C  
ATOM   5303  CG  PRO B 315      26.359  34.733 -26.757  1.00 65.83           C  
ANISOU 5303  CG  PRO B 315     8880   7340   8794    427   2736   -197       C  
ATOM   5304  CD  PRO B 315      25.611  33.443 -26.665  1.00 66.12           C  
ANISOU 5304  CD  PRO B 315     8954   7371   8798    459   2689   -220       C  
ATOM   5305  C   PRO B 315      23.275  35.774 -24.946  1.00 57.32           C  
ANISOU 5305  C   PRO B 315     7904   6281   7592    422   2531   -124       C  
ATOM   5306  O   PRO B 315      23.172  36.613 -24.054  1.00 52.61           O  
ANISOU 5306  O   PRO B 315     7269   5692   7029    414   2497    -96       O  
ATOM   5307  N   ASP B 316      22.270  35.436 -25.749  1.00 51.34           N  
ANISOU 5307  N   ASP B 316     7254   5526   6727    416   2513   -128       N  
ATOM   5308  CA  ASP B 316      20.990  36.138 -25.683  1.00 49.72           C  
ANISOU 5308  CA  ASP B 316     7130   5331   6431    396   2453    -97       C  
ATOM   5309  CB  ASP B 316      20.386  36.298 -27.092  1.00 51.64           C  
ANISOU 5309  CB  ASP B 316     7483   5577   6560    367   2474    -97       C  
ATOM   5310  CG  ASP B 316      19.982  34.964 -27.745  1.00 54.31           C  
ANISOU 5310  CG  ASP B 316     7874   5909   6851    388   2467   -128       C  
ATOM   5311  OD1 ASP B 316      20.451  33.869 -27.350  1.00 49.62           O  
ANISOU 5311  OD1 ASP B 316     7227   5307   6318    423   2470   -157       O  
ATOM   5312  OD2 ASP B 316      19.194  35.032 -28.710  1.00 49.84           O  
ANISOU 5312  OD2 ASP B 316     7402   5348   6186    367   2457   -124       O  
ATOM   5313  C   ASP B 316      20.011  35.420 -24.741  1.00 45.09           C  
ANISOU 5313  C   ASP B 316     6555   4744   5832    426   2363    -98       C  
ATOM   5314  O   ASP B 316      18.816  35.725 -24.711  1.00 44.04           O  
ANISOU 5314  O   ASP B 316     6498   4619   5615    415   2303    -78       O  
ATOM   5315  N   ALA B 317      20.539  34.492 -23.945  1.00 41.18           N  
ANISOU 5315  N   ALA B 317     5981   4242   5424    464   2349   -121       N  
ATOM   5316  CA  ALA B 317      19.706  33.693 -23.045  1.00 45.40           C  
ANISOU 5316  CA  ALA B 317     6520   4776   5955    496   2262   -125       C  
ATOM   5317  CB  ALA B 317      20.419  32.402 -22.648  1.00 40.29           C  
ANISOU 5317  CB  ALA B 317     5799   4117   5392    535   2262   -160       C  
ATOM   5318  C   ALA B 317      19.318  34.471 -21.800  1.00 41.52           C  
ANISOU 5318  C   ALA B 317     5989   4292   5496    495   2200    -96       C  
ATOM   5319  O   ALA B 317      20.079  35.311 -21.319  1.00 38.42           O  
ANISOU 5319  O   ALA B 317     5521   3902   5176    484   2227    -80       O  
ATOM   5320  N   ILE B 318      18.124  34.168 -21.292  1.00 37.86           N  
ANISOU 5320  N   ILE B 318     5578   3833   4976    508   2115    -90       N  
ATOM   5321  CA  ILE B 318      17.610  34.720 -20.039  1.00 32.57           C  
ANISOU 5321  CA  ILE B 318     4875   3169   4332    513   2043    -67       C  
ATOM   5322  CB  ILE B 318      16.306  35.497 -20.264  1.00 36.85           C  
ANISOU 5322  CB  ILE B 318     5521   3723   4759    486   1998    -39       C  
ATOM   5323  CG1 ILE B 318      16.516  36.605 -21.299  1.00 33.65           C  
ANISOU 5323  CG1 ILE B 318     5159   3323   4304    441   2064    -19       C  
ATOM   5324  CD1 ILE B 318      15.252  37.305 -21.651  1.00 40.78           C  
ANISOU 5324  CD1 ILE B 318     6166   4237   5092    412   2015      8       C  
ATOM   5325  CG2 ILE B 318      15.795  36.080 -18.957  1.00 32.23           C  
ANISOU 5325  CG2 ILE B 318     4901   3144   4203    492   1925    -18       C  
ATOM   5326  C   ILE B 318      17.374  33.566 -19.062  1.00 29.86           C  
ANISOU 5326  C   ILE B 318     4490   2819   4037    556   1966    -86       C  
ATOM   5327  O   ILE B 318      16.667  32.618 -19.385  1.00 36.67           O  
ANISOU 5327  O   ILE B 318     5416   3680   4838    570   1928   -103       O  
ATOM   5328  N   ILE B 319      17.983  33.637 -17.882  1.00 34.41           N  
ANISOU 5328  N   ILE B 319     4957   3393   4725    573   1938    -82       N  
ATOM   5329  CA  ILE B 319      18.017  32.491 -16.967  1.00 32.47           C  
ANISOU 5329  CA  ILE B 319     4652   3140   4544    611   1868   -101       C  
ATOM   5330  CB  ILE B 319      19.455  31.943 -16.835  1.00 32.90           C  
ANISOU 5330  CB  ILE B 319     4598   3187   4716    626   1916   -120       C  
ATOM   5331  CG1 ILE B 319      20.124  31.837 -18.205  1.00 39.80           C  
ANISOU 5331  CG1 ILE B 319     5505   4056   5560    612   2020   -138       C  
ATOM   5332  CD1 ILE B 319      21.174  32.888 -18.449  1.00 41.91           C  
ANISOU 5332  CD1 ILE B 319     5718   4325   5880    585   2099   -124       C  
ATOM   5333  CG2 ILE B 319      19.461  30.597 -16.134  1.00 35.22           C  
ANISOU 5333  CG2 ILE B 319     4847   3474   5060    663   1846   -142       C  
ATOM   5334  C   ILE B 319      17.503  32.798 -15.561  1.00 28.92           C  
ANISOU 5334  C   ILE B 319     4158   2695   4137    621   1769    -81       C  
ATOM   5335  O   ILE B 319      17.887  33.803 -14.963  1.00 32.15           O  
ANISOU 5335  O   ILE B 319     4504   3110   4602    603   1769    -57       O  
ATOM   5336  N   ALA B 320      16.628  31.932 -15.043  1.00 29.75           N  
ANISOU 5336  N   ALA B 320     4291   2798   4212    643   1676    -89       N  
ATOM   5337  CA  ALA B 320      16.205  31.965 -13.643  1.00 28.43           C  
ANISOU 5337  CA  ALA B 320     4071   2637   4095    652   1564    -73       C  
ATOM   5338  CB  ALA B 320      14.704  32.307 -13.507  1.00 23.81           C  
ANISOU 5338  CB  ALA B 320     3580   2069   3398    631   1467    -52       C  
ATOM   5339  C   ALA B 320      16.496  30.599 -13.040  1.00 30.43           C  
ANISOU 5339  C   ALA B 320     4264   2884   4413    686   1512    -96       C  
ATOM   5340  O   ALA B 320      16.416  29.595 -13.746  1.00 33.43           O  
ANISOU 5340  O   ALA B 320     4689   3261   4752    700   1530   -122       O  
ATOM   5341  N   THR B 321      16.857  30.555 -11.758  1.00 30.87           N  
ANISOU 5341  N   THR B 321     4217   2944   4569    695   1443    -85       N  
ATOM   5342  CA  THR B 321      17.142  29.272 -11.092  1.00 33.42           C  
ANISOU 5342  CA  THR B 321     4478   3268   4954    721   1380   -103       C  
ATOM   5343  CB  THR B 321      18.670  28.982 -10.940  1.00 33.48           C  
ANISOU 5343  CB  THR B 321     4370   3271   5080    729   1435   -113       C  
ATOM   5344  OG1 THR B 321      19.161  29.562  -9.722  1.00 34.29           O  
ANISOU 5344  OG1 THR B 321     4366   3383   5280    719   1383    -89       O  
ATOM   5345  CG2 THR B 321      19.479  29.494 -12.132  1.00 35.42           C  
ANISOU 5345  CG2 THR B 321     4632   3509   5317    715   1566   -121       C  
ATOM   5346  C   THR B 321      16.515  29.230  -9.700  1.00 31.64           C  
ANISOU 5346  C   THR B 321     4211   3053   4757    724   1250    -84       C  
ATOM   5347  O   THR B 321      15.850  30.171  -9.280  1.00 26.42           O  
ANISOU 5347  O   THR B 321     3573   2398   4069    706   1208    -57       O  
ATOM   5348  N   GLY B 322      16.729  28.136  -8.976  1.00 30.01           N  
ANISOU 5348  N   GLY B 322     3946   2851   4606    743   1182    -96       N  
ATOM   5349  CA  GLY B 322      16.231  28.044  -7.615  1.00 29.43           C  
ANISOU 5349  CA  GLY B 322     3824   2793   4564    741   1055    -78       C  
ATOM   5350  C   GLY B 322      17.256  28.496  -6.587  1.00 30.70           C  
ANISOU 5350  C   GLY B 322     3854   2965   4847    730   1037    -60       C  
ATOM   5351  O   GLY B 322      17.011  28.418  -5.381  1.00 34.01           O  
ANISOU 5351  O   GLY B 322     4218   3401   5302    723    931    -44       O  
ATOM   5352  N   ARG B 323      18.400  28.975  -7.068  1.00 33.66           N  
ANISOU 5352  N   ARG B 323     4179   3331   5279    724   1138    -62       N  
ATOM   5353  CA  ARG B 323      19.534  29.303  -6.210  1.00 33.91           C  
ANISOU 5353  CA  ARG B 323     4084   3373   5426    712   1131    -47       C  
ATOM   5354  CB  ARG B 323      20.835  28.877  -6.886  1.00 36.33           C  
ANISOU 5354  CB  ARG B 323     4348   3667   5788    721   1230    -69       C  
ATOM   5355  CG  ARG B 323      20.865  27.423  -7.286  1.00 52.05           C  
ANISOU 5355  CG  ARG B 323     6364   5648   7764    752   1229   -101       C  
ATOM   5356  CD  ARG B 323      21.751  26.645  -6.348  1.00 58.35           C  
ANISOU 5356  CD  ARG B 323     7058   6453   8659    759   1178   -104       C  
ATOM   5357  NE  ARG B 323      23.147  27.028  -6.516  1.00 59.78           N  
ANISOU 5357  NE  ARG B 323     7162   6630   8923    749   1257   -103       N  
ATOM   5358  CZ  ARG B 323      24.158  26.446  -5.883  1.00 66.98           C  
ANISOU 5358  CZ  ARG B 323     7981   7544   9922    753   1237   -106       C  
ATOM   5359  NH1 ARG B 323      23.927  25.452  -5.034  1.00 67.91           N  
ANISOU 5359  NH1 ARG B 323     8075   7671  10058    767   1142   -110       N  
ATOM   5360  NH2 ARG B 323      25.400  26.858  -6.101  1.00 69.32           N  
ANISOU 5360  NH2 ARG B 323     8215   7835  10287    742   1310   -105       N  
ATOM   5361  C   ARG B 323      19.617  30.784  -5.869  1.00 30.76           C  
ANISOU 5361  C   ARG B 323     3654   2982   5050    681   1142    -16       C  
ATOM   5362  O   ARG B 323      19.501  31.635  -6.744  1.00 31.37           O  
ANISOU 5362  O   ARG B 323     3788   3049   5081    671   1224    -11       O  
ATOM   5363  N   SER B 324      19.845  31.088  -4.597  1.00 36.71           N  
ANISOU 5363  N   SER B 324     4318   3756   5874    664   1059      7       N  
ATOM   5364  CA  SER B 324      20.022  32.475  -4.185  1.00 34.62           C  
ANISOU 5364  CA  SER B 324     4009   3501   5642    633   1064     37       C  
ATOM   5365  CB  SER B 324      19.968  32.601  -2.661  1.00 43.82           C  
ANISOU 5365  CB  SER B 324     5092   4696   6863    612    942     60       C  
ATOM   5366  OG  SER B 324      20.899  31.745  -2.026  1.00 46.96           O  
ANISOU 5366  OG  SER B 324     5406   5103   7334    616    913     50       O  
ATOM   5367  C   SER B 324      21.335  33.015  -4.736  1.00 38.16           C  
ANISOU 5367  C   SER B 324     4403   3943   6151    623   1175     36       C  
ATOM   5368  O   SER B 324      21.537  34.228  -4.783  1.00 40.04           O  
ANISOU 5368  O   SER B 324     4625   4187   6403    598   1213     57       O  
ATOM   5369  N   ASP B 325      22.200  32.085  -5.155  1.00 41.44           N  
ANISOU 5369  N   ASP B 325     4796   4349   6599    641   1223     11       N  
ATOM   5370  CA  ASP B 325      23.493  32.339  -5.811  1.00 47.18           C  
ANISOU 5370  CA  ASP B 325     5481   5068   7377    635   1330      3       C  
ATOM   5371  CB  ASP B 325      24.161  31.011  -6.191  1.00 58.16           C  
ANISOU 5371  CB  ASP B 325     6861   6447   8793    662   1357    -28       C  
ATOM   5372  CG  ASP B 325      24.394  30.108  -5.009  1.00 73.70           C  
ANISOU 5372  CG  ASP B 325     8756   8426  10820    669   1255    -28       C  
ATOM   5373  OD1 ASP B 325      25.575  29.903  -4.649  1.00 80.99           O  
ANISOU 5373  OD1 ASP B 325     9596   9351  11827    664   1268    -29       O  
ATOM   5374  OD2 ASP B 325      23.399  29.600  -4.443  1.00 79.17           O  
ANISOU 5374  OD2 ASP B 325     9480   9128  11475    679   1162    -26       O  
ATOM   5375  C   ASP B 325      23.416  33.164  -7.086  1.00 47.34           C  
ANISOU 5375  C   ASP B 325     5574   5076   7338    626   1443      1       C  
ATOM   5376  O   ASP B 325      24.320  33.938  -7.395  1.00 46.25           O  
ANISOU 5376  O   ASP B 325     5396   4939   7239    606   1515     10       O  
ATOM   5377  N   TYR B 326      22.366  32.935  -7.864  1.00 32.77           N  
ANISOU 5377  N   TYR B 326     3840   3220   5391    640   1457    -11       N  
ATOM   5378  CA  TYR B 326      22.262  33.508  -9.195  1.00 28.06           C  
ANISOU 5378  CA  TYR B 326     3328   2613   4720    631   1565    -17       C  
ATOM   5379  CB  TYR B 326      22.032  32.410 -10.227  1.00 27.18           C  
ANISOU 5379  CB  TYR B 326     3298   2488   4542    655   1607    -51       C  
ATOM   5380  CG  TYR B 326      23.099  31.334 -10.194  1.00 41.63           C  
ANISOU 5380  CG  TYR B 326     5060   4312   6446    674   1622    -75       C  
ATOM   5381  CD1 TYR B 326      24.429  31.643 -10.435  1.00 51.86           C  
ANISOU 5381  CD1 TYR B 326     6286   5605   7814    661   1696    -76       C  
ATOM   5382  CE1 TYR B 326      25.411  30.661 -10.407  1.00 55.15           C  
ANISOU 5382  CE1 TYR B 326     6642   6015   8298    679   1709    -98       C  
ATOM   5383  CZ  TYR B 326      25.058  29.355 -10.135  1.00 62.57           C  
ANISOU 5383  CZ  TYR B 326     7590   6949   9233    708   1649   -119       C  
ATOM   5384  OH  TYR B 326      26.028  28.376 -10.107  1.00 68.62           O  
ANISOU 5384  OH  TYR B 326     8299   7708  10066    726   1663   -141       O  
ATOM   5385  CE2 TYR B 326      23.742  29.024  -9.892  1.00 54.77           C  
ANISOU 5385  CE2 TYR B 326     6671   5965   8173    720   1575   -117       C  
ATOM   5386  CD2 TYR B 326      22.772  30.013  -9.924  1.00 43.15           C  
ANISOU 5386  CD2 TYR B 326     5260   4499   6634    702   1561    -96       C  
ATOM   5387  C   TYR B 326      21.135  34.511  -9.245  1.00 32.34           C  
ANISOU 5387  C   TYR B 326     3944   3160   5182    613   1543      6       C  
ATOM   5388  O   TYR B 326      20.245  34.469  -8.397  1.00 32.43           O  
ANISOU 5388  O   TYR B 326     3966   3186   5171    607   1429     21       O  
ATOM   5389  N   PRO B 327      21.175  35.420 -10.232  1.00 35.37           N  
ANISOU 5389  N   PRO B 327     4386   3548   5506    585   1624     14       N  
ATOM   5390  CA  PRO B 327      20.035  36.322 -10.424  1.00 33.43           C  
ANISOU 5390  CA  PRO B 327     4230   3320   5152    549   1577     40       C  
ATOM   5391  CB  PRO B 327      20.418  37.123 -11.670  1.00 35.24           C  
ANISOU 5391  CB  PRO B 327     4510   3547   5335    525   1695     42       C  
ATOM   5392  CG  PRO B 327      21.923  37.050 -11.724  1.00 34.52           C  
ANISOU 5392  CG  PRO B 327     4317   3443   5355    537   1787     29       C  
ATOM   5393  CD  PRO B 327      22.272  35.693 -11.181  1.00 32.63           C  
ANISOU 5393  CD  PRO B 327     4021   3191   5186    581   1755      2       C  
ATOM   5394  C   PRO B 327      18.736  35.547 -10.656  1.00 27.45           C  
ANISOU 5394  C   PRO B 327     3578   2560   4290    564   1514     28       C  
ATOM   5395  O   PRO B 327      18.769  34.349 -10.993  1.00 27.78           O  
ANISOU 5395  O   PRO B 327     3640   2584   4329    601   1533     -3       O  
ATOM   5396  N   ASN B 328      17.614  36.235 -10.466  1.00 24.35           N  
ANISOU 5396  N   ASN B 328     3250   2186   3816    535   1439     53       N  
ATOM   5397  CA  ASN B 328      16.310  35.700 -10.814  1.00 24.43           C  
ANISOU 5397  CA  ASN B 328     3373   2197   3714    542   1385     46       C  
ATOM   5398  CB  ASN B 328      16.232  35.471 -12.320  1.00 23.97           C  
ANISOU 5398  CB  ASN B 328     3414   2124   3569    547   1487     26       C  
ATOM   5399  CG  ASN B 328      16.434  36.759 -13.108  1.00 31.59           C  
ANISOU 5399  CG  ASN B 328     4412   3097   4495    508   1563     47       C  
ATOM   5400  OD1 ASN B 328      16.045  37.843 -12.658  1.00 25.99           O  
ANISOU 5400  OD1 ASN B 328     3698   2404   3772    473   1513     80       O  
ATOM   5401  ND2 ASN B 328      17.049  36.647 -14.278  1.00 30.70           N  
ANISOU 5401  ND2 ASN B 328     4331   2970   4364    512   1683     28       N  
ATOM   5402  C   ASN B 328      15.973  34.421 -10.066  1.00 23.33           C  
ANISOU 5402  C   ASN B 328     3213   2051   3601    579   1303     27       C  
ATOM   5403  O   ASN B 328      15.588  33.421 -10.671  1.00 24.71           O  
ANISOU 5403  O   ASN B 328     3453   2211   3723    607   1318      0       O  
ATOM   5404  N   GLN B 329      16.115  34.447  -8.747  1.00 23.01           N  
ANISOU 5404  N   GLN B 329     3080   2022   3641    579   1216     41       N  
ATOM   5405  CA  GLN B 329      15.783  33.254  -7.969  1.00 26.43           C  
ANISOU 5405  CA  GLN B 329     3490   2450   4101    611   1132     25       C  
ATOM   5406  CB  GLN B 329      16.346  33.315  -6.550  1.00 26.26           C  
ANISOU 5406  CB  GLN B 329     3342   2440   4197    610   1061     40       C  
ATOM   5407  CG  GLN B 329      16.171  31.974  -5.833  1.00 25.57           C  
ANISOU 5407  CG  GLN B 329     3225   2344   4148    647    988     21       C  
ATOM   5408  CD  GLN B 329      16.364  32.037  -4.333  1.00 25.49           C  
ANISOU 5408  CD  GLN B 329     3108   2349   4228    641    889     40       C  
ATOM   5409  OE1 GLN B 329      16.266  33.093  -3.726  1.00 26.18           O  
ANISOU 5409  OE1 GLN B 329     3162   2458   4327    606    848     68       O  
ATOM   5410  NE2 GLN B 329      16.650  30.886  -3.726  1.00 27.56           N  
ANISOU 5410  NE2 GLN B 329     3319   2615   4539    662    837     24       N  
ATOM   5411  C   GLN B 329      14.277  33.049  -7.898  1.00 26.04           C  
ANISOU 5411  C   GLN B 329     3541   2412   3943    606   1039     30       C  
ATOM   5412  O   GLN B 329      13.543  33.894  -7.389  1.00 21.56           O  
ANISOU 5412  O   GLN B 329     2988   1865   3337    574    966     57       O  
ATOM   5413  N   VAL B 330      13.825  31.913  -8.413  1.00 21.36           N  
ANISOU 5413  N   VAL B 330     3013   1803   3298    638   1042      2       N  
ATOM   5414  CA  VAL B 330      12.422  31.542  -8.279  1.00 22.84           C  
ANISOU 5414  CA  VAL B 330     3289   2000   3388    638    949      3       C  
ATOM   5415  CB  VAL B 330      11.994  30.602  -9.400  1.00 27.26           C  
ANISOU 5415  CB  VAL B 330     3952   2542   3865    664   1000    -27       C  
ATOM   5416  CG1 VAL B 330      10.539  30.186  -9.240  1.00 23.89           C  
ANISOU 5416  CG1 VAL B 330     3615   2124   3338    665    901    -26       C  
ATOM   5417  CG2 VAL B 330      12.246  31.284 -10.757  1.00 28.57           C  
ANISOU 5417  CG2 VAL B 330     4183   2702   3972    647   1117    -28       C  
ATOM   5418  C   VAL B 330      12.259  30.894  -6.909  1.00 20.62           C  
ANISOU 5418  C   VAL B 330     2937   1727   3173    652    836      5       C  
ATOM   5419  O   VAL B 330      12.452  29.686  -6.743  1.00 28.87           O  
ANISOU 5419  O   VAL B 330     3961   2755   4252    689    825    -18       O  
ATOM   5420  N   ASN B 331      11.944  31.725  -5.927  1.00 18.94           N  
ANISOU 5420  N   ASN B 331     2682   1538   2978    622    753     34       N  
ATOM   5421  CA  ASN B 331      11.898  31.337  -4.518  1.00 19.55           C  
ANISOU 5421  CA  ASN B 331     2675   1626   3126    627    645     42       C  
ATOM   5422  CB  ASN B 331      12.752  32.317  -3.690  1.00 25.46           C  
ANISOU 5422  CB  ASN B 331     3311   2389   3974    601    642     67       C  
