CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***    ***

elNémo ID: 21052114161798981

Job options:

ID        	=	 21052114161798981
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


REMARK Date 2021-05-20 Time 10:53:13 CEST +0200 (1621500793.59 s)               
REMARK PHENIX refinement                                                        
REMARK                                                                          
REMARK ****************** INPUT FILES AND LABELS ****************************** 
REMARK Reflections:                                                             
REMARK   file name      : /gpfs/cfel/cxi/scratch/user/lieskej/HP/Beamtimes/HP6_2
REMARK   labels         : ['I-obs,SIGI-obs']                                    
REMARK R-free flags:                                                            
REMARK   file name      : /gpfs/cfel/cxi/scratch/user/lieskej/HP/Beamtimes/HP6_2
REMARK   label          : R-free-flags                                          
REMARK   test_flag_value: 1                                                     
REMARK Model file name(s):                                                      
REMARK   /gpfs/cfel/cxi/scratch/user/lieskej/HP/Beamtimes/HP6_20210422/Refine/Mp
REMARK                                                                          
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS ******************* 
REMARK Start: r_work = 0.1630 r_free = 0.1995 bonds = 0.006 angles = 0.736      
REMARK Final: r_work = 0.1701 r_free = 0.2006 bonds = 0.002 angles = 0.526      
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 c: refinement of occupancies                                         
REMARK ------------------------------------------------------------------------ 
REMARK  stage       r-work r-free bonds angles b_min b_max b_ave n_water shift  
REMARK       0    : 0.4050 0.3911 0.006  0.74  26.7 171.3  57.1  55      0.000  
REMARK       1_bss: 0.1630 0.1995 0.006  0.74  26.7 171.3  57.1  55      0.000  
REMARK   1 ttarget: 0.1630 0.1995 0.006  0.74  26.7 171.3  57.1  55      0.000  
REMARK       1_nqh: 0.1630 0.1995 0.006  0.74  26.7 171.3  57.1  55      0.000  
REMARK    1_weight: 0.1630 0.1995 0.006  0.74  26.7 171.3  57.1  55      0.000  
REMARK    1_xyzrec: 0.1672 0.1998 0.002  0.54  26.7 171.3  57.1  55      0.019  
REMARK       1_adp: 0.1778 0.2042 0.002  0.54  29.5 134.3  55.8  55      0.019  
REMARK   1 regHadp: 0.1783 0.2045 0.002  0.54  29.5 134.3  55.8  55      0.019  
REMARK       1_occ: 0.1784 0.2048 0.002  0.54  29.5 134.3  55.8  55      0.019  
REMARK       2_bss: 0.1782 0.2047 0.002  0.54  29.0 133.8  55.3  55      0.019  
REMARK   2 ttarget: 0.1782 0.2047 0.002  0.54  29.0 133.8  55.3  55      0.019  
REMARK   2 datecdl: 0.1782 0.2047 0.002  0.54  29.0 133.8  55.3  55      0.019  
REMARK       2_nqh: 0.1783 0.2048 0.002  0.54  29.0 133.8  55.3  55      0.021  
REMARK    2_weight: 0.1783 0.2048 0.002  0.54  29.0 133.8  55.3  55      0.021  
REMARK    2_xyzrec: 0.1767 0.2058 0.002  0.52  29.0 133.8  55.3  55      0.027  
REMARK       2_adp: 0.1715 0.2014 0.002  0.52  28.3 137.6  55.7  55      0.027  
REMARK   2 regHadp: 0.1715 0.2014 0.002  0.52  28.3 137.6  55.7  55      0.027  
REMARK       2_occ: 0.1715 0.2012 0.002  0.52  28.3 137.6  55.7  55      0.027  
REMARK       3_bss: 0.1714 0.2011 0.002  0.52  28.3 137.5  55.6  55      0.027  
REMARK   3 ttarget: 0.1714 0.2011 0.002  0.52  28.3 137.5  55.6  55      0.027  
REMARK   3 datecdl: 0.1714 0.2011 0.002  0.53  28.3 137.5  55.6  55      0.027  
REMARK     3_setrh: 0.1714 0.2010 0.002  0.53  28.3 137.5  55.6  55      0.026  
REMARK       3_nqh: 0.1714 0.2010 0.002  0.53  28.3 137.5  55.6  55      0.026  
REMARK    3_weight: 0.1714 0.2010 0.002  0.53  28.3 137.5  55.6  55      0.026  
REMARK    3_xyzrec: 0.1714 0.2010 0.002  0.53  28.3 137.5  55.6  55      0.026  
REMARK       3_adp: 0.1701 0.2006 0.002  0.53  27.5 136.4  55.5  55      0.026  
REMARK   3 regHadp: 0.1701 0.2006 0.002  0.53  27.5 136.4  55.5  55      0.026  
REMARK       3_occ: 0.1701 0.2006 0.002  0.53  27.5 136.4  55.5  55      0.026  
REMARK         end: 0.1701 0.2006 0.002  0.53  27.5 136.4  55.5  55      0.026  
REMARK ------------------------------------------------------------------------ 
REMARK MODEL CONTENT.                                                           
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM                        
REMARK        H                     2356         2317.00                        
REMARK        C                     1514         1498.00                        
REMARK        S                       25           24.00                        
REMARK        O                      505          499.50                        
REMARK        N                      406          400.00                        
REMARK    TOTAL                     4806         4738.50                        
REMARK -----------------------------------------------------------------------  
REMARK r_free_flags.md5.hexdigest 8f7cd31c9e9c28300568370ccb11a894              
REMARK                                                                          
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.        
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13-2998_9999: ???)                         
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,       
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,   
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty, 
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini, 
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart    
REMARK   3                                                                      
REMARK   3  X-RAY DATA.                                                         
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ML                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.050                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.183                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.96                          
REMARK   3   NUMBER OF REFLECTIONS             : 17031                          
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 17031                      
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1731                          
REMARK   3   R VALUE            (WORKING SET) : 0.1701                          
REMARK   3   FREE R VALUE                     : 0.2006                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.00                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1703                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWOR 
REMARK   3     1 26.1856 -  4.6851    1.00     1317   146  0.1393 0.1696   0.96 
REMARK   3     2  4.6851 -  3.7221    1.00     1288   144  0.1238 0.1434   0.95 
REMARK   3     3  3.7221 -  3.2526    1.00     1293   143  0.1499 0.1913   0.94 
REMARK   3     4  3.2526 -  2.9557    1.00     1284   142  0.1842 0.2167   0.91 
REMARK   3     5  2.9557 -  2.7441    1.00     1274   142  0.2014 0.2211   0.89 
REMARK   3     6  2.7441 -  2.5824    1.00     1265   141  0.2088 0.2616   0.87 
REMARK   3     7  2.5824 -  2.4532    1.00     1279   142  0.2192 0.2539   0.87 
REMARK   3     8  2.4532 -  2.3465    1.00     1241   137  0.2339 0.2814   0.84 
REMARK   3     9  2.3465 -  2.2562    1.00     1274   143  0.2456 0.2801   0.83 
REMARK   3    10  2.2562 -  2.1784    1.00     1277   141  0.2503 0.3073   0.82 
REMARK   3    11  2.1784 -  2.1103    1.00     1277   142  0.2703 0.2839   0.75 
REMARK   3    12  2.1103 -  2.0500    1.00     1259   140  0.3006 0.3464   0.68 
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)     : 0.28             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.36            
REMARK   3                                                                      
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT                       
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3    BOND      :  0.002   0.029   2449                                 
REMARK   3    ANGLE     :  0.526   3.853   3329                                 
REMARK   3    CHIRALITY :  0.041   0.130    373                                 
REMARK   3    PLANARITY :  0.003   0.031    434                                 
REMARK   3    DIHEDRAL  : 12.394 179.737   1442                                 
REMARK   3    MIN NONBONDED DISTANCE : 2.205                                    
REMARK   3  REMARK   3                                                          
REMARK   3  MOLPROBITY STATISTICS.                                              
REMARK   3    ALL-ATOM CLASHSCORE : 1.05                                        
REMARK   3    RAMACHANDRAN PLOT:                                                
REMARK   3      OUTLIERS : 0.00  %                                              
REMARK   3      ALLOWED  : 2.67  %                                              
REMARK   3      FAVORED  : 97.33 %                                              
REMARK   3    ROTAMER OUTLIERS : 2.65 %                                         
REMARK   3    CBETA DEVIATIONS : 0                                              
REMARK   3    PEPTIDE PLANE:                                                    
REMARK   3      CIS-PROLINE     : 0.0                                           
REMARK   3      CIS-GENERAL     : 0.0                                           
REMARK   3      TWISTED PROLINE : 0.0                                           
REMARK   3      TWISTED GENERAL : 0.0                                           
REMARK   3                                                                      
REMARK   3  ATOMIC DISPLACEMENT PARAMETERS.                                     
REMARK   3   WILSON B : 42.93                                                   
REMARK   3   RMS(B_ISO_OR_EQUIVALENT_BONDED) : 3.21                             
REMARK   3   ATOMS          NUMBER OF ATOMS                                     
REMARK   3                    ISO.  ANISO.                                      
REMARK   3    ALL         :   4806    2387                                      
REMARK   3    ALL (NO H)  :   2450    2387                                      
REMARK   3    SOLVENT     :     55       0                                      
REMARK   3    NON-SOLVENT :   2395    2387                                      
REMARK   3    HYDROGENS   :   2356       0                                      
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  TLS DETAILS.                                                        
REMARK   3   NUMBER OF TLS GROUPS: 6                                            
REMARK   3   ORIGIN: CENTER OF MASS                                             
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 1 through 62 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  11.0211 -10.5315  16.3814              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4146 T22:   0.4025                                     
REMARK   3      T33:   0.3082 T12:  -0.1121                                     
REMARK   3      T13:   0.0061 T23:   0.0651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5977 L22:   2.4622                                     
REMARK   3      L33:   4.7757 L12:  -1.1850                                     
REMARK   3      L13:   4.1463 L23:  -0.3454                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4877 S12:  -0.5706 S13:  -0.3404                       
REMARK   3      S21:   0.2836 S22:  -0.1394 S23:  -0.1217                       
REMARK   3      S31:   0.9451 S32:  -0.2788 S33:  -0.3160                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 63 through 91 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0545 -20.3781  19.0101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9337 T22:   0.6237                                     
REMARK   3      T33:   0.5929 T12:  -0.1660                                     
REMARK   3      T13:  -0.2212 T23:   0.1710                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5209 L22:   6.6582                                     
REMARK   3      L33:   3.1294 L12:  -1.4184                                     
REMARK   3      L13:   1.3757 L23:  -0.4031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7674 S12:  -0.7737 S13:  -0.9911                       
REMARK   3      S21:   0.6690 S22:  -0.2327 S23:   0.3509                       
REMARK   3      S31:   1.4344 S32:  -0.4802 S33:  -0.4071                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 92 through 155 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9955  -6.0623   5.7452              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3720 T22:   0.3413                                     
REMARK   3      T33:   0.2304 T12:   0.0380                                     
REMARK   3      T13:  -0.0018 T23:   0.0485                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2973 L22:   7.6010                                     
REMARK   3      L33:   2.8866 L12:   0.4060                                     
REMARK   3      L13:   1.8056 L23:  -0.5952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2427 S12:   0.0311 S13:  -0.0167                       
REMARK   3      S21:  -0.0590 S22:  -0.2229 S23:  -0.0739                       
REMARK   3      S31:   0.4654 S32:   0.2614 S33:   0.0288                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 156 through 214 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3382   3.6441   7.6429              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2144 T22:   0.3612                                     
REMARK   3      T33:   0.3738 T12:  -0.0379                                     
REMARK   3      T13:   0.0310 T23:   0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3129 L22:   2.1941                                     
REMARK   3      L33:   6.6999 L12:  -0.1601                                     
REMARK   3      L13:   2.0255 L23:  -2.5421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1165 S12:   0.0665 S13:   0.2226                       
REMARK   3      S21:   0.1917 S22:  -0.2634 S23:  -0.2049                       
REMARK   3      S31:  -0.3301 S32:   0.3665 S33:   0.3916                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 215 through 274 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9482  18.9075 -11.3461              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5373 T22:   0.5536                                     
REMARK   3      T33:   0.5488 T12:  -0.1761                                     
REMARK   3      T13:  -0.0579 T23:   0.1992                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5015 L22:   0.4864                                     
REMARK   3      L33:   5.0410 L12:  -0.2068                                     
REMARK   3      L13:   0.6098 L23:   1.0247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2840 S12:   0.6247 S13:   0.5950                       
REMARK   3      S21:  -0.1104 S22:   0.1054 S23:  -0.0564                       
REMARK   3      S31:  -0.8968 S32:   0.6611 S33:   0.1788                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 275 through 305 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0199   8.7961  -7.9271              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2779 T22:   0.5670                                     
REMARK   3      T33:   0.4164 T12:  -0.0917                                     
REMARK   3      T13:  -0.0010 T23:   0.0721                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7792 L22:   9.3594                                     
REMARK   3      L33:   7.7751 L12:  -3.8656                                     
REMARK   3      L13:  -2.0993 L23:   5.0611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0029 S12:   0.6853 S13:  -0.0854                       
REMARK   3      S21:   0.3750 S22:  -0.7069 S23:   0.4324                       
REMARK   3      S31:   0.3813 S32:  -0.4651 S33:   0.6481                       
REMARK   3                                                                      
CRYST1  114.170   54.170   45.090  90.00 102.04  90.00 C 1 2 1                  
SCALE1      0.008759  0.000000  0.001868        0.00000                         
SCALE2      0.000000  0.018460  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022677        0.00000                         
ATOM      1  N   SER A   1      -2.908   3.978 -17.124  1.00 51.27           N  
ANISOU    1  N   SER A   1     7770   6731   4979   1316   -612    498       N  
ATOM      2  CA  SER A   1      -2.180   5.111 -16.486  1.00 52.87           C  
ANISOU    2  CA  SER A   1     7779   6935   5373   1014   -576    831       C  
ATOM      3  C   SER A   1      -2.526   5.194 -15.001  1.00 49.92           C  
ANISOU    3  C   SER A   1     7268   6288   5411    819   -613    593       C  
ATOM      4  O   SER A   1      -3.087   4.257 -14.434  1.00 47.78           O  
ANISOU    4  O   SER A   1     7010   5921   5223    895   -586    248       O  
ATOM      5  CB  SER A   1      -2.513   6.431 -17.185  1.00 56.78           C  
ANISOU    5  CB  SER A   1     8347   7307   5920    884   -825   1088       C  
ATOM      6  OG  SER A   1      -3.826   6.859 -16.875  1.00 57.49           O  
ANISOU    6  OG  SER A   1     8518   6993   6333    841  -1124    772       O  
ATOM     14  N   GLY A   2      -2.196   6.323 -14.382  1.00 45.32           N  
ANISOU   14  N   GLY A   2     6558   5587   5076    567   -703    790       N  
ATOM     15  CA  GLY A   2      -2.329   6.483 -12.950  1.00 43.96           C  
ANISOU   15  CA  GLY A   2     6237   5226   5238    410   -725    595       C  
ATOM     16  C   GLY A   2      -1.038   6.159 -12.218  1.00 44.20           C  
ANISOU   16  C   GLY A   2     6097   5466   5231    321   -469    780       C  
ATOM     17  O   GLY A   2      -0.117   5.547 -12.755  1.00 47.66           O  
ANISOU   17  O   GLY A   2     6516   6219   5373    425   -242    983       O  
ATOM     21  N   PHE A   3      -0.976   6.586 -10.958  1.00 45.13           N  
ANISOU   21  N   PHE A   3     6079   5426   5641    156   -522    687       N  
ATOM     22  CA  PHE A   3       0.217   6.360 -10.151  1.00 46.29           C  
ANISOU   22  CA  PHE A   3     6060   5733   5795     57   -319    846       C  
ATOM     23  C   PHE A   3      -0.169   6.234  -8.686  1.00 44.28           C  
ANISOU   23  C   PHE A   3     5711   5317   5796    -13   -345    535       C  
ATOM     24  O   PHE A   3      -0.838   7.115  -8.139  1.00 44.82           O  
ANISOU   24  O   PHE A   3     5760   5150   6120    -91   -588    384       O  
ATOM     25  CB  PHE A   3       1.232   7.493 -10.342  1.00 46.23           C  
ANISOU   25  CB  PHE A   3     5949   5769   5846   -148   -397   1299       C  
ATOM     26  CG  PHE A   3       2.649   7.079 -10.083  1.00 46.30           C  
ANISOU   26  CG  PHE A   3     5784   6084   5722   -195   -134   1569       C  
ATOM     27  CD1 PHE A   3       3.327   6.282 -10.991  1.00 47.83           C  
ANISOU   27  CD1 PHE A   3     5966   6669   5539    -23    124   1744       C  
ATOM     28  CD2 PHE A   3       3.304   7.480  -8.932  1.00 43.86           C  
ANISOU   28  CD2 PHE A   3     5317   5693   5654   -376   -161   1622       C  
ATOM     29  CE1 PHE A   3       4.631   5.893 -10.756  1.00 47.92           C  
ANISOU   29  CE1 PHE A   3     5785   7003   5420    -32    362   1969       C  
ATOM     30  CE2 PHE A   3       4.609   7.096  -8.691  1.00 43.91           C  
ANISOU   30  CE2 PHE A   3     5146   5988   5551   -414     67   1864       C  
ATOM     31  CZ  PHE A   3       5.273   6.301  -9.604  1.00 45.46           C  
ANISOU   31  CZ  PHE A   3     5306   6593   5375   -242    336   2040       C  
ATOM     41  N   ARG A   4       0.270   5.143  -8.057  1.00 44.22           N  
ANISOU   41  N   ARG A   4     5647   5457   5698     36   -114    439       N  
ATOM     42  CA  ARG A   4      -0.076   4.820  -6.680  1.00 43.20           C  
ANISOU   42  CA  ARG A   4     5429   5245   5739    -23    -98    169       C  
ATOM     43  C   ARG A   4       1.166   4.390  -5.916  1.00 40.91           C  
ANISOU   43  C   ARG A   4     5023   5107   5414    -79     96    310       C  
ATOM     44  O   ARG A   4       2.086   3.794  -6.482  1.00 39.98           O  
ANISOU   44  O   ARG A   4     4909   5198   5084      2    272    508       O  
ATOM     45  CB  ARG A   4      -1.113   3.689  -6.613  1.00 41.56           C  
ANISOU   45  CB  ARG A   4     5298   5025   5468     82    -59   -141       C  
ATOM     46  CG  ARG A   4      -2.537   4.124  -6.862  1.00 44.08           C  
ANISOU   46  CG  ARG A   4     5659   5184   5906    107   -273   -379       C  
ATOM     47  CD  ARG A   4      -3.101   4.838  -5.648  1.00 41.74           C  
ANISOU   47  CD  ARG A   4     5211   4803   5846     15   -395   -587       C  
ATOM     48  NE  ARG A   4      -4.498   5.222  -5.825  1.00 39.62           N  
ANISOU   48  NE  ARG A   4     4939   4433   5684     72   -599   -851       N  
ATOM     49  CZ  ARG A   4      -5.235   5.795  -4.880  1.00 37.97           C  
ANISOU   49  CZ  ARG A   4     4582   4206   5640     64   -727  -1106       C  
ATOM     50  NH1 ARG A   4      -4.708   6.049  -3.689  1.00 39.46           N  
ANISOU   50  NH1 ARG A   4     4640   4455   5897      1   -679  -1132       N  
ATOM     51  NH2 ARG A   4      -6.498   6.115  -5.123  1.00 38.49           N  
ANISOU   51  NH2 ARG A   4     4620   4220   5785    148   -912  -1353       N  
ATOM     65  N   LYS A   5       1.180   4.683  -4.619  1.00 38.88           N  
ANISOU   65  N   LYS A   5     4655   4769   5348   -188     52    186       N  
ATOM     66  CA  LYS A   5       2.217   4.155  -3.736  1.00 40.80           C  
ANISOU   66  CA  LYS A   5     4798   5134   5569   -232    217    261       C  
ATOM     67  C   LYS A   5       1.933   2.673  -3.537  1.00 42.30           C  
ANISOU   67  C   LYS A   5     5058   5409   5604   -131    377     85       C  
ATOM     68  O   LYS A   5       1.084   2.283  -2.733  1.00 44.42           O  
ANISOU   68  O   LYS A   5     5319   5620   5938   -166    349   -159       O  
ATOM     69  CB  LYS A   5       2.252   4.906  -2.413  1.00 38.52           C  
ANISOU   69  CB  LYS A   5     4395   4734   5509   -352     91    156       C  
ATOM     70  CG  LYS A   5       3.472   4.571  -1.562  1.00 41.27           C  
ANISOU   70  CG  LYS A   5     4637   5190   5853   -411    221    282       C  
ATOM     71  CD  LYS A   5       3.691   5.593  -0.458  1.00 39.07           C  
ANISOU   71  CD  LYS A   5     4258   4780   5806   -518     30    233       C  
ATOM     72  CE  LYS A   5       4.355   6.847  -0.987  1.00 39.87           C  
ANISOU   72  CE  LYS A   5     4319   4766   6065   -633   -175    524       C  
ATOM     73  NZ  LYS A   5       4.400   7.936   0.031  1.00 43.95           N  
ANISOU   73  NZ  LYS A   5     4780   5074   6843   -708   -470    421       N  
ATOM     87  N   MET A   6       2.650   1.846  -4.281  1.00 42.19           N  
ANISOU   87  N   MET A   6     5106   5550   5375     -1    521    218       N  
ATOM     88  CA  MET A   6       2.325   0.442  -4.460  1.00 42.98           C  
ANISOU   88  CA  MET A   6     5338   5673   5321    137    581     60       C  
ATOM     89  C   MET A   6       3.285  -0.412  -3.648  1.00 40.16           C  
ANISOU   89  C   MET A   6     4941   5407   4913    152    705     88       C  
ATOM     90  O   MET A   6       4.496  -0.176  -3.665  1.00 37.19           O  
ANISOU   90  O   MET A   6     4459   5187   4484    175    806    293       O  
ATOM     91  CB  MET A   6       2.412   0.091  -5.945  1.00 45.58           C  
ANISOU   91  CB  MET A   6     5798   6105   5416    352    597    131       C  
ATOM     92  CG  MET A   6       1.751  -1.191  -6.351  1.00 48.99           C  
ANISOU   92  CG  MET A   6     6419   6470   5726    514    541    -82       C  
ATOM     93  SD  MET A   6       1.623  -1.248  -8.150  1.00 52.61           S  
ANISOU   93  SD  MET A   6     7038   7038   5914    789    498    -41       S  
ATOM     94  CE  MET A   6       0.495   0.109  -8.458  1.00 51.61           C  
ANISOU   94  CE  MET A   6     6890   6745   5974    623    344    -41       C  
ATOM    104  N   ALA A   7       2.743  -1.394  -2.941  1.00 35.22           N  
ANISOU  104  N   ALA A   7     4385   4691   4305    123    678    -94       N  
ATOM    105  CA  ALA A   7       3.545  -2.364  -2.212  1.00 36.63           C  
ANISOU  105  CA  ALA A   7     4576   4914   4428    151    746    -82       C  
ATOM    106  C   ALA A   7       3.628  -3.667  -2.997  1.00 36.49           C  
ANISOU  106  C   ALA A   7     4752   4888   4223    378    705   -152       C  
ATOM    107  O   ALA A   7       2.784  -3.964  -3.846  1.00 35.68           O  
ANISOU  107  O   ALA A   7     4788   4701   4069    465    599   -258       O  
ATOM    108  CB  ALA A   7       2.956  -2.629  -0.825  1.00 33.75           C  
ANISOU  108  CB  ALA A   7     4169   4461   4194    -51    708   -198       C  
ATOM    115  N   PHE A   8       4.668  -4.443  -2.709  1.00 36.26           N  
ANISOU  115  N   PHE A   8     4743   4936   4099    500    752   -114       N  
ATOM    116  CA  PHE A   8       4.786  -5.765  -3.297  1.00 39.09           C  
ANISOU  116  CA  PHE A   8     5311   5250   4294    753    646   -230       C  
ATOM    117  C   PHE A   8       3.710  -6.693  -2.734  1.00 37.71           C  
ANISOU  117  C   PHE A   8     5297   4803   4229    606    450   -376       C  
ATOM    118  O   PHE A   8       3.296  -6.544  -1.581  1.00 36.80           O  
ANISOU  118  O   PHE A   8     5093   4621   4268    327    457   -356       O  
ATOM    119  CB  PHE A   8       6.157  -6.366  -3.013  1.00 37.41           C  
ANISOU  119  CB  PHE A   8     5069   5178   3968    935    708   -179       C  
ATOM    120  CG  PHE A   8       7.288  -5.650  -3.680  1.00 39.65           C  
ANISOU  120  CG  PHE A   8     5164   5796   4106   1099    895     -6       C  
ATOM    121  CD1 PHE A   8       7.621  -5.922  -4.997  1.00 41.02           C  
ANISOU  121  CD1 PHE A   8     5391   6183   4014   1439    915    -23       C  
ATOM    122  CD2 PHE A   8       8.032  -4.716  -2.986  1.00 37.62           C  
ANISOU  122  CD2 PHE A   8     4664   5665   3965    913   1033    188       C  
ATOM    123  CE1 PHE A   8       8.671  -5.265  -5.609  1.00 42.47           C  
ANISOU  123  CE1 PHE A   8     5352   6755   4031   1563   1107    190       C  
ATOM    124  CE2 PHE A   8       9.081  -4.059  -3.590  1.00 39.35           C  
ANISOU  124  CE2 PHE A   8     4674   6210   4067   1009   1186    406       C  
ATOM    125  CZ  PHE A   8       9.402  -4.332  -4.902  1.00 41.04           C  
ANISOU  125  CZ  PHE A   8     4906   6689   3996   1322   1241    427       C  
ATOM    135  N   PRO A   9       3.251  -7.667  -3.521  1.00 40.44           N  
ANISOU  135  N   PRO A   9     5871   5006   4489    786    253   -511       N  
ATOM    136  CA  PRO A   9       2.351  -8.690  -2.966  1.00 42.02           C  
ANISOU  136  CA  PRO A   9     6223   4932   4809    614     15   -595       C  
ATOM    137  C   PRO A   9       3.029  -9.410  -1.809  1.00 41.10           C  
ANISOU  137  C   PRO A   9     6123   4762   4732    521    -16   -536       C  
ATOM    138  O   PRO A   9       4.191  -9.809  -1.902  1.00 42.23           O  
ANISOU  138  O   PRO A   9     6310   4980   4754    769      3   -538       O  
ATOM    139  CB  PRO A   9       2.094  -9.631  -4.151  1.00 43.37           C  
ANISOU  139  CB  PRO A   9     6666   4952   4862    910   -239   -754       C  
ATOM    140  CG  PRO A   9       2.532  -8.882  -5.369  1.00 44.50           C  
ANISOU  140  CG  PRO A   9     6766   5333   4808   1204    -91   -762       C  
ATOM    141  CD  PRO A   9       3.612  -7.948  -4.920  1.00 39.19           C  
ANISOU  141  CD  PRO A   9     5844   4944   4102   1170    209   -585       C  
ATOM    149  N   SER A  10       2.289  -9.582  -0.716  1.00 38.25           N  
ANISOU  149  N   SER A  10     5710   4300   4522    170    -68   -477       N  
ATOM    150  CA  SER A  10       2.859 -10.062   0.537  1.00 40.26           C  
ANISOU  150  CA  SER A  10     5949   4538   4811     22    -71   -381       C  
ATOM    151  C   SER A  10       2.674 -11.558   0.759  1.00 41.22           C  
ANISOU  151  C   SER A  10     6328   4374   4959    -16   -401   -385       C  
ATOM    152  O   SER A  10       3.088 -12.065   1.805  1.00 38.27           O  
ANISOU  152  O   SER A  10     5975   3956   4612   -158   -450   -284       O  
ATOM    153  CB  SER A  10       2.248  -9.291   1.713  1.00 39.35           C  
ANISOU  153  CB  SER A  10     5598   4555   4798   -332     81   -291       C  
ATOM    154  OG  SER A  10       0.834  -9.383   1.704  1.00 36.32           O  
ANISOU  154  OG  SER A  10     5186   4116   4498   -561    -20   -307       O  
ATOM    160  N   GLY A  11       2.087 -12.277  -0.200  1.00 40.71           N  
ANISOU  160  N   GLY A  11     6479   4093   4896    111   -669   -494       N  
ATOM    161  CA  GLY A  11       1.774 -13.682   0.017  1.00 41.20           C  
ANISOU  161  CA  GLY A  11     6806   3816   5034     27  -1070   -481       C  
ATOM    162  C   GLY A  11       2.970 -14.507   0.453  1.00 42.72           C  
ANISOU  162  C   GLY A  11     7160   3906   5164    216  -1205   -484       C  
ATOM    163  O   GLY A  11       2.889 -15.286   1.404  1.00 45.99           O  
ANISOU  163  O   GLY A  11     7669   4137   5670    -36  -1408   -348       O  
ATOM    167  N   LYS A  12       4.099 -14.352  -0.242  1.00 42.63           N  
ANISOU  167  N   LYS A  12     7170   4039   4988    665  -1105   -625       N  
ATOM    168  CA  LYS A  12       5.273 -15.165   0.061  1.00 45.24           C  
ANISOU  168  CA  LYS A  12     7647   4294   5248    923  -1259   -675       C  
ATOM    169  C   LYS A  12       5.779 -14.936   1.481  1.00 46.77           C  
ANISOU  169  C   LYS A  12     7686   4581   5505    643  -1097   -485       C  
ATOM    170  O   LYS A  12       6.423 -15.819   2.058  1.00 50.14           O  
ANISOU  170  O   LYS A  12     8275   4835   5939    705  -1324   -475       O  
ATOM    171  CB  LYS A  12       6.384 -14.869  -0.946  1.00 47.64           C  
ANISOU  171  CB  LYS A  12     7903   4871   5329   1456  -1106   -844       C  
ATOM    172  CG  LYS A  12       6.136 -15.453  -2.327  1.00 52.93           C  
ANISOU  172  CG  LYS A  12     8807   5433   5870   1862  -1366  -1083       C  
ATOM    173  CD  LYS A  12       7.036 -14.811  -3.372  1.00 55.24           C  
ANISOU  173  CD  LYS A  12     8943   6156   5890   2321  -1091  -1188       C  
ATOM    174  CE  LYS A  12       6.791 -15.395  -4.755  1.00 56.34           C  
ANISOU  174  CE  LYS A  12     9321   6237   5847   2776  -1352  -1450       C  
ATOM    175  NZ  LYS A  12       7.234 -16.815  -4.837  1.00 59.82           N  
ANISOU  175  NZ  LYS A  12    10012   6464   6252   3051  -1804  -1608       N  
ATOM    189  N   VAL A  13       5.505 -13.768   2.058  1.00 40.37           N  
ANISOU  189  N   VAL A  13     6580   4025   4732    363   -744   -354       N  
ATOM    190  CA  VAL A  13       5.989 -13.455   3.398  1.00 42.03           C  
ANISOU  190  CA  VAL A  13     6639   4353   4978    133   -591   -201       C  
ATOM    191  C   VAL A  13       4.971 -13.845   4.465  1.00 39.79           C  
ANISOU  191  C   VAL A  13     6373   3947   4798   -332   -712    -28       C  
ATOM    192  O   VAL A  13       5.354 -14.250   5.568  1.00 37.77           O  
ANISOU  192  O   VAL A  13     6144   3659   4549   -494   -772    101       O  
ATOM    193  CB  VAL A  13       6.343 -11.960   3.493  1.00 40.03           C  
ANISOU  193  CB  VAL A  13     6063   4443   4702    120   -193   -170       C  
ATOM    194  CG1 VAL A  13       6.859 -11.620   4.886  1.00 41.51           C  
ANISOU  194  CG1 VAL A  13     6109   4742   4922    -83    -71    -45       C  
ATOM    195  CG2 VAL A  13       7.366 -11.597   2.436  1.00 38.94           C  
ANISOU  195  CG2 VAL A  13     5870   4481   4445    530    -71   -267       C  
ATOM    205  N   GLU A  14       3.678 -13.728   4.161  1.00 40.70           N  
ANISOU  205  N   GLU A  14     6455   4028   4980   -553   -749     -7       N  
ATOM    206  CA  GLU A  14       2.650 -14.091   5.129  1.00 43.05           C  
ANISOU  206  CA  GLU A  14     6709   4296   5352  -1013   -847    191       C  
ATOM    207  C   GLU A  14       2.896 -15.482   5.694  1.00 44.33           C  
ANISOU  207  C   GLU A  14     7143   4151   5551  -1128  -1226    328       C  
ATOM    208  O   GLU A  14       2.767 -15.701   6.903  1.00 48.68           O  
ANISOU  208  O   GLU A  14     7634   4769   6095  -1456  -1229    545       O  
ATOM    209  CB  GLU A  14       1.264 -14.018   4.480  1.00 42.25           C  
ANISOU  209  CB  GLU A  14     6563   4158   5331  -1179   -921    176       C  
ATOM    210  CG  GLU A  14       0.843 -12.605   4.060  1.00 38.24           C  
ANISOU  210  CG  GLU A  14     5782   3944   4803  -1120   -585     61       C  
ATOM    211  CD  GLU A  14      -0.428 -12.580   3.222  1.00 37.35           C  
ANISOU  211  CD  GLU A  14     5656   3765   4770  -1202   -696      3       C  
ATOM    212  OE1 GLU A  14      -1.351 -13.370   3.497  1.00 40.36           O  
ANISOU  212  OE1 GLU A  14     6077   4019   5239  -1507   -933    136       O  
ATOM    213  OE2 GLU A  14      -0.499 -11.764   2.281  1.00 39.15           O  
ANISOU  213  OE2 GLU A  14     5827   4070   4979   -978   -564   -155       O  
ATOM    220  N   GLY A  15       3.269 -16.432   4.837  1.00 43.83           N  
ANISOU  220  N   GLY A  15     7390   3751   5513   -841  -1575    199       N  
ATOM    221  CA  GLY A  15       3.462 -17.804   5.255  1.00 45.27           C  
ANISOU  221  CA  GLY A  15     7882   3555   5762   -923  -2038    307       C  
ATOM    222  C   GLY A  15       4.751 -18.048   6.001  1.00 43.12           C  
ANISOU  222  C   GLY A  15     7676   3288   5419   -764  -2037    320       C  
ATOM    223  O   GLY A  15       5.085 -19.197   6.302  1.00 44.31           O  
ANISOU  223  O   GLY A  15     8120   3094   5622   -760  -2462    379       O  
ATOM    227  N   CYS A  16       5.495 -16.984   6.304  1.00 48.52           N  
ANISOU  227  N   CYS A  16     8100   4334   6003   -633  -1608    267       N  
ATOM    228  CA  CYS A  16       6.726 -17.077   7.076  1.00 48.59           C  
ANISOU  228  CA  CYS A  16     8118   4394   5952   -498  -1574    283       C  
ATOM    229  C   CYS A  16       6.616 -16.447   8.455  1.00 44.60           C  
ANISOU  229  C   CYS A  16     7384   4148   5414   -864  -1316    496       C  
ATOM    230  O   CYS A  16       7.580 -16.507   9.224  1.00 45.09           O  
ANISOU  230  O   CYS A  16     7450   4250   5431   -796  -1300    530       O  
ATOM    231  CB  CYS A  16       7.880 -16.409   6.323  1.00 51.87           C  
ANISOU  231  CB  CYS A  16     8410   5025   6273    -14  -1333     54       C  
ATOM    232  SG  CYS A  16       8.300 -17.203   4.772  1.00 53.22           S  
ANISOU  232  SG  CYS A  16     8838   4994   6389    544  -1628   -237       S  
ATOM    238  N   MET A  17       5.483 -15.842   8.785  1.00 46.36           N  
ANISOU  238  N   MET A  17     7401   4570   5643  -1215  -1126    617       N  
ATOM    239  CA  MET A  17       5.348 -15.084  10.020  1.00 45.52           C  
ANISOU  239  CA  MET A  17     7043   4792   5459  -1483   -851    757       C  
ATOM    240  C   MET A  17       4.831 -15.984  11.134  1.00 46.40           C  
ANISOU  240  C   MET A  17     7254   4834   5544  -1897  -1074   1056       C  
ATOM    241  O   MET A  17       3.860 -16.724  10.946  1.00 46.16           O  
ANISOU  241  O   MET A  17     7323   4638   5577  -2162  -1317   1208       O  
ATOM    242  CB  MET A  17       4.410 -13.898   9.805  1.00 45.07           C  
ANISOU  242  CB  MET A  17     6686   5046   5393  -1589   -535    696       C  
ATOM    243  CG  MET A  17       4.872 -12.946   8.709  1.00 43.23           C  
ANISOU  243  CG  MET A  17     6354   4884   5186  -1232   -333    457       C  
ATOM    244  SD  MET A  17       6.534 -12.293   8.970  1.00 44.22           S  
ANISOU  244  SD  MET A  17     6400   5129   5274   -922   -160    367       S  
ATOM    245  CE  MET A  17       6.416 -11.632  10.632  1.00 46.67           C  
ANISOU  245  CE  MET A  17     6504   5715   5515  -1207      9    489       C  
ATOM    255  N   VAL A  18       5.486 -15.918  12.293  1.00 48.55           N  
ANISOU  255  N   VAL A  18     7492   5237   5718  -1967  -1011   1165       N  
ATOM    256  CA  VAL A  18       5.131 -16.738  13.441  1.00 50.85           C  
ANISOU  256  CA  VAL A  18     7873   5508   5941  -2360  -1211   1489       C  
ATOM    257  C   VAL A  18       5.111 -15.867  14.689  1.00 47.32           C  
ANISOU  257  C   VAL A  18     7151   5517   5312  -2515   -889   1569       C  
ATOM    258  O   VAL A  18       5.676 -14.772  14.728  1.00 44.96           O  
ANISOU  258  O   VAL A  18     6668   5437   4979  -2268   -600   1356       O  
ATOM    259  CB  VAL A  18       6.104 -17.922  13.631  1.00 51.48           C  
ANISOU  259  CB  VAL A  18     8313   5179   6068  -2249  -1618   1553       C  
ATOM    260  CG1 VAL A  18       6.042 -18.853  12.432  1.00 51.26           C  
ANISOU  260  CG1 VAL A  18     8581   4692   6202  -2067  -2007   1444       C  
ATOM    261  CG2 VAL A  18       7.526 -17.414  13.847  1.00 51.87           C  
ANISOU  261  CG2 VAL A  18     8334   5299   6075  -1870  -1469   1353       C  
ATOM    271  N   GLN A  19       4.437 -16.375  15.714  1.00 49.46           N  
ANISOU  271  N   GLN A  19     7373   5956   5464  -2873   -965   1850       N  
ATOM    272  CA  GLN A  19       4.360 -15.730  17.018  1.00 54.16           C  
ANISOU  272  CA  GLN A  19     7713   7016   5848  -2946   -716   1890       C  
ATOM    273  C   GLN A  19       5.433 -16.332  17.915  1.00 54.28           C  
ANISOU  273  C   GLN A  19     7944   6889   5793  -2948   -900   2024       C  
ATOM    274  O   GLN A  19       5.480 -17.553  18.096  1.00 60.15           O  
ANISOU  274  O   GLN A  19     8915   7354   6585  -3075  -1254   2208       O  
ATOM    275  CB  GLN A  19       2.972 -15.925  17.629  1.00 59.67           C  
ANISOU  275  CB  GLN A  19     8173   8060   6439  -3191   -685   2033       C  
ATOM    276  CG  GLN A  19       2.788 -15.315  19.007  1.00 64.61           C  
ANISOU  276  CG  GLN A  19     8547   9182   6821  -3236   -466   2061       C  
ATOM    277  CD  GLN A  19       1.613 -15.921  19.751  1.00 71.87           C  
ANISOU  277  CD  GLN A  19     9311  10382   7613  -3520   -544   2302       C  
ATOM    278  OE1 GLN A  19       1.692 -17.046  20.248  1.00 75.51           O  
ANISOU  278  OE1 GLN A  19     9931  10700   8060  -3739   -822   2570       O  
ATOM    279  NE2 GLN A  19       0.513 -15.180  19.827  1.00 72.20           N  
ANISOU  279  NE2 GLN A  19     9039  10828   7565  -3517   -321   2215       N  
ATOM    288  N   VAL A  20       6.293 -15.481  18.467  1.00 54.35           N  
ANISOU  288  N   VAL A  20     7884   7075   5693  -2798   -694   1925       N  
ATOM    289  CA  VAL A  20       7.338 -15.909  19.391  1.00 55.57           C  
ANISOU  289  CA  VAL A  20     8219   7134   5761  -2767   -849   2030       C  
ATOM    290  C   VAL A  20       7.025 -15.338  20.764  1.00 57.12           C  
ANISOU  290  C   VAL A  20     8168   7826   5710  -2874   -643   2077       C  
ATOM    291  O   VAL A  20       6.815 -14.127  20.907  1.00 56.54           O  
ANISOU  291  O   VAL A  20     7829   8107   5545  -2764   -336   1889       O  
ATOM    292  CB  VAL A  20       8.735 -15.460  18.928  1.00 55.95           C  
ANISOU  292  CB  VAL A  20     8319   6988   5951  -2309   -828   1721       C  
ATOM    293  CG1 VAL A  20       9.786 -15.909  19.940  1.00 56.36           C  
ANISOU  293  CG1 VAL A  20     8537   6954   5923  -2263  -1008   1812       C  
ATOM    294  CG2 VAL A  20       9.042 -16.003  17.543  1.00 58.42           C  
ANISOU  294  CG2 VAL A  20     8812   6897   6489  -2071  -1013   1575       C  
ATOM    305  N   THR A  21       7.005 -16.206  21.773  1.00 55.92           N  
ANISOU  305  N   THR A  21     8107   7689   5452  -3057   -840   2303       N  
ATOM    306  CA  THR A  21       6.757 -15.798  23.147  1.00 57.46           C  
ANISOU  306  CA  THR A  21     8098   8346   5387  -3140   -684   2363       C  
ATOM    307  C   THR A  21       7.888 -16.297  24.032  1.00 59.89           C  
ANISOU  307  C   THR A  21     8640   8503   5613  -3117   -880   2481       C  
ATOM    308  O   THR A  21       8.282 -17.465  23.949  1.00 61.79           O  
ANISOU  308  O   THR A  21     9162   8347   5970  -3202  -1225   2643       O  
ATOM    309  CB  THR A  21       5.412 -16.333  23.655  1.00 61.89           C  
ANISOU  309  CB  THR A  21     8478   9185   5850  -3429   -707   2566       C  
ATOM    310  OG1 THR A  21       4.342 -15.621  23.020  1.00 61.17           O  
ANISOU  310  OG1 THR A  21     8121   9334   5788  -3397   -486   2417       O  
ATOM    311  CG2 THR A  21       5.305 -16.172  25.165  1.00 63.50           C  
ANISOU  311  CG2 THR A  21     8533   9827   5766  -3516   -615   2680       C  
ATOM    319  N   CYS A  22       8.412 -15.404  24.867  1.00 61.23           N  
ANISOU  319  N   CYS A  22     8702   8975   5587  -2976   -698   2372       N  
ATOM    320  CA  CYS A  22       9.411 -15.745  25.875  1.00 66.09           C  
ANISOU  320  CA  CYS A  22     9504   9528   6080  -2941   -865   2471       C  
ATOM    321  C   CYS A  22       8.982 -15.081  27.173  1.00 70.60           C  
ANISOU  321  C   CYS A  22     9829  10655   6342  -2965   -653   2462       C  
ATOM    322  O   CYS A  22       8.951 -13.849  27.262  1.00 70.11           O  
ANISOU  322  O   CYS A  22     9560  10910   6170  -2773   -404   2216       O  
ATOM    323  CB  CYS A  22      10.809 -15.283  25.466  1.00 61.65           C  
ANISOU  323  CB  CYS A  22     9113   8704   5605  -2641   -930   2296       C  
ATOM    324  SG  CYS A  22      12.100 -15.753  26.638  1.00 67.41           S  
ANISOU  324  SG  CYS A  22    10085   9302   6226  -2546  -1200   2381       S  
ATOM    330  N   GLY A  23       8.649 -15.889  28.173  1.00 73.64           N  
ANISOU  330  N   GLY A  23    10238  11158   6584  -3185   -773   2717       N  
ATOM    331  CA  GLY A  23       8.075 -15.352  29.388  1.00 75.81           C  
ANISOU  331  CA  GLY A  23    10262  12001   6541  -3206   -573   2729       C  
ATOM    332  C   GLY A  23       6.715 -14.747  29.098  1.00 78.48           C  
ANISOU  332  C   GLY A  23    10251  12733   6835  -3245   -320   2634       C  
ATOM    333  O   GLY A  23       5.792 -15.440  28.652  1.00 79.72           O  
ANISOU  333  O   GLY A  23    10349  12844   7096  -3484   -388   2807       O  
ATOM    337  N   THR A  24       6.582 -13.442  29.336  1.00 84.56           N  
ANISOU  337  N   THR A  24    10792  13878   7459  -2989    -68   2339       N  
ATOM    338  CA  THR A  24       5.339 -12.726  29.084  1.00 87.16           C  
ANISOU  338  CA  THR A  24    10785  14583   7748  -2952    152   2187       C  
ATOM    339  C   THR A  24       5.440 -11.757  27.913  1.00 83.74           C  
ANISOU  339  C   THR A  24    10299  13995   7523  -2725    268   1862       C  
ATOM    340  O   THR A  24       4.528 -10.947  27.715  1.00 87.74           O  
ANISOU  340  O   THR A  24    10537  14798   8000  -2618    436   1664       O  
ATOM    341  CB  THR A  24       4.888 -11.963  30.335  1.00 89.64           C  
ANISOU  341  CB  THR A  24    10842  15500   7717  -2811    319   2076       C  
ATOM    342  OG1 THR A  24       3.922 -10.967  29.965  1.00 88.70           O  
ANISOU  342  OG1 THR A  24    10420  15693   7591  -2649    508   1809       O  
ATOM    343  CG2 THR A  24       6.069 -11.296  31.039  1.00 86.61           C  
ANISOU  343  CG2 THR A  24    10585  15136   7188  -2536    305   1883       C  
ATOM    351  N   THR A  25       6.517 -11.813  27.137  1.00 69.69           N  
ANISOU  351  N   THR A  25     8763  11772   5946  -2643    168   1807       N  
ATOM    352  CA  THR A  25       6.664 -10.977  25.953  1.00 64.28           C  
ANISOU  352  CA  THR A  25     8033  10924   5467  -2463    270   1543       C  
ATOM    353  C   THR A  25       6.336 -11.807  24.721  1.00 61.21           C  
ANISOU  353  C   THR A  25     7764  10143   5348  -2622    171   1677       C  
ATOM    354  O   THR A  25       6.900 -12.888  24.529  1.00 62.69           O  
ANISOU  354  O   THR A  25     8224   9958   5639  -2751    -53   1894       O  
ATOM    355  CB  THR A  25       8.081 -10.413  25.841  1.00 64.48           C  
ANISOU  355  CB  THR A  25     8215  10768   5516  -2257    226   1391       C  
ATOM    356  OG1 THR A  25       8.432  -9.743  27.057  1.00 64.86           O  
ANISOU  356  OG1 THR A  25     8191  11157   5297  -2098    248   1261       O  
ATOM    357  CG2 THR A  25       8.169  -9.430  24.678  1.00 63.64           C  
ANISOU  357  CG2 THR A  25     7991  10469   5720  -2011    320   1064       C  
ATOM    365  N   THR A  26       5.418 -11.309  23.898  1.00 65.35           N  
ANISOU  365  N   THR A  26     8105  10738   5989  -2585    299   1530       N  
ATOM    366  CA  THR A  26       5.057 -11.963  22.648  1.00 65.37           C  
ANISOU  366  CA  THR A  26     8213  10387   6237  -2688    206   1605       C  
ATOM    367  C   THR A  26       5.230 -10.972  21.507  1.00 59.65           C  
ANISOU  367  C   THR A  26     7422   9550   5694  -2471    346   1325       C  
ATOM    368  O   THR A  26       4.677  -9.869  21.548  1.00 60.61           O  
ANISOU  368  O   THR A  26     7300   9958   5771  -2322    518   1090       O  
ATOM    369  CB  THR A  26       3.618 -12.496  22.681  1.00 68.40           C  
ANISOU  369  CB  THR A  26     8447  10956   6588  -2898    184   1751       C  
ATOM    370  OG1 THR A  26       3.272 -13.025  21.394  1.00 69.69           O  
ANISOU  370  OG1 THR A  26     8719  10771   6988  -2963     79   1782       O  
ATOM    371  CG2 THR A  26       2.631 -11.398  23.057  1.00 70.04           C  
ANISOU  371  CG2 THR A  26     8313  11648   6650  -2778    405   1547       C  
ATOM    379  N   LEU A  27       6.006 -11.362  20.499  1.00 49.18           N  
ANISOU  379  N   LEU A  27     6313   7804   4568  -2440    248   1348       N  
ATOM    380  CA  LEU A  27       6.193 -10.546  19.309  1.00 49.05           C  
ANISOU  380  CA  LEU A  27     6233   7622   4782  -2194    342   1079       C  
ATOM    381  C   LEU A  27       6.298 -11.470  18.101  1.00 46.31           C  
ANISOU  381  C   LEU A  27     6102   6843   4650  -2199    173   1150       C  
ATOM    382  O   LEU A  27       6.134 -12.690  18.208  1.00 46.66           O  
ANISOU  382  O   LEU A  27     6346   6707   4675  -2414    -39   1398       O  
ATOM    383  CB  LEU A  27       7.414  -9.626  19.458  1.00 45.50           C  
ANISOU  383  CB  LEU A  27     5758   7108   4424  -1880    373    848       C  
ATOM    384  CG  LEU A  27       8.698 -10.188  20.068  1.00 50.60           C  
ANISOU  384  CG  LEU A  27     6595   7562   5070  -1805    207    929       C  
ATOM    385  CD1 LEU A  27       9.333 -11.216  19.151  1.00 52.80           C  
ANISOU  385  CD1 LEU A  27     7113   7415   5535  -1744     21   1006       C  
ATOM    386  CD2 LEU A  27       9.672  -9.047  20.377  1.00 50.63           C  
ANISOU  386  CD2 LEU A  27     6484   7606   5146  -1541    253    702       C  
ATOM    398  N   ASN A  28       6.555 -10.880  16.940  1.00 47.39           N  
ANISOU  398  N   ASN A  28     6207   6816   4984  -1957    236    934       N  
ATOM    399  CA  ASN A  28       6.541 -11.619  15.687  1.00 49.31           C  
ANISOU  399  CA  ASN A  28     6629   6713   5394  -1899     93    942       C  
ATOM    400  C   ASN A  28       7.929 -12.130  15.332  1.00 47.06           C  
ANISOU  400  C   ASN A  28     6548   6119   5214  -1644    -64    898       C  
ATOM    401  O   ASN A  28       8.947 -11.518  15.661  1.00 47.73           O  
ANISOU  401  O   ASN A  28     6562   6258   5315  -1452      7    797       O  
ATOM    402  CB  ASN A  28       6.004 -10.737  14.561  1.00 46.75           C  
ANISOU  402  CB  ASN A  28     6153   6426   5184  -1767    247    747       C  
ATOM    403  CG  ASN A  28       4.705 -10.060  14.935  1.00 46.74           C  
ANISOU  403  CG  ASN A  28     5907   6772   5081  -1949    408    729       C  
ATOM    404  OD1 ASN A  28       3.640 -10.680  14.912  1.00 46.45           O  
ANISOU  404  OD1 ASN A  28     5860   6793   4997  -2201    353    876       O  
ATOM    405  ND2 ASN A  28       4.786  -8.786  15.303  1.00 44.22           N  
ANISOU  405  ND2 ASN A  28     5378   6695   4731  -1815    577    546       N  
ATOM    412  N   GLY A  29       7.954 -13.285  14.667  1.00 42.09           N  
ANISOU  412  N   GLY A  29     6168   5168   4658  -1631   -313    966       N  
ATOM    413  CA  GLY A  29       9.189 -13.864  14.197  1.00 39.99           C  
ANISOU  413  CA  GLY A  29     6090   4632   4474  -1330   -491    884       C  
ATOM    414  C   GLY A  29       9.084 -14.224  12.729  1.00 38.92           C  
ANISOU  414  C   GLY A  29     6063   4282   4443  -1113   -585    752       C  
ATOM    415  O   GLY A  29       7.997 -14.320  12.160  1.00 38.18           O  
ANISOU  415  O   GLY A  29     5973   4157   4375  -1256   -599    772       O  
ATOM    419  N   LEU A  30      10.247 -14.427  12.124  1.00 40.98           N  
ANISOU  419  N   LEU A  30     6397   4427   4747   -744   -658    608       N  
ATOM    420  CA  LEU A  30      10.368 -14.776  10.713  1.00 42.90           C  
ANISOU  420  CA  LEU A  30     6741   4524   5036   -439   -750    446       C  
ATOM    421  C   LEU A  30      10.876 -16.211  10.625  1.00 45.09           C  
ANISOU  421  C   LEU A  30     7353   4453   5326   -271  -1170    429       C  
ATOM    422  O   LEU A  30      12.011 -16.499  11.020  1.00 43.05           O  
ANISOU  422  O   LEU A  30     7140   4166   5052    -61  -1264    388       O  
ATOM    423  CB  LEU A  30      11.305 -13.804  10.003  1.00 40.70           C  
ANISOU  423  CB  LEU A  30     6231   4475   4759   -109   -491    290       C  
ATOM    424  CG  LEU A  30      11.469 -13.991   8.497  1.00 44.13           C  
ANISOU  424  CG  LEU A  30     6710   4880   5176    243   -519    122       C  
ATOM    425  CD1 LEU A  30      10.161 -13.750   7.767  1.00 45.22           C  
ANISOU  425  CD1 LEU A  30     6856   4991   5334     94   -472    111       C  
ATOM    426  CD2 LEU A  30      12.555 -13.063   7.979  1.00 46.67           C  
ANISOU  426  CD2 LEU A  30     6763   5496   5473    522   -262     50       C  
ATOM    438  N   TRP A  31      10.035 -17.103  10.105  1.00 43.57           N  
ANISOU  438  N   TRP A  31     7399   3977   5177   -354  -1463    451       N  
ATOM    439  CA  TRP A  31      10.312 -18.538  10.060  1.00 44.19           C  
ANISOU  439  CA  TRP A  31     7851   3640   5298   -239  -1969    446       C  
ATOM    440  C   TRP A  31      10.767 -18.907   8.654  1.00 46.34           C  
ANISOU  440  C   TRP A  31     8247   3796   5563    276  -2120    148       C  
ATOM    441  O   TRP A  31       9.955 -18.989   7.729  1.00 43.63           O  
ANISOU  441  O   TRP A  31     7964   3366   5246    293  -2182     75       O  
ATOM    442  CB  TRP A  31       9.068 -19.326  10.459  1.00 49.58           C  
ANISOU  442  CB  TRP A  31     8729   4060   6050   -700  -2269    696       C  
ATOM    443  CG  TRP A  31       9.258 -20.812  10.505  1.00 53.89           C  
ANISOU  443  CG  TRP A  31     9692   4106   6676   -655  -2876    738       C  
ATOM    444  CD1 TRP A  31      10.432 -21.486  10.668  1.00 55.74           C  
ANISOU  444  CD1 TRP A  31    10134   4140   6907   -314  -3160    617       C  
ATOM    445  CD2 TRP A  31       8.235 -21.810  10.387  1.00 55.21           C  
ANISOU  445  CD2 TRP A  31    10127   3889   6963   -964  -3328    917       C  
ATOM    446  NE1 TRP A  31      10.205 -22.841  10.661  1.00 56.63           N  
ANISOU  446  NE1 TRP A  31    10636   3759   7122   -373  -3772    681       N  
ATOM    447  CE2 TRP A  31       8.865 -23.066  10.490  1.00 58.54           C  
ANISOU  447  CE2 TRP A  31    10843   3978   7423   -780  -3841    846       C  
ATOM    448  CE3 TRP A  31       6.850 -21.762  10.202  1.00 50.84           C  
ANISOU  448  CE3 TRP A  31     9485   3365   6467  -1365  -3312   1089       C  
ATOM    449  CZ2 TRP A  31       8.157 -24.264  10.413  1.00 63.49           C  
ANISOU  449  CZ2 TRP A  31    11618   4384   8121   -989  -4311    926       C  
ATOM    450  CZ3 TRP A  31       6.149 -22.952  10.128  1.00 55.20           C  
ANISOU  450  CZ3 TRP A  31    10161   3723   7088  -1544  -3759   1187       C  
ATOM    451  CH2 TRP A  31       6.803 -24.186  10.233  1.00 62.58           C  
ANISOU  451  CH2 TRP A  31    11373   4354   8052  -1368  -4267   1117       C  
ATOM    462  N   LEU A  32      12.069 -19.134   8.497  1.00 45.76           N  
ANISOU  462  N   LEU A  32     8197   3756   5436    718  -2186    -32       N  
ATOM    463  CA  LEU A  32      12.655 -19.531   7.224  1.00 47.68           C  
ANISOU  463  CA  LEU A  32     8530   3974   5610   1287  -2331   -340       C  
ATOM    464  C   LEU A  32      13.472 -20.794   7.440  1.00 50.54           C  
ANISOU  464  C   LEU A  32     9211   4006   5984   1599  -2838   -465       C  
ATOM    465  O   LEU A  32      14.316 -20.841   8.341  1.00 48.86           O  
ANISOU  465  O   LEU A  32     8957   3835   5772   1604  -2842   -403       O  
ATOM    466  CB  LEU A  32      13.538 -18.422   6.650  1.00 45.76           C  
ANISOU  466  CB  LEU A  32     7911   4227   5250   1602  -1867   -465       C  
ATOM    467  CG  LEU A  32      12.849 -17.082   6.386  1.00 43.24           C  
ANISOU  467  CG  LEU A  32     7281   4217   4930   1337  -1401   -356       C  
ATOM    468  CD1 LEU A  32      13.879 -16.001   6.106  1.00 41.62           C  
ANISOU  468  CD1 LEU A  32     6704   4465   4646   1559  -1004   -389       C  
ATOM    469  CD2 LEU A  32      11.872 -17.203   5.229  1.00 43.41           C  
ANISOU  469  CD2 LEU A  32     7413   4147   4933   1397  -1471   -457       C  
ATOM    481  N   ASP A  33      13.229 -21.808   6.611  1.00 57.09           N  
ANISOU  481  N   ASP A  33    10371   4492   6829   1885  -3301   -662       N  
ATOM    482  CA  ASP A  33      13.852 -23.109   6.826  1.00 61.76           C  
ANISOU  482  CA  ASP A  33    11251   4783   7431   2094  -3827   -806       C  
ATOM    483  C   ASP A  33      13.559 -23.545   8.259  1.00 63.21           C  
ANISOU  483  C   ASP A  33    11581   4688   7747   1557  -4035   -471       C  
ATOM    484  O   ASP A  33      12.429 -23.386   8.733  1.00 60.81           O  
ANISOU  484  O   ASP A  33    11304   4264   7538   1015  -4009   -160       O  
ATOM    485  CB  ASP A  33      15.356 -23.043   6.547  1.00 62.80           C  
ANISOU  485  CB  ASP A  33    11213   5241   7407   2668  -3712  -1089       C  
ATOM    486  CG  ASP A  33      15.670 -22.631   5.115  1.00 66.22           C  
ANISOU  486  CG  ASP A  33    11445   6075   7641   3158  -3468  -1380       C  
ATOM    487  OD1 ASP A  33      14.911 -23.014   4.199  1.00 64.12           O  
ANISOU  487  OD1 ASP A  33    11317   5712   7332   3185  -3636  -1499       O  
ATOM    488  OD2 ASP A  33      16.680 -21.924   4.909  1.00 65.72           O  
ANISOU  488  OD2 ASP A  33    11059   6463   7449   3490  -3110  -1464       O  
ATOM    493  N   ASP A  34      14.559 -24.074   8.967  1.00 64.67           N  
ANISOU  493  N   ASP A  34    11827   4828   7916   1683  -4217   -521       N  
ATOM    494  CA  ASP A  34      14.386 -24.512  10.347  1.00 64.92           C  
ANISOU  494  CA  ASP A  34    11983   4649   8033   1194  -4407   -207       C  
ATOM    495  C   ASP A  34      14.895 -23.480  11.348  1.00 62.98           C  
ANISOU  495  C   ASP A  34    11527   4645   7758   1078  -4026     20       C  
ATOM    496  O   ASP A  34      15.393 -23.847  12.418  1.00 63.89           O  
ANISOU  496  O   ASP A  34    11710   4685   7881    926  -4168    145       O  
ATOM    497  CB  ASP A  34      15.079 -25.858  10.572  1.00 70.49           C  
ANISOU  497  CB  ASP A  34    12941   5093   8747   1355  -4931   -395       C  
ATOM    498  CG  ASP A  34      16.585 -25.790  10.373  1.00 73.21           C  
ANISOU  498  CG  ASP A  34    13183   5642   8992   1944  -4859   -720       C  
ATOM    499  OD1 ASP A  34      17.106 -24.706  10.038  1.00 71.14           O  
ANISOU  499  OD1 ASP A  34    12619   5758   8653   2226  -4403   -780       O  
ATOM    500  OD2 ASP A  34      17.251 -26.832  10.555  1.00 78.96           O  
ANISOU  500  OD2 ASP A  34    14112   6176   9714   2115  -5275   -911       O  
ATOM    505  N   VAL A  35      14.772 -22.193  11.026  1.00 55.32           N  
ANISOU  505  N   VAL A  35    10189   4108   6723   1067  -3458     17       N  
ATOM    506  CA  VAL A  35      15.252 -21.118  11.884  1.00 51.71           C  
ANISOU  506  CA  VAL A  35     9385   4052   6211    900  -2995    138       C  
ATOM    507  C   VAL A  35      14.172 -20.055  11.999  1.00 50.80           C  
ANISOU  507  C   VAL A  35     9010   4212   6080    463  -2552    321       C  
ATOM    508  O   VAL A  35      13.484 -19.743  11.020  1.00 52.63           O  
ANISOU  508  O   VAL A  35     9173   4506   6316    496  -2418    236       O  
ATOM    509  CB  VAL A  35      16.556 -20.492  11.346  1.00 50.37           C  
ANISOU  509  CB  VAL A  35     8925   4241   5975   1415  -2726   -124       C  
ATOM    510  CG1 VAL A  35      17.079 -19.439  12.315  1.00 51.13           C  
ANISOU  510  CG1 VAL A  35     8697   4674   6056   1218  -2343     14       C  
ATOM    511  CG2 VAL A  35      17.599 -21.562  11.097  1.00 53.39           C  
ANISOU  511  CG2 VAL A  35     9535   4402   6348   1935  -3172   -366       C  
ATOM    521  N   VAL A  36      14.032 -19.492  13.195  1.00 52.68           N  
ANISOU  521  N   VAL A  36     9103   4626   6285     89  -2344    547       N  
ATOM    522  CA  VAL A  36      13.125 -18.381  13.447  1.00 51.50           C  
ANISOU  522  CA  VAL A  36     8672   4795   6099   -266  -1923    677       C  
ATOM    523  C   VAL A  36      13.957 -17.186  13.885  1.00 50.29           C  
ANISOU  523  C   VAL A  36     8189   5009   5911   -163  -1545    614       C  
ATOM    524  O   VAL A  36      14.789 -17.301  14.793  1.00 55.35           O  
ANISOU  524  O   VAL A  36     8848   5653   6529   -133  -1625    657       O  
ATOM    525  CB  VAL A  36      12.068 -18.734  14.508  1.00 48.66           C  
ANISOU  525  CB  VAL A  36     8414   4375   5700   -808  -2029   1003       C  
ATOM    526  CG1 VAL A  36      11.267 -17.498  14.892  1.00 46.72           C  
ANISOU  526  CG1 VAL A  36     7834   4538   5381  -1092  -1581   1081       C  
ATOM    527  CG2 VAL A  36      11.152 -19.829  13.992  1.00 50.97           C  
ANISOU  527  CG2 VAL A  36     8997   4298   6069   -971  -2419   1104       C  
ATOM    537  N   TYR A  37      13.740 -16.047  13.234  1.00 43.18           N  
ANISOU  537  N   TYR A  37     6999   4388   5018   -114  -1178    520       N  
ATOM    538  CA  TYR A  37      14.407 -14.799  13.574  1.00 43.10           C  
ANISOU  538  CA  TYR A  37     6667   4695   5012    -62   -856    481       C  
ATOM    539  C   TYR A  37      13.415 -13.875  14.265  1.00 43.57           C  
ANISOU  539  C   TYR A  37     6562   4956   5035   -429   -620    595       C  
ATOM    540  O   TYR A  37      12.251 -13.789  13.860  1.00 41.03           O  
ANISOU  540  O   TYR A  37     6242   4644   4704   -612   -557    628       O  
ATOM    541  CB  TYR A  37      14.973 -14.116  12.325  1.00 43.50           C  
ANISOU  541  CB  TYR A  37     6500   4927   5103    267   -651    314       C  
ATOM    542  CG  TYR A  37      15.858 -15.006  11.482  1.00 46.43           C  
ANISOU  542  CG  TYR A  37     6993   5192   5458    699   -858    159       C  
ATOM    543  CD1 TYR A  37      15.310 -15.954  10.627  1.00 46.05           C  
ANISOU  543  CD1 TYR A  37     7201   4911   5385    831  -1094     70       C  
ATOM    544  CD2 TYR A  37      17.241 -14.895  11.534  1.00 48.76           C  
ANISOU  544  CD2 TYR A  37     7134   5638   5756   1002   -842     81       C  
ATOM    545  CE1 TYR A  37      16.112 -16.770   9.856  1.00 47.25           C  
ANISOU  545  CE1 TYR A  37     7473   4987   5494   1295  -1318   -125       C  
ATOM    546  CE2 TYR A  37      18.053 -15.707  10.764  1.00 49.39           C  
ANISOU  546  CE2 TYR A  37     7292   5688   5786   1454  -1031    -96       C  
ATOM    547  CZ  TYR A  37      17.483 -16.641   9.928  1.00 46.87           C  
ANISOU  547  CZ  TYR A  37     7247   5141   5420   1621  -1272   -216       C  
ATOM    548  OH  TYR A  37      18.288 -17.451   9.160  1.00 50.38           O  
ANISOU  548  OH  TYR A  37     7778   5575   5789   2138  -1493   -444       O  
ATOM    558  N   CYS A  38      13.872 -13.186  15.306  1.00 45.66           N  
ANISOU  558  N   CYS A  38     6681   5394   5273   -508   -512    631       N  
ATOM    559  CA  CYS A  38      13.027 -12.242  16.023  1.00 43.04           C  
ANISOU  559  CA  CYS A  38     6179   5297   4877   -775   -310    682       C  
ATOM    560  C   CYS A  38      13.921 -11.261  16.768  1.00 42.41           C  
ANISOU  560  C   CYS A  38     5906   5389   4820   -694   -209    623       C  
ATOM    561  O   CYS A  38      15.111 -11.531  16.970  1.00 42.49           O  
ANISOU  561  O   CYS A  38     5942   5324   4877   -508   -324    602       O  
ATOM    562  CB  CYS A  38      12.088 -12.966  17.001  1.00 43.81           C  
ANISOU  562  CB  CYS A  38     6432   5386   4826  -1111   -431    878       C  
ATOM    563  SG  CYS A  38      12.936 -13.792  18.366  1.00 48.83           S  
ANISOU  563  SG  CYS A  38     7267   5925   5361  -1161   -684   1025       S  
ATOM    569  N   PRO A  39      13.382 -10.116  17.186  1.00 34.66           N  
ANISOU  569  N   PRO A  39     4727   4628   3815   -809    -30    578       N  
ATOM    570  CA  PRO A  39      14.190  -9.179  17.977  1.00 38.15           C  
ANISOU  570  CA  PRO A  39     5011   5192   4291   -738     -5    511       C  
ATOM    571  C   PRO A  39      14.592  -9.809  19.303  1.00 37.01           C  
ANISOU  571  C   PRO A  39     5012   5040   4009   -807   -167    601       C  
ATOM    572  O   PRO A  39      13.805 -10.508  19.946  1.00 36.55           O  
ANISOU  572  O   PRO A  39     5101   5018   3770  -1015   -224    731       O  
ATOM    573  CB  PRO A  39      13.258  -7.975  18.172  1.00 36.13           C  
ANISOU  573  CB  PRO A  39     4574   5146   4009   -841    151    420       C  
ATOM    574  CG  PRO A  39      12.177  -8.137  17.135  1.00 35.96           C  
ANISOU  574  CG  PRO A  39     4561   5107   3996   -912    249    423       C  
ATOM    575  CD  PRO A  39      12.018  -9.611  16.957  1.00 32.64           C  
ANISOU  575  CD  PRO A  39     4381   4513   3507   -980    116    560       C  
ATOM    583  N   ARG A  40      15.839  -9.567  19.706  1.00 36.37           N  
ANISOU  583  N   ARG A  40     4881   4927   4014   -647   -255    557       N  
ATOM    584  CA  ARG A  40      16.342 -10.196  20.921  1.00 40.16           C  
ANISOU  584  CA  ARG A  40     5517   5374   4368   -681   -439    637       C  
ATOM    585  C   ARG A  40      15.691  -9.635  22.179  1.00 39.25           C  
ANISOU  585  C   ARG A  40     5367   5498   4048   -844   -398    641       C  
ATOM    586  O   ARG A  40      15.756 -10.281  23.229  1.00 42.31           O  
ANISOU  586  O   ARG A  40     5916   5910   4250   -937   -533    757       O  
ATOM    587  CB  ARG A  40      17.863 -10.047  21.010  1.00 41.95           C  
ANISOU  587  CB  ARG A  40     5669   5519   4750   -451   -557    573       C  
ATOM    588  CG  ARG A  40      18.355  -8.623  21.199  1.00 42.95           C  
ANISOU  588  CG  ARG A  40     5530   5777   5013   -386   -484    457       C  
ATOM    589  CD  ARG A  40      19.851  -8.598  21.450  1.00 43.42           C  
ANISOU  589  CD  ARG A  40     5508   5769   5219   -204   -637    436       C  
ATOM    590  NE  ARG A  40      20.365  -7.237  21.570  1.00 42.04           N  
ANISOU  590  NE  ARG A  40     5075   5678   5223   -173   -625    356       N  
ATOM    591  CZ  ARG A  40      21.623  -6.939  21.873  1.00 44.25           C  
ANISOU  591  CZ  ARG A  40     5218   5932   5663    -55   -767    346       C  
ATOM    592  NH1 ARG A  40      22.506  -7.906  22.090  1.00 46.28           N  
ANISOU  592  NH1 ARG A  40     5568   6110   5908     76   -910    383       N  
ATOM    593  NH2 ARG A  40      21.999  -5.671  21.963  1.00 39.92           N  
ANISOU  593  NH2 ARG A  40     4442   5423   5304    -70   -803    298       N  
ATOM    607  N   HIS A  41      15.062  -8.459  22.102  1.00 38.88           N  
ANISOU  607  N   HIS A  41     5121   5643   4010   -858   -237    510       N  
ATOM    608  CA  HIS A  41      14.426  -7.894  23.288  1.00 40.82           C  
ANISOU  608  CA  HIS A  41     5316   6171   4022   -940   -208    460       C  
ATOM    609  C   HIS A  41      13.128  -8.600  23.644  1.00 41.11           C  
ANISOU  609  C   HIS A  41     5431   6408   3781  -1182   -132    617       C  
ATOM    610  O   HIS A  41      12.442  -8.168  24.578  1.00 42.00           O  
ANISOU  610  O   HIS A  41     5463   6855   3639  -1242    -70    582       O  
ATOM    611  CB  HIS A  41      14.191  -6.387  23.118  1.00 40.07           C  
ANISOU  611  CB  HIS A  41     4992   6198   4033   -831   -126    231       C  
ATOM    612  CG  HIS A  41      13.155  -6.021  22.097  1.00 42.44           C  
ANISOU  612  CG  HIS A  41     5189   6541   4395   -884     41    185       C  
ATOM    613  ND1 HIS A  41      11.812  -6.286  22.264  1.00 43.32           N  
ANISOU  613  ND1 HIS A  41     5291   6885   4282  -1041    161    225       N  
ATOM    614  CD2 HIS A  41      13.263  -5.363  20.919  1.00 39.88           C  
ANISOU  614  CD2 HIS A  41     4748   6081   4325   -805     98    110       C  
ATOM    615  CE1 HIS A  41      11.141  -5.829  21.221  1.00 39.97           C  
ANISOU  615  CE1 HIS A  41     4764   6435   3987  -1039    272    152       C  
ATOM    616  NE2 HIS A  41      11.999  -5.265  20.390  1.00 41.10           N  
ANISOU  616  NE2 HIS A  41     4855   6349   4412   -896    235     85       N  
ATOM    624  N   VAL A  42      12.784  -9.677  22.933  1.00 39.70           N  
ANISOU  624  N   VAL A  42     5395   6051   3638  -1314   -158    793       N  
ATOM    625  CA  VAL A  42      11.684 -10.531  23.367  1.00 44.91           C  
ANISOU  625  CA  VAL A  42     6144   6865   4054  -1605   -154   1025       C  
ATOM    626  C   VAL A  42      11.969 -11.106  24.748  1.00 45.71           C  
ANISOU  626  C   VAL A  42     6381   7090   3896  -1716   -293   1203       C  
ATOM    627  O   VAL A  42      11.042 -11.403  25.509  1.00 45.90           O  
ANISOU  627  O   VAL A  42     6384   7430   3625  -1958   -243   1390       O  
ATOM    628  CB  VAL A  42      11.435 -11.650  22.333  1.00 43.97           C  
ANISOU  628  CB  VAL A  42     6200   6433   4075  -1710   -258   1179       C  
ATOM    629  CG1 VAL A  42      12.627 -12.592  22.264  1.00 45.60           C  
ANISOU  629  CG1 VAL A  42     6653   6273   4399  -1590   -521   1243       C  
ATOM    630  CG2 VAL A  42      10.165 -12.415  22.672  1.00 43.31           C  
ANISOU  630  CG2 VAL A  42     6162   6510   3785  -2067   -268   1450       C  
ATOM    640  N   ILE A  43      13.251 -11.264  25.101  1.00 48.52           N  
ANISOU  640  N   ILE A  43     6859   7235   4341  -1546   -469   1164       N  
ATOM    641  CA  ILE A  43      13.614 -11.860  26.385  1.00 49.42           C  
ANISOU  641  CA  ILE A  43     7137   7424   4215  -1636   -638   1339       C  
ATOM    642  C   ILE A  43      13.564 -10.869  27.535  1.00 49.62           C  
ANISOU  642  C   ILE A  43     7013   7843   3999  -1554   -550   1200       C  
ATOM    643  O   ILE A  43      13.780 -11.264  28.689  1.00 52.39           O  
ANISOU  643  O   ILE A  43     7483   8334   4089  -1622   -670   1340       O  
ATOM    644  CB  ILE A  43      15.025 -12.481  26.320  1.00 50.79           C  
ANISOU  644  CB  ILE A  43     7509   7207   4582  -1459   -901   1335       C  
ATOM    645  CG1 ILE A  43      16.100 -11.390  26.277  1.00 51.31           C  
ANISOU  645  CG1 ILE A  43     7406   7249   4842  -1151   -876   1049       C  
ATOM    646  CG2 ILE A  43      15.151 -13.377  25.097  1.00 49.83           C  
ANISOU  646  CG2 ILE A  43     7528   6707   4697  -1438  -1014   1388       C  
ATOM    647  CD1 ILE A  43      17.509 -11.928  26.120  1.00 52.56           C  
ANISOU  647  CD1 ILE A  43     7685   7081   5205   -948  -1110   1024       C  
ATOM    659  N   CYS A  44      13.284  -9.599  27.267  1.00 47.39           N  
ANISOU  659  N   CYS A  44     6488   7734   3783  -1394   -380    923       N  
ATOM    660  CA  CYS A  44      13.284  -8.578  28.302  1.00 49.72           C  
ANISOU  660  CA  CYS A  44     6654   8365   3873  -1243   -358    720       C  
ATOM    661  C   CYS A  44      11.881  -8.361  28.851  1.00 54.71           C  
ANISOU  661  C   CYS A  44     7137   9523   4126  -1373   -169    750       C  
ATOM    662  O   CYS A  44      10.879  -8.586  28.167  1.00 54.96           O  
ANISOU  662  O   CYS A  44     7082   9640   4162  -1543    -16    844       O  
ATOM    663  CB  CYS A  44      13.826  -7.255  27.760  1.00 48.14           C  
ANISOU  663  CB  CYS A  44     6286   8029   3977   -973   -360    385       C  
ATOM    664  SG  CYS A  44      15.529  -7.335  27.176  1.00 51.72           S  
ANISOU  664  SG  CYS A  44     6811   7990   4849   -807   -558    354       S  
ATOM    670  N   THR A  45      11.822  -7.925  30.104  1.00 62.35           N  
ANISOU  670  N   THR A  45     8060  10879   4751  -1274   -189    664       N  
ATOM    671  CA  THR A  45      10.588  -7.411  30.668  1.00 66.51           C  
ANISOU  671  CA  THR A  45     8371  12004   4895  -1278     -1    586       C  
ATOM    672  C   THR A  45      10.507  -5.912  30.383  1.00 70.33           C  
ANISOU  672  C   THR A  45     8661  12531   5531   -947     17    132       C  
ATOM    673  O   THR A  45      11.362  -5.334  29.707  1.00 66.40           O  
ANISOU  673  O   THR A  45     8193  11592   5443   -785   -107    -51       O  
ATOM    674  CB  THR A  45      10.518  -7.702  32.165  1.00 67.13           C  
ANISOU  674  CB  THR A  45     8487  12496   4523  -1286    -37    701       C  
ATOM    675  OG1 THR A  45      11.378  -6.802  32.874  1.00 68.44           O  
ANISOU  675  OG1 THR A  45     8682  12699   4621   -952   -206    380       O  
ATOM    676  CG2 THR A  45      10.952  -9.132  32.446  1.00 69.57           C  
ANISOU  676  CG2 THR A  45     9051  12561   4822  -1569   -166   1128       C  
ATOM    684  N   SER A  46       9.460  -5.268  30.898  1.00 84.87           N  
ANISOU  684  N   SER A  46    10288  14924   7034   -842    151    -44       N  
ATOM    685  CA  SER A  46       9.367  -3.818  30.774  1.00 88.05           C  
ANISOU  685  CA  SER A  46    10538  15364   7555   -487     89   -507       C  
ATOM    686  C   SER A  46      10.490  -3.133  31.543  1.00 88.53           C  
ANISOU  686  C   SER A  46    10706  15266   7664   -195   -187   -757       C  
ATOM    687  O   SER A  46      11.094  -2.171  31.053  1.00 87.91           O  
ANISOU  687  O   SER A  46    10619  14817   7965      9   -368  -1027       O  
ATOM    688  CB  SER A  46       8.001  -3.340  31.264  1.00 89.96           C  
ANISOU  688  CB  SER A  46    10522  16080   7580   -370    248   -642       C  
ATOM    689  OG  SER A  46       6.975  -3.797  30.400  1.00 88.55           O  
ANISOU  689  OG  SER A  46    10212  15919   7513   -608    443   -456       O  
ATOM    695  N   GLU A  47      10.793  -3.624  32.748  1.00 80.93           N  
ANISOU  695  N   GLU A  47     9848  14572   6328   -192   -248   -646       N  
ATOM    696  CA  GLU A  47      11.875  -3.046  33.538  1.00 80.30           C  
ANISOU  696  CA  GLU A  47     9886  14340   6283     83   -541   -877       C  
ATOM    697  C   GLU A  47      13.231  -3.277  32.882  1.00 75.48           C  
ANISOU  697  C   GLU A  47     9435  13049   6193     14   -727   -772       C  
ATOM    698  O   GLU A  47      14.121  -2.422  32.966  1.00 74.72           O  
ANISOU  698  O   GLU A  47     9359  12664   6369    242   -989  -1026       O  
ATOM    699  CB  GLU A  47      11.862  -3.635  34.950  1.00 86.55           C  
ANISOU  699  CB  GLU A  47    10768  15475   6641     81   -539   -720       C  
ATOM    700  CG  GLU A  47      13.200  -3.539  35.674  1.00 89.08           C  
ANISOU  700  CG  GLU A  47    11291  15588   6968    246   -864   -815       C  
ATOM    701  CD  GLU A  47      13.099  -3.887  37.145  1.00 94.90           C  
ANISOU  701  CD  GLU A  47    12109  16630   7320    306   -861   -721       C  
ATOM    702  OE1 GLU A  47      12.236  -3.307  37.838  1.00 98.56           O  
ANISOU  702  OE1 GLU A  47    12413  17467   7569    497   -747   -899       O  
ATOM    703  OE2 GLU A  47      13.879  -4.746  37.608  1.00 95.95           O  
ANISOU  703  OE2 GLU A  47    12455  16639   7361    172   -986   -468       O  
ATOM    710  N   ASP A  48      13.413  -4.432  32.236  1.00 67.52           N  
ANISOU  710  N   ASP A  48     8532  11795   5327   -288   -623   -403       N  
ATOM    711  CA  ASP A  48      14.709  -4.761  31.650  1.00 63.29           C  
ANISOU  711  CA  ASP A  48     8123  10699   5226   -317   -787   -305       C  
ATOM    712  C   ASP A  48      15.090  -3.796  30.536  1.00 62.99           C  
ANISOU  712  C   ASP A  48     7953  10304   5676   -203   -836   -507       C  
ATOM    713  O   ASP A  48      16.277  -3.504  30.348  1.00 61.48           O  
ANISOU  713  O   ASP A  48     7782   9758   5820   -111  -1038   -555       O  
ATOM    714  CB  ASP A  48      14.696  -6.194  31.111  1.00 59.50           C  
ANISOU  714  CB  ASP A  48     7784  10044   4778   -614   -691     85       C  
ATOM    715  CG  ASP A  48      14.775  -7.239  32.209  1.00 61.54           C  
ANISOU  715  CG  ASP A  48     8235  10487   4660   -754   -764    353       C  
ATOM    716  OD1 ASP A  48      15.401  -6.967  33.255  1.00 62.30           O  
ANISOU  716  OD1 ASP A  48     8402  10675   4595   -589   -942    247       O  
ATOM    717  OD2 ASP A  48      14.215  -8.341  32.019  1.00 61.32           O  
ANISOU  717  OD2 ASP A  48     8301  10494   4505  -1038   -675    684       O  
ATOM    722  N   MET A  49      14.105  -3.293  29.787  1.00 63.99           N  
ANISOU  722  N   MET A  49     7929  10535   5849   -221   -665   -602       N  
ATOM    723  CA  MET A  49      14.398  -2.491  28.604  1.00 62.53           C  
ANISOU  723  CA  MET A  49     7633  10008   6119   -168   -702   -718       C  
ATOM    724  C   MET A  49      15.131  -1.199  28.937  1.00 62.12           C  
ANISOU  724  C   MET A  49     7523   9793   6288     74   -997  -1008       C  
ATOM    725  O   MET A  49      15.792  -0.635  28.058  1.00 61.15           O  
ANISOU  725  O   MET A  49     7325   9318   6590     76  -1100  -1014       O  
ATOM    726  CB  MET A  49      13.103  -2.167  27.856  1.00 62.31           C  
ANISOU  726  CB  MET A  49     7469  10151   6054   -217   -493   -782       C  
ATOM    727  CG  MET A  49      12.537  -3.332  27.059  1.00 62.20           C  
ANISOU  727  CG  MET A  49     7497  10124   6011   -482   -255   -482       C  
ATOM    728  SD  MET A  49      13.643  -3.907  25.753  1.00 64.58           S  
ANISOU  728  SD  MET A  49     7876   9905   6758   -569   -282   -279       S  
ATOM    729  CE  MET A  49      13.754  -2.447  24.720  1.00 61.56           C  
ANISOU  729  CE  MET A  49     7311   9319   6761   -432   -334   -498       C  
ATOM    739  N   LEU A  50      15.034  -0.714  30.176  1.00 60.94           N  
ANISOU  739  N   LEU A  50     7402   9897   5856    275  -1161  -1236       N  
ATOM    740  CA  LEU A  50      15.712   0.529  30.526  1.00 60.72           C  
ANISOU  740  CA  LEU A  50     7344   9669   6057    517  -1520  -1534       C  
ATOM    741  C   LEU A  50      17.223   0.391  30.383  1.00 61.69           C  
ANISOU  741  C   LEU A  50     7512   9377   6551    464  -1731  -1391       C  
ATOM    742  O   LEU A  50      17.894   1.306  29.894  1.00 62.79           O  
ANISOU  742  O   LEU A  50     7562   9185   7111    508  -1968  -1474       O  
ATOM    743  CB  LEU A  50      15.341   0.949  31.948  1.00 64.36           C  
ANISOU  743  CB  LEU A  50     7853  10514   6088    786  -1674  -1825       C  
ATOM    744  CG  LEU A  50      13.932   1.518  32.132  1.00 66.83           C  
ANISOU  744  CG  LEU A  50     8052  11268   6074    956  -1559  -2091       C  
ATOM    745  CD1 LEU A  50      13.628   1.719  33.614  1.00 68.00           C  
ANISOU  745  CD1 LEU A  50     8241  11893   5705   1243  -1669  -2342       C  
ATOM    746  CD2 LEU A  50      13.769   2.829  31.365  1.00 66.65           C  
ANISOU  746  CD2 LEU A  50     7927  10960   6436   1104  -1768  -2371       C  
ATOM    758  N   ASN A  51      17.775  -0.747  30.794  1.00 62.58           N  
ANISOU  758  N   ASN A  51     7748   9508   6522    359  -1669  -1157       N  
ATOM    759  CA  ASN A  51      19.216  -0.956  30.747  1.00 58.89           C  
ANISOU  759  CA  ASN A  51     7302   8704   6369    342  -1872  -1038       C  
ATOM    760  C   ASN A  51      19.495  -2.452  30.676  1.00 54.25           C  
ANISOU  760  C   ASN A  51     6843   8116   5652    179  -1705   -728       C  
ATOM    761  O   ASN A  51      19.902  -3.061  31.674  1.00 54.82           O  
ANISOU  761  O   ASN A  51     7070   8267   5493    213  -1819   -678       O  
ATOM    762  CB  ASN A  51      19.887  -0.328  31.968  1.00 62.05           C  
ANISOU  762  CB  ASN A  51     7765   9093   6718    556  -2240  -1264       C  
ATOM    763  CG  ASN A  51      21.367  -0.076  31.755  1.00 66.91           C  
ANISOU  763  CG  ASN A  51     8313   9323   7787    554  -2520  -1201       C  
ATOM    764  OD1 ASN A  51      21.978  -0.624  30.836  1.00 67.88           O  
ANISOU  764  OD1 ASN A  51     8354   9258   8178    404  -2401   -957       O  
ATOM    765  ND2 ASN A  51      21.953   0.758  32.608  1.00 67.12           N  
ANISOU  765  ND2 ASN A  51     8357   9253   7893    738  -2909  -1430       N  
ATOM    772  N   PRO A  52      19.281  -3.078  29.524  1.00 45.79           N  
ANISOU  772  N   PRO A  52     5734   6945   4718     17  -1473   -526       N  
ATOM    773  CA  PRO A  52      19.403  -4.536  29.447  1.00 46.28           C  
ANISOU  773  CA  PRO A  52     5956   6984   4645   -117  -1367   -259       C  
ATOM    774  C   PRO A  52      20.842  -4.987  29.257  1.00 47.75           C  
ANISOU  774  C   PRO A  52     6152   6884   5108    -65  -1541   -162       C  
ATOM    775  O   PRO A  52      21.621  -4.368  28.529  1.00 49.25           O  
ANISOU  775  O   PRO A  52     6156   6886   5671    -10  -1607   -198       O  
ATOM    776  CB  PRO A  52      18.546  -4.891  28.226  1.00 46.72           C  
ANISOU  776  CB  PRO A  52     5960   7036   4755   -262  -1096   -143       C  
ATOM    777  CG  PRO A  52      18.664  -3.686  27.341  1.00 44.47           C  
ANISOU  777  CG  PRO A  52     5459   6627   4812   -195  -1097   -289       C  
ATOM    778  CD  PRO A  52      18.794  -2.494  28.260  1.00 45.66           C  
ANISOU  778  CD  PRO A  52     5554   6842   4951    -38  -1322   -545       C  
ATOM    786  N   ASN A  53      21.190  -6.072  29.939  1.00 45.21           N  
ANISOU  786  N   ASN A  53     6035   6554   4589    -88  -1631    -22       N  
ATOM    787  CA  ASN A  53      22.417  -6.818  29.677  1.00 45.08           C  
ANISOU  787  CA  ASN A  53     6055   6289   4785    -29  -1777     88       C  
ATOM    788  C   ASN A  53      21.982  -8.109  28.989  1.00 45.02           C  
ANISOU  788  C   ASN A  53     6197   6213   4695   -147  -1644    294       C  
ATOM    789  O   ASN A  53      21.597  -9.077  29.651  1.00 45.14           O  
ANISOU  789  O   ASN A  53     6457   6272   4423   -250  -1697    444       O  
ATOM    790  CB  ASN A  53      23.194  -7.086  30.961  1.00 47.89           C  
ANISOU  790  CB  ASN A  53     6561   6630   5007     64  -2055     71       C  
ATOM    791  CG  ASN A  53      24.572  -7.657  30.695  1.00 51.07           C  
ANISOU  791  CG  ASN A  53     6944   6784   5677    176  -2243    130       C  
ATOM    792  OD1 ASN A  53      24.763  -8.437  29.762  1.00 51.95           O  
ANISOU  792  OD1 ASN A  53     7055   6772   5912    171  -2163    242       O  
ATOM    793  ND2 ASN A  53      25.545  -7.261  31.508  1.00 54.08           N  
ANISOU  793  ND2 ASN A  53     7299   7107   6144    307  -2513     30       N  
ATOM    800  N   TYR A  54      22.030  -8.115  27.654  1.00 45.85           N  
ANISOU  800  N   TYR A  54     6162   6209   5048   -136  -1501    312       N  
ATOM    801  CA  TYR A  54      21.422  -9.207  26.901  1.00 47.17           C  
ANISOU  801  CA  TYR A  54     6475   6307   5141   -232  -1391    462       C  
ATOM    802  C   TYR A  54      22.161 -10.523  27.098  1.00 48.06           C  
ANISOU  802  C   TYR A  54     6811   6219   5231   -167  -1612    580       C  
ATOM    803  O   TYR A  54      21.532 -11.587  27.091  1.00 48.69           O  
ANISOU  803  O   TYR A  54     7130   6228   5142   -296  -1646    737       O  
ATOM    804  CB  TYR A  54      21.352  -8.845  25.419  1.00 46.14           C  
ANISOU  804  CB  TYR A  54     6142   6129   5259   -188  -1205    425       C  
ATOM    805  CG  TYR A  54      20.268  -7.837  25.117  1.00 46.04           C  
ANISOU  805  CG  TYR A  54     5992   6280   5221   -295   -997    348       C  
ATOM    806  CD1 TYR A  54      18.938  -8.227  25.035  1.00 42.34           C  
ANISOU  806  CD1 TYR A  54     5635   5920   4533   -465   -850    416       C  
ATOM    807  CD2 TYR A  54      20.570  -6.495  24.930  1.00 43.63           C  
ANISOU  807  CD2 TYR A  54     5442   6011   5123   -232   -987    213       C  
ATOM    808  CE1 TYR A  54      17.940  -7.313  24.767  1.00 42.49           C  
ANISOU  808  CE1 TYR A  54     5515   6103   4525   -531   -676    320       C  
ATOM    809  CE2 TYR A  54      19.579  -5.572  24.660  1.00 43.05           C  
ANISOU  809  CE2 TYR A  54     5266   6055   5035   -300   -849    119       C  
ATOM    810  CZ  TYR A  54      18.264  -5.988  24.580  1.00 43.15           C  
ANISOU  810  CZ  TYR A  54     5383   6199   4812   -430   -684    156       C  
ATOM    811  OH  TYR A  54      17.270  -5.076  24.313  1.00 41.22           O  
ANISOU  811  OH  TYR A  54     5023   6089   4551   -467   -560     37       O  
ATOM    821  N   GLU A  55      23.482 -10.485  27.276  1.00 53.48           N  
ANISOU  821  N   GLU A  55     7423   6797   6098     28  -1801    513       N  
ATOM    822  CA  GLU A  55      24.217 -11.716  27.546  1.00 61.38           C  
ANISOU  822  CA  GLU A  55     8647   7600   7074    132  -2060    590       C  
ATOM    823  C   GLU A  55      23.771 -12.333  28.867  1.00 60.35           C  
ANISOU  823  C   GLU A  55     8828   7481   6620    -27  -2227    728       C  
ATOM    824  O   GLU A  55      23.486 -13.533  28.941  1.00 62.13           O  
ANISOU  824  O   GLU A  55     9339   7553   6714   -112  -2373    895       O  
ATOM    825  CB  GLU A  55      25.723 -11.445  27.553  1.00 66.54           C  
ANISOU  825  CB  GLU A  55     9109   8192   7981    381  -2228    477       C  
ATOM    826  CG  GLU A  55      26.333 -11.263  26.167  1.00 69.87           C  
ANISOU  826  CG  GLU A  55     9241   8625   8679    559  -2104    411       C  
ATOM    827  CD  GLU A  55      26.060  -9.893  25.566  1.00 72.47           C  
ANISOU  827  CD  GLU A  55     9245   9123   9166    479  -1857    363       C  
ATOM    828  OE1 GLU A  55      25.601  -8.992  26.302  1.00 73.04           O  
ANISOU  828  OE1 GLU A  55     9298   9272   9181    343  -1840    326       O  
ATOM    829  OE2 GLU A  55      26.308  -9.718  24.354  1.00 72.54           O  
ANISOU  829  OE2 GLU A  55     9025   9194   9345    570  -1705    358       O  
ATOM    836  N   ASP A  56      23.691 -11.520  29.924  1.00 54.82           N  
ANISOU  836  N   ASP A  56     8085   6969   5776    -67  -2235    671       N  
ATOM    837  CA  ASP A  56      23.256 -12.035  31.218  1.00 55.68           C  
ANISOU  837  CA  ASP A  56     8462   7179   5517   -210  -2369    818       C  
ATOM    838  C   ASP A  56      21.821 -12.542  31.161  1.00 55.32           C  
ANISOU  838  C   ASP A  56     8546   7281   5194   -494  -2199   1024       C  
ATOM    839  O   ASP A  56      21.504 -13.593  31.732  1.00 53.81           O  
ANISOU  839  O   ASP A  56     8632   7048   4767   -666  -2352   1273       O  
ATOM    840  CB  ASP A  56      23.396 -10.953  32.289  1.00 57.70           C  
ANISOU  840  CB  ASP A  56     8619   7661   5645   -143  -2400    665       C  
ATOM    841  CG  ASP A  56      24.831 -10.761  32.737  1.00 57.20           C  
ANISOU  841  CG  ASP A  56     8519   7433   5783     83  -2681    540       C  
ATOM    842  OD1 ASP A  56      25.721 -11.444  32.190  1.00 57.33           O  
ANISOU  842  OD1 ASP A  56     8550   7198   6033    200  -2822    566       O  
ATOM    843  OD2 ASP A  56      25.069  -9.931  33.638  1.00 58.63           O  
ANISOU  843  OD2 ASP A  56     8648   7744   5885    165  -2782    398       O  
ATOM    848  N   LEU A  57      20.937 -11.811  30.478  1.00 57.31           N  
ANISOU  848  N   LEU A  57     8593   7704   5478   -563  -1906    945       N  
ATOM    849  CA  LEU A  57      19.539 -12.222  30.406  1.00 56.42           C  
ANISOU  849  CA  LEU A  57     8550   7773   5116   -839  -1736   1137       C  
ATOM    850  C   LEU A  57      19.378 -13.503  29.597  1.00 59.38           C  
ANISOU  850  C   LEU A  57     9122   7848   5590   -954  -1839   1338       C  
ATOM    851  O   LEU A  57      18.545 -14.354  29.932  1.00 61.32           O  
ANISOU  851  O   LEU A  57     9555   8137   5604  -1229  -1889   1616       O  
ATOM    852  CB  LEU A  57      18.690 -11.106  29.798  1.00 55.07           C  
ANISOU  852  CB  LEU A  57     8103   7829   4991   -844  -1430    968       C  
ATOM    853  CG  LEU A  57      18.414  -9.882  30.672  1.00 58.24           C  
ANISOU  853  CG  LEU A  57     8342   8577   5208   -760  -1350    772       C  
ATOM    854  CD1 LEU A  57      17.757  -8.784  29.848  1.00 56.04           C  
ANISOU  854  CD1 LEU A  57     7806   8409   5078   -713  -1119    571       C  
ATOM    855  CD2 LEU A  57      17.542 -10.247  31.866  1.00 59.84           C  
ANISOU  855  CD2 LEU A  57     8655   9162   4920   -938  -1325    947       C  
ATOM    867  N   LEU A  58      20.162 -13.657  28.528  1.00 59.01           N  
ANISOU  867  N   LEU A  58     9029   7512   5880   -743  -1894   1208       N  
ATOM    868  CA  LEU A  58      20.007 -14.809  27.648  1.00 61.46           C  
ANISOU  868  CA  LEU A  58     9528   7528   6296   -777  -2023   1327       C  
ATOM    869  C   LEU A  58      20.500 -16.098  28.290  1.00 62.61           C  
ANISOU  869  C   LEU A  58    10024   7404   6361   -808  -2416   1516       C  
ATOM    870  O   LEU A  58      20.082 -17.183  27.873  1.00 62.54           O  
ANISOU  870  O   LEU A  58    10253   7148   6360   -929  -2602   1685       O  
ATOM    871  CB  LEU A  58      20.754 -14.568  26.335  1.00 58.49           C  
ANISOU  871  CB  LEU A  58     8978   6998   6250   -481  -1967   1106       C  
ATOM    872  CG  LEU A  58      20.581 -15.645  25.263  1.00 58.64           C  
ANISOU  872  CG  LEU A  58     9170   6734   6376   -432  -2098   1147       C  
ATOM    873  CD1 LEU A  58      19.122 -15.765  24.854  1.00 58.67           C  
ANISOU  873  CD1 LEU A  58     9211   6806   6274   -723  -1939   1287       C  
ATOM    874  CD2 LEU A  58      21.457 -15.340  24.056  1.00 59.02           C  
ANISOU  874  CD2 LEU A  58     9004   6735   6686    -81  -2027    914       C  
ATOM    886  N   ILE A  59      21.373 -16.003  29.293  1.00 67.55           N  
ANISOU  886  N   ILE A  59    10702   8042   6922   -700  -2590   1490       N  
ATOM    887  CA  ILE A  59      21.918 -17.195  29.928  1.00 69.51           C  
ANISOU  887  CA  ILE A  59    11297   8010   7104   -707  -3004   1661       C  
ATOM    888  C   ILE A  59      20.940 -17.815  30.914  1.00 73.70           C  
ANISOU  888  C   ILE A  59    12071   8653   7279  -1105  -3094   2031       C  
ATOM    889  O   ILE A  59      21.035 -19.016  31.198  1.00 78.76           O  
ANISOU  889  O   ILE A  59    13004   9006   7916  -1208  -3411   2225       O  
ATOM    890  CB  ILE A  59      23.247 -16.846  30.619  1.00 75.71           C  
ANISOU  890  CB  ILE A  59    12034   8772   7959   -433  -3171   1493       C  
ATOM    891  CG1 ILE A  59      24.306 -16.520  29.561  1.00 75.40           C  
ANISOU  891  CG1 ILE A  59    11758   8608   8283    -60  -3147   1200       C  
ATOM    892  CG2 ILE A  59      23.696 -17.977  31.538  1.00 79.60           C  
ANISOU  892  CG2 ILE A  59    12906   9023   8317   -477  -3609   1695       C  
ATOM    893  CD1 ILE A  59      25.571 -15.927  30.125  1.00 76.70           C  
ANISOU  893  CD1 ILE A  59    11765   8814   8564    189  -3255   1022       C  
ATOM    905  N   ARG A  60      20.004 -17.037  31.446  1.00 69.15           N  
ANISOU  905  N   ARG A  60    11322   8512   6440  -1315  -2787   2097       N  
ATOM    906  CA  ARG A  60      18.980 -17.564  32.335  1.00 73.93           C  
ANISOU  906  CA  ARG A  60    12038   9345   6709  -1694  -2769   2440       C  
ATOM    907  C   ARG A  60      17.786 -18.114  31.566  1.00 76.14           C  
ANISOU  907  C   ARG A  60    12286   9587   7056  -1971  -2643   2605       C  
ATOM    908  O   ARG A  60      16.787 -18.500  32.183  1.00 75.65           O  
ANISOU  908  O   ARG A  60    12173   9758   6812  -2284  -2535   2837       O  
ATOM    909  CB  ARG A  60      18.535 -16.478  33.317  1.00 80.45           C  
ANISOU  909  CB  ARG A  60    12657  10728   7182  -1730  -2503   2396       C  
ATOM    910  CG  ARG A  60      19.705 -15.717  33.934  1.00 86.06           C  
ANISOU  910  CG  ARG A  60    13329  11461   7908  -1405  -2605   2129       C  
ATOM    911  CD  ARG A  60      19.297 -14.927  35.165  1.00 93.11           C  
ANISOU  911  CD  ARG A  60    14116  12878   8384  -1429  -2462   2111       C  
ATOM    912  NE  ARG A  60      19.883 -13.589  35.168  1.00 95.93           N  
ANISOU  912  NE  ARG A  60    14223  13331   8893  -1096  -2353   1692       N  
ATOM    913  CZ  ARG A  60      21.161 -13.326  35.430  1.00 98.55           C  
ANISOU  913  CZ  ARG A  60    14582  13436   9426   -823  -2578   1490       C  
ATOM    914  NH1 ARG A  60      22.005 -14.312  35.708  1.00100.20           N  
ANISOU  914  NH1 ARG A  60    15054  13322   9696   -802  -2910   1634       N  
ATOM    915  NH2 ARG A  60      21.597 -12.074  35.408  1.00 98.32           N  
ANISOU  915  NH2 ARG A  60    14314  13487   9557   -572  -2508   1145       N  
ATOM    929  N   LYS A  61      17.877 -18.164  30.238  1.00 83.20           N  
ANISOU  929  N   LYS A  61    13192  10207   8214  -1847  -2674   2485       N  
ATOM    930  CA  LYS A  61      16.843 -18.716  29.376  1.00 82.94           C  
ANISOU  930  CA  LYS A  61    13151  10070   8294  -2066  -2615   2597       C  
ATOM    931  C   LYS A  61      17.356 -19.994  28.728  1.00 81.12           C  
ANISOU  931  C   LYS A  61    13196   9277   8349  -1973  -3007   2592       C  
ATOM    932  O   LYS A  61      18.522 -20.072  28.328  1.00 79.47           O  
ANISOU  932  O   LYS A  61    13093   8789   8315  -1612  -3214   2387       O  
ATOM    933  CB  LYS A  61      16.442 -17.721  28.283  1.00 79.74           C  
ANISOU  933  CB  LYS A  61    12492   9812   7992  -1949  -2295   2380       C  
ATOM    934  CG  LYS A  61      16.012 -16.356  28.791  1.00 76.91           C  
ANISOU  934  CG  LYS A  61    11801   9974   7447  -1939  -1901   2234       C  
ATOM    935  CD  LYS A  61      14.592 -16.384  29.324  1.00 76.13           C  
ANISOU  935  CD  LYS A  61    11615  10284   7026  -2326  -1725   2510       C  
ATOM    936  CE  LYS A  61      14.228 -15.068  29.995  1.00 75.85           C  
ANISOU  936  CE  LYS A  61    11279  10796   6747  -2248  -1398   2329       C  
ATOM    937  NZ  LYS A  61      12.845 -15.085  30.554  1.00 77.04           N  
ANISOU  937  NZ  LYS A  61    11223  11384   6663  -2509  -1170   2483       N  
ATOM    951  N   SER A  62      16.482 -20.988  28.619  1.00 74.12           N  
ANISOU  951  N   SER A  62    12399   8249   7513  -2276  -3131   2787       N  
ATOM    952  CA  SER A  62      16.802 -22.250  27.970  1.00 76.02           C  
ANISOU  952  CA  SER A  62    12910   7960   8015  -2209  -3547   2751       C  
ATOM    953  C   SER A  62      15.910 -22.426  26.747  1.00 73.40           C  
ANISOU  953  C   SER A  62    12538   7522   7831  -2288  -3507   2723       C  
ATOM    954  O   SER A  62      14.992 -21.640  26.500  1.00 69.82           O  
ANISOU  954  O   SER A  62    11843   7409   7278  -2441  -3155   2768       O  
ATOM    955  CB  SER A  62      16.635 -23.426  28.941  1.00 79.33           C  
ANISOU  955  CB  SER A  62    13520   8232   8389  -2512  -3862   3004       C  
ATOM    956  OG  SER A  62      17.198 -24.613  28.409  1.00 81.81           O  
ANISOU  956  OG  SER A  62    14126   8005   8951  -2377  -4332   2899       O  
ATOM    962  N   ASN A  63      16.192 -23.478  25.973  1.00 81.71           N  
ANISOU  962  N   ASN A  63    14484   8744   7816  -2147  -3198   3095       N  
ATOM    963  CA  ASN A  63      15.462 -23.703  24.729  1.00 79.78           C  
ANISOU  963  CA  ASN A  63    14027   8437   7851  -2213  -3132   3024       C  
ATOM    964  C   ASN A  63      13.957 -23.772  24.965  1.00 79.82           C  
ANISOU  964  C   ASN A  63    13962   8576   7791  -2667  -2790   3209       C  
ATOM    965  O   ASN A  63      13.172 -23.276  24.149  1.00 76.60           O  
ANISOU  965  O   ASN A  63    13188   8343   7574  -2716  -2552   3049       O  
ATOM    966  CB  ASN A  63      15.953 -24.985  24.053  1.00 81.11           C  
ANISOU  966  CB  ASN A  63    14422   8132   8265  -2078  -3555   3048       C  
ATOM    967  CG  ASN A  63      17.295 -24.809  23.365  1.00 79.98           C  
ANISOU  967  CG  ASN A  63    14166   7896   8326  -1570  -3786   2778       C  
ATOM    968  OD1 ASN A  63      17.735 -23.688  23.112  1.00 78.07           O  
ANISOU  968  OD1 ASN A  63    13615   7937   8112  -1342  -3617   2562       O  
ATOM    969  ND2 ASN A  63      17.948 -25.922  23.047  1.00 81.51           N  
ANISOU  969  ND2 ASN A  63    14524   7728   8717  -1380  -4091   2724       N  
ATOM    976  N   HIS A  64      13.533 -24.379  26.072  1.00 78.09           N  
ANISOU  976  N   HIS A  64    14058   8279   7334  -2983  -2743   3528       N  
ATOM    977  CA  HIS A  64      12.110 -24.562  26.333  1.00 80.63           C  
ANISOU  977  CA  HIS A  64    14290   8700   7645  -3430  -2397   3747       C  
ATOM    978  C   HIS A  64      11.444 -23.326  26.925  1.00 79.76           C  
ANISOU  978  C   HIS A  64    13948   9069   7287  -3542  -1889   3738       C  
ATOM    979  O   HIS A  64      10.257 -23.386  27.260  1.00 82.32           O  
ANISOU  979  O   HIS A  64    14134   9529   7617  -3877  -1526   3902       O  
ATOM    980  CB  HIS A  64      11.893 -25.762  27.262  1.00 86.13           C  
ANISOU  980  CB  HIS A  64    15312   9150   8265  -3651  -2461   3993       C  
ATOM    981  CG  HIS A  64      12.536 -25.618  28.606  1.00 88.31           C  
ANISOU  981  CG  HIS A  64    15872   9505   8178  -3531  -2426   4036       C  
ATOM    982  ND1 HIS A  64      13.741 -26.209  28.921  1.00 89.33           N  
ANISOU  982  ND1 HIS A  64    16301   9366   8275  -3268  -2839   3976       N  
ATOM    983  CD2 HIS A  64      12.137 -24.960  29.720  1.00 90.16           C  
ANISOU  983  CD2 HIS A  64    16144  10033   8079  -3615  -2039   4119       C  
ATOM    984  CE1 HIS A  64      14.059 -25.918  30.170  1.00 91.64           C  
ANISOU  984  CE1 HIS A  64    16817   9770   8233  -3218  -2742   4028       C  
ATOM    985  NE2 HIS A  64      13.103 -25.161  30.677  1.00 92.11           N  
ANISOU  985  NE2 HIS A  64    16746  10164   8089  -3412  -2257   4115       N  
ATOM    993  N   ASN A  65      12.166 -22.213  27.061  1.00 77.76           N  
ANISOU  993  N   ASN A  65    13598   9079   6869  -3231  -1839   3505       N  
ATOM    994  CA  ASN A  65      11.552 -20.958  27.476  1.00 77.44           C  
ANISOU  994  CA  ASN A  65    13306   9492   6625  -3266  -1373   3416       C  
ATOM    995  C   ASN A  65      10.896 -20.212  26.319  1.00 74.21           C  
ANISOU  995  C   ASN A  65    12355   9304   6535  -3204  -1160   3132       C  
ATOM    996  O   ASN A  65      10.147 -19.260  26.564  1.00 74.31           O  
ANISOU  996  O   ASN A  65    12119   9681   6435  -3273   -748   3072       O  
ATOM    997  CB  ASN A  65      12.596 -20.048  28.133  1.00 77.51           C  
ANISOU  997  CB  ASN A  65    13446   9660   6345  -2953  -1449   3260       C  
ATOM    998  CG  ASN A  65      13.050 -20.560  29.489  1.00 83.54           C  
ANISOU  998  CG  ASN A  65    14608  10277   6856  -2923  -1543   3392       C  
ATOM    999  OD1 ASN A  65      14.196 -20.973  29.655  1.00 82.64           O  
ANISOU  999  OD1 ASN A  65    14710   9916   6771  -2699  -1953   3343       O  
ATOM   1000  ND2 ASN A  65      12.153 -20.525  30.468  1.00 86.68           N  
ANISOU 1000  ND2 ASN A  65    15093  10824   7019  -3126  -1153   3555       N  
ATOM   1007  N   PHE A  66      11.152 -20.616  25.077  1.00 69.57           N  
ANISOU 1007  N   PHE A  66    11617   8496   6322  -3053  -1433   2955       N  
ATOM   1008  CA  PHE A  66      10.644 -19.919  23.902  1.00 68.07           C  
ANISOU 1008  CA  PHE A  66    10982   8467   6414  -2941  -1297   2664       C  
ATOM   1009  C   PHE A  66       9.481 -20.702  23.304  1.00 70.32           C  
ANISOU 1009  C   PHE A  66    11129   8586   7003  -3250  -1290   2778       C  
ATOM   1010  O   PHE A  66       9.638 -21.872  22.939  1.00 72.88           O  
ANISOU 1010  O   PHE A  66    11672   8515   7504  -3317  -1630   2892       O  
ATOM   1011  CB  PHE A  66      11.748 -19.738  22.860  1.00 67.06           C  
ANISOU 1011  CB  PHE A  66    10805   8201   6475  -2517  -1588   2368       C  
ATOM   1012  CG  PHE A  66      12.867 -18.846  23.308  1.00 65.04           C  
ANISOU 1012  CG  PHE A  66    10579   8113   6022  -2218  -1600   2228       C  
ATOM   1013  CD1 PHE A  66      12.778 -17.473  23.153  1.00 62.31           C  
ANISOU 1013  CD1 PHE A  66     9936   8119   5619  -2076  -1329   1995       C  
ATOM   1014  CD2 PHE A  66      14.013 -19.379  23.874  1.00 65.92           C  
ANISOU 1014  CD2 PHE A  66    11010   8004   6032  -2078  -1920   2329       C  
ATOM   1015  CE1 PHE A  66      13.807 -16.648  23.559  1.00 60.12           C  
ANISOU 1015  CE1 PHE A  66     9679   7965   5199  -1824  -1378   1873       C  
ATOM   1016  CE2 PHE A  66      15.047 -18.559  24.283  1.00 64.89           C  
ANISOU 1016  CE2 PHE A  66    10874   8003   5780  -1817  -1981   2202       C  
ATOM   1017  CZ  PHE A  66      14.943 -17.191  24.125  1.00 62.67           C  
ANISOU 1017  CZ  PHE A  66    10292   8065   5455  -1701  -1711   1977       C  
ATOM   1027  N   LEU A  67       8.326 -20.051  23.191  1.00 72.22           N  
ANISOU 1027  N   LEU A  67    11002   9111   7328  -3426   -933   2739       N  
ATOM   1028  CA  LEU A  67       7.125 -20.651  22.613  1.00 76.92           C  
ANISOU 1028  CA  LEU A  67    11376   9577   8275  -3734   -926   2830       C  
ATOM   1029  C   LEU A  67       6.929 -20.063  21.218  1.00 76.14           C  
ANISOU 1029  C   LEU A  67    10951   9508   8469  -3494  -1017   2466       C  
ATOM   1030  O   LEU A  67       6.472 -18.925  21.073  1.00 74.27           O  
ANISOU 1030  O   LEU A  67    10383   9622   8216  -3408   -722   2276       O  
ATOM   1031  CB  LEU A  67       5.908 -20.397  23.498  1.00 83.16           C  
ANISOU 1031  CB  LEU A  67    11953  10646   8998  -4110   -456   3068       C  
ATOM   1032  CG  LEU A  67       4.578 -20.975  23.002  1.00 88.95           C  
ANISOU 1032  CG  LEU A  67    12373  11262  10161  -4477   -425   3195       C  
ATOM   1033  CD1 LEU A  67       4.448 -22.448  23.371  1.00 91.92           C  
ANISOU 1033  CD1 LEU A  67    13060  11229  10638  -4829   -650   3567       C  
ATOM   1034  CD2 LEU A  67       3.399 -20.176  23.543  1.00 90.65           C  
ANISOU 1034  CD2 LEU A  67    12175  11891  10376  -4687    125   3267       C  
ATOM   1046  N   VAL A  68       7.274 -20.842  20.196  1.00 71.71           N  
ANISOU 1046  N   VAL A  68    10529   8563   8153  -3367  -1433   2367       N  
ATOM   1047  CA  VAL A  68       7.068 -20.457  18.804  1.00 67.92           C  
ANISOU 1047  CA  VAL A  68     9843   8030   7934  -3135  -1569   2041       C  
ATOM   1048  C   VAL A  68       5.769 -21.087  18.323  1.00 69.76           C  
ANISOU 1048  C   VAL A  68     9891   8082   8533  -3475  -1677   2134       C  
ATOM   1049  O   VAL A  68       5.574 -22.302  18.454  1.00 70.65           O  
ANISOU 1049  O   VAL A  68    10215   7841   8787  -3734  -1932   2374       O  
ATOM   1050  CB  VAL A  68       8.250 -20.894  17.922  1.00 66.94           C  
ANISOU 1050  CB  VAL A  68    10018   7579   7835  -2739  -1948   1858       C  
ATOM   1051  CG1 VAL A  68       8.045 -20.425  16.489  1.00 64.59           C  
ANISOU 1051  CG1 VAL A  68     9572   7229   7740  -2468  -2049   1521       C  
ATOM   1052  CG2 VAL A  68       9.558 -20.361  18.481  1.00 65.87           C  
ANISOU 1052  CG2 VAL A  68    10023   7595   7411  -2442  -1870   1807       C  
ATOM   1062  N   GLN A  69       4.887 -20.268  17.756  1.00 72.39           N  
ANISOU 1062  N   GLN A  69     9828   8632   9044  -3475  -1516   1943       N  
ATOM   1063  CA  GLN A  69       3.558 -20.711  17.351  1.00 75.37           C  
ANISOU 1063  CA  GLN A  69     9934   8880   9823  -3811  -1607   2022       C  
ATOM   1064  C   GLN A  69       3.285 -20.230  15.935  1.00 73.39           C  
ANISOU 1064  C   GLN A  69     9537   8547   9799  -3541  -1832   1657       C  
ATOM   1065  O   GLN A  69       3.295 -19.023  15.674  1.00 68.56           O  
ANISOU 1065  O   GLN A  69     8711   8258   9081  -3292  -1601   1406       O  
ATOM   1066  CB  GLN A  69       2.497 -20.186  18.323  1.00 79.88           C  
ANISOU 1066  CB  GLN A  69    10102   9837  10410  -4155  -1122   2219       C  
ATOM   1067  CG  GLN A  69       1.078 -20.605  17.997  1.00 85.99           C  
ANISOU 1067  CG  GLN A  69    10498  10503  11669  -4536  -1178   2331       C  
ATOM   1068  CD  GLN A  69       0.135 -20.416  19.170  1.00 90.11           C  
ANISOU 1068  CD  GLN A  69    10686  11346  12206  -4928   -661   2640       C  
ATOM   1069  OE1 GLN A  69       0.534 -20.539  20.329  1.00 90.87           O  
ANISOU 1069  OE1 GLN A  69    11000  11571  11954  -5031   -373   2893       O  
ATOM   1070  NE2 GLN A  69      -1.124 -20.114  18.875  1.00 92.64           N  
ANISOU 1070  NE2 GLN A  69    10484  11787  12929  -5131   -539   2621       N  
ATOM   1079  N   ALA A  70       3.049 -21.173  15.026  1.00 76.25           N  
ANISOU 1079  N   ALA A  70    10064   8455  10455  -3579  -2303   1625       N  
ATOM   1080  CA  ALA A  70       2.734 -20.878  13.630  1.00 75.50           C  
ANISOU 1080  CA  ALA A  70     9923   8194  10568  -3328  -2596   1291       C  
ATOM   1081  C   ALA A  70       1.302 -21.344  13.385  1.00 76.70           C  
ANISOU 1081  C   ALA A  70     9760   8186  11195  -3731  -2786   1393       C  
ATOM   1082  O   ALA A  70       1.056 -22.530  13.148  1.00 80.67           O  
ANISOU 1082  O   ALA A  70    10458   8247  11948  -3953  -3191   1542       O  
ATOM   1083  CB  ALA A  70       3.728 -21.559  12.694  1.00 74.47           C  
ANISOU 1083  CB  ALA A  70    10308   7628  10359  -2965  -3025   1132       C  
ATOM   1089  N   GLY A  71       0.359 -20.409  13.447  1.00 72.56           N  
ANISOU 1089  N   GLY A  71     8738   8007  10823  -3826  -2511   1315       N  
ATOM   1090  CA  GLY A  71      -1.042 -20.794  13.430  1.00 77.47           C  
ANISOU 1090  CA  GLY A  71     8948   8540  11948  -4258  -2616   1462       C  
ATOM   1091  C   GLY A  71      -1.364 -21.573  14.689  1.00 87.66           C  
ANISOU 1091  C   GLY A  71    10152   9854  13301  -4754  -2378   1918       C  
ATOM   1092  O   GLY A  71      -1.109 -21.117  15.810  1.00 89.04           O  
ANISOU 1092  O   GLY A  71    10260  10408  13162  -4811  -1867   2086       O  
ATOM   1096  N   ASN A  72      -1.925 -22.769  14.511  1.00102.73           N  
ANISOU 1096  N   ASN A  72    12102  11328  15604  -5117  -2763   2129       N  
ATOM   1097  CA  ASN A  72      -2.143 -23.707  15.605  1.00109.52           C  
ANISOU 1097  CA  ASN A  72    13005  12130  16476  -5495  -2566   2547       C  
ATOM   1098  C   ASN A  72      -1.121 -24.840  15.588  1.00109.39           C  
ANISOU 1098  C   ASN A  72    13626  11674  16265  -5445  -2952   2662       C  
ATOM   1099  O   ASN A  72      -1.415 -25.957  16.025  1.00115.11           O  
ANISOU 1099  O   ASN A  72    14471  12157  17107  -5689  -3040   2929       O  
ATOM   1100  CB  ASN A  72      -3.568 -24.262  15.555  1.00115.52           C  
ANISOU 1100  CB  ASN A  72    13358  12797  17737  -5770  -2577   2653       C  
ATOM   1101  CG  ASN A  72      -4.087 -24.417  14.139  1.00116.25           C  
ANISOU 1101  CG  ASN A  72    13409  12571  18189  -5585  -3129   2345       C  
ATOM   1102  OD1 ASN A  72      -3.366 -24.863  13.248  1.00115.00           O  
ANISOU 1102  OD1 ASN A  72    13724  12040  17933  -5316  -3637   2166       O  
ATOM   1103  ND2 ASN A  72      -5.337 -24.027  13.919  1.00118.35           N  
ANISOU 1103  ND2 ASN A  72    13137  12984  18847  -5687  -3020   2268       N  
ATOM   1110  N   VAL A  73       0.081 -24.565  15.090  1.00101.15           N  
ANISOU 1110  N   VAL A  73    12991  10557  14885  -5020  -3132   2420       N  
ATOM   1111  CA  VAL A  73       1.139 -25.558  14.963  1.00101.00           C  
ANISOU 1111  CA  VAL A  73    13581  10122  14674  -4860  -3503   2465       C  
ATOM   1112  C   VAL A  73       2.332 -25.065  15.768  1.00 96.32           C  
ANISOU 1112  C   VAL A  73    13209   9834  13554  -4584  -3148   2479       C  
ATOM   1113  O   VAL A  73       3.039 -24.143  15.342  1.00 89.79           O  
ANISOU 1113  O   VAL A  73    12404   9232  12480  -4131  -3033   2170       O  
ATOM   1114  CB  VAL A  73       1.522 -25.790  13.496  1.00 99.79           C  
ANISOU 1114  CB  VAL A  73    13743   9571  14601  -4455  -4052   2107       C  
ATOM   1115  CG1 VAL A  73       2.837 -26.551  13.392  1.00 98.35           C  
ANISOU 1115  CG1 VAL A  73    14177   9065  14127  -4145  -4317   2094       C  
ATOM   1116  CG2 VAL A  73       0.404 -26.522  12.768  1.00104.76           C  
ANISOU 1116  CG2 VAL A  73    14244   9879  15681  -4625  -4443   2097       C  
ATOM   1127  N   GLN A  74       2.562 -25.675  16.926  1.00 94.63           N  
ANISOU 1127  N   GLN A  74    13173   9607  13177  -4859  -2996   2840       N  
ATOM   1128  CA  GLN A  74       3.688 -25.301  17.767  1.00 92.09           C  
ANISOU 1128  CA  GLN A  74    13094   9522  12374  -4622  -2734   2876       C  
ATOM   1129  C   GLN A  74       4.988 -25.862  17.207  1.00 88.13           C  
ANISOU 1129  C   GLN A  74    13097   8675  11714  -4209  -3145   2720       C  
ATOM   1130  O   GLN A  74       5.053 -27.020  16.785  1.00 90.85           O  
ANISOU 1130  O   GLN A  74    13763   8524  12232  -4277  -3599   2800       O  
ATOM   1131  CB  GLN A  74       3.490 -25.819  19.190  1.00 99.04           C  
ANISOU 1131  CB  GLN A  74    14066  10458  13107  -5040  -2470   3322       C  
ATOM   1132  CG  GLN A  74       2.850 -24.844  20.165  1.00102.05           C  
ANISOU 1132  CG  GLN A  74    14063  11373  13338  -5227  -1843   3444       C  
ATOM   1133  CD  GLN A  74       1.488 -24.342  19.711  1.00104.80           C  
ANISOU 1133  CD  GLN A  74    13829  11902  14090  -5447  -1665   3381       C  
ATOM   1134  OE1 GLN A  74       1.147 -23.188  19.945  1.00103.36           O  
ANISOU 1134  OE1 GLN A  74    13291  12177  13803  -5353  -1240   3254       O  
ATOM   1135  NE2 GLN A  74       0.703 -25.203  19.071  1.00108.54           N  
ANISOU 1135  NE2 GLN A  74    14201  11997  15041  -5736  -2017   3465       N  
ATOM   1144  N   LEU A  75       6.024 -25.035  17.213  1.00 84.20           N  
ANISOU 1144  N   LEU A  75    12660   8428  10904  -3776  -2983   2503       N  
ATOM   1145  CA  LEU A  75       7.364 -25.468  16.853  1.00 85.49           C  
ANISOU 1145  CA  LEU A  75    13245   8330  10908  -3360  -3277   2381       C  
ATOM   1146  C   LEU A  75       8.186 -25.667  18.122  1.00 85.03           C  
ANISOU 1146  C   LEU A  75    13419   8354  10535  -3395  -3157   2624       C  
ATOM   1147  O   LEU A  75       7.887 -25.110  19.181  1.00 86.07           O  
ANISOU 1147  O   LEU A  75    13384   8837  10481  -3616  -2776   2794       O  
ATOM   1148  CB  LEU A  75       8.043 -24.452  15.929  1.00 84.85           C  
ANISOU 1148  CB  LEU A  75    13069   8428  10744  -2839  -3204   1983       C  
ATOM   1149  CG  LEU A  75       7.545 -24.363  14.479  1.00 84.85           C  
ANISOU 1149  CG  LEU A  75    13012   8238  10987  -2658  -3430   1692       C  
ATOM   1150  CD1 LEU A  75       6.027 -24.484  14.361  1.00 86.79           C  
ANISOU 1150  CD1 LEU A  75    12963   8465  11548  -3094  -3461   1783       C  
ATOM   1151  CD2 LEU A  75       8.015 -23.054  13.856  1.00 80.84           C  
ANISOU 1151  CD2 LEU A  75    12324   8047  10346  -2234  -3180   1357       C  
ATOM   1163  N   ARG A  76       9.228 -26.478  18.001  1.00 79.20           N  
ANISOU 1163  N   ARG A  76    13097   7268   9729  -3150  -3503   2632       N  
ATOM   1164  CA  ARG A  76      10.052 -26.886  19.130  1.00 80.83           C  
ANISOU 1164  CA  ARG A  76    13602   7438   9672  -3167  -3524   2866       C  
ATOM   1165  C   ARG A  76      11.448 -26.309  18.945  1.00 77.08           C  
ANISOU 1165  C   ARG A  76    13185   7069   9032  -2638  -3539   2625       C  
ATOM   1166  O   ARG A  76      12.101 -26.586  17.936  1.00 76.67           O  
ANISOU 1166  O   ARG A  76    13260   6770   9100  -2256  -3796   2403       O  
ATOM   1167  CB  ARG A  76      10.104 -28.410  19.213  1.00 86.35           C  
ANISOU 1167  CB  ARG A  76    14741   7597  10472  -3339  -3961   3105       C  
ATOM   1168  CG  ARG A  76      10.606 -28.975  20.520  1.00 91.27           C  
ANISOU 1168  CG  ARG A  76    15701   8141  10836  -3498  -3992   3433       C  
ATOM   1169  CD  ARG A  76      10.808 -30.479  20.395  1.00 96.97           C  
ANISOU 1169  CD  ARG A  76    16746   8432  11668  -3486  -4405   3464       C  
ATOM   1170  NE  ARG A  76       9.531 -31.186  20.323  1.00102.07           N  
ANISOU 1170  NE  ARG A  76    17305   8934  12544  -3933  -4438   3635       N  
ATOM   1171  CZ  ARG A  76       8.913 -31.727  21.370  1.00103.33           C  
ANISOU 1171  CZ  ARG A  76    17495   9130  12635  -4334  -4282   3941       C  
ATOM   1172  NH1 ARG A  76       7.753 -32.346  21.209  1.00100.60           N  
ANISOU 1172  NH1 ARG A  76    17009   8657  12557  -4709  -4307   4083       N  
ATOM   1173  NH2 ARG A  76       9.455 -31.660  22.579  1.00 97.46           N  
ANISOU 1173  NH2 ARG A  76    16924   8542  11565  -4338  -4103   4096       N  
ATOM   1187  N   VAL A  77      11.904 -25.514  19.911  1.00 71.38           N  
ANISOU 1187  N   VAL A  77    12376   6698   8047  -2607  -3267   2672       N  
ATOM   1188  CA  VAL A  77      13.228 -24.904  19.829  1.00 68.40           C  
ANISOU 1188  CA  VAL A  77    11994   6431   7562  -2144  -3283   2467       C  
ATOM   1189  C   VAL A  77      14.254 -25.913  20.327  1.00 70.94           C  
ANISOU 1189  C   VAL A  77    12732   6406   7816  -2015  -3650   2623       C  
ATOM   1190  O   VAL A  77      14.225 -26.319  21.493  1.00 73.74           O  
ANISOU 1190  O   VAL A  77    13317   6728   7972  -2271  -3682   2909       O  
ATOM   1191  CB  VAL A  77      13.299 -23.601  20.639  1.00 66.63           C  
ANISOU 1191  CB  VAL A  77    11519   6693   7104  -2157  -2901   2434       C  
ATOM   1192  CG1 VAL A  77      14.574 -22.832  20.298  1.00 62.98           C  
ANISOU 1192  CG1 VAL A  77    10950   6343   6634  -1683  -2915   2178       C  
ATOM   1193  CG2 VAL A  77      12.067 -22.745  20.387  1.00 64.92           C  
ANISOU 1193  CG2 VAL A  77    10928   6804   6934  -2372  -2535   2352       C  
ATOM   1203  N   ILE A  78      15.162 -26.320  19.441  1.00 73.40           N  
ANISOU 1203  N   ILE A  78    13159   6448   8284  -1598  -3922   2437       N  
ATOM   1204  CA  ILE A  78      16.230 -27.253  19.778  1.00 74.67           C  
ANISOU 1204  CA  ILE A  78    13665   6275   8430  -1389  -4282   2524       C  
ATOM   1205  C   ILE A  78      17.591 -26.569  19.775  1.00 71.87           C  
ANISOU 1205  C   ILE A  78    13151   6077   8079   -931  -4248   2325       C  
ATOM   1206  O   ILE A  78      18.620 -27.239  19.918  1.00 73.27           O  
ANISOU 1206  O   ILE A  78    13431   6075   8335   -676  -4438   2248       O  
ATOM   1207  CB  ILE A  78      16.219 -28.464  18.832  1.00 75.60           C  
ANISOU 1207  CB  ILE A  78    13971   5984   8768  -1259  -4565   2397       C  
ATOM   1208  CG1 ILE A  78      16.606 -28.035  17.414  1.00 75.36           C  
ANISOU 1208  CG1 ILE A  78    13804   5925   8903   -811  -4534   2074       C  
ATOM   1209  CG2 ILE A  78      14.841 -29.108  18.829  1.00 77.97           C  
ANISOU 1209  CG2 ILE A  78    14381   6119   9124  -1742  -4631   2595       C  
ATOM   1210  CD1 ILE A  78      16.295 -29.069  16.345  1.00 77.39           C  
ANISOU 1210  CD1 ILE A  78    14253   5826   9327   -722  -4768   1922       C  
ATOM   1222  N   GLY A  79      17.620 -25.248  19.627  1.00 66.77           N  
ANISOU 1222  N   GLY A  79    12150   5820   7399   -836  -3930   2168       N  
ATOM   1223  CA  GLY A  79      18.853 -24.488  19.636  1.00 65.93           C  
ANISOU 1223  CA  GLY A  79    11846   5868   7337   -449  -3889   2006       C  
ATOM   1224  C   GLY A  79      18.578 -23.004  19.513  1.00 62.79           C  
ANISOU 1224  C   GLY A  79    11043   5922   6892   -455  -3485   1831       C  
ATOM   1225  O   GLY A  79      17.692 -22.599  18.756  1.00 59.73           O  
ANISOU 1225  O   GLY A  79    10489   5656   6549   -539  -3260   1707       O  
ATOM   1229  N   HIS A  80      19.313 -22.183  20.261  1.00 67.33           N  
ANISOU 1229  N   HIS A  80    11474   6724   7382   -368  -3425   1818       N  
ATOM   1230  CA  HIS A  80      19.138 -20.739  20.223  1.00 63.76           C  
ANISOU 1230  CA  HIS A  80    10669   6680   6878   -363  -3076   1654       C  
ATOM   1231  C   HIS A  80      20.501 -20.068  20.284  1.00 63.82           C  
ANISOU 1231  C   HIS A  80    10478   6753   7017    -17  -3131   1531       C  
ATOM   1232  O   HIS A  80      21.429 -20.568  20.925  1.00 64.39           O  
ANISOU 1232  O   HIS A  80    10698   6646   7122     96  -3438   1638       O  
ATOM   1233  CB  HIS A  80      18.262 -20.238  21.380  1.00 64.53           C  
ANISOU 1233  CB  HIS A  80    10802   7051   6665   -755  -2896   1808       C  
ATOM   1234  CG  HIS A  80      18.916 -20.342  22.724  1.00 67.73           C  
ANISOU 1234  CG  HIS A  80    11434   7434   6864   -807  -3103   1987       C  
ATOM   1235  ND1 HIS A  80      18.837 -21.475  23.506  1.00 72.91           N  
ANISOU 1235  ND1 HIS A  80    12496   7827   7379   -994  -3365   2256       N  
ATOM   1236  CD2 HIS A  80      19.657 -19.452  23.426  1.00 67.26           C  
ANISOU 1236  CD2 HIS A  80    11290   7555   6712   -693  -3122   1935       C  
ATOM   1237  CE1 HIS A  80      19.503 -21.279  24.630  1.00 73.52           C  
ANISOU 1237  CE1 HIS A  80    12750   7926   7260   -976  -3535   2358       C  
ATOM   1238  NE2 HIS A  80      20.010 -20.060  24.607  1.00 71.42           N  
ANISOU 1238  NE2 HIS A  80    12186   7923   7027   -795  -3410   2161       N  
ATOM   1246  N   SER A  81      20.615 -18.929  19.609  1.00 64.12           N  
ANISOU 1246  N   SER A  81    10174   7033   7157    144  -2847   1312       N  
ATOM   1247  CA  SER A  81      21.851 -18.164  19.631  1.00 61.86           C  
ANISOU 1247  CA  SER A  81     9633   6825   7047    434  -2859   1202       C  
ATOM   1248  C   SER A  81      21.533 -16.719  19.289  1.00 61.09           C  
ANISOU 1248  C   SER A  81     9215   7070   6925    426  -2500   1021       C  
ATOM   1249  O   SER A  81      20.545 -16.428  18.609  1.00 59.42           O  
ANISOU 1249  O   SER A  81     8954   6974   6651    332  -2248    926       O  
ATOM   1250  CB  SER A  81      22.887 -18.735  18.655  1.00 60.11           C  