ATOM   5423  CG  ASN B 331      12.940  31.888  -2.233  1.00 28.39           C  
ANISOU 5423  CG  ASN B 331     3581   2771   4436    607    543     73       C  
ATOM   5424  OD1 ASN B 331      12.088  31.231  -1.636  1.00 21.03           O  
ANISOU 5424  OD1 ASN B 331     2671   1848   3470    613    444     70       O  
ATOM   5425  ND2 ASN B 331      14.065  32.293  -1.649  1.00 27.71           N  
ANISOU 5425  ND2 ASN B 331     3379   2686   4461    600    567     84       N  
ATOM   5426  C   ASN B 331      10.446  31.337  -4.040  1.00 15.00           C  
ANISOU 5426  C   ASN B 331     2168   1069   2463    613    529     52       C  
ATOM   5427  O   ASN B 331       9.754  32.362  -4.129  1.00 15.53           O  
ANISOU 5427  O   ASN B 331     2282   1153   2464    578    505     73       O  
ATOM   5428  N   ASN B 332       9.980  30.186  -3.554  1.00 16.07           N  
ANISOU 5428  N   ASN B 332     1945   1713   2448   -113   -150     69       N  
ATOM   5429  CA  ASN B 332       8.582  30.062  -3.132  1.00 16.42           C  
ANISOU 5429  CA  ASN B 332     1975   1758   2504   -101   -186     73       C  
ATOM   5430  CB  ASN B 332       8.288  28.645  -2.625  1.00 19.98           C  
ANISOU 5430  CB  ASN B 332     2397   2227   2968   -100   -208     62       C  
ATOM   5431  CG  ASN B 332       8.013  27.677  -3.757  1.00 26.93           C  
ANISOU 5431  CG  ASN B 332     3301   3107   3825    -92   -230     62       C  
ATOM   5432  OD1 ASN B 332       8.456  27.898  -4.881  1.00 27.00           O  
ANISOU 5432  OD1 ASN B 332     3348   3105   3805    -89   -219     66       O  
ATOM   5433  ND2 ASN B 332       7.267  26.615  -3.475  1.00 23.51           N  
ANISOU 5433  ND2 ASN B 332     2849   2684   3402    -88   -262     58       N  
ATOM   5434  C   ASN B 332       8.193  31.056  -2.061  1.00 14.91           C  
ANISOU 5434  C   ASN B 332     1768   1562   2335   -103   -180     78       C  
ATOM   5435  O   ASN B 332       7.015  31.369  -1.899  1.00 16.85           O  
ANISOU 5435  O   ASN B 332     2010   1802   2588    -88   -202     88       O  
ATOM   5436  N   VAL B 333       9.186  31.539  -1.317  1.00 15.97           N  
ANISOU 5436  N   VAL B 333     1893   1697   2480   -120   -152     72       N  
ATOM   5437  CA  VAL B 333       8.892  32.474  -0.245  1.00 18.00           C  
ANISOU 5437  CA  VAL B 333     2141   1944   2753   -123   -146     76       C  
ATOM   5438  CB  VAL B 333      10.141  32.758   0.611  1.00 16.75           C  
ANISOU 5438  CB  VAL B 333     1972   1787   2606   -147   -120     67       C  
ATOM   5439  CG1 VAL B 333      11.030  33.812  -0.031  1.00 14.65           C  
ANISOU 5439  CG1 VAL B 333     1733   1506   2325   -159    -93     75       C  
ATOM   5440  CG2 VAL B 333       9.724  33.165   2.026  1.00 23.23           C  
ANISOU 5440  CG2 VAL B 333     2777   2602   3447   -149   -122     65       C  
ATOM   5441  C   VAL B 333       8.298  33.784  -0.769  1.00 17.66           C  
ANISOU 5441  C   VAL B 333     2131   1882   2698   -111   -142     91       C  
ATOM   5442  O   VAL B 333       7.747  34.561   0.000  1.00 17.54           O  
ANISOU 5442  O   VAL B 333     2114   1856   2694   -106   -140     97       O  
ATOM   5443  N   LEU B 334       8.364  34.014  -2.082  1.00 15.01           N  
ANISOU 5443  N   LEU B 334     1826   1538   2337   -105   -141     99       N  
ATOM   5444  CA  LEU B 334       7.728  35.196  -2.681  1.00 15.48           C  
ANISOU 5444  CA  LEU B 334     1918   1580   2384    -92   -141    114       C  
ATOM   5445  CB  LEU B 334       8.296  35.422  -4.079  1.00 13.72           C  
ANISOU 5445  CB  LEU B 334     1733   1348   2131    -92   -130    119       C  
ATOM   5446  CG  LEU B 334       9.748  35.906  -4.101  1.00 17.90           C  
ANISOU 5446  CG  LEU B 334     2272   1873   2656   -114    -92    115       C  
ATOM   5447  CD1 LEU B 334      10.327  35.784  -5.514  1.00 20.01           C  
ANISOU 5447  CD1 LEU B 334     2573   2135   2894   -112    -79    119       C  
ATOM   5448  CD2 LEU B 334       9.851  37.346  -3.594  1.00 16.25           C  
ANISOU 5448  CD2 LEU B 334     2077   1647   2451   -121    -73    122       C  
ATOM   5449  C   LEU B 334       6.198  35.065  -2.758  1.00 15.54           C  
ANISOU 5449  C   LEU B 334     1919   1586   2398    -68   -175    126       C  
ATOM   5450  O   LEU B 334       5.489  36.056  -2.958  1.00 18.24           O  
ANISOU 5450  O   LEU B 334     2280   1913   2737    -54   -177    141       O  
ATOM   5451  N   GLY B 335       5.703  33.832  -2.618  1.00 15.18           N  
ANISOU 5451  N   GLY B 335     1847   1557   2364    -64   -201    121       N  
ATOM   5452  CA  GLY B 335       4.297  33.538  -2.823  1.00 18.08           C  
ANISOU 5452  CA  GLY B 335     2206   1925   2741    -44   -237    134       C  
ATOM   5453  C   GLY B 335       3.506  33.278  -1.557  1.00 16.01           C  
ANISOU 5453  C   GLY B 335     1902   1669   2510    -37   -246    137       C  
ATOM   5454  O   GLY B 335       2.738  34.142  -1.133  1.00 16.94           O  
ANISOU 5454  O   GLY B 335     2019   1776   2641    -23   -243    151       O  
ATOM   5455  N   PHE B 336       3.710  32.113  -0.936  1.00 17.92           N  
ANISOU 5455  N   PHE B 336     2114   1927   2766    -46   -253    123       N  
ATOM   5456  CA  PHE B 336       2.826  31.672   0.150  1.00 19.76           C  
ANISOU 5456  CA  PHE B 336     2309   2167   3030    -37   -265    126       C  
ATOM   5457  CB  PHE B 336       3.257  30.262   0.665  1.00 18.72           C  
ANISOU 5457  CB  PHE B 336     2150   2055   2908    -50   -272    108       C  
ATOM   5458  CG  PHE B 336       4.611  30.197   1.332  1.00 17.61           C  
ANISOU 5458  CG  PHE B 336     2007   1918   2764    -70   -243     88       C  
ATOM   5459  CD1 PHE B 336       4.761  30.446   2.695  1.00 20.69           C  
ANISOU 5459  CD1 PHE B 336     2381   2308   3174    -75   -225     83       C  
ATOM   5460  CE1 PHE B 336       6.019  30.374   3.303  1.00 17.78           C  
ANISOU 5460  CE1 PHE B 336     2010   1942   2803    -96   -203     66       C  
ATOM   5461  CZ  PHE B 336       7.121  30.003   2.560  1.00 15.52           C  
ANISOU 5461  CZ  PHE B 336     1734   1663   2501   -110   -196     57       C  
ATOM   5462  CE2 PHE B 336       6.973  29.720   1.218  1.00 16.35           C  
ANISOU 5462  CE2 PHE B 336     1856   1769   2586   -103   -208     62       C  
ATOM   5463  CD2 PHE B 336       5.732  29.812   0.613  1.00 15.79           C  
ANISOU 5463  CD2 PHE B 336     1792   1693   2513    -84   -233     77       C  
ATOM   5464  C   PHE B 336       2.657  32.645   1.342  1.00 18.02           C  
ANISOU 5464  C   PHE B 336     2083   1936   2827    -32   -239    131       C  
ATOM   5465  O   PHE B 336       1.556  32.726   1.899  1.00 13.48           O  
ANISOU 5465  O   PHE B 336     1489   1359   2274    -15   -248    146       O  
ATOM   5466  N   PRO B 337       3.703  33.406   1.731  1.00 16.51           N  
ANISOU 5466  N   PRO B 337     1911   1736   2626    -47   -208    121       N  
ATOM   5467  CA  PRO B 337       3.421  34.265   2.886  1.00 13.52           C  
ANISOU 5467  CA  PRO B 337     1533   1344   2261    -41   -188    127       C  
ATOM   5468  CB  PRO B 337       4.786  34.932   3.179  1.00 14.74           C  
ANISOU 5468  CB  PRO B 337     1709   1490   2401    -64   -160    114       C  
ATOM   5469  CG  PRO B 337       5.808  33.959   2.600  1.00 16.46           C  
ANISOU 5469  CG  PRO B 337     1919   1725   2610    -84   -164     98       C  
ATOM   5470  CD  PRO B 337       5.120  33.484   1.328  1.00 17.29           C  
ANISOU 5470  CD  PRO B 337     2028   1836   2704    -69   -189    107       C  
ATOM   5471  C   PRO B 337       2.338  35.309   2.582  1.00 17.26           C  
ANISOU 5471  C   PRO B 337     2021   1801   2736    -16   -189    151       C  
ATOM   5472  O   PRO B 337       1.393  35.481   3.364  1.00 17.91           O  
ANISOU 5472  O   PRO B 337     2088   1877   2839      3   -187    163       O  
ATOM   5473  N   SER B 338       2.449  35.972   1.438  1.00 17.23           N  
ANISOU 5473  N   SER B 338     2047   1788   2710    -13   -190    159       N  
ATOM   5474  CA  SER B 338       1.469  37.004   1.074  1.00 17.49           C  
ANISOU 5474  CA  SER B 338     2097   1805   2744     11   -191    182       C  
ATOM   5475  CB  SER B 338       1.956  37.824  -0.100  1.00 17.95           C  
ANISOU 5475  CB  SER B 338     2196   1852   2772      7   -186    186       C  
ATOM   5476  OG  SER B 338       3.081  38.600   0.257  1.00 17.39           O  
ANISOU 5476  OG  SER B 338     2151   1770   2688    -12   -154    174       O  
ATOM   5477  C   SER B 338       0.123  36.394   0.726  1.00 15.13           C  
ANISOU 5477  C   SER B 338     1771   1514   2463     33   -225    201       C  
ATOM   5478  O   SER B 338      -0.920  36.986   0.978  1.00 14.43           O  
ANISOU 5478  O   SER B 338     1676   1415   2390     57   -225    223       O  
ATOM   5479  N   ILE B 339       0.150  35.224   0.101  1.00 14.46           N  
ANISOU 5479  N   ILE B 339     1672   1447   2377     25   -254    194       N  
ATOM   5480  CA  ILE B 339      -1.086  34.590  -0.294  1.00 13.67           C  
ANISOU 5480  CA  ILE B 339     1546   1353   2295     41   -292    213       C  
ATOM   5481  CB  ILE B 339      -0.840  33.346  -1.152  1.00 15.91           C  
ANISOU 5481  CB  ILE B 339     1828   1652   2567     27   -324    202       C  
ATOM   5482  CG1 ILE B 339      -0.297  33.788  -2.515  1.00 24.26           C  
ANISOU 5482  CG1 ILE B 339     2930   2700   3587     22   -328    201       C  
ATOM   5483  CD1 ILE B 339       0.280  32.648  -3.339  1.00 21.12           C  
ANISOU 5483  CD1 ILE B 339     2544   2313   3169      7   -348    186       C  
ATOM   5484  CG2 ILE B 339      -2.134  32.532  -1.336  1.00 16.40           C  
ANISOU 5484  CG2 ILE B 339     1857   1722   2653     39   -368    221       C  
ATOM   5485  C   ILE B 339      -1.882  34.256   0.961  1.00 17.75           C  
ANISOU 5485  C   ILE B 339     2021   1874   2848     53   -289    221       C  
ATOM   5486  O   ILE B 339      -3.073  34.545   1.010  1.00 15.82           O  
ANISOU 5486  O   ILE B 339     1760   1625   2626     76   -300    247       O  
ATOM   5487  N   PHE B 340      -1.238  33.683   1.982  1.00 13.80           N  
ANISOU 5487  N   PHE B 340     1507   1383   2355     38   -271    200       N  
ATOM   5488  CA  PHE B 340      -1.980  33.413   3.206  1.00 13.31           C  
ANISOU 5488  CA  PHE B 340     1410   1322   2326     51   -264    208       C  
ATOM   5489  CB  PHE B 340      -1.233  32.430   4.113  1.00 11.78           C  
ANISOU 5489  CB  PHE B 340     1198   1140   2136     32   -256    183       C  
ATOM   5490  CG  PHE B 340      -1.457  30.993   3.743  1.00 12.64           C  
ANISOU 5490  CG  PHE B 340     1280   1270   2254     24   -290    178       C  
ATOM   5491  CD2 PHE B 340      -2.522  30.290   4.282  1.00 12.97           C  
ANISOU 5491  CD2 PHE B 340     1282   1318   2327     36   -306    192       C  
ATOM   5492  CE2 PHE B 340      -2.759  28.945   3.946  1.00 17.67           C  
ANISOU 5492  CE2 PHE B 340     1854   1931   2931     27   -340    188       C  
ATOM   5493  CZ  PHE B 340      -1.892  28.302   3.069  1.00 14.08           C  
ANISOU 5493  CZ  PHE B 340     1418   1484   2448      7   -356    168       C  
ATOM   5494  CE1 PHE B 340      -0.821  29.007   2.512  1.00 13.36           C  
ANISOU 5494  CE1 PHE B 340     1365   1387   2325     -3   -337    155       C  
ATOM   5495  CD1 PHE B 340      -0.619  30.354   2.849  1.00 15.91           C  
ANISOU 5495  CD1 PHE B 340     1708   1694   2643      4   -305    160       C  
ATOM   5496  C   PHE B 340      -2.318  34.693   3.965  1.00 14.62           C  
ANISOU 5496  C   PHE B 340     1591   1467   2498     70   -230    222       C  
ATOM   5497  O   PHE B 340      -3.370  34.762   4.586  1.00 14.41           O  
ANISOU 5497  O   PHE B 340     1541   1435   2499     93   -227    243       O  
ATOM   5498  N   ARG B 341      -1.450  35.703   3.918  1.00 14.35           N  
ANISOU 5498  N   ARG B 341     1597   1418   2439     61   -204    213       N  
ATOM   5499  CA  ARG B 341      -1.747  36.969   4.593  1.00 15.48           C  
ANISOU 5499  CA  ARG B 341     1762   1537   2583     79   -172    226       C  
ATOM   5500  CB  ARG B 341      -0.597  37.976   4.418  1.00 15.71           C  
ANISOU 5500  CB  ARG B 341     1838   1551   2580     61   -148    212       C  
ATOM   5501  CG  ARG B 341      -0.806  39.331   5.119  1.00 16.78           C  
ANISOU 5501  CG  ARG B 341     2005   1657   2712     77   -115    223       C  
ATOM   5502  CD  ARG B 341      -0.435  39.220   6.576  1.00 22.84           C  
ANISOU 5502  CD  ARG B 341     2775   2418   3487     69    -92    210       C  
ATOM   5503  NE  ARG B 341      -1.558  38.756   7.354  1.00 25.57           N  
ANISOU 5503  NE  ARG B 341     3088   2764   3862     95    -91    225       N  
ATOM   5504  CZ  ARG B 341      -1.480  38.180   8.550  1.00 19.00           C  
ANISOU 5504  CZ  ARG B 341     2244   1933   3043     91    -80    215       C  
ATOM   5505  NH1 ARG B 341      -0.315  37.950   9.138  1.00 17.32           N  
ANISOU 5505  NH1 ARG B 341     2044   1720   2815     62    -74    188       N  
ATOM   5506  NH2 ARG B 341      -2.604  37.817   9.160  1.00 17.66           N  
ANISOU 5506  NH2 ARG B 341     2045   1763   2901    119    -76    233       N  
ATOM   5507  C   ARG B 341      -3.043  37.560   4.053  1.00 16.38           C  
ANISOU 5507  C   ARG B 341     1871   1643   2711    111   -182    259       C  
ATOM   5508  O   ARG B 341      -3.906  37.985   4.837  1.00 17.60           O  
ANISOU 5508  O   ARG B 341     2015   1784   2887    136   -164    279       O  
ATOM   5509  N   GLY B 342      -3.186  37.577   2.722  1.00 15.23           N  
ANISOU 5509  N   GLY B 342     1733   1501   2552    111   -210    267       N  
ATOM   5510  CA  GLY B 342      -4.367  38.130   2.067  1.00 16.34           C  
ANISOU 5510  CA  GLY B 342     1869   1634   2705    139   -225    300       C  
ATOM   5511  C   GLY B 342      -5.604  37.299   2.356  1.00 20.87           C  
ANISOU 5511  C   GLY B 342     2391   2219   3319    156   -249    322       C  
ATOM   5512  O   GLY B 342      -6.697  37.821   2.595  1.00 17.97           O  
ANISOU 5512  O   GLY B 342     2008   1842   2976    186   -244    353       O  
ATOM   5513  N   ALA B 343      -5.427  35.988   2.351  1.00 13.89           N  
ANISOU 5513  N   ALA B 343     1480   1356   2442    138   -274    308       N  
ATOM   5514  CA  ALA B 343      -6.554  35.086   2.597  1.00 15.72           C  
ANISOU 5514  CA  ALA B 343     1660   1599   2713    150   -301    328       C  
ATOM   5515  CB  ALA B 343      -6.167  33.670   2.215  1.00 15.77           C  
ANISOU 5515  CB  ALA B 343     1650   1627   2716    124   -335    308       C  
ATOM   5516  C   ALA B 343      -7.010  35.150   4.063  1.00 19.27           C  
ANISOU 5516  C   ALA B 343     2086   2044   3193    167   -266    336       C  
ATOM   5517  O   ALA B 343      -8.204  35.103   4.350  1.00 21.11           O  
ANISOU 5517  O   ALA B 343     2283   2276   3463    191   -271    367       O  
ATOM   5518  N   LEU B 344      -6.062  35.243   4.989  1.00 18.44           N  
ANISOU 5518  N   LEU B 344     2000   1934   3072    154   -232    309       N  
ATOM   5519  CA  LEU B 344      -6.406  35.306   6.404  1.00 18.15           C  
ANISOU 5519  CA  LEU B 344     1951   1889   3059    169   -198    314       C  
ATOM   5520  CB  LEU B 344      -5.160  35.149   7.268  1.00 16.88           C  
ANISOU 5520  CB  LEU B 344     1813   1725   2875    145   -173    278       C  
ATOM   5521  CG  LEU B 344      -4.536  33.764   7.357  1.00 18.20           C  
ANISOU 5521  CG  LEU B 344     1958   1916   3042    117   -195    252       C  
ATOM   5522  CD1 LEU B 344      -3.171  33.910   7.987  1.00 19.13           C  
ANISOU 5522  CD1 LEU B 344     2108   2029   3134     92   -172    220       C  
ATOM   5523  CD2 LEU B 344      -5.422  32.796   8.173  1.00 18.44           C  
ANISOU 5523  CD2 LEU B 344     1942   1954   3109    129   -199    264       C  
ATOM   5524  C   LEU B 344      -7.095  36.614   6.764  1.00 18.65           C  
ANISOU 5524  C   LEU B 344     2031   1927   3129    202   -165    341       C  
ATOM   5525  O   LEU B 344      -8.054  36.623   7.529  1.00 21.47           O  
ANISOU 5525  O   LEU B 344     2362   2276   3518    229   -148    365       O  
ATOM   5526  N   ASP B 345      -6.587  37.721   6.235  1.00 17.69           N  
ANISOU 5526  N   ASP B 345     1954   1789   2977    201   -153    338       N  
ATOM   5527  CA  ASP B 345      -7.110  39.003   6.681  1.00 17.97           C  
ANISOU 5527  CA  ASP B 345     2015   1799   3015    232   -116    360       C  
ATOM   5528  CB  ASP B 345      -6.151  40.119   6.293  1.00 20.64           C  
ANISOU 5528  CB  ASP B 345     2411   2119   3311    220   -100    345       C  
ATOM   5529  CG  ASP B 345      -4.836  40.035   7.066  1.00 26.52           C  
ANISOU 5529  CG  ASP B 345     3184   2859   4031    189    -80    309       C  
ATOM   5530  OD1 ASP B 345      -4.799  39.302   8.086  1.00 29.66           O  
ANISOU 5530  OD1 ASP B 345     3563   3262   4444    185    -71    299       O  
ATOM   5531  OD2 ASP B 345      -3.867  40.706   6.671  1.00 33.27           O  
ANISOU 5531  OD2 ASP B 345     4081   3706   4854    169    -73    292       O  
ATOM   5532  C   ASP B 345      -8.503  39.271   6.146  1.00 24.89           C  
ANISOU 5532  C   ASP B 345     2862   2674   3923    266   -130    403       C  
ATOM   5533  O   ASP B 345      -9.247  40.059   6.732  1.00 27.57           O  
ANISOU 5533  O   ASP B 345     3205   2992   4277    300    -98    429       O  
ATOM   5534  N   THR B 346      -8.867  38.608   5.055  1.00 21.49           N  
ANISOU 5534  N   THR B 346     2402   2262   3500    259   -178    412       N  
ATOM   5535  CA  THR B 346     -10.225  38.677   4.540  1.00 22.37           C  
ANISOU 5535  CA  THR B 346     2477   2375   3647    288   -201    454       C  
ATOM   5536  CB  THR B 346     -10.267  38.645   2.993  1.00 25.49           C  
ANISOU 5536  CB  THR B 346     2878   2778   4027    277   -250    460       C  
ATOM   5537  OG1 THR B 346      -9.530  37.512   2.513  1.00 22.87           O  
ANISOU 5537  OG1 THR B 346     2544   2467   3679    241   -284    430       O  
ATOM   5538  CG2 THR B 346      -9.678  39.939   2.399  1.00 19.48           C  
ANISOU 5538  CG2 THR B 346     2176   1999   3227    279   -232    454       C  
ATOM   5539  C   THR B 346     -11.068  37.524   5.065  1.00 20.74           C  
ANISOU 5539  C   THR B 346     2210   2185   3487    293   -217    470       C  
ATOM   5540  O   THR B 346     -12.204  37.349   4.627  1.00 20.36           O  
ANISOU 5540  O   THR B 346     2120   2141   3473    311   -244    507       O  
ATOM   5541  N   ARG B 347     -10.492  36.748   5.981  1.00 18.93           N  
ANISOU 5541  N   ARG B 347     1975   1963   3256    275   -203    443       N  
ATOM   5542  CA  ARG B 347     -11.144  35.566   6.549  1.00 23.55           C  
ANISOU 5542  CA  ARG B 347     2505   2564   3881    275   -216    453       C  
ATOM   5543  CB  ARG B 347     -12.161  35.983   7.620  1.00 27.11           C  
ANISOU 5543  CB  ARG B 347     2932   2999   4370    314   -175    487       C  
ATOM   5544  CG  ARG B 347     -11.501  36.752   8.771  1.00 29.85           C  
ANISOU 5544  CG  ARG B 347     3325   3322   4692    322   -116    468       C  
ATOM   5545  CD  ARG B 347     -12.491  37.165   9.854  1.00 35.70           C  
ANISOU 5545  CD  ARG B 347     4051   4045   5468    364    -69    502       C  
ATOM   5546  NE  ARG B 347     -11.830  37.932  10.911  1.00 35.71           N  
ANISOU 5546  NE  ARG B 347     4108   4020   5441    370    -16    483       N  
ATOM   5547  CZ  ARG B 347     -12.459  38.432  11.971  1.00 42.63           C  
ANISOU 5547  CZ  ARG B 347     4991   4873   6335    406     34    505       C  
ATOM   5548  NH1 ARG B 347     -13.762  38.235  12.114  1.00 37.40           N  
ANISOU 5548  NH1 ARG B 347     4289   4229   5692    421     41    532       N  
ATOM   5549  NH2 ARG B 347     -11.785  39.111  12.895  1.00 39.95           N  
ANISOU 5549  NH2 ARG B 347     4709   4506   5963    407     78    485       N  
ATOM   5550  C   ARG B 347     -11.795  34.731   5.453  1.00 30.21           C  
ANISOU 5550  C   ARG B 347     3308   3426   4743    266   -277    471       C  
ATOM   5551  O   ARG B 347     -12.949  34.318   5.564  1.00 25.96           O  
ANISOU 5551  O   ARG B 347     2721   2894   4248    282   -291    504       O  
ATOM   5552  N   SER B 348     -11.029  34.479   4.394  1.00 21.52           N  
ANISOU 5552  N   SER B 348     2234   2335   3608    238   -311    447       N  
ATOM   5553  CA  SER B 348     -11.524  33.752   3.229  1.00 20.35           C  
ANISOU 5553  CA  SER B 348     2064   2201   3468    226   -373    460       C  
ATOM   5554  CB  SER B 348     -10.568  33.902   2.044  1.00 26.67           C  
ANISOU 5554  CB  SER B 348     2913   3002   4219    202   -396    434       C  
ATOM   5555  OG  SER B 348     -10.655  35.216   1.500  1.00 28.69           O  
ANISOU 5555  OG  SER B 348     3202   3240   4459    221   -383    449       O  
ATOM   5556  C   SER B 348     -11.732  32.275   3.517  1.00 22.49           C  
ANISOU 5556  C   SER B 348     2293   2491   3762    208   -401    454       C  
ATOM   5557  O   SER B 348     -11.098  31.698   4.405  1.00 24.43           O  
ANISOU 5557  O   SER B 348     2539   2742   4003    195   -377    427       O  
ATOM   5558  N   THR B 349     -12.625  31.671   2.746  1.00 24.06           N  
ANISOU 5558  N   THR B 349     2464   2701   3979    202   -450    476       N  
ATOM   5559  CA  THR B 349     -12.916  30.259   2.898  1.00 26.94           C  
ANISOU 5559  CA  THR B 349     2805   3085   4345    174   -471    464       C  
ATOM   5560  CB  THR B 349     -14.406  29.957   2.630  1.00 26.96           C  
ANISOU 5560  CB  THR B 349     2780   3098   4367    173   -489    494       C  
ATOM   5561  OG1 THR B 349     -14.763  30.401   1.312  1.00 26.51           O  
ANISOU 5561  OG1 THR B 349     2736   3036   4301    174   -532    512       O  
ATOM   5562  CG2 THR B 349     -15.304  30.667   3.653  1.00 32.01           C  
ANISOU 5562  CG2 THR B 349     3396   3732   5033    201   -438    519       C  
ATOM   5563  C   THR B 349     -12.064  29.422   1.954  1.00 23.92           C  
ANISOU 5563  C   THR B 349     2444   2710   3936    146   -519    438       C  
ATOM   5564  O   THR B 349     -12.036  28.193   2.062  1.00 24.79           O  
ANISOU 5564  O   THR B 349     2544   2834   4040    121   -535    421       O  
ATOM   5565  N   GLN B 350     -11.392  30.085   1.013  1.00 22.49           N  
ANISOU 5565  N   GLN B 350     2301   2517   3726    146   -534    432       N  
ATOM   5566  CA  GLN B 350     -10.525  29.405   0.049  1.00 20.78           C  
ANISOU 5566  CA  GLN B 350     2122   2307   3467    117   -565    402       C  
ATOM   5567  CB  GLN B 350     -11.283  28.988  -1.219  1.00 33.55           C  
ANISOU 5567  CB  GLN B 350     3737   3923   5087    110   -633    426       C  
ATOM   5568  CG  GLN B 350     -12.772  28.777  -1.116  1.00 38.47           C  
ANISOU 5568  CG  GLN B 350     4321   4553   5742    115   -647    458       C  
ATOM   5569  CD  GLN B 350     -13.401  28.561  -2.483  1.00 40.90           C  
ANISOU 5569  CD  GLN B 350     4645   4857   6036    103   -706    474       C  
ATOM   5570  OE1 GLN B 350     -12.715  28.590  -3.505  1.00 39.65           O  
ANISOU 5570  OE1 GLN B 350     4528   4690   5848     96   -742    465       O  
ATOM   5571  NE2 GLN B 350     -14.707  28.350  -2.506  1.00 39.24           N  
ANISOU 5571  NE2 GLN B 350     4407   4653   5848    101   -716    499       N  
ATOM   5572  C   GLN B 350      -9.362  30.271  -0.413  1.00 23.51           C  
ANISOU 5572  C   GLN B 350     2526   2643   3763    113   -536    376       C  
ATOM   5573  O   GLN B 350      -9.405  31.502  -0.316  1.00 21.35           O  
ANISOU 5573  O   GLN B 350     2269   2357   3486    132   -506    387       O  
ATOM   5574  N   ILE B 351      -8.348  29.612  -0.953  1.00 18.34           N  
ANISOU 5574  N   ILE B 351     1904   1995   3070     88   -546    344       N  
ATOM   5575  CA  ILE B 351      -7.375  30.245  -1.849  1.00 19.52           C  
ANISOU 5575  CA  ILE B 351     2110   2135   3171     80   -537    325       C  
ATOM   5576  CB  ILE B 351      -5.903  29.943  -1.485  1.00 18.60           C  
ANISOU 5576  CB  ILE B 351     2019   2024   3024     61   -501    284       C  
ATOM   5577  CG1 ILE B 351      -5.486  30.658  -0.188  1.00 16.60           C  
ANISOU 5577  CG1 ILE B 351     1757   1768   2782     69   -445    276       C  
ATOM   5578  CD1 ILE B 351      -4.254  30.020   0.491  1.00 17.92           C  
ANISOU 5578  CD1 ILE B 351     1929   1945   2935     48   -419    240       C  
ATOM   5579  CG2 ILE B 351      -4.974  30.361  -2.641  1.00 20.42           C  
ANISOU 5579  CG2 ILE B 351     2306   2246   3206     51   -499    269       C  
ATOM   5580  C   ILE B 351      -7.691  29.678  -3.234  1.00 20.06           C  
ANISOU 5580  C   ILE B 351     2199   2201   3221     70   -595    333       C  
ATOM   5581  O   ILE B 351      -7.434  28.482  -3.506  1.00 22.57           O  
ANISOU 5581  O   ILE B 351     2519   2528   3530     51   -622    318       O  
ATOM   5582  N   ASN B 352      -8.286  30.500  -4.086  1.00 19.75           N  
ANISOU 5582  N   ASN B 352     2177   2149   3178     84   -616    358       N  
ATOM   5583  CA  ASN B 352      -8.748  30.027  -5.383  1.00 21.07           C  
ANISOU 5583  CA  ASN B 352     2366   2311   3331     76   -677    371       C  
ATOM   5584  CB  ASN B 352     -10.191  30.509  -5.652  1.00 21.00           C  
ANISOU 5584  CB  ASN B 352     2326   2294   3358     95   -714    416       C  
ATOM   5585  CG  ASN B 352     -10.351  32.015  -5.486  1.00 25.60           C  
ANISOU 5585  CG  ASN B 352     2916   2865   3944    122   -677    433       C  
ATOM   5586  OD1 ASN B 352      -9.384  32.762  -5.591  1.00 21.61           O  
ANISOU 5586  OD1 ASN B 352     2454   2353   3404    122   -637    411       O  
ATOM   5587  ND2 ASN B 352     -11.580  32.466  -5.229  1.00 23.40           N  
ANISOU 5587  ND2 ASN B 352     2595   2584   3710    144   -690    473       N  
ATOM   5588  C   ASN B 352      -7.816  30.459  -6.504  1.00 22.09           C  
ANISOU 5588  C   ASN B 352     2563   2428   3404     69   -673    352       C  
ATOM   5589  O   ASN B 352      -6.780  31.106  -6.255  1.00 19.49           O  
ANISOU 5589  O   ASN B 352     2259   2095   3050     68   -621    330       O  
ATOM   5590  N   GLU B 353      -8.156  30.096  -7.742  1.00 22.86           N  
ANISOU 5590  N   GLU B 353     2691   2515   3480     62   -726    362       N  
ATOM   5591  CA  GLU B 353      -7.265  30.404  -8.860  1.00 25.20           C  
ANISOU 5591  CA  GLU B 353     3057   2798   3721     55   -722    345       C  
ATOM   5592  CB  GLU B 353      -7.731  29.713 -10.148  1.00 30.56           C  
ANISOU 5592  CB  GLU B 353     3770   3465   4376     45   -789    355       C  
ATOM   5593  CG  GLU B 353      -7.687  28.186 -10.069  1.00 36.06           C  
ANISOU 5593  CG  GLU B 353     4457   4171   5073     24   -820    341       C  
ATOM   5594  CD  GLU B 353      -6.329  27.653  -9.623  1.00 43.91           C  
ANISOU 5594  CD  GLU B 353     5466   5175   6043     12   -770    302       C  
ATOM   5595  OE1 GLU B 353      -5.307  27.987 -10.268  1.00 48.07           O  
ANISOU 5595  OE1 GLU B 353     6047   5692   6525     10   -742    283       O  
ATOM   5596  OE2 GLU B 353      -6.283  26.907  -8.616  1.00 39.95           O  
ANISOU 5596  OE2 GLU B 353     4920   4690   5569      5   -758    292       O  
ATOM   5597  C   GLU B 353      -7.141  31.914  -9.091  1.00 25.58           C  
ANISOU 5597  C   GLU B 353     3130   2832   3757     74   -690    354       C  
ATOM   5598  O   GLU B 353      -6.073  32.393  -9.478  1.00 26.16           O  
ANISOU 5598  O   GLU B 353     3251   2897   3791     69   -654    333       O  
ATOM   5599  N   GLU B 354      -8.225  32.651  -8.860  1.00 22.78           N  
ANISOU 5599  N   GLU B 354     2744   2473   3436     94   -702    388       N  
ATOM   5600  CA  GLU B 354      -8.221  34.109  -8.944  1.00 25.49           C  
ANISOU 5600  CA  GLU B 354     3107   2803   3774    114   -670    400       C  
ATOM   5601  CB  GLU B 354      -9.601  34.659  -8.590  1.00 30.16           C  
ANISOU 5601  CB  GLU B 354     3653   3394   4414    139   -689    441       C  
ATOM   5602  CG  GLU B 354     -10.674  34.349  -9.642  1.00 29.47           C  
ANISOU 5602  CG  GLU B 354     3566   3299   4334    141   -763    473       C  
ATOM   5603  CD  GLU B 354     -11.487  33.079  -9.368  1.00 40.67           C  
ANISOU 5603  CD  GLU B 354     4933   4730   5790    129   -812    486       C  
ATOM   5604  OE1 GLU B 354     -11.036  32.174  -8.627  1.00 31.11           O  
ANISOU 5604  OE1 GLU B 354     3700   3535   4587    114   -795    463       O  
ATOM   5605  OE2 GLU B 354     -12.599  32.974  -9.929  1.00 41.78           O  
ANISOU 5605  OE2 GLU B 354     5055   4865   5953    134   -870    522       O  
ATOM   5606  C   GLU B 354      -7.167  34.737  -8.031  1.00 20.55           C  
ANISOU 5606  C   GLU B 354     2488   2181   3141    114   -599    374       C  
ATOM   5607  O   GLU B 354      -6.462  35.662  -8.420  1.00 19.24           O  
ANISOU 5607  O   GLU B 354     2366   2002   2943    117   -568    365       O  
ATOM   5608  N   MET B 355      -7.093  34.231  -6.809  1.00 21.41           N  
ANISOU 5608  N   MET B 355     2552   2305   3279    110   -576    365       N  
ATOM   5609  CA  MET B 355      -6.127  34.701  -5.839  1.00 18.44           C  
ANISOU 5609  CA  MET B 355     2177   1931   2898    107   -514    341       C  
ATOM   5610  CB  MET B 355      -6.461  34.115  -4.462  1.00 15.41           C  
ANISOU 5610  CB  MET B 355     1738   1562   2556    108   -501    340       C  
ATOM   5611  CG  MET B 355      -7.744  34.763  -3.870  1.00 19.33           C  
ANISOU 5611  CG  MET B 355     2196   2053   3095    137   -500    377       C  
ATOM   5612  SD  MET B 355      -8.583  33.775  -2.628  1.00 19.62           S  
ANISOU 5612  SD  MET B 355     2163   2106   3187    141   -506    388       S  
ATOM   5613  CE  MET B 355      -7.523  34.033  -1.210  1.00 17.81           C  
ANISOU 5613  CE  MET B 355     1937   1879   2952    135   -439    357       C  
ATOM   5614  C   MET B 355      -4.697  34.355  -6.266  1.00 15.22           C  
ANISOU 5614  C   MET B 355     1812   1525   2448     84   -495    306       C  
ATOM   5615  O   MET B 355      -3.787  35.178  -6.109  1.00 17.43           O  
ANISOU 5615  O   MET B 355     2119   1798   2708     81   -450    292       O  
ATOM   5616  N   LYS B 356      -4.493  33.145  -6.800  1.00 18.21           N  
ANISOU 5616  N   LYS B 356     2195   1911   2813     67   -526    294       N  
ATOM   5617  CA  LYS B 356      -3.167  32.753  -7.249  1.00 14.54           C  
ANISOU 5617  CA  LYS B 356     1768   1447   2309     48   -506    264       C  
ATOM   5618  CB  LYS B 356      -3.153  31.280  -7.707  1.00 15.46           C  
ANISOU 5618  CB  LYS B 356     1885   1572   2417     34   -544    254       C  
ATOM   5619  CG  LYS B 356      -3.452  30.281  -6.602  1.00 19.35           C  
ANISOU 5619  CG  LYS B 356     2323   2084   2945     27   -549    248       C  
ATOM   5620  CD  LYS B 356      -3.317  28.858  -7.176  1.00 24.00           C  
ANISOU 5620  CD  LYS B 356     2923   2678   3518     11   -585    236       C  
ATOM   5621  CE  LYS B 356      -3.940  27.818  -6.288  1.00 36.00           C  
ANISOU 5621  CE  LYS B 356     4390   4213   5075      6   -606    238       C  
ATOM   5622  NZ  LYS B 356      -4.036  26.518  -7.032  1.00 27.22           N  
ANISOU 5622  NZ  LYS B 356     3296   3102   3945     -8   -652    233       N  
ATOM   5623  C   LYS B 356      -2.702  33.670  -8.379  1.00 17.81           C  
ANISOU 5623  C   LYS B 356     2241   1842   2683     52   -496    266       C  
ATOM   5624  O   LYS B 356      -1.547  34.140  -8.390  1.00 16.92           O  
ANISOU 5624  O   LYS B 356     2155   1725   2547     44   -453    248       O  
ATOM   5625  N   LEU B 357      -3.610  33.942  -9.317  1.00 17.88           N  
ANISOU 5625  N   LEU B 357     2268   1838   2686     64   -538    290       N  
ATOM   5626  CA  LEU B 357      -3.308  34.826 -10.444  1.00 20.11           C  
ANISOU 5626  CA  LEU B 357     2610   2100   2930     69   -534    294       C  
ATOM   5627  CB  LEU B 357      -4.471  34.872 -11.443  1.00 23.97           C  
ANISOU 5627  CB  LEU B 357     3114   2577   3416     81   -594    323       C  
ATOM   5628  CG  LEU B 357      -4.355  33.948 -12.660  1.00 49.62           C  
ANISOU 5628  CG  LEU B 357     6409   5818   6629     69   -636    317       C  
ATOM   5629  CD1 LEU B 357      -3.026  34.146 -13.384  1.00 46.50           C  
ANISOU 5629  CD1 LEU B 357     6074   5410   6182     61   -598    294       C  
ATOM   5630  CD2 LEU B 357      -4.528  32.499 -12.256  1.00 57.44           C  
ANISOU 5630  CD2 LEU B 357     7365   6823   7635     55   -664    308       C  
ATOM   5631  C   LEU B 357      -2.995  36.244 -10.012  1.00 19.00           C  
ANISOU 5631  C   LEU B 357     2476   1951   2791     80   -486    298       C  
ATOM   5632  O   LEU B 357      -2.115  36.879 -10.592  1.00 19.20           O  
ANISOU 5632  O   LEU B 357     2549   1964   2782     76   -457    288       O  
ATOM   5633  N   ALA B 358      -3.740  36.738  -9.021  1.00 20.59           N  
ANISOU 5633  N   ALA B 358     2635   2157   3031     94   -479    314       N  
ATOM   5634  CA  ALA B 358      -3.520  38.064  -8.478  1.00 19.79           C  
ANISOU 5634  CA  ALA B 358     2541   2045   2933    105   -434    318       C  
ATOM   5635  CB  ALA B 358      -4.551  38.397  -7.390  1.00 17.92           C  
ANISOU 5635  CB  ALA B 358     2255   1813   2742    124   -431    339       C  
ATOM   5636  C   ALA B 358      -2.098  38.163  -7.933  1.00 19.53           C  
ANISOU 5636  C   ALA B 358     2520   2016   2884     85   -383    288       C  
ATOM   5637  O   ALA B 358      -1.424  39.167  -8.149  1.00 16.67           O  
ANISOU 5637  O   ALA B 358     2195   1640   2501     84   -349    284       O  
ATOM   5638  N   ALA B 359      -1.636  37.116  -7.249  1.00 17.23           N  
ANISOU 5638  N   ALA B 359     2199   1743   2606     69   -378    268       N  
ATOM   5639  CA  ALA B 359      -0.260  37.088  -6.764  1.00 14.92           C  
ANISOU 5639  CA  ALA B 359     1915   1455   2301     49   -335    242       C  
ATOM   5640  CB  ALA B 359      -0.021  35.855  -5.906  1.00 16.75           C  
ANISOU 5640  CB  ALA B 359     2105   1707   2553     36   -338    225       C  
ATOM   5641  C   ALA B 359       0.754  37.124  -7.914  1.00 14.77           C  
ANISOU 5641  C   ALA B 359     1945   1427   2240     37   -324    230       C  
ATOM   5642  O   ALA B 359       1.743  37.850  -7.848  1.00 15.36           O  
ANISOU 5642  O   ALA B 359     2042   1494   2300     27   -284    221       O  
ATOM   5643  N   VAL B 360       0.524  36.308  -8.942  1.00 15.02           N  
ANISOU 5643  N   VAL B 360     1995   1458   2252     37   -360    232       N  
ATOM   5644  CA  VAL B 360       1.393  36.330 -10.123  1.00 15.94           C  
ANISOU 5644  CA  VAL B 360     2165   1563   2326     29   -349    223       C  
ATOM   5645  CB  VAL B 360       0.853  35.447 -11.259  1.00 17.24           C  
ANISOU 5645  CB  VAL B 360     2357   1724   2471     33   -398    229       C  
ATOM   5646  CG1 VAL B 360       1.711  35.630 -12.516  1.00 21.30           C  
ANISOU 5646  CG1 VAL B 360     2935   2220   2937     30   -381    223       C  
ATOM   5647  CG2 VAL B 360       0.830  33.994 -10.830  1.00 16.72           C  
ANISOU 5647  CG2 VAL B 360     2258   1676   2418     23   -418    216       C  
ATOM   5648  C   VAL B 360       1.563  37.745 -10.671  1.00 14.96           C  
ANISOU 5648  C   VAL B 360     2082   1418   2182     38   -326    234       C  
ATOM   5649  O   VAL B 360       2.676  38.218 -10.874  1.00 14.92           O  
ANISOU 5649  O   VAL B 360     2104   1406   2157     27   -285    223       O  
ATOM   5650  N   HIS B 361       0.449  38.416 -10.932  1.00 18.31           N  
ANISOU 5650  N   HIS B 361     2511   1832   2613     57   -352    257       N  
ATOM   5651  CA  HIS B 361       0.520  39.732 -11.542  1.00 15.13           C  
ANISOU 5651  CA  HIS B 361     2152   1407   2188     67   -335    268       C  
ATOM   5652  CB  HIS B 361      -0.874  40.163 -11.970  1.00 17.36           C  
ANISOU 5652  CB  HIS B 361     2437   1681   2480     90   -377    296       C  
ATOM   5653  CG  HIS B 361      -1.345  39.456 -13.204  1.00 20.03           C  
ANISOU 5653  CG  HIS B 361     2804   2012   2794     93   -427    304       C  
ATOM   5654  ND1 HIS B 361      -0.817  39.710 -14.450  1.00 28.95           N  
ANISOU 5654  ND1 HIS B 361     3998   3124   3879     91   -424    301       N  
ATOM   5655  CE1 HIS B 361      -1.413  38.941 -15.346  1.00 32.74           C  
ANISOU 5655  CE1 HIS B 361     4498   3598   4343     94   -476    309       C  
ATOM   5656  NE2 HIS B 361      -2.308  38.196 -14.722  1.00 30.90           N  
ANISOU 5656  NE2 HIS B 361     4213   3381   4147     95   -514    317       N  
ATOM   5657  CD2 HIS B 361      -2.288  38.500 -13.382  1.00 26.57           C  
ANISOU 5657  CD2 HIS B 361     3610   2848   3637     96   -482    314       C  
ATOM   5658  C   HIS B 361       1.165  40.762 -10.620  1.00 17.24           C  
ANISOU 5658  C   HIS B 361     2412   1672   2466     61   -284    263       C  
ATOM   5659  O   HIS B 361       1.885  41.632 -11.085  1.00 16.56           O  
ANISOU 5659  O   HIS B 361     2367   1571   2356     57   -253    261       O  
ATOM   5660  N   ALA B 362       0.939  40.635  -9.311  1.00 15.89           N  
ANISOU 5660  N   ALA B 362     2193   1513   2330     60   -276    260       N  
ATOM   5661  CA  ALA B 362       1.525  41.568  -8.347  1.00 15.28           C  
ANISOU 5661  CA  ALA B 362     2113   1431   2263     53   -231    255       C  
ATOM   5662  CB  ALA B 362       0.894  41.373  -6.966  1.00 19.83           C  
ANISOU 5662  CB  ALA B 362     2640   2019   2878     60   -232    257       C  
ATOM   5663  C   ALA B 362       3.037  41.412  -8.266  1.00 15.45           C  