ANISOU 1250  CB  SER A  81     9348   6334   7158    849  -2966   1113       C  
ATOM   1251  OG  SER A  81      22.377 -18.782  17.336  1.00 62.61           O  
ANISOU 1251  OG  SER A  81     9634   6606   7549    978  -2741    963       O  
ATOM   1257  N   MET A  82      22.378 -15.820  19.775  1.00 56.20           N  
ANISOU 1257  N   MET A  82     8390   6590   6374    526  -2517    973       N  
ATOM   1258  CA  MET A  82      22.211 -14.391  19.558  1.00 56.64           C  
ANISOU 1258  CA  MET A  82     8161   6946   6414    525  -2221    810       C  
ATOM   1259  C   MET A  82      23.206 -13.937  18.499  1.00 57.75           C  
ANISOU 1259  C   MET A  82     7995   7034   6914    881  -2100    655       C  
ATOM   1260  O   MET A  82      24.417 -14.122  18.660  1.00 60.29           O  
ANISOU 1260  O   MET A  82     8202   7211   7495   1088  -2300    690       O  
ATOM   1261  CB  MET A  82      22.418 -13.629  20.866  1.00 56.60           C  
ANISOU 1261  CB  MET A  82     8167   7116   6223    369  -2333    866       C  
ATOM   1262  CG  MET A  82      22.081 -12.153  20.795  1.00 54.50           C  
ANISOU 1262  CG  MET A  82     7674   7155   5877    325  -2052    706       C  
ATOM   1263  SD  MET A  82      22.131 -11.379  22.421  1.00 58.24           S  
ANISOU 1263  SD  MET A  82     8293   7798   6037    133  -2218    774       S  
ATOM   1264  CE  MET A  82      23.856 -11.586  22.858  1.00 59.36           C  
ANISOU 1264  CE  MET A  82     8352   7696   6507    358  -2669    824       C  
ATOM   1274  N   GLN A  83      22.695 -13.367  17.411  1.00 61.51           N  
ANISOU 1274  N   GLN A  83     8343   7613   7416    959  -1770    495       N  
ATOM   1275  CA  GLN A  83      23.526 -12.741  16.388  1.00 63.24           C  
ANISOU 1275  CA  GLN A  83     8285   7818   7926   1276  -1559    355       C  
ATOM   1276  C   GLN A  83      23.206 -11.253  16.380  1.00 56.86           C  
ANISOU 1276  C   GLN A  83     7265   7299   7041   1184  -1302    229       C  
ATOM   1277  O   GLN A  83      22.152 -10.842  15.883  1.00 54.66           O  
ANISOU 1277  O   GLN A  83     7037   7153   6577   1088  -1081    128       O  
ATOM   1278  CB  GLN A  83      23.292 -13.356  15.010  1.00 66.43           C  
ANISOU 1278  CB  GLN A  83     8796   8040   8404   1506  -1400    267       C  
ATOM   1279  CG  GLN A  83      24.279 -12.848  13.966  1.00 68.59           C  
ANISOU 1279  CG  GLN A  83     8827   8261   8972   1876  -1149    159       C  
ATOM   1280  CD  GLN A  83      23.991 -13.358  12.568  1.00 69.16           C  
ANISOU 1280  CD  GLN A  83     9083   8151   9042   2135   -965     54       C  
ATOM   1281  OE1 GLN A  83      22.922 -13.907  12.299  1.00 70.00           O  
ANISOU 1281  OE1 GLN A  83     9468   8194   8934   2009  -1028     30       O  
ATOM   1282  NE2 GLN A  83      24.950 -13.175  11.665  1.00 69.33           N  
ANISOU 1282  NE2 GLN A  83     8957   8072   9312   2506   -736     -4       N  
ATOM   1291  N   ASN A  84      24.113 -10.450  16.931  1.00 50.00           N  
ANISOU 1291  N   ASN A  84     6162   6505   6329   1217  -1367    232       N  
ATOM   1292  CA  ASN A  84      23.939  -8.999  17.017  1.00 48.78           C  
ANISOU 1292  CA  ASN A  84     5823   6593   6121   1135  -1176    118       C  
ATOM   1293  C   ASN A  84      22.646  -8.743  17.780  1.00 46.93           C  
ANISOU 1293  C   ASN A  84     5795   6565   5470    828  -1166    119       C  
ATOM   1294  O   ASN A  84      22.569  -9.117  18.962  1.00 48.42           O  
ANISOU 1294  O   ASN A  84     6159   6760   5480    651  -1418    244       O  
ATOM   1295  CB  ASN A  84      24.017  -8.412  15.607  1.00 48.14           C  
ANISOU 1295  CB  ASN A  84     5574   6515   6203   1356   -810    -25       C  
ATOM   1296  CG  ASN A  84      25.369  -8.634  14.959  1.00 47.56           C  
ANISOU 1296  CG  ASN A  84     5272   6248   6551   1668   -767      3       C  
ATOM   1297  OD1 ASN A  84      26.410  -8.358  15.556  1.00 49.64           O  
ANISOU 1297  OD1 ASN A  84     5301   6479   7080   1698   -939     69       O  
ATOM   1298  ND2 ASN A  84      25.360  -9.148  13.736  1.00 47.87           N  
ANISOU 1298  ND2 ASN A  84     5381   6143   6663   1917   -546    -47       N  
ATOM   1305  N   CYS A  85      21.621  -8.143  17.176  1.00 43.43           N  
ANISOU 1305  N   CYS A  85     5353   6283   4865    771   -885    -10       N  
ATOM   1306  CA  CYS A  85      20.410  -7.787  17.902  1.00 44.72           C  
ANISOU 1306  CA  CYS A  85     5649   6667   4676    504   -830    -15       C  
ATOM   1307  C   CYS A  85      19.225  -8.691  17.582  1.00 43.93           C  
ANISOU 1307  C   CYS A  85     5727   6535   4430    376   -774     24       C  
ATOM   1308  O   CYS A  85      18.109  -8.401  18.023  1.00 42.15           O  
ANISOU 1308  O   CYS A  85     5555   6500   3959    165   -664     17       O  
ATOM   1309  CB  CYS A  85      20.049  -6.326  17.626  1.00 43.91           C  
ANISOU 1309  CB  CYS A  85     5392   6787   4507    512   -588   -192       C  
ATOM   1310  SG  CYS A  85      21.250  -5.165  18.307  1.00 40.72           S  
ANISOU 1310  SG  CYS A  85     4809   6427   4237    565   -715   -218       S  
ATOM   1316  N   VAL A  86      19.433  -9.786  16.850  1.00 42.15           N  
ANISOU 1316  N   VAL A  86     5590   6062   4364    499   -857     69       N  
ATOM   1317  CA  VAL A  86      18.361 -10.733  16.567  1.00 44.44           C  
ANISOU 1317  CA  VAL A  86     6061   6266   4560    358   -877    120       C  
ATOM   1318  C   VAL A  86      18.662 -12.046  17.274  1.00 48.19           C  
ANISOU 1318  C   VAL A  86     6753   6529   5028    264  -1168    333       C  
ATOM   1319  O   VAL A  86      19.821 -12.444  17.439  1.00 48.19           O  
ANISOU 1319  O   VAL A  86     6764   6362   5185    433  -1356    395       O  
ATOM   1320  CB  VAL A  86      18.156 -10.978  15.056  1.00 44.47           C  
ANISOU 1320  CB  VAL A  86     6080   6108   4707    574   -773    -20       C  
ATOM   1321  CG1 VAL A  86      17.897  -9.664  14.327  1.00 42.24           C  
ANISOU 1321  CG1 VAL A  86     5626   6006   4415    685   -497   -225       C  
ATOM   1322  CG2 VAL A  86      19.344 -11.722  14.463  1.00 45.51           C  
ANISOU 1322  CG2 VAL A  86     6266   5955   5071    874   -889      6       C  
ATOM   1332  N   LEU A  87      17.597 -12.719  17.693  1.00 49.52           N  
ANISOU 1332  N   LEU A  87     7085   6695   5034    -10  -1206    452       N  
ATOM   1333  CA  LEU A  87      17.680 -14.054  18.265  1.00 51.64           C  
ANISOU 1333  CA  LEU A  87     7612   6730   5280   -134  -1474    669       C  
ATOM   1334  C   LEU A  87      17.353 -15.065  17.174  1.00 52.88           C  
ANISOU 1334  C   LEU A  87     7890   6607   5595    -53  -1563    646       C  
ATOM   1335  O   LEU A  87      16.354 -14.915  16.463  1.00 50.06           O  
ANISOU 1335  O   LEU A  87     7484   6295   5244   -123  -1428    548       O  
ATOM   1336  CB  LEU A  87      16.714 -14.201  19.440  1.00 52.35           C  
ANISOU 1336  CB  LEU A  87     7829   6965   5097   -507  -1440    850       C  
ATOM   1337  CG  LEU A  87      17.232 -14.881  20.707  1.00 56.27           C  
ANISOU 1337  CG  LEU A  87     8586   7351   5443   -626  -1686   1085       C  
ATOM   1338  CD1 LEU A  87      18.461 -14.165  21.249  1.00 55.32           C  
ANISOU 1338  CD1 LEU A  87     8404   7287   5330   -432  -1803   1033       C  
ATOM   1339  CD2 LEU A  87      16.128 -14.924  21.755  1.00 58.65           C  
ANISOU 1339  CD2 LEU A  87     9023   7820   5442   -988  -1544   1263       C  
ATOM   1351  N   LYS A  88      18.202 -16.077  17.033  1.00 55.83           N  
ANISOU 1351  N   LYS A  88     8435   6674   6103    117  -1818    725       N  
ATOM   1352  CA  LYS A  88      18.007 -17.138  16.052  1.00 54.07           C  
ANISOU 1352  CA  LYS A  88     8404   6130   6011    230  -1960    705       C  
ATOM   1353  C   LYS A  88      17.562 -18.392  16.796  1.00 56.00           C  
ANISOU 1353  C   LYS A  88     8934   6165   6179    -49  -2229    947       C  
ATOM   1354  O   LYS A  88      18.354 -19.008  17.517  1.00 57.10           O  
ANISOU 1354  O   LYS A  88     9227   6157   6313    -16  -2459   1096       O  
ATOM   1355  CB  LYS A  88      19.283 -17.379  15.250  1.00 58.45           C  
ANISOU 1355  CB  LYS A  88     8962   6468   6777    671  -2025    606       C  
ATOM   1356  CG  LYS A  88      19.703 -16.174  14.411  1.00 60.48           C  
ANISOU 1356  CG  LYS A  88     8954   6901   7125    941  -1719    390       C  
ATOM   1357  CD  LYS A  88      20.447 -16.584  13.150  1.00 61.48           C  
ANISOU 1357  CD  LYS A  88     9157   6767   7437   1372  -1692    269       C  
ATOM   1358  CE  LYS A  88      21.932 -16.769  13.400  1.00 63.34           C  
ANISOU 1358  CE  LYS A  88     9285   6901   7880   1651  -1768    324       C  
ATOM   1359  NZ  LYS A  88      22.605 -17.374  12.218  1.00 65.48           N  
ANISOU 1359  NZ  LYS A  88     9676   6887   8317   2088  -1730    233       N  
ATOM   1373  N   LEU A  89      16.292 -18.757  16.629  1.00 52.88           N  
ANISOU 1373  N   LEU A  89     8603   5745   5744   -330  -2212    995       N  
ATOM   1374  CA  LEU A  89      15.711 -19.924  17.281  1.00 54.92           C  
ANISOU 1374  CA  LEU A  89     9118   5795   5952   -652  -2431   1247       C  
ATOM   1375  C   LEU A  89      15.723 -21.089  16.297  1.00 58.30           C  
ANISOU 1375  C   LEU A  89     9797   5798   6556   -511  -2713   1219       C  
ATOM   1376  O   LEU A  89      14.924 -21.122  15.354  1.00 58.14           O  
ANISOU 1376  O   LEU A  89     9753   5703   6633   -526  -2697   1095       O  
ATOM   1377  CB  LEU A  89      14.290 -19.631  17.758  1.00 54.41           C  
ANISOU 1377  CB  LEU A  89     8933   5953   5787  -1074  -2231   1344       C  
ATOM   1378  CG  LEU A  89      14.109 -18.447  18.707  1.00 54.33           C  
ANISOU 1378  CG  LEU A  89     8711   6367   5564  -1203  -1924   1355       C  
ATOM   1379  CD1 LEU A  89      12.640 -18.282  19.066  1.00 57.82           C  
ANISOU 1379  CD1 LEU A  89     9021   7001   5948  -1589  -1701   1455       C  
ATOM   1380  CD2 LEU A  89      14.955 -18.625  19.959  1.00 53.86           C  
ANISOU 1380  CD2 LEU A  89     8841   6307   5314  -1226  -2038   1540       C  
ATOM   1392  N   LYS A  90      16.633 -22.036  16.513  1.00 64.26           N  
ANISOU 1392  N   LYS A  90    10813   6254   7351   -356  -3001   1324       N  
ATOM   1393  CA  LYS A  90      16.666 -23.253  15.713  1.00 66.71           C  
ANISOU 1393  CA  LYS A  90    11432   6118   7797   -221  -3311   1318       C  
ATOM   1394  C   LYS A  90      15.523 -24.162  16.141  1.00 67.92           C  
ANISOU 1394  C   LYS A  90    11781   6093   7933   -680  -3488   1543       C  
ATOM   1395  O   LYS A  90      15.377 -24.472  17.327  1.00 71.08           O  
ANISOU 1395  O   LYS A  90    12269   6531   8206   -992  -3526   1801       O  
ATOM   1396  CB  LYS A  90      18.010 -23.964  15.882  1.00 72.39           C  
ANISOU 1396  CB  LYS A  90    12357   6577   8572    103  -3564   1363       C  
ATOM   1397  CG  LYS A  90      18.136 -25.288  15.127  1.00 79.27           C  
ANISOU 1397  CG  LYS A  90    13606   6952   9559    285  -3912   1358       C  
ATOM   1398  CD  LYS A  90      18.290 -25.073  13.628  1.00 81.37           C  
ANISOU 1398  CD  LYS A  90    13868   7115   9934    696  -3820   1073       C  
ATOM   1399  CE  LYS A  90      19.494 -25.832  13.084  1.00 85.50           C  
ANISOU 1399  CE  LYS A  90    14488   7438  10562   1127  -3878    920       C  
ATOM   1400  NZ  LYS A  90      19.827 -25.439  11.685  1.00 84.50           N  
ANISOU 1400  NZ  LYS A  90    14291   7333  10483   1542  -3636    628       N  
ATOM   1414  N   VAL A  91      14.710 -24.587  15.176  1.00 61.55           N  
ANISOU 1414  N   VAL A  91    11056   5071   7259   -724  -3604   1455       N  
ATOM   1415  CA  VAL A  91      13.518 -25.375  15.455  1.00 64.57           C  
ANISOU 1415  CA  VAL A  91    11551   5278   7705  -1189  -3765   1661       C  
ATOM   1416  C   VAL A  91      13.619 -26.710  14.723  1.00 67.46           C  
ANISOU 1416  C   VAL A  91    12328   5093   8211  -1071  -4211   1664       C  
ATOM   1417  O   VAL A  91      14.509 -26.932  13.903  1.00 66.96           O  
ANISOU 1417  O   VAL A  91    12447   4817   8177   -601  -4346   1475       O  
ATOM   1418  CB  VAL A  91      12.227 -24.630  15.068  1.00 63.34           C  
ANISOU 1418  CB  VAL A  91    11074   5362   7629  -1436  -3542   1570       C  
ATOM   1419  CG1 VAL A  91      12.044 -23.408  15.949  1.00 61.16           C  
ANISOU 1419  CG1 VAL A  91    10440   5607   7190  -1586  -3115   1601       C  
ATOM   1420  CG2 VAL A  91      12.255 -24.230  13.599  1.00 61.38           C  
ANISOU 1420  CG2 VAL A  91    10805   5031   7484  -1060  -3569   1235       C  
ATOM   1430  N   ASP A  92      12.680 -27.606  15.039  1.00 74.88           N  
ANISOU 1430  N   ASP A  92    12679   6044   9727     -7  -3745   2296       N  
ATOM   1431  CA  ASP A  92      12.721 -28.959  14.495  1.00 80.53           C  
ANISOU 1431  CA  ASP A  92    13450   6384  10763    114  -4011   2225       C  
ATOM   1432  C   ASP A  92      12.168 -29.047  13.079  1.00 81.30           C  
ANISOU 1432  C   ASP A  92    13508   6380  11001    283  -3916   1949       C  
ATOM   1433  O   ASP A  92      12.623 -29.891  12.299  1.00 82.67           O  
ANISOU 1433  O   ASP A  92    13677   6286  11448    551  -4097   1747       O  
ATOM   1434  CB  ASP A  92      11.945 -29.920  15.401  1.00 85.22           C  
ANISOU 1434  CB  ASP A  92    14246   6810  11323   -241  -4171   2517       C  
ATOM   1435  CG  ASP A  92      10.548 -29.421  15.728  1.00 83.43           C  
ANISOU 1435  CG  ASP A  92    14081   6773  10846   -606  -3887   2675       C  
ATOM   1436  OD1 ASP A  92      10.222 -28.273  15.362  1.00 78.18           O  
ANISOU 1436  OD1 ASP A  92    13314   6377  10015   -595  -3586   2567       O  
ATOM   1437  OD2 ASP A  92       9.776 -30.178  16.354  1.00 87.78           O  
ANISOU 1437  OD2 ASP A  92    14766   7199  11386   -903  -3956   2917       O  
ATOM   1442  N   THR A  93      11.193 -28.212  12.728  1.00 75.63           N  
ANISOU 1442  N   THR A  93    12776   5858  10102    134  -3649   1922       N  
ATOM   1443  CA  THR A  93      10.518 -28.295  11.441  1.00 74.68           C  
ANISOU 1443  CA  THR A  93    12658   5631  10087    238  -3599   1678       C  
ATOM   1444  C   THR A  93      10.972 -27.176  10.515  1.00 69.66           C  
ANISOU 1444  C   THR A  93    11896   5208   9364    527  -3373   1421       C  
ATOM   1445  O   THR A  93      10.974 -26.003  10.903  1.00 64.53           O  
ANISOU 1445  O   THR A  93    11161   4862   8495    445  -3149   1503       O  
ATOM   1446  CB  THR A  93       9.003 -28.215  11.621  1.00 72.92           C  
ANISOU 1446  CB  THR A  93    12486   5436   9783   -148  -3492   1838       C  
ATOM   1447  OG1 THR A  93       8.575 -29.221  12.546  1.00 76.12           O  
ANISOU 1447  OG1 THR A  93    12998   5670  10255   -432  -3665   2114       O  
ATOM   1448  CG2 THR A  93       8.301 -28.415  10.295  1.00 71.57           C  
ANISOU 1448  CG2 THR A  93    12328   5112   9753    -58  -3529   1584       C  
ATOM   1456  N   ALA A  94      11.338 -27.540   9.290  1.00 62.38           N  
ANISOU 1456  N   ALA A  94    10978   4129   8594    862  -3422   1103       N  
ATOM   1457  CA  ALA A  94      11.606 -26.552   8.258  1.00 60.36           C  
ANISOU 1457  CA  ALA A  94    10642   4060   8233   1131  -3189    846       C  
ATOM   1458  C   ALA A  94      10.276 -26.055   7.706  1.00 57.45           C  
ANISOU 1458  C   ALA A  94    10348   3746   7734    923  -3084    811       C  
ATOM   1459  O   ALA A  94       9.368 -26.853   7.449  1.00 59.28           O  
ANISOU 1459  O   ALA A  94    10697   3756   8072    755  -3250    802       O  
ATOM   1460  CB  ALA A  94      12.466 -27.152   7.145  1.00 62.93           C  
ANISOU 1460  CB  ALA A  94    10972   4215   8723   1569  -3230    501       C  
ATOM   1466  N   ASN A  95      10.150 -24.741   7.554  1.00 53.50           N  
ANISOU 1466  N   ASN A  95     9760   3533   7035    920  -2834    808       N  
ATOM   1467  CA  ASN A  95       8.925 -24.155   7.026  1.00 54.28           C  
ANISOU 1467  CA  ASN A  95     9854   3737   7033    717  -2707    763       C  
ATOM   1468  C   ASN A  95       8.698 -24.676   5.609  1.00 55.61           C  
ANISOU 1468  C   ASN A  95    10178   3684   7267    936  -2833    441       C  
ATOM   1469  O   ASN A  95       9.522 -24.408   4.723  1.00 53.93           O  
ANISOU 1469  O   ASN A  95     9952   3571   6966   1286  -2705    169       O  
ATOM   1470  CB  ASN A  95       9.014 -22.626   7.041  1.00 53.68           C  
ANISOU 1470  CB  ASN A  95     9536   4133   6727    690  -2339    735       C  
ATOM   1471  CG  ASN A  95       7.726 -21.950   6.595  1.00 53.01           C  
ANISOU 1471  CG  ASN A  95     9379   4181   6580    462  -2206    703       C  
ATOM   1472  OD1 ASN A  95       6.736 -22.612   6.291  1.00 54.43           O  
ANISOU 1472  OD1 ASN A  95     9667   4114   6901    304  -2391    713       O  
ATOM   1473  ND2 ASN A  95       7.734 -20.619   6.566  1.00 54.08           N  
ANISOU 1473  ND2 ASN A  95     9314   4683   6551    441  -1916    673       N  
ATOM   1480  N   PRO A  96       7.628 -25.435   5.353  1.00 63.04           N  
ANISOU 1480  N   PRO A  96    11239   4371   8344    726  -3054    446       N  
ATOM   1481  CA  PRO A  96       7.381 -25.893   3.977  1.00 65.17           C  
ANISOU 1481  CA  PRO A  96    11673   4471   8617    911  -3195    110       C  
ATOM   1482  C   PRO A  96       7.079 -24.757   3.023  1.00 64.79           C  
ANISOU 1482  C   PRO A  96    11622   4641   8354    994  -3011    -69       C  
ATOM   1483  O   PRO A  96       7.226 -24.929   1.807  1.00 66.58           O  
ANISOU 1483  O   PRO A  96    12047   4778   8472   1245  -3073   -385       O  
ATOM   1484  CB  PRO A  96       6.179 -26.835   4.129  1.00 66.52           C  
ANISOU 1484  CB  PRO A  96    11882   4394   8999    576  -3476    228       C  
ATOM   1485  CG  PRO A  96       5.470 -26.339   5.335  1.00 65.56           C  
ANISOU 1485  CG  PRO A  96    11581   4404   8924    185  -3348    604       C  
ATOM   1486  CD  PRO A  96       6.545 -25.840   6.268  1.00 64.49           C  
ANISOU 1486  CD  PRO A  96    11373   4473   8658    288  -3146    751       C  
ATOM   1494  N   LYS A  97       6.667 -23.600   3.537  1.00 63.67           N  
ANISOU 1494  N   LYS A  97    11222   4863   8107    769  -2747    109       N  
ATOM   1495  CA  LYS A  97       6.348 -22.440   2.720  1.00 62.44           C  
ANISOU 1495  CA  LYS A  97    10968   5004   7751    792  -2545    -24       C  
ATOM   1496  C   LYS A  97       7.520 -21.474   2.601  1.00 58.18           C  
ANISOU 1496  C   LYS A  97    10288   4826   6992   1042  -2205    -99       C  
ATOM   1497  O   LYS A  97       7.312 -20.288   2.325  1.00 57.77           O  
ANISOU 1497  O   LYS A  97    10082   5075   6792    989  -1988   -100       O  
ATOM   1498  CB  LYS A  97       5.130 -21.719   3.298  1.00 63.95           C  
ANISOU 1498  CB  LYS A  97    10935   5339   8025    409  -2469    195       C  
ATOM   1499  CG  LYS A  97       3.851 -22.546   3.292  1.00 71.09           C  
ANISOU 1499  CG  LYS A  97    11904   5904   9201    129  -2782    286       C  
ATOM   1500  CD  LYS A  97       2.747 -21.837   4.070  1.00 73.89           C  
ANISOU 1500  CD  LYS A  97    11958   6427   9691   -239  -2618    531       C  
ATOM   1501  CE  LYS A  97       1.395 -21.923   3.373  1.00 77.06           C  
ANISOU 1501  CE  LYS A  97    12310   6640  10328   -439  -2860    504       C  
ATOM   1502  NZ  LYS A  97       0.555 -20.729   3.686  1.00 76.80           N  
ANISOU 1502  NZ  LYS A  97    11929   6884  10367   -643  -2608    617       N  
ATOM   1516  N   THR A  98       8.741 -21.949   2.805  1.00 53.35           N  
ANISOU 1516  N   THR A  98     9700   4167   6404   1306  -2173   -149       N  
ATOM   1517  CA  THR A  98       9.906 -21.080   2.693  1.00 51.30           C  
ANISOU 1517  CA  THR A  98     9257   4227   6007   1534  -1860   -201       C  
ATOM   1518  C   THR A  98      10.090 -20.650   1.244  1.00 51.71           C  
ANISOU 1518  C   THR A  98     9416   4396   5835   1768  -1704   -472       C  
ATOM   1519  O   THR A  98      10.220 -21.514   0.367  1.00 51.17           O  
ANISOU 1519  O   THR A  98     9616   4089   5739   1994  -1830   -715       O  
ATOM   1520  CB  THR A  98      11.166 -21.788   3.178  1.00 52.92           C  
ANISOU 1520  CB  THR A  98     9430   4308   6368   1782  -1900   -197       C  
ATOM   1521  OG1 THR A  98      11.013 -22.165   4.549  1.00 50.93           O  
ANISOU 1521  OG1 THR A  98     9132   3949   6271   1545  -2074     88       O  
ATOM   1522  CG2 THR A  98      12.375 -20.870   3.033  1.00 52.43           C  
ANISOU 1522  CG2 THR A  98     9119   4570   6233   2002  -1580   -236       C  
ATOM   1530  N   PRO A  99      10.116 -19.357   0.943  1.00 50.51           N  
ANISOU 1530  N   PRO A  99     9101   4587   5504   1724  -1441   -442       N  
ATOM   1531  CA  PRO A  99      10.373 -18.924  -0.431  1.00 51.60           C  
ANISOU 1531  CA  PRO A  99     9374   4852   5380   1936  -1272   -659       C  
ATOM   1532  C   PRO A  99      11.868 -18.869  -0.718  1.00 54.12           C  
ANISOU 1532  C   PRO A  99     9590   5312   5660   2277   -978   -761       C  
ATOM   1533  O   PRO A  99      12.709 -18.950   0.178  1.00 56.89           O  
ANISOU 1533  O   PRO A  99     9704   5695   6217   2332   -920   -642       O  
ATOM   1534  CB  PRO A  99       9.749 -17.526  -0.474  1.00 49.06           C  
ANISOU 1534  CB  PRO A  99     8885   4813   4943   1705  -1141   -520       C  
ATOM   1535  CG  PRO A  99       9.961 -17.007   0.918  1.00 47.83           C  
ANISOU 1535  CG  PRO A  99     8412   4796   4963   1527  -1056   -279       C  
ATOM   1536  CD  PRO A  99       9.855 -18.211   1.836  1.00 46.68           C  
ANISOU 1536  CD  PRO A  99     8332   4371   5032   1466  -1294   -209       C  
ATOM   1544  N   LYS A 100      12.187 -18.741  -2.000  1.00 56.44           N  
ANISOU 1544  N   LYS A 100    10071   5684   5691   2506   -796   -979       N  
ATOM   1545  CA  LYS A 100      13.530 -18.338  -2.389  1.00 59.68           C  
ANISOU 1545  CA  LYS A 100    10309   6324   6043   2789   -400  -1039       C  
ATOM   1546  C   LYS A 100      13.794 -16.954  -1.807  1.00 57.03           C  
ANISOU 1546  C   LYS A 100     9600   6323   5747   2597   -192   -775       C  
ATOM   1547  O   LYS A 100      13.074 -15.998  -2.113  1.00 50.18           O  
ANISOU 1547  O   LYS A 100     8751   5612   4702   2387   -171   -686       O  
ATOM   1548  CB  LYS A 100      13.650 -18.333  -3.913  1.00 67.88           C  
ANISOU 1548  CB  LYS A 100    11668   7420   6702   3016   -201  -1298       C  
ATOM   1549  CG  LYS A 100      15.058 -18.559  -4.452  1.00 77.71           C  
ANISOU 1549  CG  LYS A 100    12830   8767   7928   3412    202  -1466       C  
ATOM   1550  CD  LYS A 100      15.919 -17.313  -4.334  1.00 82.30           C  
ANISOU 1550  CD  LYS A 100    13007   9733   8531   3385    605  -1257       C  
ATOM   1551  CE  LYS A 100      17.190 -17.438  -5.165  1.00 89.26           C  
ANISOU 1551  CE  LYS A 100    13824  10752   9338   3767   1083  -1431       C  
ATOM   1552  NZ  LYS A 100      18.059 -16.229  -5.065  1.00 89.82           N  
ANISOU 1552  NZ  LYS A 100    13462  11180   9486   3716   1473  -1195       N  
ATOM   1566  N   TYR A 101      14.790 -16.848  -0.930  1.00 55.61           N  
ANISOU 1566  N   TYR A 101     9083   6217   5830   2657    -93   -648       N  
ATOM   1567  CA  TYR A 101      15.006 -15.605  -0.208  1.00 52.52           C  
ANISOU 1567  CA  TYR A 101     8356   6083   5515   2449     20   -404       C  
ATOM   1568  C   TYR A 101      16.492 -15.317  -0.073  1.00 50.54           C  
ANISOU 1568  C   TYR A 101     7761   5984   5457   2654    280   -358       C  
ATOM   1569  O   TYR A 101      17.342 -16.188  -0.270  1.00 48.75           O  
ANISOU 1569  O   TYR A 101     7503   5637   5382   2952    341   -490       O  
ATOM   1570  CB  TYR A 101      14.368 -15.649   1.188  1.00 48.08           C  
ANISOU 1570  CB  TYR A 101     7721   5423   5123   2162   -267   -218       C  
ATOM   1571  CG  TYR A 101      15.078 -16.574   2.151  1.00 49.66           C  
ANISOU 1571  CG  TYR A 101     7834   5438   5597   2259   -442   -167       C  
ATOM   1572  CD1 TYR A 101      14.723 -17.912   2.245  1.00 48.78           C  
ANISOU 1572  CD1 TYR A 101     7966   5001   5568   2324   -703   -253       C  
ATOM   1573  CD2 TYR A 101      16.103 -16.110   2.966  1.00 50.25           C  
ANISOU 1573  CD2 TYR A 101     7592   5631   5871   2275   -396    -18       C  
ATOM   1574  CE1 TYR A 101      15.365 -18.762   3.119  1.00 49.87           C  
ANISOU 1574  CE1 TYR A 101     8042   4936   5969   2409   -906   -178       C  
ATOM   1575  CE2 TYR A 101      16.755 -16.955   3.844  1.00 48.56           C  
ANISOU 1575  CE2 TYR A 101     7312   5222   5916   2360   -619     51       C  
ATOM   1576  CZ  TYR A 101      16.380 -18.280   3.917  1.00 51.72           C  
ANISOU 1576  CZ  TYR A 101     7967   5300   6384   2430   -870    -22       C  
ATOM   1577  OH  TYR A 101      17.019 -19.132   4.789  1.00 55.78           O  
ANISOU 1577  OH  TYR A 101     8436   5588   7170   2511  -1134     73       O  
ATOM   1587  N   LYS A 102      16.789 -14.067   0.274  1.00 47.90           N  
ANISOU 1587  N   LYS A 102     7144   5895   5163   2491    417   -168       N  
ATOM   1588  CA  LYS A 102      18.131 -13.684   0.678  1.00 55.99           C  
ANISOU 1588  CA  LYS A 102     7768   7041   6463   2601    577    -60       C  
ATOM   1589  C   LYS A 102      18.022 -12.498   1.622  1.00 49.24           C  
ANISOU 1589  C   LYS A 102     6689   6327   5694   2299    488    167       C  
ATOM   1590  O   LYS A 102      17.005 -11.800   1.661  1.00 48.15           O  
ANISOU 1590  O   LYS A 102     6680   6245   5368   2057    428    216       O  
ATOM   1591  CB  LYS A 102      19.021 -13.351  -0.527  1.00 61.92           C  
ANISOU 1591  CB  LYS A 102     8399   7981   7145   2839   1016   -136       C  
ATOM   1592  CG  LYS A 102      18.523 -12.211  -1.395  1.00 66.73           C  
ANISOU 1592  CG  LYS A 102     9106   8813   7436   2683   1232    -73       C  
ATOM   1593  CD  LYS A 102      19.580 -11.793  -2.414  1.00 72.14           C  
ANISOU 1593  CD  LYS A 102     9618   9715   8076   2882   1711    -74       C  
ATOM   1594  CE  LYS A 102      18.967 -11.038  -3.584  1.00 72.98           C  
ANISOU 1594  CE  LYS A 102    10003   9982   7743   2785   1907    -62       C  
ATOM   1595  NZ  LYS A 102      19.971 -10.202  -4.305  1.00 75.91           N  
ANISOU 1595  NZ  LYS A 102    10125  10617   8100   2844   2378     72       N  
ATOM   1609  N   PHE A 103      19.075 -12.293   2.404  1.00 48.52           N  
ANISOU 1609  N   PHE A 103     6258   6264   5912   2326    450    292       N  
ATOM   1610  CA  PHE A 103      19.182 -11.143   3.288  1.00 46.76           C  
ANISOU 1610  CA  PHE A 103     5820   6159   5789   2070    356    481       C  
ATOM   1611  C   PHE A 103      20.024 -10.072   2.607  1.00 48.17           C  
ANISOU 1611  C   PHE A 103     5687   6557   6059   2100    671    567       C  
ATOM   1612  O   PHE A 103      21.095 -10.370   2.067  1.00 49.97           O  
ANISOU 1612  O   PHE A 103     5680   6826   6479   2341    896    547       O  
ATOM   1613  CB  PHE A 103      19.811 -11.533   4.626  1.00 47.43           C  
ANISOU 1613  CB  PHE A 103     5755   6114   6153   2042     41    586       C  
ATOM   1614  CG  PHE A 103      19.010 -12.537   5.415  1.00 45.63           C  
ANISOU 1614  CG  PHE A 103     5839   5669   5829   1964   -271    563       C  
ATOM   1615  CD1 PHE A 103      17.648 -12.695   5.201  1.00 43.14           C  
ANISOU 1615  CD1 PHE A 103     5847   5314   5229   1821   -285    493       C  
ATOM   1616  CD2 PHE A 103      19.625 -13.318   6.381  1.00 46.74           C  
ANISOU 1616  CD2 PHE A 103     5933   5630   6195   2019   -570    641       C  
ATOM   1617  CE1 PHE A 103      16.920 -13.616   5.933  1.00 42.80           C  
ANISOU 1617  CE1 PHE A 103     6061   5070   5132   1721   -546    509       C  
ATOM   1618  CE2 PHE A 103      18.901 -14.241   7.114  1.00 46.77           C  
ANISOU 1618  CE2 PHE A 103     6240   5427   6101   1919   -851    665       C  
ATOM   1619  CZ  PHE A 103      17.546 -14.389   6.889  1.00 43.55           C  
ANISOU 1619  CZ  PHE A 103     6137   4996   5413   1763   -816    604       C  
ATOM   1629  N   VAL A 104      19.540  -8.834   2.632  1.00 43.50           N  
ANISOU 1629  N   VAL A 104     5076   6091   5360   1856    698    669       N  
ATOM   1630  CA  VAL A 104      20.248  -7.712   2.031  1.00 45.57           C  
ANISOU 1630  CA  VAL A 104     5058   6540   5716   1824    965    799       C  
ATOM   1631  C   VAL A 104      20.148  -6.518   2.968  1.00 42.29           C  
ANISOU 1631  C   VAL A 104     4495   6145   5427   1540    763    944       C  
ATOM   1632  O   VAL A 104      19.105  -6.285   3.587  1.00 41.85           O  
ANISOU 1632  O   VAL A 104     4661   6024   5217   1355    552    909       O  
ATOM   1633  CB  VAL A 104      19.689  -7.362   0.634  1.00 47.08           C  
ANISOU 1633  CB  VAL A 104     5464   6850   5573   1847   1257    759       C  
ATOM   1634  CG1 VAL A 104      19.682  -8.597  -0.270  1.00 47.85           C  
ANISOU 1634  CG1 VAL A 104     5802   6898   5482   2131   1420    560       C  
ATOM   1635  CG2 VAL A 104      18.297  -6.769   0.747  1.00 45.93           C  
ANISOU 1635  CG2 VAL A 104     5588   6669   5193   1608   1072    756       C  
ATOM   1645  N   ARG A 105      21.239  -5.768   3.075  1.00 44.12           N  
ANISOU 1645  N   ARG A 105     4343   6456   5965   1509    833   1098       N  
ATOM   1646  CA  ARG A 105      21.266  -4.524   3.835  1.00 45.10           C  
ANISOU 1646  CA  ARG A 105     4323   6582   6233   1246    643   1225       C  
ATOM   1647  C   ARG A 105      21.116  -3.381   2.838  1.00 46.40           C  
ANISOU 1647  C   ARG A 105     4436   6874   6320   1140    902   1335       C  
ATOM   1648  O   ARG A 105      21.987  -3.174   1.988  1.00 51.13           O  
ANISOU 1648  O   ARG A 105     4788   7592   7048   1227   1207   1452       O  
ATOM   1649  CB  ARG A 105      22.560  -4.405   4.637  1.00 46.39           C  
ANISOU 1649  CB  ARG A 105     4093   6702   6831   1245    469   1344       C  
ATOM   1650  CG  ARG A 105      22.613  -3.186   5.537  1.00 46.97           C  
ANISOU 1650  CG  ARG A 105     4063   6730   7051    973    195   1440       C  
ATOM   1651  CD  ARG A 105      23.826  -3.221   6.449  1.00 51.21           C  
ANISOU 1651  CD  ARG A 105     4265   7180   8012    964    -93   1541       C  
ATOM   1652  NE  ARG A 105      23.895  -2.042   7.306  1.00 54.27           N  
ANISOU 1652  NE  ARG A 105     4597   7497   8526    699   -396   1606       N  
ATOM   1653  CZ  ARG A 105      23.258  -1.915   8.466  1.00 52.80           C  
ANISOU 1653  CZ  ARG A 105     4716   7202   8145    550   -743   1504       C  
ATOM   1654  NH1 ARG A 105      22.492  -2.897   8.925  1.00 51.55           N  
ANISOU 1654  NH1 ARG A 105     4914   7002   7671    615   -820   1372       N  
ATOM   1655  NH2 ARG A 105      23.389  -0.799   9.170  1.00 51.92           N  
ANISOU 1655  NH2 ARG A 105     4564   7013   8149    331  -1003   1532       N  
ATOM   1670  N   ILE A 106      20.008  -2.653   2.930  1.00 45.52           N  
ANISOU 1670  N   ILE A 106     4554   6732   6010    955    792   1310       N  
ATOM   1671  CA  ILE A 106      19.705  -1.610   1.964  1.00 46.18           C  
ANISOU 1671  CA  ILE A 106     4653   6894   5997    849    976   1426       C  
ATOM   1672  C   ILE A 106      20.381  -0.313   2.386  1.00 46.53           C  
ANISOU 1672  C   ILE A 106     4386   6925   6369    652    889   1608       C  
ATOM   1673  O   ILE A 106      20.784  -0.130   3.536  1.00 45.76           O  
ANISOU 1673  O   ILE A 106     4142   6736   6509    567    619   1598       O  
ATOM   1674  CB  ILE A 106      18.185  -1.406   1.797  1.00 45.82           C  
ANISOU 1674  CB  ILE A 106     4962   6785   5662    756    868   1321       C  
ATOM   1675  CG1 ILE A 106      17.549  -0.993   3.129  1.00 44.46           C  
ANISOU 1675  CG1 ILE A 106     4832   6485   5577    592    556   1236       C  
ATOM   1676  CG2 ILE A 106      17.543  -2.674   1.237  1.00 46.36           C  
ANISOU 1676  CG2 ILE A 106     5332   6845   5438    932    932   1160       C  
ATOM   1677  CD1 ILE A 106      16.119  -0.530   3.001  1.00 44.11           C  
ANISOU 1677  CD1 ILE A 106     5021   6369   5369    487    474   1156       C  
ATOM   1689  N   GLN A 107      20.497   0.596   1.438  1.00 51.09           N  
ANISOU 1689  N   GLN A 107     4891   7576   6944    565   1092   1785       N  
ATOM   1690  CA  GLN A 107      21.046   1.920   1.657  1.00 53.60           C  
ANISOU 1690  CA  GLN A 107     4933   7852   7582    351   1009   1986       C  
ATOM   1691  C   GLN A 107      19.923   2.920   1.871  1.00 47.78           C  
ANISOU 1691  C   GLN A 107     4408   6984   6761    167    787   1951       C  
ATOM   1692  O   GLN A 107      18.788   2.698   1.442  1.00 43.22           O  
ANISOU 1692  O   GLN A 107     4148   6396   5879    205    797   1842       O  
ATOM   1693  CB  GLN A 107      21.892   2.350   0.454  1.00 59.28           C  
ANISOU 1693  CB  GLN A 107     5430   8718   8376    347   1390   2249       C  
ATOM   1694  CG  GLN A 107      23.012   1.385   0.094  1.00 64.17           C  
ANISOU 1694  CG  GLN A 107     5800   9478   9104    566   1700   2271       C  
ATOM   1695  CD  GLN A 107      24.222   1.518   1.002  1.00 67.56           C  
ANISOU 1695  CD  GLN A 107     5752   9849  10068    523   1543   2364       C  
ATOM   1696  OE1 GLN A 107      24.880   2.562   1.032  1.00 68.83           O  
ANISOU 1696  OE1 GLN A 107     5590   9986  10576    326   1523   2599       O  
ATOM   1697  NE2 GLN A 107      24.524   0.458   1.746  1.00 66.26           N  
ANISOU 1697  NE2 GLN A 107     5542   9636   9999    696   1389   2197       N  
ATOM   1706  N   PRO A 108      20.203   4.046   2.524  1.00 46.96           N  
ANISOU 1706  N   PRO A 108     4125   6753   6963    -30    563   2034       N  
ATOM   1707  CA  PRO A 108      19.168   5.074   2.674  1.00 43.41           C  
ANISOU 1707  CA  PRO A 108     3854   6151   6489   -181    369   1989       C  
ATOM   1708  C   PRO A 108      18.618   5.499   1.320  1.00 40.46           C  
ANISOU 1708  C   PRO A 108     3622   5823   5929   -201    561   2146       C  
ATOM   1709  O   PRO A 108      19.309   5.460   0.300  1.00 42.21           O  
ANISOU 1709  O   PRO A 108     3741   6184   6111   -180    847   2368       O  
ATOM   1710  CB  PRO A 108      19.904   6.228   3.367  1.00 45.40           C  
ANISOU 1710  CB  PRO A 108     3841   6255   7152   -379    135   2097       C  
ATOM   1711  CG  PRO A 108      21.113   5.612   3.980  1.00 49.53           C  
ANISOU 1711  CG  PRO A 108     4098   6832   7889   -329     98   2121       C  
ATOM   1712  CD  PRO A 108      21.497   4.477   3.082  1.00 48.73           C  
ANISOU 1712  CD  PRO A 108     3960   6942   7614   -124    461   2178       C  
ATOM   1720  N   GLY A 109      17.352   5.907   1.322  1.00 40.48           N  
ANISOU 1720  N   GLY A 109     3867   5702   5813   -240    403   2033       N  
ATOM   1721  CA  GLY A 109      16.675   6.295   0.107  1.00 41.19           C  
ANISOU 1721  CA  GLY A 109     4141   5793   5718   -263    486   2173       C  
ATOM   1722  C   GLY A 109      16.053   5.156  -0.667  1.00 41.78           C  
ANISOU 1722  C   GLY A 109     4494   5990   5390    -93    636   2076       C  
ATOM   1723  O   GLY A 109      15.239   5.411  -1.564  1.00 43.37           O  
ANISOU 1723  O   GLY A 109     4919   6156   5405   -111    606   2143       O  
ATOM   1727  N   GLN A 110      16.408   3.912  -0.360  1.00 41.50           N  
ANISOU 1727  N   GLN A 110     4468   6069   5232     69    751   1924       N  
ATOM   1728  CA  GLN A 110      15.775   2.776  -1.007  1.00 44.03           C  
ANISOU 1728  CA  GLN A 110     5074   6458   5195    232    841   1793       C  
ATOM   1729  C   GLN A 110      14.426   2.490  -0.362  1.00 39.77           C  
ANISOU 1729  C   GLN A 110     4711   5779   4623    228    589   1565       C  
ATOM   1730  O   GLN A 110      14.202   2.771   0.819  1.00 36.38           O  
ANISOU 1730  O   GLN A 110     4176   5250   4398    160    423   1448       O  
ATOM   1731  CB  GLN A 110      16.671   1.539  -0.934  1.00 48.60           C  
ANISOU 1731  CB  GLN A 110     5590   7171   5704    418   1045   1713       C  
ATOM   1732  CG  GLN A 110      17.842   1.576  -1.913  1.00 59.15           C  
ANISOU 1732  CG  GLN A 110     6793   8680   7000    478   1401   1915       C  
ATOM   1733  CD  GLN A 110      18.504   0.223  -2.088  1.00 65.24           C  
ANISOU 1733  CD  GLN A 110     7564   9561   7661    725   1626   1785       C  
ATOM   1734  OE1 GLN A 110      19.387  -0.157  -1.317  1.00 66.53           O  
ANISOU 1734  OE1 GLN A 110     7445   9733   8101    789   1632   1758       O  
ATOM   1735  NE2 GLN A 110      18.078  -0.514  -3.109  1.00 66.30           N  
ANISOU 1735  NE2 GLN A 110     8030   9756   7405    871   1779   1695       N  
ATOM   1744  N   THR A 111      13.522   1.938  -1.159  1.00 37.36           N  
ANISOU 1744  N   THR A 111     4679   5461   4054    295    566   1504       N  
ATOM   1745  CA  THR A 111      12.173   1.627  -0.718  1.00 37.54           C  
ANISOU 1745  CA  THR A 111     4835   5349   4081    284    349   1319       C  
ATOM   1746  C   THR A 111      12.025   0.129  -0.481  1.00 35.17           C  
ANISOU 1746  C   THR A 111     4668   5079   3616    420    378   1138       C  
ATOM   1747  O   THR A 111      12.789  -0.690  -0.999  1.00 36.79           O  
ANISOU 1747  O   THR A 111     4941   5392   3645    556    549   1141       O  
ATOM   1748  CB  THR A 111      11.144   2.098  -1.750  1.00 37.20           C  
ANISOU 1748  CB  THR A 111     4985   5212   3936    237    204   1392       C  
ATOM   1749  OG1 THR A 111      11.417   1.490  -3.019  1.00 37.10           O  
ANISOU 1749  OG1 THR A 111     5221   5306   3570    332    329   1464       O  
ATOM   1750  CG2 THR A 111      11.188   3.614  -1.891  1.00 36.39           C  
ANISOU 1750  CG2 THR A 111     4753   5022   4049     92    119   1579       C  
ATOM   1758  N   PHE A 112      11.029  -0.216   0.328  1.00 32.86           N  
ANISOU 1758  N   PHE A 112     4402   4676   3408    384    222    980       N  
ATOM   1759  CA  PHE A 112      10.681  -1.606   0.574  1.00 34.45           C  
ANISOU 1759  CA  PHE A 112     4745   4856   3490    472    198    833       C  
ATOM   1760  C   PHE A 112       9.267  -1.656   1.136  1.00 34.52           C  
ANISOU 1760  C   PHE A 112     4773   4727   3618    378     32    723       C  
ATOM   1761  O   PHE A 112       8.730  -0.647   1.603  1.00 31.82           O  
ANISOU 1761  O   PHE A 112     4296   4320   3474    273    -28    723       O  
ATOM   1762  CB  PHE A 112      11.680  -2.276   1.525  1.00 35.57           C  
ANISOU 1762  CB  PHE A 112     4783   5059   3673    534    281    793       C  
ATOM   1763  CG  PHE A 112      11.838  -1.570   2.841  1.00 37.49           C  
ANISOU 1763  CG  PHE A 112     4846   5282   4117    415    226    782       C  
ATOM   1764  CD1 PHE A 112      12.694  -0.488   2.966  1.00 39.80           C  
ANISOU 1764  CD1 PHE A 112     4947   5616   4558    357    257    892       C  
ATOM   1765  CD2 PHE A 112      11.143  -1.998   3.958  1.00 34.74           C  
ANISOU 1765  CD2 PHE A 112     4541   4864   3796    352    142    663       C  
ATOM   1766  CE1 PHE A 112      12.845   0.157   4.178  1.00 39.55           C  
ANISOU 1766  CE1 PHE A 112     4801   5540   4688    250    163    849       C  
ATOM   1767  CE2 PHE A 112      11.291  -1.358   5.171  1.00 38.36           C  
ANISOU 1767  CE2 PHE A 112     4903   5308   4366    250     99    626       C  
ATOM   1768  CZ  PHE A 112      12.142  -0.279   5.281  1.00 36.98           C  
ANISOU 1768  CZ  PHE A 112     4568   5157   4327    206     88    701       C  
ATOM   1778  N   SER A 113       8.669  -2.843   1.069  1.00 35.83           N  
ANISOU 1778  N   SER A 113     5091   4831   3692    422    -36    626       N  
ATOM   1779  CA  SER A 113       7.339  -3.077   1.615  1.00 35.90           C  
ANISOU 1779  CA  SER A 113     5081   4712   3849    324   -160    539       C  
ATOM   1780  C   SER A 113       7.443  -3.615   3.034  1.00 36.73           C  
ANISOU 1780  C   SER A 113     5119   4829   4010    278    -88    473       C  
ATOM   1781  O   SER A 113       8.317  -4.429   3.337  1.00 36.03           O  
ANISOU 1781  O   SER A 113     5095   4789   3804    353    -38    474       O  
ATOM   1782  CB  SER A 113       6.564  -4.072   0.751  1.00 35.23           C  
ANISOU 1782  CB  SER A 113     5200   4519   3668    359   -317    495       C  
ATOM   1783  OG  SER A 113       6.325  -3.560  -0.545  1.00 36.44           O  
ANISOU 1783  OG  SER A 113     5473   4645   3726    382   -432    559       O  
ATOM   1789  N   VAL A 114       6.532  -3.170   3.896  1.00 35.41           N  
ANISOU 1789  N   VAL A 114     4831   4606   4018    160    -80    417       N  
ATOM   1790  CA  VAL A 114       6.455  -3.628   5.277  1.00 34.83           C  
ANISOU 1790  CA  VAL A 114     4744   4546   3943     85      6    363       C  
ATOM   1791  C   VAL A 114       5.169  -4.420   5.450  1.00 35.50           C  
ANISOU 1791  C   VAL A 114     4842   4525   4122      1    -23    329       C  
ATOM   1792  O   VAL A 114       4.089  -3.956   5.065  1.00 34.64           O  
ANISOU 1792  O   VAL A 114     4616   4330   4215    -47    -71    303       O  
ATOM   1793  CB  VAL A 114       6.506  -2.453   6.270  1.00 36.93           C  
ANISOU 1793  CB  VAL A 114     4880   4849   4305     13    100    308       C  
ATOM   1794  CG1 VAL A 114       6.258  -2.943   7.693  1.00 35.52           C  
ANISOU 1794  CG1 VAL A 114     4754   4689   4053    -80    205    248       C  
ATOM   1795  CG2 VAL A 114       7.840  -1.736   6.183  1.00 38.81           C  
ANISOU 1795  CG2 VAL A 114     5083   5165   4497     66     90    364       C  
ATOM   1805  N   LEU A 115       5.285  -5.611   6.028  1.00 34.25           N  
ANISOU 1805  N   LEU A 115     4804   4350   3860    -25    -16    346       N  
ATOM   1806  CA  LEU A 115       4.132  -6.412   6.430  1.00 34.77           C  
ANISOU 1806  CA  LEU A 115     4863   4312   4036   -149    -15    349       C  
ATOM   1807  C   LEU A 115       3.978  -6.258   7.940  1.00 32.48           C  
ANISOU 1807  C   LEU A 115     4541   4091   3709   -273    185    338       C  
ATOM   1808  O   LEU A 115       4.690  -6.901   8.717  1.00 33.38           O  
ANISOU 1808  O   LEU A 115     4808   4244   3632   -290    200    389       O  
ATOM   1809  CB  LEU A 115       4.311  -7.871   6.024  1.00 34.77           C  
ANISOU 1809  CB  LEU A 115     5052   4209   3948   -113   -164    394       C  
ATOM   1810  CG  LEU A 115       3.145  -8.790   6.390  1.00 37.52           C  
ANISOU 1810  CG  LEU A 115     5389   4418   4450   -271   -197    435       C  
ATOM   1811  CD1 LEU A 115       1.865  -8.321   5.707  1.00 38.48           C  
ANISOU 1811  CD1 LEU A 115     5326   4442   4851   -336   -273    404       C  
ATOM   1812  CD2 LEU A 115       3.451 -10.235   6.027  1.00 40.87           C  
ANISOU 1812  CD2 LEU A 115     6032   4700   4799   -228   -385    472       C  
ATOM   1824  N   ALA A 116       3.057  -5.390   8.353  1.00 33.48           N  
ANISOU 1824  N   ALA A 116     4486   4224   4013   -351    334    266       N  
ATOM   1825  CA  ALA A 116       2.797  -5.177   9.770  1.00 36.45           C  
ANISOU 1825  CA  ALA A 116     4863   4674   4313   -464    579    223       C  
ATOM   1826  C   ALA A 116       2.026  -6.357  10.351  1.00 39.11           C  
ANISOU 1826  C   ALA A 116     5246   4962   4651   -616    670    315       C  
ATOM   1827  O   ALA A 116       0.963  -6.730   9.844  1.00 35.63           O  
ANISOU 1827  O   ALA A 116     4650   4412   4477   -678    646    344       O  
ATOM   1828  CB  ALA A 116       2.013  -3.881   9.971  1.00 38.12           C  
ANISOU 1828  CB  ALA A 116     4850   4887   4748   -469    743     83       C  
ATOM   1834  N   CYS A 117       2.564  -6.941  11.423  1.00 35.29           N  
ANISOU 1834  N   CYS A 117     4979   4543   3887   -693    746    382       N  
ATOM   1835  CA  CYS A 117       1.998  -8.134  12.032  1.00 39.85           C  
ANISOU 1835  CA  CYS A 117     5651   5067   4423   -861    818    524       C  
ATOM   1836  C   CYS A 117       1.801  -7.924  13.524  1.00 43.25           C  
ANISOU 1836  C   CYS A 117     6196   5619   4620  -1006   1123    523       C  
ATOM   1837  O   CYS A 117       2.456  -7.088  14.150  1.00 41.39           O  
ANISOU 1837  O   CYS A 117     6067   5496   4165   -957   1185    417       O  
ATOM   1838  CB  CYS A 117       2.892  -9.362  11.829  1.00 42.97           C  
ANISOU 1838  CB  CYS A 117     6284   5376   4665   -825    552    663       C  
ATOM   1839  SG  CYS A 117       3.012  -9.953  10.136  1.00 44.28           S  
ANISOU 1839  SG  CYS A 117     6410   5378   5037   -668    231    653       S  
ATOM   1845  N   TYR A 118       0.894  -8.722  14.087  1.00 48.79           N  
ANISOU 1845  N   TYR A 118     6894   6287   5355  -1199   1306    652       N  
ATOM   1846  CA  TYR A 118       0.633  -8.725  15.522  1.00 54.04           C  
ANISOU 1846  CA  TYR A 118     7726   7075   5731  -1368   1640    691       C  
ATOM   1847  C   TYR A 118       0.280 -10.149  15.925  1.00 59.58           C  
ANISOU 1847  C   TYR A 118     8567   7689   6380  -1577   1638    960       C  
ATOM   1848  O   TYR A 118      -0.636 -10.746  15.349  1.00 59.52           O  
ANISOU 1848  O   TYR A 118     8337   7552   6726  -1665   1631   1052       O  
ATOM   1849  CB  TYR A 118      -0.496  -7.757  15.884  1.00 57.09           C  
ANISOU 1849  CB  TYR A 118     7846   7546   6301  -1404   2059    524       C  
ATOM   1850  CG  TYR A 118      -0.175  -6.314  15.571  1.00 58.66           C  
ANISOU 1850  CG  TYR A 118     7926   7792   6572  -1208   2044    262       C  
ATOM   1851  CD1 TYR A 118       0.512  -5.525  16.482  1.00 59.68           C  
ANISOU 1851  CD1 TYR A 118     8294   8041   6343  -1169   2142    116       C  
ATOM   1852  CD2 TYR A 118      -0.549  -5.741  14.360  1.00 58.02           C  
ANISOU 1852  CD2 TYR A 118     7522   7608   6915  -1073   1889    172       C  
ATOM   1853  CE1 TYR A 118       0.813  -4.209  16.204  1.00 57.88           C  
ANISOU 1853  CE1 TYR A 118     7959   7814   6217  -1005   2097   -114       C  
ATOM   1854  CE2 TYR A 118      -0.249  -4.421  14.070  1.00 55.87           C  
ANISOU 1854  CE2 TYR A 118     7152   7349   6728   -912   1851    -32       C  
ATOM   1855  CZ  TYR A 118       0.435  -3.660  14.995  1.00 58.13           C  
ANISOU 1855  CZ  TYR A 118     7654   7739   6693   -879   1959   -175       C  
ATOM   1856  OH  TYR A 118       0.739  -2.345  14.716  1.00 54.64           O  
ANISOU 1856  OH  TYR A 118     7117   7271   6372   -734   1891   -370       O  
ATOM   1867  N   ASN A 119       1.010 -10.694  16.898  1.00 60.66           N  
ANISOU 1867  N   ASN A 119     9079   7868   6101  -1667   1596   1101       N  
ATOM   1868  CA  ASN A 119       0.822 -12.075  17.341  1.00 62.98           C  
ANISOU 1868  CA  ASN A 119     9565   8050   6315  -1875   1540   1398       C  
ATOM   1869  C   ASN A 119       1.102 -13.070  16.217  1.00 61.72           C  
ANISOU 1869  C   ASN A 119     9356   7652   6443  -1792   1117   1494       C  
ATOM   1870  O   ASN A 119       0.503 -14.148  16.164  1.00 61.98           O  
ANISOU 1870  O   ASN A 119     9387   7520   6642  -1962   1066   1701       O  
ATOM   1871  CB  ASN A 119      -0.587 -12.291  17.901  1.00 68.29           C  
ANISOU 1871  CB  ASN A 119    10077   8757   7111  -2129   1983   1509       C  
ATOM   1872  CG  ASN A 119      -0.812 -11.557  19.206  1.00 73.59           C  
ANISOU 1872  CG  ASN A 119    10888   9661   7412  -2203   2423   1428       C  
ATOM   1873  OD1 ASN A 119       0.041 -11.568  20.095  1.00 75.76           O  
ANISOU 1873  OD1 ASN A 119    11504  10014   7269  -2151   2293   1440       O  
ATOM   1874  ND2 ASN A 119      -1.964 -10.908  19.327  1.00 77.24           N  
ANISOU 1874  ND2 ASN A 119    11014  10216   8118  -2227   2849   1298       N  
ATOM   1881  N   GLY A 120       2.016 -12.718  15.315  1.00 56.78           N  
ANISOU 1881  N   GLY A 120     8700   6997   5875  -1534    821   1341       N  
ATOM   1882  CA  GLY A 120       2.362 -13.582  14.206  1.00 55.00           C  
ANISOU 1882  CA  GLY A 120     8466   6559   5872  -1411    451   1372       C  
ATOM   1883  C   GLY A 120       1.352 -13.625  13.082  1.00 54.05           C  
ANISOU 1883  C   GLY A 120     8061   6320   6156  -1405    418   1302       C  
ATOM   1884  O   GLY A 120       1.443 -14.511  12.225  1.00 53.10           O  
ANISOU 1884  O   GLY A 120     7983   5988   6204  -1344    115   1333       O  
ATOM   1888  N   SER A 121       0.396 -12.697  13.051  1.00 53.46           N  
ANISOU 1888  N   SER A 121     7705   6349   6257  -1456    691   1195       N  
ATOM   1889  CA  SER A 121      -0.646 -12.673  12.040  1.00 52.23           C  
ANISOU 1889  CA  SER A 121     7254   6064   6526  -1469    620   1144       C  
ATOM   1890  C   SER A 121      -0.561 -11.386  11.228  1.00 52.57           C  
ANISOU 1890  C   SER A 121     7107   6196   6670  -1267    605    919       C  
ATOM   1891  O   SER A 121      -0.482 -10.296  11.814  1.00 47.65           O  
ANISOU 1891  O   SER A 121     6414   5752   5939  -1233    863    809       O  
ATOM   1892  CB  SER A 121      -2.036 -12.784  12.686  1.00 54.87           C  
ANISOU 1892  CB  SER A 121     7346   6396   7108  -1731    941   1257       C  
ATOM   1893  OG  SER A 121      -2.274 -14.094  13.167  1.00 59.13           O  
ANISOU 1893  OG  SER A 121     8028   6789   7649  -1951    893   1511       O  
ATOM   1899  N   PRO A 122      -0.580 -11.461   9.896  1.00 56.63           N  
ANISOU 1899  N   PRO A 122     7567   6577   7374  -1137    297    849       N  
ATOM   1900  CA  PRO A 122      -0.542 -10.234   9.091  1.00 53.65           C  
ANISOU 1900  CA  PRO A 122     7031   6267   7086   -971    263    681       C  
ATOM   1901  C   PRO A 122      -1.700  -9.307   9.419  1.00 52.48           C  
ANISOU 1901  C   PRO A 122     6539   6164   7237  -1059    519    623       C  
ATOM   1902  O   PRO A 122      -2.823  -9.747   9.671  1.00 58.62           O  
ANISOU 1902  O   PRO A 122     7111   6851   8309  -1235    617    707       O  
ATOM   1903  CB  PRO A 122      -0.634 -10.747   7.650  1.00 55.67           C  
ANISOU 1903  CB  PRO A 122     7334   6334   7484   -879   -120    659       C  
ATOM   1904  CG  PRO A 122      -0.143 -12.150   7.708  1.00 60.08           C  
ANISOU 1904  CG  PRO A 122     8160   6760   7909   -903   -297    756       C  
ATOM   1905  CD  PRO A 122      -0.545 -12.673   9.056  1.00 59.71           C  
ANISOU 1905  CD  PRO A 122     8098   6734   7855  -1127    -58    913       C  
ATOM   1913  N   SER A 123      -1.417  -8.012   9.400  1.00 46.37           N  
ANISOU 1913  N   SER A 123     5678   5511   6431   -931    623    481       N  
ATOM   1914  CA  SER A 123      -2.429  -6.985   9.599  1.00 45.95           C  
ANISOU 1914  CA  SER A 123     5285   5472   6701   -952    841    381       C  
ATOM   1915  C   SER A 123      -2.581  -6.067   8.399  1.00 43.86           C  
ANISOU 1915  C   SER A 123     4865   5123   6676   -806    590    293       C  
ATOM   1916  O   SER A 123      -3.699  -5.661   8.074  1.00 43.65           O  
ANISOU 1916  O   SER A 123     4516   4988   7084   -836    578    266       O  
ATOM   1917  CB  SER A 123      -2.088  -6.147  10.840  1.00 48.47           C  
ANISOU 1917  CB  SER A 123     5649   5977   6791   -944   1211    271       C  
ATOM   1918  OG  SER A 123      -2.990  -5.065  10.987  1.00 53.15           O  
ANISOU 1918  OG  SER A 123     5916   6564   7713   -914   1427    127       O  
ATOM   1924  N   GLY A 124      -1.486  -5.734   7.729  1.00 36.24           N  
ANISOU 1924  N   GLY A 124     4112   4197   5459   -656    387    267       N  
ATOM   1925  CA  GLY A 124      -1.545  -4.841   6.589  1.00 33.63           C  
ANISOU 1925  CA  GLY A 124     3693   3794   5291   -536    152    223       C  
ATOM   1926  C   GLY A 124      -0.169  -4.701   5.979  1.00 34.74           C  
ANISOU 1926  C   GLY A 124     4107   4013   5078   -399      7    237       C  
ATOM   1927  O   GLY A 124       0.844  -5.090   6.571  1.00 35.42           O  
ANISOU 1927  O   GLY A 124     4390   4215   4853   -380    108    251       O  
ATOM   1932  N   VAL A 125      -0.148  -4.127   4.780  1.00 30.04           N  
ANISOU 1932  N   VAL A 125     3515   3349   4552   -311   -236    248       N  
ATOM   1933  CA  VAL A 125       1.080  -3.961   4.016  1.00 32.62           C  
ANISOU 1933  CA  VAL A 125     4073   3751   4569   -187   -343    283       C  
ATOM   1934  C   VAL A 125       1.129  -2.540   3.474  1.00 31.30           C  
ANISOU 1934  C   VAL A 125     3801   3573   4520   -129   -407    283       C  
ATOM   1935  O   VAL A 125       0.120  -2.010   2.994  1.00 29.55           O  
ANISOU 1935  O   VAL A 125     3408   3210   4607   -152   -560    285       O  
ATOM   1936  CB  VAL A 125       1.182  -4.996   2.873  1.00 34.99           C  
ANISOU 1936  CB  VAL A 125     4609   3966   4719   -142   -602    330       C  
ATOM   1937  CG1 VAL A 125       0.072  -4.791   1.856  1.00 36.57           C  
ANISOU 1937  CG1 VAL A 125     4738   3987   5170   -173   -898    350       C  
ATOM   1938  CG2 VAL A 125       2.546  -4.923   2.206  1.00 36.16           C  
ANISOU 1938  CG2 VAL A 125     4990   4229   4522     -1   -604    356       C  
ATOM   1948  N   TYR A 126       2.301  -1.914   3.575  1.00 29.69           N  
ANISOU 1948  N   TYR A 126     3677   3491   4114    -63   -314    299       N  
ATOM   1949  CA  TYR A 126       2.498  -0.579   3.032  1.00 33.15           C  
ANISOU 1949  CA  TYR A 126     4042   3901   4651    -25   -390    337       C  
ATOM   1950  C   TYR A 126       3.935  -0.439   2.553  1.00 31.10           C  
ANISOU 1950  C   TYR A 126     3953   3770   4094     44   -364    429       C  
ATOM   1951  O   TYR A 126       4.823  -1.201   2.946  1.00 27.52           O  
ANISOU 1951  O   TYR A 126     3609   3432   3414     76   -249    426       O  
ATOM   1952  CB  TYR A 126       2.162   0.513   4.058  1.00 33.38           C  
ANISOU 1952  CB  TYR A 126     3848   3903   4932    -55   -240    227       C  
ATOM   1953  CG  TYR A 126       2.911   0.392   5.363  1.00 35.43           C  
ANISOU 1953  CG  TYR A 126     4151   4295   5014    -76     -3    143       C  
ATOM   1954  CD1 TYR A 126       2.378  -0.324   6.426  1.00 38.83           C  
ANISOU 1954  CD1 TYR A 126     4564   4760   5432   -141    180     55       C  
ATOM   1955  CD2 TYR A 126       4.145   0.998   5.536  1.00 32.60           C  
ANISOU 1955  CD2 TYR A 126     3861   4019   4508    -48     18    171       C  
ATOM   1956  CE1 TYR A 126       3.055  -0.437   7.622  1.00 39.23           C  
ANISOU 1956  CE1 TYR A 126     4715   4922   5267   -173    355     -7       C  
ATOM   1957  CE2 TYR A 126       4.832   0.890   6.730  1.00 37.71           C  
ANISOU 1957  CE2 TYR A 126     4570   4761   4995    -75    160     97       C  
ATOM   1958  CZ  TYR A 126       4.282   0.172   7.769  1.00 40.06           C  
ANISOU 1958  CZ  TYR A 126     4902   5092   5226   -135    316      6       C  
ATOM   1959  OH  TYR A 126       4.964   0.064   8.960  1.00 44.33           O  
ANISOU 1959  OH  TYR A 126     5565   5721   5557   -174    417    -52       O  
ATOM   1969  N   GLN A 127       4.142   0.548   1.687  1.00 33.39           N  
ANISOU 1969  N   GLN A 127     4243   4024   4420     62   -477    531       N  
ATOM   1970  CA  GLN A 127       5.436   0.846   1.091  1.00 36.62           C  
ANISOU 1970  CA  GLN A 127     4767   4549   4598    107   -425    659       C  
ATOM   1971  C   GLN A 127       6.032   2.070   1.770  1.00 38.12           C  
ANISOU 1971  C   GLN A 127     4792   4748   4944     67   -345    671       C  
ATOM   1972  O   GLN A 127       5.327   3.047   2.035  1.00 45.18           O  
ANISOU 1972  O   GLN A 127     5539   5505   6122     26   -423    627       O  
ATOM   1973  CB  GLN A 127       5.281   1.111  -0.408  1.00 39.68           C  
ANISOU 1973  CB  GLN A 127     5315   4886   4876    125   -607    807       C  
ATOM   1974  CG  GLN A 127       6.579   1.327  -1.165  1.00 39.17           C  
ANISOU 1974  CG  GLN A 127     5382   4963   4539    166   -490    964       C  
ATOM   1975  CD  GLN A 127       7.211   0.025  -1.596  1.00 36.21           C  
ANISOU 1975  CD  GLN A 127     5218   4712   3827    272   -375    929       C  
ATOM   1976  OE1 GLN A 127       6.799  -1.049  -1.160  1.00 33.94           O  
ANISOU 1976  OE1 GLN A 127     4975   4395   3524    304   -396    790       O  
ATOM   1977  NE2 GLN A 127       8.210   0.110  -2.464  1.00 41.08           N  
ANISOU 1977  NE2 GLN A 127     5966   5455   4188    328   -240   1058       N  
ATOM   1986  N   CYS A 128       7.333   2.020   2.043  1.00 37.41           N  
ANISOU 1986  N   CYS A 128     4714   4791   4708     85   -213    722       N  
ATOM   1987  CA  CYS A 128       8.006   3.148   2.666  1.00 40.71           C  
ANISOU 1987  CA  CYS A 128     4988   5195   5284     30   -187    740       C  
ATOM   1988  C   CYS A 128       9.448   3.200   2.187  1.00 36.84           C  
ANISOU 1988  C   CYS A 128     4501   4833   4662     46   -102    912       C  
ATOM   1989  O   CYS A 128       9.916   2.328   1.450  1.00 36.04           O  
ANISOU 1989  O   CYS A 128     4517   4846   4332    124    -18    984       O  
ATOM   1990  CB  CYS A 128       7.940   3.056   4.192  1.00 45.36           C  
ANISOU 1990  CB  CYS A 128     5514   5784   5937      1   -117    551       C  