ANISOU 5663  C   ALA B 362     2145   1456   2270     26   -195    232       C  
ATOM   5664  O   ALA B 362       3.783  42.406  -8.203  1.00 15.70           O  
ANISOU 5664  O   ALA B 362     2202   1474   2289     17   -159    231       O  
ATOM   5665  N   LEU B 363       3.501  40.167  -8.264  1.00 15.19           N  
ANISOU 5665  N   LEU B 363     2093   1441   2239     13   -203    217       N  
ATOM   5666  CA  LEU B 363       4.943  39.929  -8.244  1.00 13.93           C  
ANISOU 5666  CA  LEU B 363     1939   1285   2069    -11   -169    199       C  
ATOM   5667  CB  LEU B 363       5.260  38.432  -8.108  1.00 12.22           C  
ANISOU 5667  CB  LEU B 363     1694   1089   1859    -21   -182    184       C  
ATOM   5668  CG  LEU B 363       5.030  37.851  -6.708  1.00 14.66           C  
ANISOU 5668  CG  LEU B 363     1950   1416   2203    -26   -187    176       C  
ATOM   5669  CD1 LEU B 363       5.129  36.348  -6.763  1.00 16.29           C  
ANISOU 5669  CD1 LEU B 363     2134   1641   2413    -31   -207    164       C  
ATOM   5670  CD2 LEU B 363       6.034  38.414  -5.728  1.00 12.96           C  
ANISOU 5670  CD2 LEU B 363     1724   1200   1999    -45   -149    166       C  
ATOM   5671  C   LEU B 363       5.583  40.470  -9.512  1.00 15.14           C  
ANISOU 5671  C   LEU B 363     2145   1422   2185    -13   -152    203       C  
ATOM   5672  O   LEU B 363       6.671  41.062  -9.477  1.00 15.62           O  
ANISOU 5672  O   LEU B 363     2220   1475   2238    -29   -113    198       O  
ATOM   5673  N   ALA B 364       4.905  40.279 -10.641  1.00 12.92           N  
ANISOU 5673  N   ALA B 364     1894   1132   1882      3   -182    213       N  
ATOM   5674  CA  ALA B 364       5.478  40.730 -11.907  1.00 13.05           C  
ANISOU 5674  CA  ALA B 364     1967   1131   1861      4   -166    216       C  
ATOM   5675  CB  ALA B 364       4.658  40.211 -13.079  1.00 16.62           C  
ANISOU 5675  CB  ALA B 364     2451   1575   2289     20   -208    226       C  
ATOM   5676  C   ALA B 364       5.568  42.243 -11.951  1.00 17.27           C  
ANISOU 5676  C   ALA B 364     2529   1645   2388      7   -140    227       C  
ATOM   5677  O   ALA B 364       6.601  42.815 -12.326  1.00 16.81           O  
ANISOU 5677  O   ALA B 364     2500   1576   2313     -6   -101    225       O  
ATOM   5678  N   LYS B 365       4.481  42.889 -11.562  1.00 14.39           N  
ANISOU 5678  N   LYS B 365     2155   1274   2037     24   -160    241       N  
ATOM   5679  CA  LYS B 365       4.454  44.344 -11.577  1.00 13.69           C  
ANISOU 5679  CA  LYS B 365     2096   1166   1941     29   -137    253       C  
ATOM   5680  CB  LYS B 365       3.076  44.853 -11.177  1.00 16.78           C  
ANISOU 5680  CB  LYS B 365     2473   1552   2351     54   -164    271       C  
ATOM   5681  CG  LYS B 365       2.080  44.902 -12.307  1.00 31.80           C  
ANISOU 5681  CG  LYS B 365     4403   3444   4235     77   -203    289       C  
ATOM   5682  CD  LYS B 365       0.799  45.611 -11.831  1.00 47.77           C  
ANISOU 5682  CD  LYS B 365     6410   5461   6281    102   -221    311       C  
ATOM   5683  CE  LYS B 365       1.096  46.857 -10.983  1.00 52.58           C  
ANISOU 5683  CE  LYS B 365     7025   6057   6897    102   -179    313       C  
ATOM   5684  NZ  LYS B 365       1.687  47.984 -11.760  1.00 58.32           N  
ANISOU 5684  NZ  LYS B 365     7810   6760   7590    100   -152    316       N  
ATOM   5685  C   LYS B 365       5.509  44.920 -10.648  1.00 17.77           C  
ANISOU 5685  C   LYS B 365     2601   1681   2468      7    -93    242       C  
ATOM   5686  O   LYS B 365       6.159  45.901 -10.992  1.00 18.40           O  
ANISOU 5686  O   LYS B 365     2717   1744   2532     -1    -62    245       O  
ATOM   5687  N   LEU B 366       5.685  44.315  -9.475  1.00 13.85           N  
ANISOU 5687  N   LEU B 366     2057   1203   2001     -5    -91    231       N  
ATOM   5688  CA  LEU B 366       6.644  44.867  -8.507  1.00 15.52           C  
ANISOU 5688  CA  LEU B 366     2260   1413   2226    -29    -55    222       C  
ATOM   5689  CB  LEU B 366       6.611  44.081  -7.187  1.00 15.20           C  
ANISOU 5689  CB  LEU B 366     2167   1391   2217    -37    -62    210       C  
ATOM   5690  CG  LEU B 366       7.670  44.434  -6.132  1.00 14.43           C  
ANISOU 5690  CG  LEU B 366     2057   1293   2133    -65    -31    200       C  
ATOM   5691  CD1 LEU B 366       7.581  45.917  -5.730  1.00 13.68           C  
ANISOU 5691  CD1 LEU B 366     1992   1172   2033    -65    -12    209       C  
ATOM   5692  CD2 LEU B 366       7.460  43.536  -4.901  1.00 12.86           C  
ANISOU 5692  CD2 LEU B 366     1809   1113   1964    -69    -44    189       C  
ATOM   5693  C   LEU B 366       8.049  44.856  -9.087  1.00 17.25           C  
ANISOU 5693  C   LEU B 366     2498   1629   2429    -52    -23    214       C  
ATOM   5694  O   LEU B 366       8.821  45.797  -8.886  1.00 14.34           O  
ANISOU 5694  O   LEU B 366     2146   1246   2056    -69      9    216       O  
ATOM   5695  N   ALA B 367       8.385  43.808  -9.840  1.00 16.93           N  
ANISOU 5695  N   ALA B 367     2456   1599   2377    -53    -30    208       N  
ATOM   5696  CA  ALA B 367       9.737  43.742 -10.381  1.00 19.22           C  
ANISOU 5696  CA  ALA B 367     2761   1887   2654    -73      5    204       C  
ATOM   5697  CB  ALA B 367       9.995  42.351 -10.973  1.00 16.29           C  
ANISOU 5697  CB  ALA B 367     2381   1531   2275    -71     -4    195       C  
ATOM   5698  C   ALA B 367      10.019  44.816 -11.421  1.00 18.12           C  
ANISOU 5698  C   ALA B 367     2677   1724   2486    -70     28    216       C  
ATOM   5699  O   ALA B 367      11.176  45.164 -11.662  1.00 19.15           O  
ANISOU 5699  O   ALA B 367     2818   1846   2610    -89     66    216       O  
ATOM   5700  N   ARG B 368       8.974  45.352 -12.036  1.00 18.13           N  
ANISOU 5700  N   ARG B 368     2710   1710   2468    -46      6    227       N  
ATOM   5701  CA  ARG B 368       9.169  46.390 -13.045  1.00 17.77           C  
ANISOU 5701  CA  ARG B 368     2721   1639   2393    -41     26    239       C  
ATOM   5702  CB  ARG B 368       7.952  46.465 -13.944  1.00 18.92           C  
ANISOU 5702  CB  ARG B 368     2898   1773   2516    -11    -11    251       C  
ATOM   5703  CG  ARG B 368       7.697  45.189 -14.732  1.00 22.55           C  
ANISOU 5703  CG  ARG B 368     3362   2243   2961     -2    -39    246       C  
ATOM   5704  CD  ARG B 368       6.673  45.466 -15.820  1.00 34.88           C  
ANISOU 5704  CD  ARG B 368     4969   3787   4495     24    -73    261       C  
ATOM   5705  NE  ARG B 368       6.367  44.298 -16.628  1.00 50.89           N  
ANISOU 5705  NE  ARG B 368     7011   5820   6506     33   -105    258       N  
ATOM   5706  CZ  ARG B 368       5.215  43.646 -16.573  1.00 54.90           C  
ANISOU 5706  CZ  ARG B 368     7500   6336   7023     47   -157    262       C  
ATOM   5707  NH1 ARG B 368       4.270  44.057 -15.735  1.00 55.64           N  
ANISOU 5707  NH1 ARG B 368     7558   6436   7147     56   -179    271       N  
ATOM   5708  NH2 ARG B 368       5.014  42.586 -17.351  1.00 49.72           N  
ANISOU 5708  NH2 ARG B 368     6863   5680   6347     51   -187    259       N  
ATOM   5709  C   ARG B 368       9.453  47.771 -12.450  1.00 20.97           C  
ANISOU 5709  C   ARG B 368     3136   2028   2804    -53     52    245       C  
ATOM   5710  O   ARG B 368       9.880  48.676 -13.161  1.00 22.73           O  
ANISOU 5710  O   ARG B 368     3402   2229   3004    -55     77    254       O  
ATOM   5711  N   GLU B 369       9.219  47.937 -11.149  1.00 18.36           N  
ANISOU 5711  N   GLU B 369     2769   1704   2502    -60     47    241       N  
ATOM   5712  CA  GLU B 369       9.440  49.242 -10.513  1.00 18.92           C  
ANISOU 5712  CA  GLU B 369     2856   1757   2577    -71     69    246       C  
ATOM   5713  CB  GLU B 369       8.664  49.332  -9.203  1.00 16.82           C  
ANISOU 5713  CB  GLU B 369     2560   1496   2336    -64     52    245       C  
ATOM   5714  CG  GLU B 369       7.202  49.099  -9.376  1.00 16.56           C  
ANISOU 5714  CG  GLU B 369     2522   1465   2304    -29     17    253       C  
ATOM   5715  CD  GLU B 369       6.477  50.184 -10.182  1.00 24.95           C  
ANISOU 5715  CD  GLU B 369     3633   2504   3343     -5     14    271       C  
ATOM   5716  OE1 GLU B 369       7.033  51.281 -10.467  1.00 21.33           O  
ANISOU 5716  OE1 GLU B 369     3214   2023   2866    -15     43    276       O  
ATOM   5717  OE2 GLU B 369       5.315  49.925 -10.553  1.00 22.99           O  
ANISOU 5717  OE2 GLU B 369     3381   2258   3094     23    -18    282       O  
ATOM   5718  C   GLU B 369      10.913  49.508 -10.234  1.00 20.93           C  
ANISOU 5718  C   GLU B 369     3106   2008   2837   -107    107    242       C  
ATOM   5719  O   GLU B 369      11.718  48.562 -10.167  1.00 20.27           O  
ANISOU 5719  O   GLU B 369     2994   1943   2766   -123    114    232       O  
ATOM   5720  N   ASP B 370      11.254  50.790 -10.083  1.00 21.69           N  
ANISOU 5720  N   ASP B 370     3233   2081   2927   -119    130    249       N  
ATOM   5721  CA  ASP B 370      12.571  51.183  -9.591  1.00 21.33           C  
ANISOU 5721  CA  ASP B 370     3179   2030   2893   -157    160    248       C  
ATOM   5722  CB  ASP B 370      12.680  52.700  -9.377  1.00 23.47           C  
ANISOU 5722  CB  ASP B 370     3491   2271   3155   -167    179    257       C  
ATOM   5723  CG  ASP B 370      12.400  53.526 -10.642  1.00 26.11           C  
ANISOU 5723  CG  ASP B 370     3882   2584   3456   -149    190    271       C  
ATOM   5724  OD1 ASP B 370      12.459  53.000 -11.778  1.00 22.97           O  
ANISOU 5724  OD1 ASP B 370     3496   2191   3041   -136    192    273       O  
ATOM   5725  OD2 ASP B 370      12.147  54.742 -10.484  1.00 26.11           O  
ANISOU 5725  OD2 ASP B 370     3917   2558   3444   -148    198    279       O  
ATOM   5726  C   ASP B 370      12.818  50.471  -8.266  1.00 23.95           C  
ANISOU 5726  C   ASP B 370     3459   2381   3258   -174    149    235       C  
ATOM   5727  O   ASP B 370      11.911  50.368  -7.437  1.00 23.30           O  
ANISOU 5727  O   ASP B 370     3363   2304   3187   -160    126    231       O  
ATOM   5728  N   VAL B 371      14.037  49.975  -8.072  1.00 21.99           N  
ANISOU 5728  N   VAL B 371     3183   2145   3026   -204    166    231       N  
ATOM   5729  CA  VAL B 371      14.409  49.321  -6.821  1.00 20.59           C  
ANISOU 5729  CA  VAL B 371     2959   1985   2879   -224    156    219       C  
ATOM   5730  CB  VAL B 371      15.452  48.225  -7.066  1.00 19.48           C  
ANISOU 5730  CB  VAL B 371     2781   1866   2753   -241    168    215       C  
ATOM   5731  CG1 VAL B 371      15.795  47.535  -5.751  1.00 20.88           C  
ANISOU 5731  CG1 VAL B 371     2910   2061   2963   -260    154    204       C  
ATOM   5732  CG2 VAL B 371      14.925  47.220  -8.075  1.00 20.08           C  
ANISOU 5732  CG2 VAL B 371     2858   1957   2814   -211    158    212       C  
ATOM   5733  C   VAL B 371      14.966  50.301  -5.789  1.00 22.22           C  
ANISOU 5733  C   VAL B 371     3171   2173   3098   -255    165    222       C  
ATOM   5734  O   VAL B 371      15.925  51.030  -6.069  1.00 24.28           O  
ANISOU 5734  O   VAL B 371     3449   2419   3357   -281    190    231       O  
ATOM   5735  N   PRO B 372      14.361  50.341  -4.596  1.00 20.97           N  
ANISOU 5735  N   PRO B 372     3002   2013   2951   -252    146    214       N  
ATOM   5736  CA  PRO B 372      14.782  51.322  -3.590  1.00 21.33           C  
ANISOU 5736  CA  PRO B 372     3063   2036   3003   -280    151    216       C  
ATOM   5737  CB  PRO B 372      13.733  51.167  -2.486  1.00 27.81           C  
ANISOU 5737  CB  PRO B 372     3879   2858   3831   -260    129    208       C  
ATOM   5738  CG  PRO B 372      12.549  50.480  -3.163  1.00 26.60           C  
ANISOU 5738  CG  PRO B 372     3717   2721   3670   -217    114    208       C  
ATOM   5739  CD  PRO B 372      13.204  49.548  -4.129  1.00 23.90           C  
ANISOU 5739  CD  PRO B 372     3351   2400   3329   -222    118    206       C  
ATOM   5740  C   PRO B 372      16.189  51.032  -3.049  1.00 25.92           C  
ANISOU 5740  C   PRO B 372     3614   2625   3609   -324    159    214       C  
ATOM   5741  O   PRO B 372      16.645  49.880  -3.090  1.00 23.91           O  
ANISOU 5741  O   PRO B 372     3315   2397   3372   -329    155    208       O  
ATOM   5742  N   ASP B 373      16.859  52.075  -2.561  1.00 29.68           N  
ANISOU 5742  N   ASP B 373     4114   3076   4087   -357    168    221       N  
ATOM   5743  CA  ASP B 373      18.180  51.925  -1.956  1.00 31.98           C  
ANISOU 5743  CA  ASP B 373     4376   3371   4404   -402    170    223       C  
ATOM   5744  CB  ASP B 373      18.653  53.260  -1.374  1.00 44.82           C  
ANISOU 5744  CB  ASP B 373     6041   4963   6027   -436    174    231       C  
ATOM   5745  CG  ASP B 373      18.943  54.290  -2.441  1.00 62.08           C  
ANISOU 5745  CG  ASP B 373     8267   7128   8193   -440    201    247       C  
ATOM   5746  OD1 ASP B 373      19.354  53.890  -3.553  1.00 64.69           O  
ANISOU 5746  OD1 ASP B 373     8583   7472   8523   -434    220    254       O  
ATOM   5747  OD2 ASP B 373      18.770  55.498  -2.163  1.00 68.18           O  
ANISOU 5747  OD2 ASP B 373     9088   7868   8950   -449    203    252       O  
ATOM   5748  C   ASP B 373      18.183  50.858  -0.865  1.00 28.64           C  
ANISOU 5748  C   ASP B 373     3908   2969   4004   -407    147    209       C  
ATOM   5749  O   ASP B 373      19.155  50.132  -0.707  1.00 31.91           O  
ANISOU 5749  O   ASP B 373     4279   3401   4443   -431    147    209       O  
ATOM   5750  N   LYS B 374      17.085  50.790  -0.116  1.00 32.08           N  
ANISOU 5750  N   LYS B 374     4354   3402   4434   -382    128    199       N  
ATOM   5751  CA  LYS B 374      16.910  49.837   0.969  1.00 34.63           C  
ANISOU 5751  CA  LYS B 374     4641   3741   4775   -382    106    185       C  
ATOM   5752  CB  LYS B 374      15.485  49.955   1.523  1.00 42.09           C  
ANISOU 5752  CB  LYS B 374     5607   4679   5708   -346     93    179       C  
ATOM   5753  CG  LYS B 374      15.171  49.068   2.712  1.00 54.70           C  
ANISOU 5753  CG  LYS B 374     7174   6288   7322   -342     73    165       C  
ATOM   5754  CD  LYS B 374      13.745  49.302   3.211  1.00 60.57           C  
ANISOU 5754  CD  LYS B 374     7940   7020   8053   -304     66    163       C  
ATOM   5755  CE  LYS B 374      13.403  48.389   4.384  1.00 65.23           C  
ANISOU 5755  CE  LYS B 374     8502   7623   8661   -299     49    151       C  
ATOM   5756  NZ  LYS B 374      12.010  48.602   4.878  1.00 66.14           N  
ANISOU 5756  NZ  LYS B 374     8636   7726   8768   -260     47    153       N  
ATOM   5757  C   LYS B 374      17.192  48.400   0.530  1.00 34.95           C  
ANISOU 5757  C   LYS B 374     4629   3819   4833   -375    103    179       C  
ATOM   5758  O   LYS B 374      17.825  47.639   1.265  1.00 32.44           O  
ANISOU 5758  O   LYS B 374     4273   3516   4539   -395     92    172       O  
ATOM   5759  N   VAL B 375      16.734  48.030  -0.668  1.00 26.97           N  
ANISOU 5759  N   VAL B 375     3618   2820   3808   -346    112    181       N  
ATOM   5760  CA  VAL B 375      16.932  46.669  -1.159  1.00 28.38           C  
ANISOU 5760  CA  VAL B 375     3755   3030   3997   -336    110    175       C  
ATOM   5761  CB  VAL B 375      16.003  46.335  -2.370  1.00 27.47           C  
ANISOU 5761  CB  VAL B 375     3656   2923   3861   -296    110    176       C  
ATOM   5762  CG1 VAL B 375      16.328  44.959  -2.940  1.00 27.39           C  
ANISOU 5762  CG1 VAL B 375     3610   2940   3857   -288    110    171       C  
ATOM   5763  CG2 VAL B 375      14.554  46.384  -1.952  1.00 27.75           C  
ANISOU 5763  CG2 VAL B 375     3703   2955   3888   -264     88    171       C  
ATOM   5764  C   VAL B 375      18.383  46.440  -1.557  1.00 30.58           C  
ANISOU 5764  C   VAL B 375     4010   3316   4292   -367    130    183       C  
ATOM   5765  O   VAL B 375      18.966  45.389  -1.250  1.00 31.10           O  
ANISOU 5765  O   VAL B 375     4032   3404   4379   -376    125    178       O  
ATOM   5766  N   SER B 376      18.971  47.415  -2.246  1.00 31.39           N  
ANISOU 5766  N   SER B 376     4141   3400   4386   -382    153    198       N  
ATOM   5767  CA  SER B 376      20.392  47.345  -2.580  1.00 35.44           C  
ANISOU 5767  CA  SER B 376     4631   3917   4918   -413    176    210       C  
ATOM   5768  CB  SER B 376      20.835  48.584  -3.364  1.00 31.82           C  
ANISOU 5768  CB  SER B 376     4211   3433   4445   -426    203    228       C  
ATOM   5769  OG  SER B 376      20.314  48.537  -4.676  1.00 37.74           O  
ANISOU 5769  OG  SER B 376     4987   4183   5168   -394    219    231       O  
ATOM   5770  C   SER B 376      21.243  47.200  -1.328  1.00 29.93           C  
ANISOU 5770  C   SER B 376     3898   3222   4252   -451    162    209       C  
ATOM   5771  O   SER B 376      22.161  46.393  -1.295  1.00 30.87           O  
ANISOU 5771  O   SER B 376     3973   3361   4397   -467    168    213       O  
ATOM   5772  N   ALA B 377      20.932  47.981  -0.298  1.00 31.63           N  
ANISOU 5772  N   ALA B 377     4137   3417   4466   -466    143    205       N  
ATOM   5773  CA  ALA B 377      21.692  47.907   0.946  1.00 29.67           C  
ANISOU 5773  CA  ALA B 377     3863   3167   4244   -504    124    204       C  
ATOM   5774  CB  ALA B 377      21.246  48.991   1.905  1.00 32.36           C  
ANISOU 5774  CB  ALA B 377     4247   3475   4571   -516    107    201       C  
ATOM   5775  C   ALA B 377      21.560  46.526   1.590  1.00 38.71           C  
ANISOU 5775  C   ALA B 377     4962   4340   5406   -493    104    189       C  
ATOM   5776  O   ALA B 377      22.529  45.987   2.133  1.00 32.71           O  
ANISOU 5776  O   ALA B 377     4162   3592   4676   -522     97    192       O  
ATOM   5777  N   THR B 378      20.368  45.939   1.513  1.00 30.90           N  
ANISOU 5777  N   THR B 378     3977   3362   4401   -453     95    175       N  
ATOM   5778  CA  THR B 378      20.176  44.585   2.030  1.00 32.94           C  
ANISOU 5778  CA  THR B 378     4194   3647   4674   -441     78    161       C  
ATOM   5779  CB  THR B 378      18.694  44.137   1.908  1.00 23.51           C  
ANISOU 5779  CB  THR B 378     3012   2460   3460   -396     67    149       C  
ATOM   5780  OG1 THR B 378      17.869  45.017   2.684  1.00 35.10           O  
ANISOU 5780  OG1 THR B 378     4517   3904   4916   -391     56    146       O  
ATOM   5781  CG2 THR B 378      18.516  42.715   2.405  1.00 32.14           C  
ANISOU 5781  CG2 THR B 378     4062   3580   4568   -385     50    135       C  
ATOM   5782  C   THR B 378      21.087  43.606   1.294  1.00 33.96           C  
ANISOU 5782  C   THR B 378     4280   3801   4820   -444     94    167       C  
ATOM   5783  O   THR B 378      21.655  42.692   1.896  1.00 38.53           O  
ANISOU 5783  O   THR B 378     4817   4399   5423   -456     84    162       O  