ATOM   1991  SG  CYS A 128       8.810   1.636   4.879  1.00 43.33           S  
ANISOU 1991  SG  CYS A 128     5361   5684   5418     43     -8    523       S  
ATOM   1997  N   ALA A 129      10.151   4.242   2.613  1.00 37.34           N  
ANISOU 1997  N   ALA A 129     4422   4863   4902    -26   -120    968       N  
ATOM   1998  CA  ALA A 129      11.545   4.440   2.257  1.00 37.56           C  
ANISOU 1998  CA  ALA A 129     4369   4997   4906    -40    -33   1153       C  
ATOM   1999  C   ALA A 129      12.397   4.489   3.518  1.00 35.62           C  
ANISOU 1999  C   ALA A 129     3998   4768   4769    -74    -45   1072       C  
ATOM   2000  O   ALA A 129      11.947   4.932   4.579  1.00 35.61           O  
ANISOU 2000  O   ALA A 129     3985   4659   4886   -125   -146    900       O  
ATOM   2001  CB  ALA A 129      11.731   5.730   1.445  1.00 38.29           C  
ANISOU 2001  CB  ALA A 129     4394   5002   5152   -136    -97   1370       C  
ATOM   2008  N   MET A 130      13.627   4.001   3.394  1.00 37.49           N  
ANISOU 2008  N   MET A 130     4148   5134   4961    -36     56   1185       N  
ATOM   2009  CA  MET A 130      14.635   4.190   4.430  1.00 42.02           C  
ANISOU 2009  CA  MET A 130     4570   5703   5693    -88    -24   1171       C  
ATOM   2010  C   MET A 130      15.098   5.640   4.373  1.00 42.10           C  
ANISOU 2010  C   MET A 130     4411   5598   5988   -231   -131   1302       C  
ATOM   2011  O   MET A 130      15.701   6.066   3.383  1.00 45.71           O  
ANISOU 2011  O   MET A 130     4749   6098   6519   -267    -31   1544       O  
ATOM   2012  CB  MET A 130      15.797   3.224   4.213  1.00 46.77           C  
ANISOU 2012  CB  MET A 130     5074   6453   6243     13    103   1269       C  
ATOM   2013  CG  MET A 130      16.948   3.355   5.206  1.00 50.10           C  
ANISOU 2013  CG  MET A 130     5302   6856   6878    -39    -34   1290       C  
ATOM   2014  SD  MET A 130      16.538   2.781   6.863  1.00 49.91           S  
ANISOU 2014  SD  MET A 130     5462   6759   6741    -52   -252   1043       S  
ATOM   2015  CE  MET A 130      16.249   1.040   6.554  1.00 48.42           C  
ANISOU 2015  CE  MET A 130     5436   6678   6286    129   -107    994       C  
ATOM   2025  N   ARG A 131      14.793   6.412   5.412  1.00 36.19           N  
ANISOU 2025  N   ARG A 131     3671   4690   5390   -319   -326   1145       N  
ATOM   2026  CA  ARG A 131      15.162   7.814   5.424  1.00 36.18           C  
ANISOU 2026  CA  ARG A 131     3531   4521   5696   -460   -482   1241       C  
ATOM   2027  C   ARG A 131      16.684   7.961   5.454  1.00 36.37           C  
ANISOU 2027  C   ARG A 131     3311   4589   5919   -537   -515   1445       C  
ATOM   2028  O   ARG A 131      17.399   7.038   5.850  1.00 38.95           O  
ANISOU 2028  O   ARG A 131     3584   5041   6174   -472   -480   1434       O  
ATOM   2029  CB  ARG A 131      14.550   8.523   6.629  1.00 38.27           C  
ANISOU 2029  CB  ARG A 131     3891   4591   6060   -509   -683    967       C  
ATOM   2030  CG  ARG A 131      13.036   8.393   6.761  1.00 38.47           C  
ANISOU 2030  CG  ARG A 131     4090   4565   5963   -428   -620    744       C  
ATOM   2031  CD  ARG A 131      12.301   8.833   5.505  1.00 35.14           C  
ANISOU 2031  CD  ARG A 131     3648   4083   5622   -414   -583    891       C  
ATOM   2032  NE  ARG A 131      12.778  10.117   5.000  1.00 35.61           N  
ANISOU 2032  NE  ARG A 131     3579   3974   5977   -531   -727   1086       N  
ATOM   2033  CZ  ARG A 131      12.404  10.645   3.838  1.00 37.10           C  
ANISOU 2033  CZ  ARG A 131     3757   4092   6246   -557   -745   1299       C  
ATOM   2034  NH1 ARG A 131      11.545   9.999   3.063  1.00 35.07           N  
ANISOU 2034  NH1 ARG A 131     3616   3916   5792   -466   -653   1319       N  
ATOM   2035  NH2 ARG A 131      12.891  11.815   3.446  1.00 38.34           N  
ANISOU 2035  NH2 ARG A 131     3806   4077   6683   -690   -888   1508       N  
ATOM   2049  N   PRO A 132      17.204   9.116   5.029  1.00 41.06           N  
ANISOU 2049  N   PRO A 132     3729   5061   6811   -682   -599   1653       N  
ATOM   2050  CA  PRO A 132      18.659   9.331   5.099  1.00 42.64           C  
ANISOU 2050  CA  PRO A 132     3632   5280   7289   -784   -643   1866       C  
ATOM   2051  C   PRO A 132      19.227   9.275   6.506  1.00 43.23           C  
ANISOU 2051  C   PRO A 132     3673   5263   7491   -826   -929   1687       C  
ATOM   2052  O   PRO A 132      20.439   9.075   6.652  1.00 42.63           O  
ANISOU 2052  O   PRO A 132     3337   5232   7629   -869   -978   1839       O  
ATOM   2053  CB  PRO A 132      18.837  10.725   4.480  1.00 43.16           C  
ANISOU 2053  CB  PRO A 132     3561   5168   7669   -969   -729   2108       C  
ATOM   2054  CG  PRO A 132      17.661  10.882   3.575  1.00 41.09           C  
ANISOU 2054  CG  PRO A 132     3513   4898   7200   -914   -610   2124       C  
ATOM   2055  CD  PRO A 132      16.527  10.185   4.271  1.00 40.35           C  
ANISOU 2055  CD  PRO A 132     3677   4816   6840   -761   -639   1763       C  
ATOM   2063  N   ASN A 133      18.412   9.457   7.545  1.00 40.37           N  
ANISOU 2063  N   ASN A 133     3563   4768   7007   -817  -1122   1373       N  
ATOM   2064  CA  ASN A 133      18.887   9.308   8.915  1.00 43.86           C  
ANISOU 2064  CA  ASN A 133     4073   5135   7456   -854  -1403   1185       C  
ATOM   2065  C   ASN A 133      18.660   7.902   9.464  1.00 40.66           C  
ANISOU 2065  C   ASN A 133     3853   4904   6691   -709  -1311   1040       C  
ATOM   2066  O   ASN A 133      18.751   7.701  10.679  1.00 42.43           O  
ANISOU 2066  O   ASN A 133     4252   5070   6800   -732  -1538    850       O  
ATOM   2067  CB  ASN A 133      18.227  10.346   9.830  1.00 41.65           C  
ANISOU 2067  CB  ASN A 133     4006   4603   7218   -933  -1656    907       C  
ATOM   2068  CG  ASN A 133      16.722  10.182   9.922  1.00 41.43           C  
ANISOU 2068  CG  ASN A 133     4254   4587   6902   -814  -1475    653       C  
ATOM   2069  OD1 ASN A 133      16.148   9.233   9.387  1.00 40.09           O  
ANISOU 2069  OD1 ASN A 133     4137   4605   6489   -692  -1209    681       O  
ATOM   2070  ND2 ASN A 133      16.074  11.111  10.615  1.00 44.08           N  
ANISOU 2070  ND2 ASN A 133     4752   4701   7294   -847  -1625    391       N  
ATOM   2077  N   PHE A 134      18.363   6.934   8.597  1.00 41.21           N  
ANISOU 2077  N   PHE A 134     3921   5168   6570   -571  -1006   1130       N  
ATOM   2078  CA  PHE A 134      18.261   5.519   8.948  1.00 44.69           C  
ANISOU 2078  CA  PHE A 134     4500   5752   6726   -436   -922   1048       C  
ATOM   2079  C   PHE A 134      17.052   5.202   9.819  1.00 45.99           C  
ANISOU 2079  C   PHE A 134     5010   5889   6574   -411   -933    770       C  
ATOM   2080  O   PHE A 134      17.035   4.174  10.503  1.00 45.36           O  
ANISOU 2080  O   PHE A 134     5088   5874   6272   -357   -961    694       O  
ATOM   2081  CB  PHE A 134      19.538   5.025   9.638  1.00 43.83           C  
ANISOU 2081  CB  PHE A 134     4245   5650   6759   -446  -1137   1122       C  
ATOM   2082  CG  PHE A 134      20.758   5.102   8.771  1.00 44.27           C  
ANISOU 2082  CG  PHE A 134     3898   5766   7156   -442  -1051   1405       C  
ATOM   2083  CD1 PHE A 134      21.037   4.100   7.859  1.00 43.57           C  
ANISOU 2083  CD1 PHE A 134     3696   5853   7007   -275   -752   1523       C  
ATOM   2084  CD2 PHE A 134      21.623   6.179   8.864  1.00 46.45           C  
ANISOU 2084  CD2 PHE A 134     3906   5914   7829   -607  -1253   1546       C  
ATOM   2085  CE1 PHE A 134      22.160   4.167   7.056  1.00 45.71           C  
ANISOU 2085  CE1 PHE A 134     3582   6199   7588   -257   -595   1772       C  
ATOM   2086  CE2 PHE A 134      22.748   6.253   8.064  1.00 48.77           C  
ANISOU 2086  CE2 PHE A 134     3782   6275   8472   -619  -1121   1832       C  
ATOM   2087  CZ  PHE A 134      23.016   5.245   7.158  1.00 47.45           C  
ANISOU 2087  CZ  PHE A 134     3496   6313   8221   -436   -761   1943       C  
ATOM   2097  N   THR A 135      16.040   6.060   9.814  1.00 41.87           N  
ANISOU 2097  N   THR A 135     4596   5262   6051   -451   -903    631       N  
ATOM   2098  CA  THR A 135      14.754   5.761  10.425  1.00 41.95           C  
ANISOU 2098  CA  THR A 135     4870   5268   5803   -411   -806    385       C  
ATOM   2099  C   THR A 135      13.738   5.477   9.328  1.00 39.62           C  
ANISOU 2099  C   THR A 135     4560   5030   5464   -326   -567    429       C  
ATOM   2100  O   THR A 135      13.978   5.728   8.144  1.00 33.18           O  
ANISOU 2100  O   THR A 135     3589   4236   4784   -311   -504    626       O  
ATOM   2101  CB  THR A 135      14.268   6.921  11.304  1.00 41.43           C  
ANISOU 2101  CB  THR A 135     4926   5016   5800   -489   -940    146       C  
ATOM   2102  OG1 THR A 135      13.983   8.065  10.485  1.00 39.92           O  
ANISOU 2102  OG1 THR A 135     4581   4687   5901   -515   -946    202       O  
ATOM   2103  CG2 THR A 135      15.313   7.287  12.352  1.00 40.89           C  
ANISOU 2103  CG2 THR A 135     4909   4856   5771   -591  -1251     96       C  
ATOM   2111  N   ILE A 136      12.590   4.943   9.730  1.00 39.97           N  
ANISOU 2111  N   ILE A 136     4778   5096   5313   -284   -442    256       N  
ATOM   2112  CA  ILE A 136      11.451   4.830   8.832  1.00 41.00           C  
ANISOU 2112  CA  ILE A 136     4893   5226   5460   -224   -288    261       C  
ATOM   2113  C   ILE A 136      10.237   5.415   9.535  1.00 41.27           C  
ANISOU 2113  C   ILE A 136     4999   5145   5535   -237   -236     14       C  
ATOM   2114  O   ILE A 136      10.130   5.390  10.765  1.00 41.31           O  
ANISOU 2114  O   ILE A 136     5150   5143   5403   -269   -226   -177       O  
ATOM   2115  CB  ILE A 136      11.180   3.375   8.377  1.00 43.10           C  
ANISOU 2115  CB  ILE A 136     5233   5628   5516   -144   -159    328       C  
ATOM   2116  CG1 ILE A 136      10.594   2.522   9.503  1.00 44.47           C  
ANISOU 2116  CG1 ILE A 136     5586   5836   5475   -158    -94    173       C  
ATOM   2117  CG2 ILE A 136      12.464   2.732   7.853  1.00 41.95           C  
ANISOU 2117  CG2 ILE A 136     5017   5588   5334    -96   -180    520       C  
ATOM   2118  CD1 ILE A 136      10.059   1.187   9.014  1.00 44.55           C  
ANISOU 2118  CD1 ILE A 136     5665   5916   5344    -99      7    229       C  
ATOM   2130  N   LYS A 137       9.317   5.943   8.738  1.00 40.62           N  
ANISOU 2130  N   LYS A 137     4821   4970   5641   -204   -201     18       N  
ATOM   2131  CA  LYS A 137       8.073   6.517   9.232  1.00 42.92           C  
ANISOU 2131  CA  LYS A 137     5106   5135   6066   -183   -124   -214       C  
ATOM   2132  C   LYS A 137       6.964   5.528   8.892  1.00 41.49           C  
ANISOU 2132  C   LYS A 137     4920   5023   5820   -136     32   -217       C  
ATOM   2133  O   LYS A 137       6.268   5.658   7.886  1.00 44.35           O  
ANISOU 2133  O   LYS A 137     5173   5316   6363   -101     -8   -131       O  
ATOM   2134  CB  LYS A 137       7.850   7.873   8.615  1.00 46.42           C  
ANISOU 2134  CB  LYS A 137     5409   5370   6858   -180   -261   -194       C  
ATOM   2135  CG  LYS A 137       9.000   8.832   8.883  1.00 50.72           C  
ANISOU 2135  CG  LYS A 137     5941   5818   7512   -255   -450   -156       C  
ATOM   2136  CD  LYS A 137       9.116   9.910   7.824  1.00 54.35           C  
ANISOU 2136  CD  LYS A 137     6256   6104   8290   -285   -617     33       C  
ATOM   2137  CE  LYS A 137       9.055  11.300   8.441  1.00 57.31           C  
ANISOU 2137  CE  LYS A 137     6609   6205   8961   -311   -779   -150       C  
ATOM   2138  NZ  LYS A 137       7.646  11.716   8.688  1.00 59.21           N  
ANISOU 2138  NZ  LYS A 137     6822   6286   9389   -204   -704   -407       N  
ATOM   2152  N   GLY A 138       6.824   4.512   9.737  1.00 38.67           N  
ANISOU 2152  N   GLY A 138     4696   4788   5210   -154    173   -293       N  
ATOM   2153  CA  GLY A 138       5.865   3.452   9.533  1.00 39.09           C  
ANISOU 2153  CA  GLY A 138     4747   4897   5210   -143    306   -275       C  
ATOM   2154  C   GLY A 138       4.609   3.633  10.358  1.00 38.82           C  
ANISOU 2154  C   GLY A 138     4665   4812   5273   -151    519   -491       C  
ATOM   2155  O   GLY A 138       4.301   4.725  10.849  1.00 37.81           O  
ANISOU 2155  O   GLY A 138     4480   4576   5311   -126    564   -679       O  
ATOM   2159  N   SER A 139       3.865   2.539  10.499  1.00 40.65           N  
ANISOU 2159  N   SER A 139     4908   5110   5425   -183    665   -465       N  
ATOM   2160  CA  SER A 139       2.669   2.483  11.338  1.00 43.38           C  
ANISOU 2160  CA  SER A 139     5187   5447   5849   -211    945   -636       C  
ATOM   2161  C   SER A 139       2.795   1.215  12.175  1.00 42.98           C  
ANISOU 2161  C   SER A 139     5345   5540   5446   -309   1091   -576       C  
ATOM   2162  O   SER A 139       2.551   0.108  11.682  1.00 43.37           O  
ANISOU 2162  O   SER A 139     5387   5612   5478   -347   1054   -415       O  
ATOM   2163  CB  SER A 139       1.392   2.485  10.503  1.00 43.48           C  
ANISOU 2163  CB  SER A 139     4920   5346   6256   -179    953   -613       C  
ATOM   2164  OG  SER A 139       0.246   2.537  11.336  1.00 48.15           O  
ANISOU 2164  OG  SER A 139     5373   5925   6995   -197   1270   -784       O  
ATOM   2170  N   PHE A 140       3.192   1.379  13.432  1.00 42.55           N  
ANISOU 2170  N   PHE A 140     5509   5558   5099   -355   1222   -702       N  
ATOM   2171  CA  PHE A 140       3.471   0.259  14.319  1.00 44.54           C  
ANISOU 2171  CA  PHE A 140     6023   5933   4965   -464   1311   -616       C  
ATOM   2172  C   PHE A 140       2.812   0.501  15.667  1.00 47.96           C  
ANISOU 2172  C   PHE A 140     6593   6426   5204   -529   1660   -812       C  
ATOM   2173  O   PHE A 140       2.942   1.588  16.240  1.00 48.78           O  
ANISOU 2173  O   PHE A 140     6763   6495   5274   -481   1713  -1042       O  
ATOM   2174  CB  PHE A 140       4.980   0.067  14.507  1.00 43.87           C  
ANISOU 2174  CB  PHE A 140     6168   5892   4610   -469   1031   -515       C  
ATOM   2175  CG  PHE A 140       5.703  -0.361  13.260  1.00 40.33           C  
ANISOU 2175  CG  PHE A 140     5610   5419   4295   -400    767   -316       C  
ATOM   2176  CD1 PHE A 140       5.558  -1.645  12.764  1.00 39.52           C  
ANISOU 2176  CD1 PHE A 140     5522   5332   4162   -414    736   -145       C  
ATOM   2177  CD2 PHE A 140       6.544   0.517  12.594  1.00 44.46           C  
ANISOU 2177  CD2 PHE A 140     6032   5895   4966   -325    565   -304       C  
ATOM   2178  CE1 PHE A 140       6.228  -2.043  11.621  1.00 40.07           C  
ANISOU 2178  CE1 PHE A 140     5529   5381   4316   -327    532     -4       C  
ATOM   2179  CE2 PHE A 140       7.217   0.124  11.451  1.00 40.94           C  
ANISOU 2179  CE2 PHE A 140     5501   5451   4603   -258    394   -126       C  
ATOM   2180  CZ  PHE A 140       7.059  -1.156  10.965  1.00 38.64           C  
ANISOU 2180  CZ  PHE A 140     5248   5187   4247   -245    389      5       C  
ATOM   2190  N   LEU A 141       2.101  -0.505  16.160  1.00 49.92           N  
ANISOU 2190  N   LEU A 141     6894   6751   5321   -642   1906   -722       N  
ATOM   2191  CA  LEU A 141       1.603  -0.531  17.526  1.00 54.23           C  
ANISOU 2191  CA  LEU A 141     7652   7398   5555   -737   2282   -851       C  
ATOM   2192  C   LEU A 141       2.402  -1.552  18.325  1.00 57.60           C  
ANISOU 2192  C   LEU A 141     8486   7923   5477   -874   2180   -668       C  
ATOM   2193  O   LEU A 141       3.142  -2.369  17.769  1.00 51.93           O  
ANISOU 2193  O   LEU A 141     7810   7179   4743   -885   1859   -440       O  
ATOM   2194  CB  LEU A 141       0.109  -0.868  17.557  1.00 54.78           C  
ANISOU 2194  CB  LEU A 141     7448   7479   5886   -792   2690   -856       C  
ATOM   2195  CG  LEU A 141      -0.822   0.158  16.909  1.00 55.32           C  
ANISOU 2195  CG  LEU A 141     7090   7426   6502   -651   2802  -1049       C  
ATOM   2196  CD1 LEU A 141      -2.233  -0.400  16.811  1.00 56.00           C  
ANISOU 2196  CD1 LEU A 141     6839   7506   6930   -724   3132   -983       C  
ATOM   2197  CD2 LEU A 141      -0.811   1.459  17.696  1.00 57.88           C  
ANISOU 2197  CD2 LEU A 141     7505   7737   6749   -546   2998  -1394       C  
ATOM   2209  N   ASN A 142       2.254  -1.490  19.646  1.00 72.22           N  
ANISOU 2209  N   ASN A 142    10659   9876   6905   -970   2452   -776       N  
ATOM   2210  CA  ASN A 142       2.908  -2.458  20.515  1.00 77.38           C  
ANISOU 2210  CA  ASN A 142    11742  10609   7049  -1123   2348   -580       C  
ATOM   2211  C   ASN A 142       2.610  -3.876  20.043  1.00 75.02           C  
ANISOU 2211  C   ASN A 142    11351  10294   6857  -1229   2308   -253       C  
ATOM   2212  O   ASN A 142       1.479  -4.201  19.673  1.00 76.01           O  
ANISOU 2212  O   ASN A 142    11191  10411   7280  -1271   2588   -208       O  
ATOM   2213  CB  ASN A 142       2.444  -2.271  21.959  1.00 85.99           C  
ANISOU 2213  CB  ASN A 142    13093  11795   7783  -1178   2637   -693       C  
ATOM   2214  CG  ASN A 142       2.864  -3.416  22.856  1.00 94.17           C  
ANISOU 2214  CG  ASN A 142    14462  12880   8436  -1312   2481   -418       C  
ATOM   2215  OD1 ASN A 142       3.984  -3.443  23.366  1.00 96.82           O  
ANISOU 2215  OD1 ASN A 142    15112  13197   8480  -1319   2116   -378       O  
ATOM   2216  ND2 ASN A 142       1.963  -4.372  23.055  1.00 98.71           N  
ANISOU 2216  ND2 ASN A 142    14952  13499   9054  -1426   2737   -219       N  
ATOM   2223  N   GLY A 143       3.640  -4.719  20.052  1.00 68.39           N  
ANISOU 2223  N   GLY A 143    10741   9422   5820  -1268   1928    -29       N  
ATOM   2224  CA  GLY A 143       3.522  -6.068  19.546  1.00 64.58           C  
ANISOU 2224  CA  GLY A 143    10202   8873   5462  -1341   1805    262       C  
ATOM   2225  C   GLY A 143       3.768  -6.211  18.060  1.00 55.26           C  
ANISOU 2225  C   GLY A 143     8689   7575   4733  -1187   1524    304       C  
ATOM   2226  O   GLY A 143       3.611  -7.318  17.528  1.00 56.45           O  
ANISOU 2226  O   GLY A 143     8787   7638   5022  -1226   1407    505       O  
ATOM   2230  N   SER A 144       4.141  -5.135  17.375  1.00 46.35           N  
ANISOU 2230  N   SER A 144     7363   6428   3820  -1020   1409    123       N  
ATOM   2231  CA  SER A 144       4.459  -5.200  15.954  1.00 41.86           C  
ANISOU 2231  CA  SER A 144     6536   5768   3602   -875   1157    167       C  
ATOM   2232  C   SER A 144       5.924  -5.557  15.728  1.00 42.06           C  
ANISOU 2232  C   SER A 144     6694   5765   3521   -789    784    275       C  
ATOM   2233  O   SER A 144       6.314  -5.924  14.619  1.00 37.37           O  
ANISOU 2233  O   SER A 144     5958   5105   3138   -673    594    346       O  
ATOM   2234  CB  SER A 144       4.149  -3.866  15.271  1.00 43.74           C  
ANISOU 2234  CB  SER A 144     6496   5988   4136   -753   1211    -34       C  
ATOM   2235  OG  SER A 144       4.967  -2.833  15.789  1.00 47.68           O  
ANISOU 2235  OG  SER A 144     7108   6518   4491   -704   1130   -177       O  
HETATM 2241  N   CSO A 145       6.737  -5.428  16.774  1.00 45.01           N  
ANISOU 2241  N   CSO A 145     7341   6183   3578   -839    677    277       N  
HETATM 2242  CA  CSO A 145       8.152  -5.778  16.685  1.00 45.92           C  
ANISOU 2242  CA  CSO A 145     7544   6257   3648   -762    306    390       C  
HETATM 2243  C   CSO A 145       8.317  -7.172  16.099  1.00 46.78           C  
ANISOU 2243  C   CSO A 145     7647   6276   3852   -728    158    594       C  
HETATM 2244  O   CSO A 145       7.606  -8.104  16.475  1.00 43.36           O  
ANISOU 2244  O   CSO A 145     7345   5809   3320   -852    260    712       O  
HETATM 2245  CB  CSO A 145       8.821  -5.690  18.058  1.00 47.13           C  
ANISOU 2245  CB  CSO A 145     8047   6441   3419   -865    168    403       C  
HETATM 2246  SG  CSO A 145       8.458  -4.087  18.810  1.00 47.06           S  
ANISOU 2246  SG  CSO A 145     8109   6506   3265   -903    369    104       S  
HETATM 2247  OD  CSO A 145       7.087  -4.211  19.934  1.00 49.20           O  
ANISOU 2247  OD  CSO A 145     8631   6875   3189  -1076    833     24       O  
ATOM   2253  N   GLY A 146       9.255  -7.304  15.167  1.00 47.75           N  
ANISOU 2253  N   GLY A 146     7614   6347   4182   -559    -67    630       N  
ATOM   2254  CA  GLY A 146       9.447  -8.554  14.461  1.00 47.56           C  
ANISOU 2254  CA  GLY A 146     7574   6213   4283   -476   -203    764       C  
ATOM   2255  C   GLY A 146       8.870  -8.501  13.060  1.00 44.85           C  
ANISOU 2255  C   GLY A 146     7001   5842   4197   -368   -105    694       C  
ATOM   2256  O   GLY A 146       9.219  -9.317  12.207  1.00 47.62           O  
ANISOU 2256  O   GLY A 146     7321   6101   4671   -240   -231    743       O  
ATOM   2260  N   SER A 147       7.970  -7.545  12.829  1.00 39.91           N  
ANISOU 2260  N   SER A 147     6234   5279   3652   -413    103    569       N  
ATOM   2261  CA  SER A 147       7.504  -7.270  11.477  1.00 40.24           C  
ANISOU 2261  CA  SER A 147     6073   5291   3927   -313    135    507       C  
ATOM   2262  C   SER A 147       8.704  -6.973  10.584  1.00 41.99           C  
ANISOU 2262  C   SER A 147     6201   5532   4221   -129     -3    508       C  
ATOM   2263  O   SER A 147       9.710  -6.415  11.030  1.00 37.91           O  
ANISOU 2263  O   SER A 147     5670   5073   3661   -100    -74    511       O  
ATOM   2264  CB  SER A 147       6.528  -6.091  11.477  1.00 39.09           C  
ANISOU 2264  CB  SER A 147     5768   5190   3893   -373    330    378       C  
ATOM   2265  OG  SER A 147       5.382  -6.368  12.268  1.00 41.72           O  
ANISOU 2265  OG  SER A 147     6135   5518   4198   -532    527    374       O  
ATOM   2271  N   VAL A 148       8.606  -7.362   9.315  1.00 39.26           N  
ANISOU 2271  N   VAL A 148     5799   5134   3985    -12    -42    507       N  
ATOM   2272  CA  VAL A 148       9.759  -7.306   8.427  1.00 37.06           C  
ANISOU 2272  CA  VAL A 148     5454   4883   3745    171   -111    522       C  
ATOM   2273  C   VAL A 148       9.433  -6.471   7.199  1.00 38.12           C  
ANISOU 2273  C   VAL A 148     5470   5050   3965    228    -45    476       C  
ATOM   2274  O   VAL A 148       8.274  -6.337   6.792  1.00 35.80           O  
ANISOU 2274  O   VAL A 148     5169   4705   3729    164    -22    435       O  
ATOM   2275  CB  VAL A 148      10.235  -8.717   8.008  1.00 39.73           C  
ANISOU 2275  CB  VAL A 148     5910   5118   4066    302   -224    561       C  
ATOM   2276  CG1 VAL A 148      10.714  -9.497   9.222  1.00 43.05           C  
ANISOU 2276  CG1 VAL A 148     6453   5483   4420    249   -346    649       C  
ATOM   2277  CG2 VAL A 148       9.130  -9.463   7.281  1.00 38.08           C  
ANISOU 2277  CG2 VAL A 148     5798   4790   3882    285   -247    524       C  
ATOM   2287  N   GLY A 149      10.482  -5.896   6.618  1.00 33.99           N  
ANISOU 2287  N   GLY A 149     4842   4604   3469    339    -27    505       N  
ATOM   2288  CA  GLY A 149      10.401  -5.220   5.338  1.00 33.03           C  
ANISOU 2288  CA  GLY A 149     4656   4516   3377    402     29    509       C  
ATOM   2289  C   GLY A 149      11.077  -6.071   4.282  1.00 34.57           C  
ANISOU 2289  C   GLY A 149     4932   4714   3489    587     48    519       C  
ATOM   2290  O   GLY A 149      11.987  -6.848   4.583  1.00 32.37           O  
ANISOU 2290  O   GLY A 149     4658   4432   3210    693     35    532       O  
ATOM   2294  N   PHE A 150      10.632  -5.928   3.038  1.00 30.76           N  
ANISOU 2294  N   PHE A 150     4529   4225   2935    637     69    504       N  
ATOM   2295  CA  PHE A 150      11.080  -6.850   2.010  1.00 34.16           C  
ANISOU 2295  CA  PHE A 150     5114   4640   3224    821    101    462       C  
ATOM   2296  C   PHE A 150      10.883  -6.233   0.636  1.00 38.01           C  
ANISOU 2296  C   PHE A 150     5690   5177   3575    857    155    484       C  
ATOM   2297  O   PHE A 150      10.055  -5.338   0.440  1.00 35.28           O  
ANISOU 2297  O   PHE A 150     5320   4814   3273    727     84    526       O  
ATOM   2298  CB  PHE A 150      10.329  -8.183   2.109  1.00 38.29           C  
ANISOU 2298  CB  PHE A 150     5839   4996   3713    834    -51    368       C  
ATOM   2299  CG  PHE A 150       8.858  -8.066   1.825  1.00 35.71           C  
ANISOU 2299  CG  PHE A 150     5595   4564   3411    693   -191    340       C  
ATOM   2300  CD1 PHE A 150       7.972  -7.670   2.817  1.00 35.63           C  
ANISOU 2300  CD1 PHE A 150     5458   4522   3559    503   -226    367       C  
ATOM   2301  CD2 PHE A 150       8.361  -8.341   0.562  1.00 34.29           C  
ANISOU 2301  CD2 PHE A 150     5615   4310   3102    756   -289    281       C  
ATOM   2302  CE1 PHE A 150       6.617  -7.555   2.553  1.00 34.80           C  
ANISOU 2302  CE1 PHE A 150     5355   4309   3560    383   -345    347       C  
ATOM   2303  CE2 PHE A 150       7.009  -8.228   0.292  1.00 37.08           C  
ANISOU 2303  CE2 PHE A 150     6007   4539   3541    621   -478    269       C  
ATOM   2304  CZ  PHE A 150       6.136  -7.835   1.288  1.00 38.67           C  
ANISOU 2304  CZ  PHE A 150     6010   4705   3977    437   -500    308       C  
ATOM   2314  N   ASN A 151      11.680  -6.725  -0.307  1.00 41.01           N  
ANISOU 2314  N   ASN A 151     6182   5612   3788   1044    287    457       N  
ATOM   2315  CA  ASN A 151      11.502  -6.482  -1.727  1.00 46.12           C  
ANISOU 2315  CA  ASN A 151     7038   6296   4191   1103    339    460       C  
ATOM   2316  C   ASN A 151      11.376  -7.827  -2.427  1.00 50.44           C  
ANISOU 2316  C   ASN A 151     7895   6737   4534   1275    287    288       C  
ATOM   2317  O   ASN A 151      11.897  -8.841  -1.953  1.00 48.83           O  
ANISOU 2317  O   ASN A 151     7681   6472   4400   1404    306    194       O  
ATOM   2318  CB  ASN A 151      12.674  -5.693  -2.317  1.00 47.45           C  
ANISOU 2318  CB  ASN A 151     7079   6654   4294   1169    624    589       C  
ATOM   2319  CG  ASN A 151      12.721  -4.266  -1.818  1.00 46.78           C  
ANISOU 2319  CG  ASN A 151     6733   6630   4411    983    624    762       C  
ATOM   2320  OD1 ASN A 151      13.391  -3.959  -0.832  1.00 48.53           O  
ANISOU 2320  OD1 ASN A 151     6684   6888   4866    942    661    811       O  
ATOM   2321  ND2 ASN A 151      12.003  -3.384  -2.497  1.00 47.97           N  
ANISOU 2321  ND2 ASN A 151     6981   6763   4484    868    538    852       N  
ATOM   2328  N   ILE A 152      10.668  -7.833  -3.551  1.00 47.26           N  
ANISOU 2328  N   ILE A 152     7790   6281   3888   1276    177    243       N  
ATOM   2329  CA  ILE A 152      10.514  -9.027  -4.370  1.00 48.53           C  
ANISOU 2329  CA  ILE A 152     8313   6318   3807   1440     95     51       C  
ATOM   2330  C   ILE A 152      11.085  -8.727  -5.747  1.00 52.99           C  
ANISOU 2330  C   ILE A 152     9129   7022   3983   1577    313     45       C  
ATOM   2331  O   ILE A 152      10.763  -7.694  -6.346  1.00 48.30           O  
ANISOU 2331  O   ILE A 152     8588   6509   3257   1455    298    192       O  
ATOM   2332  CB  ILE A 152       9.044  -9.474  -4.466  1.00 49.18           C  
ANISOU 2332  CB  ILE A 152     8591   6167   3927   1304   -304    -22       C  
ATOM   2333  CG1 ILE A 152       8.491  -9.754  -3.066  1.00 47.14           C  
ANISOU 2333  CG1 ILE A 152     8073   5798   4039   1152   -441     11       C  
ATOM   2334  CG2 ILE A 152       8.922 -10.713  -5.353  1.00 52.86           C  
ANISOU 2334  CG2 ILE A 152     9475   6468   4141   1472   -439   -242       C  
ATOM   2335  CD1 ILE A 152       7.079 -10.303  -3.058  1.00 50.16           C  
ANISOU 2335  CD1 ILE A 152     8571   5942   4547   1006   -799    -41       C  
ATOM   2347  N   ASP A 153      11.941  -9.623  -6.235  1.00 68.66           N  
ANISOU 2347  N   ASP A 153    11275   9029   5785   1834    528   -119       N  
ATOM   2348  CA  ASP A 153      12.501  -9.538  -7.580  1.00 77.41           C  
ANISOU 2348  CA  ASP A 153    12686  10274   6454   1997    800   -168       C  
ATOM   2349  C   ASP A 153      12.312 -10.895  -8.244  1.00 81.90           C  
ANISOU 2349  C   ASP A 153    13634  10646   6840   2178    676   -464       C  
ATOM   2350  O   ASP A 153      12.977 -11.867  -7.873  1.00 83.44           O  
ANISOU 2350  O   ASP A 153    13790  10777   7136   2406    797   -636       O  
ATOM   2351  CB  ASP A 153      13.977  -9.144  -7.541  1.00 81.20           C  
ANISOU 2351  CB  ASP A 153    12860  10999   6992   2134   1298    -69       C  
ATOM   2352  CG  ASP A 153      14.539  -8.848  -8.917  1.00 87.66           C  
ANISOU 2352  CG  ASP A 153    13825  11954   7528   2158   1580    -53       C  
ATOM   2353  OD1 ASP A 153      14.330  -9.664  -9.840  1.00 92.22           O  
ANISOU 2353  OD1 ASP A 153    14763  12429   7847   2262   1523   -265       O  
ATOM   2354  OD2 ASP A 153      15.184  -7.790  -9.078  1.00 88.68           O  
ANISOU 2354  OD2 ASP A 153    13715  12285   7695   2057   1848    178       O  
ATOM   2359  N   TYR A 154      11.403 -10.960  -9.218  1.00 83.42           N  
ANISOU 2359  N   TYR A 154    14168  10713   6816   2070    399   -518       N  
ATOM   2360  CA  TYR A 154      11.095 -12.210  -9.905  1.00 88.52           C  
ANISOU 2360  CA  TYR A 154    15187  11134   7314   2202    209   -789       C  
ATOM   2361  C   TYR A 154      10.494 -13.211  -8.922  1.00 79.66           C  
ANISOU 2361  C   TYR A 154    14070   9740   6456   2219   -129   -922       C  
ATOM   2362  O   TYR A 154       9.306 -13.129  -8.595  1.00 74.25           O  
ANISOU 2362  O   TYR A 154    13422   8887   5902   2010   -539   -869       O  
ATOM   2363  CB  TYR A 154      12.353 -12.777 -10.575  1.00100.70           C  
ANISOU 2363  CB  TYR A 154    16787  12788   8685   2471    635   -944       C  
ATOM   2364  CG  TYR A 154      12.130 -14.019 -11.425  1.00112.55           C  
ANISOU 2364  CG  TYR A 154    18701  14070   9995   2622    474  -1235       C  
ATOM   2365  CD1 TYR A 154      10.850 -14.469 -11.730  1.00116.15           C  
ANISOU 2365  CD1 TYR A 154    19472  14251  10410   2493    -39  -1314       C  
ATOM   2366  CD2 TYR A 154      13.209 -14.744 -11.917  1.00120.23           C  
ANISOU 2366  CD2 TYR A 154    19721  15096  10866   2891    830  -1433       C  
ATOM   2367  CE1 TYR A 154      10.653 -15.600 -12.504  1.00123.12           C  
ANISOU 2367  CE1 TYR A 154    20735  14916  11131   2625   -212  -1573       C  
ATOM   2368  CE2 TYR A 154      13.022 -15.872 -12.693  1.00127.35           C  
ANISOU 2368  CE2 TYR A 154    21008  15791  11590   3035    683  -1714       C  
ATOM   2369  CZ  TYR A 154      11.743 -16.297 -12.982  1.00129.27           C  
ANISOU 2369  CZ  TYR A 154    21588  15758  11771   2900    152  -1780       C  
ATOM   2370  OH  TYR A 154      11.557 -17.423 -13.752  1.00136.36           O  
ANISOU 2370  OH  TYR A 154    22876  16432  12503   3038    -22  -2057       O  
ATOM   2380  N   ASP A 155      11.303 -14.157  -8.448  1.00 76.79           N  
ANISOU 2380  N   ASP A 155    13649   9318   6212   2457     29  -1084       N  
ATOM   2381  CA  ASP A 155      10.840 -15.191  -7.535  1.00 74.03           C  
ANISOU 2381  CA  ASP A 155    13328   8678   6120   2475   -291  -1210       C  
ATOM   2382  C   ASP A 155      11.542 -15.144  -6.188  1.00 69.10           C  
ANISOU 2382  C   ASP A 155    12210   8125   5919   2466   -131  -1059       C  
ATOM   2383  O   ASP A 155      11.286 -16.009  -5.342  1.00 68.51           O  
ANISOU 2383  O   ASP A 155    12067   7819   6146   2432   -371  -1084       O  
ATOM   2384  CB  ASP A 155      11.041 -16.579  -8.163  1.00 77.19           C  
ANISOU 2384  CB  ASP A 155    14015   8837   6477   2688   -382  -1484       C  
ATOM   2385  CG  ASP A 155      12.491 -16.851  -8.524  1.00 80.39           C  
ANISOU 2385  CG  ASP A 155    14316   9401   6827   2991     93  -1591       C  
ATOM   2386  OD1 ASP A 155      13.317 -15.918  -8.434  1.00 80.16           O  
ANISOU 2386  OD1 ASP A 155    14001   9676   6779   3016    494  -1436       O  
ATOM   2387  OD2 ASP A 155      12.808 -18.001  -8.895  1.00 85.03           O  
ANISOU 2387  OD2 ASP A 155    15078   9801   7429   3192     60  -1825       O  
ATOM   2392  N   CYS A 156      12.406 -14.159  -5.960  1.00 68.25           N  
ANISOU 2392  N   CYS A 156    13165   6700   6069   1899   -112    -59       N  
ATOM   2393  CA  CYS A 156      13.264 -14.112  -4.785  1.00 67.34           C  
ANISOU 2393  CA  CYS A 156    12693   6782   6110   2082     39    -31       C  
ATOM   2394  C   CYS A 156      12.810 -12.998  -3.855  1.00 60.93           C  
ANISOU 2394  C   CYS A 156    11179   6266   5705   1658     97     59       C  
ATOM   2395  O   CYS A 156      12.672 -11.846  -4.279  1.00 56.97           O  
ANISOU 2395  O   CYS A 156    10236   6023   5386   1542    231    105       O  
ATOM   2396  CB  CYS A 156      14.723 -13.896  -5.194  1.00 66.78           C  
ANISOU 2396  CB  CYS A 156    12442   6993   5937   2696    353    -24       C  
ATOM   2397  SG  CYS A 156      15.892 -13.900  -3.819  1.00 66.97           S  
ANISOU 2397  SG  CYS A 156    12043   7285   6119   2947    521     47       S  
ATOM   2403  N   VAL A 157      12.585 -13.344  -2.592  1.00 52.71           N  
ANISOU 2403  N   VAL A 157    10072   5173   4783   1448    -10     83       N  
ATOM   2404  CA  VAL A 157      12.228 -12.369  -1.568  1.00 49.01           C  
ANISOU 2404  CA  VAL A 157     8994   4973   4657   1115     52    154       C  
ATOM   2405  C   VAL A 157      13.513 -11.865  -0.923  1.00 49.38           C  
ANISOU 2405  C   VAL A 157     8621   5306   4833   1420    292    185       C  
ATOM   2406  O   VAL A 157      14.294 -12.652  -0.378  1.00 47.30           O  
ANISOU 2406  O   VAL A 157     8535   4977   4462   1692    300    175       O  
ATOM   2407  CB  VAL A 157      11.291 -12.983  -0.517  1.00 47.56           C  
ANISOU 2407  CB  VAL A 157     8936   4626   4510    713   -186    187       C  
ATOM   2408  CG1 VAL A 157      11.019 -11.986   0.601  1.00 45.27           C  
ANISOU 2408  CG1 VAL A 157     8039   4631   4532    456    -92    249       C  
ATOM   2409  CG2 VAL A 157       9.994 -13.440  -1.162  1.00 46.90           C  
ANISOU 2409  CG2 VAL A 157     9218   4311   4292    345   -454    216       C  
ATOM   2419  N   SER A 158      13.732 -10.555  -0.982  1.00 48.34           N  
ANISOU 2419  N   SER A 158     7954   5490   4923   1361    463    242       N  
ATOM   2420  CA  SER A 158      14.873  -9.924  -0.323  1.00 45.99           C  
ANISOU 2420  CA  SER A 158     7217   5492   4766   1541    648    315       C  
ATOM   2421  C   SER A 158      14.385  -9.302   0.979  1.00 45.59           C  
ANISOU 2421  C   SER A 158     6827   5522   4972   1186    599    341       C  
ATOM   2422  O   SER A 158      13.733  -8.255   0.971  1.00 43.51           O  
ANISOU 2422  O   SER A 158     6282   5364   4884    921    604    357       O  
ATOM   2423  CB  SER A 158      15.519  -8.875  -1.222  1.00 46.03           C  
ANISOU 2423  CB  SER A 158     6893   5783   4812   1687    835    388       C  
ATOM   2424  OG  SER A 158      16.180  -9.482  -2.317  1.00 51.86           O  
ANISOU 2424  OG  SER A 158     7912   6514   5280   2100    925    380       O  
ATOM   2430  N   PHE A 159      14.696  -9.952   2.097  1.00 43.82           N  
ANISOU 2430  N   PHE A 159     6659   5243   4748   1207    548    344       N  
ATOM   2431  CA  PHE A 159      14.396  -9.393   3.406  1.00 42.20           C  
ANISOU 2431  CA  PHE A 159     6147   5137   4752    927    521    370       C  
ATOM   2432  C   PHE A 159      15.464  -8.374   3.776  1.00 39.10           C  
ANISOU 2432  C   PHE A 159     5317   5034   4506   1028    672    455       C  
ATOM   2433  O   PHE A 159      16.661  -8.674   3.735  1.00 39.22           O  
ANISOU 2433  O   PHE A 159     5291   5167   4445   1334    762    522       O  
ATOM   2434  CB  PHE A 159      14.322 -10.497   4.458  1.00 40.99           C  
ANISOU 2434  CB  PHE A 159     6237   4813   4526    886    391    355       C  
ATOM   2435  CG  PHE A 159      13.199 -11.467   4.235  1.00 40.52           C  
ANISOU 2435  CG  PHE A 159     6608   4469   4319    683    186    313       C  
ATOM   2436  CD1 PHE A 159      11.909 -11.149   4.621  1.00 39.28           C  
ANISOU 2436  CD1 PHE A 159     6345   4327   4253    275     81    334       C  
ATOM   2437  CD2 PHE A 159      13.432 -12.694   3.640  1.00 43.57           C  
ANISOU 2437  CD2 PHE A 159     7520   4584   4450    902     81    274       C  
ATOM   2438  CE1 PHE A 159      10.872 -12.036   4.419  1.00 42.48           C  
ANISOU 2438  CE1 PHE A 159     7115   4515   4510     28   -138    351       C  
ATOM   2439  CE2 PHE A 159      12.397 -13.587   3.434  1.00 47.12           C  
ANISOU 2439  CE2 PHE A 159     8416   4747   4743    653   -163    263       C  
ATOM   2440  CZ  PHE A 159      11.116 -13.257   3.825  1.00 45.44           C  
ANISOU 2440  CZ  PHE A 159     8045   4584   4636    184   -280    318       C  
ATOM   2450  N   CYS A 160      15.030  -7.167   4.139  1.00 38.58           N  
ANISOU 2450  N   CYS A 160     4938   5091   4630    774    683    471       N  
ATOM   2451  CA  CYS A 160      15.952  -6.069   4.382  1.00 39.26           C  
ANISOU 2451  CA  CYS A 160     4657   5418   4841    794    773    570       C  
ATOM   2452  C   CYS A 160      15.749  -5.356   5.709  1.00 39.56           C  
ANISOU 2452  C   CYS A 160     4497   5499   5036    555    720    574       C  
ATOM   2453  O   CYS A 160      16.584  -4.517   6.062  1.00 42.49           O  
ANISOU 2453  O   CYS A 160     4617   6037   5490    537    747    671       O  
ATOM   2454  CB  CYS A 160      15.846  -5.028   3.255  1.00 39.54           C  
ANISOU 2454  CB  CYS A 160     4548   5556   4919    764    831    603       C  
ATOM   2455  SG  CYS A 160      14.205  -4.281   3.085  1.00 40.36           S  
ANISOU 2455  SG  CYS A 160     4668   5539   5127    459    747    508       S  
ATOM   2461  N   TYR A 161      14.691  -5.656   6.455  1.00 36.61           N  
ANISOU 2461  N   TYR A 161     4235   4995   4680    365    635    490       N  
ATOM   2462  CA  TYR A 161      14.370  -4.876   7.640  1.00 36.81           C  
ANISOU 2462  CA  TYR A 161     4096   5068   4820    170    601    479       C  
ATOM   2463  C   TYR A 161      13.589  -5.733   8.622  1.00 35.60           C  
ANISOU 2463  C   TYR A 161     4089   4820   4619     45    525    429       C  
ATOM   2464  O   TYR A 161      12.749  -6.543   8.224  1.00 34.55           O  
ANISOU 2464  O   TYR A 161     4154   4576   4397    -10    468    400       O  
ATOM   2465  CB  TYR A 161      13.557  -3.626   7.271  1.00 34.06           C  
ANISOU 2465  CB  TYR A 161     3627   4754   4562     39    606    447       C  
ATOM   2466  CG  TYR A 161      13.163  -2.762   8.449  1.00 31.26           C  
ANISOU 2466  CG  TYR A 161     3166   4430   4280   -100    573    416       C  
ATOM   2467  CD1 TYR A 161      14.039  -1.816   8.963  1.00 34.28           C  
ANISOU 2467  CD1 TYR A 161     3426   4871   4727   -120    555    467       C  
ATOM   2468  CD2 TYR A 161      11.912  -2.884   9.041  1.00 31.24           C  
ANISOU 2468  CD2 TYR A 161     3200   4413   4255   -210    548    355       C  
ATOM   2469  CE1 TYR A 161      13.687  -1.021  10.034  1.00 33.09           C  
ANISOU 2469  CE1 TYR A 161     3260   4708   4605   -220    508    423       C  
ATOM   2470  CE2 TYR A 161      11.550  -2.091  10.117  1.00 29.75           C  
ANISOU 2470  CE2 TYR A 161     2943   4269   4094   -272    538    319       C  
ATOM   2471  CZ  TYR A 161      12.444  -1.162  10.608  1.00 32.80           C  
ANISOU 2471  CZ  TYR A 161     3276   4657   4532   -264    515    336       C  
ATOM   2472  OH  TYR A 161      12.102  -0.364  11.676  1.00 32.90           O  
ANISOU 2472  OH  TYR A 161     3297   4670   4532   -302    487    285       O  
ATOM   2482  N   MET A 162      13.886  -5.550   9.905  1.00 33.58           N  
ANISOU 2482  N   MET A 162     3743   4609   4404    -26    504    441       N  
ATOM   2483  CA  MET A 162      13.085  -6.101  10.987  1.00 32.39           C  
ANISOU 2483  CA  MET A 162     3672   4422   4212   -182    440    412       C  
ATOM   2484  C   MET A 162      12.845  -4.990  11.996  1.00 32.56           C  
ANISOU 2484  C   MET A 162     3526   4541   4305   -288    454    389       C  
ATOM   2485  O   MET A 162      13.793  -4.331  12.432  1.00 28.33           O  
ANISOU 2485  O   MET A 162     2891   4047   3825   -253    458    419       O  
ATOM   2486  CB  MET A 162      13.775  -7.294  11.651  1.00 34.90           C  
ANISOU 2486  CB  MET A 162     4142   4666   4454   -120    384    447       C  
ATOM   2487  CG  MET A 162      13.027  -7.838  12.857  1.00 38.24           C  
ANISOU 2487  CG  MET A 162     4634   5071   4824   -313    307    442       C  
ATOM   2488  SD  MET A 162      13.664  -9.425  13.427  1.00 43.58           S  
ANISOU 2488  SD  MET A 162     5578   5597   5383   -252    199    486       S  
ATOM   2489  CE  MET A 162      12.791 -10.556  12.346  1.00 44.62           C  
ANISOU 2489  CE  MET A 162     6052   5533   5368   -295     91    479       C  
ATOM   2499  N   HIS A 163      11.583  -4.778  12.356  1.00 32.17           N  
ANISOU 2499  N   HIS A 163     3456   4540   4229   -409    452    353       N  
ATOM   2500  CA  HIS A 163      11.232  -3.688  13.253  1.00 32.83           C  
ANISOU 2500  CA  HIS A 163     3431   4708   4333   -443    477    312       C  
ATOM   2501  C   HIS A 163      11.591  -4.043  14.690  1.00 33.25           C  
ANISOU 2501  C   HIS A 163     3516   4777   4339   -501    443    319       C  
ATOM   2502  O   HIS A 163      11.298  -5.148  15.158  1.00 31.93           O  
ANISOU 2502  O   HIS A 163     3427   4607   4096   -583    406    352       O  
ATOM   2503  CB  HIS A 163       9.743  -3.370  13.153  1.00 32.91           C  
ANISOU 2503  CB  HIS A 163     3379   4828   4299   -492    509    294       C  
ATOM   2504  CG  HIS A 163       9.312  -2.260  14.056  1.00 31.33           C  
ANISOU 2504  CG  HIS A 163     3111   4717   4075   -446    549    240       C  
ATOM   2505  ND1 HIS A 163       9.778  -0.972  13.920  1.00 31.85           N  
ANISOU 2505  ND1 HIS A 163     3183   4720   4199   -349    549    187       N  
ATOM   2506  CD2 HIS A 163       8.475  -2.248  15.120  1.00 33.14           C  
ANISOU 2506  CD2 HIS A 163     3301   5091   4199   -466    582    235       C  
ATOM   2507  CE1 HIS A 163       9.241  -0.210  14.855  1.00 33.16           C  
ANISOU 2507  CE1 HIS A 163     3365   4947   4288   -286    572    130       C  
ATOM   2508  NE2 HIS A 163       8.446  -0.960  15.596  1.00 35.03           N  
ANISOU 2508  NE2 HIS A 163     3554   5334   4422   -335    612    157       N  
ATOM   2516  N   HIS A 164      12.214  -3.097  15.393  1.00 31.05           N  
ANISOU 2516  N   HIS A 164     3209   4499   4091   -482    432    298       N  
ATOM   2517  CA  HIS A 164      12.628  -3.315  16.772  1.00 30.16           C  
ANISOU 2517  CA  HIS A 164     3140   4393   3925   -543    388    306       C  
ATOM   2518  C   HIS A 164      12.026  -2.320  17.749  1.00 35.25           C  
ANISOU 2518  C   HIS A 164     3807   5087   4499   -546    402    233       C  
ATOM   2519  O   HIS A 164      11.498  -2.729  18.789  1.00 38.30           O  
ANISOU 2519  O   HIS A 164     4221   5549   4780   -595    414    223       O  
ATOM   2520  CB  HIS A 164      14.157  -3.254  16.891  1.00 32.44           C  
ANISOU 2520  CB  HIS A 164     3417   4633   4275   -529    322    380       C  
ATOM   2521  CG  HIS A 164      14.854  -4.485  16.408  1.00 33.17           C  
ANISOU 2521  CG  HIS A 164     3524   4704   4377   -465    313    458       C  
ATOM   2522  ND1 HIS A 164      15.480  -5.368  17.260  1.00 33.58           N  
ANISOU 2522  ND1 HIS A 164     3628   4742   4388   -479    256    513       N  
ATOM   2523  CD2 HIS A 164      15.034  -4.974  15.159  1.00 34.31           C  
ANISOU 2523  CD2 HIS A 164     3672   4826   4540   -351    349    485       C  
ATOM   2524  CE1 HIS A 164      16.012  -6.352  16.557  1.00 34.34           C  
ANISOU 2524  CE1 HIS A 164     3771   4803   4475   -350    258    569       C  
ATOM   2525  NE2 HIS A 164      15.755  -6.137  15.279  1.00 35.51           N  
ANISOU 2525  NE2 HIS A 164     3900   4944   4648   -264    318    548       N  
ATOM   2533  N   MET A 165      12.080  -1.025  17.455  1.00 36.20           N  
ANISOU 2533  N   MET A 165     3944   5161   4648   -481    393    185       N  
ATOM   2534  CA  MET A 165      11.700  -0.053  18.465  1.00 39.74           C  
ANISOU 2534  CA  MET A 165     4503   5605   4991   -436    382    104       C  
ATOM   2535  C   MET A 165      11.113   1.191  17.821  1.00 38.92           C  
ANISOU 2535  C   MET A 165     4439   5464   4886   -308    400     35       C  
ATOM   2536  O   MET A 165      11.373   1.507  16.658  1.00 36.26           O  
ANISOU 2536  O   MET A 165     4051   5070   4655   -304    383     65       O  
ATOM   2537  CB  MET A 165      12.901   0.329  19.337  1.00 42.08           C  
ANISOU 2537  CB  MET A 165     4920   5791   5278   -523    254    130       C  
ATOM   2538  CG  MET A 165      14.017   1.012  18.570  1.00 41.06           C  
ANISOU 2538  CG  MET A 165     4784   5559   5257   -581    146    207       C  
ATOM   2539  SD  MET A 165      15.527   1.171  19.539  1.00 44.90           S  
ANISOU 2539  SD  MET A 165     5343   5981   5734   -756    -36    322       S  
ATOM   2540  CE  MET A 165      14.879   1.854  21.062  1.00 45.87           C  
ANISOU 2540  CE  MET A 165     5746   6020   5664   -736    -82    183       C  
ATOM   2567  N   GLU A 166      10.311   1.890  18.614  1.00 39.27           N  
ANISOU 2567  N   GLU A 166     4590   5545   4786   -178    435    -55       N  
ATOM   2568  CA  GLU A 166       9.782   3.203  18.278  1.00 43.57           C  
ANISOU 2568  CA  GLU A 166     5255   6019   5282      0    430   -139       C  
ATOM   2569  C   GLU A 166      10.499   4.225  19.149  1.00 46.18           C  
ANISOU 2569  C   GLU A 166     5888   6141   5518      3    284   -200       C  
ATOM   2570  O   GLU A 166      10.582   4.052  20.369  1.00 44.77           O  
ANISOU 2570  O   GLU A 166     5823   5977   5209     -2    273   -233       O  
ATOM   2571  CB  GLU A 166       8.272   3.271  18.512  1.00 48.45           C  
ANISOU 2571  CB  GLU A 166     5794   6857   5759    213    581   -185       C  
ATOM   2572  CG  GLU A 166       7.641   4.606  18.142  1.00 51.52           C  
ANISOU 2572  CG  GLU A 166     6315   7182   6077    468    584   -271       C  
ATOM   2573  CD  GLU A 166       6.131   4.598  18.298  1.00 49.47           C  
ANISOU 2573  CD  GLU A 166     5902   7224   5672    715    755   -273       C  
ATOM   2574  OE1 GLU A 166       5.643   4.692  19.445  1.00 51.89           O  
ANISOU 2574  OE1 GLU A 166     6275   7668   5774    877    832   -317       O  
ATOM   2575  OE2 GLU A 166       5.434   4.482  17.271  1.00 44.29           O  
ANISOU 2575  OE2 GLU A 166     5043   6696   5091    745    813   -211       O  
ATOM   2582  N   LEU A 167      11.027   5.271  18.527  1.00 45.61           N  
ANISOU 2582  N   LEU A 167     5968   5867   5494    -15    148   -202       N  
ATOM   2583  CA  LEU A 167      11.751   6.284  19.273  1.00 47.64           C  
ANISOU 2583  CA  LEU A 167     6572   5884   5647    -69    -52   -234       C  
ATOM   2584  C   LEU A 167      10.778   7.258  19.930  1.00 50.49           C  
ANISOU 2584  C   LEU A 167     7238   6166   5780    229    -34   -397       C  
ATOM   2585  O   LEU A 167       9.632   7.396  19.494  1.00 50.97           O  
ANISOU 2585  O   LEU A 167     7205   6358   5801    483    119   -458       O  
ATOM   2586  CB  LEU A 167      12.708   7.035  18.353  1.00 47.86           C  
ANISOU 2586  CB  LEU A 167     6663   5731   5790   -248   -241   -134       C  
ATOM   2587  CG  LEU A 167      13.685   6.171  17.552  1.00 46.61           C  
ANISOU 2587  CG  LEU A 167     6186   5694   5828   -471   -237     43       C  
ATOM   2588  CD1 LEU A 167      14.665   7.047  16.785  1.00 48.25           C  
ANISOU 2588  CD1 LEU A 167     6456   5773   6105   -663   -438    178       C  
ATOM   2589  CD2 LEU A 167      14.430   5.200  18.454  1.00 46.99           C  
ANISOU 2589  CD2 LEU A 167     6142   5833   5879   -611   -245    117       C  
ATOM   2601  N   PRO A 168      11.211   7.949  20.989  1.00 55.17           N  
ANISOU 2601  N   PRO A 168     8214   6552   6198    223   -195   -461       N  
ATOM   2602  CA  PRO A 168      10.314   8.915  21.645  1.00 56.65           C  
ANISOU 2602  CA  PRO A 168     8767   6641   6117    577   -179   -632       C  
ATOM   2603  C   PRO A 168       9.765   9.971  20.702  1.00 54.84           C  
ANISOU 2603  C   PRO A 168     8687   6274   5877    791   -216   -690       C  
ATOM   2604  O   PRO A 168       8.750  10.599  21.026  1.00 56.18           O  
ANISOU 2604  O   PRO A 168     9058   6454   5834   1189   -127   -825       O  
ATOM   2605  CB  PRO A 168      11.201   9.540  22.731  1.00 59.38           C  
ANISOU 2605  CB  PRO A 168     9577   6692   6294    442   -434   -665       C  
ATOM   2606  CG  PRO A 168      12.263   8.526  22.988  1.00 58.51           C  
ANISOU 2606  CG  PRO A 168     9214   6674   6343     65   -485   -510       C  
ATOM   2607  CD  PRO A 168      12.515   7.857  21.669  1.00 56.05           C  
ANISOU 2607  CD  PRO A 168     8457   6521   6317    -88   -404   -371       C  
ATOM   2615  N   THR A 169      10.398  10.186  19.550  1.00 52.53           N  
ANISOU 2615  N   THR A 169     8298   5871   5790    563   -340   -581       N  
ATOM   2616  CA  THR A 169       9.910  11.144  18.566  1.00 53.75           C  
ANISOU 2616  CA  THR A 169     8578   5892   5953    732   -389   -616       C  
ATOM   2617  C   THR A 169       8.849  10.559  17.641  1.00 52.17           C  
ANISOU 2617  C   THR A 169     7955   6000   5868    914   -131   -599       C  
ATOM   2618  O   THR A 169       8.327  11.286  16.789  1.00 54.28           O  
ANISOU 2618  O   THR A 169     8283   6195   6145   1079   -149   -622       O  
ATOM   2619  CB  THR A 169      11.078  11.671  17.728  1.00 53.97           C  
ANISOU 2619  CB  THR A 169     8689   5687   6128    375   -652   -476       C  
ATOM   2620  OG1 THR A 169      11.699  10.583  17.034  1.00 52.23           O  
ANISOU 2620  OG1 THR A 169     7994   5699   6151     99   -560   -312       O  
ATOM   2621  CG2 THR A 169      12.110  12.355  18.618  1.00 55.29           C  
ANISOU 2621  CG2 THR A 169     9303   5544   6160    145   -964   -452       C  
ATOM   2629  N   GLY A 170       8.516   9.278  17.781  1.00 54.21           N  
ANISOU 2629  N   GLY A 170     7811   6584   6201    865     79   -546       N  
ATOM   2630  CA  GLY A 170       7.483   8.666  16.974  1.00 52.18           C  
ANISOU 2630  CA  GLY A 170     7176   6623   6026    985    286   -503       C  
ATOM   2631  C   GLY A 170       7.954   8.015  15.693  1.00 51.93           C  
ANISOU 2631  C   GLY A 170     6855   6634   6243    719    282   -375       C  
ATOM   2632  O   GLY A 170       7.119   7.492  14.944  1.00 51.82           O  
ANISOU 2632  O   GLY A 170     6560   6837   6291    778    419   -328       O  
ATOM   2636  N   VAL A 171       9.253   8.048  15.401  1.00 48.48           N  
ANISOU 2636  N   VAL A 171     6478   6018   5925    436    122   -301       N  
ATOM   2637  CA  VAL A 171       9.786   7.378  14.221  1.00 43.74           C  
ANISOU 2637  CA  VAL A 171     5610   5485   5522    227    137   -176       C  
ATOM   2638  C   VAL A 171      10.267   5.993  14.632  1.00 40.94           C  
ANISOU 2638  C   VAL A 171     5046   5285   5223     67    215   -108       C  
ATOM   2639  O   VAL A 171      10.339   5.673  15.825  1.00 41.71           O  
ANISOU 2639  O   VAL A 171     5213   5408   5225     66    223   -144       O  
ATOM   2640  CB  VAL A 171      10.917   8.186  13.557  1.00 45.31           C  
ANISOU 2640  CB  VAL A 171     5943   5475   5800     33    -65    -88       C  
ATOM   2641  CG1 VAL A 171      10.376   9.496  13.007  1.00 48.22           C  
ANISOU 2641  CG1 VAL A 171     6541   5666   6115    183   -161   -146       C  
ATOM   2642  CG2 VAL A 171      12.057   8.434  14.537  1.00 46.12           C  
ANISOU 2642  CG2 VAL A 171     6239   5435   5847   -159   -243    -44       C  
ATOM   2652  N   HIS A 172      10.608   5.166  13.652  1.00 37.08           N  
ANISOU 2652  N   HIS A 172     4336   4884   4870    -52    263    -12       N  
ATOM   2653  CA  HIS A 172      10.836   3.749  13.881  1.00 36.73           C  
ANISOU 2653  CA  HIS A 172     4123   4975   4857   -144    343     42       C  
ATOM   2654  C   HIS A 172      12.244   3.353  13.463  1.00 36.99           C  
ANISOU 2654  C   HIS A 172     4093   4976   4987   -301    274    161       C  
ATOM   2655  O   HIS A 172      12.784   3.872  12.482  1.00 34.07           O  
ANISOU 2655  O   HIS A 172     3695   4564   4687   -344    221    232       O  
ATOM   2656  CB  HIS A 172       9.791   2.925  13.130  1.00 34.62           C  
ANISOU 2656  CB  HIS A 172     3686   4861   4607    -95    468     52       C  
ATOM   2657  CG  HIS A 172       8.384   3.281  13.495  1.00 33.94           C  
ANISOU 2657  CG  HIS A 172     3584   4897   4415     67    548    -11       C  
ATOM   2658  ND1 HIS A 172       7.520   3.900  12.618  1.00 37.50           N  
ANISOU 2658  ND1 HIS A 172     3987   5386   4874    188    577    -19       N  
ATOM   2659  CD2 HIS A 172       7.701   3.132  14.654  1.00 36.57           C  
ANISOU 2659  CD2 HIS A 172     3922   5360   4612    149    610    -49       C  
ATOM   2660  CE1 HIS A 172       6.359   4.101  13.216  1.00 39.08           C  
ANISOU 2660  CE1 HIS A 172     4144   5757   4948    358    661    -49       C  
ATOM   2661  NE2 HIS A 172       6.443   3.645  14.453  1.00 38.24           N  
ANISOU 2661  NE2 HIS A 172     4065   5721   4745    340    690    -66       N  
ATOM   2669  N   ALA A 173      12.834   2.438  14.229  1.00 36.41           N  
ANISOU 2669  N   ALA A 173     3983   4950   4900   -372    276    202       N  
ATOM   2670  CA  ALA A 173      14.187   1.959  13.994  1.00 35.37           C  
ANISOU 2670  CA  ALA A 173     3762   4845   4833   -469    226    337       C  
ATOM   2671  C   ALA A 173      14.204   0.440  14.057  1.00 33.99           C  
ANISOU 2671  C   ALA A 173     3504   4756   4655   -440    312    360       C  
ATOM   2672  O   ALA A 173      13.432  -0.177  14.796  1.00 33.91           O  
ANISOU 2672  O   ALA A 173     3536   4769   4580   -430    355    292       O  
ATOM   2673  CB  ALA A 173      15.173   2.535  15.018  1.00 36.94           C  
ANISOU 2673  CB  ALA A 173     4052   4984   5000   -598     77    399       C  
ATOM   2679  N   GLY A 174      15.095  -0.155  13.274  1.00 32.77           N  
ANISOU 2679  N   GLY A 174     3249   4656   4547   -415    328    468       N  
ATOM   2680  CA  GLY A 174      15.187  -1.593  13.192  1.00 32.21           C  
ANISOU 2680  CA  GLY A 174     3173   4618   4447   -345    385    487       C  
ATOM   2681  C   GLY A 174      16.515  -2.020  12.609  1.00 33.77           C  
ANISOU 2681  C   GLY A 174     3270   4900   4663   -263    389    629       C  
ATOM   2682  O   GLY A 174      17.404  -1.201  12.366  1.00 30.50           O  
ANISOU 2682  O   GLY A 174     2740   4562   4287   -306    343    746       O  
ATOM   2686  N   THR A 175      16.631  -3.323  12.376  1.00 29.91           N  
ANISOU 2686  N   THR A 175     2835   4406   4121   -137    435    637       N  
ATOM   2687  CA  THR A 175      17.867  -3.946  11.937  1.00 34.01           C  
ANISOU 2687  CA  THR A 175     3277   5031   4614     30    462    771       C  
ATOM   2688  C   THR A 175      17.672  -4.608  10.580  1.00 34.15           C  
ANISOU 2688  C   THR A 175     3377   5027   4570    222    548    749       C  
ATOM   2689  O   THR A 175      16.549  -4.783  10.098  1.00 32.47           O  
ANISOU 2689  O   THR A 175     3305   4694   4338    183    558    634       O  
ATOM   2690  CB  THR A 175      18.344  -5.004  12.944  1.00 36.84           C  
ANISOU 2690  CB  THR A 175     3702   5375   4920     81    423    802       C  
ATOM   2691  OG1 THR A 175      17.418  -6.101  12.956  1.00 32.77           O  
ANISOU 2691  OG1 THR A 175     3418   4704   4331    111    423    689       O  
ATOM   2692  CG2 THR A 175      18.465  -4.416  14.354  1.00 34.89           C  
ANISOU 2692  CG2 THR A 175     3415   5132   4710   -121    328    814       C  
ATOM   2700  N   ASP A 176      18.794  -4.972   9.962  1.00 33.82           N  
ANISOU 2700  N   ASP A 176     3246   5126   4477    439    604    877       N  
ATOM   2701  CA  ASP A 176      18.768  -5.953   8.890  1.00 37.94           C  
ANISOU 2701  CA  ASP A 176     3937   5599   4877    700    678    848       C  
ATOM   2702  C   ASP A 176      18.560  -7.337   9.506  1.00 37.13           C  
ANISOU 2702  C   ASP A 176     4106   5325   4678    793    626    780       C  
ATOM   2703  O   ASP A 176      18.420  -7.488  10.722  1.00 37.37           O  
ANISOU 2703  O   ASP A 176     4148   5305   4746    642    548    765       O  
ATOM   2704  CB  ASP A 176      20.046  -5.868   8.049  1.00 38.08           C  
ANISOU 2704  CB  ASP A 176     3764   5871   4834    957    777   1022       C  
ATOM   2705  CG  ASP A 176      21.312  -6.129   8.850  1.00 39.27           C  
ANISOU 2705  CG  ASP A 176     3727   6223   4970   1067    768   1197       C  
ATOM   2706  OD1 ASP A 176      21.241  -6.734   9.938  1.00 37.98           O  
ANISOU 2706  OD1 ASP A 176     3673   5947   4811   1023    692   1155       O  
ATOM   2707  OD2 ASP A 176      22.394  -5.720   8.379  1.00 42.22           O  
ANISOU 2707  OD2 ASP A 176     3822   6901   5318   1188    832   1405       O  
ATOM   2712  N   LEU A 177      18.521  -8.364   8.663  1.00 35.95           N  
ANISOU 2712  N   LEU A 177     4219   5063   4379   1039    651    739       N  
ATOM   2713  CA  LEU A 177      18.252  -9.710   9.153  1.00 40.87           C  
ANISOU 2713  CA  LEU A 177     5184   5463   4880   1109    557    675       C  
ATOM   2714  C   LEU A 177      19.481 -10.377   9.754  1.00 45.81           C  
ANISOU 2714  C   LEU A 177     5786   6178   5441   1375    564    781       C  
ATOM   2715  O   LEU A 177      19.365 -11.494  10.271  1.00 46.03           O  
ANISOU 2715  O   LEU A 177     6116   6009   5366   1441    466    741       O  
ATOM   2716  CB  LEU A 177      17.680 -10.574   8.028  1.00 43.71           C  
ANISOU 2716  CB  LEU A 177     5934   5604   5069   1254    531    585       C  
ATOM   2717  CG  LEU A 177      16.149 -10.590   7.961  1.00 41.94           C  
ANISOU 2717  CG  LEU A 177     5884   5190   4861    913    419    486       C  
ATOM   2718  CD1 LEU A 177      15.571 -11.338   9.155  1.00 42.13           C  
ANISOU 2718  CD1 LEU A 177     6078   5065   4865    694    269    469       C  
ATOM   2719  CD2 LEU A 177      15.580  -9.175   7.895  1.00 40.19           C  
ANISOU 2719  CD2 LEU A 177     5324   5129   4818    666    479    483       C  
ATOM   2731  N   GLU A 178      20.642  -9.728   9.702  1.00 52.98           N  
ANISOU 2731  N   GLU A 178     6343   7389   6398   1512    660    939       N  
ATOM   2732  CA  GLU A 178      21.810 -10.174  10.448  1.00 54.61           C  
ANISOU 2732  CA  GLU A 178     6426   7752   6571   1712    657   1085       C  
ATOM   2733  C   GLU A 178      21.898  -9.535  11.830  1.00 53.38           C  
ANISOU 2733  C   GLU A 178     6049   7664   6570   1378    564   1142       C  
ATOM   2734  O   GLU A 178      22.862  -9.796  12.557  1.00 55.50           O  
ANISOU 2734  O   GLU A 178     6179   8081   6829   1482    538   1285       O  
ATOM   2735  CB  GLU A 178      23.088  -9.885   9.653  1.00 56.75           C  
ANISOU 2735  CB  GLU A 178     6400   8385   6779   2045    800   1285       C  
ATOM   2736  CG  GLU A 178      23.330 -10.872   8.520  1.00 60.47           C  
ANISOU 2736  CG  GLU A 178     7149   8808   7019   2534    899   1250       C  
ATOM   2737  CD  GLU A 178      24.584 -10.564   7.727  1.00 63.64           C  
ANISOU 2737  CD  GLU A 178     7208   9647   7327   2894   1072   1477       C  
ATOM   2738  OE1 GLU A 178      24.853  -9.371   7.475  1.00 64.32           O  
ANISOU 2738  OE1 GLU A 178     6895  10011   7532   2672   1117   1615       O  
ATOM   2739  OE2 GLU A 178      25.302 -11.517   7.359  1.00 66.99           O  
ANISOU 2739  OE2 GLU A 178     7769  10146   7537   3410   1154   1531       O  
ATOM   2746  N   GLY A 179      20.919  -8.716  12.209  1.00 47.01           N  
ANISOU 2746  N   GLY A 179     5222   6758   5882   1005    511   1038       N  
ATOM   2747  CA  GLY A 179      20.859  -8.155  13.542  1.00 44.01           C  
ANISOU 2747  CA  GLY A 179     4725   6392   5603    709    417   1056       C  
ATOM   2748  C   GLY A 179      21.574  -6.837  13.729  1.00 42.90           C  
ANISOU 2748  C   GLY A 179     4254   6479   5565    550    404   1201       C  
ATOM   2749  O   GLY A 179      21.661  -6.358  14.866  1.00 40.85           O  
ANISOU 2749  O   GLY A 179     3937   6223   5362    319    305   1227       O  
ATOM   2753  N   ASN A 180      22.084  -6.234  12.659  1.00 44.84           N  
ANISOU 2753  N   ASN A 180     4310   6909   5817    645    482   1307       N  
ATOM   2754  CA  ASN A 180      22.794  -4.965  12.743  1.00 44.69           C  
ANISOU 2754  CA  ASN A 180     3998   7106   5875    447    430   1486       C  
ATOM   2755  C   ASN A 180      21.824  -3.812  12.530  1.00 43.88           C  
ANISOU 2755  C   ASN A 180     3959   6861   5853    184    393   1357       C  
ATOM   2756  O   ASN A 180      21.128  -3.756  11.510  1.00 40.70           O  
ANISOU 2756  O   ASN A 180     3640   6383   5441    257    475   1250       O  
ATOM   2757  CB  ASN A 180      23.911  -4.905  11.702  1.00 44.96           C  
ANISOU 2757  CB  ASN A 180     3764   7468   5852    676    525   1718       C  
ATOM   2758  CG  ASN A 180      24.903  -6.033  11.854  1.00 47.83           C  
ANISOU 2758  CG  ASN A 180     4054   8011   6107   1023    581   1861       C  
ATOM   2759  OD1 ASN A 180      25.091  -6.839  10.944  1.00 49.65           O  
ANISOU 2759  OD1 ASN A 180     4356   8296   6214   1405    715   1854       O  
ATOM   2760  ND2 ASN A 180      25.545  -6.100  13.013  1.00 49.28           N  
ANISOU 2760  ND2 ASN A 180     4124   8281   6318    915    470   1991       N  
ATOM   2767  N   PHE A 181      21.794  -2.887  13.483  1.00 38.66           N  
ANISOU 2767  N   PHE A 181     3282   6156   5250   -102    259   1371       N  
ATOM   2768  CA  PHE A 181      20.870  -1.768  13.399  1.00 37.85           C  
ANISOU 2768  CA  PHE A 181     3286   5898   5196   -302    211   1241       C  
ATOM   2769  C   PHE A 181      21.192  -0.883  12.203  1.00 38.39           C  
ANISOU 2769  C   PHE A 181     3211   6086   5288   -327    225   1355       C  
ATOM   2770  O   PHE A 181      22.358  -0.660  11.866  1.00 34.24           O  
ANISOU 2770  O   PHE A 181     2449   5809   4750   -335    199   1603       O  
ATOM   2771  CB  PHE A 181      20.923  -0.938  14.682  1.00 35.35           C  
ANISOU 2771  CB  PHE A 181     3042   5498   4892   -564     45   1244       C  
ATOM   2772  CG  PHE A 181      19.751  -1.160  15.590  1.00 37.52           C  
ANISOU 2772  CG  PHE A 181     3549   5566   5140   -594     51   1017       C  
ATOM   2773  CD1 PHE A 181      18.565  -0.473  15.394  1.00 36.59           C  
ANISOU 2773  CD1 PHE A 181     3574   5306   5022   -624     75    844       C  
ATOM   2774  CD2 PHE A 181      19.831  -2.064  16.634  1.00 37.51           C  
ANISOU 2774  CD2 PHE A 181     3608   5545   5098   -581     36    998       C  
ATOM   2775  CE1 PHE A 181      17.481  -0.682  16.227  1.00 37.05           C  
ANISOU 2775  CE1 PHE A 181     3795   5254   5030   -628    100    673       C  
ATOM   2776  CE2 PHE A 181      18.751  -2.277  17.470  1.00 37.85           C  
ANISOU 2776  CE2 PHE A 181     3835   5453   5094   -621     48    822       C  
ATOM   2777  CZ  PHE A 181      17.575  -1.585  17.267  1.00 38.74           C  
ANISOU 2777  CZ  PHE A 181     4052   5472   5195   -639     89    667       C  
ATOM   2787  N   TYR A 182      20.143  -0.388  11.554  1.00 38.35           N  
ANISOU 2787  N   TYR A 182     3331   5933   5307   -344    262   1197       N  
ATOM   2788  CA  TYR A 182      20.286   0.747  10.655  1.00 40.03           C  
ANISOU 2788  CA  TYR A 182     3465   6197   5547   -450    220   1286       C  
ATOM   2789  C   TYR A 182      20.405   2.014  11.495  1.00 39.08           C  
ANISOU 2789  C   TYR A 182     3425   5976   5447   -734     18   1326       C  
ATOM   2790  O   TYR A 182      19.550   2.287  12.344  1.00 42.02           O  
ANISOU 2790  O   TYR A 182     4015   6137   5814   -787    -32   1143       O  
ATOM   2791  CB  TYR A 182      19.095   0.847   9.704  1.00 36.10           C  
ANISOU 2791  CB  TYR A 182     3091   5563   5063   -365    311   1108       C  
ATOM   2792  CG  TYR A 182      19.039  -0.232   8.643  1.00 37.41           C  
ANISOU 2792  CG  TYR A 182     3233   5803   5178   -115    472   1091       C  
ATOM   2793  CD1 TYR A 182      19.881  -0.196   7.536  1.00 38.97           C  
ANISOU 2793  CD1 TYR A 182     3257   6214   5335     -9    539   1263       C  
ATOM   2794  CD2 TYR A 182      18.128  -1.275   8.735  1.00 33.93           C  
ANISOU 2794  CD2 TYR A 182     2970   5220   4702      5    540    917       C  
ATOM   2795  CE1 TYR A 182      19.825  -1.176   6.561  1.00 39.84           C  
ANISOU 2795  CE1 TYR A 182     3413   6365   5357    260    681   1230       C  
ATOM   2796  CE2 TYR A 182      18.064  -2.260   7.766  1.00 35.17           C  
ANISOU 2796  CE2 TYR A 182     3196   5388   4780    222    645    895       C  
ATOM   2797  CZ  TYR A 182      18.913  -2.206   6.681  1.00 40.92           C  
ANISOU 2797  CZ  TYR A 182     3792   6299   5455    372    721   1035       C  
ATOM   2798  OH  TYR A 182      18.848  -3.185   5.716  1.00 38.87           O  
ANISOU 2798  OH  TYR A 182     3665   6027   5078    626    822    997       O  
ATOM   2808  N   GLY A 183      21.468   2.777  11.271  1.00 39.49           N  
ANISOU 2808  N   GLY A 183     3320   6190   5496   -914   -111   1581       N  
ATOM   2809  CA  GLY A 183      21.706   3.976  12.036  1.00 39.09           C  
ANISOU 2809  CA  GLY A 183     3406   6015   5432  -1219   -359   1650       C  
ATOM   2810  C   GLY A 183      22.406   3.673  13.344  1.00 40.89           C  
ANISOU 2810  C   GLY A 183     3626   6280   5629  -1336   -476   1743       C  
ATOM   2811  O   GLY A 183      22.773   2.529  13.628  1.00 41.68           O  
ANISOU 2811  O   GLY A 183     3580   6527   5728  -1170   -359   1772       O  
ATOM   2815  N   PRO A 184      22.589   4.698  14.178  1.00 42.22           N  
ANISOU 2815  N   PRO A 184     3996   6290   5757  -1621   -729   1787       N  
ATOM   2816  CA  PRO A 184      23.386   4.525  15.399  1.00 43.90           C  
ANISOU 2816  CA  PRO A 184     4203   6550   5926  -1790   -885   1922       C  
ATOM   2817  C   PRO A 184      22.573   4.090  16.608  1.00 46.40           C  
ANISOU 2817  C   PRO A 184     4785   6639   6206  -1695   -850   1653       C  
ATOM   2818  O   PRO A 184      23.021   4.256  17.747  1.00 51.58           O  
ANISOU 2818  O   PRO A 184     5560   7237   6801  -1877  -1028   1714       O  
ATOM   2819  CB  PRO A 184      23.971   5.925  15.612  1.00 47.31           C  
ANISOU 2819  CB  PRO A 184     4785   6893   6299  -2184  -1219   2118       C  
ATOM   2820  CG  PRO A 184      22.869   6.833  15.127  1.00 48.13           C  
ANISOU 2820  CG  PRO A 184     5205   6693   6391  -2141  -1231   1884       C  
ATOM   2821  CD  PRO A 184      22.149   6.094  14.005  1.00 45.10           C  
ANISOU 2821  CD  PRO A 184     4638   6409   6089  -1808   -916   1738       C  
ATOM   2829  N   PHE A 185      21.389   3.533  16.381  1.00 42.78           N  
ANISOU 2829  N   PHE A 185     4414   6074   5767  -1432   -634   1380       N  
ATOM   2830  CA  PHE A 185      20.482   3.235  17.478  1.00 42.55           C  
ANISOU 2830  CA  PHE A 185     4625   5865   5679  -1353   -595   1142       C  
ATOM   2831  C   PHE A 185      20.812   1.890  18.120  1.00 41.27           C  
ANISOU 2831  C   PHE A 185     4330   5830   5521  -1262   -505   1170       C  
ATOM   2832  O   PHE A 185      21.475   1.031  17.533  1.00 40.51           O  
ANISOU 2832  O   PHE A 185     3979   5937   5476  -1154   -413   1310       O  
ATOM   2833  CB  PHE A 185      19.034   3.226  16.992  1.00 41.71           C  
ANISOU 2833  CB  PHE A 185     4634   5640   5573  -1144   -423    888       C  
ATOM   2834  CG  PHE A 185      18.668   4.419  16.156  1.00 42.57           C  
ANISOU 2834  CG  PHE A 185     4851   5636   5688  -1174   -486    861       C  
ATOM   2835  CD1 PHE A 185      18.606   5.683  16.718  1.00 42.27           C  
ANISOU 2835  CD1 PHE A 185     5119   5382   5559  -1311   -695    828       C  
ATOM   2836  CD2 PHE A 185      18.380   4.275  14.808  1.00 39.49           C  
ANISOU 2836  CD2 PHE A 185     4302   5329   5374  -1059   -354    868       C  
ATOM   2837  CE1 PHE A 185      18.270   6.783  15.953  1.00 42.93           C  
ANISOU 2837  CE1 PHE A 185     5346   5329   5636  -1330   -778    806       C  
ATOM   2838  CE2 PHE A 185      18.042   5.373  14.037  1.00 43.19           C  
ANISOU 2838  CE2 PHE A 185     4875   5688   5846  -1093   -424    853       C  
ATOM   2839  CZ  PHE A 185      17.987   6.627  14.611  1.00 44.47           C  
ANISOU 2839  CZ  PHE A 185     5341   5629   5925  -1226   -639    824       C  
ATOM   2849  N   VAL A 186      20.324   1.718  19.347  1.00 40.46           N  
ANISOU 2849  N   VAL A 186     4428   5602   5340  -1280   -533   1033       N  
ATOM   2850  CA  VAL A 186      20.502   0.490  20.109  1.00 41.63           C  
ANISOU 2850  CA  VAL A 186     4515   5828   5476  -1217   -474   1041       C  
ATOM   2851  C   VAL A 186      19.157   0.098  20.703  1.00 42.43           C  
ANISOU 2851  C   VAL A 186     4799   5815   5506  -1106   -354    797       C  
ATOM   2852  O   VAL A 186      18.290   0.947  20.939  1.00 40.76           O  
ANISOU 2852  O   VAL A 186     4787   5477   5224  -1099   -360    644       O  
ATOM   2853  CB  VAL A 186      21.568   0.649  21.217  1.00 44.85           C  
ANISOU 2853  CB  VAL A 186     4942   6265   5836  -1431   -682   1211       C  
ATOM   2854  CG1 VAL A 186      22.910   1.014  20.607  1.00 45.22           C  
ANISOU 2854  CG1 VAL A 186     4740   6504   5939  -1566   -807   1516       C  
ATOM   2855  CG2 VAL A 186      21.141   1.700  22.232  1.00 44.96           C  
ANISOU 2855  CG2 VAL A 186     5299   6058   5727  -1590   -841   1092       C  
ATOM   2865  N   ASP A 187      18.981  -1.204  20.940  1.00 40.28           N  
ANISOU 2865  N   ASP A 187     4462   5607   5233  -1007   -253    780       N  
ATOM   2866  CA  ASP A 187      17.711  -1.730  21.443  1.00 38.31           C  
ANISOU 2866  CA  ASP A 187     4334   5316   4908   -938   -144    606       C  
ATOM   2867  C   ASP A 187      17.687  -1.578  22.962  1.00 42.58           C  
ANISOU 2867  C   ASP A 187     5043   5809   5328  -1050   -234    570       C  
ATOM   2868  O   ASP A 187      17.898  -2.519  23.731  1.00 39.47           O  
ANISOU 2868  O   ASP A 187     4648   5450   4897  -1083   -250    610       O  
ATOM   2869  CB  ASP A 187      17.502  -3.177  21.006  1.00 37.99           C  
ANISOU 2869  CB  ASP A 187     4211   5331   4894   -830    -41    621       C  
ATOM   2870  CG  ASP A 187      18.725  -4.051  21.227  1.00 37.77           C  
ANISOU 2870  CG  ASP A 187     4096   5361   4893   -815   -107    781       C  
ATOM   2871  OD1 ASP A 187      19.776  -3.533  21.653  1.00 37.32           O  
ANISOU 2871  OD1 ASP A 187     3978   5349   4852   -910   -227    912       O  
ATOM   2872  OD2 ASP A 187      18.632  -5.268  20.961  1.00 40.16           O  
ANISOU 2872  OD2 ASP A 187     4408   5664   5188   -705    -56    790       O  
ATOM   2877  N   ARG A 188      17.409  -0.352  23.392  1.00 43.14           N  
ANISOU 2877  N   ARG A 188     5298   5779   5313  -1095   -306    487       N  
ATOM   2878  CA  ARG A 188      17.278  -0.035  24.805  1.00 46.89           C  
ANISOU 2878  CA  ARG A 188     6000   6187   5629  -1169   -390    424       C  
ATOM   2879  C   ARG A 188      16.395   1.198  24.924  1.00 43.69           C  
ANISOU 2879  C   ARG A 188     5835   5670   5095  -1072   -380    260       C  
ATOM   2880  O   ARG A 188      16.461   2.097  24.083  1.00 43.77           O  
ANISOU 2880  O   ARG A 188     5878   5596   5157  -1052   -425    257       O  
ATOM   2881  CB  ARG A 188      18.660   0.179  25.439  1.00 51.07           C  
ANISOU 2881  CB  ARG A 188     6567   6676   6161  -1378   -613    590       C  
ATOM   2882  CG  ARG A 188      18.752   1.311  26.437  1.00 59.69           C  
ANISOU 2882  CG  ARG A 188     7997   7599   7086  -1496   -794    536       C  
ATOM   2883  CD  ARG A 188      20.056   1.232  27.226  1.00 66.25           C  
ANISOU 2883  CD  ARG A 188     8843   8425   7904  -1746  -1027    731       C  
ATOM   2884  NE  ARG A 188      20.013   2.052  28.436  1.00 72.87           N  
ANISOU 2884  NE  ARG A 188    10075   9080   8531  -1860  -1204    655       N  
ATOM   2885  CZ  ARG A 188      20.831   3.068  28.707  1.00 77.62           C  
ANISOU 2885  CZ  ARG A 188    10899   9529   9065  -2097  -1492    765       C  
ATOM   2886  NH1 ARG A 188      21.795   3.417  27.863  1.00 78.09           N  
ANISOU 2886  NH1 ARG A 188    10769   9642   9260  -2274  -1636    989       N  
ATOM   2887  NH2 ARG A 188      20.686   3.735  29.843  1.00 80.59           N  
ANISOU 2887  NH2 ARG A 188    11707   9705   9210  -2170  -1652    665       N  
ATOM   2901  N   GLN A 189      15.549   1.218  25.952  1.00 43.88           N  
ANISOU 2901  N   GLN A 189     6030   5707   4934   -985   -315    132       N  
ATOM   2902  CA  GLN A 189      14.595   2.310  26.140  1.00 49.51           C  
ANISOU 2902  CA  GLN A 189     6987   6346   5478   -798   -273    -35       C  
ATOM   2903  C   GLN A 189      15.328   3.507  26.731  1.00 48.32           C  
ANISOU 2903  C   GLN A 189     7205   5945   5209   -898   -518    -49       C  
ATOM   2904  O   GLN A 189      15.365   3.711  27.946  1.00 50.62           O  
ANISOU 2904  O   GLN A 189     7766   6165   5303   -916   -597   -104       O  
ATOM   2905  CB  GLN A 189      13.438   1.871  27.028  1.00 54.69           C  
ANISOU 2905  CB  GLN A 189     7667   7169   5942   -637    -98   -137       C  
ATOM   2906  CG  GLN A 189      12.360   2.928  27.187  1.00 62.16           C  
ANISOU 2906  CG  GLN A 189     8830   8104   6685   -350    -10   -300       C  
ATOM   2907  CD  GLN A 189      11.194   2.454  28.032  1.00 67.36           C  
ANISOU 2907  CD  GLN A 189     9437   9026   7130   -171    192   -355       C  
ATOM   2908  OE1 GLN A 189      10.935   1.255  28.137  1.00 68.32           O  
ANISOU 2908  OE1 GLN A 189     9291   9364   7303   -278    290   -261       O  
ATOM   2909  NE2 GLN A 189      10.486   3.397  28.644  1.00 69.44           N  
ANISOU 2909  NE2 GLN A 189     9974   9282   7129    111    245   -495       N  
ATOM   2918  N   THR A 190      15.919   4.312  25.853  1.00 53.47           N  
ANISOU 2918  N   THR A 190     7895   6456   5964   -987   -661     16       N  
ATOM   2919  CA  THR A 190      16.579   5.542  26.261  1.00 57.05           C  
ANISOU 2919  CA  THR A 190     8743   6638   6295  -1129   -946     29       C  
ATOM   2920  C   THR A 190      16.422   6.565  25.148  1.00 57.30           C  
ANISOU 2920  C   THR A 190     8861   6532   6378  -1076  -1007     12       C  
ATOM   2921  O   THR A 190      16.132   6.222  23.999  1.00 56.61           O  
ANISOU 2921  O   THR A 190     8459   6583   6467   -997   -852     42       O  
ATOM   2922  CB  THR A 190      18.065   5.322  26.573  1.00 55.67           C  
ANISOU 2922  CB  THR A 190     8503   6451   6200  -1489  -1190    263       C  
ATOM   2923  OG1 THR A 190      18.607   6.500  27.184  1.00 59.19           O  
ANISOU 2923  OG1 THR A 190     9403   6615   6472  -1673  -1509    281       O  
ATOM   2924  CG2 THR A 190      18.841   5.014  25.299  1.00 51.56           C  
ANISOU 2924  CG2 THR A 190     7592   6070   5927  -1619  -1193    470       C  
ATOM   2932  N   ALA A 191      16.617   7.832  25.502  1.00 65.01           N  
ANISOU 2932  N   ALA A 191    10311   7210   7182  -1129  -1258    -34       N  
ATOM   2933  CA  ALA A 191      16.557   8.905  24.519  1.00 66.10           C  
ANISOU 2933  CA  ALA A 191    10606   7165   7344  -1117  -1378    -33       C  
ATOM   2934  C   ALA A 191      17.699   8.745  23.521  1.00 64.33           C  
ANISOU 2934  C   ALA A 191    10049   7038   7355  -1446  -1502    238       C  
ATOM   2935  O   ALA A 191      18.874   8.760  23.902  1.00 64.92           O  
ANISOU 2935  O   ALA A 191    10127   7099   7442  -1787  -1741    446       O  
ATOM   2936  CB  ALA A 191      16.630  10.262  25.214  1.00 69.41           C  
ANISOU 2936  CB  ALA A 191    11690   7192   7491  -1138  -1682   -124       C  
ATOM   2942  N   GLN A 192      17.354   8.584  22.246  1.00 56.48           N  
ANISOU 2942  N   GLN A 192     8752   6175   6531  -1339  -1337    256       N  
ATOM   2943  CA  GLN A 192      18.333   8.419  21.180  1.00 56.17           C  
ANISOU 2943  CA  GLN A 192     8371   6281   6691  -1582  -1403    510       C  
ATOM   2944  C   GLN A 192      18.060   9.452  20.101  1.00 57.95           C  
ANISOU 2944  C   GLN A 192     8723   6361   6934  -1562  -1484    506       C  
ATOM   2945  O   GLN A 192      16.920   9.595  19.649  1.00 57.43           O  
ANISOU 2945  O   GLN A 192     8698   6266   6858  -1259  -1301    314       O  
ATOM   2946  CB  GLN A 192      18.281   7.008  20.589  1.00 51.34           C  
ANISOU 2946  CB  GLN A 192     7246   5996   6265  -1469  -1111    557       C  
ATOM   2947  CG  GLN A 192      18.477   5.913  21.616  1.00 48.22           C  
ANISOU 2947  CG  GLN A 192     6738   5731   5851  -1469  -1031    559       C  
ATOM   2948  CD  GLN A 192      18.495   4.534  20.999  1.00 45.93           C  
ANISOU 2948  CD  GLN A 192     6025   5707   5719  -1363   -794    616       C  
ATOM   2949  OE1 GLN A 192      19.269   4.262  20.083  1.00 46.85           O  
ANISOU 2949  OE1 GLN A 192     5867   5971   5964  -1436   -793    799       O  
ATOM   2950  NE2 GLN A 192      17.637   3.655  21.494  1.00 44.54           N  
ANISOU 2950  NE2 GLN A 192     5817   5599   5508  -1185   -602    469       N  
ATOM   2959  N   ALA A 193      19.104  10.159  19.684  1.00 63.53           N  
ANISOU 2959  N   ALA A 193     9475   7003   7662  -1902  -1768    744       N  
ATOM   2960  CA  ALA A 193      18.965  11.244  18.724  1.00 65.74           C  
ANISOU 2960  CA  ALA A 193     9933   7110   7936  -1951  -1912    774       C  
ATOM   2961  C   ALA A 193      19.004  10.685  17.307  1.00 64.03           C  
ANISOU 2961  C   ALA A 193     9224   7178   7927  -1900  -1697    883       C  
ATOM   2962  O   ALA A 193      19.946   9.975  16.938  1.00 61.17           O  
ANISOU 2962  O   ALA A 193     8450   7106   7684  -2068  -1658   1119       O  
ATOM   2963  CB  ALA A 193      20.070  12.281  18.922  1.00 65.72           C  
ANISOU 2963  CB  ALA A 193    10223   6913   7833  -2399  -2357   1020       C  
ATOM   2969  N   ALA A 194      17.974  10.990  16.526  1.00 66.28           N  
ANISOU 2969  N   ALA A 194     9558   7392   8233  -1640  -1553    714       N  
ATOM   2970  CA  ALA A 194      18.021  10.801  15.085  1.00 65.94           C  
ANISOU 2970  CA  ALA A 194     9172   7536   8344  -1634  -1429    824       C  
ATOM   2971  C   ALA A 194      18.536  12.086  14.448  1.00 65.35           C  
ANISOU 2971  C   ALA A 194     9322   7280   8228  -1903  -1738    992       C  
ATOM   2972  O   ALA A 194      18.257  13.188  14.932  1.00 67.49           O  
ANISOU 2972  O   ALA A 194    10102   7197   8342  -1932  -1985    901       O  
ATOM   2973  CB  ALA A 194      16.643  10.440  14.531  1.00 69.20           C  
ANISOU 2973  CB  ALA A 194     9507   7984   8801  -1254  -1137    588       C  
ATOM   2979  N   GLY A 195      19.310  11.941  13.377  1.00 58.17           N  
ANISOU 2979  N   GLY A 195     8057   6612   7431  -2096  -1738   1249       N  
ATOM   2980  CA  GLY A 195      19.872  13.085  12.694  1.00 55.15           C  
ANISOU 2980  CA  GLY A 195     7829   6116   7010  -2407  -2038   1465       C  
ATOM   2981  C   GLY A 195      18.845  13.819  11.855  1.00 53.68           C  
ANISOU 2981  C   GLY A 195     7865   5714   6817  -2207  -2015   1296       C  
ATOM   2982  O   GLY A 195      17.661  13.485  11.816  1.00 50.28           O  
ANISOU 2982  O   GLY A 195     7460   5238   6407  -1820  -1766   1017       O  
ATOM   2986  N   THR A 196      19.322  14.856  11.171  1.00 53.07           N  
ANISOU 2986  N   THR A 196     7944   5519   6700  -2500  -2299   1499       N  
ATOM   2987  CA  THR A 196      18.467  15.599  10.259  1.00 53.38           C  
ANISOU 2987  CA  THR A 196     8183   5362   6735  -2343  -2309   1383       C  
ATOM   2988  C   THR A 196      17.896  14.650   9.212  1.00 51.99           C  
ANISOU 2988  C   THR A 196     7539   5496   6720  -2063  -1915   1310       C  
ATOM   2989  O   THR A 196      18.616  13.821   8.648  1.00 48.54           O  
ANISOU 2989  O   THR A 196     6632   5430   6383  -2161  -1761   1502       O  
ATOM   2990  CB  THR A 196      19.259  16.727   9.593  1.00 54.60           C  
ANISOU 2990  CB  THR A 196     8511   5404   6831  -2778  -2689   1682       C  
ATOM   2991  OG1 THR A 196      19.854  17.558  10.599  1.00 56.55           O  
ANISOU 2991  OG1 THR A 196     9202   5398   6885  -3033  -3072   1757       O  
ATOM   2992  CG2 THR A 196      18.355  17.580   8.712  1.00 54.97           C  
ANISOU 2992  CG2 THR A 196     8835   5193   6858  -2613  -2738   1555       C  
ATOM   3000  N   ASP A 197      16.590  14.750   8.976  1.00 55.00           N  
ANISOU 3000  N   ASP A 197     8062   5733   7104  -1695  -1757   1038       N  
ATOM   3001  CA  ASP A 197      15.917  13.952   7.951  1.00 54.51           C  
ANISOU 3001  CA  ASP A 197     7630   5912   7169  -1454  -1433    967       C  
ATOM   3002  C   ASP A 197      15.863  14.793   6.681  1.00 53.67           C  
ANISOU 3002  C   ASP A 197     7577   5735   7079  -1557  -1556   1080       C  
ATOM   3003  O   ASP A 197      15.053  15.714   6.567  1.00 56.93           O  
ANISOU 3003  O   ASP A 197     8348   5858   7426  -1414  -1675    947       O  
ATOM   3004  CB  ASP A 197      14.525  13.537   8.416  1.00 53.95           C  
ANISOU 3004  CB  ASP A 197     7625   5789   7083  -1034  -1204    663       C  
ATOM   3005  CG  ASP A 197      13.849  12.565   7.461  1.00 51.81           C  
ANISOU 3005  CG  ASP A 197     6979   5777   6931   -838   -897    613       C  
ATOM   3006  OD1 ASP A 197      14.506  12.096   6.509  1.00 48.14           O  
ANISOU 3006  OD1 ASP A 197     6216   5525   6550   -986   -833    784       O  
ATOM   3007  OD2 ASP A 197      12.653  12.272   7.668  1.00 52.50           O  
ANISOU 3007  OD2 ASP A 197     7076   5869   7004   -536   -729    417       O  
ATOM   3012  N   THR A 198      16.742  14.490   5.732  1.00 50.43           N  
ANISOU 3012  N   THR A 198     6820   5603   6737  -1785  -1529   1336       N  
ATOM   3013  CA  THR A 198      16.779  15.207   4.467  1.00 49.96           C  
ANISOU 3013  CA  THR A 198     6765   5530   6687  -1916  -1634   1478       C  
ATOM   3014  C   THR A 198      15.868  14.532   3.441  1.00 45.97           C  
ANISOU 3014  C   THR A 198     6018   5176   6271  -1620  -1329   1344       C  
ATOM   3015  O   THR A 198      15.439  13.388   3.609  1.00 44.67           O  
ANISOU 3015  O   THR A 198     5626   5183   6163  -1381  -1047   1204       O  
ATOM   3016  CB  THR A 198      18.216  15.287   3.940  1.00 50.00           C  
ANISOU 3016  CB  THR A 198     6505   5810   6684  -2322  -1765   1864       C  
ATOM   3017  OG1 THR A 198      18.793  13.975   3.891  1.00 48.44           O  
ANISOU 3017  OG1 THR A 198     5839   6020   6547  -2242  -1484   1942       O  
ATOM   3018  CG2 THR A 198      19.071  16.172   4.848  1.00 48.61           C  
ANISOU 3018  CG2 THR A 198     6625   5446   6397  -2701  -2156   2047       C  
ATOM   3026  N   THR A 199      15.565  15.271   2.374  1.00 44.29           N  
ANISOU 3026  N   THR A 199     5892   4878   6059  -1664  -1421   1401       N  
ATOM   3027  CA  THR A 199      14.709  14.785   1.298  1.00 43.62           C  
ANISOU 3027  CA  THR A 199     5621   4911   6042  -1433  -1188   1304       C  
ATOM   3028  C   THR A 199      15.535  14.062   0.241  1.00 41.01           C  
ANISOU 3028  C   THR A 199     4891   4949   5743  -1559  -1037   1519       C  
ATOM   3029  O   THR A 199      16.574  14.563  -0.201  1.00 40.46           O  
ANISOU 3029  O   THR A 199     4746   4995   5630  -1866  -1196   1799       O  
ATOM   3030  CB  THR A 199      13.949  15.941   0.648  1.00 46.52           C  
ANISOU 3030  CB  THR A 199     6289   5005   6382  -1394  -1364   1261       C  
ATOM   3031  OG1 THR A 199      13.149  16.607   1.631  1.00 46.21           O  
ANISOU 3031  OG1 THR A 199     6648   4634   6276  -1190  -1485   1050       O  
ATOM   3032  CG2 THR A 199      13.055  15.432  -0.475  1.00 46.27           C  
ANISOU 3032  CG2 THR A 199     6056   5108   6417  -1181  -1141   1181       C  
ATOM   3040  N   ILE A 200      15.047  12.899  -0.185  1.00 40.14           N  
ANISOU 3040  N   ILE A 200     4542   5028   5680  -1319   -743   1404       N  
ATOM   3041  CA  ILE A 200      15.769  12.051  -1.127  1.00 38.16           C  
ANISOU 3041  CA  ILE A 200     3959   5121   5420  -1340   -562   1566       C  
ATOM   3042  C   ILE A 200      15.607  12.620  -2.531  1.00 39.68           C  
ANISOU 3042  C   ILE A 200     4142   5340   5593  -1411   -601   1672       C  
ATOM   3043  O   ILE A 200      14.642  12.308  -3.238  1.00 35.62           O  
ANISOU 3043  O   ILE A 200     3644   4786   5103  -1224   -477   1529       O  
ATOM   3044  CB  ILE A 200      15.276  10.596  -1.048  1.00 36.22           C  
ANISOU 3044  CB  ILE A 200     3564   5000   5196  -1061   -278   1392       C  
ATOM   3045  CG1 ILE A 200      15.315  10.091   0.397  1.00 38.78           C  
ANISOU 3045  CG1 ILE A 200     3927   5271   5536   -998   -257   1278       C  
ATOM   3046  CG2 ILE A 200      16.139   9.700  -1.914  1.00 37.93           C  
ANISOU 3046  CG2 ILE A 200     3506   5549   5357  -1027   -101   1552       C  
ATOM   3047  CD1 ILE A 200      14.266   9.025   0.706  1.00 37.28           C  
ANISOU 3047  CD1 ILE A 200     3739   5056   5371   -744    -66   1046       C  
ATOM   3059  N   THR A 201      16.575  13.439  -2.948  1.00 40.87           N  
ANISOU 3059  N   THR A 201     4258   5581   5691  -1712   -787   1952       N  
ATOM   3060  CA  THR A 201      16.430  14.221  -4.172  1.00 42.48           C  
ANISOU 3060  CA  THR A 201     4511   5764   5865  -1836   -889   2075       C  
ATOM   3061  C   THR A 201      16.236  13.331  -5.394  1.00 40.44           C  
ANISOU 3061  C   THR A 201     4024   5757   5585  -1654   -621   2066       C  
ATOM   3062  O   THR A 201      15.379  13.606  -6.243  1.00 38.27           O  
ANISOU 3062  O   THR A 201     3857   5362   5323  -1579   -620   1980       O  
ATOM   3063  CB  THR A 201      17.656  15.114  -4.350  1.00 43.05           C  
ANISOU 3063  CB  THR A 201     4535   5962   5859  -2244  -1139   2437       C  
ATOM   3064  OG1 THR A 201      17.837  15.913  -3.173  1.00 46.23           O  
ANISOU 3064  OG1 THR A 201     5222   6085   6257  -2433  -1427   2440       O  
ATOM   3065  CG2 THR A 201      17.496  16.015  -5.565  1.00 42.22           C  
ANISOU 3065  CG2 THR A 201     4517   5811   5714  -2411  -1283   2579       C  
ATOM   3073  N   VAL A 202      17.029  12.265  -5.512  1.00 40.83           N  
ANISOU 3073  N   VAL A 202     3784   6149   5579  -1563   -403   2159       N  
ATOM   3074  CA  VAL A 202      16.942  11.424  -6.700  1.00 42.96           C  
ANISOU 3074  CA  VAL A 202     3905   6642   5778  -1371   -164   2158       C  
ATOM   3075  C   VAL A 202      15.553  10.812  -6.820  1.00 39.44           C  
ANISOU 3075  C   VAL A 202     3627   5970   5389  -1116    -51   1846       C  
ATOM   3076  O   VAL A 202      15.037  10.635  -7.930  1.00 38.22           O  
ANISOU 3076  O   VAL A 202     3496   5834   5191  -1036     24   1815       O  
ATOM   3077  CB  VAL A 202      18.045  10.346  -6.680  1.00 43.21           C  
ANISOU 3077  CB  VAL A 202     3647   7063   5708  -1242     50   2296       C  
ATOM   3078  CG1 VAL A 202      17.824   9.361  -5.541  1.00 39.39           C  
ANISOU 3078  CG1 VAL A 202     3198   6490   5278  -1039    158   2086       C  
ATOM   3079  CG2 VAL A 202      18.106   9.624  -8.020  1.00 44.10           C  
ANISOU 3079  CG2 VAL A 202     3671   7401   5684  -1029    265   2316       C  
ATOM   3089  N   ASN A 203      14.914  10.502  -5.689  1.00 36.52           N  
ANISOU 3089  N   ASN A 203     3369   5403   5101  -1008    -52   1634       N  
ATOM   3090  CA  ASN A 203      13.565   9.947  -5.729  1.00 34.32           C  
ANISOU 3090  CA  ASN A 203     3212   4960   4867   -808     33   1388       C  
ATOM   3091  C   ASN A 203      12.542  10.994  -6.151  1.00 36.94           C  
ANISOU 3091  C   ASN A 203     3717   5069   5250   -847   -121   1332       C  
ATOM   3092  O   ASN A 203      11.579  10.677  -6.860  1.00 35.70           O  
ANISOU 3092  O   ASN A 203     3597   4876   5094   -739    -61   1239       O  
ATOM   3093  CB  ASN A 203      13.202   9.365  -4.365  1.00 33.17           C  
ANISOU 3093  CB  ASN A 203     3107   4720   4774   -698     73   1219       C  
ATOM   3094  CG  ASN A 203      13.967   8.100  -4.057  1.00 34.06           C  
ANISOU 3094  CG  ASN A 203     3082   5028   4831   -598    241   1238       C  
ATOM   3095  OD1 ASN A 203      14.924   7.756  -4.749  1.00 35.41           O  
ANISOU 3095  OD1 ASN A 203     3113   5428   4914   -591    328   1396       O  
ATOM   3096  ND2 ASN A 203      13.553   7.399  -3.013  1.00 34.08           N  
ANISOU 3096  ND2 ASN A 203     3125   4958   4866   -497    291   1088       N  
ATOM   3103  N   VAL A 204      12.720  12.241  -5.713  1.00 39.00           N  
ANISOU 3103  N   VAL A 204     4113   5166   5540   -998   -340   1396       N  
ATOM   3104  CA  VAL A 204      11.835  13.314  -6.159  1.00 38.64           C  
ANISOU 3104  CA  VAL A 204     4268   4894   5521  -1004   -506   1359       C  
ATOM   3105  C   VAL A 204      11.891  13.443  -7.675  1.00 36.37           C  
ANISOU 3105  C   VAL A 204     3915   4716   5188  -1085   -493   1490       C  
ATOM   3106  O   VAL A 204      10.858  13.569  -8.346  1.00 36.62           O  
ANISOU 3106  O   VAL A 204     4017   4659   5239   -984   -496   1410       O  
ATOM   3107  CB  VAL A 204      12.213  14.639  -5.468  1.00 41.59           C  
ANISOU 3107  CB  VAL A 204     4875   5039   5889  -1168   -783   1428       C  
ATOM   3108  CG1 VAL A 204      11.368  15.777  -6.013  1.00 41.26           C  
ANISOU 3108  CG1 VAL A 204     5082   4744   5850  -1144   -973   1403       C  
ATOM   3109  CG2 VAL A 204      12.057  14.522  -3.953  1.00 40.47           C  
ANISOU 3109  CG2 VAL A 204     4843   4769   5765  -1057   -795   1275       C  
ATOM   3119  N   LEU A 205      13.100  13.408  -8.240  1.00 33.80           N  
ANISOU 3119  N   LEU A 205     3436   4620   4788  -1265   -477   1715       N  
ATOM   3120  CA  LEU A 205      13.251  13.533  -9.685  1.00 37.45           C  
ANISOU 3120  CA  LEU A 205     3830   5225   5174  -1342   -453   1861       C  
ATOM   3121  C   LEU A 205      12.539  12.402 -10.414  1.00 34.88           C  
ANISOU 3121  C   LEU A 205     3454   4984   4816  -1119   -234   1721       C  
ATOM   3122  O   LEU A 205      11.868  12.632 -11.427  1.00 33.46           O  
ANISOU 3122  O   LEU A 205     3344   4753   4618  -1115   -262   1717       O  
ATOM   3123  CB  LEU A 205      14.734  13.561 -10.055  1.00 36.41           C  
ANISOU 3123  CB  LEU A 205     3485   5416   4935  -1539   -434   2154       C  
ATOM   3124  CG  LEU A 205      15.496  14.827  -9.663  1.00 38.63           C  
ANISOU 3124  CG  LEU A 205     3831   5634   5211  -1875   -722   2382       C  
ATOM   3125  CD1 LEU A 205      16.992  14.643  -9.878  1.00 40.86           C  
ANISOU 3125  CD1 LEU A 205     3820   6333   5371  -2041   -675   2690       C  
ATOM   3126  CD2 LEU A 205      14.987  16.024 -10.453  1.00 41.27           C  
ANISOU 3126  CD2 LEU A 205     4382   5754   5545  -2040   -957   2450       C  
ATOM   3138  N   ALA A 206      12.681  11.169  -9.922  1.00 32.15           N  
ANISOU 3138  N   ALA A 206     3018   4750   4448   -951    -41   1618       N  
ATOM   3139  CA  ALA A 206      11.977  10.050 -10.537  1.00 35.34           C  
ANISOU 3139  CA  ALA A 206     3451   5181   4796   -768    118   1486       C  
ATOM   3140  C   ALA A 206      10.469  10.250 -10.461  1.00 37.14           C  
ANISOU 3140  C   ALA A 206     3815   5182   5116   -714     33   1324       C  
ATOM   3141  O   ALA A 206       9.741   9.923 -11.405  1.00 37.22           O  
ANISOU 3141  O   ALA A 206     3882   5180   5079   -678     54   1294       O  
ATOM   3142  CB  ALA A 206      12.381   8.741  -9.863  1.00 31.87           C  
ANISOU 3142  CB  ALA A 206     2953   4846   4310   -606    291   1404       C  
ATOM   3148  N   TRP A 207       9.985  10.792  -9.342  1.00 35.35           N  
ANISOU 3148  N   TRP A 207     3638   4794   4999   -696    -65   1234       N  
ATOM   3149  CA  TRP A 207       8.558  11.048  -9.186  1.00 36.64           C  
ANISOU 3149  CA  TRP A 207     3884   4808   5231   -599   -132   1112       C  
ATOM   3150  C   TRP A 207       8.083  12.120 -10.162  1.00 38.69           C  
ANISOU 3150  C   TRP A 207     4230   4971   5499   -661   -282   1189       C  
ATOM   3151  O   TRP A 207       7.003  11.996 -10.753  1.00 34.11           O  
ANISOU 3151  O   TRP A 207     3665   4371   4924   -597   -293   1151       O  
ATOM   3152  CB  TRP A 207       8.285  11.447  -7.737  1.00 38.61           C  
ANISOU 3152  CB  TRP A 207     4178   4939   5553   -517   -187   1011       C  
ATOM   3153  CG  TRP A 207       6.867  11.767  -7.395  1.00 38.84           C  
ANISOU 3153  CG  TRP A 207     4254   4877   5627   -358   -234    907       C  
ATOM   3154  CD1 TRP A 207       5.833  10.887  -7.258  1.00 36.02           C  
ANISOU 3154  CD1 TRP A 207     3806   4612   5267   -252   -141    834       C  
ATOM   3155  CD2 TRP A 207       6.333  13.062  -7.102  1.00 40.23           C  
ANISOU 3155  CD2 TRP A 207     4580   4876   5831   -268   -395    888       C  
ATOM   3156  NE1 TRP A 207       4.686  11.556  -6.911  1.00 37.38           N  
ANISOU 3156  NE1 TRP A 207     3998   4737   5467    -92   -210    792       N  
ATOM   3157  CE2 TRP A 207       4.966  12.893  -6.809  1.00 39.50           C  
ANISOU 3157  CE2 TRP A 207     4433   4824   5750    -63   -358    806       C  
ATOM   3158  CE3 TRP A 207       6.878  14.349  -7.063  1.00 42.55           C  
ANISOU 3158  CE3 TRP A 207     5070   4977   6119   -343   -587    948       C  
ATOM   3159  CZ2 TRP A 207       4.136  13.962  -6.486  1.00 43.53           C  
ANISOU 3159  CZ2 TRP A 207     5069   5211   6261    141   -471    768       C  
ATOM   3160  CZ3 TRP A 207       6.051  15.410  -6.743  1.00 47.11           C  
ANISOU 3160  CZ3 TRP A 207     5842   5362   6695   -162   -731    890       C  
ATOM   3161  CH2 TRP A 207       4.695  15.209  -6.457  1.00 46.17           C  
ANISOU 3161  CH2 TRP A 207     5653   5308   6581    112   -656    793       C  
ATOM   3172  N   LEU A 208       8.884  13.170 -10.360  1.00 39.72           N  
ANISOU 3172  N   LEU A 208     4423   5047   5622   -813   -419   1321       N  
ATOM   3173  CA  LEU A 208       8.532  14.185 -11.347  1.00 40.91           C  
ANISOU 3173  CA  LEU A 208     4682   5096   5768   -896   -581   1414       C  
ATOM   3174  C   LEU A 208       8.502  13.592 -12.751  1.00 39.25           C  
ANISOU 3174  C   LEU A 208     4397   5043   5474   -942   -485   1487       C  
ATOM   3175  O   LEU A 208       7.651  13.960 -13.570  1.00 40.38           O  
ANISOU 3175  O   LEU A 208     4607   5114   5622   -931   -565   1496       O  
ATOM   3176  CB  LEU A 208       9.515  15.354 -11.275  1.00 43.18           C  
ANISOU 3176  CB  LEU A 208     5072   5299   6037  -1112   -777   1578       C  
ATOM   3177  CG  LEU A 208       9.487  16.190  -9.991  1.00 43.37           C  
ANISOU 3177  CG  LEU A 208     5288   5084   6107  -1084   -948   1512       C  
ATOM   3178  CD1 LEU A 208      10.583  17.246 -10.017  1.00 48.05           C  
ANISOU 3178  CD1 LEU A 208     6010   5598   6650  -1381  -1183   1721       C  
ATOM   3179  CD2 LEU A 208       8.131  16.844  -9.785  1.00 43.31           C  
ANISOU 3179  CD2 LEU A 208     5473   4840   6145   -856  -1054   1369       C  
ATOM   3191  N   TYR A 209       9.426  12.675 -13.053  1.00 38.18           N  
ANISOU 3191  N   TYR A 209     4141   5124   5241   -969   -316   1544       N  
ATOM   3192  CA  TYR A 209       9.371  11.975 -14.332  1.00 38.75           C  
ANISOU 3192  CA  TYR A 209     4200   5333   5190   -957   -208   1583       C  
ATOM   3193  C   TYR A 209       8.077  11.182 -14.460  1.00 39.32           C  
ANISOU 3193  C   TYR A 209     4336   5329   5277   -832   -172   1430       C  
ATOM   3194  O   TYR A 209       7.428  11.200 -15.513  1.00 38.54           O  
ANISOU 3194  O   TYR A 209     4305   5210   5127   -862   -217   1457       O  
ATOM   3195  CB  TYR A 209      10.583  11.054 -14.487  1.00 38.23           C  
ANISOU 3195  CB  TYR A 209     4024   5519   4984   -918    -14   1653       C  
ATOM   3196  CG  TYR A 209      11.807  11.740 -15.055  1.00 40.52           C  
ANISOU 3196  CG  TYR A 209     4204   6009   5182  -1079    -35   1898       C  
ATOM   3197  CD1 TYR A 209      11.872  12.083 -16.401  1.00 38.00           C  
ANISOU 3197  CD1 TYR A 209     3908   5785   4748  -1165    -54   2032       C  
ATOM   3198  CD2 TYR A 209      12.898  12.040 -14.251  1.00 38.15           C  
ANISOU 3198  CD2 TYR A 209     3768   5832   4897  -1170    -49   2023       C  
ATOM   3199  CE1 TYR A 209      12.984  12.708 -16.926  1.00 38.64           C  
ANISOU 3199  CE1 TYR A 209     3857   6101   4725  -1338    -77   2297       C  
ATOM   3200  CE2 TYR A 209      14.019  12.665 -14.770  1.00 38.31           C  
ANISOU 3200  CE2 TYR A 209     3648   6092   4816  -1362    -88   2304       C  
ATOM   3201  CZ  TYR A 209      14.055  12.997 -16.108  1.00 40.50           C  
ANISOU 3201  CZ  TYR A 209     3929   6484   4974  -1446    -97   2445       C  
ATOM   3202  OH  TYR A 209      15.159  13.619 -16.641  1.00 42.16           O  
ANISOU 3202  OH  TYR A 209     3972   6982   5065  -1662   -139   2761       O  
ATOM   3212  N   ALA A 210       7.681  10.481 -13.395  1.00 38.29           N  
ANISOU 3212  N   ALA A 210     4179   5166   5202   -721   -109   1294       N  
ATOM   3213  CA  ALA A 210       6.409   9.768 -13.411  1.00 38.16           C  
ANISOU 3213  CA  ALA A 210     4197   5107   5194   -655   -111   1196       C  
ATOM   3214  C   ALA A 210       5.254  10.721 -13.678  1.00 38.08           C  
ANISOU 3214  C   ALA A 210     4198   4999   5269   -659   -269   1218       C  
ATOM   3215  O   ALA A 210       4.300  10.373 -14.384  1.00 39.52           O  
ANISOU 3215  O   ALA A 210     4404   5195   5419   -678   -311   1231       O  
ATOM   3216  CB  ALA A 210       6.200   9.034 -12.088  1.00 38.31           C  
ANISOU 3216  CB  ALA A 210     4165   5129   5263   -564    -40   1081       C  
ATOM   3222  N   ALA A 211       5.321  11.932 -13.121  1.00 36.68           N  
ANISOU 3222  N   ALA A 211     4032   4718   5186   -634   -376   1232       N  
ATOM   3223  CA  ALA A 211       4.269  12.916 -13.348  1.00 37.72           C  
ANISOU 3223  CA  ALA A 211     4206   4747   5381   -571   -531   1253       C  
ATOM   3224  C   ALA A 211       4.159  13.267 -14.827  1.00 38.19           C  
ANISOU 3224  C   ALA A 211     4325   4803   5384   -692   -616   1369       C  
ATOM   3225  O   ALA A 211       3.059  13.290 -15.392  1.00 38.34           O  
ANISOU 3225  O   ALA A 211     4330   4828   5409   -659   -684   1392       O  
ATOM   3226  CB  ALA A 211       4.539  14.167 -12.514  1.00 38.27           C  
ANISOU 3226  CB  ALA A 211     4375   4651   5516   -507   -654   1240       C  
ATOM   3232  N   VAL A 212       5.294  13.546 -15.473  1.00 41.63           N  
ANISOU 3232  N   VAL A 212     4806   5259   5752   -842   -616   1468       N  
ATOM   3233  CA  VAL A 212       5.280  13.875 -16.896  1.00 44.74           C  
ANISOU 3233  CA  VAL A 212     5260   5670   6068   -968   -687   1590       C  
ATOM   3234  C   VAL A 212       4.700  12.721 -17.703  1.00 43.58           C  
ANISOU 3234  C   VAL A 212     5112   5624   5824   -967   -599   1564       C  
ATOM   3235  O   VAL A 212       3.980  12.930 -18.687  1.00 43.62           O  
ANISOU 3235  O   VAL A 212     5169   5606   5797  -1021   -697   1626       O  
ATOM   3236  CB  VAL A 212       6.698  14.236 -17.376  1.00 42.89           C  
ANISOU 3236  CB  VAL A 212     5030   5522   5744  -1134   -671   1732       C  
ATOM   3237  CG1 VAL A 212       6.715  14.430 -18.887  1.00 44.64           C  
ANISOU 3237  CG1 VAL A 212     5305   5804   5850  -1260   -714   1864       C  
ATOM   3238  CG2 VAL A 212       7.194  15.482 -16.667  1.00 45.70           C  
ANISOU 3238  CG2 VAL A 212     5447   5738   6179  -1208   -837   1795       C  
ATOM   3248  N   ILE A 213       5.013  11.485 -17.307  1.00 49.81           N  
ANISOU 3248  N   ILE A 213     5875   6503   6548   -917   -438   1480       N  
ATOM   3249  CA  ILE A 213       4.494  10.317 -18.010  1.00 51.28           C  
ANISOU 3249  CA  ILE A 213     6145   6734   6606   -931   -392   1451       C  
ATOM   3250  C   ILE A 213       2.976  10.251 -17.909  1.00 53.11           C  
ANISOU 3250  C   ILE A 213     6345   6924   6912   -931   -515   1440       C  
ATOM   3251  O   ILE A 213       2.304   9.799 -18.844  1.00 54.27           O  
ANISOU 3251  O   ILE A 213     6580   7077   6964  -1021   -584   1486       O  
ATOM   3252  CB  ILE A 213       5.159   9.038 -17.459  1.00 50.24           C  
ANISOU 3252  CB  ILE A 213     6042   6665   6380   -854   -223   1359       C  
ATOM   3253  CG1 ILE A 213       6.627   8.970 -17.898  1.00 51.07           C  
ANISOU 3253  CG1 ILE A 213     6161   6891   6351   -829    -87   1419       C  
ATOM   3254  CG2 ILE A 213       4.395   7.803 -17.909  1.00 52.92           C  
ANISOU 3254  CG2 ILE A 213     6537   6980   6592   -878   -237   1312       C  
ATOM   3255  CD1 ILE A 213       7.420   7.837 -17.257  1.00 47.01           C  
ANISOU 3255  CD1 ILE A 213     5663   6452   5746   -694     84   1340       C  
ATOM   3267  N   ASN A 214       2.410  10.705 -16.789  1.00 51.50           N  
ANISOU 3267  N   ASN A 214     6011   6701   6854   -828   -548   1398       N  
ATOM   3268  CA  ASN A 214       0.975  10.628 -16.545  1.00 52.36           C  
ANISOU 3268  CA  ASN A 214     6018   6858   7020   -791   -639   1421       C  
ATOM   3269  C   ASN A 214       0.235  11.916 -16.890  1.00 54.15           C  
ANISOU 3269  C   ASN A 214     6201   7043   7330   -724   -790   1505       C  
ATOM   3270  O   ASN A 214      -0.948  12.044 -16.559  1.00 60.71           O  
ANISOU 3270  O   ASN A 214     6895   7961   8212   -628   -855   1547       O  
ATOM   3271  CB  ASN A 214       0.711  10.255 -15.085  1.00 52.35           C  
ANISOU 3271  CB  ASN A 214     5887   6915   7090   -669   -563   1338       C  
ATOM   3272  CG  ASN A 214       0.933   8.780 -14.815  1.00 53.51           C  
ANISOU 3272  CG  ASN A 214     6080   7112   7141   -751   -469   1284       C  
ATOM   3273  OD1 ASN A 214       0.065   7.952 -15.090  1.00 56.29           O  
ANISOU 3273  OD1 ASN A 214     6432   7531   7424   -860   -532   1338       O  
ATOM   3274  ND2 ASN A 214       2.099   8.443 -14.276  1.00 51.93           N  
ANISOU 3274  ND2 ASN A 214     5933   6874   6922   -712   -341   1197       N  
ATOM   3281  N   GLY A 215       0.896  12.872 -17.541  1.00 48.28           N  
ANISOU 3281  N   GLY A 215     4940   7791   5612   -141   -267    789       N  
ATOM   3282  CA  GLY A 215       0.226  14.037 -18.077  1.00 47.73           C  
ANISOU 3282  CA  GLY A 215     4887   7814   5435     48   -405    913       C  
ATOM   3283  C   GLY A 215       0.381  15.310 -17.272  1.00 51.50           C  
ANISOU 3283  C   GLY A 215     5588   7984   5997    177   -530   1078       C  
ATOM   3284  O   GLY A 215      -0.073  16.367 -17.730  1.00 49.36           O  
ANISOU 3284  O   GLY A 215     5382   7727   5645    355   -667   1210       O  
ATOM   3288  N   ASP A 216       0.994  15.248 -16.093  1.00 57.50           N  
ANISOU 3288  N   ASP A 216     6474   8464   6910    106   -495   1069       N  
ATOM   3289  CA  ASP A 216       1.252  16.441 -15.290  1.00 58.83           C  
ANISOU 3289  CA  ASP A 216     6861   8324   7169    207   -615   1198       C  
ATOM   3290  C   ASP A 216       2.584  17.040 -15.725  1.00 59.12           C  
ANISOU 3290  C   ASP A 216     7043   8192   7226     75   -663   1437       C  
ATOM   3291  O   ASP A 216       3.649  16.482 -15.436  1.00 61.61           O  
ANISOU 3291  O   ASP A 216     7363   8442   7605   -107   -579   1441       O  
ATOM   3292  CB  ASP A 216       1.262  16.105 -13.802  1.00 59.18           C  
ANISOU 3292  CB  ASP A 216     6948   8195   7342    191   -556   1061       C  
ATOM   3293  CG  ASP A 216      -0.060  16.409 -13.128  1.00 63.43           C  
ANISOU 3293  CG  ASP A 216     7440   8802   7859    396   -600    909       C  
ATOM   3294  OD1 ASP A 216      -0.748  17.355 -13.564  1.00 66.88           O  
ANISOU 3294  OD1 ASP A 216     7910   9277   8223    607   -734    958       O  
ATOM   3295  OD2 ASP A 216      -0.410  15.705 -12.159  1.00 65.86           O  
ANISOU 3295  OD2 ASP A 216     7678   9139   8206    355   -505    744       O  
ATOM   3323  N   ARG A 217       2.527  18.178 -16.424  1.00 59.12           N  
ANISOU 3323  N   ARG A 217     7166   8137   7160    164   -803   1642       N  
ATOM   3324  CA  ARG A 217       3.737  18.819 -16.924  1.00 59.39           C  
ANISOU 3324  CA  ARG A 217     7339   8039   7187     -2   -850   1894       C  
ATOM   3325  C   ARG A 217       3.743  20.327 -16.701  1.00 60.75           C  
ANISOU 3325  C   ARG A 217     7790   7883   7408     95  -1026   2090       C  
ATOM   3326  O   ARG A 217       4.613  21.013 -17.254  1.00 61.49           O  
ANISOU 3326  O   ARG A 217     8022   7869   7474    -57  -1084   2335       O  
ATOM   3327  CB  ARG A 217       3.923  18.526 -18.420  1.00 61.50           C  
ANISOU 3327  CB  ARG A 217     7468   8624   7276    -84   -824   2006       C  
ATOM   3328  CG  ARG A 217       2.734  17.843 -19.074  1.00 62.27           C  
ANISOU 3328  CG  ARG A 217     7345   9064   7249     60   -787   1838       C  
ATOM   3329  CD  ARG A 217       2.857  17.817 -20.588  1.00 63.80           C  
ANISOU 3329  CD  ARG A 217     7423   9577   7241     16   -796   1973       C  
ATOM   3330  NE  ARG A 217       1.942  18.764 -21.218  1.00 63.25           N  
ANISOU 3330  NE  ARG A 217     7417   9567   7048    241   -940   2112       N  
ATOM   3331  CZ  ARG A 217       0.627  18.585 -21.305  1.00 62.31           C  
ANISOU 3331  CZ  ARG A 217     7167   9651   6857    466   -963   1941       C  
ATOM   3332  NH1 ARG A 217       0.067  17.495 -20.796  1.00 59.84           N  
ANISOU 3332  NH1 ARG A 217     6661   9485   6591    450   -843   1634       N  
ATOM   3333  NH2 ARG A 217      -0.131  19.499 -21.896  1.00 63.89           N  
ANISOU 3333  NH2 ARG A 217     7433   9913   6929    704  -1111   2082       N  
ATOM   3346  N   TRP A 218       2.814  20.868 -15.910  1.00 60.88           N  
ANISOU 3346  N   TRP A 218     7899   7739   7491    337  -1116   1983       N  
ATOM   3347  CA  TRP A 218       2.779  22.311 -15.693  1.00 60.93           C  
ANISOU 3347  CA  TRP A 218     8201   7394   7556    463  -1302   2143       C  
ATOM   3348  C   TRP A 218       4.070  22.821 -15.066  1.00 59.23           C  
ANISOU 3348  C   TRP A 218     8182   6850   7474    227  -1317   2254       C  
ATOM   3349  O   TRP A 218       4.441  23.983 -15.267  1.00 58.41           O  
ANISOU 3349  O   TRP A 218     8342   6452   7399    198  -1457   2467       O  
ATOM   3350  CB  TRP A 218       1.586  22.680 -14.811  1.00 61.87           C  
ANISOU 3350  CB  TRP A 218     8350   7433   7723    786  -1387   1943       C  
ATOM   3351  CG  TRP A 218       1.651  22.108 -13.418  1.00 60.19           C  
ANISOU 3351  CG  TRP A 218     8067   7171   7633    752  -1294   1702       C  
ATOM   3352  CD1 TRP A 218       1.036  20.974 -12.968  1.00 60.38           C  
ANISOU 3352  CD1 TRP A 218     7843   7471   7630    768  -1155   1464       C  
ATOM   3353  CD2 TRP A 218       2.369  22.645 -12.298  1.00 57.70           C  
ANISOU 3353  CD2 TRP A 218     7933   6519   7470    682  -1334   1685       C  
ATOM   3354  NE1 TRP A 218       1.326  20.774 -11.641  1.00 58.88           N  
ANISOU 3354  NE1 TRP A 218     7673   7142   7555    723  -1106   1324       N  
ATOM   3355  CE2 TRP A 218       2.144  21.783 -11.206  1.00 59.25           C  
ANISOU 3355  CE2 TRP A 218     7970   6832   7712    681  -1215   1443       C  
ATOM   3356  CE3 TRP A 218       3.179  23.770 -12.114  1.00 58.17           C  
ANISOU 3356  CE3 TRP A 218     8278   6196   7628    601  -1460   1848       C  
ATOM   3357  CZ2 TRP A 218       2.698  22.013  -9.946  1.00 58.36           C  
ANISOU 3357  CZ2 TRP A 218     7954   6498   7722    632  -1221   1357       C  
ATOM   3358  CZ3 TRP A 218       3.731  23.994 -10.863  1.00 59.21           C  
ANISOU 3358  CZ3 TRP A 218     8502   6101   7895    537  -1465   1736       C  
ATOM   3359  CH2 TRP A 218       3.487  23.120  -9.796  1.00 58.44           C  
ANISOU 3359  CH2 TRP A 218     8221   6158   7824    568  -1347   1491       C  
ATOM   3371  N   PHE A 219       4.767  21.975 -14.308  1.00 54.18           N  
ANISOU 3371  N   PHE A 219     7423   6254   6909     52  -1181   2113       N  
ATOM   3372  CA  PHE A 219       5.972  22.400 -13.609  1.00 57.40           C  
ANISOU 3372  CA  PHE A 219     7975   6404   7428   -163  -1191   2175       C  
ATOM   3373  C   PHE A 219       7.194  22.487 -14.516  1.00 56.28           C  
ANISOU 3373  C   PHE A 219     7841   6331   7213   -467  -1161   2405       C  
ATOM   3374  O   PHE A 219       8.222  23.020 -14.087  1.00 55.47           O  
ANISOU 3374  O   PHE A 219     7868   6030   7179   -675  -1188   2488       O  
ATOM   3375  CB  PHE A 219       6.267  21.447 -12.442  1.00 54.08           C  
ANISOU 3375  CB  PHE A 219     7416   6041   7089   -208  -1063   1944       C  
ATOM   3376  CG  PHE A 219       6.411  20.006 -12.851  1.00 53.96           C  
ANISOU 3376  CG  PHE A 219     7142   6365   6997   -294   -892   1851       C  
ATOM   3377  CD1 PHE A 219       7.637  19.504 -13.255  1.00 55.51           C  
ANISOU 3377  CD1 PHE A 219     7257   6681   7154   -533   -808   1926       C  
ATOM   3378  CD2 PHE A 219       5.319  19.153 -12.824  1.00 55.06           C  
ANISOU 3378  CD2 PHE A 219     7116   6708   7097   -137   -821   1673       C  
ATOM   3379  CE1 PHE A 219       7.770  18.179 -13.631  1.00 56.38           C  
ANISOU 3379  CE1 PHE A 219     7150   7072   7199   -579   -667   1818       C  
ATOM   3380  CE2 PHE A 219       5.446  17.828 -13.199  1.00 55.09           C  
ANISOU 3380  CE2 PHE A 219     6914   6972   7044   -226   -673   1576       C  
ATOM   3381  CZ  PHE A 219       6.673  17.341 -13.603  1.00 55.51           C  
ANISOU 3381  CZ  PHE A 219     6914   7106   7073   -430   -602   1644       C  
ATOM   3391  N   LEU A 220       7.115  21.989 -15.746  1.00 57.81           N  
ANISOU 3391  N   LEU A 220     7882   6833   7252   -507  -1106   2498       N  
ATOM   3392  CA  LEU A 220       8.264  22.051 -16.637  1.00 59.49           C  
ANISOU 3392  CA  LEU A 220     8066   7178   7360   -796  -1072   2708       C  
ATOM   3393  C   LEU A 220       8.553  23.488 -17.048  1.00 67.01           C  
ANISOU 3393  C   LEU A 220     9307   7850   8303   -896  -1226   3007       C  
ATOM   3394  O   LEU A 220       7.642  24.300 -17.237  1.00 70.74           O  
ANISOU 3394  O   LEU A 220     9965   8133   8781   -681  -1363   3095       O  
ATOM   3395  CB  LEU A 220       8.030  21.213 -17.891  1.00 57.67           C  
ANISOU 3395  CB  LEU A 220     7595   7371   6946   -792   -988   2720       C  
ATOM   3396  CG  LEU A 220       7.930  19.698 -17.733  1.00 55.60           C  
ANISOU 3396  CG  LEU A 220     7055   7397   6675   -758   -828   2448       C  
ATOM   3397  CD1 LEU A 220       7.351  19.095 -19.004  1.00 56.03           C  
ANISOU 3397  CD1 LEU A 220     6911   7825   6553   -693   -786   2438       C  
ATOM   3398  CD2 LEU A 220       9.280  19.080 -17.418  1.00 54.90           C  
ANISOU 3398  CD2 LEU A 220     6867   7392   6602   -985   -725   2401       C  
ATOM   3410  N   ASN A 221       9.835  23.793 -17.202  1.00 68.24           N  
ANISOU 3410  N   ASN A 221     9505   7990   8435  -1228  -1206   3165       N  
ATOM   3411  CA  ASN A 221      10.273  25.076 -17.726  1.00 74.45           C  
ANISOU 3411  CA  ASN A 221    10563   8535   9190  -1415  -1333   3486       C  
ATOM   3412  C   ASN A 221      11.485  24.825 -18.609  1.00 78.79           C  
ANISOU 3412  C   ASN A 221    10960   9408   9569  -1779  -1240   3661       C  
ATOM   3413  O   ASN A 221      12.146  23.789 -18.502  1.00 72.66           O  
ANISOU 3413  O   ASN A 221     9905   8955   8748  -1879  -1097   3494       O  
ATOM   3414  CB  ASN A 221      10.597  26.072 -16.601  1.00 79.37           C  
ANISOU 3414  CB  ASN A 221    11478   8672  10008  -1484  -1442   3474       C  
ATOM   3415  CG  ASN A 221      11.743  25.614 -15.711  1.00 79.97           C  
ANISOU 3415  CG  ASN A 221    11425   8807  10151  -1726  -1339   3316       C  
ATOM   3416  OD1 ASN A 221      12.600  24.833 -16.122  1.00 78.02           O  
ANISOU 3416  OD1 ASN A 221    10930   8929   9787  -1929  -1208   3311       O  
ATOM   3417  ND2 ASN A 221      11.761  26.110 -14.479  1.00 81.17           N  
ANISOU 3417  ND2 ASN A 221    11741   8619  10483  -1682  -1406   3170       N  
ATOM   3424  N   ARG A 222      11.774  25.773 -19.494  1.00111.03           N  
ANISOU 3424  N   ARG A 222    15226  13417  13542  -1970  -1326   4001       N  
ATOM   3425  CA  ARG A 222      12.908  25.602 -20.391  1.00119.38           C  
ANISOU 3425  CA  ARG A 222    16101  14843  14413  -2301  -1223   4117       C  
ATOM   3426  C   ARG A 222      14.225  26.077 -19.789  1.00116.62           C  
ANISOU 3426  C   ARG A 222    15792  14382  14134  -2629  -1193   4070       C  
ATOM   3427  O   ARG A 222      15.261  25.982 -20.455  1.00121.60           O  
ANISOU 3427  O   ARG A 222    16251  15341  14608  -2907  -1113   4128       O  
ATOM   3428  CB  ARG A 222      12.666  26.323 -21.715  1.00127.39           C  
ANISOU 3428  CB  ARG A 222    17210  15929  15265  -2310  -1274   4364       C  
ATOM   3429  CG  ARG A 222      13.459  25.706 -22.851  1.00131.23           C  
ANISOU 3429  CG  ARG A 222    17386  16972  15504  -2531  -1153   4426       C  
ATOM   3430  CD  ARG A 222      12.780  24.471 -23.404  1.00131.18           C  
ANISOU 3430  CD  ARG A 222    17086  17403  15351  -2327  -1082   4344       C  
ATOM   3431  NE  ARG A 222      13.677  23.319 -23.412  1.00131.64           N  
ANISOU 3431  NE  ARG A 222    16798  17905  15314  -2485   -931   4177       N  
ATOM   3432  CZ  ARG A 222      13.562  22.285 -24.239  1.00132.76           C  
ANISOU 3432  CZ  ARG A 222    16626  18548  15267  -2410   -836   4081       C  
ATOM   3433  NH1 ARG A 222      12.595  22.256 -25.148  1.00134.44           N  
ANISOU 3433  NH1 ARG A 222    16809  18918  15353  -2210   -874   4155       N  
ATOM   3434  NH2 ARG A 222      14.424  21.282 -24.164  1.00131.68           N  
ANISOU 3434  NH2 ARG A 222    16196  18761  15076  -2505   -706   3861       N  