ATOM   5784  N   TYR B 379      21.261  43.815  -0.007  1.00 29.96           N  
ANISOU 5784  N   TYR B 379     3788   3295   4301   -433    121    178       N  
ATOM   5785  CA  TYR B 379      22.045  42.884  -0.802  1.00 27.86           C  
ANISOU 5785  CA  TYR B 379     3489   3050   4047   -430    142    185       C  
ATOM   5786  CB  TYR B 379      21.309  42.553  -2.103  1.00 34.44           C  
ANISOU 5786  CB  TYR B 379     4347   3888   4851   -391    156    183       C  
ATOM   5787  CG  TYR B 379      20.135  41.605  -1.875  1.00 37.23           C  
ANISOU 5787  CG  TYR B 379     4695   4257   5193   -359    130    164       C  
ATOM   5788  CD1 TYR B 379      20.326  40.226  -1.850  1.00 35.23           C  
ANISOU 5788  CD1 TYR B 379     4405   4028   4952   -349    126    156       C  
ATOM   5789  CE1 TYR B 379      19.267  39.344  -1.628  1.00 33.69           C  
ANISOU 5789  CE1 TYR B 379     4205   3847   4749   -322    101    140       C  
ATOM   5790  CZ  TYR B 379      17.997  39.841  -1.431  1.00 26.40           C  
ANISOU 5790  CZ  TYR B 379     3309   2912   3809   -304     81    134       C  
ATOM   5791  OH  TYR B 379      16.961  38.959  -1.203  1.00 21.87           O  
ANISOU 5791  OH  TYR B 379     2726   2352   3231   -279     56    121       O  
ATOM   5792  CE2 TYR B 379      17.773  41.212  -1.434  1.00 24.49           C  
ANISOU 5792  CE2 TYR B 379     3104   2647   3556   -310     86    143       C  
ATOM   5793  CD2 TYR B 379      18.844  42.089  -1.655  1.00 31.05           C  
ANISOU 5793  CD2 TYR B 379     3943   3462   4391   -338    110    156       C  
ATOM   5794  C   TYR B 379      23.456  43.417  -1.083  1.00 34.49           C  
ANISOU 5794  C   TYR B 379     4315   3883   4908   -465    168    206       C  
ATOM   5795  O   TYR B 379      23.974  43.295  -2.194  1.00 36.76           O  
ANISOU 5795  O   TYR B 379     4601   4173   5191   -458    200    219       O  
ATOM   5796  N   GLY B 380      24.066  44.003  -0.059  1.00 38.52           N  
ANISOU 5796  N   GLY B 380     4815   4381   5439   -503    153    211       N  
ATOM   5797  CA  GLY B 380      25.473  44.370  -0.112  1.00 48.79           C  
ANISOU 5797  CA  GLY B 380     6091   5678   6770   -542    170    234       C  
ATOM   5798  C   GLY B 380      25.826  45.496  -1.061  1.00 46.09           C  
ANISOU 5798  C   GLY B 380     5782   5315   6417   -552    201    253       C  
ATOM   5799  O   GLY B 380      26.996  45.700  -1.386  1.00 53.14           O  
ANISOU 5799  O   GLY B 380     6651   6206   7335   -579    223    276       O  
ATOM   5800  N   GLY B 381      24.818  46.234  -1.506  1.00 36.48           N  
ANISOU 5800  N   GLY B 381     4618   4080   5164   -530    202    246       N  
ATOM   5801  CA  GLY B 381      25.046  47.382  -2.369  1.00 42.56           C  
ANISOU 5801  CA  GLY B 381     5425   4826   5918   -537    229    263       C  
ATOM   5802  C   GLY B 381      24.924  47.094  -3.855  1.00 47.70           C  
ANISOU 5802  C   GLY B 381     6092   5484   6549   -505    264    269       C  
ATOM   5803  O   GLY B 381      25.153  47.977  -4.684  1.00 47.30           O  
ANISOU 5803  O   GLY B 381     6073   5414   6485   -509    291    284       O  
ATOM   5804  N   LYS B 382      24.565  45.861  -4.196  1.00 43.24           N  
ANISOU 5804  N   LYS B 382     5507   4942   5979   -473    264    258       N  
ATOM   5805  CA  LYS B 382      24.359  45.488  -5.591  1.00 40.21           C  
ANISOU 5805  CA  LYS B 382     5145   4563   5571   -440    293    261       C  
ATOM   5806  CB  LYS B 382      24.054  43.989  -5.706  1.00 39.73           C  
ANISOU 5806  CB  LYS B 382     5057   4528   5509   -411    285    248       C  
ATOM   5807  CG  LYS B 382      23.846  43.506  -7.135  1.00 46.94           C  
ANISOU 5807  CG  LYS B 382     5997   5443   6394   -377    313    251       C  
ATOM   5808  CD  LYS B 382      23.964  41.996  -7.245  1.00 52.55           C  
ANISOU 5808  CD  LYS B 382     6677   6179   7111   -357    313    243       C  
ATOM   5809  CE  LYS B 382      23.800  41.533  -8.688  1.00 58.68           C  
ANISOU 5809  CE  LYS B 382     7488   6952   7855   -324    340    247       C  
ATOM   5810  NZ  LYS B 382      24.711  42.251  -9.626  1.00 61.36           N  
ANISOU 5810  NZ  LYS B 382     7847   7274   8192   -332    389    271       N  
ATOM   5811  C   LYS B 382      23.230  46.315  -6.212  1.00 40.53           C  
ANISOU 5811  C   LYS B 382     5246   4582   5570   -415    289    256       C  
ATOM   5812  O   LYS B 382      22.253  46.643  -5.540  1.00 40.83           O  
ANISOU 5812  O   LYS B 382     5302   4615   5598   -407    258    242       O  
ATOM   5813  N   SER B 383      23.384  46.668  -7.485  1.00 43.73           N  
ANISOU 5813  N   SER B 383     5685   4977   5955   -401    322    269       N  
ATOM   5814  CA  SER B 383      22.367  47.426  -8.206  1.00 42.66           C  
ANISOU 5814  CA  SER B 383     5609   4822   5780   -376    320    266       C  
ATOM   5815  CB  SER B 383      23.016  48.372  -9.218  1.00 47.87           C  
ANISOU 5815  CB  SER B 383     6303   5459   6428   -385    360    287       C  
ATOM   5816  OG  SER B 383      23.795  49.356  -8.564  1.00 55.57           O  
ANISOU 5816  OG  SER B 383     7270   6419   7426   -427    366    300       O  
ATOM   5817  C   SER B 383      21.384  46.506  -8.920  1.00 43.55           C  
ANISOU 5817  C   SER B 383     5737   4946   5865   -333    308    253       C  
ATOM   5818  O   SER B 383      21.772  45.504  -9.526  1.00 40.24           O  
ANISOU 5818  O   SER B 383     5303   4541   5445   -320    324    254       O  
ATOM   5819  N   PHE B 384      20.105  46.851  -8.844  1.00 32.09           N  
ANISOU 5819  N   PHE B 384     4317   3487   4390   -311    279    243       N  
ATOM   5820  CA  PHE B 384      19.069  46.074  -9.510  1.00 35.27           C  
ANISOU 5820  CA  PHE B 384     4736   3897   4766   -272    261    233       C  
ATOM   5821  CB  PHE B 384      18.163  45.356  -8.500  1.00 27.77           C  
ANISOU 5821  CB  PHE B 384     3757   2966   3828   -262    219    215       C  
ATOM   5822  CG  PHE B 384      18.887  44.386  -7.619  1.00 31.22           C  
ANISOU 5822  CG  PHE B 384     4138   3426   4298   -280    216    208       C  
ATOM   5823  CD1 PHE B 384      19.321  43.168  -8.116  1.00 34.90           C  
ANISOU 5823  CD1 PHE B 384     4583   3910   4767   -271    226    206       C  
ATOM   5824  CE1 PHE B 384      19.992  42.275  -7.301  1.00 37.30           C  
ANISOU 5824  CE1 PHE B 384     4836   4235   5103   -287    223    200       C  
ATOM   5825  CZ  PHE B 384      20.219  42.588  -5.977  1.00 31.96           C  
ANISOU 5825  CZ  PHE B 384     4128   3560   4453   -313    207    196       C  
ATOM   5826  CE2 PHE B 384      19.790  43.797  -5.470  1.00 34.70           C  
ANISOU 5826  CE2 PHE B 384     4500   3888   4797   -323    197    198       C  
ATOM   5827  CD2 PHE B 384      19.123  44.687  -6.290  1.00 28.75           C  
ANISOU 5827  CD2 PHE B 384     3797   3114   4013   -306    202    204       C  
ATOM   5828  C   PHE B 384      18.229  46.980 -10.377  1.00 31.97           C  
ANISOU 5828  C   PHE B 384     4378   3458   4314   -250    260    238       C  
ATOM   5829  O   PHE B 384      17.792  48.046  -9.933  1.00 32.71           O  
ANISOU 5829  O   PHE B 384     4491   3535   4404   -256    251    240       O  
ATOM   5830  N   LYS B 385      18.000  46.562 -11.612  1.00 27.03           N  
ANISOU 5830  N   LYS B 385     3783   2829   3659   -225    268    241       N  
ATOM   5831  CA  LYS B 385      17.068  47.279 -12.459  1.00 32.60           C  
ANISOU 5831  CA  LYS B 385     4544   3513   4329   -200    260    246       C  
ATOM   5832  CB  LYS B 385      17.789  48.372 -13.256  1.00 37.78           C  
ANISOU 5832  CB  LYS B 385     5241   4144   4970   -211    300    262       C  
ATOM   5833  CG  LYS B 385      18.713  47.859 -14.338  1.00 46.78           C  
ANISOU 5833  CG  LYS B 385     6394   5283   6099   -209    339    272       C  
ATOM   5834  CD  LYS B 385      19.317  49.009 -15.135  1.00 57.71           C  
ANISOU 5834  CD  LYS B 385     7821   6639   7466   -217    379    289       C  
ATOM   5835  CE  LYS B 385      19.963  48.503 -16.425  1.00 64.07           C  
ANISOU 5835  CE  LYS B 385     8655   7438   8251   -204    418    299       C  
ATOM   5836  NZ  LYS B 385      20.726  47.236 -16.221  1.00 64.45           N  
ANISOU 5836  NZ  LYS B 385     8656   7509   8322   -208    432    297       N  
ATOM   5837  C   LYS B 385      16.369  46.277 -13.371  1.00 28.13           C  
ANISOU 5837  C   LYS B 385     3997   2955   3738   -168    242    240       C  
ATOM   5838  O   LYS B 385      16.980  45.300 -13.817  1.00 28.94           O  
ANISOU 5838  O   LYS B 385     4089   3067   3840   -166    257    239       O  
ATOM   5839  N   PHE B 386      15.081  46.505 -13.617  1.00 26.54           N  
ANISOU 5839  N   PHE B 386     3822   2745   3515   -143    207    238       N  
ATOM   5840  CA  PHE B 386      14.274  45.570 -14.389  1.00 23.97           C  
ANISOU 5840  CA  PHE B 386     3515   2425   3168   -114    179    234       C  
ATOM   5841  CB  PHE B 386      12.876  46.134 -14.631  1.00 23.58           C  
ANISOU 5841  CB  PHE B 386     3495   2363   3099    -90    142    237       C  
ATOM   5842  CG  PHE B 386      11.998  45.225 -15.420  1.00 24.26           C  
ANISOU 5842  CG  PHE B 386     3602   2453   3164    -64    107    235       C  
ATOM   5843  CD1 PHE B 386      11.715  43.946 -14.963  1.00 20.15           C  
ANISOU 5843  CD1 PHE B 386     3042   1955   2659    -61     80    223       C  
ATOM   5844  CE1 PHE B 386      10.900  43.108 -15.691  1.00 30.10           C  
ANISOU 5844  CE1 PHE B 386     4322   3216   3899    -40     43    222       C  
ATOM   5845  CZ  PHE B 386      10.375  43.528 -16.898  1.00 26.98           C  
ANISOU 5845  CZ  PHE B 386     3988   2798   3466    -21     32    233       C  
ATOM   5846  CE2 PHE B 386      10.656  44.791 -17.372  1.00 32.31           C  
ANISOU 5846  CE2 PHE B 386     4703   3451   4125    -21     60    244       C  
ATOM   5847  CD2 PHE B 386      11.470  45.635 -16.633  1.00 32.15           C  
ANISOU 5847  CD2 PHE B 386     4660   3430   4125    -43     98    245       C  
ATOM   5848  C   PHE B 386      14.926  45.242 -15.724  1.00 31.17           C  
ANISOU 5848  C   PHE B 386     4468   3325   4049   -106    209    240       C  
ATOM   5849  O   PHE B 386      15.258  46.135 -16.501  1.00 32.11           O  
ANISOU 5849  O   PHE B 386     4631   3421   4147   -106    237    252       O  
ATOM   5850  N   GLY B 387      15.109  43.956 -15.985  1.00 28.71           N  
ANISOU 5850  N   GLY B 387     4145   3028   3736    -99    206    233       N  
ATOM   5851  CA  GLY B 387      15.730  43.526 -17.219  1.00 35.23           C  
ANISOU 5851  CA  GLY B 387     5013   3842   4532    -88    236    239       C  
ATOM   5852  C   GLY B 387      16.050  42.051 -17.150  1.00 36.29           C  
ANISOU 5852  C   GLY B 387     5120   3995   4672    -84    234    229       C  
ATOM   5853  O   GLY B 387      15.440  41.305 -16.388  1.00 27.23           O  
ANISOU 5853  O   GLY B 387     3935   2868   3543    -83    196    217       O  
ATOM   5854  N   ARG B 388      17.030  41.624 -17.933  1.00 28.93           N  
ANISOU 5854  N   ARG B 388     4210   3056   3727    -82    278    236       N  
ATOM   5855  CA  ARG B 388      17.331  40.202 -18.022  1.00 30.50           C  
ANISOU 5855  CA  ARG B 388     4394   3269   3925    -74    279    228       C  
ATOM   5856  CB  ARG B 388      18.275  39.951 -19.204  1.00 37.81           C  
ANISOU 5856  CB  ARG B 388     5367   4177   4824    -63    333    240       C  
ATOM   5857  CG  ARG B 388      17.609  40.189 -20.542  1.00 42.51           C  
ANISOU 5857  CG  ARG B 388     6046   4743   5365    -38    323    244       C  
ATOM   5858  CD  ARG B 388      18.576  40.091 -21.722  1.00 44.57           C  
ANISOU 5858  CD  ARG B 388     6359   4980   5595    -26    383    258       C  
ATOM   5859  NE  ARG B 388      17.866  40.371 -22.966  1.00 46.14           N  
ANISOU 5859  NE  ARG B 388     6644   5148   5740     -2    368    261       N  
ATOM   5860  CZ  ARG B 388      17.849  39.569 -24.025  1.00 45.38           C  
ANISOU 5860  CZ  ARG B 388     6609   5032   5599     21    375    261       C  
ATOM   5861  NH1 ARG B 388      18.532  38.432 -24.015  1.00 43.96           N  
ANISOU 5861  NH1 ARG B 388     6416   4863   5425     26    400    259       N  
ATOM   5862  NH2 ARG B 388      17.156  39.916 -25.102  1.00 41.60           N  
ANISOU 5862  NH2 ARG B 388     6210   4524   5071     40    355    265       N  
ATOM   5863  C   ARG B 388      17.931  39.632 -16.743  1.00 29.55           C  
ANISOU 5863  C   ARG B 388     4198   3178   3853    -95    282    221       C  
ATOM   5864  O   ARG B 388      17.847  38.429 -16.502  1.00 31.92           O  
ANISOU 5864  O   ARG B 388     4476   3494   4158    -88    267    210       O  
ATOM   5865  N   ASP B 389      18.545  40.487 -15.932  1.00 29.18           N  
ANISOU 5865  N   ASP B 389     4113   3136   3840   -120    302    227       N  
ATOM   5866  CA  ASP B 389      19.136  40.047 -14.674  1.00 28.52           C  
ANISOU 5866  CA  ASP B 389     3958   3076   3800   -143    302    221       C  
ATOM   5867  CB  ASP B 389      20.499  40.702 -14.476  1.00 38.48           C  
ANISOU 5867  CB  ASP B 389     5196   4335   5089   -169    352    237       C  
ATOM   5868  CG  ASP B 389      21.532  40.204 -15.468  1.00 52.39           C  
ANISOU 5868  CG  ASP B 389     6976   6090   6840   -160    404    251       C  
ATOM   5869  OD1 ASP B 389      21.393  39.057 -15.942  1.00 57.31           O  
ANISOU 5869  OD1 ASP B 389     7612   6718   7446   -138    402    244       O  
ATOM   5870  OD2 ASP B 389      22.481  40.959 -15.769  1.00 58.81           O  
ANISOU 5870  OD2 ASP B 389     7791   6890   7663   -174    450    270       O  
ATOM   5871  C   ASP B 389      18.249  40.324 -13.445  1.00 26.83           C  
ANISOU 5871  C   ASP B 389     3710   2875   3609   -153    255    209       C  
ATOM   5872  O   ASP B 389      18.668  40.104 -12.313  1.00 25.21           O  
ANISOU 5872  O   ASP B 389     3451   2688   3441   -173    251    204       O  
ATOM   5873  N   TYR B 390      17.035  40.813 -13.666  1.00 28.29           N  
ANISOU 5873  N   TYR B 390     3927   3049   3772   -137    220    206       N  
ATOM   5874  CA  TYR B 390      16.125  41.083 -12.553  1.00 25.79           C  
ANISOU 5874  CA  TYR B 390     3581   2742   3476   -142    179    197       C  
ATOM   5875  CB  TYR B 390      16.484  42.423 -11.883  1.00 22.36           C  
ANISOU 5875  CB  TYR B 390     3140   2298   3060   -164    195    204       C  
ATOM   5876  CG  TYR B 390      15.535  42.866 -10.776  1.00 23.99           C  
ANISOU 5876  CG  TYR B 390     3327   2507   3282   -166    159    197       C  
ATOM   5877  CD1 TYR B 390      15.527  42.236  -9.539  1.00 24.30           C  
ANISOU 5877  CD1 TYR B 390     3315   2567   3352   -177    141    186       C  
ATOM   5878  CE1 TYR B 390      14.644  42.645  -8.522  1.00 23.01           C  
ANISOU 5878  CE1 TYR B 390     3138   2404   3202   -176    112    181       C  
ATOM   5879  CZ  TYR B 390      13.791  43.698  -8.751  1.00 24.54           C  
ANISOU 5879  CZ  TYR B 390     3367   2577   3379   -163    103    189       C  
ATOM   5880  OH  TYR B 390      12.923  44.104  -7.760  1.00 20.47           O  
ANISOU 5880  OH  TYR B 390     2841   2061   2877   -158     80    186       O  
ATOM   5881  CE2 TYR B 390      13.789  44.346  -9.977  1.00 25.02           C  
ANISOU 5881  CE2 TYR B 390     3477   2619   3410   -152    119    200       C  
ATOM   5882  CD2 TYR B 390      14.662  43.932 -10.974  1.00 24.42           C  
ANISOU 5882  CD2 TYR B 390     3417   2542   3319   -154    146    204       C  
ATOM   5883  C   TYR B 390      14.684  41.057 -13.083  1.00 23.91           C  
ANISOU 5883  C   TYR B 390     3378   2496   3211   -115    137    194       C  
ATOM   5884  O   TYR B 390      14.163  42.059 -13.564  1.00 27.46           O  
ANISOU 5884  O   TYR B 390     3866   2926   3642   -106    133    203       O  
ATOM   5885  N   LEU B 391      14.073  39.875 -13.015  1.00 22.76           N  
ANISOU 5885  N   LEU B 391     3218   2365   3065   -102    104    184       N  
ATOM   5886  CA  LEU B 391      12.770  39.572 -13.607  1.00 25.32           C  
ANISOU 5886  CA  LEU B 391     3571   2683   3365    -77     60    184       C  
ATOM   5887  CB  LEU B 391      12.830  38.251 -14.403  1.00 35.24           C  
ANISOU 5887  CB  LEU B 391     4847   3944   4600    -65     52    178       C  
ATOM   5888  CG  LEU B 391      13.668  38.046 -15.662  1.00 23.93           C  
ANISOU 5888  CG  LEU B 391     3464   2495   3134    -58     89    184       C  
ATOM   5889  CD1 LEU B 391      13.872  36.559 -15.902  1.00 31.84           C  
ANISOU 5889  CD1 LEU B 391     4464   3507   4128    -50     84    175       C  
ATOM   5890  CD2 LEU B 391      12.927  38.632 -16.818  1.00 31.70           C  
ANISOU 5890  CD2 LEU B 391     4513   3453   4077    -39     73    193       C  
ATOM   5891  C   LEU B 391      11.685  39.422 -12.537  1.00 15.06           C  
ANISOU 5891  C   LEU B 391     2232   1399   2092    -75     17    177       C  
ATOM   5892  O   LEU B 391      10.498  39.399 -12.849  1.00 19.34           O  
ANISOU 5892  O   LEU B 391     2790   1936   2623    -57    -22    181       O  
ATOM   5893  N   ILE B 392      12.121  39.256 -11.294  1.00 17.66           N  
ANISOU 5893  N   ILE B 392     2509   1745   2455    -93     25    169       N  
ATOM   5894  CA  ILE B 392      11.208  39.012 -10.170  1.00 16.05           C  
ANISOU 5894  CA  ILE B 392     2266   1556   2279    -91    -10    163       C  
ATOM   5895  CB  ILE B 392      11.003  37.517  -9.896  1.00 22.46           C  
ANISOU 5895  CB  ILE B 392     3047   2388   3100    -87    -34    151       C  
ATOM   5896  CG1 ILE B 392      12.304  36.779 -10.224  1.00 23.86           C  
ANISOU 5896  CG1 ILE B 392     3221   2572   3273    -98     -1    146       C  
ATOM   5897  CD1 ILE B 392      12.254  35.293  -9.941  1.00 42.92           C  
ANISOU 5897  CD1 ILE B 392     5607   5005   5695    -96    -19    133       C  
ATOM   5898  CG2 ILE B 392       9.782  37.003 -10.649  1.00 33.11           C  
ANISOU 5898  CG2 ILE B 392     4418   3732   4429    -65    -77    155       C  
ATOM   5899  C   ILE B 392      11.814  39.677  -8.948  1.00 17.98           C  
ANISOU 5899  C   ILE B 392     2478   1803   2552   -113     11    161       C  
ATOM   5900  O   ILE B 392      13.024  39.901  -8.890  1.00 19.47           O  
ANISOU 5900  O   ILE B 392     2661   1990   2745   -133     46    161       O  
ATOM   5901  N   PRO B 393      10.969  40.016  -7.965  1.00 17.73           N  
ANISOU 5901  N   PRO B 393     2424   1773   2538   -109    -11    160       N  
ATOM   5902  CA  PRO B 393      11.486  40.692  -6.776  1.00 17.18           C  
ANISOU 5902  CA  PRO B 393     2333   1702   2492   -130      6    158       C  
ATOM   5903  CB  PRO B 393      10.212  40.995  -5.962  1.00 18.25           C  
ANISOU 5903  CB  PRO B 393     2458   1836   2641   -115    -21    159       C  
ATOM   5904  CG  PRO B 393       9.111  40.968  -6.974  1.00 14.66           C  
ANISOU 5904  CG  PRO B 393     2029   1375   2166    -87    -46    169       C  
ATOM   5905  CD  PRO B 393       9.502  39.859  -7.910  1.00 17.50           C  
ANISOU 5905  CD  PRO B 393     2393   1744   2510    -86    -50    164       C  
ATOM   5906  C   PRO B 393      12.435  39.797  -5.987  1.00 19.80           C  
ANISOU 5906  C   PRO B 393     2622   2053   2848   -151     15    146       C  
ATOM   5907  O   PRO B 393      12.327  38.563  -6.043  1.00 19.78           O  
ANISOU 5907  O   PRO B 393     2599   2068   2849   -145      0    137       O  
ATOM   5908  N   LYS B 394      13.374  40.432  -5.287  1.00 19.25           N  
ANISOU 5908  N   LYS B 394     2543   1979   2793   -177     38    146       N  
ATOM   5909  CA  LYS B 394      14.247  39.727  -4.347  1.00 21.14           C  
ANISOU 5909  CA  LYS B 394     2739   2234   3058   -199     43    137       C  
ATOM   5910  CB  LYS B 394      15.401  40.639  -3.904  1.00 23.57           C  
ANISOU 5910  CB  LYS B 394     3046   2531   3379   -230     70    143       C  
ATOM   5911  CG  LYS B 394      16.194  41.264  -5.049  1.00 22.70           C  
ANISOU 5911  CG  LYS B 394     2966   2408   3252   -236    102    156       C  
ATOM   5912  CD  LYS B 394      16.857  40.198  -5.887  1.00 25.22           C  
ANISOU 5912  CD  LYS B 394     3274   2740   3567   -231    118    156       C  
ATOM   5913  CE  LYS B 394      17.915  39.454  -5.090  1.00 31.94           C  
ANISOU 5913  CE  LYS B 394     4077   3609   4448   -254    126    152       C  
ATOM   5914  NZ  LYS B 394      18.522  38.358  -5.907  1.00 37.62           N  
ANISOU 5914  NZ  LYS B 394     4788   4342   5164   -245    143    153       N  
ATOM   5915  C   LYS B 394      13.454  39.263  -3.128  1.00 19.62           C  
ANISOU 5915  C   LYS B 394     2517   2052   2885   -194     15    126       C  
ATOM   5916  O   LYS B 394      12.549  39.954  -2.658  1.00 19.98           O  
ANISOU 5916  O   LYS B 394     2575   2086   2931   -184      3    129       O  
ATOM   5917  N   PRO B 395      13.792  38.076  -2.598  1.00 23.77           N  
ANISOU 5917  N   PRO B 395     3006   2599   3429   -200      8    115       N  
ATOM   5918  CA  PRO B 395      13.080  37.542  -1.427  1.00 23.97           C  
ANISOU 5918  CA  PRO B 395     3002   2633   3472   -195    -17    105       C  
ATOM   5919  CB  PRO B 395      13.836  36.231  -1.127  1.00 22.87           C  
ANISOU 5919  CB  PRO B 395     2826   2516   3348   -205    -18     94       C  
ATOM   5920  CG  PRO B 395      14.396  35.819  -2.440  1.00 27.41           C  
ANISOU 5920  CG  PRO B 395     3414   3094   3905   -200     -1     99       C  
ATOM   5921  CD  PRO B 395      14.758  37.116  -3.150  1.00 23.62           C  
ANISOU 5921  CD  PRO B 395     2971   2594   3410   -206     22    112       C  
ATOM   5922  C   PRO B 395      13.100  38.470  -0.209  1.00 23.95           C  
ANISOU 5922  C   PRO B 395     3001   2618   3483   -210    -15    105       C  
ATOM   5923  O   PRO B 395      12.112  38.510   0.524  1.00 29.62           O  
ANISOU 5923  O   PRO B 395     3715   3332   4207   -196    -32    103       O  
ATOM   5924  N   PHE B 396      14.167  39.245  -0.003  1.00 20.02           N  
ANISOU 5924  N   PHE B 396     2510   2108   2989   -237      6    110       N  
ATOM   5925  CA  PHE B 396      14.224  40.098   1.170  1.00 20.95           C  
ANISOU 5925  CA  PHE B 396     2634   2209   3116   -253      5    110       C  
ATOM   5926  CB  PHE B 396      15.647  40.080   1.747  1.00 22.40           C  
ANISOU 5926  CB  PHE B 396     2798   2395   3318   -290     15    108       C  
ATOM   5927  CG  PHE B 396      15.994  38.768   2.410  1.00 30.83           C  
ANISOU 5927  CG  PHE B 396     3822   3485   4406   -295      2     96       C  
ATOM   5928  CD1 PHE B 396      16.551  37.730   1.678  1.00 32.93           C  
ANISOU 5928  CD1 PHE B 396     4064   3773   4676   -293      9     95       C  
ATOM   5929  CE1 PHE B 396      16.846  36.513   2.278  1.00 37.51           C  
ANISOU 5929  CE1 PHE B 396     4605   4373   5272   -296     -2     84       C  
ATOM   5930  CZ  PHE B 396      16.576  36.327   3.625  1.00 31.13           C  
ANISOU 5930  CZ  PHE B 396     3783   3565   4479   -303    -21     75       C  
ATOM   5931  CE2 PHE B 396      16.012  37.352   4.363  1.00 32.03           C  
ANISOU 5931  CE2 PHE B 396     3924   3657   4589   -305    -27     76       C  
ATOM   5932  CD2 PHE B 396      15.714  38.562   3.752  1.00 36.44           C  
ANISOU 5932  CD2 PHE B 396     4521   4196   5131   -301    -15     87       C  
ATOM   5933  C   PHE B 396      13.748  41.536   0.911  1.00 26.44           C  
ANISOU 5933  C   PHE B 396     3374   2877   3794   -247     14    121       C  
ATOM   5934  O   PHE B 396      13.970  42.437   1.717  1.00 26.48           O  
ANISOU 5934  O   PHE B 396     3396   2863   3802   -264     18    123       O  
ATOM   5935  N   ASP B 397      13.055  41.732  -0.205  1.00 26.55           N  
ANISOU 5935  N   ASP B 397     3410   2888   3788   -222     15    129       N  
ATOM   5936  CA  ASP B 397      12.409  43.013  -0.500  1.00 21.45           C  
ANISOU 5936  CA  ASP B 397     2807   2218   3126   -210     21    140       C  
ATOM   5937  CB  ASP B 397      12.145  43.111  -2.011  1.00 19.06           C  
ANISOU 5937  CB  ASP B 397     2527   1914   2800   -192     25    149       C  
ATOM   5938  CG  ASP B 397      11.609  44.457  -2.454  1.00 24.90           C  
ANISOU 5938  CG  ASP B 397     3312   2628   3520   -180     34    162       C  
ATOM   5939  OD1 ASP B 397      11.161  45.277  -1.616  1.00 22.29           O  
ANISOU 5939  OD1 ASP B 397     2997   2281   3193   -178     34    165       O  
ATOM   5940  OD2 ASP B 397      11.613  44.667  -3.691  1.00 23.29           O  
ANISOU 5940  OD2 ASP B 397     3133   2419   3296   -170     41    170       O  
ATOM   5941  C   ASP B 397      11.118  43.110   0.303  1.00 20.70           C  
ANISOU 5941  C   ASP B 397     2712   2118   3035   -186      4    140       C  
ATOM   5942  O   ASP B 397      10.187  42.346   0.080  1.00 23.08           O  
ANISOU 5942  O   ASP B 397     2997   2433   3339   -161    -15    139       O  
ATOM   5943  N   THR B 398      11.056  44.047   1.242  1.00 22.86           N  
ANISOU 5943  N   THR B 398     3006   2370   3310   -194     10    142       N  
ATOM   5944  CA  THR B 398       9.882  44.158   2.105  1.00 24.56           C  
ANISOU 5944  CA  THR B 398     3223   2578   3532   -169      0    144       C  
ATOM   5945  CB  THR B 398      10.153  45.083   3.322  1.00 34.24           C  
ANISOU 5945  CB  THR B 398     4475   3778   4758   -186     11    143       C  
ATOM   5946  OG1 THR B 398      10.505  46.402   2.876  1.00 32.35           O  
ANISOU 5946  OG1 THR B 398     4279   3512   4499   -195     28    153       O  
ATOM   5947  CG2 THR B 398      11.275  44.511   4.178  1.00 36.06           C  
ANISOU 5947  CG2 THR B 398     4681   4016   5003   -221      7    129       C  
ATOM   5948  C   THR B 398       8.657  44.657   1.354  1.00 21.73           C  
ANISOU 5948  C   THR B 398     2886   2211   3161   -133     -3    158       C  
ATOM   5949  O   THR B 398       7.540  44.608   1.874  1.00 25.43           O  
ANISOU 5949  O   THR B 398     3348   2677   3638   -107    -11    164       O  
ATOM   5950  N   ARG B 399       8.849  45.136   0.126  1.00 18.15           N  
ANISOU 5950  N   ARG B 399     2455   1752   2688   -132      4    166       N  
ATOM   5951  CA  ARG B 399       7.700  45.539  -0.681  1.00 15.44           C  
ANISOU 5951  CA  ARG B 399     2131   1402   2334    -98     -4    181       C  
ATOM   5952  CB  ARG B 399       8.141  46.250  -1.955  1.00 16.18           C  
ANISOU 5952  CB  ARG B 399     2260   1484   2403   -101      8    189       C  
ATOM   5953  CG  ARG B 399       8.770  47.608  -1.691  1.00 17.67           C  
ANISOU 5953  CG  ARG B 399     2488   1645   2580   -120     33    194       C  
ATOM   5954  CD  ARG B 399       9.217  48.286  -2.978  1.00 17.72           C  
ANISOU 5954  CD  ARG B 399     2531   1641   2563   -123     47    203       C  
ATOM   5955  NE  ARG B 399      10.193  47.455  -3.654  1.00 15.21           N  
ANISOU 5955  NE  ARG B 399     2194   1341   2244   -143     51    195       N  
ATOM   5956  CZ  ARG B 399      10.591  47.619  -4.904  1.00 16.36           C  
ANISOU 5956  CZ  ARG B 399     2362   1483   2370   -143     62    201       C  
ATOM   5957  NH1 ARG B 399      10.121  48.627  -5.651  1.00 16.02           N  
ANISOU 5957  NH1 ARG B 399     2363   1419   2306   -127     68    214       N  
ATOM   5958  NH2 ARG B 399      11.488  46.770  -5.400  1.00 15.73           N  
ANISOU 5958  NH2 ARG B 399     2264   1420   2293   -158     69    195       N  
ATOM   5959  C   ARG B 399       6.823  44.362  -1.076  1.00 14.38           C  
ANISOU 5959  C   ARG B 399     1963   1291   2209    -75    -31    182       C  
ATOM   5960  O   ARG B 399       5.663  44.558  -1.429  1.00 16.19           O  
ANISOU 5960  O   ARG B 399     2197   1516   2438    -45    -44    196       O  
ATOM   5961  N   VAL B 400       7.371  43.153  -1.061  1.00 15.25           N  
ANISOU 5961  N   VAL B 400     2041   1425   2330    -89    -40    168       N  
ATOM   5962  CA  VAL B 400       6.627  42.025  -1.616  1.00 13.48           C  
ANISOU 5962  CA  VAL B 400     1791   1221   2110    -71    -67    169       C  
ATOM   5963  CB  VAL B 400       7.462  40.727  -1.595  1.00 14.81           C  
ANISOU 5963  CB  VAL B 400     1929   1413   2286    -90    -72    152       C  
ATOM   5964  CG1 VAL B 400       6.594  39.532  -1.978  1.00 18.92           C  
ANISOU 5964  CG1 VAL B 400     2425   1952   2814    -72   -103    152       C  
ATOM   5965  CG2 VAL B 400       8.696  40.872  -2.531  1.00 17.86           C  
ANISOU 5965  CG2 VAL B 400     2335   1797   2653   -110    -52    149       C  
ATOM   5966  C   VAL B 400       5.289  41.835  -0.875  1.00 13.38           C  
ANISOU 5966  C   VAL B 400     1756   1209   2117    -45    -85    177       C  
ATOM   5967  O   VAL B 400       4.245  41.741  -1.503  1.00 16.17           O  
ANISOU 5967  O   VAL B 400     2109   1564   2471    -20   -105    191       O  
ATOM   5968  N   LEU B 401       5.321  41.800   0.457  1.00 15.39           N  
ANISOU 5968  N   LEU B 401     1996   1463   2390    -50    -76    170       N  
ATOM   5969  CA  LEU B 401       4.081  41.612   1.225  1.00 15.54           C  
ANISOU 5969  CA  LEU B 401     1993   1482   2429    -24    -87    180       C  
ATOM   5970  CB  LEU B 401       4.376  41.537   2.728  1.00 15.19           C  
ANISOU 5970  CB  LEU B 401     1938   1433   2400    -35    -73    169       C  
ATOM   5971  CG  LEU B 401       3.188  41.239   3.655  1.00 18.83           C  
ANISOU 5971  CG  LEU B 401     2376   1894   2884     -9    -78    178       C  
ATOM   5972  CD1 LEU B 401       2.742  39.805   3.479  1.00 18.32           C  
ANISOU 5972  CD1 LEU B 401     2267   1857   2838     -4   -105    175       C  
ATOM   5973  CD2 LEU B 401       3.579  41.487   5.112  1.00 26.05           C  
ANISOU 5973  CD2 LEU B 401     3298   2795   3805    -20    -59    169       C  
ATOM   5974  C   LEU B 401       3.104  42.750   0.948  1.00 16.27           C  
ANISOU 5974  C   LEU B 401     2112   1552   2516      4    -82    202       C  
ATOM   5975  O   LEU B 401       1.896  42.522   0.784  1.00 16.71           O  
ANISOU 5975  O   LEU B 401     2151   1612   2586     32    -99    219       O  
ATOM   5976  N   LEU B 402       3.634  43.975   0.879  1.00 15.43           N  
ANISOU 5976  N   LEU B 402     2048   1423   2391     -4    -58    205       N  
ATOM   5977  CA  LEU B 402       2.802  45.147   0.671  1.00 20.07           C  
ANISOU 5977  CA  LEU B 402     2666   1988   2971     22    -49    226       C  
ATOM   5978  CB  LEU B 402       3.641  46.417   0.881  1.00 19.71           C  
ANISOU 5978  CB  LEU B 402     2668   1915   2904      5    -20    223       C  
ATOM   5979  CG  LEU B 402       4.331  46.494   2.252  1.00 33.63           C  
ANISOU 5979  CG  LEU B 402     4434   3671   4675    -18     -4    209       C  
ATOM   5980  CD1 LEU B 402       5.215  47.759   2.373  1.00 40.91           C  
ANISOU 5980  CD1 LEU B 402     5405   4563   5574    -40     20    207       C  
ATOM   5981  CD2 LEU B 402       3.314  46.393   3.403  1.00 41.97           C  
ANISOU 5981  CD2 LEU B 402     5477   4720   5750      8     -1    216       C  
ATOM   5982  C   LEU B 402       2.143  45.182  -0.702  1.00 18.60           C  
ANISOU 5982  C   LEU B 402     2486   1806   2776     42    -70    241       C  
ATOM   5983  O   LEU B 402       1.073  45.752  -0.861  1.00 19.81           O  
ANISOU 5983  O   LEU B 402     2646   1948   2934     72    -73    263       O  
ATOM   5984  N   TRP B 403       2.791  44.600  -1.701  1.00 17.89           N  
ANISOU 5984  N   TRP B 403     2395   1729   2672     25    -82    232       N  
ATOM   5985  CA  TRP B 403       2.216  44.529  -3.041  1.00 18.69           C  
ANISOU 5985  CA  TRP B 403     2508   1833   2762     42   -105    245       C  
ATOM   5986  CB  TRP B 403       3.336  44.527  -4.087  1.00 18.10           C  
ANISOU 5986  CB  TRP B 403     2460   1757   2658     19    -98    234       C  
ATOM   5987  CG  TRP B 403       3.890  45.905  -4.341  1.00 22.59           C  
ANISOU 5987  CG  TRP B 403     3076   2301   3205     13    -69    239       C  
ATOM   5988  CD1 TRP B 403       4.460  46.745  -3.424  1.00 19.20           C  
ANISOU 5988  CD1 TRP B 403     2662   1857   2777     -1    -40    234       C  
ATOM   5989  NE1 TRP B 403       4.845  47.925  -4.034  1.00 20.93           N  
ANISOU 5989  NE1 TRP B 403     2928   2053   2972     -5    -20    242       N  
ATOM   5990  CE2 TRP B 403       4.522  47.856  -5.363  1.00 20.35           C  
ANISOU 5990  CE2 TRP B 403     2872   1981   2881      9    -35    251       C  
ATOM   5991  CD2 TRP B 403       3.916  46.602  -5.592  1.00 21.01           C  
ANISOU 5991  CD2 TRP B 403     2919   2087   2978     20    -67    249       C  
ATOM   5992  CE3 TRP B 403       3.492  46.280  -6.888  1.00 21.80           C  
ANISOU 5992  CE3 TRP B 403     3032   2189   3061     33    -91    258       C  
ATOM   5993  CZ3 TRP B 403       3.677  47.203  -7.893  1.00 25.69           C  
ANISOU 5993  CZ3 TRP B 403     3574   2662   3526     37    -81    267       C  
ATOM   5994  CH2 TRP B 403       4.273  48.455  -7.632  1.00 24.12           C  
ANISOU 5994  CH2 TRP B 403     3408   2441   3315     27    -46    268       C  
ATOM   5995  CZ2 TRP B 403       4.709  48.790  -6.378  1.00 22.46           C  
ANISOU 5995  CZ2 TRP B 403     3185   2228   3120     12    -24    260       C  
ATOM   5996  C   TRP B 403       1.308  43.320  -3.255  1.00 18.39           C  
ANISOU 5996  C   TRP B 403     2430   1816   2742     56   -142    250       C  
ATOM   5997  O   TRP B 403       0.252  43.416  -3.891  1.00 18.78           O  
ANISOU 5997  O   TRP B 403     2479   1862   2794     81   -167    271       O  
ATOM   5998  N   VAL B 404       1.716  42.168  -2.749  1.00 14.15           N  
ANISOU 5998  N   VAL B 404     1860   1299   2219     40   -149    233       N  
ATOM   5999  CA  VAL B 404       0.994  40.958  -3.068  1.00 20.08           C  
ANISOU 5999  CA  VAL B 404     2577   2069   2983     48   -186    237       C  
ATOM   6000  CB  VAL B 404       1.921  39.722  -3.006  1.00 13.59           C  
ANISOU 6000  CB  VAL B 404     1736   1267   2160     23   -190    213       C  
ATOM   6001  CG1 VAL B 404       1.147  38.447  -3.372  1.00 16.12           C  
ANISOU 6001  CG1 VAL B 404     2026   1605   2492     31   -230    216       C  
ATOM   6002  CG2 VAL B 404       3.121  39.928  -3.933  1.00 22.55           C  
ANISOU 6002  CG2 VAL B 404     2906   2397   3263      3   -174    202       C  
ATOM   6003  C   VAL B 404      -0.214  40.715  -2.174  1.00 18.15           C  
ANISOU 6003  C   VAL B 404     2294   1828   2773     70   -198    251       C  
ATOM   6004  O   VAL B 404      -1.269  40.343  -2.676  1.00 16.92           O  
ANISOU 6004  O   VAL B 404     2122   1678   2629     89   -230    269       O  
ATOM   6005  N   ALA B 405      -0.075  40.863  -0.860  1.00 14.16           N  
ANISOU 6005  N   ALA B 405     1776   1321   2285     68   -174    245       N  
ATOM   6006  CA  ALA B 405      -1.198  40.510   0.018  1.00 12.94           C  
ANISOU 6006  CA  ALA B 405     1582   1170   2163     89   -181    259       C  
ATOM   6007  CB  ALA B 405      -0.807  40.661   1.490  1.00 16.20           C  
ANISOU 6007  CB  ALA B 405     1990   1577   2587     83   -150    247       C  
ATOM   6008  C   ALA B 405      -2.479  41.319  -0.293  1.00 16.02           C  
ANISOU 6008  C   ALA B 405     1976   1546   2564    124   -188    292       C  
ATOM   6009  O   ALA B 405      -3.550  40.744  -0.336  1.00 18.60           O  
ANISOU 6009  O   ALA B 405     2268   1883   2917    142   -214    310       O  
ATOM   6010  N   PRO B 406      -2.363  42.635  -0.550  1.00 14.80           N  
ANISOU 6010  N   PRO B 406     1863   1370   2391    133   -166    301       N  
ATOM   6011  CA  PRO B 406      -3.589  43.381  -0.862  1.00 16.49           C  
ANISOU 6011  CA  PRO B 406     2079   1571   2617    168   -172    333       C  
ATOM   6012  CB  PRO B 406      -3.086  44.822  -0.998  1.00 19.36           C  
ANISOU 6012  CB  PRO B 406     2496   1908   2952    169   -140    334       C  
ATOM   6013  CG  PRO B 406      -1.890  44.871  -0.141  1.00 19.23           C  
ANISOU 6013  CG  PRO B 406     2494   1888   2923    141   -110    307       C  
ATOM   6014  CD  PRO B 406      -1.217  43.552  -0.392  1.00 16.33           C  
ANISOU 6014  CD  PRO B 406     2101   1546   2556    114   -132    284       C  
ATOM   6015  C   PRO B 406      -4.254  42.930  -2.155  1.00 22.25           C  
ANISOU 6015  C   PRO B 406     2799   2310   3347    176   -217    349       C  
ATOM   6016  O   PRO B 406      -5.475  42.977  -2.260  1.00 21.10           O  
ANISOU 6016  O   PRO B 406     2629   2164   3226    204   -237    379       O  
ATOM   6017  N   GLU B 407      -3.466  42.518  -3.145  1.00 17.81           N  
ANISOU 6017  N   GLU B 407     2256   1754   2755    153   -234    332       N  
ATOM   6018  CA  GLU B 407      -4.068  42.042  -4.392  1.00 18.62           C  
ANISOU 6018  CA  GLU B 407     2358   1863   2854    159   -280    346       C  
ATOM   6019  CB  GLU B 407      -3.019  41.985  -5.512  1.00 19.98           C  
ANISOU 6019  CB  GLU B 407     2574   2033   2985    136   -283    327       C  
ATOM   6020  CG  GLU B 407      -2.501  43.370  -5.942  1.00 21.85           C  
ANISOU 6020  CG  GLU B 407     2862   2246   3192    139   -252    329       C  
ATOM   6021  CD  GLU B 407      -3.613  44.359  -6.293  1.00 39.76           C  
ANISOU 6021  CD  GLU B 407     5142   4498   5467    171   -262    361       C  
ATOM   6022  OE1 GLU B 407      -4.663  43.932  -6.819  1.00 37.59           O  
ANISOU 6022  OE1 GLU B 407     4847   4229   5208    188   -304    383       O  
ATOM   6023  OE2 GLU B 407      -3.429  45.571  -6.046  1.00 48.02           O  
ANISOU 6023  OE2 GLU B 407     6219   5525   6503    180   -228    366       O  
ATOM   6024  C   GLU B 407      -4.729  40.681  -4.223  1.00 16.80           C  