ATOM   3448  N   PHE A 223      14.219  26.584 -18.560  1.00 99.67           N  
ANISOU 3448  N   PHE A 223    13848  11821  12201  -2601  -1260   3953       N  
ATOM   3449  CA  PHE A 223      15.471  26.856 -17.876  1.00 91.00           C  
ANISOU 3449  CA  PHE A 223    12733  10690  11155  -2904  -1223   3866       C  
ATOM   3450  C   PHE A 223      16.286  25.570 -17.777  1.00 82.45           C  
ANISOU 3450  C   PHE A 223    11275  10086   9965  -3019  -1074   3723       C  
ATOM   3451  O   PHE A 223      15.759  24.460 -17.882  1.00 81.27           O  
ANISOU 3451  O   PHE A 223    10930  10177   9773  -2831  -1005   3648       O  
ATOM   3452  CB  PHE A 223      15.217  27.416 -16.476  1.00 87.16           C  
ANISOU 3452  CB  PHE A 223    12481   9729  10909  -2808  -1315   3715       C  
ATOM   3453  CG  PHE A 223      14.583  28.782 -16.467  1.00 90.27           C  
ANISOU 3453  CG  PHE A 223    13256   9629  11413  -2701  -1466   3817       C  
ATOM   3454  CD1 PHE A 223      13.266  28.958 -16.864  1.00 90.54           C  
ANISOU 3454  CD1 PHE A 223    13432   9509  11460  -2355  -1555   3891       C  
ATOM   3455  CD2 PHE A 223      15.303  29.889 -16.044  1.00 93.80           C  
ANISOU 3455  CD2 PHE A 223    13916   9778  11945  -2934  -1523   3828       C  
ATOM   3456  CE1 PHE A 223      12.684  30.213 -16.851  1.00 94.45           C  
ANISOU 3456  CE1 PHE A 223    14280   9558  12050  -2216  -1697   3972       C  
ATOM   3457  CE2 PHE A 223      14.726  31.145 -16.028  1.00 97.13           C  
ANISOU 3457  CE2 PHE A 223    14702   9728  12475  -2822  -1660   3913       C  
ATOM   3458  CZ  PHE A 223      13.414  31.308 -16.432  1.00 97.59           C  
ANISOU 3458  CZ  PHE A 223    14904   9631  12545  -2447  -1747   3984       C  
ATOM   3468  N   THR A 224      17.588  25.727 -17.587  1.00 72.98           N  
ANISOU 3468  N   THR A 224     9974   9042   8713  -3323  -1025   3680       N  
ATOM   3469  CA  THR A 224      18.449  24.603 -17.256  1.00 71.71           C  
ANISOU 3469  CA  THR A 224     9481   9296   8470  -3402   -899   3506       C  
ATOM   3470  C   THR A 224      19.346  25.028 -16.103  1.00 70.87           C  
ANISOU 3470  C   THR A 224     9422   9040   8467  -3588   -915   3376       C  
ATOM   3471  O   THR A 224      19.258  26.152 -15.599  1.00 70.99           O  
ANISOU 3471  O   THR A 224     9723   8631   8617  -3657  -1019   3412       O  
ATOM   3472  CB  THR A 224      19.269  24.132 -18.465  1.00 73.91           C  
ANISOU 3472  CB  THR A 224     9470  10127   8486  -3572   -808   3565       C  
ATOM   3473  OG1 THR A 224      19.788  22.817 -18.210  1.00 71.30           O  
ANISOU 3473  OG1 THR A 224     8808  10208   8075  -3519   -686   3369       O  
ATOM   3474  CG2 THR A 224      20.423  25.087 -18.747  1.00 75.84           C  
ANISOU 3474  CG2 THR A 224     9753  10426   8638  -3925   -835   3656       C  
ATOM   3482  N   THR A 225      20.216  24.123 -15.679  1.00 70.94           N  
ANISOU 3482  N   THR A 225     9143   9411   8401  -3655   -814   3210       N  
ATOM   3483  CA  THR A 225      21.076  24.393 -14.538  1.00 71.63           C  
ANISOU 3483  CA  THR A 225     9227   9428   8561  -3814   -823   3064       C  
ATOM   3484  C   THR A 225      22.270  23.457 -14.610  1.00 70.20           C  
ANISOU 3484  C   THR A 225     8667   9816   8191  -3924   -706   2932       C  
ATOM   3485  O   THR A 225      22.337  22.563 -15.457  1.00 67.24           O  
ANISOU 3485  O   THR A 225     8052   9841   7655  -3841   -621   2931       O  
ATOM   3486  CB  THR A 225      20.320  24.220 -13.214  1.00 67.50           C  
ANISOU 3486  CB  THR A 225     8839   8544   8266  -3584   -867   2915       C  
ATOM   3487  OG1 THR A 225      21.153  24.629 -12.123  1.00 67.04           O  
ANISOU 3487  OG1 THR A 225     8791   8410   8271  -3767   -892   2783       O  
ATOM   3488  CG2 THR A 225      19.916  22.766 -13.016  1.00 61.37           C  
ANISOU 3488  CG2 THR A 225     7824   8018   7475  -3207   -764   2689       C  
ATOM   3496  N   THR A 226      23.217  23.683 -13.711  1.00 66.00           N  
ANISOU 3496  N   THR A 226     8076   9332   7668  -4094   -707   2800       N  
ATOM   3497  CA  THR A 226      24.368  22.811 -13.555  1.00 64.62           C  
ANISOU 3497  CA  THR A 226     7540   9695   7320  -4151   -610   2633       C  
ATOM   3498  C   THR A 226      24.191  21.966 -12.300  1.00 58.33           C  
ANISOU 3498  C   THR A 226     6660   8858   6647  -3886   -583   2400       C  
ATOM   3499  O   THR A 226      23.445  22.321 -11.384  1.00 56.18           O  
ANISOU 3499  O   THR A 226     6623   8138   6584  -3725   -651   2337       O  
ATOM   3500  CB  THR A 226      25.664  23.622 -13.471  1.00 66.81           C  
ANISOU 3500  CB  THR A 226     7773  10140   7474  -4492   -630   2614       C  
ATOM   3501  OG1 THR A 226      25.721  24.312 -12.217  1.00 68.35           O  
ANISOU 3501  OG1 THR A 226     8145   9981   7845  -4577   -698   2524       O  
ATOM   3502  CG2 THR A 226      25.732  24.639 -14.603  1.00 67.89           C  
ANISOU 3502  CG2 THR A 226     8071  10202   7522  -4719   -679   2841       C  
ATOM   3510  N   LEU A 227      24.882  20.826 -12.275  1.00 61.64           N  
ANISOU 3510  N   LEU A 227     6757   9744   6919  -3736   -493   2218       N  
ATOM   3511  CA  LEU A 227      24.816  19.952 -11.109  1.00 63.80           C  
ANISOU 3511  CA  LEU A 227     6967   9992   7280  -3389   -471   1962       C  
ATOM   3512  C   LEU A 227      25.304  20.672  -9.856  1.00 66.65           C  
ANISOU 3512  C   LEU A 227     7407  10191   7726  -3532   -533   1869       C  
ATOM   3513  O   LEU A 227      24.734  20.502  -8.771  1.00 62.09           O  
ANISOU 3513  O   LEU A 227     6953   9331   7308  -3278   -561   1737       O  
ATOM   3514  CB  LEU A 227      25.637  18.688 -11.363  1.00 67.65           C  
ANISOU 3514  CB  LEU A 227     7109  11021   7573  -3221   -381   1796       C  
ATOM   3515  CG  LEU A 227      25.487  17.546 -10.356  1.00 69.99           C  
ANISOU 3515  CG  LEU A 227     7354  11301   7938  -2803   -352   1563       C  
ATOM   3516  CD1 LEU A 227      24.031  17.133 -10.205  1.00 68.49           C  
ANISOU 3516  CD1 LEU A 227     7390  10689   7944  -2498   -354   1568       C  
ATOM   3517  CD2 LEU A 227      26.338  16.359 -10.782  1.00 71.08           C  
ANISOU 3517  CD2 LEU A 227     7174  11961   7870  -2633   -281   1413       C  
ATOM   3529  N   ASN A 228      26.358  21.483  -9.986  1.00 70.16           N  
ANISOU 3529  N   ASN A 228     7770  10833   8053  -3955   -552   1929       N  
ATOM   3530  CA  ASN A 228      26.853  22.256  -8.850  1.00 71.35           C  
ANISOU 3530  CA  ASN A 228     7993  10838   8278  -4141   -616   1827       C  
ATOM   3531  C   ASN A 228      25.841  23.309  -8.415  1.00 69.13           C  
ANISOU 3531  C   ASN A 228     8111   9910   8246  -4167   -724   1913       C  
ATOM   3532  O   ASN A 228      25.539  23.439  -7.223  1.00 68.28           O  
ANISOU 3532  O   ASN A 228     8111   9551   8282  -4004   -774   1750       O  
ATOM   3533  CB  ASN A 228      28.183  22.921  -9.206  1.00 76.54           C  
ANISOU 3533  CB  ASN A 228     8494  11848   8739  -4588   -609   1858       C  
ATOM   3534  CG  ASN A 228      29.377  22.045  -8.890  1.00 76.16           C  
ANISOU 3534  CG  ASN A 228     8042  12427   8469  -4528   -538   1646       C  
ATOM   3535  OD1 ASN A 228      29.912  22.080  -7.781  1.00 73.36           O  
ANISOU 3535  OD1 ASN A 228     7589  12164   8120  -4547   -562   1462       O  
ATOM   3536  ND2 ASN A 228      29.806  21.255  -9.866  1.00 78.81           N  
ANISOU 3536  ND2 ASN A 228     8138  13215   8592  -4426   -460   1651       N  
ATOM   3543  N   ASP A 229      25.319  24.085  -9.367  1.00 68.30           N  
ANISOU 3543  N   ASP A 229     8227   9544   8181  -4357   -768   2165       N  
ATOM   3544  CA  ASP A 229      24.366  25.135  -9.021  1.00 70.04           C  
ANISOU 3544  CA  ASP A 229     8843   9142   8628  -4353   -889   2246       C  
ATOM   3545  C   ASP A 229      23.114  24.550  -8.383  1.00 64.07           C  
ANISOU 3545  C   ASP A 229     8191   8115   8036  -3851   -901   2114       C  
ATOM   3546  O   ASP A 229      22.567  25.123  -7.434  1.00 62.83           O  
ANISOU 3546  O   ASP A 229     8249   7567   8055  -3745   -989   2012       O  
ATOM   3547  CB  ASP A 229      24.008  25.950 -10.264  1.00 75.17           C  
ANISOU 3547  CB  ASP A 229     9705   9604   9250  -4450   -925   2490       C  
ATOM   3548  CG  ASP A 229      25.124  26.888 -10.685  1.00 83.75           C  
ANISOU 3548  CG  ASP A 229    10799  10813  10207  -4822   -934   2548       C  
ATOM   3549  OD1 ASP A 229      26.184  26.396 -11.127  1.00 85.61           O  
ANISOU 3549  OD1 ASP A 229    10731  11580  10216  -4970   -846   2515       O  
ATOM   3550  OD2 ASP A 229      24.941  28.119 -10.572  1.00 87.99           O  
ANISOU 3550  OD2 ASP A 229    11647  10919  10864  -4960  -1031   2618       O  
ATOM   3555  N   PHE A 230      22.645  23.409  -8.886  1.00 58.43           N  
ANISOU 3555  N   PHE A 230     7322   7621   7259  -3549   -813   2100       N  
ATOM   3556  CA  PHE A 230      21.480  22.772  -8.285  1.00 57.16           C  
ANISOU 3556  CA  PHE A 230     7235   7253   7232  -3113   -808   1973       C  
ATOM   3557  C   PHE A 230      21.770  22.357  -6.847  1.00 53.15           C  
ANISOU 3557  C   PHE A 230     6642   6784   6767  -2950   -798   1724       C  
ATOM   3558  O   PHE A 230      20.969  22.612  -5.941  1.00 52.99           O  
ANISOU 3558  O   PHE A 230     6787   6448   6897  -2753   -855   1624       O  
ATOM   3559  CB  PHE A 230      21.046  21.565  -9.117  1.00 55.34           C  
ANISOU 3559  CB  PHE A 230     6838   7277   6911  -2873   -709   1989       C  
ATOM   3560  CG  PHE A 230      19.944  20.768  -8.483  1.00 55.94           C  
ANISOU 3560  CG  PHE A 230     6954   7201   7100  -2470   -684   1848       C  
ATOM   3561  CD1 PHE A 230      18.617  21.119  -8.674  1.00 57.11           C  
ANISOU 3561  CD1 PHE A 230     7307   7025   7366  -2306   -738   1911       C  
ATOM   3562  CD2 PHE A 230      20.235  19.677  -7.682  1.00 55.03           C  
ANISOU 3562  CD2 PHE A 230     6672   7281   6957  -2260   -611   1659       C  
ATOM   3563  CE1 PHE A 230      17.602  20.392  -8.084  1.00 57.91           C  
ANISOU 3563  CE1 PHE A 230     7422   7032   7550  -1975   -707   1777       C  
ATOM   3564  CE2 PHE A 230      19.226  18.947  -7.089  1.00 56.28           C  
ANISOU 3564  CE2 PHE A 230     6877   7301   7207  -1936   -581   1552       C  
ATOM   3565  CZ  PHE A 230      17.908  19.303  -7.290  1.00 58.14           C  
ANISOU 3565  CZ  PHE A 230     7293   7244   7552  -1812   -624   1606       C  
ATOM   3575  N   ASN A 231      22.924  21.721  -6.617  1.00 57.87           N  
ANISOU 3575  N   ASN A 231     6969   7804   7217  -3016   -729   1618       N  
ATOM   3576  CA  ASN A 231      23.256  21.255  -5.274  1.00 59.86           C  
ANISOU 3576  CA  ASN A 231     7122   8144   7476  -2839   -719   1396       C  
ATOM   3577  C   ASN A 231      23.364  22.406  -4.282  1.00 59.80           C  
ANISOU 3577  C   ASN A 231     7278   7863   7579  -3003   -823   1314       C  
ATOM   3578  O   ASN A 231      23.076  22.225  -3.094  1.00 56.83           O  
ANISOU 3578  O   ASN A 231     6923   7400   7270  -2785   -842   1144       O  
ATOM   3579  CB  ASN A 231      24.560  20.455  -5.299  1.00 56.44           C  
ANISOU 3579  CB  ASN A 231     6363   8245   6836  -2879   -644   1303       C  
ATOM   3580  CG  ASN A 231      24.354  19.022  -5.752  1.00 54.97           C  
ANISOU 3580  CG  ASN A 231     6025   8289   6572  -2557   -549   1275       C  
ATOM   3581  OD1 ASN A 231      23.282  18.451  -5.566  1.00 52.93           O  
ANISOU 3581  OD1 ASN A 231     5885   7801   6423  -2264   -530   1263       O  
ATOM   3582  ND2 ASN A 231      25.384  18.434  -6.347  1.00 55.23           N  
ANISOU 3582  ND2 ASN A 231     5791   8786   6407  -2617   -491   1251       N  
ATOM   3589  N   LEU A 232      23.779  23.591  -4.739  1.00 71.40           N  
ANISOU 3589  N   LEU A 232     8870   9195   9063  -3395   -894   1430       N  
ATOM   3590  CA  LEU A 232      23.812  24.745  -3.845  1.00 75.22           C  
ANISOU 3590  CA  LEU A 232     9551   9353   9675  -3560  -1008   1338       C  
ATOM   3591  C   LEU A 232      22.419  25.071  -3.324  1.00 73.05           C  
ANISOU 3591  C   LEU A 232     9551   8604   9600  -3258  -1085   1297       C  
ATOM   3592  O   LEU A 232      22.247  25.385  -2.141  1.00 74.88           O  
ANISOU 3592  O   LEU A 232     9848   8684   9919  -3150  -1145   1102       O  
ATOM   3593  CB  LEU A 232      24.402  25.960  -4.559  1.00 77.91           C  
ANISOU 3593  CB  LEU A 232    10032   9562  10010  -4055  -1074   1505       C  
ATOM   3594  CG  LEU A 232      25.909  26.204  -4.453  1.00 82.77           C  
ANISOU 3594  CG  LEU A 232    10422  10563  10462  -4472  -1050   1444       C  
ATOM   3595  CD1 LEU A 232      26.260  27.541  -5.093  1.00 85.05           C  
ANISOU 3595  CD1 LEU A 232    10935  10600  10780  -4957  -1124   1624       C  
ATOM   3596  CD2 LEU A 232      26.393  26.167  -3.010  1.00 84.04           C  
ANISOU 3596  CD2 LEU A 232    10468  10831  10630  -4403  -1074   1151       C  
ATOM   3608  N   VAL A 233      21.412  25.011  -4.196  1.00 64.29           N  
ANISOU 3608  N   VAL A 233     8584   7297   8547  -3112  -1087   1463       N  
ATOM   3609  CA  VAL A 233      20.045  25.288  -3.771  1.00 61.42           C  
ANISOU 3609  CA  VAL A 233     8447   6544   8345  -2802  -1160   1414       C  
ATOM   3610  C   VAL A 233      19.471  24.107  -3.000  1.00 59.53           C  
ANISOU 3610  C   VAL A 233     8050   6477   8091  -2411  -1077   1251       C  
ATOM   3611  O   VAL A 233      18.770  24.288  -1.999  1.00 59.35           O  
ANISOU 3611  O   VAL A 233     8120   6268   8163  -2191  -1128   1094       O  
ATOM   3612  CB  VAL A 233      19.173  25.643  -4.988  1.00 58.75           C  
ANISOU 3612  CB  VAL A 233     8296   5978   8047  -2776  -1197   1645       C  
ATOM   3613  CG1 VAL A 233      17.735  25.905  -4.554  1.00 59.07           C  
ANISOU 3613  CG1 VAL A 233     8538   5676   8232  -2424  -1276   1571       C  
ATOM   3614  CG2 VAL A 233      19.746  26.845  -5.713  1.00 60.12           C  
ANISOU 3614  CG2 VAL A 233     8662   5951   8228  -3182  -1285   1841       C  
ATOM   3624  N   ALA A 234      19.751  22.883  -3.453  1.00 56.89           N  
ANISOU 3624  N   ALA A 234     7485   6500   7630  -2320   -951   1283       N  
ATOM   3625  CA  ALA A 234      19.255  21.707  -2.748  1.00 57.56           C  
ANISOU 3625  CA  ALA A 234     7449   6726   7697  -1980   -869   1155       C  
ATOM   3626  C   ALA A 234      19.761  21.673  -1.311  1.00 60.25           C  
ANISOU 3626  C   ALA A 234     7716   7154   8024  -1923   -883    954       C  
ATOM   3627  O   ALA A 234      19.006  21.350  -0.387  1.00 60.01           O  
ANISOU 3627  O   ALA A 234     7714   7048   8038  -1662   -880    837       O  
ATOM   3628  CB  ALA A 234      19.666  20.437  -3.493  1.00 55.11           C  
ANISOU 3628  CB  ALA A 234     6923   6765   7253  -1921   -746   1211       C  
ATOM   3634  N   MET A 235      21.037  22.010  -1.102  1.00 64.86           N  
ANISOU 3634  N   MET A 235     8186   7932   8525  -2174   -898    908       N  
ATOM   3635  CA  MET A 235      21.596  21.984   0.247  1.00 71.96           C  
ANISOU 3635  CA  MET A 235     8988   8969   9385  -2124   -916    706       C  
ATOM   3636  C   MET A 235      20.814  22.894   1.187  1.00 67.09           C  
ANISOU 3636  C   MET A 235     8572   8008   8910  -2047  -1021    578       C  
ATOM   3637  O   MET A 235      20.547  22.528   2.337  1.00 64.72           O  
ANISOU 3637  O   MET A 235     8221   7774   8595  -1818  -1014    421       O  
ATOM   3638  CB  MET A 235      23.069  22.398   0.218  1.00 84.04           C  
ANISOU 3638  CB  MET A 235    10364  10767  10800  -2458   -930    668       C  
ATOM   3639  CG  MET A 235      24.031  21.316   0.681  1.00 91.55           C  
ANISOU 3639  CG  MET A 235    11021  12198  11565  -2338   -848    571       C  
ATOM   3640  SD  MET A 235      24.479  20.177  -0.642  1.00 94.28           S  
ANISOU 3640  SD  MET A 235    11176  12880  11766  -2300   -736    718       S  
ATOM   3641  CE  MET A 235      26.117  20.770  -1.066  1.00 95.01           C  
ANISOU 3641  CE  MET A 235    11047  13365  11686  -2732   -749    699       C  
ATOM   3651  N   LYS A 236      20.432  24.082   0.711  1.00 60.53           N  
ANISOU 3651  N   LYS A 236     7978   6813   8208  -2221  -1126    642       N  
ATOM   3652  CA  LYS A 236      19.761  25.053   1.570  1.00 61.56           C  
ANISOU 3652  CA  LYS A 236     8313   6602   8475  -2143  -1249    490       C  
ATOM   3653  C   LYS A 236      18.387  24.570   2.017  1.00 58.79           C  
ANISOU 3653  C   LYS A 236     8009   6154   8174  -1746  -1233    432       C  
ATOM   3654  O   LYS A 236      17.929  24.938   3.104  1.00 57.51           O  
ANISOU 3654  O   LYS A 236     7899   5894   8059  -1586  -1298    236       O  
ATOM   3655  CB  LYS A 236      19.644  26.391   0.837  1.00 68.92           C  
ANISOU 3655  CB  LYS A 236     9525   7127   9536  -2397  -1374    597       C  
ATOM   3656  CG  LYS A 236      18.601  27.342   1.407  1.00 75.12           C  
ANISOU 3656  CG  LYS A 236    10578   7479  10484  -2219  -1515    472       C  
ATOM   3657  CD  LYS A 236      18.624  28.676   0.675  1.00 81.01           C  
ANISOU 3657  CD  LYS A 236    11639   7788  11355  -2482  -1652    596       C  
ATOM   3658  CE  LYS A 236      17.340  29.463   0.893  1.00 84.90           C  
ANISOU 3658  CE  LYS A 236    12418   7839  12003  -2203  -1793    522       C  
ATOM   3659  NZ  LYS A 236      16.915  30.170  -0.349  1.00 86.74           N  
ANISOU 3659  NZ  LYS A 236    12925   7722  12310  -2293  -1873    780       N  
ATOM   3674  N   TYR A 237      17.712  23.762   1.200  1.00 57.82           N  
ANISOU 3674  N   TYR A 237     7856   6083   8029  -1595  -1149    583       N  
ATOM   3675  CA  TYR A 237      16.390  23.246   1.531  1.00 55.04           C  
ANISOU 3675  CA  TYR A 237     7525   5684   7705  -1259  -1120    537       C  
ATOM   3676  C   TYR A 237      16.440  21.828   2.094  1.00 53.18           C  
ANISOU 3676  C   TYR A 237     7076   5778   7350  -1077   -984    500       C  
ATOM   3677  O   TYR A 237      15.435  21.112   2.046  1.00 50.60           O  
ANISOU 3677  O   TYR A 237     6735   5472   7018   -861   -920    521       O  
ATOM   3678  CB  TYR A 237      15.485  23.301   0.299  1.00 50.97           C  
ANISOU 3678  CB  TYR A 237     7122   5005   7240  -1210  -1124    709       C  
ATOM   3679  CG  TYR A 237      15.156  24.712  -0.137  1.00 53.01           C  
ANISOU 3679  CG  TYR A 237     7643   4880   7620  -1302  -1278    752       C  
ATOM   3680  CD1 TYR A 237      14.059  25.383   0.389  1.00 54.89           C  
ANISOU 3680  CD1 TYR A 237     8040   4866   7951  -1069  -1385    625       C  
ATOM   3681  CD2 TYR A 237      15.947  25.376  -1.065  1.00 53.75           C  
ANISOU 3681  CD2 TYR A 237     7831   4867   7723  -1618  -1322    920       C  
ATOM   3682  CE1 TYR A 237      13.757  26.673  -0.001  1.00 57.39           C  
ANISOU 3682  CE1 TYR A 237     8630   4792   8382  -1115  -1544    662       C  
ATOM   3683  CE2 TYR A 237      15.652  26.666  -1.461  1.00 56.17           C  
ANISOU 3683  CE2 TYR A 237     8422   4777   8143  -1708  -1472    987       C  
ATOM   3684  CZ  TYR A 237      14.556  27.309  -0.926  1.00 57.44           C  
ANISOU 3684  CZ  TYR A 237     8765   4649   8411  -1439  -1588    855       C  
ATOM   3685  OH  TYR A 237      14.256  28.594  -1.316  1.00 60.71           O  
ANISOU 3685  OH  TYR A 237     9495   4631   8943  -1490  -1754    920       O  
ATOM   3695  N   ASN A 238      17.585  21.418   2.636  1.00 56.94           N  
ANISOU 3695  N   ASN A 238     7395   6514   7726  -1160   -943    445       N  
ATOM   3696  CA  ASN A 238      17.753  20.090   3.225  1.00 57.72           C  
ANISOU 3696  CA  ASN A 238     7322   6904   7703   -975   -829    424       C  
ATOM   3697  C   ASN A 238      17.374  18.993   2.231  1.00 55.47           C  
ANISOU 3697  C   ASN A 238     6998   6685   7392   -895   -721    579       C  
ATOM   3698  O   ASN A 238      16.622  18.064   2.539  1.00 53.50           O  
ANISOU 3698  O   ASN A 238     6730   6479   7120   -688   -644    583       O  
ATOM   3699  CB  ASN A 238      16.952  19.966   4.522  1.00 59.44           C  
ANISOU 3699  CB  ASN A 238     7550   7121   7914   -739   -834    282       C  
ATOM   3700  CG  ASN A 238      17.556  20.777   5.656  1.00 63.61           C  
ANISOU 3700  CG  ASN A 238     8056   7690   8422   -793   -924     92       C  
ATOM   3701  OD1 ASN A 238      18.766  21.005   5.693  1.00 63.22           O  
ANISOU 3701  OD1 ASN A 238     7920   7783   8317   -978   -945     62       O  
ATOM   3702  ND2 ASN A 238      16.717  21.217   6.585  1.00 65.28           N  
ANISOU 3702  ND2 ASN A 238     8326   7812   8664   -634   -978    -58       N  
ATOM   3709  N   TYR A 239      17.911  19.113   1.021  1.00 50.47           N  
ANISOU 3709  N   TYR A 239     6351   6071   6754  -1081   -716    701       N  
ATOM   3710  CA  TYR A 239      17.812  18.084  -0.002  1.00 48.06           C  
ANISOU 3710  CA  TYR A 239     5977   5880   6404  -1034   -620    820       C  
ATOM   3711  C   TYR A 239      19.171  17.419  -0.166  1.00 47.40           C  
ANISOU 3711  C   TYR A 239     5711   6112   6186  -1100   -569    823       C  
ATOM   3712  O   TYR A 239      20.201  18.099  -0.212  1.00 49.28           O  
ANISOU 3712  O   TYR A 239     5887   6460   6379  -1315   -618    805       O  
ATOM   3713  CB  TYR A 239      17.354  18.673  -1.340  1.00 44.31           C  
ANISOU 3713  CB  TYR A 239     5599   5245   5991  -1167   -652    954       C  
ATOM   3714  CG  TYR A 239      15.859  18.667  -1.544  1.00 43.45           C  
ANISOU 3714  CG  TYR A 239     5608   4936   5966  -1000   -655    972       C  
ATOM   3715  CD1 TYR A 239      15.020  19.385  -0.705  1.00 46.48           C  
ANISOU 3715  CD1 TYR A 239     6111   5118   6431   -891   -731    875       C  
ATOM   3716  CD2 TYR A 239      15.287  17.950  -2.586  1.00 44.85           C  
ANISOU 3716  CD2 TYR A 239     5755   5159   6126   -947   -587   1062       C  
ATOM   3717  CE1 TYR A 239      13.651  19.381  -0.892  1.00 46.50           C  
ANISOU 3717  CE1 TYR A 239     6188   4997   6484   -726   -736    872       C  
ATOM   3718  CE2 TYR A 239      13.922  17.941  -2.781  1.00 45.43           C  
ANISOU 3718  CE2 TYR A 239     5905   5100   6255   -804   -589   1061       C  
ATOM   3719  CZ  TYR A 239      13.109  18.658  -1.931  1.00 46.21           C  
ANISOU 3719  CZ  TYR A 239     6109   5027   6424   -691   -663    969       C  
ATOM   3720  OH  TYR A 239      11.749  18.651  -2.124  1.00 49.16           O  
ANISOU 3720  OH  TYR A 239     6526   5325   6827   -536   -668    949       O  
ATOM   3731  N   GLU A 240      19.173  16.094  -0.243  1.00 45.06           N  
ANISOU 3731  N   GLU A 240     5330   5967   5822   -916   -476    834       N  
ATOM   3732  CA  GLU A 240      20.424  15.376  -0.429  1.00 46.36           C  
ANISOU 3732  CA  GLU A 240     5319   6449   5848   -914   -436    819       C  
ATOM   3733  C   GLU A 240      21.091  15.837  -1.723  1.00 43.84           C  
ANISOU 3733  C   GLU A 240     4922   6249   5486  -1158   -448    895       C  
ATOM   3734  O   GLU A 240      20.407  16.042  -2.734  1.00 44.19           O  
ANISOU 3734  O   GLU A 240     5046   6153   5593  -1226   -443    995       O  
ATOM   3735  CB  GLU A 240      20.178  13.867  -0.469  1.00 49.80           C  
ANISOU 3735  CB  GLU A 240     5730   6952   6241   -659   -345    827       C  
ATOM   3736  CG  GLU A 240      19.858  13.251   0.887  1.00 52.24           C  
ANISOU 3736  CG  GLU A 240     6083   7231   6533   -435   -323    774       C  
ATOM   3737  CD  GLU A 240      21.054  13.245   1.823  1.00 55.13           C  
ANISOU 3737  CD  GLU A 240     6321   7856   6770   -388   -356    690       C  
ATOM   3738  OE1 GLU A 240      22.199  13.227   1.324  1.00 58.37           O  
ANISOU 3738  OE1 GLU A 240     6579   8523   7077   -463   -368    666       O  
ATOM   3739  OE2 GLU A 240      20.851  13.262   3.056  1.00 52.27           O  
ANISOU 3739  OE2 GLU A 240     5991   7482   6388   -273   -370    640       O  
ATOM   3746  N   PRO A 241      22.412  16.014  -1.736  1.00 44.97           N  
ANISOU 3746  N   PRO A 241     4896   6688   5501  -1298   -464    853       N  
ATOM   3747  CA  PRO A 241      23.074  16.422  -2.979  1.00 46.90           C  
ANISOU 3747  CA  PRO A 241     5043   7103   5673  -1558   -466    936       C  
ATOM   3748  C   PRO A 241      22.931  15.344  -4.040  1.00 47.01           C  
ANISOU 3748  C   PRO A 241     4980   7250   5629  -1420   -389    981       C  
ATOM   3749  O   PRO A 241      22.778  14.157  -3.740  1.00 45.95           O  
ANISOU 3749  O   PRO A 241     4821   7164   5475  -1136   -336    918       O  
ATOM   3750  CB  PRO A 241      24.541  16.617  -2.569  1.00 49.37           C  
ANISOU 3750  CB  PRO A 241     5145   7787   5828  -1697   -485    840       C  
ATOM   3751  CG  PRO A 241      24.564  16.563  -1.068  1.00 50.32           C  
ANISOU 3751  CG  PRO A 241     5285   7871   5964  -1533   -514    711       C  
ATOM   3752  CD  PRO A 241      23.379  15.763  -0.653  1.00 47.39           C  
ANISOU 3752  CD  PRO A 241     5064   7248   5695  -1219   -475    726       C  
ATOM   3760  N   LEU A 242      22.972  15.773  -5.293  1.00 55.09           N  
ANISOU 3760  N   LEU A 242     5981   8327   6624  -1629   -388   1092       N  
ATOM   3761  CA  LEU A 242      22.860  14.874  -6.431  1.00 56.06           C  
ANISOU 3761  CA  LEU A 242     6014   8607   6678  -1531   -324   1119       C  
ATOM   3762  C   LEU A 242      24.247  14.609  -6.999  1.00 57.11           C  
ANISOU 3762  C   LEU A 242     5879   9219   6603  -1631   -302   1073       C  
ATOM   3763  O   LEU A 242      25.064  15.526  -7.124  1.00 58.57           O  
ANISOU 3763  O   LEU A 242     5976   9575   6704  -1933   -338   1112       O  
ATOM   3764  CB  LEU A 242      21.949  15.477  -7.501  1.00 54.45           C  
ANISOU 3764  CB  LEU A 242     5936   8207   6546  -1670   -336   1271       C  
ATOM   3765  CG  LEU A 242      21.093  14.497  -8.304  1.00 54.53           C  
ANISOU 3765  CG  LEU A 242     5955   8191   6575  -1473   -276   1269       C  
ATOM   3766  CD1 LEU A 242      20.050  13.832  -7.417  1.00 51.55           C  
ANISOU 3766  CD1 LEU A 242     5720   7533   6332  -1208   -253   1194       C  
ATOM   3767  CD2 LEU A 242      20.432  15.217  -9.470  1.00 55.60           C  
ANISOU 3767  CD2 LEU A 242     6163   8237   6724  -1640   -298   1427       C  
ATOM   3779  N   THR A 243      24.516  13.348  -7.321  1.00 51.88           N  
ANISOU 3779  N   THR A 243     5085   8776   5849  -1380   -248    976       N  
ATOM   3780  CA  THR A 243      25.797  12.936  -7.870  1.00 51.99           C  
ANISOU 3780  CA  THR A 243     4817   9294   5644  -1399   -229    893       C  
ATOM   3781  C   THR A 243      25.608  12.403  -9.283  1.00 51.58           C  
ANISOU 3781  C   THR A 243     4679   9401   5519  -1378   -184    914       C  
ATOM   3782  O   THR A 243      24.487  12.179  -9.749  1.00 48.67           O  
ANISOU 3782  O   THR A 243     4468   8751   5273  -1307   -164    973       O  
ATOM   3783  CB  THR A 243      26.459  11.854  -7.009  1.00 55.44           C  
ANISOU 3783  CB  THR A 243     5151   9914   6001  -1062   -222    722       C  
ATOM   3784  OG1 THR A 243      25.741  10.621  -7.165  1.00 56.34           O  
ANISOU 3784  OG1 THR A 243     5372   9848   6189   -733   -182    673       O  
ATOM   3785  CG2 THR A 243      26.472  12.264  -5.540  1.00 55.05           C  
ANISOU 3785  CG2 THR A 243     5200   9693   6023  -1033   -264    696       C  
ATOM   3793  N   GLN A 244      26.737  12.190  -9.960  1.00 55.22           N  
ANISOU 3793  N   GLN A 244     4859  10365   5756  -1437   -169    845       N  
ATOM   3794  CA  GLN A 244      26.705  11.619 -11.300  1.00 59.81           C  
ANISOU 3794  CA  GLN A 244     5311  11186   6228  -1396   -128    826       C  
ATOM   3795  C   GLN A 244      26.081  10.230 -11.294  1.00 58.36           C  
ANISOU 3795  C   GLN A 244     5212  10835   6127   -992    -99    690       C  
ATOM   3796  O   GLN A 244      25.441   9.833 -12.275  1.00 51.77           O  
ANISOU 3796  O   GLN A 244     4395   9969   5307   -952    -69    694       O  
ATOM   3797  CB  GLN A 244      28.121  11.570 -11.877  1.00 62.24           C  
ANISOU 3797  CB  GLN A 244     5267  12131   6252  -1497   -119    737       C  
ATOM   3798  CG  GLN A 244      28.190  11.114 -13.326  1.00 65.04           C  
ANISOU 3798  CG  GLN A 244     5443  12817   6451  -1492    -79    710       C  
ATOM   3799  CD  GLN A 244      27.389  12.003 -14.261  1.00 64.36           C  
ANISOU 3799  CD  GLN A 244     5475  12568   6413  -1802    -71    939       C  
ATOM   3800  OE1 GLN A 244      27.518  13.227 -14.238  1.00 65.50           O  
ANISOU 3800  OE1 GLN A 244     5671  12664   6554  -2173    -95   1126       O  
ATOM   3801  NE2 GLN A 244      26.551  11.388 -15.086  1.00 61.27           N  
ANISOU 3801  NE2 GLN A 244     5136  12081   6063  -1646    -44    922       N  
ATOM   3810  N   ASP A 245      26.255   9.476 -10.205  1.00 55.75           N  
ANISOU 3810  N   ASP A 245     4942  10397   5845   -699   -110    572       N  
ATOM   3811  CA  ASP A 245      25.615   8.170 -10.102  1.00 57.38           C  
ANISOU 3811  CA  ASP A 245     5285  10367   6150   -343    -86    466       C  
ATOM   3812  C   ASP A 245      24.099   8.299 -10.176  1.00 57.04           C  
ANISOU 3812  C   ASP A 245     5502   9848   6322   -398    -62    576       C  
ATOM   3813  O   ASP A 245      23.428   7.475 -10.809  1.00 54.23           O  
ANISOU 3813  O   ASP A 245     5208   9381   6018   -262    -29    515       O  
ATOM   3814  CB  ASP A 245      26.035   7.479  -8.804  1.00 58.02           C  
ANISOU 3814  CB  ASP A 245     5426  10377   6243    -48   -109    373       C  
ATOM   3815  CG  ASP A 245      27.497   7.076  -8.806  1.00 62.63           C  
ANISOU 3815  CG  ASP A 245     5733  11470   6591    107   -138    217       C  
ATOM   3816  OD1 ASP A 245      28.189   7.349  -9.811  1.00 62.80           O  
ANISOU 3816  OD1 ASP A 245     5501  11922   6436    -39   -132    175       O  
ATOM   3817  OD2 ASP A 245      27.955   6.486  -7.804  1.00 63.72           O  
ANISOU 3817  OD2 ASP A 245     5898  11611   6702    382   -167    138       O  
ATOM   3822  N   HIS A 246      23.543   9.334  -9.539  1.00 55.56           N  
ANISOU 3822  N   HIS A 246     5460   9397   6253   -593    -84    718       N  
ATOM   3823  CA  HIS A 246      22.104   9.570  -9.604  1.00 52.63           C  
ANISOU 3823  CA  HIS A 246     5306   8629   6061   -641    -71    813       C  
ATOM   3824  C   HIS A 246      21.669   9.947 -11.015  1.00 51.11           C  
ANISOU 3824  C   HIS A 246     5058   8531   5830   -813    -59    887       C  
ATOM   3825  O   HIS A 246      20.595   9.534 -11.470  1.00 46.64           O  
ANISOU 3825  O   HIS A 246     4592   7776   5353   -746    -31    882       O  
ATOM   3826  CB  HIS A 246      21.712  10.671  -8.619  1.00 52.78           C  
ANISOU 3826  CB  HIS A 246     5471   8391   6192   -787   -113    922       C  
ATOM   3827  CG  HIS A 246      21.937  10.308  -7.185  1.00 53.37           C  
ANISOU 3827  CG  HIS A 246     5613   8361   6304   -611   -123    857       C  
ATOM   3828  ND1 HIS A 246      22.366  11.220  -6.246  1.00 54.41           N  
ANISOU 3828  ND1 HIS A 246     5752   8484   6438   -729   -173    883       N  
ATOM   3829  CD2 HIS A 246      21.783   9.135  -6.528  1.00 54.44           C  
ANISOU 3829  CD2 HIS A 246     5821   8396   6468   -329    -93    773       C  
ATOM   3830  CE1 HIS A 246      22.473  10.623  -5.072  1.00 53.69           C  
ANISOU 3830  CE1 HIS A 246     5710   8331   6358   -514   -170    816       C  
ATOM   3831  NE2 HIS A 246      22.124   9.357  -5.216  1.00 53.76           N  
ANISOU 3831  NE2 HIS A 246     5771   8272   6382   -271   -122    765       N  
ATOM   3839  N   VAL A 247      22.483  10.740 -11.716  1.00 47.57           N  
ANISOU 3839  N   VAL A 247     4443   8397   5234  -1049    -79    960       N  
ATOM   3840  CA  VAL A 247      22.172  11.103 -13.096  1.00 46.62           C  
ANISOU 3840  CA  VAL A 247     4254   8423   5037  -1215    -69   1052       C  
ATOM   3841  C   VAL A 247      22.094   9.853 -13.963  1.00 47.06           C  
ANISOU 3841  C   VAL A 247     4191   8668   5019  -1004    -21    891       C  
ATOM   3842  O   VAL A 247      21.151   9.671 -14.741  1.00 43.83           O  
ANISOU 3842  O   VAL A 247     3833   8170   4651   -992     -2    907       O  
ATOM   3843  CB  VAL A 247      23.217  12.099 -13.634  1.00 48.73           C  
ANISOU 3843  CB  VAL A 247     4351   9040   5125  -1529    -93   1167       C  
ATOM   3844  CG1 VAL A 247      23.011  12.345 -15.125  1.00 48.62           C  
ANISOU 3844  CG1 VAL A 247     4238   9253   4984  -1683    -77   1269       C  
ATOM   3845  CG2 VAL A 247      23.158  13.409 -12.858  1.00 48.63           C  
ANISOU 3845  CG2 VAL A 247     4499   8766   5211  -1767   -151   1324       C  
ATOM   3855  N   ASP A 248      23.089   8.971 -13.841  1.00 51.38           N  
ANISOU 3855  N   ASP A 248     4578   9492   5453   -818     -9    715       N  
ATOM   3856  CA  ASP A 248      23.087   7.736 -14.618  1.00 51.77           C  
ANISOU 3856  CA  ASP A 248     4530   9704   5438   -586     23    522       C  
ATOM   3857  C   ASP A 248      21.823   6.926 -14.356  1.00 51.63           C  
ANISOU 3857  C   ASP A 248     4744   9253   5621   -405     48    461       C  
ATOM   3858  O   ASP A 248      21.184   6.427 -15.289  1.00 52.53           O  
ANISOU 3858  O   ASP A 248     4842   9383   5734   -369     74    389       O  
ATOM   3859  CB  ASP A 248      24.327   6.907 -14.287  1.00 51.06           C  
ANISOU 3859  CB  ASP A 248     4275   9913   5214   -350     13    329       C  
ATOM   3860  CG  ASP A 248      25.602   7.509 -14.846  1.00 51.85           C  
ANISOU 3860  CG  ASP A 248     4067  10577   5058   -529      2    336       C  
ATOM   3861  OD1 ASP A 248      25.516   8.464 -15.644  1.00 52.52           O  
ANISOU 3861  OD1 ASP A 248     4073  10818   5062   -845      9    497       O  
ATOM   3862  OD2 ASP A 248      26.692   7.022 -14.486  1.00 53.85           O  
ANISOU 3862  OD2 ASP A 248     4153  11132   5176   -354    -16    185       O  
ATOM   3867  N   ILE A 249      21.448   6.783 -13.084  1.00 47.72           N  
ANISOU 3867  N   ILE A 249     4452   8394   5284   -306     42    484       N  
ATOM   3868  CA  ILE A 249      20.301   5.951 -12.731  1.00 49.38           C  
ANISOU 3868  CA  ILE A 249     4878   8215   5669   -160     74    427       C  
ATOM   3869  C   ILE A 249      19.027   6.469 -13.385  1.00 45.60           C  
ANISOU 3869  C   ILE A 249     4468   7591   5268   -329     91    519       C  
ATOM   3870  O   ILE A 249      18.134   5.685 -13.731  1.00 46.38           O  
ANISOU 3870  O   ILE A 249     4644   7536   5442   -250    127    424       O  
ATOM   3871  CB  ILE A 249      20.170   5.877 -11.197  1.00 48.45           C  
ANISOU 3871  CB  ILE A 249     4948   7789   5672    -65     66    472       C  
ATOM   3872  CG1 ILE A 249      21.380   5.152 -10.601  1.00 52.70           C  
ANISOU 3872  CG1 ILE A 249     5421   8483   6118    167     44    360       C  
ATOM   3873  CG2 ILE A 249      18.897   5.162 -10.799  1.00 50.29           C  
ANISOU 3873  CG2 ILE A 249     5403   7633   6073     14    107    451       C  
ATOM   3874  CD1 ILE A 249      21.646   5.489  -9.151  1.00 53.98           C  
ANISOU 3874  CD1 ILE A 249     5679   8510   6320    206     19    437       C  
ATOM   3886  N   LEU A 250      18.918   7.783 -13.574  1.00 42.45           N  
ANISOU 3886  N   LEU A 250     4047   7237   4844   -558     59    699       N  
ATOM   3887  CA  LEU A 250      17.729   8.382 -14.166  1.00 43.21           C  
ANISOU 3887  CA  LEU A 250     4211   7211   4996   -685     57    802       C  
ATOM   3888  C   LEU A 250      17.749   8.375 -15.690  1.00 41.11           C  
ANISOU 3888  C   LEU A 250     3773   7263   4584   -760     66    789       C  
ATOM   3889  O   LEU A 250      16.775   8.824 -16.303  1.00 43.83           O  
ANISOU 3889  O   LEU A 250     4153   7556   4945   -841     59    870       O  
ATOM   3890  CB  LEU A 250      17.568   9.820 -13.668  1.00 42.85           C  
ANISOU 3890  CB  LEU A 250     4260   7026   4996   -867      1   1005       C  
ATOM   3891  CG  LEU A 250      17.178   9.979 -12.198  1.00 39.69           C  
ANISOU 3891  CG  LEU A 250     4040   6292   4748   -802    -12   1017       C  
ATOM   3892  CD1 LEU A 250      17.504  11.380 -11.709  1.00 39.16           C  
ANISOU 3892  CD1 LEU A 250     4028   6159   4692   -978    -81   1171       C  
ATOM   3893  CD2 LEU A 250      15.699   9.675 -12.002  1.00 40.52           C  
ANISOU 3893  CD2 LEU A 250     4284   6131   4982   -725     13    989       C  
ATOM   3905  N   GLY A 251      18.819   7.881 -16.308  1.00 43.45           N  
ANISOU 3905  N   GLY A 251     3871   7919   4720   -717     77    682       N  
ATOM   3906  CA  GLY A 251      18.949   7.881 -17.746  1.00 47.48           C  
ANISOU 3906  CA  GLY A 251     4185   8800   5055   -789     87    662       C  
ATOM   3907  C   GLY A 251      17.751   7.300 -18.473  1.00 46.81           C  
ANISOU 3907  C   GLY A 251     4132   8635   5018   -722    114    566       C  
ATOM   3908  O   GLY A 251      17.219   7.903 -19.410  1.00 43.50           O  
ANISOU 3908  O   GLY A 251     3654   8357   4517   -850    104    675       O  
ATOM   3912  N   PRO A 252      17.306   6.108 -18.063  1.00 50.72           N  
ANISOU 3912  N   PRO A 252     4723   8910   5636   -527    147    362       N  
ATOM   3913  CA  PRO A 252      16.163   5.489 -18.760  1.00 52.32           C  
ANISOU 3913  CA  PRO A 252     4943   9054   5881   -492    177    236       C  
ATOM   3914  C   PRO A 252      14.904   6.335 -18.723  1.00 48.67           C  
ANISOU 3914  C   PRO A 252     4588   8409   5497   -620    166    401       C  
ATOM   3915  O   PRO A 252      14.145   6.353 -19.699  1.00 48.51           O  
ANISOU 3915  O   PRO A 252     4488   8533   5413   -660    171    371       O  
ATOM   3916  CB  PRO A 252      15.980   4.158 -18.015  1.00 55.38           C  
ANISOU 3916  CB  PRO A 252     5479   9146   6418   -301    211     27       C  
ATOM   3917  CG  PRO A 252      17.320   3.879 -17.394  1.00 55.16           C  
ANISOU 3917  CG  PRO A 252     5424   9188   6346   -171    191    -10       C  
ATOM   3918  CD  PRO A 252      17.867   5.224 -17.026  1.00 51.93           C  
ANISOU 3918  CD  PRO A 252     4971   8883   5878   -335    156    232       C  
ATOM   3926  N   LEU A 253      14.650   7.035 -17.616  1.00 46.89           N  
ANISOU 3926  N   LEU A 253     4529   7891   5394   -663    143    556       N  
ATOM   3927  CA  LEU A 253      13.497   7.927 -17.566  1.00 45.89           C  
ANISOU 3927  CA  LEU A 253     4496   7613   5326   -748    116    702       C  
ATOM   3928  C   LEU A 253      13.719   9.146 -18.452  1.00 47.26           C  
ANISOU 3928  C   LEU A 253     4584   8015   5356   -893     60    912       C  
ATOM   3929  O   LEU A 253      12.779   9.641 -19.086  1.00 48.08           O  
ANISOU 3929  O   LEU A 253     4688   8152   5426   -926     35    988       O  
ATOM   3930  CB  LEU A 253      13.219   8.346 -16.125  1.00 43.78           C  
ANISOU 3930  CB  LEU A 253     4422   6997   5216   -734    100    785       C  
ATOM   3931  CG  LEU A 253      12.762   7.225 -15.187  1.00 45.25           C  
ANISOU 3931  CG  LEU A 253     4725   6930   5540   -617    157    627       C  
ATOM   3932  CD1 LEU A 253      12.580   7.754 -13.773  1.00 41.64           C  
ANISOU 3932  CD1 LEU A 253     4426   6196   5197   -610    137    725       C  
ATOM   3933  CD2 LEU A 253      11.477   6.588 -15.690  1.00 45.67           C  
ANISOU 3933  CD2 LEU A 253     4774   6953   5625   -609    200    499       C  
ATOM   3945  N   SER A 254      14.960   9.633 -18.517  1.00 44.46           N  
ANISOU 3945  N   SER A 254     4156   7837   4901   -987     37   1013       N  
ATOM   3946  CA  SER A 254      15.282  10.739 -19.411  1.00 46.79           C  
ANISOU 3946  CA  SER A 254     4378   8363   5039  -1166    -10   1233       C  
ATOM   3947  C   SER A 254      15.010  10.367 -20.863  1.00 49.86           C  
ANISOU 3947  C   SER A 254     4581   9109   5253  -1163     11   1177       C  
ATOM   3948  O   SER A 254      14.504  11.186 -21.640  1.00 48.96           O  
ANISOU 3948  O   SER A 254     4466   9091   5045  -1255    -30   1358       O  
ATOM   3949  CB  SER A 254      16.745  11.142 -19.227  1.00 47.77           C  
ANISOU 3949  CB  SER A 254     4418   8670   5063  -1298    -20   1311       C  
ATOM   3950  OG  SER A 254      17.094  12.207 -20.091  1.00 54.50           O  
ANISOU 3950  OG  SER A 254     5212   9742   5752  -1518    -60   1547       O  
ATOM   3956  N   ALA A 255      15.334   9.131 -21.246  1.00 51.96           N  
ANISOU 3956  N   ALA A 255     4698   9577   5468  -1042     67    920       N  
ATOM   3957  CA  ALA A 255      15.177   8.719 -22.636  1.00 54.06           C  
ANISOU 3957  CA  ALA A 255     4759  10232   5550  -1032     86    824       C  
ATOM   3958  C   ALA A 255      13.708   8.549 -23.002  1.00 58.08           C  
ANISOU 3958  C   ALA A 255     5318  10633   6117   -973     87    768       C  
ATOM   3959  O   ALA A 255      13.291   8.918 -24.107  1.00 55.81           O  
ANISOU 3959  O   ALA A 255     4914  10624   5668  -1023     69    840       O  
ATOM   3960  CB  ALA A 255      15.943   7.419 -22.883  1.00 54.52           C  
ANISOU 3960  CB  ALA A 255     4657  10509   5548   -890    133    524       C  
ATOM   3966  N   GLN A 256      12.907   7.995 -22.090  1.00 63.61           N  
ANISOU 3966  N   GLN A 256     6177  10967   7025   -874    109    641       N  
ATOM   3967  CA  GLN A 256      11.507   7.738 -22.403  1.00 66.46           C  
ANISOU 3967  CA  GLN A 256     6554  11271   7428   -831    118    548       C  
ATOM   3968  C   GLN A 256      10.708   9.030 -22.524  1.00 62.93           C  
ANISOU 3968  C   GLN A 256     6180  10775   6954   -889     51    805       C  
ATOM   3969  O   GLN A 256       9.749   9.089 -23.303  1.00 64.74           O  
ANISOU 3969  O   GLN A 256     6333  11166   7102   -866     39    778       O  
ATOM   3970  CB  GLN A 256      10.890   6.830 -21.337  1.00 71.69           C  
ANISOU 3970  CB  GLN A 256     7365  11571   8304   -749    165    363       C  
ATOM   3971  CG  GLN A 256       9.402   6.567 -21.530  1.00 76.41           C  
ANISOU 3971  CG  GLN A 256     7968  12120   8943   -739    182    254       C  
ATOM   3972  CD  GLN A 256       8.860   5.517 -20.577  1.00 78.82           C  
ANISOU 3972  CD  GLN A 256     8404  12110   9433   -704    244     60       C  
ATOM   3973  OE1 GLN A 256       9.619   4.752 -19.981  1.00 80.17           O  
ANISOU 3973  OE1 GLN A 256     8654  12121   9687   -656    276    -32       O  
ATOM   3974  NE2 GLN A 256       7.541   5.478 -20.427  1.00 79.53           N  
ANISOU 3974  NE2 GLN A 256     8519  12127   9573   -730    260      4       N  
ATOM   3983  N   THR A 257      11.079  10.069 -21.774  1.00 47.56           N  
ANISOU 3983  N   THR A 257     4386   8614   5071   -951     -1   1040       N  
ATOM   3984  CA  THR A 257      10.335  11.322 -21.778  1.00 46.80           C  
ANISOU 3984  CA  THR A 257     4409   8400   4974   -972    -83   1276       C  
ATOM   3985  C   THR A 257      10.961  12.401 -22.651  1.00 49.30           C  
ANISOU 3985  C   THR A 257     4694   8928   5110  -1104   -146   1555       C  
ATOM   3986  O   THR A 257      10.316  13.427 -22.890  1.00 51.17           O  
ANISOU 3986  O   THR A 257     5037   9091   5315  -1102   -227   1764       O  
ATOM   3987  CB  THR A 257      10.197  11.871 -20.351  1.00 45.72           C  
ANISOU 3987  CB  THR A 257     4494   7845   5033   -952   -116   1350       C  
ATOM   3988  OG1 THR A 257      11.497  12.045 -19.774  1.00 42.61           O  
ANISOU 3988  OG1 THR A 257     4137   7389   4665  -1046   -112   1416       O  
ATOM   3989  CG2 THR A 257       9.374  10.925 -19.488  1.00 42.05           C  
ANISOU 3989  CG2 THR A 257     4073   7180   4724   -841    -56   1119       C  
ATOM   3997  N   GLY A 258      12.190  12.205 -23.124  1.00 49.89           N  
ANISOU 3997  N   GLY A 258     4632   9270   5054  -1215   -115   1569       N  
ATOM   3998  CA  GLY A 258      12.856  13.231 -23.899  1.00 51.32           C  
ANISOU 3998  CA  GLY A 258     4784   9664   5049  -1392   -165   1855       C  
ATOM   3999  C   GLY A 258      13.256  14.453 -23.107  1.00 53.24           C  
ANISOU 3999  C   GLY A 258     5254   9588   5386  -1526   -235   2114       C  
ATOM   4000  O   GLY A 258      13.439  15.525 -23.691  1.00 52.16           O  
ANISOU 4000  O   GLY A 258     5183   9508   5130  -1678   -300   2404       O  
ATOM   4004  N   ILE A 259      13.404  14.324 -21.791  1.00 54.40           N  
ANISOU 4004  N   ILE A 259     5532   9397   5740  -1483   -228   2018       N  
ATOM   4005  CA  ILE A 259      13.733  15.442 -20.913  1.00 55.64           C  
ANISOU 4005  CA  ILE A 259     5909   9223   6009  -1598   -299   2211       C  
ATOM   4006  C   ILE A 259      15.031  15.110 -20.190  1.00 52.29           C  
ANISOU 4006  C   ILE A 259     5421   8838   5609  -1697   -252   2125       C  
ATOM   4007  O   ILE A 259      15.099  14.123 -19.446  1.00 49.54           O  
ANISOU 4007  O   ILE A 259     5030   8427   5363  -1555   -194   1888       O  
ATOM   4008  CB  ILE A 259      12.606  15.731 -19.909  1.00 53.32           C  
ANISOU 4008  CB  ILE A 259     5829   8505   5926  -1431   -348   2169       C  
ATOM   4009  CG1 ILE A 259      11.322  16.114 -20.652  1.00 56.50           C  
ANISOU 4009  CG1 ILE A 259     6272   8919   6277  -1309   -406   2247       C  
ATOM   4010  CG2 ILE A 259      13.029  16.832 -18.939  1.00 55.62           C  
ANISOU 4010  CG2 ILE A 259     6341   8454   6337  -1539   -425   2319       C  
ATOM   4011  CD1 ILE A 259      10.102  16.223 -19.753  1.00 56.57           C  
ANISOU 4011  CD1 ILE A 259     6426   8611   6457  -1109   -444   2148       C  
ATOM   4023  N   ALA A 260      16.050  15.939 -20.400  1.00 51.05           N  
ANISOU 4023  N   ALA A 260     5261   8791   5346  -1947   -281   2323       N  
ATOM   4024  CA  ALA A 260      17.348  15.715 -19.785  1.00 52.54           C  
ANISOU 4024  CA  ALA A 260     5352   9092   5517  -2059   -244   2244       C  
ATOM   4025  C   ALA A 260      17.265  15.871 -18.270  1.00 49.56           C  
ANISOU 4025  C   ALA A 260     5157   8307   5365  -1986   -270   2165       C  
ATOM   4026  O   ALA A 260      16.443  16.625 -17.743  1.00 48.05           O  
ANISOU 4026  O   ALA A 260     5198   7740   5321  -1950   -340   2257       O  
ATOM   4027  CB  ALA A 260      18.379  16.688 -20.354  1.00 51.02           C  
ANISOU 4027  CB  ALA A 260     5116   9119   5149  -2395   -271   2488       C  
ATOM   4033  N   VAL A 261      18.138  15.146 -17.569  1.00 50.74           N  
ANISOU 4033  N   VAL A 261     5191   8562   5524  -1941   -219   1985       N  
ATOM   4034  CA  VAL A 261      18.133  15.183 -16.109  1.00 48.22           C  
ANISOU 4034  CA  VAL A 261     5013   7919   5388  -1858   -237   1896       C  
ATOM   4035  C   VAL A 261      18.358  16.605 -15.611  1.00 47.24           C  
ANISOU 4035  C   VAL A 261     5072   7552   5324  -2080   -323   2088       C  
ATOM   4036  O   VAL A 261      17.673  17.074 -14.693  1.00 45.92           O  
ANISOU 4036  O   VAL A 261     5112   7005   5332  -1998   -376   2084       O  
ATOM   4037  CB  VAL A 261      19.189  14.211 -15.549  1.00 50.97           C  
ANISOU 4037  CB  VAL A 261     5190   8484   5691  -1773   -177   1695       C  
ATOM   4038  CG1 VAL A 261      19.240  14.293 -14.036  1.00 47.25           C  
ANISOU 4038  CG1 VAL A 261     4854   7721   5380  -1694   -198   1621       C  
ATOM   4039  CG2 VAL A 261      18.889  12.781 -15.995  1.00 52.23           C  
ANISOU 4039  CG2 VAL A 261     5223   8800   5822  -1530   -106   1489       C  
ATOM   4049  N   LEU A 262      19.313  17.318 -16.209  1.00 52.94           N  
ANISOU 4049  N   LEU A 262     5723   8494   5895  -2375   -340   2249       N  
ATOM   4050  CA  LEU A 262      19.617  18.669 -15.751  1.00 56.75           C  
ANISOU 4050  CA  LEU A 262     6399   8725   6438  -2630   -425   2425       C  
ATOM   4051  C   LEU A 262      18.470  19.632 -16.028  1.00 56.78           C  
ANISOU 4051  C   LEU A 262     6679   8351   6542  -2615   -519   2616       C  
ATOM   4052  O   LEU A 262      18.276  20.591 -15.271  1.00 58.00           O  
ANISOU 4052  O   LEU A 262     7073   8125   6841  -2678   -607   2679       O  
ATOM   4053  CB  LEU A 262      20.906  19.165 -16.408  1.00 59.32           C  
ANISOU 4053  CB  LEU A 262     6575   9407   6557  -2995   -413   2564       C  
ATOM   4054  CG  LEU A 262      22.183  18.463 -15.938  1.00 60.04           C  
ANISOU 4054  CG  LEU A 262     6400   9872   6542  -3028   -346   2370       C  
ATOM   4055  CD1 LEU A 262      23.410  19.027 -16.645  1.00 63.94           C  
ANISOU 4055  CD1 LEU A 262     6719  10773   6801  -3424   -331   2510       C  
ATOM   4056  CD2 LEU A 262      22.339  18.579 -14.425  1.00 60.68           C  
ANISOU 4056  CD2 LEU A 262     6588   9673   6794  -2954   -377   2227       C  
ATOM   4068  N   ASP A 263      17.704  19.408 -17.098  1.00 53.61           N  
ANISOU 4068  N   ASP A 263     6249   8060   6061  -2514   -510   2695       N  
ATOM   4069  CA  ASP A 263      16.509  20.213 -17.320  1.00 55.55           C  
ANISOU 4069  CA  ASP A 263     6744   7970   6393  -2420   -606   2847       C  
ATOM   4070  C   ASP A 263      15.479  19.966 -16.228  1.00 53.56           C  
ANISOU 4070  C   ASP A 263     6617   7381   6350  -2122   -629   2660       C  
ATOM   4071  O   ASP A 263      14.882  20.912 -15.701  1.00 54.22           O  
ANISOU 4071  O   ASP A 263     6953   7083   6566  -2079   -734   2732       O  
ATOM   4072  CB  ASP A 263      15.912  19.912 -18.695  1.00 60.11           C  
ANISOU 4072  CB  ASP A 263     7217   8810   6812  -2349   -586   2942       C  
ATOM   4073  CG  ASP A 263      16.804  20.374 -19.827  1.00 64.33           C  
ANISOU 4073  CG  ASP A 263     7657   9669   7116  -2661   -579   3181       C  
ATOM   4074  OD1 ASP A 263      17.675  21.236 -19.580  1.00 65.25           O  
ANISOU 4074  OD1 ASP A 263     7871   9700   7221  -2959   -617   3334       O  
ATOM   4075  OD2 ASP A 263      16.630  19.881 -20.963  1.00 65.69           O  
ANISOU 4075  OD2 ASP A 263     7651  10201   7108  -2624   -534   3209       O  
ATOM   4080  N   MET A 264      15.261  18.700 -15.868  1.00 46.10           N  
ANISOU 4080  N   MET A 264     5508   6577   5433  -1915   -536   2417       N  
ATOM   4081  CA  MET A 264      14.335  18.400 -14.783  1.00 45.81           C  
ANISOU 4081  CA  MET A 264     5568   6269   5569  -1669   -543   2244       C  
ATOM   4082  C   MET A 264      14.829  19.000 -13.472  1.00 46.54           C  
ANISOU 4082  C   MET A 264     5793   6101   5788  -1730   -591   2205       C  
ATOM   4083  O   MET A 264      14.031  19.497 -12.668  1.00 46.74           O  
ANISOU 4083  O   MET A 264     5991   5818   5950  -1594   -658   2162       O  
ATOM   4084  CB  MET A 264      14.148  16.888 -14.657  1.00 43.17           C  
ANISOU 4084  CB  MET A 264     5047   6129   5227  -1490   -428   2014       C  
ATOM   4085  CG  MET A 264      12.989  16.494 -13.761  1.00 42.80           C  
ANISOU 4085  CG  MET A 264     5082   5860   5322  -1257   -420   1861       C  
ATOM   4086  SD  MET A 264      11.394  16.961 -14.462  1.00 48.22           S  
ANISOU 4086  SD  MET A 264     5850   6465   6007  -1110   -483   1923       S  
ATOM   4087  CE  MET A 264      10.828  15.373 -15.066  1.00 47.47           C  
ANISOU 4087  CE  MET A 264     5541   6646   5849   -990   -359   1727       C  
ATOM   4097  N   CYS A 265      16.146  18.977 -13.243  1.00 47.93           N  
ANISOU 4097  N   CYS A 265     5872   6434   5905  -1929   -562   2200       N  
ATOM   4098  CA  CYS A 265      16.700  19.611 -12.052  1.00 48.88           C  
ANISOU 4098  CA  CYS A 265     6100   6347   6123  -2019   -613   2156       C  
ATOM   4099  C   CYS A 265      16.332  21.088 -11.995  1.00 50.72           C  
ANISOU 4099  C   CYS A 265     6608   6219   6445  -2133   -746   2318       C  
ATOM   4100  O   CYS A 265      16.017  21.617 -10.923  1.00 50.76           O  
ANISOU 4100  O   CYS A 265     6772   5922   6591  -2057   -815   2232       O  
ATOM   4101  CB  CYS A 265      18.220  19.440 -12.024  1.00 51.75           C  
ANISOU 4101  CB  CYS A 265     6286   7010   6368  -2248   -566   2140       C  
ATOM   4102  SG  CYS A 265      18.787  17.783 -11.568  1.00 50.51           S  
ANISOU 4102  SG  CYS A 265     5863   7182   6147  -2043   -443   1895       S  
ATOM   4108  N   ALA A 266      16.368  21.771 -13.143  1.00 54.07           N  
ANISOU 4108  N   ALA A 266     7101   6664   6779  -2308   -792   2553       N  
ATOM   4109  CA  ALA A 266      16.015  23.186 -13.180  1.00 54.63           C  
ANISOU 4109  CA  ALA A 266     7477   6346   6932  -2407   -933   2734       C  
ATOM   4110  C   ALA A 266      14.555  23.411 -12.808  1.00 55.86           C  
ANISOU 4110  C   ALA A 266     7809   6193   7222  -2070  -1011   2668       C  
ATOM   4111  O   ALA A 266      14.223  24.426 -12.183  1.00 53.15           O  
ANISOU 4111  O   ALA A 266     7722   5461   7010  -2042  -1135   2680       O  
ATOM   4112  CB  ALA A 266      16.299  23.760 -14.569  1.00 55.20           C  
ANISOU 4112  CB  ALA A 266     7588   6533   6853  -2647   -959   3030       C  
ATOM   4118  N   SER A 267      13.670  22.485 -13.186  1.00 57.22           N  
ANISOU 4118  N   SER A 267     7840   6546   7354  -1814   -945   2580       N  
ATOM   4119  CA  SER A 267      12.267  22.599 -12.802  1.00 58.39           C  
ANISOU 4119  CA  SER A 267     8101   6485   7600  -1493  -1006   2485       C  
ATOM   4120  C   SER A 267      12.089  22.390 -11.304  1.00 54.45           C  
ANISOU 4120  C   SER A 267     7615   5834   7238  -1350   -999   2245       C  
ATOM   4121  O   SER A 267      11.313  23.103 -10.658  1.00 57.74           O  
ANISOU 4121  O   SER A 267     8213   5963   7763  -1179  -1104   2187       O  
ATOM   4122  CB  SER A 267      11.424  21.594 -13.587  1.00 58.17           C  
ANISOU 4122  CB  SER A 267     7885   6740   7477  -1305   -924   2431       C  
ATOM   4123  OG  SER A 267      11.259  22.010 -14.932  1.00 62.97           O  
ANISOU 4123  OG  SER A 267     8519   7449   7958  -1366   -966   2655       O  
ATOM   4129  N   LEU A 268      12.797  21.412 -10.735  1.00 45.35           N  
ANISOU 4129  N   LEU A 268     6272   4891   6069  -1397   -883   2100       N  
ATOM   4130  CA  LEU A 268      12.739  21.200  -9.293  1.00 44.00           C  
ANISOU 4130  CA  LEU A 268     6106   4612   6000  -1280   -872   1896       C  
ATOM   4131  C   LEU A 268      13.290  22.408  -8.543  1.00 49.53           C  
ANISOU 4131  C   LEU A 268     6998   5030   6790  -1416   -988   1909       C  
ATOM   4132  O   LEU A 268      12.705  22.851  -7.547  1.00 53.45           O  
ANISOU 4132  O   LEU A 268     7611   5304   7392  -1256  -1057   1777       O  
ATOM   4133  CB  LEU A 268      13.511  19.932  -8.929  1.00 41.85           C  
ANISOU 4133  CB  LEU A 268     5610   4622   5670  -1306   -735   1775       C  
ATOM   4134  CG  LEU A 268      13.664  19.594  -7.446  1.00 42.66           C  
ANISOU 4134  CG  LEU A 268     5693   4677   5839  -1207   -711   1590       C  
ATOM   4135  CD1 LEU A 268      12.317  19.546  -6.748  1.00 41.28           C  
ANISOU 4135  CD1 LEU A 268     5586   4356   5741   -952   -731   1471       C  
ATOM   4136  CD2 LEU A 268      14.399  18.267  -7.291  1.00 41.03           C  
ANISOU 4136  CD2 LEU A 268     5284   4751   5555  -1199   -584   1507       C  
ATOM   4148  N   LYS A 269      14.411  22.958  -9.016  1.00 53.08           N  
ANISOU 4148  N   LYS A 269     7474   5502   7191  -1724  -1009   2054       N  
ATOM   4149  CA  LYS A 269      14.983  24.158  -8.411  1.00 59.13           C  
ANISOU 4149  CA  LYS A 269     8439   5985   8043  -1914  -1123   2072       C  
ATOM   4150  C   LYS A 269      13.934  25.253  -8.245  1.00 61.07           C  
ANISOU 4150  C   LYS A 269     8977   5811   8413  -1748  -1279   2094       C  
ATOM   4151  O   LYS A 269      13.834  25.880  -7.184  1.00 57.69           O  
ANISOU 4151  O   LYS A 269     8687   5128   8102  -1688  -1365   1947       O  
ATOM   4152  CB  LYS A 269      16.152  24.652  -9.267  1.00 61.82           C  
ANISOU 4152  CB  LYS A 269     8778   6423   8287  -2307  -1125   2279       C  
ATOM   4153  CG  LYS A 269      16.756  25.983  -8.838  1.00 67.45           C  
ANISOU 4153  CG  LYS A 269     9728   6815   9085  -2578  -1249   2331       C  
ATOM   4154  CD  LYS A 269      17.982  26.303  -9.681  1.00 70.59           C  
ANISOU 4154  CD  LYS A 269    10069   7401   9350  -3016  -1221   2533       C  
ATOM   4155  CE  LYS A 269      18.538  27.689  -9.391  1.00 76.41           C  
ANISOU 4155  CE  LYS A 269    11079   7782  10173  -3346  -1348   2614       C  
ATOM   4156  NZ  LYS A 269      17.547  28.770  -9.661  1.00 79.64           N  
ANISOU 4156  NZ  LYS A 269    11845   7716  10699  -3190  -1489   2715       N  
ATOM   4170  N   GLU A 270      13.145  25.494  -9.297  1.00 66.10           N  
ANISOU 4170  N   GLU A 270     9708   6393   9016  -1650  -1323   2262       N  
ATOM   4171  CA  GLU A 270      12.098  26.509  -9.238  1.00 68.81           C  
ANISOU 4171  CA  GLU A 270    10330   6358   9457  -1436  -1485   2286       C  
ATOM   4172  C   GLU A 270      11.043  26.156  -8.198  1.00 67.98           C  
ANISOU 4172  C   GLU A 270    10176   6227   9425  -1070  -1490   2018       C  
ATOM   4173  O   GLU A 270      10.555  27.033  -7.475  1.00 70.58           O  