ANISOU 6024  C   GLU B 407     2077   1653   2652    158   -317    350       C  
ATOM   6025  O   GLU B 407      -5.746  40.377  -4.860  1.00 17.97           O  
ANISOU 6025  O   GLU B 407     2209   1805   2815    172   -359    374       O  
ATOM   6026  N   VAL B 408      -4.132  39.831  -3.389  1.00 15.83           N  
ANISOU 6026  N   VAL B 408     1931   1546   2538    139   -305    327       N  
ATOM   6027  CA  VAL B 408      -4.785  38.573  -3.035  1.00 15.65           C  
ANISOU 6027  CA  VAL B 408     1859   1542   2546    138   -336    331       C  
ATOM   6028  CB  VAL B 408      -3.851  37.734  -2.177  1.00 12.81           C  
ANISOU 6028  CB  VAL B 408     1484   1195   2186    114   -317    300       C  
ATOM   6029  CG1 VAL B 408      -4.578  36.544  -1.571  1.00 14.24           C  
ANISOU 6029  CG1 VAL B 408     1613   1394   2403    116   -341    305       C  
ATOM   6030  CG2 VAL B 408      -2.650  37.277  -3.033  1.00 14.68           C  
ANISOU 6030  CG2 VAL B 408     1753   1438   2387     87   -321    274       C  
ATOM   6031  C   VAL B 408      -6.117  38.829  -2.314  1.00 18.72           C  
ANISOU 6031  C   VAL B 408     2209   1928   2977    168   -338    362       C  
ATOM   6032  O   VAL B 408      -7.134  38.211  -2.624  1.00 19.82           O  
ANISOU 6032  O   VAL B 408     2314   2075   3141    177   -377    384       O  
ATOM   6033  N   ALA B 409      -6.098  39.761  -1.370  1.00 17.54           N  
ANISOU 6033  N   ALA B 409     2065   1764   2834    182   -294    366       N  
ATOM   6034  CA  ALA B 409      -7.293  40.125  -0.609  1.00 17.05           C  
ANISOU 6034  CA  ALA B 409     1972   1696   2811    214   -284    397       C  
ATOM   6035  CB  ALA B 409      -6.932  41.164   0.464  1.00 18.27           C  
ANISOU 6035  CB  ALA B 409     2151   1831   2960    224   -229    392       C  
ATOM   6036  C   ALA B 409      -8.401  40.661  -1.524  1.00 19.47           C  
ANISOU 6036  C   ALA B 409     2275   1995   3128    240   -313    434       C  
ATOM   6037  O   ALA B 409      -9.575  40.309  -1.365  1.00 21.57           O  
ANISOU 6037  O   ALA B 409     2495   2266   3434    260   -335    465       O  
ATOM   6038  N   LYS B 410      -8.024  41.507  -2.477  1.00 22.04           N  
ANISOU 6038  N   LYS B 410     2647   2306   3419    239   -314    434       N  
ATOM   6039  CA  LYS B 410      -8.982  42.066  -3.427  1.00 22.60           C  
ANISOU 6039  CA  LYS B 410     2722   2368   3496    263   -344    468       C  
ATOM   6040  CB  LYS B 410      -8.324  43.137  -4.284  1.00 20.87           C  
ANISOU 6040  CB  LYS B 410     2565   2131   3234    260   -331    461       C  
ATOM   6041  CG  LYS B 410      -7.991  44.412  -3.552  1.00 27.50           C  
ANISOU 6041  CG  LYS B 410     3436   2950   4063    274   -276    459       C  
ATOM   6042  CD  LYS B 410      -7.451  45.433  -4.550  1.00 44.15           C  
ANISOU 6042  CD  LYS B 410     5604   5040   6130    272   -269    456       C  
ATOM   6043  CE  LYS B 410      -7.030  46.722  -3.874  1.00 53.04           C  
ANISOU 6043  CE  LYS B 410     6768   6143   7242    281   -216    453       C  
ATOM   6044  NZ  LYS B 410      -6.531  47.705  -4.881  1.00 61.58           N  
ANISOU 6044  NZ  LYS B 410     7907   7206   8283    278   -210    451       N  
ATOM   6045  C   LYS B 410      -9.568  40.979  -4.321  1.00 25.10           C  
ANISOU 6045  C   LYS B 410     3011   2700   3824    254   -407    479       C  
ATOM   6046  O   LYS B 410     -10.767  40.993  -4.636  1.00 21.35           O  
ANISOU 6046  O   LYS B 410     2507   2225   3381    276   -440    516       O  
ATOM   6047  N   ALA B 411      -8.730  40.025  -4.729  1.00 19.50           N  
ANISOU 6047  N   ALA B 411     2313   2003   3091    222   -425    448       N  
ATOM   6048  CA  ALA B 411      -9.228  38.931  -5.549  1.00 23.01           C  
ANISOU 6048  CA  ALA B 411     2740   2461   3543    211   -485    456       C  
ATOM   6049  CB  ALA B 411      -8.085  38.103  -6.124  1.00 22.90           C  
ANISOU 6049  CB  ALA B 411     2757   2454   3490    179   -494    419       C  
ATOM   6050  C   ALA B 411     -10.172  38.045  -4.739  1.00 20.00           C  
ANISOU 6050  C   ALA B 411     2293   2094   3213    218   -503    474       C  
ATOM   6051  O   ALA B 411     -11.130  37.510  -5.293  1.00 24.15           O  
ANISOU 6051  O   ALA B 411     2791   2625   3762    221   -555    500       O  
ATOM   6052  N   ALA B 412      -9.896  37.873  -3.445  1.00 20.01           N  
ANISOU 6052  N   ALA B 412     2269   2102   3232    217   -462    461       N  
ATOM   6053  CA  ALA B 412     -10.769  37.073  -2.586  1.00 17.36           C  
ANISOU 6053  CA  ALA B 412     1871   1778   2945    225   -471    478       C  
ATOM   6054  CB  ALA B 412     -10.156  36.892  -1.201  1.00 20.27           C  
ANISOU 6054  CB  ALA B 412     2230   2152   3321    220   -421    454       C  
ATOM   6055  C   ALA B 412     -12.143  37.732  -2.470  1.00 22.01           C  
ANISOU 6055  C   ALA B 412     2427   2359   3576    261   -477    527       C  
ATOM   6056  O   ALA B 412     -13.174  37.053  -2.502  1.00 22.04           O  
ANISOU 6056  O   ALA B 412     2381   2372   3622    266   -515    556       O  
ATOM   6057  N   MET B 413     -12.136  39.054  -2.313  1.00 20.13           N  
ANISOU 6057  N   MET B 413     2216   2103   3330    284   -438    537       N  
ATOM   6058  CA  MET B 413     -13.376  39.820  -2.182  1.00 21.21           C  
ANISOU 6058  CA  MET B 413     2325   2228   3504    323   -434    584       C  
ATOM   6059  CB  MET B 413     -13.071  41.250  -1.743  1.00 25.80           C  
ANISOU 6059  CB  MET B 413     2948   2788   4068    346   -377    584       C  
ATOM   6060  CG  MET B 413     -12.705  41.350  -0.271  1.00 28.27           C  
ANISOU 6060  CG  MET B 413     3256   3096   4388    351   -317    569       C  
ATOM   6061  SD  MET B 413     -12.224  43.004   0.308  1.00 35.24           S  
ANISOU 6061  SD  MET B 413     4198   3949   5243    373   -250    565       S  
ATOM   6062  CE  MET B 413     -10.662  43.264  -0.522  1.00 43.93           C  
ANISOU 6062  CE  MET B 413     5365   5048   6279    334   -252    519       C  
ATOM   6063  C   MET B 413     -14.147  39.798  -3.491  1.00 27.78           C  
ANISOU 6063  C   MET B 413     3153   3060   4342    327   -497    614       C  
ATOM   6064  O   MET B 413     -15.361  39.585  -3.498  1.00 28.51           O  
ANISOU 6064  O   MET B 413     3194   3156   4482    345   -526    656       O  
ATOM   6065  N   LYS B 414     -13.435  39.991  -4.596  1.00 27.76           N  
ANISOU 6065  N   LYS B 414     3204   3052   4292    308   -518    594       N  
ATOM   6066  CA  LYS B 414     -14.047  40.044  -5.920  1.00 30.89           C  
ANISOU 6066  CA  LYS B 414     3609   3443   4683    310   -578    618       C  
ATOM   6067  CB  LYS B 414     -12.998  40.462  -6.954  1.00 33.94           C  
ANISOU 6067  CB  LYS B 414     4069   3819   5007    293   -579    589       C  
ATOM   6068  CG  LYS B 414     -13.534  40.722  -8.352  1.00 36.41           C  
ANISOU 6068  CG  LYS B 414     4406   4121   5306    297   -636    612       C  
ATOM   6069  CD  LYS B 414     -12.445  41.354  -9.215  1.00 47.36           C  
ANISOU 6069  CD  LYS B 414     5871   5494   6631    285   -620    584       C  
ATOM   6070  CE  LYS B 414     -12.957  41.780 -10.581  1.00 55.32           C  
ANISOU 6070  CE  LYS B 414     6912   6486   7620    293   -670    608       C  
ATOM   6071  NZ  LYS B 414     -11.937  42.589 -11.312  1.00 55.82           N  
ANISOU 6071  NZ  LYS B 414     7051   6532   7625    287   -644    583       N  
ATOM   6072  C   LYS B 414     -14.683  38.715  -6.319  1.00 37.97           C  
ANISOU 6072  C   LYS B 414     4464   4356   5606    293   -644    631       C  
ATOM   6073  O   LYS B 414     -15.738  38.680  -6.961  1.00 35.04           O  
ANISOU 6073  O   LYS B 414     4070   3984   5258    302   -692    667       O  
ATOM   6074  N   SER B 415     -14.044  37.621  -5.923  1.00 26.43           N  
ANISOU 6074  N   SER B 415     2996   2910   4138    265   -643    598       N  
ATOM   6075  CA  SER B 415     -14.495  36.295  -6.305  1.00 25.29           C  
ANISOU 6075  CA  SER B 415     2820   2778   4010    243   -705    604       C  
ATOM   6076  CB  SER B 415     -13.300  35.342  -6.445  1.00 32.10           C  
ANISOU 6076  CB  SER B 415     3716   3650   4831    208   -704    556       C  
ATOM   6077  OG  SER B 415     -12.642  35.156  -5.202  1.00 22.76           O  
ANISOU 6077  OG  SER B 415     2518   2476   3653    204   -648    529       O  
ATOM   6078  C   SER B 415     -15.498  35.739  -5.302  1.00 31.12           C  
ANISOU 6078  C   SER B 415     3491   3536   4797    247   -691    620       C  
ATOM   6079  O   SER B 415     -16.042  34.649  -5.504  1.00 31.58           O  
ANISOU 6079  O   SER B 415     3525   3610   4862    222   -727    618       O  
ATOM   6080  N   GLY B 416     -15.734  36.482  -4.223  1.00 28.66           N  
ANISOU 6080  N   GLY B 416     3159   3222   4509    273   -632    630       N  
ATOM   6081  CA  GLY B 416     -16.754  36.122  -3.252  1.00 35.59           C  
ANISOU 6081  CA  GLY B 416     3982   4118   5423    278   -606    643       C  
ATOM   6082  C   GLY B 416     -16.409  35.078  -2.200  1.00 34.89           C  
ANISOU 6082  C   GLY B 416     3867   4043   5346    260   -584    619       C  
ATOM   6083  O   GLY B 416     -17.309  34.503  -1.581  1.00 34.63           O  
ANISOU 6083  O   GLY B 416     3792   4025   5340    256   -575    630       O  
ATOM   6084  N   VAL B 417     -15.122  34.826  -1.972  1.00 25.01           N  
ANISOU 6084  N   VAL B 417     2642   2787   4076    250   -575    588       N  
ATOM   6085  CA  VAL B 417     -14.750  33.847  -0.961  1.00 20.04           C  
ANISOU 6085  CA  VAL B 417     1989   2170   3455    234   -554    564       C  
ATOM   6086  CB  VAL B 417     -13.593  32.918  -1.436  1.00 22.35           C  
ANISOU 6086  CB  VAL B 417     2305   2465   3721    204   -588    531       C  
ATOM   6087  CG1 VAL B 417     -14.035  32.079  -2.632  1.00 26.99           C  
ANISOU 6087  CG1 VAL B 417     2899   3062   4296    179   -653    534       C  
ATOM   6088  CG2 VAL B 417     -12.331  33.714  -1.775  1.00 25.70           C  
ANISOU 6088  CG2 VAL B 417     2794   2879   4093    200   -558    499       C  
ATOM   6089  C   VAL B 417     -14.365  34.526   0.349  1.00 24.88           C  
ANISOU 6089  C   VAL B 417     2601   2772   4079    257   -487    559       C  
ATOM   6090  O   VAL B 417     -14.250  33.867   1.381  1.00 27.74           O  
ANISOU 6090  O   VAL B 417     2942   3144   4453    249   -461    544       O  
ATOM   6091  N   ALA B 418     -14.185  35.844   0.313  1.00 22.26           N  
ANISOU 6091  N   ALA B 418     2297   2419   3742    284   -459    572       N  
ATOM   6092  CA  ALA B 418     -13.898  36.591   1.538  1.00 26.01           C  
ANISOU 6092  CA  ALA B 418     2782   2881   4220    305   -391    567       C  
ATOM   6093  CB  ALA B 418     -13.439  38.017   1.214  1.00 24.77           C  
ANISOU 6093  CB  ALA B 418     2682   2704   4028    320   -360    563       C  
ATOM   6094  C   ALA B 418     -15.133  36.626   2.428  1.00 26.17           C  
ANISOU 6094  C   ALA B 418     2762   2909   4272    325   -360    592       C  
ATOM   6095  O   ALA B 418     -16.253  36.712   1.928  1.00 29.47           O  
ANISOU 6095  O   ALA B 418     3157   3336   4703    331   -379    619       O  
ATOM   6096  N   THR B 419     -14.938  36.563   3.740  1.00 25.26           N  
ANISOU 6096  N   THR B 419     2641   2790   4165    332   -310    581       N  
ATOM   6097  CA  THR B 419     -16.065  36.762   4.649  1.00 31.94           C  
ANISOU 6097  CA  THR B 419     3461   3640   5034    354   -270    605       C  
ATOM   6098  CB  THR B 419     -16.194  35.610   5.667  1.00 32.60           C  
ANISOU 6098  CB  THR B 419     3514   3740   5132    337   -256    591       C  
ATOM   6099  OG1 THR B 419     -15.121  35.666   6.613  1.00 34.93           O  
ANISOU 6099  OG1 THR B 419     3836   4021   5416    338   -219    563       O  
ATOM   6100  CG2 THR B 419     -16.182  34.266   4.954  1.00 32.95           C  
ANISOU 6100  CG2 THR B 419     3535   3806   5176    300   -314    578       C  
ATOM   6101  C   THR B 419     -15.935  38.095   5.384  1.00 35.50           C  
ANISOU 6101  C   THR B 419     3945   4064   5478    389   -209    613       C  
ATOM   6102  O   THR B 419     -16.850  38.523   6.088  1.00 33.63           O  
ANISOU 6102  O   THR B 419     3695   3825   5257    413   -170    635       O  
ATOM   6103  N   ARG B 420     -14.809  38.765   5.189  1.00 27.51           N  
ANISOU 6103  N   ARG B 420     2980   3029   4443    391   -200    596       N  
ATOM   6104  CA  ARG B 420     -14.553  40.034   5.854  1.00 32.02           C  
ANISOU 6104  CA  ARG B 420     3595   3570   5001    419   -143    600       C  
ATOM   6105  CB  ARG B 420     -13.653  39.818   7.069  1.00 36.16           C  
ANISOU 6105  CB  ARG B 420     4141   4081   5516    412   -103    570       C  
ATOM   6106  CG  ARG B 420     -13.703  40.924   8.098  1.00 43.10           C  
ANISOU 6106  CG  ARG B 420     5061   4930   6385    442    -38    577       C  
ATOM   6107  CD  ARG B 420     -12.545  41.873   7.937  1.00 47.20           C  
ANISOU 6107  CD  ARG B 420     5652   5430   6850    427    -20    546       C  
ATOM   6108  NE  ARG B 420     -11.280  41.257   8.324  1.00 50.48           N  
ANISOU 6108  NE  ARG B 420     6091   5855   7235    385    -23    498       N  
ATOM   6109  CZ  ARG B 420     -10.804  41.248   9.565  1.00 51.44           C  
ANISOU 6109  CZ  ARG B 420     6236   5962   7346    382     16    479       C  
ATOM   6110  NH1 ARG B 420     -11.495  41.815  10.544  1.00 51.35           N  
ANISOU 6110  NH1 ARG B 420     6234   5926   7352    420     63    503       N  
ATOM   6111  NH2 ARG B 420      -9.636  40.670   9.825  1.00 50.98           N  
ANISOU 6111  NH2 ARG B 420     6195   5913   7261    343      7    437       N  
ATOM   6112  C   ARG B 420     -13.918  41.016   4.886  1.00 34.83           C  
ANISOU 6112  C   ARG B 420     4001   3909   5324    419   -153    595       C  
ATOM   6113  O   ARG B 420     -12.860  40.749   4.325  1.00 30.21           O  
ANISOU 6113  O   ARG B 420     3446   3332   4699    383   -174    557       O  
ATOM   6114  N   ALA B 421     -14.561  42.160   4.688  1.00 31.50           N  
ANISOU 6114  N   ALA B 421     3593   3468   4907    454   -133    627       N  
ATOM   6115  CA  ALA B 421     -14.019  43.170   3.786  1.00 41.15           C  
ANISOU 6115  CA  ALA B 421     4869   4676   6088    451   -137    619       C  
ATOM   6116  CB  ALA B 421     -15.095  44.171   3.402  1.00 42.17           C  
ANISOU 6116  CB  ALA B 421     4994   4792   6236    492   -130    664       C  
ATOM   6117  C   ALA B 421     -12.845  43.886   4.434  1.00 39.26           C  
ANISOU 6117  C   ALA B 421     4696   4418   5803    438    -91    581       C  
ATOM   6118  O   ALA B 421     -12.815  44.058   5.648  1.00 41.63           O  
ANISOU 6118  O   ALA B 421     5005   4704   6108    451    -44    579       O  
ATOM   6119  N   ILE B 422     -11.877  44.301   3.627  1.00 42.59           N  
ANISOU 6119  N   ILE B 422     5165   4838   6180    412   -103    554       N  
ATOM   6120  CA  ILE B 422     -10.790  45.134   4.125  1.00 48.49           C  
ANISOU 6120  CA  ILE B 422     5976   5563   6884    399    -62    524       C  
ATOM   6121  CB  ILE B 422      -9.422  44.504   3.854  1.00 56.34           C  
ANISOU 6121  CB  ILE B 422     6990   6573   7844    350    -80    478       C  
ATOM   6122  CG1 ILE B 422      -9.209  43.301   4.769  1.00 57.99           C  
ANISOU 6122  CG1 ILE B 422     7164   6798   8071    333    -81    459       C  
ATOM   6123  CD1 ILE B 422      -7.917  42.577   4.506  1.00 51.05           C  
ANISOU 6123  CD1 ILE B 422     6297   5936   7163    286    -99    417       C  
ATOM   6124  CG2 ILE B 422      -8.322  45.527   4.070  1.00 61.04           C  
ANISOU 6124  CG2 ILE B 422     7652   7145   8395    335    -46    453       C  
ATOM   6125  C   ILE B 422     -10.840  46.514   3.483  1.00 60.73           C  
ANISOU 6125  C   ILE B 422     7575   7090   8410    418    -49    539       C  
ATOM   6126  O   ILE B 422     -11.120  46.636   2.291  1.00 64.41           O  
ANISOU 6126  O   ILE B 422     8037   7563   8873    419    -84    552       O  
TER    6128      ILE B 422                                                      
HETATM 6127 MG    MG C   1     -10.891  21.158  31.875  1.00 27.13          Mg  
HETATM 6128 MG    MG C   2       8.491  21.594   0.178  1.00 22.29          Mg  
TER    6131       MG C   2                                                      
HETATM 6129  O   HOH S   1     -10.634  23.156  31.108  1.00 28.26           O  
HETATM 6130  O   HOH S   2     -12.790  21.477  32.860  1.00 27.85           O  
HETATM 6131  O   HOH S   3       9.934  20.586  -0.935  1.00 21.42           O  
HETATM 6132  O   HOH S   4       9.668  21.822   1.904  1.00 22.45           O  
HETATM 6133  O   HOH S   5       9.482  23.394  -0.620  1.00 25.25           O  
HETATM 6134  O   HOH S   6      -8.731  26.702  -0.619  1.00 20.10           O  
HETATM 6135  O   HOH S   7      -8.026  32.630  23.261  1.00 20.43           O  
HETATM 6136  O   HOH S   8      13.303  43.245  -5.179  1.00 20.08           O  
HETATM 6137  O   HOH S   9      11.452  46.494  -8.286  1.00 18.24           O  
HETATM 6138  O   HOH S  10      13.062  18.149  21.521  1.00 21.95           O  
HETATM 6139  O   HOH S  11      13.570  21.740  13.738  1.00 16.89           O  
HETATM 6140  O   HOH S  12       3.666  51.690 -11.467  1.00 21.80           O  
HETATM 6141  O   HOH S  13      -7.749  35.665  15.380  1.00 19.03           O  
HETATM 6142  O   HOH S  14      -4.345  28.773  19.001  1.00 18.96           O  
HETATM 6143  O   HOH S  15       5.836  25.719  14.181  1.00 18.42           O  
HETATM 6144  O   HOH S  16      -2.416  41.617  -9.025  1.00 20.46           O  
HETATM 6145  O   HOH S  17       9.128  52.708  -9.616  1.00 20.56           O  
HETATM 6146  O   HOH S  18      -5.839   6.642  12.384  1.00 21.30           O  
HETATM 6147  O   HOH S  19       4.911  36.743  -0.140  1.00 18.43           O  
HETATM 6148  O   HOH S  20      -2.100   5.609   6.611  1.00 22.59           O  
HETATM 6149  O   HOH S  21       4.751  30.124  -2.803  1.00 21.98           O  
HETATM 6150  O   HOH S  22     -18.050  25.743  19.092  1.00 18.44           O  
HETATM 6151  O   HOH S  23       7.244  21.776  16.503  1.00 17.23           O  
HETATM 6152  O   HOH S  24      10.512   9.746   9.891  1.00 20.33           O  
HETATM 6153  O   HOH S  25      28.636  26.570  13.384  1.00 24.48           O  
HETATM 6154  O   HOH S  26      18.586  32.080  -9.137  1.00 25.85           O  
HETATM 6155  O   HOH S  27      -7.163  37.299 -10.357  1.00 26.66           O  
HETATM 6156  O   HOH S  28       9.908  52.325  -7.038  1.00 23.50           O  
HETATM 6157  O   HOH S  29     -17.007  24.558  16.607  1.00 26.02           O  
HETATM 6158  O   HOH S  30      12.637  22.792  22.616  1.00 20.74           O  
HETATM 6159  O   HOH S  31       3.048  20.491  39.006  1.00 27.80           O  
HETATM 6160  O   HOH S  32      10.408  24.334  22.163  1.00 28.63           O  