ANISOU 4173  O   GLU A 270    10712   6237   9867   -916  -1625   1912       O  
ATOM   4174  CB  GLU A 270      11.446  26.664 -10.613  1.00 69.70           C  
ANISOU 4174  CB  GLU A 270    10501   6506   9477  -1365  -1519   2517       C  
ATOM   4175  CG  GLU A 270      11.631  28.026 -11.263  1.00 73.56           C  
ANISOU 4175  CG  GLU A 270    11324   6637   9990  -1528  -1677   2783       C  
ATOM   4176  CD  GLU A 270      10.320  28.636 -11.722  1.00 73.68           C  
ANISOU 4176  CD  GLU A 270    11543   6433  10019  -1188  -1817   2857       C  
ATOM   4177  OE1 GLU A 270       9.316  28.517 -10.989  1.00 73.28           O  
ANISOU 4177  OE1 GLU A 270    11478   6327  10037   -830  -1855   2627       O  
ATOM   4178  OE2 GLU A 270      10.293  29.233 -12.819  1.00 74.50           O  
ANISOU 4178  OE2 GLU A 270    11811   6449  10046  -1272  -1890   3147       O  
ATOM   4200  N   LEU A 271      10.665  24.878  -8.121  1.00 58.55           N  
ANISOU 4200  N   LEU A 271     8715   5372   8161   -931  -1346   1900       N  
ATOM   4201  CA  LEU A 271       9.642  24.459  -7.169  1.00 56.91           C  
ANISOU 4201  CA  LEU A 271     8436   5196   7992   -622  -1332   1663       C  
ATOM   4202  C   LEU A 271      10.085  24.719  -5.735  1.00 58.38           C  
ANISOU 4202  C   LEU A 271     8654   5262   8264   -632  -1357   1470       C  
ATOM   4203  O   LEU A 271       9.278  25.129  -4.893  1.00 60.97           O  
ANISOU 4203  O   LEU A 271     9056   5456   8654   -393  -1436   1298       O  
ATOM   4204  CB  LEU A 271       9.309  22.980  -7.371  1.00 55.31           C  
ANISOU 4204  CB  LEU A 271     7956   5365   7695   -549  -1161   1594       C  
ATOM   4205  CG  LEU A 271       8.483  22.640  -8.616  1.00 54.54           C  
ANISOU 4205  CG  LEU A 271     7792   5423   7506   -450  -1140   1698       C  
ATOM   4206  CD1 LEU A 271       8.315  21.137  -8.770  1.00 50.57           C  
ANISOU 4206  CD1 LEU A 271     7030   5259   6926   -434   -968   1607       C  
ATOM   4207  CD2 LEU A 271       7.122  23.322  -8.563  1.00 56.96           C  
ANISOU 4207  CD2 LEU A 271     8212   5593   7836   -151  -1262   1640       C  
ATOM   4219  N   LEU A 272      11.366  24.489  -5.435  1.00 60.83           N  
ANISOU 4219  N   LEU A 272     8891   5660   8562   -895  -1295   1480       N  
ATOM   4220  CA  LEU A 272      11.860  24.723  -4.082  1.00 64.63           C  
ANISOU 4220  CA  LEU A 272     9380   6071   9103   -915  -1319   1291       C  
ATOM   4221  C   LEU A 272      11.842  26.207  -3.737  1.00 68.71           C  
ANISOU 4221  C   LEU A 272    10183   6183   9740   -941  -1504   1264       C  
ATOM   4222  O   LEU A 272      11.498  26.585  -2.611  1.00 69.11           O  
ANISOU 4222  O   LEU A 272    10287   6114   9858   -781  -1572   1049       O  
ATOM   4223  CB  LEU A 272      13.275  24.163  -3.938  1.00 62.76           C  
ANISOU 4223  CB  LEU A 272     8983   6060   8802  -1185  -1218   1310       C  
ATOM   4224  CG  LEU A 272      13.434  22.669  -4.226  1.00 61.26           C  
ANISOU 4224  CG  LEU A 272     8535   6241   8501  -1147  -1048   1319       C  
ATOM   4225  CD1 LEU A 272      14.905  22.279  -4.238  1.00 61.03           C  
ANISOU 4225  CD1 LEU A 272     8361   6435   8392  -1397   -978   1347       C  
ATOM   4226  CD2 LEU A 272      12.669  21.835  -3.209  1.00 59.03           C  
ANISOU 4226  CD2 LEU A 272     8147   6065   8216   -883   -980   1135       C  
ATOM   4238  N   GLN A 273      12.200  27.062  -4.696  1.00 75.08           N  
ANISOU 4238  N   GLN A 273    11187   6770  10569  -1144  -1591   1479       N  
ATOM   4239  CA  GLN A 273      12.305  28.492  -4.429  1.00 79.23           C  
ANISOU 4239  CA  GLN A 273    12031   6852  11219  -1216  -1775   1474       C  
ATOM   4240  C   GLN A 273      10.943  29.175  -4.434  1.00 79.66           C  
ANISOU 4240  C   GLN A 273    12295   6624  11346   -850  -1922   1421       C  
ATOM   4241  O   GLN A 273      10.708  30.098  -3.646  1.00 82.03           O  
ANISOU 4241  O   GLN A 273    12803   6602  11762   -737  -2069   1257       O  
ATOM   4242  CB  GLN A 273      13.224  29.145  -5.461  1.00 81.73           C  
ANISOU 4242  CB  GLN A 273    12501   7032  11519  -1604  -1812   1755       C  
ATOM   4243  CG  GLN A 273      14.675  28.705  -5.366  1.00 82.44           C  
ANISOU 4243  CG  GLN A 273    12395   7397  11532  -1987  -1696   1774       C  
ATOM   4244  CD  GLN A 273      15.507  29.187  -6.538  1.00 84.64           C  
ANISOU 4244  CD  GLN A 273    12762   7652  11744  -2382  -1703   2073       C  
ATOM   4245  OE1 GLN A 273      14.972  29.643  -7.549  1.00 86.60           O  
ANISOU 4245  OE1 GLN A 273    13191   7732  11983  -2355  -1769   2301       O  
ATOM   4246  NE2 GLN A 273      16.825  29.088  -6.408  1.00 85.36           N  
ANISOU 4246  NE2 GLN A 273    12715   7949  11769  -2752  -1636   2075       N  
ATOM   4255  N   ASN A 274      10.036  28.744  -5.311  1.00 78.10           N  
ANISOU 4255  N   ASN A 274    12038   6563  11074   -646  -1892   1534       N  
ATOM   4256  CA  ASN A 274       8.751  29.406  -5.480  1.00 81.76           C  
ANISOU 4256  CA  ASN A 274    12683   6806  11575   -283  -2040   1503       C  
ATOM   4257  C   ASN A 274       7.569  28.593  -4.972  1.00 81.88           C  
ANISOU 4257  C   ASN A 274    12467   7115  11529     85  -1973   1284       C  
ATOM   4258  O   ASN A 274       6.448  29.112  -4.956  1.00 86.05           O  
ANISOU 4258  O   ASN A 274    13100   7524  12069    429  -2096   1200       O  
ATOM   4259  CB  ASN A 274       8.528  29.743  -6.962  1.00 81.91           C  
ANISOU 4259  CB  ASN A 274    12839   6748  11533   -319  -2091   1816       C  
ATOM   4260  CG  ASN A 274       9.615  30.639  -7.525  1.00 83.55           C  
ANISOU 4260  CG  ASN A 274    13306   6655  11786   -706  -2166   2067       C  
ATOM   4261  OD1 ASN A 274      10.083  31.561  -6.857  1.00 84.86           O  
ANISOU 4261  OD1 ASN A 274    13708   6457  12078   -823  -2284   1996       O  
ATOM   4262  ND2 ASN A 274      10.028  30.366  -8.758  1.00 83.75           N  
ANISOU 4262  ND2 ASN A 274    13278   6849  11695   -928  -2095   2354       N  
ATOM   4269  N   GLY A 275       7.782  27.347  -4.558  1.00 71.96           N  
ANISOU 4269  N   GLY A 275     9639   7198  10506   -659   -341   2378       N  
ATOM   4270  CA  GLY A 275       6.688  26.534  -4.070  1.00 69.58           C  
ANISOU 4270  CA  GLY A 275     9172   7335   9931   -413   -617   2164       C  
ATOM   4271  C   GLY A 275       5.781  26.071  -5.201  1.00 71.79           C  
ANISOU 4271  C   GLY A 275     9482   7952   9843      6   -594   2260       C  
ATOM   4272  O   GLY A 275       6.045  26.277  -6.386  1.00 69.29           O  
ANISOU 4272  O   GLY A 275     9364   7560   9403    159   -392   2528       O  
ATOM   4276  N   MET A 276       4.681  25.433  -4.802  1.00 82.10           N  
ANISOU 4276  N   MET A 276    10593   9629  10972    203   -789   1994       N  
ATOM   4277  CA  MET A 276       3.734  24.859  -5.747  1.00 87.55           C  
ANISOU 4277  CA  MET A 276    11178  10719  11370    590   -848   1922       C  
ATOM   4278  C   MET A 276       2.517  25.745  -5.988  1.00 93.65           C  
ANISOU 4278  C   MET A 276    12154  11502  11926   1121   -980   1807       C  
ATOM   4279  O   MET A 276       1.648  25.373  -6.781  1.00 94.14           O  
ANISOU 4279  O   MET A 276    12098  11925  11747   1529  -1107   1654       O  
ATOM   4280  CB  MET A 276       3.278  23.477  -5.260  1.00 85.88           C  
ANISOU 4280  CB  MET A 276    10549  10918  11163    436   -921   1619       C  
ATOM   4281  CG  MET A 276       4.421  22.569  -4.809  1.00 82.94           C  
ANISOU 4281  CG  MET A 276    10029  10522  10963     -7   -845   1687       C  
ATOM   4282  SD  MET A 276       4.333  20.883  -5.455  1.00 78.62           S  
ANISOU 4282  SD  MET A 276     9169  10398  10303    -55   -805   1580       S  
ATOM   4283  CE  MET A 276       2.601  20.505  -5.198  1.00 78.01           C  
ANISOU 4283  CE  MET A 276     8876  10639  10124    156   -864   1139       C  
ATOM   4293  N   ASN A 277       2.432  26.902  -5.332  1.00102.32           N  
ANISOU 4293  N   ASN A 277    13545  12224  13106   1167   -988   1828       N  
ATOM   4294  CA  ASN A 277       1.346  27.857  -5.564  1.00105.75           C  
ANISOU 4294  CA  ASN A 277    14240  12617  13322   1744  -1124   1730       C  
ATOM   4295  C   ASN A 277      -0.028  27.215  -5.379  1.00101.89           C  
ANISOU 4295  C   ASN A 277    13315  12666  12734   2037  -1337   1263       C  
ATOM   4296  O   ASN A 277      -0.983  27.552  -6.080  1.00105.56           O  
ANISOU 4296  O   ASN A 277    13821  13335  12952   2641  -1522   1105       O  
ATOM   4297  CB  ASN A 277       1.448  28.478  -6.961  1.00110.27           C  
ANISOU 4297  CB  ASN A 277    15288  13018  13591   2210  -1054   2051       C  
ATOM   4298  CG  ASN A 277       2.505  29.559  -7.046  1.00113.37           C  
ANISOU 4298  CG  ASN A 277    16237  12729  14110   1999   -749   2455       C  
ATOM   4299  OD1 ASN A 277       3.506  29.412  -7.748  1.00113.02           O  
ANISOU 4299  OD1 ASN A 277    16335  12502  14105   1764   -466   2768       O  
ATOM   4300  ND2 ASN A 277       2.282  30.659  -6.336  1.00116.14           N  
ANISOU 4300  ND2 ASN A 277    16897  12679  14552   2063   -764   2417       N  
ATOM   4307  N   GLY A 278      -0.137  26.286  -4.432  1.00 85.58           N  
ANISOU 4307  N   GLY A 278    10838  10817  10860   1632  -1294   1003       N  
ATOM   4308  CA  GLY A 278      -1.392  25.602  -4.197  1.00 82.41           C  
ANISOU 4308  CA  GLY A 278     9975  10879  10457   1779  -1364    516       C  
ATOM   4309  C   GLY A 278      -1.790  24.603  -5.260  1.00 79.98           C  
ANISOU 4309  C   GLY A 278     9313  11027  10047   1933  -1440    338       C  
ATOM   4310  O   GLY A 278      -2.845  23.973  -5.128  1.00 78.17           O  
ANISOU 4310  O   GLY A 278     8614  11193   9894   2003  -1470   -153       O  
ATOM   4314  N   ARG A 279      -0.988  24.441  -6.308  1.00 80.01           N  
ANISOU 4314  N   ARG A 279     9513  10982   9905   1977  -1443    677       N  
ATOM   4315  CA  ARG A 279      -1.228  23.408  -7.302  1.00 81.77           C  
ANISOU 4315  CA  ARG A 279     9434  11620  10016   2094  -1522    509       C  
ATOM   4316  C   ARG A 279      -0.837  22.044  -6.732  1.00 72.03           C  
ANISOU 4316  C   ARG A 279     7861  10502   9006   1495  -1323    406       C  
ATOM   4317  O   ARG A 279      -0.449  21.912  -5.568  1.00 68.64           O  
ANISOU 4317  O   ARG A 279     7460   9855   8764   1067  -1151    453       O  
ATOM   4318  CB  ARG A 279      -0.440  23.708  -8.573  1.00 90.68           C  
ANISOU 4318  CB  ARG A 279    10976  12610  10867   2356  -1529    939       C  
ATOM   4319  CG  ARG A 279      -1.240  24.248  -9.758  1.00102.76           C  
ANISOU 4319  CG  ARG A 279    12701  14338  12004   3163  -1812    829       C  
ATOM   4320  CD  ARG A 279      -0.273  24.472 -10.918  1.00110.66           C  
ANISOU 4320  CD  ARG A 279    14239  15106  12699   3339  -1676   1341       C  
ATOM   4321  NE  ARG A 279      -0.877  24.536 -12.249  1.00119.79           N  
ANISOU 4321  NE  ARG A 279    15602  16524  13389   4092  -1933   1225       N  
ATOM   4322  CZ  ARG A 279      -1.559  23.550 -12.828  1.00124.22           C  
ANISOU 4322  CZ  ARG A 279    15713  17577  13908   4185  -2135    733       C  
ATOM   4323  NH1 ARG A 279      -1.774  22.404 -12.191  1.00122.90           N  
ANISOU 4323  NH1 ARG A 279    14865  17763  14068   3772  -2180    380       N  
ATOM   4324  NH2 ARG A 279      -2.044  23.718 -14.051  1.00129.57           N  
ANISOU 4324  NH2 ARG A 279    16655  18361  14214   4686  -2259    560       N  
ATOM   4338  N   THR A 280      -0.929  21.014  -7.571  1.00 63.32           N  
ANISOU 4338  N   THR A 280     6499   9721   7840   1515  -1358    255       N  
ATOM   4339  CA  THR A 280      -0.589  19.660  -7.164  1.00 53.90           C  
ANISOU 4339  CA  THR A 280     5057   8605   6819   1007  -1155    154       C  
ATOM   4340  C   THR A 280       0.142  18.956  -8.296  1.00 51.57           C  
ANISOU 4340  C   THR A 280     4801   8418   6374   1036  -1175    351       C  
ATOM   4341  O   THR A 280       0.068  19.358  -9.461  1.00 51.59           O  
ANISOU 4341  O   THR A 280     4940   8544   6120   1495  -1354    431       O  
ATOM   4342  CB  THR A 280      -1.836  18.852  -6.775  1.00 52.35           C  
ANISOU 4342  CB  THR A 280     4360   8724   6807    907  -1089   -466       C  
ATOM   4343  OG1 THR A 280      -2.731  18.774  -7.892  1.00 53.73           O  
ANISOU 4343  OG1 THR A 280     4223   9312   6881   1368  -1360   -862       O  
ATOM   4344  CG2 THR A 280      -2.550  19.498  -5.594  1.00 50.22           C  
ANISOU 4344  CG2 THR A 280     4052   8344   6686    861   -988   -672       C  
ATOM   4352  N   ILE A 281       0.859  17.897  -7.929  1.00 49.06           N  
ANISOU 4352  N   ILE A 281     4427   8037   6176    592   -981    429       N  
ATOM   4353  CA  ILE A 281       1.522  17.009  -8.877  1.00 47.85           C  
ANISOU 4353  CA  ILE A 281     4260   8006   5916    570   -960    546       C  
ATOM   4354  C   ILE A 281       1.162  15.583  -8.486  1.00 47.66           C  
ANISOU 4354  C   ILE A 281     3945   8115   6048    231   -811    187       C  
ATOM   4355  O   ILE A 281       1.459  15.152  -7.366  1.00 42.42           O  
ANISOU 4355  O   ILE A 281     3355   7232   5532   -146   -604    221       O  
ATOM   4356  CB  ILE A 281       3.048  17.201  -8.887  1.00 42.43           C  
ANISOU 4356  CB  ILE A 281     3871   7026   5227    385   -836   1063       C  
ATOM   4357  CG1 ILE A 281       3.401  18.642  -9.266  1.00 44.01           C  
ANISOU 4357  CG1 ILE A 281     4400   6996   5324    644   -867   1404       C  
ATOM   4358  CG2 ILE A 281       3.698  16.219  -9.853  1.00 41.95           C  
ANISOU 4358  CG2 ILE A 281     3770   7115   5055    382   -784   1148       C  
ATOM   4359  CD1 ILE A 281       4.880  18.959  -9.169  1.00 43.13           C  
ANISOU 4359  CD1 ILE A 281     4489   6564   5333    381   -682   1821       C  
ATOM   4371  N   LEU A 282       0.525  14.855  -9.402  1.00 50.57           N  
ANISOU 4371  N   LEU A 282     4038   8810   6364    388   -907   -174       N  
ATOM   4372  CA  LEU A 282       0.071  13.491  -9.136  1.00 49.45           C  
ANISOU 4372  CA  LEU A 282     3619   8756   6412     44   -714   -586       C  
ATOM   4373  C   LEU A 282      -0.746  13.437  -7.846  1.00 49.36           C  
ANISOU 4373  C   LEU A 282     3470   8625   6660   -267   -464   -891       C  
ATOM   4374  O   LEU A 282      -0.544  12.580  -6.983  1.00 48.85           O  
ANISOU 4374  O   LEU A 282     3519   8327   6716   -683   -129   -902       O  
ATOM   4375  CB  LEU A 282       1.251  12.520  -9.076  1.00 46.30           C  
ANISOU 4375  CB  LEU A 282     3449   8161   5981   -241   -531   -277       C  
ATOM   4376  CG  LEU A 282       1.988  12.262 -10.391  1.00 46.22           C  
ANISOU 4376  CG  LEU A 282     3519   8298   5745     12   -678    -73       C  
ATOM   4377  CD1 LEU A 282       3.189  11.350 -10.167  1.00 45.35           C  
ANISOU 4377  CD1 LEU A 282     3609   7983   5638   -256   -489    210       C  
ATOM   4378  CD2 LEU A 282       1.047  11.671 -11.435  1.00 48.21           C  
ANISOU 4378  CD2 LEU A 282     3449   8921   5947    237   -847   -591       C  
ATOM   4390  N   GLY A 283      -1.673  14.384  -7.717  1.00 46.73           N  
ANISOU 4390  N   GLY A 283     2949   8431   6374    -15   -605  -1133       N  
ATOM   4391  CA  GLY A 283      -2.580  14.416  -6.589  1.00 47.36           C  
ANISOU 4391  CA  GLY A 283     2847   8444   6702   -258   -338  -1486       C  
ATOM   4392  C   GLY A 283      -1.971  14.840  -5.275  1.00 48.47           C  
ANISOU 4392  C   GLY A 283     3418   8179   6818   -489   -122  -1094       C  
ATOM   4393  O   GLY A 283      -2.640  14.745  -4.242  1.00 49.04           O  
ANISOU 4393  O   GLY A 283     3443   8142   7050   -719    191  -1348       O  
ATOM   4397  N   SER A 284      -0.730  15.315  -5.273  1.00 48.09           N  
ANISOU 4397  N   SER A 284     3778   7907   6586   -427   -265   -531       N  
ATOM   4398  CA  SER A 284      -0.032  15.669  -4.047  1.00 46.32           C  
ANISOU 4398  CA  SER A 284     3949   7316   6333   -612   -146   -218       C  
ATOM   4399  C   SER A 284       0.350  17.141  -4.069  1.00 47.03           C  
ANISOU 4399  C   SER A 284     4228   7294   6349   -342   -408     75       C  
ATOM   4400  O   SER A 284       0.772  17.670  -5.102  1.00 42.90           O  
ANISOU 4400  O   SER A 284     3728   6842   5728    -87   -626    292       O  
ATOM   4401  CB  SER A 284       1.220  14.804  -3.861  1.00 48.32           C  
ANISOU 4401  CB  SER A 284     4488   7366   6506   -832    -69     96       C  
ATOM   4402  OG  SER A 284       1.954  15.203  -2.717  1.00 49.87           O  
ANISOU 4402  OG  SER A 284     5054   7246   6647   -916    -63    341       O  
ATOM   4408  N   ALA A 285       0.195  17.796  -2.920  1.00 52.07           N  
ANISOU 4408  N   ALA A 285     5056   7713   7017   -395   -342     75       N  
ATOM   4409  CA  ALA A 285       0.629  19.174  -2.740  1.00 51.96           C  
ANISOU 4409  CA  ALA A 285     5283   7492   6967   -209   -546    332       C  
ATOM   4410  C   ALA A 285       2.049  19.275  -2.196  1.00 50.85           C  
ANISOU 4410  C   ALA A 285     5457   7041   6822   -403   -598    682       C  
ATOM   4411  O   ALA A 285       2.555  20.390  -2.031  1.00 54.11           O  
ANISOU 4411  O   ALA A 285     6060   7230   7270   -328   -739    868       O  
ATOM   4412  CB  ALA A 285      -0.336  19.912  -1.808  1.00 51.79           C  
ANISOU 4412  CB  ALA A 285     5280   7411   6986   -116   -484     81       C  
ATOM   4418  N   LEU A 286       2.697  18.147  -1.916  1.00 47.66           N  
ANISOU 4418  N   LEU A 286     5106   6610   6393   -629   -495    728       N  
ATOM   4419  CA  LEU A 286       4.083  18.114  -1.477  1.00 48.12           C  
ANISOU 4419  CA  LEU A 286     5373   6450   6461   -748   -611    968       C  
ATOM   4420  C   LEU A 286       4.914  17.316  -2.474  1.00 45.47           C  
ANISOU 4420  C   LEU A 286     4900   6245   6132   -791   -625   1127       C  
ATOM   4421  O   LEU A 286       4.391  16.506  -3.245  1.00 46.20           O  
ANISOU 4421  O   LEU A 286     4817   6563   6175   -772   -515   1026       O  
ATOM   4422  CB  LEU A 286       4.214  17.488  -0.083  1.00 51.97           C  
ANISOU 4422  CB  LEU A 286     6154   6755   6835   -861   -521    865       C  
ATOM   4423  CG  LEU A 286       3.448  18.163   1.056  1.00 56.43           C  
ANISOU 4423  CG  LEU A 286     6931   7167   7343   -814   -453    698       C  
ATOM   4424  CD1 LEU A 286       3.483  17.289   2.300  1.00 57.61           C  
ANISOU 4424  CD1 LEU A 286     7476   7136   7277   -877   -265    609       C  
ATOM   4425  CD2 LEU A 286       4.015  19.545   1.352  1.00 53.81           C  
ANISOU 4425  CD2 LEU A 286     6698   6644   7103   -727   -731    798       C  
ATOM   4437  N   LEU A 287       6.222  17.550  -2.453  1.00 42.32           N  
ANISOU 4437  N   LEU A 287     4546   5712   5822   -849   -760   1323       N  
ATOM   4438  CA  LEU A 287       7.141  16.783  -3.284  1.00 41.21           C  
ANISOU 4438  CA  LEU A 287     4270   5686   5702   -884   -749   1457       C  
ATOM   4439  C   LEU A 287       7.387  15.420  -2.642  1.00 42.65           C  
ANISOU 4439  C   LEU A 287     4573   5870   5760   -941   -709   1354       C  
ATOM   4440  O   LEU A 287       7.815  15.338  -1.486  1.00 43.75           O  
ANISOU 4440  O   LEU A 287     4940   5831   5851   -945   -813   1296       O  
ATOM   4441  CB  LEU A 287       8.447  17.550  -3.471  1.00 43.42           C  
ANISOU 4441  CB  LEU A 287     4481   5822   6193   -949   -854   1629       C  
ATOM   4442  CG  LEU A 287       8.282  18.917  -4.144  1.00 44.77           C  
ANISOU 4442  CG  LEU A 287     4665   5877   6470   -900   -798   1778       C  
ATOM   4443  CD1 LEU A 287       9.623  19.604  -4.320  1.00 43.41           C  
ANISOU 4443  CD1 LEU A 287     4405   5502   6587  -1065   -778   1904       C  
ATOM   4444  CD2 LEU A 287       7.575  18.783  -5.484  1.00 45.19           C  
ANISOU 4444  CD2 LEU A 287     4683   6141   6348   -700   -668   1873       C  
ATOM   4456  N   GLU A 288       7.117  14.356  -3.395  1.00 42.86           N  
ANISOU 4456  N   GLU A 288     4509   6072   5703   -941   -567   1318       N  
ATOM   4457  CA  GLU A 288       7.195  12.990  -2.893  1.00 41.38           C  
ANISOU 4457  CA  GLU A 288     4521   5828   5373   -984   -449   1222       C  
ATOM   4458  C   GLU A 288       8.574  12.396  -3.149  1.00 37.38           C  
ANISOU 4458  C   GLU A 288     4000   5333   4871   -917   -583   1351       C  
ATOM   4459  O   GLU A 288       9.124  12.528  -4.246  1.00 39.58           O  
ANISOU 4459  O   GLU A 288     4014   5773   5250   -890   -612   1472       O  
ATOM   4460  CB  GLU A 288       6.125  12.132  -3.570  1.00 43.71           C  
ANISOU 4460  CB  GLU A 288     4704   6277   5627  -1049   -204   1036       C  
ATOM   4461  CG  GLU A 288       6.083  10.684  -3.122  1.00 49.41           C  
ANISOU 4461  CG  GLU A 288     5697   6857   6220  -1139     27    926       C  
ATOM   4462  CD  GLU A 288       5.511  10.527  -1.734  1.00 50.88           C  
ANISOU 4462  CD  GLU A 288     6277   6762   6294  -1222    248    811       C  
ATOM   4463  OE1 GLU A 288       4.349  10.938  -1.520  1.00 52.72           O  
ANISOU 4463  OE1 GLU A 288     6398   7020   6611  -1332    438    610       O  
ATOM   4464  OE2 GLU A 288       6.226  10.001  -0.856  1.00 51.53           O  
ANISOU 4464  OE2 GLU A 288     6800   6599   6180  -1130    234    904       O  
ATOM   4471  N   ASP A 289       9.127  11.722  -2.131  1.00 36.21           N  
ANISOU 4471  N   ASP A 289     4170   5008   4580   -841   -652   1309       N  
ATOM   4472  CA  ASP A 289      10.457  11.133  -2.255  1.00 37.24           C  
ANISOU 4472  CA  ASP A 289     4268   5170   4713   -698   -837   1359       C  
ATOM   4473  C   ASP A 289      10.489   9.659  -1.861  1.00 39.73           C  
ANISOU 4473  C   ASP A 289     4984   5357   4754   -574   -721   1303       C  
ATOM   4474  O   ASP A 289      11.569   9.123  -1.592  1.00 38.43           O  
ANISOU 4474  O   ASP A 289     4921   5168   4512   -347   -933   1297       O  
ATOM   4475  CB  ASP A 289      11.487  11.927  -1.436  1.00 36.49           C  
ANISOU 4475  CB  ASP A 289     4137   4994   4732   -595  -1186   1317       C  
ATOM   4476  CG  ASP A 289      11.328  11.758   0.069  1.00 39.38           C  
ANISOU 4476  CG  ASP A 289     5012   5121   4829   -430  -1307   1194       C  
ATOM   4477  OD1 ASP A 289      10.322  11.180   0.529  1.00 39.37           O  
ANISOU 4477  OD1 ASP A 289     5415   4970   4573   -454  -1025   1181       O  
ATOM   4478  OD2 ASP A 289      12.233  12.218   0.799  1.00 40.92           O  
ANISOU 4478  OD2 ASP A 289     5205   5269   5072   -269  -1671   1077       O  
ATOM   4483  N   GLU A 290       9.340   8.980  -1.849  1.00 40.78           N  
ANISOU 4483  N   GLU A 290     5343   5394   4760   -709   -370   1227       N  
ATOM   4484  CA  GLU A 290       9.291   7.557  -1.529  1.00 42.23           C  
ANISOU 4484  CA  GLU A 290     5990   5361   4695   -641   -146   1180       C  
ATOM   4485  C   GLU A 290       9.116   6.681  -2.768  1.00 35.63           C  
ANISOU 4485  C   GLU A 290     4937   4671   3931   -737     36   1139       C  
ATOM   4486  O   GLU A 290       8.596   5.566  -2.667  1.00 37.07           O  
ANISOU 4486  O   GLU A 290     5458   4642   3985   -819    366   1035       O  
ATOM   4487  CB  GLU A 290       8.179   7.276  -0.519  1.00 42.02           C  
ANISOU 4487  CB  GLU A 290     6447   5023   4495   -772    235   1072       C  
ATOM   4488  CG  GLU A 290       8.507   7.742   0.888  1.00 42.02           C  
ANISOU 4488  CG  GLU A 290     6914   4792   4261   -554     73   1109       C  
ATOM   4489  CD  GLU A 290       7.696   7.018   1.945  1.00 45.61           C  
ANISOU 4489  CD  GLU A 290     8096   4830   4404   -587    552   1052       C  
ATOM   4490  OE1 GLU A 290       6.494   6.762   1.709  1.00 44.22           O  
ANISOU 4490  OE1 GLU A 290     7839   4599   4363   -932   1047    913       O  
ATOM   4491  OE2 GLU A 290       8.265   6.695   3.008  1.00 45.22           O  
ANISOU 4491  OE2 GLU A 290     8712   4500   3972   -247    451   1114       O  
ATOM   4498  N   PHE A 291       9.545   7.162  -3.934  1.00 34.13           N  
ANISOU 4498  N   PHE A 291     4238   4800   3930   -727   -136   1208       N  
ATOM   4499  CA  PHE A 291       9.616   6.348  -5.141  1.00 34.15           C  
ANISOU 4499  CA  PHE A 291     4064   4964   3946   -723    -38   1173       C  
ATOM   4500  C   PHE A 291      11.034   6.427  -5.685  1.00 34.02           C  
ANISOU 4500  C   PHE A 291     3829   5118   3981   -505   -284   1323       C  
ATOM   4501  O   PHE A 291      11.509   7.515  -6.025  1.00 33.46           O  
ANISOU 4501  O   PHE A 291     3416   5213   4087   -505   -436   1434       O  
ATOM   4502  CB  PHE A 291       8.620   6.823  -6.202  1.00 33.12           C  
ANISOU 4502  CB  PHE A 291     3550   5087   3948   -870     49   1066       C  
ATOM   4503  CG  PHE A 291       7.183   6.688  -5.798  1.00 34.17           C  
ANISOU 4503  CG  PHE A 291     3746   5122   4118  -1096    305    805       C  
ATOM   4504  CD1 PHE A 291       6.539   7.714  -5.131  1.00 41.26           C  
ANISOU 4504  CD1 PHE A 291     4595   5994   5089  -1169    292    779       C  
ATOM   4505  CD2 PHE A 291       6.471   5.542  -6.103  1.00 39.44           C  
ANISOU 4505  CD2 PHE A 291     4481   5715   4788  -1252    588    535       C  
ATOM   4506  CE1 PHE A 291       5.214   7.596  -4.766  1.00 39.53           C  
ANISOU 4506  CE1 PHE A 291     4359   5713   4950  -1380    570    484       C  
ATOM   4507  CE2 PHE A 291       5.146   5.417  -5.741  1.00 40.80           C  
ANISOU 4507  CE2 PHE A 291     4614   5802   5085  -1516    885    212       C  
ATOM   4508  CZ  PHE A 291       4.517   6.446  -5.072  1.00 40.69           C  
ANISOU 4508  CZ  PHE A 291     4513   5800   5149  -1572    883    183       C  
ATOM   4519  N   THR A 292      11.706   5.284  -5.768  1.00 35.26           N  
ANISOU 4519  N   THR A 292     4188   5207   4004   -325   -279   1306       N  
ATOM   4520  CA  THR A 292      13.001   5.234  -6.422  1.00 35.90           C  
ANISOU 4520  CA  THR A 292     3981   5491   4167   -116   -456   1382       C  
ATOM   4521  C   THR A 292      12.824   5.264  -7.934  1.00 36.49           C  
ANISOU 4521  C   THR A 292     3716   5836   4313   -182   -313   1415       C  
ATOM   4522  O   THR A 292      11.732   5.009  -8.447  1.00 34.50           O  
ANISOU 4522  O   THR A 292     3502   5605   4001   -323   -140   1315       O  
ATOM   4523  CB  THR A 292      13.755   3.970  -6.029  1.00 38.49           C  
ANISOU 4523  CB  THR A 292     4666   5665   4295    183   -520   1326       C  
ATOM   4524  OG1 THR A 292      13.091   2.828  -6.585  1.00 41.73           O  
ANISOU 4524  OG1 THR A 292     5332   5968   4557    121   -240   1248       O  
ATOM   4525  CG2 THR A 292      13.827   3.832  -4.521  1.00 39.66           C  
ANISOU 4525  CG2 THR A 292     5321   5505   4243    350   -655   1291       C  
ATOM   4533  N   PRO A 293      13.889   5.571  -8.678  1.00 37.47           N  
ANISOU 4533  N   PRO A 293     3502   6173   4564    -61   -372   1511       N  
ATOM   4534  CA  PRO A 293      13.791   5.463 -10.140  1.00 35.92           C  
ANISOU 4534  CA  PRO A 293     3110   6206   4333    -37   -203   1556       C  
ATOM   4535  C   PRO A 293      13.354   4.082 -10.594  1.00 41.59           C  
ANISOU 4535  C   PRO A 293     4068   6892   4842     40    -96   1401       C  
ATOM   4536  O   PRO A 293      12.625   3.964 -11.588  1.00 41.14           O  
ANISOU 4536  O   PRO A 293     3958   6977   4698     12     11   1328       O  
ATOM   4537  CB  PRO A 293      15.210   5.808 -10.614  1.00 38.63           C  
ANISOU 4537  CB  PRO A 293     3116   6709   4852     88   -205   1659       C  
ATOM   4538  CG  PRO A 293      15.783   6.648  -9.512  1.00 38.21           C  
ANISOU 4538  CG  PRO A 293     2934   6553   5032     21   -398   1653       C  
ATOM   4539  CD  PRO A 293      15.204   6.079  -8.244  1.00 39.22           C  
ANISOU 4539  CD  PRO A 293     3476   6441   4986     55   -567   1537       C  
ATOM   4547  N   PHE A 294      13.757   3.032  -9.875  1.00 37.36           N  
ANISOU 4547  N   PHE A 294     3840   6148   4207    168   -136   1319       N  
ATOM   4548  CA  PHE A 294      13.344   1.681 -10.237  1.00 44.30           C  
ANISOU 4548  CA  PHE A 294     5021   6902   4909    210     16   1156       C  
ATOM   4549  C   PHE A 294      11.853   1.476  -9.997  1.00 41.48           C  
ANISOU 4549  C   PHE A 294     4858   6370   4534    -88    198    968       C  
ATOM   4550  O   PHE A 294      11.178   0.815 -10.795  1.00 41.23           O  
ANISOU 4550  O   PHE A 294     4824   6375   4467   -169    337    758       O  
ATOM   4551  CB  PHE A 294      14.162   0.657  -9.451  1.00 55.31           C  
ANISOU 4551  CB  PHE A 294     6809   8044   6163    479    -52   1135       C  
ATOM   4552  CG  PHE A 294      15.648   0.837  -9.588  1.00 65.50           C  
ANISOU 4552  CG  PHE A 294     7810   9544   7533    800   -268   1213       C  
ATOM   4553  CD1 PHE A 294      16.307   0.428 -10.736  1.00 69.22           C  
ANISOU 4553  CD1 PHE A 294     8038  10253   8011    972   -204   1200       C  
ATOM   4554  CD2 PHE A 294      16.387   1.418  -8.569  1.00 68.32           C  
ANISOU 4554  CD2 PHE A 294     8103   9876   7980    937   -531   1238       C  
ATOM   4555  CE1 PHE A 294      17.674   0.595 -10.867  1.00 70.61           C  
ANISOU 4555  CE1 PHE A 294     7862  10639   8326   1240   -342   1210       C  
ATOM   4556  CE2 PHE A 294      17.755   1.586  -8.693  1.00 70.46           C  
ANISOU 4556  CE2 PHE A 294     7988  10373   8412   1211   -734   1197       C  
ATOM   4557  CZ  PHE A 294      18.399   1.174  -9.843  1.00 71.03           C  
ANISOU 4557  CZ  PHE A 294     7770  10684   8536   1344   -611   1181       C  
ATOM   4567  N   ASP A 295      11.319   2.031  -8.906  1.00 37.27           N  
ANISOU 4567  N   ASP A 295     4459   5653   4049   -254    207    984       N  
ATOM   4568  CA  ASP A 295       9.888   1.914  -8.645  1.00 37.52           C  
ANISOU 4568  CA  ASP A 295     4585   5538   4131   -567    438    755       C  
ATOM   4569  C   ASP A 295       9.081   2.530  -9.781  1.00 39.13           C  
ANISOU 4569  C   ASP A 295     4329   6094   4445   -659    397    609       C  
ATOM   4570  O   ASP A 295       8.126   1.925 -10.282  1.00 40.09           O  
ANISOU 4570  O   ASP A 295     4394   6228   4612   -815    545    279       O  
ATOM   4571  CB  ASP A 295       9.531   2.583  -7.317  1.00 37.13           C  
ANISOU 4571  CB  ASP A 295     4728   5278   4102   -685    461    820       C  
ATOM   4572  CG  ASP A 295      10.169   1.896  -6.123  1.00 39.10           C  
ANISOU 4572  CG  ASP A 295     5573   5140   4143   -513    495    918       C  
ATOM   4573  OD1 ASP A 295      10.463   0.686  -6.215  1.00 40.90           O  
ANISOU 4573  OD1 ASP A 295     6167   5153   4222   -398    632    867       O  
ATOM   4574  OD2 ASP A 295      10.368   2.570  -5.090  1.00 38.68           O  
ANISOU 4574  OD2 ASP A 295     5671   4983   4041   -445    368   1029       O  
ATOM   4580  N   VAL A 296       9.459   3.738 -10.205  1.00 43.72           N  
ANISOU 4580  N   VAL A 296     4601   6944   5066   -538    195    818       N  
ATOM   4581  CA  VAL A 296       8.745   4.412 -11.285  1.00 41.00           C  
ANISOU 4581  CA  VAL A 296     3938   6912   4728   -495    121    718       C  
ATOM   4582  C   VAL A 296       8.764   3.554 -12.544  1.00 43.94           C  
ANISOU 4582  C   VAL A 296     4258   7464   4972   -346    134    548       C  
ATOM   4583  O   VAL A 296       7.724   3.306 -13.165  1.00 41.41           O  
ANISOU 4583  O   VAL A 296     3801   7284   4648   -377    119    195       O  
ATOM   4584  CB  VAL A 296       9.353   5.804 -11.536  1.00 37.92           C  
ANISOU 4584  CB  VAL A 296     3377   6673   4357   -356    -15   1040       C  
ATOM   4585  CG1 VAL A 296       8.735   6.452 -12.768  1.00 40.87           C  
ANISOU 4585  CG1 VAL A 296     3577   7334   4619   -175    -88    989       C  
ATOM   4586  CG2 VAL A 296       9.159   6.684 -10.314  1.00 40.31           C  
ANISOU 4586  CG2 VAL A 296     3724   6798   4793   -507    -57   1127       C  
ATOM   4596  N   VAL A 297       9.951   3.087 -12.937  1.00 49.20           N  
ANISOU 4596  N   VAL A 297     5004   8148   5543   -157    140    740       N  
ATOM   4597  CA  VAL A 297      10.063   2.223 -14.109  1.00 52.55           C  
ANISOU 4597  CA  VAL A 297     5429   8724   5812     19    164    583       C  
ATOM   4598  C   VAL A 297       9.216   0.972 -13.926  1.00 54.47           C  
ANISOU 4598  C   VAL A 297     5835   8768   6093   -176    285    171       C  
ATOM   4599  O   VAL A 297       8.507   0.538 -14.843  1.00 55.27           O  
ANISOU 4599  O   VAL A 297     5823   9030   6146   -146    253   -176       O  
ATOM   4600  CB  VAL A 297      11.538   1.864 -14.370  1.00 52.92           C  
ANISOU 4600  CB  VAL A 297     5532   8789   5788    247    196    835       C  
ATOM   4601  CG1 VAL A 297      11.636   0.744 -15.395  1.00 55.17           C  
ANISOU 4601  CG1 VAL A 297     5905   9158   5898    425    249    635       C  
ATOM   4602  CG2 VAL A 297      12.315   3.086 -14.833  1.00 51.59           C  
ANISOU 4602  CG2 VAL A 297     5143   8823   5635    385    185   1163       C  
ATOM   4612  N   ARG A 298       9.280   0.370 -12.738  1.00 47.68           N  
ANISOU 4612  N   ARG A 298     5278   7525   5313   -366    445    174       N  
ATOM   4613  CA  ARG A 298       8.525  -0.850 -12.479  1.00 50.49           C  
ANISOU 4613  CA  ARG A 298     5883   7569   5730   -610    693   -197       C  
ATOM   4614  C   ARG A 298       7.031  -0.614 -12.657  1.00 47.48           C  
ANISOU 4614  C   ARG A 298     5205   7288   5547   -897    750   -637       C  
ATOM   4615  O   ARG A 298       6.334  -1.416 -13.289  1.00 49.04           O  
ANISOU 4615  O   ARG A 298     5315   7491   5827  -1022    835  -1094       O  
ATOM   4616  CB  ARG A 298       8.828  -1.362 -11.068  1.00 58.53           C  
ANISOU 4616  CB  ARG A 298     7408   8099   6731   -714    908    -51       C  
ATOM   4617  CG  ARG A 298       8.772  -2.879 -10.939  1.00 68.89           C  
ANISOU 4617  CG  ARG A 298     9204   8984   7988   -793   1210   -261       C  
ATOM   4618  CD  ARG A 298       9.008  -3.362  -9.507  1.00 74.90           C  
ANISOU 4618  CD  ARG A 298    10627   9199   8633   -815   1456    -91       C  
ATOM   4619  NE  ARG A 298      10.285  -2.901  -8.960  1.00 76.74           N  
ANISOU 4619  NE  ARG A 298    10985   9498   8674   -406   1153    309       N  
ATOM   4620  CZ  ARG A 298      10.420  -2.027  -7.963  1.00 74.43           C  
ANISOU 4620  CZ  ARG A 298    10738   9180   8362   -375   1039    513       C  
ATOM   4621  NH1 ARG A 298       9.357  -1.501  -7.364  1.00 73.20           N  
ANISOU 4621  NH1 ARG A 298    10558   8921   8332   -717   1237    413       N  
ATOM   4622  NH2 ARG A 298      11.634  -1.685  -7.554  1.00 73.98           N  
ANISOU 4622  NH2 ARG A 298    10719   9214   8177     12    715    766       N  
ATOM   4636  N   GLN A 299       6.520   0.493 -12.114  1.00 49.32           N  
ANISOU 4636  N   GLN A 299     5241   7616   5884   -989    684   -564       N  
ATOM   4637  CA  GLN A 299       5.085   0.745 -12.161  1.00 50.96           C  
ANISOU 4637  CA  GLN A 299     5113   7933   6315  -1232    733  -1036       C  
ATOM   4638  C   GLN A 299       4.634   1.231 -13.532  1.00 53.13           C  
ANISOU 4638  C   GLN A 299     4959   8705   6523   -959    390  -1284       C  
ATOM   4639  O   GLN A 299       3.493   0.972 -13.928  1.00 56.21           O  
ANISOU 4639  O   GLN A 299     5026   9237   7093  -1087    371  -1870       O  
ATOM   4640  CB  GLN A 299       4.686   1.762 -11.086  1.00 49.16           C  
ANISOU 4640  CB  GLN A 299     4851   7631   6195  -1367    779   -888       C  
ATOM   4641  CG  GLN A 299       3.171   1.862 -10.882  1.00 50.19           C  
ANISOU 4641  CG  GLN A 299     4641   7809   6620  -1670    933  -1440       C  
ATOM   4642  CD  GLN A 299       2.750   2.781  -9.738  1.00 46.17           C  
ANISOU 4642  CD  GLN A 299     4144   7188   6209  -1804   1041  -1316       C  
ATOM   4643  OE1 GLN A 299       1.630   3.289  -9.732  1.00 47.68           O  
ANISOU 4643  OE1 GLN A 299     3936   7565   6614  -1908   1039  -1705       O  
ATOM   4644  NE2 GLN A 299       3.632   2.984  -8.763  1.00 45.06           N  
ANISOU 4644  NE2 GLN A 299     4448   6761   5911  -1765   1110   -830       N  
ATOM   4653  N   CYS A 300       5.503   1.919 -14.269  1.00 63.05           N  
ANISOU 4653  N   CYS A 300     6221  10217   7518   -563    137   -890       N  
ATOM   4654  CA  CYS A 300       5.158   2.433 -15.587  1.00 66.25           C  
ANISOU 4654  CA  CYS A 300     6386  11053   7734   -191   -172  -1051       C  
ATOM   4655  C   CYS A 300       5.498   1.459 -16.713  1.00 70.94           C  
ANISOU 4655  C   CYS A 300     7050  11766   8136     18   -228  -1240       C  
ATOM   4656  O   CYS A 300       5.346   1.814 -17.886  1.00 71.69           O  
ANISOU 4656  O   CYS A 300     7056  12212   7972    421   -489  -1345       O  
ATOM   4657  CB  CYS A 300       5.855   3.777 -15.823  1.00 61.55           C  
ANISOU 4657  CB  CYS A 300     5849  10603   6932    124   -311   -514       C  
ATOM   4658  SG  CYS A 300       5.263   5.108 -14.741  1.00 62.31           S  
ANISOU 4658  SG  CYS A 300     5836  10624   7214    -23   -336   -384       S  
ATOM   4664  N   SER A 301       5.946   0.242 -16.385  1.00 67.72           N  
ANISOU 4664  N   SER A 301     6870  11054   7805   -194     11  -1290       N  
ATOM   4665  CA  SER A 301       6.185  -0.795 -17.381  1.00 72.80           C  
ANISOU 4665  CA  SER A 301     7600  11764   8298    -27    -20  -1542       C  
ATOM   4666  C   SER A 301       5.372  -2.062 -17.151  1.00 78.21           C  
ANISOU 4666  C   SER A 301     8280  12181   9254   -412    177  -2149       C  
ATOM   4667  O   SER A 301       5.137  -2.801 -18.114  1.00 78.06           O  
ANISOU 4667  O   SER A 301     8202  12290   9166   -292     68  -2578       O  
ATOM   4668  CB  SER A 301       7.676  -1.172 -17.427  1.00 76.36           C  
ANISOU 4668  CB  SER A 301     8377  12084   8553    167     99  -1046       C  
ATOM   4669  OG  SER A 301       7.906  -2.453 -16.864  1.00 80.43           O  
ANISOU 4669  OG  SER A 301     9186  12195   9179    -57    347  -1171       O  
ATOM   4675  N   GLY A 302       4.939  -2.333 -15.921  1.00 87.43           N  
ANISOU 4675  N   GLY A 302     9546  12951  10722   -870    503  -2216       N  
ATOM   4676  CA  GLY A 302       4.078  -3.469 -15.648  1.00 92.80           C  
ANISOU 4676  CA  GLY A 302    10241  13297  11721  -1322    822  -2816       C  
ATOM   4677  C   GLY A 302       4.832  -4.754 -15.377  1.00 93.88           C  
ANISOU 4677  C   GLY A 302    10937  12941  11791  -1410   1145  -2694       C  
ATOM   4678  O   GLY A 302       4.646  -5.751 -16.082  1.00 97.04           O  
ANISOU 4678  O   GLY A 302    11368  13267  12236  -1455   1190  -3133       O  
ATOM   4682  N   VAL A 303       5.681  -4.745 -14.352  1.00 82.05           N  
ANISOU 4682  N   VAL A 303     9907  11097  10171  -1388   1341  -2136       N  
ATOM   4683  CA  VAL A 303       6.483  -5.907 -13.983  1.00 83.17           C  
ANISOU 4683  CA  VAL A 303    10675  10747  10179  -1349   1611  -1965       C  
ATOM   4684  C   VAL A 303       5.687  -6.782 -13.026  1.00 87.01           C  
ANISOU 4684  C   VAL A 303    11548  10590  10921  -1870   2181  -2269       C  
ATOM   4685  O   VAL A 303       4.992  -6.283 -12.133  1.00 85.08           O  
ANISOU 4685  O   VAL A 303    11253  10210  10865  -2186   2408  -2294       O  
ATOM   4686  CB  VAL A 303       7.821  -5.467 -13.356  1.00 80.19           C  
ANISOU 4686  CB  VAL A 303    10610  10340   9519   -973   1479  -1284       C  
ATOM   4687  CG1 VAL A 303       8.422  -6.588 -12.515  1.00 83.26           C  
ANISOU 4687  CG1 VAL A 303    11750  10110   9774   -936   1796  -1131       C  
ATOM   4688  CG2 VAL A 303       8.796  -5.036 -14.440  1.00 76.38           C  
ANISOU 4688  CG2 VAL A 303     9863  10349   8808   -494   1095  -1044       C  
ATOM   4698  N   THR A 304       5.795  -8.095 -13.209  1.00 95.04           N  
ANISOU 4698  N   THR A 304    13001  11171  11941  -1962   2471  -2499       N  
ATOM   4699  CA  THR A 304       5.128  -9.083 -12.372  1.00 99.20           C  
ANISOU 4699  CA  THR A 304    14042  10956  12691  -2469   3142  -2779       C  
ATOM   4700  C   THR A 304       6.172  -9.928 -11.644  1.00 98.30           C  
ANISOU 4700  C   THR A 304    14889  10240  12222  -2190   3385  -2313       C  
ATOM   4701  O   THR A 304       7.379  -9.785 -11.854  1.00 98.48           O  
ANISOU 4701  O   THR A 304    15047  10484  11888  -1617   2990  -1869       O  
ATOM   4702  CB  THR A 304       4.202  -9.973 -13.207  1.00104.56           C  
ANISOU 4702  CB  THR A 304    14455  11535  13737  -2873   3345  -3573       C  
ATOM   4703  OG1 THR A 304       4.975 -10.718 -14.157  1.00105.34           O  
ANISOU 4703  OG1 THR A 304    14739  11687  13600  -2502   3108  -3586       O  
ATOM   4704  CG2 THR A 304       3.176  -9.132 -13.944  1.00104.70           C  
ANISOU 4704  CG2 THR A 304    13505  12207  14068  -3023   2999  -4107       C  
ATOM   4712  N   PHE A 305       5.690 -10.820 -10.781  1.00 97.38           N  
ANISOU 4712  N   PHE A 305    15457   9337  12206  -2578   4070  -2447       N  
ATOM   4713  CA  PHE A 305       6.565 -11.699 -10.011  1.00 94.46           C  
ANISOU 4713  CA  PHE A 305    16158   8291  11442  -2261   4348  -2038       C  
ATOM   4714  C   PHE A 305       6.038 -13.131 -10.011  1.00 97.40           C  
ANISOU 4714  C   PHE A 305    17169   7857  11983  -2670   5046  -2451       C  
ATOM   4715  O   PHE A 305       4.851 -13.368  -9.785  1.00100.79           O  
ANISOU 4715  O   PHE A 305    17343   8148  12805  -3281   5535  -2816       O  
ATOM   4716  CB  PHE A 305       6.705 -11.189  -8.573  1.00 91.80           C  
ANISOU 4716  CB  PHE A 305    16356   7651  10873  -2174   4545  -1573       C  
ATOM   4717  CG  PHE A 305       7.161  -9.760  -8.481  1.00 87.84           C  
ANISOU 4717  CG  PHE A 305    15243   7863  10267  -1849   3917  -1221       C  
ATOM   4718  CD1 PHE A 305       8.445  -9.402  -8.857  1.00 87.91           C  
ANISOU 4718  CD1 PHE A 305    15118   8310   9973  -1205   3290   -849       C  
ATOM   4719  CD2 PHE A 305       6.304  -8.774  -8.018  1.00 85.99           C  
ANISOU 4719  CD2 PHE A 305    14559   7838  10275  -2205   3993  -1299       C  
ATOM   4720  CE1 PHE A 305       8.867  -8.087  -8.776  1.00 85.34           C  
ANISOU 4720  CE1 PHE A 305    14239   8574   9612   -975   2787   -564       C  
ATOM   4721  CE2 PHE A 305       6.721  -7.458  -7.935  1.00 83.72           C  
ANISOU 4721  CE2 PHE A 305    13767   8142   9902  -1920   3445   -986       C  
ATOM   4722  CZ  PHE A 305       8.003  -7.115  -8.314  1.00 83.67           C  
ANISOU 4722  CZ  PHE A 305    13651   8521   9618  -1330   2859   -620       C  
TER    4665      PHE A 305                                                      
HETATM 4732  O   DMS B 801       5.885  -0.689  -7.451  1.00 80.97           O  
HETATM 4733  C1  DMS B 801       6.658  -1.607  -5.025  1.00 78.83           C  
HETATM 4734  C2  DMS B 801       5.237  -3.231  -6.760  1.00 78.09           C  
HETATM 4735  S   DMS B 801       6.471  -1.901  -6.804  1.00 80.61           S  
HETATM 4742  O   DMS B 901       7.055   0.131  17.424  1.00 91.29           O  
HETATM 4743  C1  DMS B 901       7.136  -0.367  20.080  1.00 92.58           C  
HETATM 4744  C2  DMS B 901       5.089   1.159  18.982  1.00 91.13           C  
HETATM 4745  S   DMS B 901       6.157  -0.246  18.557  1.00 92.59           S  
TER    4686      DMS B 901                                                      
HETATM 4752  O   HOH C   1      15.967  -6.244  20.118  1.00 32.07           O  
HETATM 4753  O   HOH C   2      10.890  -0.942  -3.585  1.00 45.10           O  
HETATM 4754  O   HOH C   4       8.001   3.089  -3.712  1.00 39.99           O  
HETATM 4755  O   HOH C   5       4.120 -12.480  -2.471  1.00 39.49           O  
HETATM 4756  O   HOH C   6      16.950   5.936  -4.247  1.00 38.00           O  
HETATM 4757  O   HOH C   7      16.896   2.011  12.028  1.00 36.35           O  
HETATM 4758  O   HOH C   8       6.157  -9.083   8.794  1.00 60.73           O  
HETATM 4759  O   HOH C   9      13.135  10.700  10.559  1.00 48.62           O  
HETATM 4760  O   HOH C  10       2.621   3.839   2.318  1.00 52.77           O  
HETATM 4761  O   HOH C  11      23.543  -3.034  15.737  1.00 39.11           O  
HETATM 4762  O   HOH C  12      -0.000  16.214   0.000  1.00 47.89           O  
HETATM 4763  O   HOH C  13      19.428  12.018  -3.897  1.00 40.97           O  
HETATM 4764  O   HOH C  14       5.607   2.009  -5.020  1.00 37.03           O  
HETATM 4765  O   HOH C  15      22.347   6.491 -18.043  1.00 39.96           O  
HETATM 4766  O   HOH C  16       6.092   1.809  -7.827  1.00 39.34           O  
HETATM 4767  O   HOH C  18      19.946  13.170 -19.357  1.00 52.61           O  
HETATM 4768  O   HOH C  19       5.043 -18.289   1.877  1.00 51.64           O  
HETATM 4769  O   HOH C  20      13.646   0.342  -5.648  1.00 50.19           O  
HETATM 4770  O   HOH C  21       1.918  11.291  -5.608  1.00 54.04           O  
HETATM 4771  O   HOH C  22      -0.230  19.739 -16.097  1.00 55.43           O  
HETATM 4772  O   HOH C  23      11.597 -17.766  30.645  1.00 52.66           O  
HETATM 4773  O   HOH C  24      14.702  -0.231  -3.294  1.00 49.00           O  
HETATM 4774  O   HOH C  25       7.387  11.555   0.914  1.00 53.19           O  
HETATM 4775  O   HOH C  27       9.802   6.102   5.663  1.00 33.48           O  
HETATM 4776  O   HOH C  28      -1.100   6.264  -3.173  1.00 41.32           O  
HETATM 4777  O   HOH C  29      21.412 -19.162  26.662  1.00 49.81           O  
HETATM 4778  O   HOH C  30      15.671 -26.670  27.105  1.00 51.40           O  
HETATM 4779  O   HOH C  31      18.896  -8.201   5.906  1.00 54.55           O  
HETATM 4780  O   HOH C  32       9.840   0.725  21.310  1.00 43.48           O  
HETATM 4781  O   HOH C  34       9.615   9.849  -4.828  1.00 29.84           O  
HETATM 4782  O   HOH C  35      14.798  18.504 -21.983  1.00 60.38           O  
HETATM 4783  O   HOH C  36      17.251 -19.467   7.957  1.00 66.77           O  
HETATM 4784  O   HOH C  38      22.126  -8.418   5.785  1.00 55.64           O  
HETATM 4785  O   HOH C  40      23.378  -1.265  17.542  1.00 53.03           O  
HETATM 4786  O   HOH C  41      23.991   1.139  15.959  1.00 68.14           O  
HETATM 4787  O   HOH C  42      23.906   2.320   9.413  1.00 57.03           O  
HETATM 4788  O   HOH C  43      22.325   6.473  -0.173  1.00 56.01           O  
HETATM 4789  O   HOH C  44      20.300  10.339  -2.062  1.00 47.51           O  
HETATM 4790  O   HOH C  45      -1.422  12.821  -2.419  1.00 56.42           O  
HETATM 4791  O   HOH C  46      28.040  -7.880  11.917  1.00 55.73           O  
HETATM 4792  O   HOH C  47      21.639 -23.722  21.550  1.00 50.16           O  
HETATM 4793  O   HOH C  48      19.126 -24.917  26.028  1.00 51.04           O  
HETATM 4794  O   HOH C  49      -2.082  -2.307  12.798  1.00 57.49           O  
HETATM 4795  O   HOH C  50       6.733  -5.064  22.063  1.00 57.55           O  
HETATM 4796  O   HOH C  51      11.446   0.221  24.177  1.00 59.06           O  
HETATM 4797  O   HOH C  52       8.596   4.309  22.481  1.00 52.24           O  
HETATM 4798  O   HOH C  53      24.870  -0.788  13.066  1.00 52.63           O  
HETATM 4799  O   HOH C  55      20.330   9.166  12.245  1.00 51.64           O  
HETATM 4800  O   HOH C  56      23.806  25.783   0.115  1.00 53.35           O  
HETATM 4801  O   HOH C  57       9.252   8.329   4.112  1.00 44.02           O  
HETATM 4802  O   HOH C  58       4.307  -9.148  24.586  1.00 79.07           O  
HETATM 4803  O   HOH C  61       6.445  27.194  -9.627  1.00 52.17           O  
HETATM 4804  O   HOH C  62       0.309  -1.436  12.362  1.00 66.03           O  
HETATM 4805  O   HOH C  63      21.173  16.320 -18.175  1.00 52.75           O  
HETATM 4806  O   HOH C  65      10.010  13.473   3.133  1.00 54.06           O  
TER    4742      HOH C  65                                                      
END


A second structure was input as follows:


REMARK Date 2021-05-20 Time 11:16:33 CEST +0200 (1621502193.34 s)               
REMARK PHENIX refinement                                                        
REMARK                                                                          
REMARK ****************** INPUT FILES AND LABELS ****************************** 
REMARK Reflections:                                                             
REMARK   file name      : /gpfs/cfel/cxi/scratch/user/lieskej/HP/Beamtimes/HP6_2
REMARK   labels         : ['I-obs,SIGI-obs']                                    
REMARK R-free flags:                                                            
REMARK   file name      : /gpfs/cfel/cxi/scratch/user/lieskej/HP/Beamtimes/HP6_2
REMARK   label          : R-free-flags                                          
REMARK   test_flag_value: 1                                                     
REMARK Model file name(s):                                                      
REMARK   /gpfs/cfel/cxi/scratch/user/lieskej/HP/Beamtimes/HP6_20210422/Refine/Mp
REMARK                                                                          
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS ******************* 
REMARK Start: r_work = 0.1816 r_free = 0.2139 bonds = 0.003 angles = 0.589      
REMARK Final: r_work = 0.1742 r_free = 0.2187 bonds = 0.003 angles = 0.556      
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 c: refinement of occupancies                                         
REMARK ------------------------------------------------------------------------ 
REMARK  stage       r-work r-free bonds angles b_min b_max b_ave n_water shift  
REMARK       0    : 0.3835 0.4850 0.003  0.59  24.0 129.9  54.0  30      0.000  
REMARK       1_bss: 0.1816 0.2139 0.003  0.59  23.8 129.8  53.8  30      0.000  
REMARK   1 ttarget: 0.1816 0.2139 0.003  0.59  23.8 129.8  53.8  30      0.000  
REMARK       1_nqh: 0.1816 0.2139 0.003  0.59  23.8 129.8  53.8  30      0.000  
REMARK    1_weight: 0.1816 0.2139 0.003  0.59  23.8 129.8  53.8  30      0.000  
REMARK    1_xyzrec: 0.1820 0.2159 0.003  0.53  23.8 129.8  53.8  30      0.018  
REMARK       1_adp: 0.1794 0.2198 0.003  0.53  23.9 129.1  57.4  30      0.018  
REMARK   1 regHadp: 0.1795 0.2201 0.003  0.53  23.9 129.1  57.4  30      0.018  
REMARK       1_occ: 0.1795 0.2202 0.003  0.53  23.9 129.1  57.4  30      0.018  
REMARK       2_bss: 0.1794 0.2229 0.003  0.53  23.4 128.6  56.9  30      0.018  
REMARK   2 ttarget: 0.1794 0.2229 0.003  0.53  23.4 128.6  56.9  30      0.018  
REMARK   2 datecdl: 0.1794 0.2229 0.003  0.54  23.4 128.6  56.9  30      0.018  
REMARK       2_nqh: 0.1794 0.2229 0.003  0.54  23.4 128.6  56.9  30      0.018  
REMARK    2_weight: 0.1794 0.2229 0.003  0.54  23.4 128.6  56.9  30      0.018  
REMARK    2_xyzrec: 0.1773 0.2228 0.003  0.55  23.4 128.6  56.9  30      0.019  
REMARK       2_adp: 0.1719 0.2209 0.003  0.55  21.3 127.2  55.9  30      0.019  
REMARK   2 regHadp: 0.1718 0.2209 0.003  0.55  21.3 127.2  55.9  30      0.019  
REMARK       2_occ: 0.1718 0.2208 0.003  0.55  21.3 127.2  55.9  30      0.019  
REMARK       3_bss: 0.1712 0.2193 0.003  0.55  21.2 126.8  55.5  30      0.019  
REMARK   3 ttarget: 0.1712 0.2193 0.003  0.55  21.2 126.8  55.5  30      0.019  
REMARK   3 datecdl: 0.1712 0.2193 0.003  0.56  21.2 126.8  55.5  30      0.019  
REMARK     3_setrh: 0.1712 0.2193 0.003  0.56  21.2 126.8  55.5  30      0.019  
REMARK       3_nqh: 0.1712 0.2193 0.003  0.56  21.2 126.8  55.5  30      0.019  
REMARK    3_weight: 0.1712 0.2193 0.003  0.56  21.2 126.8  55.5  30      0.019  
REMARK    3_xyzrec: 0.1715 0.2192 0.003  0.56  21.2 126.8  55.5  30      0.019  
REMARK       3_adp: 0.1739 0.2189 0.003  0.56  23.6 124.7  55.2  30      0.019  
REMARK   3 regHadp: 0.1742 0.2188 0.003  0.56  23.6 124.7  55.2  30      0.019  
REMARK       3_occ: 0.1741 0.2189 0.003  0.56  23.6 124.7  55.2  30      0.019  
REMARK         end: 0.1742 0.2187 0.003  0.56  23.2 124.4  54.9  30      0.019  
REMARK ------------------------------------------------------------------------ 
REMARK MODEL CONTENT.                                                           
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM                        
REMARK        H                     2345         2317.00                        
REMARK        C                     1507         1498.00                        
REMARK        S                       25           24.00                        
REMARK        O                      477          474.50                        
REMARK        N                      402          400.00                        
REMARK    TOTAL                     4756         4713.50                        
REMARK -----------------------------------------------------------------------  
REMARK r_free_flags.md5.hexdigest acb111f55e98e2ab545718d02393276f              
REMARK                                                                          
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.        
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13-2998_9999: ???)                         
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,       
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,   
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty, 
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini, 
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart    
REMARK   3                                                                      
REMARK   3  X-RAY DATA.                                                         
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ML                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.350                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.954                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.71                          
REMARK   3   NUMBER OF REFLECTIONS             : 11116                          
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 11116                      
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1786                          
REMARK   3   R VALUE            (WORKING SET) : 0.1742                          
REMARK   3   FREE R VALUE                     : 0.2187                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.99                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1111                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWOR 
REMARK   3     1 25.9555 -  4.6919    0.99     1308   144  0.1386 0.1721   0.95 
REMARK   3     2  4.6919 -  3.7276    1.00     1271   141  0.1259 0.1459   0.95 
REMARK   3     3  3.7276 -  3.2575    0.99     1289   143  0.1566 0.2315   0.92 
REMARK   3     4  3.2575 -  2.9601    1.00     1270   141  0.2005 0.2564   0.88 
REMARK   3     5  2.9601 -  2.7482    1.00     1266   141  0.2296 0.3201   0.85 
REMARK   3     6  2.7482 -  2.5863    0.98     1260   140  0.2598 0.2803   0.79 
REMARK   3     7  2.5863 -  2.4569    0.98     1234   138  0.2763 0.3524   0.74 
REMARK   3     8  2.4569 -  2.3500    0.88     1107   123  0.2968 0.3557   0.67 
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)     : 0.32             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.05            
REMARK   3                                                                      
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT                       
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3    BOND      :  0.003   0.023   2434                                 
REMARK   3    ANGLE     :  0.556   4.087   3308                                 
REMARK   3    CHIRALITY :  0.040   0.121    372                                 
REMARK   3    PLANARITY :  0.004   0.032    430                                 
REMARK   3    DIHEDRAL  : 12.092 109.470   1433                                 
REMARK   3    MIN NONBONDED DISTANCE : 2.282                                    
REMARK   3  REMARK   3                                                          
REMARK   3  MOLPROBITY STATISTICS.                                              
REMARK   3    ALL-ATOM CLASHSCORE : 0.64                                        
REMARK   3    RAMACHANDRAN PLOT:                                                
REMARK   3      OUTLIERS : 0.67  %                                              
REMARK   3      ALLOWED  : 2.67  %                                              
REMARK   3      FAVORED  : 96.67 %                                              
REMARK   3    ROTAMER OUTLIERS : 3.80 %                                         
REMARK   3    CBETA DEVIATIONS : 0                                              
REMARK   3    PEPTIDE PLANE:                                                    
REMARK   3      CIS-PROLINE     : 0.0                                           
REMARK   3      CIS-GENERAL     : 0.0                                           
REMARK   3      TWISTED PROLINE : 0.0                                           
REMARK   3      TWISTED GENERAL : 0.0                                           
REMARK   3                                                                      
REMARK   3  ATOMIC DISPLACEMENT PARAMETERS.                                     
REMARK   3   WILSON B : 41.23                                                   
REMARK   3   RMS(B_ISO_OR_EQUIVALENT_BONDED) : 3.35                             
REMARK   3   ATOMS          NUMBER OF ATOMS                                     
REMARK   3                    ISO.  ANISO.                                      