HETATM 6161  O   HOH S  33      11.656  27.818  -3.251  1.00 23.95           O  
HETATM 6162  O   HOH S  34      -1.919   5.859   9.418  1.00 19.57           O  
HETATM 6163  O   HOH S  35      15.885  50.080 -10.173  1.00 22.71           O  
HETATM 6164  O   HOH S  36      -8.658   4.559   4.916  1.00 22.56           O  
HETATM 6165  O   HOH S  37      13.157  25.615  20.158  1.00 23.92           O  
HETATM 6166  O   HOH S  38       8.871  10.965  -2.587  1.00 24.44           O  
HETATM 6167  O   HOH S  39     -19.379  27.959  17.973  1.00 22.86           O  
HETATM 6168  O   HOH S  40      10.894  56.569 -11.831  1.00 24.23           O  
HETATM 6169  O   HOH S  41      -5.463  26.653  -2.869  1.00 26.17           O  
HETATM 6170  O   HOH S  42       0.238   7.320  28.773  1.00 23.83           O  
HETATM 6171  O   HOH S  43       5.136  17.990  -2.151  1.00 20.98           O  
HETATM 6172  O   HOH S  44      11.360  14.649  -2.061  1.00 24.36           O  
HETATM 6173  O   HOH S  45      12.858  20.019  23.608  1.00 24.97           O  
HETATM 6174  O   HOH S  46      -9.471  32.001   7.776  1.00 24.63           O  
HETATM 6175  O   HOH S  47     -10.957  25.457   1.183  1.00 27.64           O  
HETATM 6176  O   HOH S  48       4.978  33.329  27.494  1.00 32.35           O  
HETATM 6177  O   HOH S  49     -13.337  16.515  30.573  1.00 25.49           O  
HETATM 6178  O   HOH S  50       4.935  47.980 -12.342  1.00 27.61           O  
HETATM 6179  O   HOH S  51     -18.723  21.163  30.934  1.00 30.45           O  
HETATM 6180  O   HOH S  52      15.363  38.590  -9.007  1.00 25.58           O  
HETATM 6181  O   HOH S  53      -9.895   2.384  53.429  1.00 32.28           O  
HETATM 6182  O   HOH S  54       7.951  12.089  25.277  1.00 32.19           O  
HETATM 6183  O   HOH S  55      10.471  34.797  15.805  1.00 29.98           O  
HETATM 6184  O   HOH S  56      -9.460  16.872  37.538  1.00 28.41           O  
HETATM 6185  O   HOH S  57     -16.117  28.951  14.676  1.00 25.61           O  
HETATM 6186  O   HOH S  58     -17.907  27.038  15.625  1.00 26.15           O  
HETATM 6187  O   HOH S  59       7.211  37.082   0.802  1.00 26.39           O  
HETATM 6188  O   HOH S  60     -11.233  37.596  -8.249  1.00 29.24           O  
HETATM 6189  O   HOH S  61      -4.801  26.874 -24.594  1.00 48.82           O  
HETATM 6190  O   HOH S  62      21.642   9.857  12.598  1.00 30.27           O  
HETATM 6191  O   HOH S  63       6.282  13.529  -5.673  1.00 28.28           O  
HETATM 6192  O   HOH S  64      -6.765  43.457  18.685  1.00 31.64           O  
HETATM 6193  O   HOH S  65      11.717   8.185  -1.645  1.00 27.99           O  
HETATM 6194  O   HOH S  66      25.777  26.735  13.378  1.00 23.50           O  
HETATM 6195  O   HOH S  67      -1.755   9.078  31.547  1.00 28.47           O  
HETATM 6196  O   HOH S  68     -15.052  20.326  32.083  1.00 33.05           O  
HETATM 6197  O   HOH S  69      -0.030   6.900  17.029  1.00 29.37           O  
HETATM 6198  O   HOH S  70      -9.921  25.832  49.017  1.00 40.71           O  
HETATM 6199  O   HOH S  71     -20.768  18.171  28.762  1.00 29.11           O  
HETATM 6200  O   HOH S  72      12.457  29.513   0.310  1.00 33.53           O  
HETATM 6201  O   HOH S  73      30.699  23.243  10.528  1.00 28.99           O  
HETATM 6202  O   HOH S  74      17.881  39.062  -9.869  1.00 25.53           O  
HETATM 6203  O   HOH S  75      -5.485  27.490 -16.732  1.00 35.22           O  
HETATM 6204  O   HOH S  76     -24.117  20.615  27.216  1.00 31.47           O  
HETATM 6205  O   HOH S  77      -1.255  20.488  -9.523  1.00 31.52           O  
HETATM 6206  O   HOH S  78     -13.818  30.450  -5.852  1.00 31.55           O  
HETATM 6207  O   HOH S  79     -20.289  38.290  24.817  1.00 34.62           O  
HETATM 6208  O   HOH S  80      13.296  45.983   1.720  1.00 33.28           O  
HETATM 6209  O   HOH S  81      15.143  53.035   0.121  1.00 33.23           O  
HETATM 6210  O   HOH S  82     -21.799  36.176  20.794  1.00 30.69           O  
HETATM 6211  O   HOH S  83       5.413  23.835  52.548  1.00 39.74           O  
HETATM 6212  O   HOH S  84       7.879  40.748   4.595  1.00 30.35           O  
HETATM 6213  O   HOH S  85       6.705  24.863  -5.725  1.00 23.94           O  
HETATM 6214  O   HOH S  86      -6.419  41.659  -7.101  1.00 30.12           O  
HETATM 6215  O   HOH S  87      16.952  30.497  -0.730  1.00 35.45           O  
HETATM 6216  O   HOH S  88      16.238  28.997   2.928  1.00 33.78           O  
HETATM 6217  O   HOH S  89       7.352  17.962  -3.801  1.00 29.11           O  
HETATM 6218  O   HOH S  90      -3.063  24.584  51.000  1.00 36.17           O  
HETATM 6219  O   HOH S  91      13.996  36.416  -6.258  1.00 26.76           O  
HETATM 6220  O   HOH S  92      29.446  23.931  12.801  1.00 28.86           O  
HETATM 6221  O   HOH S  93     -10.545  10.428  -1.375  1.00 37.71           O  
HETATM 6222  O   HOH S  94      -4.532   6.151  -0.345  1.00 28.44           O  
HETATM 6223  O   HOH S  95       6.959  43.668   4.323  1.00 35.09           O  
HETATM 6224  O   HOH S  96       2.837  26.462  49.465  1.00 32.45           O  
HETATM 6225  O   HOH S  97      -3.395  18.117  37.250  1.00 30.36           O  
HETATM 6226  O   HOH S  98       3.419   7.577   8.106  1.00 26.78           O  
HETATM 6227  O   HOH S  99      26.864  28.651  11.408  1.00 37.32           O  
HETATM 6228  O   HOH S 100       5.478  30.448  13.083  1.00 29.13           O  
HETATM 6229  O   HOH S 101     -18.689  39.344  22.490  1.00 32.07           O  
HETATM 6230  O   HOH S 102      -1.442   4.702  13.099  1.00 29.27           O  
HETATM 6231  O   HOH S 103     -16.422  14.396  12.887  1.00 28.37           O  
HETATM 6232  O   HOH S 104     -14.668  12.680  10.463  1.00 34.28           O  
HETATM 6233  O   HOH S 105       6.697   9.745  18.387  1.00 38.07           O  
HETATM 6234  O   HOH S 106      16.891  18.261  -0.664  1.00 35.43           O  
HETATM 6235  O   HOH S 107      -8.503  22.881  39.177  1.00 46.47           O  
HETATM 6236  O   HOH S 108      -7.568   4.718   1.078  1.00 36.48           O  
HETATM 6237  O   HOH S 109      19.287   9.438   6.263  1.00 31.79           O  
HETATM 6238  O   HOH S 110       1.389  20.423 -10.564  1.00 41.26           O  
HETATM 6239  O   HOH S 111       6.337   7.421   4.949  1.00 27.43           O  
HETATM 6240  O   HOH S 112      23.550  10.933  10.896  1.00 34.53           O  
HETATM 6241  O   HOH S 113      12.505   8.540  11.467  1.00 26.26           O  
HETATM 6242  O   HOH S 114     -12.136  43.514  -4.555  1.00 33.96           O  
HETATM 6243  O   HOH S 115       4.295   9.000   6.124  1.00 30.89           O  
HETATM 6244  O   HOH S 116      12.133  47.556  -0.231  1.00 34.99           O  
HETATM 6245  O   HOH S 117     -18.926  14.673  31.474  1.00 37.31           O  
HETATM 6246  O   HOH S 118      17.564  35.373  -3.924  1.00 32.17           O  
HETATM 6247  O   HOH S 119     -17.482  27.318  33.789  1.00 39.54           O  
HETATM 6248  O   HOH S 120      23.366  13.794  14.026  1.00 30.77           O  
HETATM 6249  O   HOH S 121      -9.383  19.557  40.920  1.00 52.77           O  
HETATM 6250  O   HOH S 122      -0.817  41.313  22.440  1.00 32.48           O  
HETATM 6251  O   HOH S 123     -12.843   8.453   3.552  1.00 35.22           O  
HETATM 6252  O   HOH S 124      23.596  36.302   5.252  1.00 27.39           O  
HETATM 6253  O   HOH S 125       9.366  18.144  -1.888  1.00 28.24           O  
HETATM 6254  O   HOH S 126      -1.321  27.086  22.163  1.00 25.93           O  
HETATM 6255  O   HOH S 127      14.589  29.325  13.063  1.00 30.12           O  
HETATM 6256  O   HOH S 128       8.001   9.285  11.718  1.00 34.14           O  
HETATM 6257  O   HOH S 129      22.957  14.667   8.846  1.00 29.75           O  
HETATM 6258  O   HOH S 130      -4.633  25.093  -4.614  1.00 28.20           O  
HETATM 6259  O   HOH S 131     -17.492  12.540  14.822  1.00 30.98           O  
HETATM 6260  O   HOH S 132      -1.352   6.047  -0.452  1.00 34.36           O  
HETATM 6261  O   HOH S 133     -14.888  17.551  32.671  1.00 27.64           O  
HETATM 6262  O   HOH S 134      13.816  48.507 -12.034  1.00 34.10           O  
HETATM 6263  O   HOH S 135     -23.272  11.223  58.184  1.00 45.17           O  
HETATM 6264  O   HOH S 136      16.331  36.593  14.314  1.00 30.69           O  
HETATM 6265  O   HOH S 137      14.026  51.357 -12.742  1.00 43.26           O  
HETATM 6266  O   HOH S 138       1.773   8.088   0.278  1.00 44.11           O  
HETATM 6267  O   HOH S 139       6.179  25.263  40.529  1.00 42.78           O  
HETATM 6268  O   HOH S 140       2.682  29.696  25.959  1.00 32.95           O  
HETATM 6269  O   HOH S 141       7.276  11.115  45.227  1.00 36.78           O  
HETATM 6270  O   HOH S 142       2.423  27.205  25.472  1.00 34.69           O  
HETATM 6271  O   HOH S 143       5.296   5.732  42.196  1.00 39.82           O  
HETATM 6272  O   HOH S 144      13.094  23.526  25.152  1.00 41.78           O  
HETATM 6273  O   HOH S 145       7.909   6.419   6.759  1.00 39.63           O  
HETATM 6274  O   HOH S 146      18.582  31.565   2.854  1.00 32.20           O  
HETATM 6275  O   HOH S 147     -22.017  27.402  18.325  1.00 27.22           O  
HETATM 6276  O   HOH S 148      18.370  43.395 -15.374  1.00 33.66           O  
HETATM 6277  O   HOH S 149      -8.872  41.563  -8.036  1.00 36.34           O  
HETATM 6278  O   HOH S 150      -9.656  40.823  18.030  1.00 28.18           O  
HETATM 6279  O   HOH S 151      23.380  31.305  14.055  1.00 34.66           O  
HETATM 6280  O   HOH S 152      20.246  33.636 -13.266  1.00 34.83           O  
HETATM 6281  O   HOH S 153     -23.375  17.602  27.676  1.00 44.13           O  
HETATM 6282  O   HOH S 154      -6.251   1.676  42.100  1.00 38.30           O  
HETATM 6283  O   HOH S 155      24.033  13.456  11.177  1.00 34.87           O  
HETATM 6284  O   HOH S 156      20.551  38.577   4.431  1.00 40.95           O  
HETATM 6285  O   HOH S 157      16.377  16.960  23.889  1.00 51.67           O  
HETATM 6286  O   HOH S 158       0.560   6.507  25.808  1.00 39.26           O  
HETATM 6287  O   HOH S 159     -17.512  18.425  16.484  1.00 30.50           O  
HETATM 6288  O   HOH S 160      19.213  19.104  21.282  1.00 30.75           O  
HETATM 6289  O   HOH S 161       2.299  17.815 -11.983  1.00 31.54           O  
HETATM 6290  O   HOH S 162      -5.280   1.929  27.941  1.00 34.65           O  
HETATM 6291  O   HOH S 163     -13.355  27.544  10.401  1.00 32.61           O  
HETATM 6292  O   HOH S 164       1.664   6.876  14.503  1.00 43.19           O  
HETATM 6293  O   HOH S 165      -4.192   8.293  32.363  1.00 36.86           O  
HETATM 6294  O   HOH S 166      23.104  29.826  15.942  1.00 48.51           O  
HETATM 6295  O   HOH S 167       4.160   7.670  14.532  1.00 35.28           O  
HETATM 6296  O   HOH S 168       0.478   6.038  12.231  1.00 33.16           O  
HETATM 6297  O   HOH S 169     -18.546  20.291  15.698  1.00 33.64           O  
HETATM 6298  O   HOH S 170       3.335  37.731  31.796  1.00 33.94           O  
HETATM 6299  O   HOH S 171     -10.626  24.909  53.358  1.00 34.24           O  
HETATM 6300  O   HOH S 172      -9.239  39.108  -9.448  1.00 32.15           O  
HETATM 6301  O   HOH S 173      27.369  19.505  14.653  1.00 42.52           O  
HETATM 6302  O   HOH S 174     -23.143  30.893  25.004  1.00 32.80           O  
HETATM 6303  O   HOH S 175      30.127  28.299  11.466  1.00 38.92           O  
HETATM 6304  O   HOH S 176      -3.991  26.579  52.667  1.00 34.40           O  
HETATM 6305  O   HOH S 177      11.508   2.547  28.018  1.00 47.26           O  
HETATM 6306  O   HOH S 178       9.045   2.679  26.896  1.00 41.04           O  
HETATM 6307  O   HOH S 179      16.199  36.900  -7.293  1.00 30.41           O  
HETATM 6308  O   HOH S 180      12.891   7.295   7.217  1.00 36.13           O  
HETATM 6309  O   HOH S 181      15.165  35.078  16.429  1.00 44.13           O  
HETATM 6310  O   HOH S 182      15.540  44.796   1.546  1.00 34.98           O  
HETATM 6311  O   HOH S 183      13.990  15.308  25.208  1.00 49.90           O  
HETATM 6312  O   HOH S 184     -15.200  36.732  11.338  1.00 48.30           O  
HETATM 6313  O   HOH S 185     -23.735  16.375  25.028  1.00 47.78           O  
HETATM 6314  O   HOH S 186      22.604  11.683   8.112  1.00 41.56           O  
HETATM 6315  O   HOH S 187      10.440  14.149  -4.528  1.00 43.12           O  
HETATM 6316  O   HOH S 188      17.701  28.650  21.466  1.00 34.30           O  
HETATM 6317  O   HOH S 189     -19.601  36.328  26.800  1.00 27.76           O  
HETATM 6318  O   HOH S 190     -11.009   7.625  35.029  1.00 35.27           O  
HETATM 6319  O   HOH S 191       0.865  10.074   1.075  1.00 41.48           O  
HETATM 6320  O   HOH S 192       7.420  38.959  11.828  1.00 37.87           O  
HETATM 6321  O   HOH S 193     -18.704  15.926  15.519  1.00 33.33           O  
HETATM 6322  O   HOH S 194       7.876   4.750  41.515  1.00 46.32           O  
HETATM 6323  O   HOH S 195      24.449  16.947  16.358  1.00 40.67           O  
HETATM 6324  O   HOH S 196      18.089  25.476  -9.484  1.00 38.53           O  
HETATM 6325  O   HOH S 197       8.244  11.815  -4.778  1.00 37.10           O  
HETATM 6326  O   HOH S 198      -0.145   1.332  45.466  1.00 43.99           O  
HETATM 6327  O   HOH S 199      17.960  48.090   3.936  1.00 38.62           O  
HETATM 6328  O   HOH S 200      17.149  33.534  -0.480  1.00 44.40           O  
HETATM 6329  O   HOH S 201      15.550  54.579  -2.655  1.00 43.64           O  
HETATM 6330  O   HOH S 202      -8.855  38.057  11.331  1.00 49.64           O  
HETATM 6331  O   HOH S 203      -2.555  24.404  59.393  1.00 49.35           O  
HETATM 6332  O   HOH S 204       7.189  27.499  12.804  1.00 30.28           O  
HETATM 6333  O   HOH S 205       7.562  15.933  -5.324  1.00 35.23           O  
HETATM 6334  O   HOH S 206      -9.766  40.103 -12.108  1.00 49.41           O  
HETATM 6335  O   HOH S 207      -9.450  22.716  57.207  1.00 39.77           O  
HETATM 6336  O   HOH S 208      10.697  26.789  24.908  1.00 38.62           O  
HETATM 6337  O   HOH S 209      19.147  29.396   1.394  1.00 38.81           O  
HETATM 6338  O   HOH S 210       4.119  39.845 -20.737  1.00 43.13           O  
HETATM 6339  O   HOH S 211       3.455  37.531  29.150  1.00 38.65           O  
HETATM 6340  O   HOH S 212      24.013  35.728   9.563  1.00 40.96           O  
HETATM 6341  O   HOH S 213       6.180  13.017  -8.652  1.00 38.73           O  
HETATM 6342  O   HOH S 214      20.858  36.997  12.736  1.00 43.15           O  
HETATM 6343  O   HOH S 215     -18.666  34.235  32.142  1.00 48.99           O  
HETATM 6344  O   HOH S 216      13.115  45.083 -23.742  1.00 37.63           O  
HETATM 6345  O   HOH S 217     -15.447  42.050  23.024  1.00 36.58           O  
HETATM 6346  O   HOH S 218     -19.631  19.097  20.125  1.00 41.89           O  
HETATM 6347  O   HOH S 219      -9.476  14.113  -4.267  1.00 33.86           O  
HETATM 6348  O   HOH S 220      23.940  33.772  14.373  1.00 40.43           O  
HETATM 6349  O   HOH S 221      -1.574   4.791  15.970  1.00 27.42           O  
HETATM 6350  O   HOH S 222      -0.868  27.924  24.830  1.00 30.71           O  
HETATM 6351  O   HOH S 223      22.727  17.526   4.009  1.00 48.63           O  
HETATM 6352  O   HOH S 224       7.616  19.130 -10.173  1.00 42.99           O  
HETATM 6353  O   HOH S 225      19.837  21.430  22.761  1.00 37.88           O  
HETATM 6354  O   HOH S 226      -8.825  -2.747  47.758  1.00 45.22           O  
HETATM 6355  O   HOH S 227      13.235   6.469   9.966  1.00 47.41           O  
HETATM 6356  O   HOH S 228     -13.458  37.226  -9.810  1.00 36.16           O  
HETATM 6357  O   HOH S 229      21.460  35.281 -15.207  1.00 43.17           O  
HETATM 6358  O   HOH S 230      -7.056  33.746 -16.992  1.00 45.80           O  
HETATM 6359  O   HOH S 231      17.783  35.030  17.913  1.00 52.38           O  
HETATM 6360  O   HOH S 232     -15.634   8.732  37.011  1.00 35.30           O  
HETATM 6361  O   HOH S 233      13.602  14.378 -19.798  1.00 57.61           O  
HETATM 6362  O   HOH S 234       3.712   1.283  32.593  1.00 40.84           O  
HETATM 6363  O   HOH S 235      -1.252  43.689  -9.813  1.00 35.80           O  
HETATM 6364  O   HOH S 236      -5.982  25.285 -17.929  1.00 47.93           O  
HETATM 6365  O   HOH S 237      -9.482   7.252  -1.129  1.00 48.81           O  
HETATM 6366  O   HOH S 238     -11.212  20.937  -4.854  1.00 29.88           O  
HETATM 6367  O   HOH S 239     -17.201  18.237  19.206  1.00 38.91           O  
HETATM 6368  O   HOH S 240      -3.020  18.866 -10.850  1.00 36.35           O  
HETATM 6369  O   HOH S 241      -4.332  -3.178  22.824  1.00 43.88           O  
HETATM 6370  O   HOH S 242       9.593   8.822  42.463  1.00 36.65           O  
HETATM 6371  O   HOH S 243       8.055  12.053  47.599  1.00 43.52           O  
HETATM 6372  O   HOH S 244      18.908  50.227  -5.894  1.00 38.06           O  
HETATM 6373  O   HOH S 245     -12.769  22.973  -4.304  1.00 44.23           O  
HETATM 6374  O   HOH S 246     -10.649   3.700  -0.346  1.00 46.29           O  
HETATM 6375  O   HOH S 247      -5.274  -4.117  25.087  1.00 41.88           O  
HETATM 6376  O   HOH S 248      -1.379   3.061   5.609  1.00 38.45           O  
HETATM 6377  O   HOH S 249      -5.475  36.823  14.751  1.00 24.18           O  
HETATM 6378  O   HOH S 250      -0.561  -0.663  58.372  1.00 54.15           O  
HETATM 6379  O   HOH S 251      25.101  34.694   3.341  1.00 53.31           O  
HETATM 6380  O   HOH S 252      -3.513  36.509  16.797  1.00 19.29           O  
HETATM 6381  O   HOH S 253      30.437  22.501  14.684  1.00 36.43           O  
HETATM 6382  O   HOH S 254       2.075  29.734 -26.214  1.00 41.80           O  
HETATM 6383  O   HOH S 255      -4.104  36.990 -16.519  1.00 43.01           O  
HETATM 6384  O   HOH S 256       1.762  15.745 -13.483  1.00 50.95           O  
HETATM 6385  O   HOH S 257      -8.087   9.287  10.225  1.00 27.04           O  
HETATM 6386  O   HOH S 258      24.645  27.401  15.763  1.00 30.39           O  
HETATM 6387  O   HOH S 259       8.843   7.005   9.485  1.00 43.24           O  
HETATM 6388  O   HOH S 260      20.554  29.666  19.981  1.00 45.85           O  
HETATM 6389  O   HOH S 261      19.947  44.518 -12.605  1.00 35.83           O  
HETATM 6390  O   HOH S 262      -0.251  44.276   3.742  1.00 48.30           O  
HETATM 6391  O   HOH S 263      -5.161  41.191  -9.597  1.00 33.47           O  
HETATM 6392  O   HOH S 264     -14.993  23.958  45.321  1.00 45.30           O  
HETATM 6393  O   HOH S 265      -1.519  42.895   5.248  1.00 56.18           O  
HETATM 6394  O   HOH S 266      14.373   8.548   0.447  1.00 42.46           O  
HETATM 6395  O   HOH S 267      -3.288  42.080   4.443  1.00 49.10           O  
HETATM 6396  O   HOH S 268     -12.125   6.837  -0.502  1.00 46.94           O  
HETATM 6397  O   HOH S 269      -2.218  36.242  20.496  1.00 24.69           O  
HETATM 6398  O   HOH S 270      -9.823  21.693  33.959  1.00 34.81           O  
HETATM 6399  O   HOH S 271      21.635  38.945  -8.026  1.00 46.62           O  
HETATM 6400  O   HOH S 272     -12.121  19.349  35.298  1.00 39.44           O  
HET