REMARK   3    ALL         :   4756    2373                                      
REMARK   3    ALL (NO H)  :   2411    2373                                      
REMARK   3    SOLVENT     :     30       0                                      
REMARK   3    NON-SOLVENT :   2381    2373                                      
REMARK   3    HYDROGENS   :   2345       0                                      
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  TLS DETAILS.                                                        
REMARK   3   NUMBER OF TLS GROUPS: 6                                            
REMARK   3   ORIGIN: CENTER OF MASS                                             
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 1 through 69 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8555 -11.4953  17.1702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5225 T22:   0.4659                                     
REMARK   3      T33:   0.3434 T12:  -0.1207                                     
REMARK   3      T13:  -0.0092 T23:   0.1089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5518 L22:   1.6136                                     
REMARK   3      L33:   2.5995 L12:  -0.0361                                     
REMARK   3      L13:   2.8884 L23:   0.6712                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6923 S12:  -0.7478 S13:  -0.4052                       
REMARK   3      S21:   0.3540 S22:  -0.2355 S23:  -0.1088                       
REMARK   3      S31:   1.1933 S32:  -0.5421 S33:  -0.3706                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 70 through 155 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9872  -9.3321   8.6885              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4520 T22:   0.3188                                     
REMARK   3      T33:   0.2001 T12:   0.0064                                     
REMARK   3      T13:  -0.0222 T23:   0.0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3650 L22:   5.0125                                     
REMARK   3      L33:   3.1057 L12:  -0.2807                                     
REMARK   3      L13:   2.3826 L23:  -0.5034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4859 S12:  -0.0837 S13:  -0.2166                       
REMARK   3      S21:  -0.0094 S22:  -0.2395 S23:   0.0425                       
REMARK   3      S31:   0.8019 S32:   0.1437 S33:  -0.1424                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 156 through 214 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3219   3.8268   7.8884              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1566 T22:   0.2924                                     
REMARK   3      T33:   0.3678 T12:  -0.0205                                     
REMARK   3      T13:   0.0270 T23:   0.0603                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1690 L22:   2.8772                                     
REMARK   3      L33:   6.9032 L12:  -0.0927                                     
REMARK   3      L13:   1.3535 L23:  -2.9376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1147 S12:   0.1124 S13:   0.3441                       
REMARK   3      S21:   0.2016 S22:  -0.2425 S23:  -0.2129                       
REMARK   3      S31:  -0.2172 S32:   0.2343 S33:   0.3714                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 215 through 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4965  22.6145 -11.7283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7470 T22:   0.6493                                     
REMARK   3      T33:   0.6689 T12:  -0.2249                                     
REMARK   3      T13:  -0.0971 T23:   0.2300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0841 L22:   1.5867                                     
REMARK   3      L33:   1.8173 L12:   2.3302                                     
REMARK   3      L13:  -1.1177 L23:   0.5190                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4972 S12:   1.1179 S13:   0.8303                       
REMARK   3      S21:  -0.1991 S22:   0.2293 S23:  -0.0568                       
REMARK   3      S31:  -1.6153 S32:   0.8139 S33:   0.1819                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 237 through 274 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7298  16.4522 -11.1194              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3277 T22:   0.5672                                     
REMARK   3      T33:   0.5770 T12:  -0.1735                                     
REMARK   3      T13:   0.0146 T23:   0.1960                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0888 L22:   1.7274                                     
REMARK   3      L33:   7.6302 L12:  -0.3545                                     
REMARK   3      L13:  -0.0750 L23:   2.7639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1220 S12:   0.4804 S13:   0.6390                       
REMARK   3      S21:  -0.1983 S22:   0.2315 S23:  -0.0664                       
REMARK   3      S31:  -0.5493 S32:   0.7856 S33:  -0.0989                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 275 through 305 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0087   9.1077  -7.9214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3627 T22:   0.4471                                     
REMARK   3      T33:   0.3974 T12:  -0.0158                                     
REMARK   3      T13:   0.1079 T23:   0.1188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4477 L22:   6.3527                                     
REMARK   3      L33:   4.3590 L12:  -3.2995                                     
REMARK   3      L13:  -0.1391 L23:   3.6167                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0035 S12:   0.5537 S13:  -0.0348                       
REMARK   3      S21:   0.1219 S22:  -0.4825 S23:   0.1988                       
REMARK   3      S31:   0.2053 S32:  -0.2354 S33:   0.5823                       
REMARK   3                                                                      
CRYST1  113.580   54.500   45.050  90.00 101.25  90.00 C 1 2 1                  
SCALE1      0.008804  0.000000  0.001751        0.00000                         
SCALE2      0.000000  0.018349  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022632        0.00000                         
ATOM      1  N   SER A   1      -3.018   4.066 -17.109  1.00 56.31           N  
ANISOU    1  N   SER A   1     7222   7020   7153   1014   -362    591       N  
ATOM      2  CA  SER A   1      -2.142   5.078 -16.451  1.00 56.84           C  
ANISOU    2  CA  SER A   1     7108   7124   7366    892   -320    787       C  
ATOM      3  C   SER A   1      -2.489   5.195 -14.969  1.00 50.66           C  
ANISOU    3  C   SER A   1     6165   6202   6880    807   -314    580       C  
ATOM      4  O   SER A   1      -3.110   4.299 -14.399  1.00 51.60           O  
ANISOU    4  O   SER A   1     6311   6274   7022    837   -265    333       O  
ATOM      5  CB  SER A   1      -2.274   6.435 -17.144  1.00 62.65           C  
ANISOU    5  CB  SER A   1     7817   7780   8208    787   -546   1010       C  
ATOM      6  OG  SER A   1      -3.550   7.006 -16.920  1.00 63.59           O  
ANISOU    6  OG  SER A   1     7907   7631   8624    733   -804    814       O  
ATOM      7  N   GLY A   2      -2.087   6.302 -14.352  1.00 44.68           N  
ANISOU    7  N   GLY A   2     5238   5393   6345    695   -378    687       N  
ATOM      8  CA  GLY A   2      -2.237   6.497 -12.925  1.00 37.45           C  
ANISOU    8  CA  GLY A   2     4149   4399   5680    629   -362    502       C  
ATOM      9  C   GLY A   2      -0.961   6.164 -12.171  1.00 35.62           C  
ANISOU    9  C   GLY A   2     3845   4324   5365    631   -129    607       C  
ATOM     10  O   GLY A   2      -0.025   5.555 -12.695  1.00 40.26           O  
ANISOU   10  O   GLY A   2     4517   5092   5688    705     43    769       O  
ATOM     11  N   PHE A   3      -0.928   6.577 -10.903  1.00 34.70           N  
ANISOU   11  N   PHE A   3     3556   4151   5476    563   -134    489       N  
ATOM     12  CA  PHE A   3       0.261   6.363 -10.078  1.00 37.15           C  
ANISOU   12  CA  PHE A   3     3784   4586   5745    560     58    575       C  
ATOM     13  C   PHE A   3      -0.130   6.246  -8.614  1.00 39.25           C  
ANISOU   13  C   PHE A   3     3918   4810   6184    516     80    324       C  
ATOM     14  O   PHE A   3      -0.722   7.174  -8.055  1.00 40.72           O  
ANISOU   14  O   PHE A   3     3956   4884   6633    457    -95    194       O  
ATOM     15  CB  PHE A   3       1.269   7.499 -10.270  1.00 39.61           C  
ANISOU   15  CB  PHE A   3     3986   4916   6147    496      0    860       C  
ATOM     16  CG  PHE A   3       2.684   7.093  -9.997  1.00 41.40           C  
ANISOU   16  CG  PHE A   3     4179   5332   6220    525    226   1027       C  
ATOM     17  CD1 PHE A   3       3.388   6.351 -10.931  1.00 44.79           C  
ANISOU   17  CD1 PHE A   3     4725   5963   6332    614    389   1183       C  
ATOM     18  CD2 PHE A   3       3.308   7.438  -8.809  1.00 39.78           C  
ANISOU   18  CD2 PHE A   3     3816   5116   6183    481    265   1003       C  
ATOM     19  CE1 PHE A   3       4.690   5.961 -10.689  1.00 47.31           C  
ANISOU   19  CE1 PHE A   3     4991   6474   6511    659    588   1305       C  
ATOM     20  CE2 PHE A   3       4.612   7.053  -8.560  1.00 41.75           C  
ANISOU   20  CE2 PHE A   3     4027   5534   6301    514    461   1144       C  
ATOM     21  CZ  PHE A   3       5.304   6.313  -9.504  1.00 45.93           C  
ANISOU   21  CZ  PHE A   3     4663   6268   6522    604    623   1292       C  
ATOM     22  N   ARG A   4       0.242   5.126  -7.991  1.00 37.78           N  
ANISOU   22  N   ARG A   4     3782   4728   5845    548    278    255       N  
ATOM     23  CA  ARG A   4      -0.105   4.835  -6.609  1.00 34.97           C  
ANISOU   23  CA  ARG A   4     3321   4380   5586    490    324     40       C  
ATOM     24  C   ARG A   4       1.126   4.402  -5.825  1.00 33.37           C  
ANISOU   24  C   ARG A   4     3095   4284   5300    506    501    131       C  
ATOM     25  O   ARG A   4       2.012   3.727  -6.355  1.00 32.93           O  
ANISOU   25  O   ARG A   4     3158   4311   5044    587    627    282       O  
ATOM     26  CB  ARG A   4      -1.153   3.716  -6.518  1.00 35.53           C  
ANISOU   26  CB  ARG A   4     3496   4448   5557    475    350   -158       C  
ATOM     27  CG  ARG A   4      -2.575   4.156  -6.759  1.00 39.28           C  
ANISOU   27  CG  ARG A   4     3917   4831   6178    432    171   -348       C  
ATOM     28  CD  ARG A   4      -3.181   4.721  -5.495  1.00 42.59           C  
ANISOU   28  CD  ARG A   4     4109   5277   6798    346    116   -576       C  
ATOM     29  NE  ARG A   4      -4.575   5.101  -5.687  1.00 46.07           N  
ANISOU   29  NE  ARG A   4     4467   5657   7379    319    -57   -801       N  
ATOM     30  CZ  ARG A   4      -5.311   5.716  -4.766  1.00 51.79           C  
ANISOU   30  CZ  ARG A   4     4964   6427   8287    271   -147  -1055       C  
ATOM     31  NH1 ARG A   4      -4.784   6.021  -3.589  1.00 56.19           N  
ANISOU   31  NH1 ARG A   4     5381   7084   8883    240    -80  -1100       N  
ATOM     32  NH2 ARG A   4      -6.573   6.027  -5.027  1.00 52.13           N  
ANISOU   32  NH2 ARG A   4     4925   6428   8454    264   -313  -1276       N  
ATOM     33  N   LYS A   5       1.167   4.786  -4.549  1.00 37.37           N  
ANISOU   33  N   LYS A   5     3440   4802   5957    444    500     15       N  
ATOM     34  CA  LYS A   5       2.135   4.208  -3.623  1.00 41.88           C  
ANISOU   34  CA  LYS A   5     4002   5465   6447    450    656     49       C  
ATOM     35  C   LYS A   5       1.840   2.715  -3.536  1.00 45.69           C  
ANISOU   35  C   LYS A   5     4658   5986   6718    457    760    -23       C  
ATOM     36  O   LYS A   5       0.857   2.302  -2.911  1.00 51.83           O  
ANISOU   36  O   LYS A   5     5420   6766   7508    369    738   -204       O  
ATOM     37  CB  LYS A   5       2.058   4.876  -2.252  1.00 44.71           C  
ANISOU   37  CB  LYS A   5     4161   5838   6987    383    612    -97       C  
ATOM     38  CG  LYS A   5       3.138   4.433  -1.270  1.00 47.10           C  
ANISOU   38  CG  LYS A   5     4531   6228   7135    372    701    -47       C  
ATOM     39  CD  LYS A   5       4.507   5.004  -1.615  1.00 50.11           C  
ANISOU   39  CD  LYS A   5     4902   6605   7534    418    710    160       C  
ATOM     40  CE  LYS A   5       4.604   6.499  -1.329  1.00 52.15           C  
ANISOU   40  CE  LYS A   5     5036   6790   7989    375    535    160       C  
ATOM     41  NZ  LYS A   5       4.458   6.821   0.115  1.00 54.17           N  
ANISOU   41  NZ  LYS A   5     5276   7079   8227    327    463    -15       N  
ATOM     42  N   MET A   6       2.670   1.905  -4.177  1.00 42.38           N  
ANISOU   42  N   MET A   6     4393   5603   6106    557    855    113       N  
ATOM     43  CA  MET A   6       2.393   0.492  -4.378  1.00 41.76           C  
ANISOU   43  CA  MET A   6     4511   5513   5841    591    890     55       C  
ATOM     44  C   MET A   6       3.353  -0.349  -3.552  1.00 37.02           C  
ANISOU   44  C   MET A   6     3961   4960   5146    617    988     83       C  
ATOM     45  O   MET A   6       4.532  -0.013  -3.424  1.00 37.84           O  
ANISOU   45  O   MET A   6     4000   5129   5250    686   1059    199       O  
ATOM     46  CB  MET A   6       2.524   0.142  -5.860  1.00 47.49           C  
ANISOU   46  CB  MET A   6     5390   6243   6411    727    876    143       C  
ATOM     47  CG  MET A   6       1.760  -1.082  -6.301  1.00 50.83           C  
ANISOU   47  CG  MET A   6     6010   6599   6705    757    824     35       C  
ATOM     48  SD  MET A   6       1.756  -1.214  -8.099  1.00 51.97           S  
ANISOU   48  SD  MET A   6     6301   6767   6679    929    777    103       S  
ATOM     49  CE  MET A   6       0.690   0.156  -8.534  1.00 51.37           C  
ANISOU   49  CE  MET A   6     6106   6624   6790    825    655     97       C  
ATOM     50  N   ALA A   7       2.840  -1.436  -2.986  1.00 32.88           N  
ANISOU   50  N   ALA A   7     3548   4395   4549    550    972    -13       N  
ATOM     51  CA  ALA A   7       3.652  -2.394  -2.254  1.00 33.83           C  
ANISOU   51  CA  ALA A   7     3759   4521   4572    571   1017     13       C  
ATOM     52  C   ALA A   7       3.747  -3.695  -3.039  1.00 35.01           C  
ANISOU   52  C   ALA A   7     4146   4600   4556    689    963     11       C  
ATOM     53  O   ALA A   7       2.938  -3.971  -3.930  1.00 34.54           O  
ANISOU   53  O   ALA A   7     4182   4482   4458    711    889    -36       O  
ATOM     54  CB  ALA A   7       3.073  -2.662  -0.860  1.00 32.79           C  
ANISOU   54  CB  ALA A   7     3576   4401   4481    377   1006    -71       C  
ATOM     55  N   PHE A   8       4.751  -4.497  -2.698  1.00 34.16           N  
ANISOU   55  N   PHE A   8     4133   4487   4360    780    976     45       N  
ATOM     56  CA  PHE A   8       4.909  -5.795  -3.332  1.00 33.91           C  
ANISOU   56  CA  PHE A   8     4326   4369   4188    916    880      8       C  
ATOM     57  C   PHE A   8       3.840  -6.765  -2.828  1.00 32.96           C  
ANISOU   57  C   PHE A   8     4346   4106   4072    745    745    -56       C  
ATOM     58  O   PHE A   8       3.368  -6.646  -1.694  1.00 27.54           O  
ANISOU   58  O   PHE A   8     3583   3427   3453    528    756    -52       O  
ATOM     59  CB  PHE A   8       6.292  -6.368  -3.043  1.00 37.32           C  
ANISOU   59  CB  PHE A   8     4806   4826   4546   1073    897     36       C  
ATOM     60  CG  PHE A   8       7.411  -5.619  -3.703  1.00 42.12           C  
ANISOU   60  CG  PHE A   8     5282   5604   5117   1253   1022    105       C  
ATOM     61  CD1 PHE A   8       7.774  -5.904  -5.008  1.00 43.09           C  
ANISOU   61  CD1 PHE A   8     5468   5811   5094   1472   1019     85       C  
ATOM     62  CD2 PHE A   8       8.104  -4.634  -3.020  1.00 44.07           C  
ANISOU   62  CD2 PHE A   8     5330   5947   5466   1197   1135    191       C  
ATOM     63  CE1 PHE A   8       8.805  -5.218  -5.620  1.00 43.72           C  
ANISOU   63  CE1 PHE A   8     5402   6100   5111   1608   1146    172       C  
ATOM     64  CE2 PHE A   8       9.134  -3.945  -3.629  1.00 43.48           C  
ANISOU   64  CE2 PHE A   8     5123   6035   5364   1316   1230    282       C  
ATOM     65  CZ  PHE A   8       9.488  -4.239  -4.929  1.00 43.22           C  
ANISOU   65  CZ  PHE A   8     5148   6102   5170   1481   1221    282       C  
ATOM     66  N   PRO A   9       3.443  -7.735  -3.652  1.00 40.47           N  
ANISOU   66  N   PRO A   9     5493   4940   4945    833    606   -112       N  
ATOM     67  CA  PRO A   9       2.577  -8.809  -3.147  1.00 40.70           C  
ANISOU   67  CA  PRO A   9     5671   4810   4983    657    443   -140       C  
ATOM     68  C   PRO A   9       3.237  -9.476  -1.951  1.00 35.25           C  
ANISOU   68  C   PRO A   9     5041   4072   4282    573    401    -83       C  
ATOM     69  O   PRO A   9       4.407  -9.863  -2.002  1.00 34.20           O  
ANISOU   69  O   PRO A   9     4977   3922   4094    768    383    -77       O  
ATOM     70  CB  PRO A   9       2.448  -9.766  -4.338  1.00 45.81           C  
ANISOU   70  CB  PRO A   9     6534   5324   5549    849    273   -216       C  
ATOM     71  CG  PRO A   9       2.854  -8.973  -5.532  1.00 46.23           C  
ANISOU   71  CG  PRO A   9     6511   5514   5540   1077    381   -236       C  
ATOM     72  CD  PRO A   9       3.868  -7.978  -5.041  1.00 44.12           C  
ANISOU   72  CD  PRO A   9     6051   5418   5293   1102    574   -151       C  
ATOM     73  N   SER A  10       2.485  -9.592  -0.862  1.00 32.76           N  
ANISOU   73  N   SER A  10     4684   3756   4008    281    383    -43       N  
ATOM     74  CA  SER A  10       3.029 -10.035   0.413  1.00 34.38           C  
ANISOU   74  CA  SER A  10     4918   3952   4193    154    359     36       C  
ATOM     75  C   SER A  10       2.818 -11.519   0.672  1.00 38.93           C  
ANISOU   75  C   SER A  10     5746   4316   4729     51    110     85       C  
ATOM     76  O   SER A  10       3.186 -12.002   1.747  1.00 42.44           O  
ANISOU   76  O   SER A  10     6246   4730   5149    -87     48    175       O  
ATOM     77  CB  SER A  10       2.396  -9.226   1.549  1.00 32.19           C  
ANISOU   77  CB  SER A  10     4423   3854   3955   -115    490     58       C  
ATOM     78  OG  SER A  10       0.988  -9.383   1.543  1.00 28.98           O  
ANISOU   78  OG  SER A  10     3987   3463   3561   -342    443     32       O  
ATOM     79  N   GLY A  11       2.245 -12.251  -0.284  1.00 38.07           N  
ANISOU   79  N   GLY A  11     5799   4046   4620    114    -61     34       N  
ATOM     80  CA  GLY A  11       1.877 -13.633  -0.025  1.00 38.40           C  
ANISOU   80  CA  GLY A  11     6076   3855   4658    -26   -344     92       C  
ATOM     81  C   GLY A  11       3.047 -14.486   0.422  1.00 38.39           C  
ANISOU   81  C   GLY A  11     6253   3704   4630     96   -508    130       C  
ATOM     82  O   GLY A  11       2.915 -15.308   1.332  1.00 43.11           O  
ANISOU   82  O   GLY A  11     6977   4175   5227   -135   -687    252       O  
ATOM     83  N   LYS A  12       4.210 -14.304  -0.206  1.00 34.95           N  
ANISOU   83  N   LYS A  12     5821   3292   4167    452   -461     29       N  
ATOM     84  CA  LYS A  12       5.363 -15.135   0.118  1.00 36.21           C  
ANISOU   84  CA  LYS A  12     6140   3307   4313    618   -641     20       C  
ATOM     85  C   LYS A  12       5.893 -14.859   1.519  1.00 35.07           C  
ANISOU   85  C   LYS A  12     5918   3241   4167    439   -554    145       C  
ATOM     86  O   LYS A  12       6.509 -15.741   2.127  1.00 37.77           O  
ANISOU   86  O   LYS A  12     6430   3408   4511    441   -773    189       O  
ATOM     87  CB  LYS A  12       6.467 -14.916  -0.912  1.00 39.82           C  
ANISOU   87  CB  LYS A  12     6562   3844   4722   1046   -577   -137       C  
ATOM     88  CG  LYS A  12       6.125 -15.484  -2.266  1.00 47.53           C  
ANISOU   88  CG  LYS A  12     7669   4720   5669   1272   -736   -284       C  
ATOM     89  CD  LYS A  12       7.127 -15.082  -3.322  1.00 53.18           C  
ANISOU   89  CD  LYS A  12     8292   5623   6291   1670   -611   -432       C  
ATOM     90  CE  LYS A  12       6.907 -15.893  -4.588  1.00 60.19           C  
ANISOU   90  CE  LYS A  12     9345   6400   7124   1934   -833   -611       C  
ATOM     91  NZ  LYS A  12       6.936 -15.052  -5.816  1.00 63.52           N  
ANISOU   91  NZ  LYS A  12     9619   7082   7433   2139   -617   -688       N  
ATOM     92  N   VAL A  13       5.678 -13.652   2.044  1.00 33.95           N  
ANISOU   92  N   VAL A  13     5527   3347   4026    297   -267    191       N  
ATOM     93  CA  VAL A  13       6.140 -13.339   3.392  1.00 38.28           C  
ANISOU   93  CA  VAL A  13     5990   3991   4562    135   -186    291       C  
ATOM     94  C   VAL A  13       5.126 -13.806   4.427  1.00 41.24           C  
ANISOU   94  C   VAL A  13     6414   4351   4904   -273   -279    433       C  
ATOM     95  O   VAL A  13       5.500 -14.289   5.502  1.00 45.46           O  
ANISOU   95  O   VAL A  13     7032   4842   5400   -423   -383    547       O  
ATOM     96  CB  VAL A  13       6.433 -11.833   3.519  1.00 37.36           C  
ANISOU   96  CB  VAL A  13     5580   4143   4471    188    127    256       C  
ATOM     97  CG1 VAL A  13       6.839 -11.477   4.944  1.00 37.46           C  
ANISOU   97  CG1 VAL A  13     5498   4265   4471     24    200    337       C  
ATOM     98  CG2 VAL A  13       7.522 -11.425   2.541  1.00 35.89           C  
ANISOU   98  CG2 VAL A  13     5341   3997   4300    553    210    160       C  
ATOM     99  N   GLU A  14       3.831 -13.687   4.117  1.00 41.30           N  
ANISOU   99  N   GLU A  14     6364   4411   4918   -466   -251    435       N  
ATOM    100  CA  GLU A  14       2.795 -14.128   5.046  1.00 41.79           C  
ANISOU  100  CA  GLU A  14     6435   4514   4930   -878   -324    576       C  
ATOM    101  C   GLU A  14       3.058 -15.542   5.545  1.00 44.22           C  
ANISOU  101  C   GLU A  14     7031   4558   5212  -1007   -654    725       C  
ATOM    102  O   GLU A  14       2.883 -15.832   6.733  1.00 49.05           O  
ANISOU  102  O   GLU A  14     7654   5238   5745  -1318   -699    891       O  
ATOM    103  CB  GLU A  14       1.424 -14.052   4.372  1.00 40.62           C  
ANISOU  103  CB  GLU A  14     6223   4399   4812  -1015   -314    534       C  
ATOM    104  CG  GLU A  14       0.975 -12.640   4.042  1.00 37.84           C  
ANISOU  104  CG  GLU A  14     5578   4305   4493   -951    -27    399       C  
ATOM    105  CD  GLU A  14      -0.254 -12.612   3.160  1.00 37.92           C  
ANISOU  105  CD  GLU A  14     5554   4301   4554  -1011    -53    327       C  
ATOM    106  OE1 GLU A  14      -1.149 -13.460   3.348  1.00 42.09           O  
ANISOU  106  OE1 GLU A  14     6171   4753   5067  -1276   -217    415       O  
ATOM    107  OE2 GLU A  14      -0.322 -11.748   2.266  1.00 38.92           O  
ANISOU  107  OE2 GLU A  14     5565   4485   4738   -801     74    194       O  
ATOM    108  N   GLY A  15       3.489 -16.432   4.656  1.00 43.91           N  
ANISOU  108  N   GLY A  15     7229   4221   5234   -769   -909    665       N  
ATOM    109  CA  GLY A  15       3.744 -17.806   5.032  1.00 46.88           C  
ANISOU  109  CA  GLY A  15     7901   4289   5623   -862  -1292    788       C  
ATOM    110  C   GLY A  15       4.925 -18.016   5.949  1.00 48.46           C  
ANISOU  110  C   GLY A  15     8178   4443   5793   -807  -1363    852       C  
ATOM    111  O   GLY A  15       5.168 -19.153   6.366  1.00 48.27           O  
ANISOU  111  O   GLY A  15     8411   4144   5786   -901  -1715    970       O  
ATOM    112  N   CYS A  16       5.660 -16.958   6.282  1.00 50.38           N  
ANISOU  112  N   CYS A  16     8211   4926   6005   -662  -1068    782       N  
ATOM    113  CA  CYS A  16       6.859 -17.061   7.100  1.00 49.26           C  
ANISOU  113  CA  CYS A  16     8121   4749   5845   -570  -1121    815       C  
ATOM    114  C   CYS A  16       6.718 -16.383   8.453  1.00 45.50           C  
ANISOU  114  C   CYS A  16     7476   4539   5273   -860   -922    946       C  
ATOM    115  O   CYS A  16       7.663 -16.412   9.249  1.00 45.11           O  
ANISOU  115  O   CYS A  16     7460   4478   5201   -812   -961    984       O  
ATOM    116  CB  CYS A  16       8.051 -16.458   6.348  1.00 47.01           C  
ANISOU  116  CB  CYS A  16     7735   4512   5613   -117   -978    610       C  
ATOM    117  SG  CYS A  16       8.281 -17.119   4.679  1.00 45.92           S  
ANISOU  117  SG  CYS A  16     7744   4163   5542    279  -1165    406       S  
ATOM    118  N   MET A  17       5.571 -15.779   8.742  1.00 42.75           N  
ANISOU  118  N   MET A  17     6939   4442   4863  -1142   -724    994       N  
ATOM    119  CA  MET A  17       5.390 -15.017   9.968  1.00 42.68           C  
ANISOU  119  CA  MET A  17     6724   4747   4744  -1379   -513   1064       C  
ATOM    120  C   MET A  17       4.877 -15.940  11.066  1.00 46.56           C  
ANISOU  120  C   MET A  17     7362   5224   5105  -1799   -715   1312       C  
ATOM    121  O   MET A  17       3.843 -16.594  10.905  1.00 48.35           O  
ANISOU  121  O   MET A  17     7666   5398   5306  -2068   -848   1426       O  
ATOM    122  CB  MET A  17       4.425 -13.857   9.739  1.00 42.54           C  
ANISOU  122  CB  MET A  17     6400   5042   4723  -1447   -211    953       C  
ATOM    123  CG  MET A  17       4.903 -12.873   8.687  1.00 40.50           C  
ANISOU  123  CG  MET A  17     5995   4806   4588  -1073    -25    748       C  
ATOM    124  SD  MET A  17       6.597 -12.327   8.976  1.00 40.91           S  
ANISOU  124  SD  MET A  17     6006   4849   4689   -753     48    684       S  
ATOM    125  CE  MET A  17       6.515 -11.818  10.693  1.00 44.39           C  
ANISOU  125  CE  MET A  17     6292   5564   5009  -1033    156    767       C  
ATOM    126  N   VAL A  18       5.610 -15.988  12.179  1.00 48.28           N  
ANISOU  126  N   VAL A  18     7615   5492   5236  -1868   -750   1410       N  
ATOM    127  CA  VAL A  18       5.246 -16.801  13.328  1.00 49.88           C  
ANISOU  127  CA  VAL A  18     7956   5715   5283  -2282   -940   1676       C  
ATOM    128  C   VAL A  18       5.202 -15.921  14.569  1.00 48.38           C  
ANISOU  128  C   VAL A  18     7523   5937   4921  -2455   -688   1697       C  
ATOM    129  O   VAL A  18       5.739 -14.811  14.599  1.00 45.19           O  
ANISOU  129  O   VAL A  18     6904   5707   4558  -2205   -440   1506       O  
ATOM    130  CB  VAL A  18       6.227 -17.974  13.549  1.00 51.19           C  
ANISOU  130  CB  VAL A  18     8471   5486   5492  -2215  -1333   1803       C  
ATOM    131  CG1 VAL A  18       6.118 -18.980  12.423  1.00 50.08           C  
ANISOU  131  CG1 VAL A  18     8580   4944   5506  -2085  -1644   1781       C  
ATOM    132  CG2 VAL A  18       7.651 -17.450  13.668  1.00 52.38           C  
ANISOU  132  CG2 VAL A  18     8591   5601   5711  -1836  -1261   1646       C  
ATOM    133  N   GLN A  19       4.556 -16.445  15.603  1.00 51.07           N  
ANISOU  133  N   GLN A  19     7902   6441   5063  -2895   -773   1938       N  
ATOM    134  CA  GLN A  19       4.416 -15.769  16.884  1.00 53.96           C  
ANISOU  134  CA  GLN A  19     8025   7239   5239  -3052   -572   1928       C  
ATOM    135  C   GLN A  19       5.474 -16.302  17.839  1.00 54.84           C  
ANISOU  135  C   GLN A  19     8337   7218   5283  -3057   -776   2064       C  
ATOM    136  O   GLN A  19       5.658 -17.518  17.952  1.00 55.96           O  
ANISOU  136  O   GLN A  19     8748   7062   5451  -3155  -1117   2227       O  
ATOM    137  CB  GLN A  19       3.015 -15.996  17.452  1.00 63.34           C  
ANISOU  137  CB  GLN A  19     9026   8749   6291  -3364   -543   1956       C  
ATOM    138  CG  GLN A  19       2.700 -15.200  18.701  1.00 72.18           C  
ANISOU  138  CG  GLN A  19     9851  10351   7222  -3457   -333   1866       C  
ATOM    139  CD  GLN A  19       1.665 -15.888  19.571  1.00 80.73           C  
ANISOU  139  CD  GLN A  19    10879  11674   8120  -3807   -442   1999       C  
ATOM    140  OE1 GLN A  19       0.553 -15.390  19.747  1.00 81.55           O  
ANISOU  140  OE1 GLN A  19    10717  12131   8137  -3897   -280   1882       O  
ATOM    141  NE2 GLN A  19       2.031 -17.040  20.122  1.00 85.73           N  
ANISOU  141  NE2 GLN A  19    11765  12114   8693  -3999   -739   2243       N  
ATOM    142  N   VAL A  20       6.168 -15.395  18.519  1.00 56.33           N  
ANISOU  142  N   VAL A  20     8386   7620   5398  -2943   -589   1981       N  
ATOM    143  CA  VAL A  20       7.235 -15.757  19.444  1.00 59.95           C  
ANISOU  143  CA  VAL A  20     9018   7970   5792  -2921   -765   2091       C  
ATOM    144  C   VAL A  20       6.913 -15.175  20.810  1.00 60.99           C  
ANISOU  144  C   VAL A  20     8899   8563   5711  -3097   -595   2060       C  
ATOM    145  O   VAL A  20       6.695 -13.965  20.939  1.00 61.33           O  
ANISOU  145  O   VAL A  20     8638   8945   5719  -3002   -292   1864       O  
ATOM    146  CB  VAL A  20       8.608 -15.259  18.959  1.00 57.88           C  
ANISOU  146  CB  VAL A  20     8778   7475   5737  -2446   -747   1891       C  
ATOM    147  CG1 VAL A  20       9.622 -15.356  20.083  1.00 58.94           C  
ANISOU  147  CG1 VAL A  20     9012   7600   5783  -2433   -866   1967       C  
ATOM    148  CG2 VAL A  20       9.070 -16.055  17.753  1.00 56.67           C  
ANISOU  148  CG2 VAL A  20     8867   6857   5809  -2195   -983   1857       C  
ATOM    149  N   THR A  21       6.893 -16.037  21.826  1.00 59.05           N  
ANISOU  149  N   THR A  21     8777   8323   5336  -3337   -812   2236       N  
ATOM    150  CA  THR A  21       6.678 -15.628  23.208  1.00 57.00           C  
ANISOU  150  CA  THR A  21     8323   8480   4853  -3508   -702   2231       C  
ATOM    151  C   THR A  21       7.787 -16.214  24.066  1.00 56.19           C  
ANISOU  151  C   THR A  21     8464   8185   4699  -3519   -944   2384       C  
ATOM    152  O   THR A  21       7.977 -17.436  24.089  1.00 58.16           O  
ANISOU  152  O   THR A  21     8992   8110   4998  -3643  -1275   2571       O  
ATOM    153  CB  THR A  21       5.313 -16.093  23.726  1.00 58.73           C  
ANISOU  153  CB  THR A  21     8408   8990   4917  -3859   -719   2310       C  
ATOM    154  OG1 THR A  21       4.279 -15.242  23.217  1.00 55.10           O  
ANISOU  154  OG1 THR A  21     7646   8819   4469  -3814   -451   2105       O  
ATOM    155  CG2 THR A  21       5.289 -16.071  25.244  1.00 60.81           C  
ANISOU  155  CG2 THR A  21     8574   9594   4937  -4069   -723   2379       C  
ATOM    156  N   CYS A  22       8.517 -15.352  24.766  1.00 56.03           N  
ANISOU  156  N   CYS A  22     8337   8357   4596  -3379   -803   2289       N  
ATOM    157  CA  CYS A  22       9.523 -15.774  25.734  1.00 60.63           C  
ANISOU  157  CA  CYS A  22     9115   8819   5103  -3389  -1012   2413       C  
ATOM    158  C   CYS A  22       9.143 -15.176  27.079  1.00 65.49           C  
ANISOU  158  C   CYS A  22     9483   9938   5464  -3557   -844   2372       C  
ATOM    159  O   CYS A  22       9.197 -13.953  27.258  1.00 61.26           O  
ANISOU  159  O   CYS A  22     8685   9715   4877  -3394   -575   2159       O  
ATOM    160  CB  CYS A  22      10.925 -15.332  25.331  1.00 58.15           C  
ANISOU  160  CB  CYS A  22     8937   8234   4925  -3023  -1052   2337       C  
ATOM    161  SG  CYS A  22      12.116 -15.582  26.664  1.00 60.73           S  
ANISOU  161  SG  CYS A  22     9435   8500   5140  -3006  -1269   2433       S  
ATOM    162  N   GLY A  23       8.765 -16.030  28.021  1.00 74.58           N  
ANISOU  162  N   GLY A  23    10708  11170   6459  -3876  -1019   2563       N  
ATOM    163  CA  GLY A  23       8.257 -15.548  29.285  1.00 80.03           C  
ANISOU  163  CA  GLY A  23    11151  12368   6887  -4060   -871   2530       C  
ATOM    164  C   GLY A  23       6.918 -14.872  29.092  1.00 83.23           C  
ANISOU  164  C   GLY A  23    11203  13195   7227  -4136   -605   2358       C  
ATOM    165  O   GLY A  23       5.925 -15.537  28.788  1.00 85.05           O  
ANISOU  165  O   GLY A  23    11428  13441   7448  -4369   -674   2460       O  
ATOM    166  N   THR A  24       6.886 -13.543  29.223  1.00 85.30           N  
ANISOU  166  N   THR A  24    11168  13780   7461  -3921   -328   2079       N  
ATOM    167  CA  THR A  24       5.633 -12.802  29.217  1.00 89.39           C  
ANISOU  167  CA  THR A  24    11326  14723   7914  -3959   -107   1866       C  
ATOM    168  C   THR A  24       5.419 -11.938  27.981  1.00 87.87           C  
ANISOU  168  C   THR A  24    10992  14448   7948  -3675     75   1619       C  
ATOM    169  O   THR A  24       4.267 -11.613  27.677  1.00 90.27           O  
ANISOU  169  O   THR A  24    11074  14972   8252  -3720    186   1482       O  
ATOM    170  CB  THR A  24       5.543 -11.904  30.463  1.00 91.87           C  
ANISOU  170  CB  THR A  24    11358  15530   8018  -3942     36   1689       C  
ATOM    171  OG1 THR A  24       4.315 -11.165  30.437  1.00 91.92           O  
ANISOU  171  OG1 THR A  24    11015  15932   7979  -3945    212   1450       O  
ATOM    172  CG2 THR A  24       6.727 -10.938  30.527  1.00 89.03           C  
ANISOU  172  CG2 THR A  24    10977  15111   7739  -3600    124   1508       C  
ATOM    173  N   THR A  25       6.476 -11.561  27.268  1.00 82.97           N  
ANISOU  173  N   THR A  25    10488  13523   7512  -3390     97   1562       N  
ATOM    174  CA  THR A  25       6.324 -10.729  26.082  1.00 77.72           C  
ANISOU  174  CA  THR A  25     9683  12777   7070  -3129    267   1340       C  
ATOM    175  C   THR A  25       6.161 -11.597  24.840  1.00 70.91           C  
ANISOU  175  C   THR A  25     9050  11521   6371  -3165    156   1495       C  
ATOM    176  O   THR A  25       6.693 -12.709  24.759  1.00 71.48           O  
ANISOU  176  O   THR A  25     9447  11262   6451  -3272    -80   1748       O  
ATOM    177  CB  THR A  25       7.523  -9.797  25.894  1.00 77.37           C  
ANISOU  177  CB  THR A  25     9604  12651   7141  -2806    362   1190       C  
ATOM    178  OG1 THR A  25       8.687 -10.564  25.560  1.00 77.96           O  
ANISOU  178  OG1 THR A  25    10032  12321   7268  -2764    180   1416       O  
ATOM    179  CG2 THR A  25       7.780  -8.999  27.163  1.00 79.42           C  
ANISOU  179  CG2 THR A  25     9661  13276   7239  -2758    432   1036       C  
ATOM    180  N   THR A  26       5.424 -11.072  23.866  1.00 63.92           N  
ANISOU  180  N   THR A  26     8000  10654   5632  -3055    297   1322       N  
ATOM    181  CA  THR A  26       5.150 -11.794  22.632  1.00 61.27           C  
ANISOU  181  CA  THR A  26     7847   9984   5448  -3075    209   1433       C  
ATOM    182  C   THR A  26       5.284 -10.847  21.450  1.00 56.57           C  
ANISOU  182  C   THR A  26     7120   9295   5079  -2778    389   1217       C  
ATOM    183  O   THR A  26       4.732  -9.744  21.469  1.00 56.40           O  
ANISOU  183  O   THR A  26     6796   9532   5102  -2646    568    954       O  
ATOM    184  CB  THR A  26       3.748 -12.414  22.658  1.00 65.43           C  
ANISOU  184  CB  THR A  26     8319  10654   5887  -3347    154   1497       C  
ATOM    185  OG1 THR A  26       3.583 -13.269  21.520  1.00 66.56           O  
ANISOU  185  OG1 THR A  26     8684  10435   6171  -3380     17   1631       O  
ATOM    186  CG2 THR A  26       2.675 -11.332  22.633  1.00 66.15           C  
ANISOU  186  CG2 THR A  26     8053  11108   5974  -3269    367   1212       C  
ATOM    187  N   LEU A  27       6.014 -11.280  20.423  1.00 54.90           N  
ANISOU  187  N   LEU A  27     7144   8700   5015  -2663    310   1324       N  
ATOM    188  CA  LEU A  27       6.170 -10.495  19.205  1.00 51.95           C  
ANISOU  188  CA  LEU A  27     6656   8190   4892  -2351    444   1118       C  
ATOM    189  C   LEU A  27       6.289 -11.449  18.022  1.00 52.11           C  
ANISOU  189  C   LEU A  27     6950   7777   5071  -2275    264   1224       C  
ATOM    190  O   LEU A  27       6.166 -12.670  18.165  1.00 51.59           O  
ANISOU  190  O   LEU A  27     7152   7533   4917  -2500     35   1460       O  
ATOM    191  CB  LEU A  27       7.371  -9.547  19.313  1.00 45.66           C  
ANISOU  191  CB  LEU A  27     5758   7335   4254  -1989    512    938       C  
ATOM    192  CG  LEU A  27       8.637 -10.071  19.993  1.00 49.25           C  
ANISOU  192  CG  LEU A  27     6431   7596   4687  -1913    335   1056       C  
ATOM    193  CD1 LEU A  27       9.266 -11.188  19.178  1.00 53.29           C  
ANISOU  193  CD1 LEU A  27     7270   7648   5328  -1809    101   1191       C  
ATOM    194  CD2 LEU A  27       9.633  -8.940  20.227  1.00 46.23           C  
ANISOU  194  CD2 LEU A  27     5866   7249   4450  -1597    437    855       C  
ATOM    195  N   ASN A  28       6.522 -10.881  16.840  1.00 51.71           N  
ANISOU  195  N   ASN A  28     6831   7562   5254  -1957    347   1047       N  
ATOM    196  CA  ASN A  28       6.554 -11.653  15.608  1.00 52.26           C  
ANISOU  196  CA  ASN A  28     7116   7275   5466  -1844    201   1090       C  
ATOM    197  C   ASN A  28       7.954 -12.168  15.311  1.00 47.33           C  
ANISOU  197  C   ASN A  28     6719   6302   4963  -1562     23   1110       C  
ATOM    198  O   ASN A  28       8.960 -11.574  15.710  1.00 47.44           O  
ANISOU  198  O   ASN A  28     6656   6341   5029  -1361     82   1029       O  
ATOM    199  CB  ASN A  28       6.075 -10.813  14.424  1.00 52.57           C  
ANISOU  199  CB  ASN A  28     6969   7339   5667  -1647    374    895       C  
ATOM    200  CG  ASN A  28       4.815 -10.051  14.731  1.00 55.99           C  
ANISOU  200  CG  ASN A  28     7117   8140   6015  -1849    562    800       C  
ATOM    201  OD1 ASN A  28       3.710 -10.580  14.612  1.00 60.27           O  
ANISOU  201  OD1 ASN A  28     7675   8752   6472  -2109    529    877       O  
ATOM    202  ND2 ASN A  28       4.969  -8.798  15.143  1.00 55.69           N  
ANISOU  202  ND2 ASN A  28     6806   8343   6012  -1726    742    620       N  
ATOM    203  N   GLY A  29       8.007 -13.287  14.590  1.00 42.26           N  
ANISOU  203  N   GLY A  29     6347   5333   4376  -1538   -213   1199       N  
ATOM    204  CA  GLY A  29       9.260 -13.830  14.122  1.00 38.91           C  
ANISOU  204  CA  GLY A  29     6123   4582   4079  -1230   -400   1168       C  
ATOM    205  C   GLY A  29       9.161 -14.219  12.660  1.00 38.25           C  
ANISOU  205  C   GLY A  29     6133   4269   4130  -1013   -473   1076       C  
ATOM    206  O   GLY A  29       8.076 -14.442  12.120  1.00 35.99           O  
ANISOU  206  O   GLY A  29     5853   3991   3829  -1165   -474   1101       O  
ATOM    207  N   LEU A  30      10.326 -14.296  12.025  1.00 39.73           N  
ANISOU  207  N   LEU A  30     6380   4274   4441   -644   -537    957       N  
ATOM    208  CA  LEU A  30      10.442 -14.697  10.626  1.00 41.82           C  
ANISOU  208  CA  LEU A  30     6733   4345   4810   -378   -620    840       C  
ATOM    209  C   LEU A  30      10.954 -16.134  10.580  1.00 45.29           C  
ANISOU  209  C   LEU A  30     7505   4429   5275   -314  -1020    891       C  
ATOM    210  O   LEU A  30      12.095 -16.408  10.964  1.00 47.05           O  
ANISOU  210  O   LEU A  30     7808   4536   5533   -136  -1153    860       O  
ATOM    211  CB  LEU A  30      11.370 -13.747   9.874  1.00 39.69           C  
ANISOU  211  CB  LEU A  30     6263   4176   4643     -5   -406    657       C  
ATOM    212  CG  LEU A  30      11.492 -13.971   8.368  1.00 41.05           C  
ANISOU  212  CG  LEU A  30     6471   4244   4883    287   -433    519       C  
ATOM    213  CD1 LEU A  30      10.172 -13.715   7.663  1.00 42.22           C  
ANISOU  213  CD1 LEU A  30     6561   4467   5015    146   -330    518       C  
ATOM    214  CD2 LEU A  30      12.582 -13.083   7.799  1.00 40.72           C  
ANISOU  214  CD2 LEU A  30     6224   4337   4912    618   -236    383       C  
ATOM    215  N   TRP A  31      10.105 -17.047  10.112  1.00 45.92           N  
ANISOU  215  N   TRP A  31     7774   4321   5353   -454  -1239    957       N  
ATOM    216  CA  TRP A  31      10.409 -18.474  10.077  1.00 46.07           C  
ANISOU  216  CA  TRP A  31     8128   3960   5416   -432  -1687   1015       C  
ATOM    217  C   TRP A  31      10.876 -18.845   8.673  1.00 44.87           C  
ANISOU  217  C   TRP A  31     8045   3628   5377    -14  -1804    785       C  
ATOM    218  O   TRP A  31      10.074 -18.893   7.734  1.00 46.04           O  
ANISOU  218  O   TRP A  31     8184   3767   5543     -1  -1778    728       O  
ATOM    219  CB  TRP A  31       9.180 -19.287  10.482  1.00 47.84           C  
ANISOU  219  CB  TRP A  31     8520   4079   5577   -871  -1899   1248       C  
ATOM    220  CG  TRP A  31       9.387 -20.764  10.492  1.00 50.72           C  
ANISOU  220  CG  TRP A  31     9245   4016   6010   -898  -2416   1340       C  
ATOM    221  CD1 TRP A  31      10.575 -21.428  10.570  1.00 51.68           C  
ANISOU  221  CD1 TRP A  31     9557   3863   6215   -628  -2719   1261       C  
ATOM    222  CD2 TRP A  31       8.367 -21.769  10.421  1.00 54.39           C  
ANISOU  222  CD2 TRP A  31     9921   4260   6486  -1214  -2729   1523       C  
ATOM    223  NE1 TRP A  31      10.359 -22.787  10.553  1.00 55.16           N  
ANISOU  223  NE1 TRP A  31    10244   3995   6721   -741  -3166   1316       N  
ATOM    224  CE2 TRP A  31       9.013 -23.021  10.463  1.00 56.47           C  
ANISOU  224  CE2 TRP A  31    10406   4206   6844  -1100  -3171   1471       C  
ATOM    225  CE3 TRP A  31       6.973 -21.732  10.325  1.00 54.20           C  
ANISOU  225  CE3 TRP A  31     9827   4359   6406  -1570  -2643   1659       C  
ATOM    226  CZ2 TRP A  31       8.313 -24.223  10.410  1.00 60.63           C  
ANISOU  226  CZ2 TRP A  31    11068   4558   7410  -1328  -3522   1545       C  
ATOM    227  CZ3 TRP A  31       6.278 -22.929  10.276  1.00 57.79           C  
ANISOU  227  CZ3 TRP A  31    10427   4629   6901  -1793  -2991   1753       C  
ATOM    228  CH2 TRP A  31       6.949 -24.157  10.318  1.00 60.66           C  
ANISOU  228  CH2 TRP A  31    10999   4691   7359  -1670  -3429   1698       C  
ATOM    229  N   LEU A  32      12.173 -19.104   8.537  1.00 42.45           N  
ANISOU  229  N   LEU A  32     7793   3202   5135    336  -1935    638       N  
ATOM    230  CA  LEU A  32      12.780 -19.490   7.270  1.00 44.17           C  
ANISOU  230  CA  LEU A  32     8053   3298   5430    773  -2055    386       C  
ATOM    231  C   LEU A  32      13.567 -20.771   7.488  1.00 49.94           C  
ANISOU  231  C   LEU A  32     9073   3662   6239    930  -2541    336       C  
ATOM    232  O   LEU A  32      14.389 -20.848   8.408  1.00 46.44           O  
ANISOU  232  O   LEU A  32     8665   3174   5806    930  -2629    383       O  
ATOM    233  CB  LEU A  32      13.691 -18.385   6.736  1.00 40.72           C  
ANISOU  233  CB  LEU A  32     7324   3154   4993   1106  -1699    203       C  
ATOM    234  CG  LEU A  32      12.978 -17.072   6.418  1.00 38.75           C  
ANISOU  234  CG  LEU A  32     6793   3234   4695    986  -1262    235       C  
ATOM    235  CD1 LEU A  32      13.984 -15.988   6.075  1.00 37.30           C  
ANISOU  235  CD1 LEU A  32     6331   3315   4525   1262   -956    111       C  
ATOM    236  CD2 LEU A  32      11.982 -17.269   5.282  1.00 38.01           C  
ANISOU  236  CD2 LEU A  32     6741   3110   4592    996  -1274    180       C  
ATOM    237  N   ASP A  33      13.315 -21.771   6.647  1.00 56.59           N  
ANISOU  237  N   ASP A  33    10117   4239   7147   1073  -2878    224       N  
ATOM    238  CA  ASP A  33      13.889 -23.111   6.827  1.00 60.88           C  
ANISOU  238  CA  ASP A  33    10817   4568   7748   1114  -3300    116       C  
ATOM    239  C   ASP A  33      13.548 -23.550   8.255  1.00 63.53           C  
ANISOU  239  C   ASP A  33    11303   4773   8063    662  -3483    417       C  
ATOM    240  O   ASP A  33      12.378 -23.471   8.644  1.00 61.84           O  
ANISOU  240  O   ASP A  33    11135   4566   7796    263  -3440    672       O  
ATOM    241  CB  ASP A  33      15.370 -23.080   6.484  1.00 59.63           C  
ANISOU  241  CB  ASP A  33    10530   4513   7612   1548  -3281   -174       C  
ATOM    242  CG  ASP A  33      15.625 -22.740   5.031  1.00 60.02           C  
ANISOU  242  CG  ASP A  33    10406   4767   7633   1936  -3096   -454       C  
ATOM    243  OD1 ASP A  33      14.839 -23.180   4.168  1.00 61.79           O  
ANISOU  243  OD1 ASP A  33    10700   4926   7850   1937  -3201   -514       O  
ATOM    244  OD2 ASP A  33      16.613 -22.031   4.752  1.00 60.30           O  
ANISOU  244  OD2 ASP A  33    10217   5054   7640   2220  -2842   -606       O  
ATOM    245  N   ASP A  34      14.521 -24.002   9.049  1.00 67.49           N  
ANISOU  245  N   ASP A  34    11862   5194   8589    697  -3673    392       N  
ATOM    246  CA  ASP A  34      14.252 -24.420  10.421  1.00 70.20           C  
ANISOU  246  CA  ASP A  34    12336   5449   8887    270  -3842    673       C  
ATOM    247  C   ASP A  34      14.861 -23.433  11.410  1.00 68.69           C  
ANISOU  247  C   ASP A  34    12029   5441   8630    240  -3574    785       C  
ATOM    248  O   ASP A  34      15.523 -23.835  12.373  1.00 73.27           O  
ANISOU  248  O   ASP A  34    12687   5944   9208    161  -3756    837       O  
ATOM    249  CB  ASP A  34      14.787 -25.835  10.671  1.00 73.75           C  
ANISOU  249  CB  ASP A  34    12982   5624   9415    277  -4344    583       C  
ATOM    250  CG  ASP A  34      16.296 -25.935  10.519  1.00 74.30           C  
ANISOU  250  CG  ASP A  34    13004   5676   9551    702  -4422    290       C  
ATOM    251  OD1 ASP A  34      16.925 -24.956  10.071  1.00 72.38           O  
ANISOU  251  OD1 ASP A  34    12555   5648   9298   1015  -4083    141       O  
ATOM    252  OD2 ASP A  34      16.855 -27.002  10.852  1.00 77.96           O  
ANISOU  252  OD2 ASP A  34    13624   5923  10076    710  -4834    208       O  
ATOM    253  N   VAL A  35      14.642 -22.140  11.177  1.00 60.60           N  
ANISOU  253  N   VAL A  35    10822   4653   7551    304  -3165    819       N  
ATOM    254  CA  VAL A  35      15.144 -21.087  12.052  1.00 53.38           C  
ANISOU  254  CA  VAL A  35     9755   3960   6568    273  -2884    905       C  
ATOM    255  C   VAL A  35      14.090 -19.996  12.165  1.00 51.55           C  
ANISOU  255  C   VAL A  35     9266   4104   6216    -10  -2431   1011       C  
ATOM    256  O   VAL A  35      13.432 -19.648  11.178  1.00 47.37           O  
ANISOU  256  O   VAL A  35     8619   3680   5700     52  -2243    919       O  
ATOM    257  CB  VAL A  35      16.470 -20.492  11.534  1.00 49.28           C  
ANISOU  257  CB  VAL A  35     9036   3554   6133    760  -2718    616       C  
ATOM    258  CG1 VAL A  35      16.970 -19.416  12.486  1.00 49.63           C  
ANISOU  258  CG1 VAL A  35     8855   3881   6122    688  -2404    670       C  
ATOM    259  CG2 VAL A  35      17.509 -21.581  11.354  1.00 51.37           C  
ANISOU  259  CG2 VAL A  35     9434   3580   6503   1031  -3092    410       C  
ATOM    260  N   VAL A  36      13.940 -19.445  13.366  1.00 55.01           N  
ANISOU  260  N   VAL A  36     9613   4752   6535   -300  -2269   1185       N  
ATOM    261  CA  VAL A  36      13.018 -18.344  13.622  1.00 55.13           C  
ANISOU  261  CA  VAL A  36     9358   5152   6438   -544  -1855   1248       C  
ATOM    262  C   VAL A  36      13.834 -17.133  14.046  1.00 53.36           C  
ANISOU  262  C   VAL A  36     8862   5193   6218   -370  -1540   1132       C  
ATOM    263  O   VAL A  36      14.549 -17.181  15.055  1.00 57.03           O  
ANISOU  263  O   VAL A  36     9376   5643   6649   -399  -1632   1194       O  
ATOM    264  CB  VAL A  36      11.975 -18.703  14.691  1.00 56.86           C  
ANISOU  264  CB  VAL A  36     9668   5453   6485  -1066  -1931   1540       C  
ATOM    265  CG1 VAL A  36      11.178 -17.468  15.088  1.00 54.42           C  
ANISOU  265  CG1 VAL A  36     9034   5591   6053  -1264  -1500   1546       C  
ATOM    266  CG2 VAL A  36      11.052 -19.796  14.177  1.00 58.84           C  
ANISOU  266  CG2 VAL A  36    10149   5457   6752  -1269  -2224   1669       C  
ATOM    267  N   TYR A  37      13.730 -16.055  13.280  1.00 47.98           N  
ANISOU  267  N   TYR A  37     7904   4738   5588   -195  -1195    973       N  
ATOM    268  CA  TYR A  37      14.399 -14.800  13.591  1.00 42.17           C  
ANISOU  268  CA  TYR A  37     6886   4251   4884    -49   -899    871       C  
ATOM    269  C   TYR A  37      13.414 -13.871  14.288  1.00 40.86           C  
ANISOU  269  C   TYR A  37     6513   4405   4607   -350   -635    946       C  
ATOM    270  O   TYR A  37      12.255 -13.764  13.878  1.00 41.85           O  
ANISOU  270  O   TYR A  37     6587   4628   4686   -527   -537    973       O  
ATOM    271  CB  TYR A  37      14.931 -14.133  12.319  1.00 40.77           C  
ANISOU  271  CB  TYR A  37     6521   4133   4837    316   -707    667       C  
ATOM    272  CG  TYR A  37      15.845 -15.011  11.492  1.00 42.37           C  
ANISOU  272  CG  TYR A  37     6881   4090   5129    652   -943    541       C  
ATOM    273  CD1 TYR A  37      15.331 -16.037  10.707  1.00 44.36           C  
ANISOU  273  CD1 TYR A  37     7349   4124   5380    674  -1175    527       C  
ATOM    274  CD2 TYR A  37      17.218 -14.810  11.489  1.00 43.07           C  
ANISOU  274  CD2 TYR A  37     6884   4177   5303    959   -947    414       C  
ATOM    275  CE1 TYR A  37      16.161 -16.845   9.951  1.00 44.54           C  
ANISOU  275  CE1 TYR A  37     7504   3940   5481   1014  -1414    366       C  
ATOM    276  CE2 TYR A  37      18.056 -15.611  10.735  1.00 44.99           C  
ANISOU  276  CE2 TYR A  37     7240   4239   5616   1290  -1164    258       C  
ATOM    277  CZ  TYR A  37      17.522 -16.625   9.968  1.00 45.11           C  
ANISOU  277  CZ  TYR A  37     7472   4046   5622   1328  -1402    222       C  
ATOM    278  OH  TYR A  37      18.357 -17.421   9.219  1.00 46.50           O  
ANISOU  278  OH  TYR A  37     7747   4059   5863   1690  -1641     23       O  
ATOM    279  N   CYS A  38      13.876 -13.201  15.337  1.00 41.17           N  
ANISOU  279  N   CYS A  38     6422   4614   4606   -392   -534    954       N  
ATOM    280  CA  CYS A  38      13.047 -12.248  16.059  1.00 39.24           C  
ANISOU  280  CA  CYS A  38     5950   4705   4255   -627   -296    971       C  
ATOM    281  C   CYS A  38      13.952 -11.234  16.739  1.00 37.36           C  
ANISOU  281  C   CYS A  38     5510   4614   4070   -474   -162    872       C  
ATOM    282  O   CYS A  38      15.145 -11.492  16.931  1.00 39.32           O  
ANISOU  282  O   CYS A  38     5843   4701   4395   -275   -294    850       O  
ATOM    283  CB  CYS A  38      12.153 -12.950  17.089  1.00 43.61           C  
ANISOU  283  CB  CYS A  38     6643   5340   4588  -1043   -421   1176       C  
ATOM    284  SG  CYS A  38      13.043 -13.747  18.455  1.00 46.93           S  
ANISOU  284  SG  CYS A  38     7301   5637   4894  -1149   -704   1341       S  
ATOM    285  N   PRO A  39      13.421 -10.064  17.100  1.00 35.19           N  
ANISOU  285  N   PRO A  39     4960   4638   3774   -548     76    793       N  
ATOM    286  CA  PRO A  39      14.208  -9.121  17.909  1.00 35.29           C  
ANISOU  286  CA  PRO A  39     4788   4787   3834   -434    160    703       C  
ATOM    287  C   PRO A  39      14.576  -9.735  19.253  1.00 37.64           C  
ANISOU  287  C   PRO A  39     5246   5087   3967   -591    -14    822       C  
ATOM    288  O   PRO A  39      13.774 -10.427  19.883  1.00 39.90           O  
ANISOU  288  O   PRO A  39     5668   5453   4041   -902   -102    973       O  
ATOM    289  CB  PRO A  39      13.270  -7.917  18.069  1.00 35.83           C  
ANISOU  289  CB  PRO A  39     4560   5170   3885   -530    391    591       C  
ATOM    290  CG  PRO A  39      12.272  -8.047  16.950  1.00 37.49           C  
ANISOU  290  CG  PRO A  39     4766   5360   4120   -582    462    586       C  
ATOM    291  CD  PRO A  39      12.098  -9.521  16.740  1.00 36.67           C  
ANISOU  291  CD  PRO A  39     4980   5036   3917   -709    254    752       C  
ATOM    292  N   ARG A  40      15.807  -9.478  19.695  1.00 34.27           N  
ANISOU  292  N   ARG A  40     4802   4583   3637   -386    -74    767       N  
ATOM    293  CA  ARG A  40      16.301 -10.139  20.893  1.00 36.66           C  
ANISOU  293  CA  ARG A  40     5292   4838   3798   -501   -281    883       C  
ATOM    294  C   ARG A  40      15.701  -9.566  22.169  1.00 37.06           C  
ANISOU  294  C   ARG A  40     5209   5234   3638   -737   -188    895       C  
ATOM    295  O   ARG A  40      15.766 -10.221  23.215  1.00 40.12           O  
ANISOU  295  O   ARG A  40     5771   5645   3826   -932   -354   1041       O  
ATOM    296  CB  ARG A  40      17.827 -10.055  20.961  1.00 38.28           C  
ANISOU  296  CB  ARG A  40     5511   4851   4181   -193   -387    801       C  
ATOM    297  CG  ARG A  40      18.359  -8.654  21.178  1.00 39.83           C  
ANISOU  297  CG  ARG A  40     5393   5221   4519    -12   -198    633       C  
ATOM    298  CD  ARG A  40      19.851  -8.676  21.425  1.00 38.04           C  
ANISOU  298  CD  ARG A  40     5188   4820   4446    246   -331    576       C  
ATOM    299  NE  ARG A  40      20.407  -7.332  21.509  1.00 32.31           N  
ANISOU  299  NE  ARG A  40     4153   4225   3898    422   -172    426       N  
ATOM    300  CZ  ARG A  40      21.676  -7.073  21.798  1.00 34.37           C  
ANISOU  300  CZ  ARG A  40     4354   4390   4314    639   -250    357       C  
ATOM    301  NH1 ARG A  40      22.517  -8.072  22.036  1.00 35.81           N  
ANISOU  301  NH1 ARG A  40     4764   4353   4491    722   -483    405       N  
ATOM    302  NH2 ARG A  40      22.102  -5.819  21.853  1.00 32.96           N  
ANISOU  302  NH2 ARG A  40     3887   4323   4313    770   -123    238       N  
ATOM    303  N   HIS A  41      15.111  -8.374  22.113  1.00 36.39           N  
ANISOU  303  N   HIS A  41     4819   5426   3583   -722     53    740       N  
ATOM    304  CA  HIS A  41      14.516  -7.842  23.337  1.00 37.10           C  
ANISOU  304  CA  HIS A  41     4760   5885   3452   -920    131    707       C  
ATOM    305  C   HIS A  41      13.239  -8.552  23.713  1.00 37.73           C  
ANISOU  305  C   HIS A  41     4926   6172   3238  -1303    127    866       C  
ATOM    306  O   HIS A  41      12.574  -8.109  24.656  1.00 40.58           O  
ANISOU  306  O   HIS A  41     5124   6918   3376  -1487    223    824       O  
ATOM    307  CB  HIS A  41      14.270  -6.335  23.222  1.00 38.68           C  
ANISOU  307  CB  HIS A  41     4597   6313   3785   -769    343    459       C  
ATOM    308  CG  HIS A  41      13.305  -5.937  22.147  1.00 36.91           C  
ANISOU  308  CG  HIS A  41     4234   6137   3655   -778    498    384       C  
ATOM    309  ND1 HIS A  41      11.968  -6.268  22.181  1.00 39.02           N  
ANISOU  309  ND1 HIS A  41     4487   6620   3720  -1055    563    434       N  
ATOM    310  CD2 HIS A  41      13.480  -5.195  21.027  1.00 34.83           C  
ANISOU  310  CD2 HIS A  41     3827   5748   3660   -551    592    267       C  
ATOM    311  CE1 HIS A  41      11.365  -5.765  21.118  1.00 36.85           C  
ANISOU  311  CE1 HIS A  41     4077   6326   3598   -980    683    334       C  
ATOM    312  NE2 HIS A  41      12.261  -5.110  20.401  1.00 35.51           N  
ANISOU  312  NE2 HIS A  41     3836   5950   3708   -680    699    240       N  
ATOM    313  N   VAL A  42      12.897  -9.633  23.006  1.00 38.10           N  
ANISOU  313  N   VAL A  42     5209   5989   3280  -1423      9   1038       N  
ATOM    314  CA  VAL A  42      11.802 -10.495  23.426  1.00 44.46           C  
ANISOU  314  CA  VAL A  42     6138   6946   3810  -1828    -53   1249       C  
ATOM    315  C   VAL A  42      12.098 -11.140  24.772  1.00 49.45           C  
ANISOU  315  C   VAL A  42     6945   7664   4181  -2060   -233   1446       C  
ATOM    316  O   VAL A  42      11.171 -11.532  25.489  1.00 51.82           O  
ANISOU  316  O   VAL A  42     7253   8255   4182  -2437   -230   1609       O  
ATOM    317  CB  VAL A  42      11.531 -11.570  22.349  1.00 42.98           C  
ANISOU  317  CB  VAL A  42     6196   6415   3718  -1876   -206   1393       C  
ATOM    318  CG1 VAL A  42      12.684 -12.562  22.278  1.00 43.83           C  
ANISOU  318  CG1 VAL A  42     6630   6095   3928  -1741   -512   1509       C  
ATOM    319  CG2 VAL A  42      10.217 -12.289  22.626  1.00 43.69           C  
ANISOU  319  CG2 VAL A  42     6350   6688   3563  -2313   -238   1600       C  
ATOM    320  N   ILE A  43      13.372 -11.257  25.139  1.00 50.18           N  
ANISOU  320  N   ILE A  43     7171   7527   4368  -1853   -393   1440       N  
ATOM    321  CA  ILE A  43      13.746 -11.930  26.376  1.00 53.40           C  
ANISOU  321  CA  ILE A  43     7784   7965   4541  -2057   -608   1640       C  
ATOM    322  C   ILE A  43      13.780 -10.926  27.521  1.00 51.25           C  
ANISOU  322  C   ILE A  43     7263   8114   4094  -2059   -451   1502       C  
ATOM    323  O   ILE A  43      14.247 -11.243  28.621  1.00 51.30           O  
ANISOU  323  O   ILE A  43     7399   8185   3909  -2167   -604   1619       O  
ATOM    324  CB  ILE A  43      15.104 -12.640  26.236  1.00 56.52           C  
ANISOU  324  CB  ILE A  43     8463   7887   5125  -1828   -904   1693       C  
ATOM    325  CG1 ILE A  43      16.246 -11.622  26.224  1.00 56.76           C  
ANISOU  325  CG1 ILE A  43     8306   7877   5385  -1423   -808   1431       C  
ATOM    326  CG2 ILE A  43      15.141 -13.466  24.965  1.00 56.68           C  
ANISOU  326  CG2 ILE A  43     8675   7503   5356  -1728  -1048   1738       C  
ATOM    327  CD1 ILE A  43      17.616 -12.244  26.071  1.00 58.66           C  
ANISOU  327  CD1 ILE A  43     8773   7692   5822  -1167  -1081   1440       C  
ATOM    328  N   CYS A  44      13.301  -9.714  27.273  1.00 49.39           N  
ANISOU  328  N   CYS A  44     6678   8158   3929  -1928   -173   1242       N  
ATOM    329  CA  CYS A  44      13.307  -8.670  28.283  1.00 50.02           C  
ANISOU  329  CA  CYS A  44     6494   8636   3877  -1880    -41   1050       C  
ATOM    330  C   CYS A  44      11.923  -8.486  28.888  1.00 56.79           C  
ANISOU  330  C   CYS A  44     7154  10032   4390  -2207    124   1051       C  
ATOM    331  O   CYS A  44      10.902  -8.644  28.220  1.00 57.27           O  
ANISOU  331  O   CYS A  44     7150  10174   4435  -2361    231   1080       O  
ATOM    332  CB  CYS A  44      13.774  -7.339  27.691  1.00 44.99           C  
ANISOU  332  CB  CYS A  44     5575   7949   3570  -1490    112    728       C  
ATOM    333  SG  CYS A  44      15.507  -7.320  27.262  1.00 48.68           S  
ANISOU  333  SG  CYS A  44     6176   7924   4396  -1104    -49    689       S  
ATOM    334  N   THR A  45      11.906  -8.162  30.175  1.00 64.31           N  
ANISOU  334  N   THR A  45     8003  11376   5056  -2307    139   1010       N  
ATOM    335  CA  THR A  45      10.721  -7.604  30.801  1.00 73.11           C  
ANISOU  335  CA  THR A  45     8804  13028   5945  -2469    322    860       C  
ATOM    336  C   THR A  45      10.735  -6.088  30.616  1.00 80.24           C  
ANISOU  336  C   THR A  45     9345  14150   6991  -2153    509    459       C  
ATOM    337  O   THR A  45      11.704  -5.507  30.121  1.00 76.52           O  
ANISOU  337  O   THR A  45     8868  13334   6874  -1802    464    313       O  
ATOM    338  CB  THR A  45      10.667  -7.979  32.277  1.00 75.18           C  
ANISOU  338  CB  THR A  45     9091  13546   5927  -2667    225    958       C  
ATOM    339  OG1 THR A  45      11.864  -7.546  32.926  1.00 75.80           O  
ANISOU  339  OG1 THR A  45     9230  13633   5939  -2470    143    889       O  
ATOM    340  CG2 THR A  45      10.541  -9.482  32.431  1.00 77.11           C  
ANISOU  340  CG2 THR A  45     9666  13550   6084  -2989     20   1343       C  
ATOM    341  N   SER A  46       9.639  -5.441  31.010  1.00 91.52           N  
ANISOU  341  N   SER A  46    10456  15920   8396  -2178    614    231       N  
ATOM    342  CA  SER A  46       9.549  -3.996  30.839  1.00 96.79           C  
ANISOU  342  CA  SER A  46    10784  16732   9259  -1866    721   -168       C  
ATOM    343  C   SER A  46      10.646  -3.284  31.620  1.00 98.13           C  
ANISOU  343  C   SER A  46    10887  17011   9386  -1636    683   -339       C  
ATOM    344  O   SER A  46      11.187  -2.270  31.162  1.00 97.92           O  
ANISOU  344  O   SER A  46    10705  16822   9679  -1303    692   -592       O  
ATOM    345  CB  SER A  46       8.169  -3.506  31.273  1.00101.06           C  
ANISOU  345  CB  SER A  46    11039  17620   9739  -1941    758   -371       C  
ATOM    346  OG  SER A  46       7.153  -4.279  30.660  1.00102.29           O  
ANISOU  346  OG  SER A  46    11275  17704   9886  -2173    768   -202       O  
ATOM    347  N   GLU A  47      10.998  -3.809  32.798  1.00 96.80           N  
ANISOU  347  N   GLU A  47    10850  17006   8924  -1783    582   -198       N  
ATOM    348  CA  GLU A  47      12.051  -3.204  33.607  1.00 91.70           C  
ANISOU  348  CA  GLU A  47    10174  16419   8250  -1551    492   -359       C  
ATOM    349  C   GLU A  47      13.425  -3.390  32.977  1.00 81.35           C  
ANISOU  349  C   GLU A  47     9103  14467   7341  -1306    331   -253       C  
ATOM    350  O   GLU A  47      14.313  -2.551  33.169  1.00 81.65           O  
ANISOU  350  O   GLU A  47     9037  14366   7621   -992    257   -464       O  
ATOM    351  CB  GLU A  47      12.036  -3.814  35.010  1.00 97.12           C  
ANISOU  351  CB  GLU A  47    10961  17372   8567  -1779    400   -201       C  
ATOM    352  CG  GLU A  47      12.468  -5.274  35.031  1.00 99.62           C  
ANISOU  352  CG  GLU A  47    11705  17399   8746  -2051    245    250       C  
ATOM    353  CD  GLU A  47      11.932  -6.039  36.226  1.00104.97           C  
ANISOU  353  CD  GLU A  47    12441  18309   9132  -2369    191    455       C  
ATOM    354  OE1 GLU A  47      11.819  -5.445  37.320  1.00107.15           O  
ANISOU  354  OE1 GLU A  47    12510  18958   9245  -2318    222    268       O  
ATOM    355  OE2 GLU A  47      11.618  -7.238  36.068  1.00106.45           O  
ANISOU  355  OE2 GLU A  47    12875  18308   9262  -2668    106    796       O  
ATOM    356  N   ASP A  48      13.622  -4.479  32.230  1.00 70.95           N  
ANISOU  356  N   ASP A  48     8091  12765   6102  -1439    262     60       N  
ATOM    357  CA  ASP A  48      14.929  -4.769  31.658  1.00 61.48           C  
ANISOU  357  CA  ASP A  48     7112  11004   5244  -1211    103    153       C  
ATOM    358  C   ASP A  48      15.291  -3.825  30.522  1.00 55.80           C  
ANISOU  358  C   ASP A  48     6209  10009   4985   -880    180    -59       C  
ATOM    359  O   ASP A  48      16.481  -3.640  30.243  1.00 48.44           O  
ANISOU  359  O   ASP A  48     5335   8723   4347   -623     74    -82       O  
ATOM    360  CB  ASP A  48      14.971  -6.211  31.144  1.00 60.24           C  
ANISOU  360  CB  ASP A  48     7320  10529   5040  -1427    -19    509       C  
ATOM    361  CG  ASP A  48      15.082  -7.226  32.261  1.00 64.51           C  
ANISOU  361  CG  ASP A  48     8124  11176   5210  -1714   -198    778       C  
ATOM    362  OD1 ASP A  48      15.830  -6.968  33.229  1.00 66.45           O  
ANISOU  362  OD1 ASP A  48     8381  11491   5377  -1614   -304    717       O  
ATOM    363  OD2 ASP A  48      14.425  -8.284  32.167  1.00 66.48           O  
ANISOU  363  OD2 ASP A  48     8577  11430   5252  -2047   -253   1062       O  
ATOM    364  N   MET A  49      14.299  -3.224  29.863  1.00 59.54           N  
ANISOU  364  N   MET A  49     6454  10645   5522   -889    352   -205       N  
ATOM    365  CA  MET A  49      14.567  -2.456  28.656  1.00 60.58           C  
ANISOU  365  CA  MET A  49     6450  10492   6075   -627    408   -341       C  
ATOM    366  C   MET A  49      15.361  -1.185  28.928  1.00 62.89           C  
ANISOU  366  C   MET A  49     6515  10744   6636   -313    360   -603       C  
ATOM    367  O   MET A  49      15.917  -0.609  27.987  1.00 59.49           O  
ANISOU  367  O   MET A  49     6010  10015   6578    -94    359   -658       O  
ATOM    368  CB  MET A  49      13.251  -2.104  27.960  1.00 60.16           C  
ANISOU  368  CB  MET A  49     6212  10633   6012   -724    574   -440       C  
ATOM    369  CG  MET A  49      12.627  -3.260  27.201  1.00 61.13           C  
ANISOU  369  CG  MET A  49     6557  10636   6032   -963    607   -181       C  
ATOM    370  SD  MET A  49      13.705  -3.912  25.905  1.00 63.22           S  
ANISOU  370  SD  MET A  49     7090  10304   6628   -787    511      7       S  
ATOM    371  CE  MET A  49      14.045  -2.448  24.923  1.00 59.81           C  
ANISOU  371  CE  MET A  49     6370   9731   6624   -448    597   -243       C  
ATOM    372  N   LEU A  50      15.441  -0.738  30.183  1.00 67.55           N  
ANISOU  372  N   LEU A  50     6991  11630   7044   -293    305   -759       N  
ATOM    373  CA  LEU A  50      16.153   0.502  30.472  1.00 70.50           C  
ANISOU  373  CA  LEU A  50     7140  11956   7692      7    224  -1026       C  
ATOM    374  C   LEU A  50      17.656   0.319  30.303  1.00 66.44           C  
ANISOU  374  C   LEU A  50     6783  11018   7445    191     81   -909       C  
ATOM    375  O   LEU A  50      18.327   1.148  29.677  1.00 66.38           O  
ANISOU  375  O   LEU A  50     6635  10759   7828    426     45  -1009       O  
ATOM    376  CB  LEU A  50      15.826   0.985  31.882  1.00 81.49           C  
ANISOU  376  CB  LEU A  50     8369  13798   8796     -4    186  -1248       C  
ATOM    377  CG  LEU A  50      15.749   2.507  32.027  1.00 87.44           C  
ANISOU  377  CG  LEU A  50     8769  14661   9792    264    143  -1636       C  
ATOM    378  CD1 LEU A  50      17.023   3.179  31.526  1.00 86.45           C  
ANISOU  378  CD1 LEU A  50     8618  14080  10148    547      5  -1665       C  
ATOM    379  CD2 LEU A  50      14.526   3.039  31.286  1.00 88.05           C  
ANISOU  379  CD2 LEU A  50     8630  14897   9927    231    274  -1791       C  
ATOM    380  N   ASN A  51      18.206  -0.758  30.857  1.00 64.97           N  
ANISOU  380  N   ASN A  51     6877  10752   7055     78    -18   -694       N  
ATOM    381  CA  ASN A  51      19.631  -1.061  30.721  1.00 62.26           C  
ANISOU  381  CA  ASN A  51     6691  10019   6947    252   -168   -592       C  
ATOM    382  C   ASN A  51      19.804  -2.570  30.730  1.00 57.17           C  
ANISOU  382  C   ASN A  51     6410   9219   6094     61   -251   -292       C  
ATOM    383  O   ASN A  51      20.225  -3.166  31.729  1.00 61.12           O  
ANISOU  383  O   ASN A  51     7090   9755   6377    -16   -401   -199       O  
ATOM    384  CB  ASN A  51      20.449  -0.407  31.834  1.00 66.17           C  
ANISOU  384  CB  ASN A  51     7089  10577   7475    422   -315   -761       C  
ATOM    385  CG  ASN A  51      21.840  -0.017  31.377  1.00 68.13           C  
ANISOU  385  CG  ASN A  51     7305  10437   8143    695   -426   -783       C  
ATOM    386  OD1 ASN A  51      22.013   0.558  30.303  1.00 67.36           O  
ANISOU  386  OD1 ASN A  51     7062  10151   8379    824   -357   -816       O  
ATOM    387  ND2 ASN A  51      22.842  -0.347  32.181  1.00 71.53           N  
ANISOU  387  ND2 ASN A  51     7867  10761   8551    772   -605   -751       N  
ATOM    388  N   PRO A  52      19.480  -3.230  29.623  1.00 48.01           N  
ANISOU  388  N   PRO A  52     5373   7870   4999    -16   -186   -137       N  
ATOM    389  CA  PRO A  52      19.538  -4.696  29.601  1.00 47.09           C  
ANISOU  389  CA  PRO A  52     5608   7586   4698   -203   -307    138       C  
ATOM    390  C   PRO A  52      20.935  -5.216  29.307  1.00 45.53           C  
ANISOU  390  C   PRO A  52     5589   6979   4733      3   -490    208       C  
ATOM    391  O   PRO A  52      21.634  -4.716  28.422  1.00 43.93           O  
ANISOU  391  O   PRO A  52     5260   6561   4869    253   -450    114       O  
ATOM    392  CB  PRO A  52      18.565  -5.062  28.472  1.00 44.90           C  
ANISOU  392  CB  PRO A  52     5351   7282   4426   -335   -170    223       C  
ATOM    393  CG  PRO A  52      18.671  -3.902  27.522  1.00 42.25           C  
ANISOU  393  CG  PRO A  52     4734   6887   4432    -93    -24     25       C  
ATOM    394  CD  PRO A  52      18.938  -2.673  28.369  1.00 42.46           C  
ANISOU  394  CD  PRO A  52     4497   7114   4520     50    -19   -209       C  
ATOM    395  N   ASN A  53      21.338  -6.234  30.062  1.00 47.69           N  
ANISOU  395  N   ASN A  53     6150   7158   4813   -111   -705    377       N  
ATOM    396  CA  ASN A  53      22.525  -7.026  29.736  1.00 48.94           C  
ANISOU  396  CA  ASN A  53     6529   6912   5154     53   -920    460       C  
ATOM    397  C   ASN A  53      22.024  -8.266  28.996  1.00 47.50           C  
ANISOU  397  C   ASN A  53     6614   6543   4892   -114   -993    667       C  
ATOM    398  O   ASN A  53      21.672  -9.278  29.605  1.00 47.98           O  
ANISOU  398  O   ASN A  53     6948   6597   4687   -371  -1169    876       O  
ATOM    399  CB  ASN A  53      23.314  -7.381  30.989  1.00 54.41           C  
ANISOU  399  CB  ASN A  53     7387   7568   5718     53  -1163    505       C  
ATOM    400  CG  ASN A  53      24.672  -7.980  30.670  1.00 56.41           C  
ANISOU  400  CG  ASN A  53     7802   7411   6222    293  -1393    516       C  
ATOM    401  OD1 ASN A  53      24.781  -8.923  29.885  1.00 55.35           O  
ANISOU  401  OD1 ASN A  53     7864   7011   6154    299  -1497    624       O  
ATOM    402  ND2 ASN A  53      25.718  -7.426  31.271  1.00 59.29           N  
ANISOU  402  ND2 ASN A  53     8069   7726   6732    508  -1487    381       N  
ATOM    403  N   TYR A  54      21.991  -8.178  27.661  1.00 43.82           N  
ANISOU  403  N   TYR A  54     6067   5924   4659     27   -876    614       N  
ATOM    404  CA  TYR A  54      21.367  -9.228  26.859  1.00 45.06           C  
ANISOU  404  CA  TYR A  54     6439   5930   4753   -117   -928    772       C  
ATOM    405  C   TYR A  54      22.081 -10.564  27.009  1.00 48.21           C  
ANISOU  405  C   TYR A  54     7193   5988   5138   -110  -1268    919       C  
ATOM    406  O   TYR A  54      21.442 -11.619  26.930  1.00 49.42           O  
ANISOU  406  O   TYR A  54     7601   6044   5131   -344  -1414   1112       O  
ATOM    407  CB  TYR A  54      21.323  -8.810  25.387  1.00 45.68           C  
ANISOU  407  CB  TYR A  54     6351   5919   5088     79   -747    660       C  
ATOM    408  CG  TYR A  54      20.222  -7.822  25.072  1.00 46.52           C  
ANISOU  408  CG  TYR A  54     6191   6319   5165    -18   -463    576       C  
ATOM    409  CD1 TYR A  54      18.891  -8.220  25.065  1.00 46.56           C  
ANISOU  409  CD1 TYR A  54     6260   6490   4940   -315   -398    686       C  
ATOM    410  CD2 TYR A  54      20.508  -6.493  24.782  1.00 43.48           C  
ANISOU  410  CD2 TYR A  54     5486   6038   4997    183   -286    386       C  
ATOM    411  CE1 TYR A  54      17.877  -7.324  24.781  1.00 44.37           C  
ANISOU  411  CE1 TYR A  54     5729   6483   4646   -385   -159    581       C  
ATOM    412  CE2 TYR A  54      19.499  -5.590  24.494  1.00 41.17           C  
ANISOU  412  CE2 TYR A  54     4958   5985   4698    109    -73    293       C  
ATOM    413  CZ  TYR A  54      18.186  -6.012  24.496  1.00 41.21           C  
ANISOU  413  CZ  TYR A  54     5027   6161   4470   -163     -7    376       C  
ATOM    414  OH  TYR A  54      17.174  -5.122  24.212  1.00 40.45           O  
ANISOU  414  OH  TYR A  54     4687   6305   4376   -220    187    257       O  
ATOM    415  N   GLU A  55      23.397 -10.551  27.221  1.00 52.65           N  
ANISOU  415  N   GLU A  55     7774   6350   5881    154  -1425    827       N  
ATOM    416  CA  GLU A  55      24.114 -11.798  27.464  1.00 60.23           C  
ANISOU  416  CA  GLU A  55     9071   6977   6838    180  -1795    938       C  
ATOM    417  C   GLU A  55      23.619 -12.469  28.740  1.00 55.37           C  
ANISOU  417  C   GLU A  55     8712   6438   5887   -168  -1999   1169       C  
ATOM    418  O   GLU A  55      23.154 -13.615  28.716  1.00 57.35           O  
ANISOU  418  O   GLU A  55     9262   6525   6003   -391  -2224   1382       O  
ATOM    419  CB  GLU A  55      25.614 -11.526  27.543  1.00 73.24           C  
ANISOU  419  CB  GLU A  55    10642   8446   8741    535  -1910    766       C  
ATOM    420  CG  GLU A  55      26.303 -11.484  26.196  1.00 83.22           C  
ANISOU  420  CG  GLU A  55    11777   9534  10307    863  -1851    604       C  
ATOM    421  CD  GLU A  55      27.655 -10.807  26.268  1.00 92.48           C  
ANISOU  421  CD  GLU A  55    12739  10665  11735   1188  -1850    414       C  
ATOM    422  OE1 GLU A  55      27.694  -9.558  26.260  1.00 94.19           O  
ANISOU  422  OE1 GLU A  55    12638  11098  12051   1250  -1594    309       O  
ATOM    423  OE2 GLU A  55      28.677 -11.523  26.352  1.00 96.85           O  
ANISOU  423  OE2 GLU A  55    13437  10962  12398   1378  -2129    366       O  
ATOM    424  N   ASP A  56      23.704 -11.762  29.870  1.00 50.03           N  
ANISOU  424  N   ASP A  56     7920   6022   5068   -228  -1938   1137       N  
ATOM    425  CA  ASP A  56      23.292 -12.346  31.143  1.00 51.86           C  
ANISOU  425  CA  ASP A  56     8377   6385   4943   -563  -2123   1363       C  
ATOM    426  C   ASP A  56      21.828 -12.768  31.114  1.00 52.75           C  
ANISOU  426  C   ASP A  56     8555   6725   4764   -969  -2026   1575       C  
ATOM    427  O   ASP A  56      21.459 -13.791  31.704  1.00 54.41           O  
ANISOU  427  O   ASP A  56     9061   6888   4724  -1288  -2271   1855       O  
ATOM    428  CB  ASP A  56      23.531 -11.353  32.281  1.00 52.79           C  
ANISOU  428  CB  ASP A  56     8299   6818   4939   -533  -2022   1244       C  
ATOM    429  CG  ASP A  56      24.998 -11.235  32.663  1.00 53.19           C  
ANISOU  429  CG  ASP A  56     8381   6622   5207   -220  -2230   1114       C  
ATOM    430  OD1 ASP A  56      25.861 -11.678  31.875  1.00 52.08           O  
ANISOU  430  OD1 ASP A  56     8319   6110   5360     33  -2375   1052       O  
ATOM    431  OD2 ASP A  56      25.283 -10.708  33.760  1.00 53.96           O  
ANISOU  431  OD2 ASP A  56     8414   6915   5174   -220  -2255   1060       O  
ATOM    432  N   LEU A  57      20.975 -11.989  30.446  1.00 51.75           N  
ANISOU  432  N   LEU A  57     8148   6846   4668   -977  -1686   1455       N  
ATOM    433  CA  LEU A  57      19.563 -12.345  30.356  1.00 55.75           C  
ANISOU  433  CA  LEU A  57     8678   7586   4920  -1350  -1579   1632       C  
ATOM    434  C   LEU A  57      19.379 -13.637  29.570  1.00 61.31           C  
ANISOU  434  C   LEU A  57     9689   7918   5688  -1459  -1814   1833       C  
ATOM    435  O   LEU A  57      18.697 -14.564  30.022  1.00 62.71           O  
ANISOU  435  O   LEU A  57    10100   8118   5610  -1837  -1990   2121       O  
ATOM    436  CB  LEU A  57      18.774 -11.210  29.705  1.00 52.10           C  
ANISOU  436  CB  LEU A  57     7846   7418   4531  -1281  -1195   1421       C  
ATOM    437  CG  LEU A  57      18.494  -9.979  30.567  1.00 52.24           C  
ANISOU  437  CG  LEU A  57     7549   7892   4408  -1274   -971   1238       C  
ATOM    438  CD1 LEU A  57      17.802  -8.897  29.740  1.00 51.45           C  
ANISOU  438  CD1 LEU A  57     7105   7983   4459  -1157   -654   1011       C  
ATOM    439  CD2 LEU A  57      17.657 -10.347  31.787  1.00 53.98           C  
ANISOU  439  CD2 LEU A  57     7835   8506   4168  -1677   -999   1426       C  
ATOM    440  N   LEU A  58      19.983 -13.712  28.381  1.00 64.57           N  
ANISOU  440  N   LEU A  58    10098   7997   6439  -1134  -1835   1685       N  
ATOM    441  CA  LEU A  58      19.815 -14.882  27.529  1.00 67.57           C  
ANISOU  441  CA  LEU A  58    10746   8020   6908  -1179  -2068   1816       C  
ATOM    442  C   LEU A  58      20.329 -16.147  28.202  1.00 66.27           C  
ANISOU  442  C   LEU A  58    10979   7536   6664  -1310  -2533   2044       C  
ATOM    443  O   LEU A  58      19.813 -17.240  27.947  1.00 72.58           O  
ANISOU  443  O   LEU A  58    12048   8120   7409  -1535  -2784   2259       O  
ATOM    444  CB  LEU A  58      20.540 -14.665  26.202  1.00 69.81           C  
ANISOU  444  CB  LEU A  58    10924   8051   7549   -753  -2008   1573       C  
ATOM    445  CG  LEU A  58      20.329 -15.736  25.131  1.00 72.35           C  
ANISOU  445  CG  LEU A  58    11468   8035   7986   -728  -2215   1631       C  
ATOM    446  CD1 LEU A  58      18.909 -15.680  24.584  1.00 71.91           C  
ANISOU  446  CD1 LEU A  58    11337   8170   7814   -990  -2010   1719       C  
ATOM    447  CD2 LEU A  58      21.349 -15.575  24.013  1.00 71.50           C  
ANISOU  447  CD2 LEU A  58    11263   7704   8198   -261  -2203   1370       C  
ATOM    448  N   ILE A  59      21.340 -16.020  29.062  1.00 60.32           N  
ANISOU  448  N   ILE A  59    10275   6728   5917  -1176  -2684   2002       N  
ATOM    449  CA  ILE A  59      21.922 -17.194  29.699  1.00 59.17           C  
ANISOU  449  CA  ILE A  59    10511   6244   5728  -1270  -3160   2197       C  
ATOM    450  C   ILE A  59      20.933 -17.851  30.651  1.00 64.44           C  
ANISOU  450  C   ILE A  59    11255   7106   6124  -1767  -3173   2442       C  
ATOM    451  O   ILE A  59      20.929 -19.079  30.798  1.00 67.49           O  
ANISOU  451  O   ILE A  59    11859   7205   6579  -1926  -3457   2549       O  
ATOM    452  CB  ILE A  59      23.226 -16.807  30.420  1.00 57.76           C  
ANISOU  452  CB  ILE A  59    10315   5992   5641   -994  -3279   2054       C  
ATOM    453  CG1 ILE A  59      24.316 -16.516  29.387  1.00 65.40           C  
ANISOU  453  CG1 ILE A  59    11141   6701   7007   -485  -3252   1735       C  
ATOM    454  CG2 ILE A  59      23.639 -17.905  31.385  1.00 61.70           C  
ANISOU  454  CG2 ILE A  59    11077   6269   6099  -1165  -3620   2184       C  
ATOM    455  CD1 ILE A  59      25.545 -15.856  29.955  1.00 74.20           C  
ANISOU  455  CD1 ILE A  59    12121   7815   8255   -186  -3264   1539       C  
ATOM    456  N   ARG A  60      20.092 -17.064  31.316  1.00 67.38           N  
ANISOU  456  N   ARG A  60    11430   7979   6193  -2015  -2882   2512       N  
ATOM    457  CA  ARG A  60      19.104 -17.633  32.222  1.00 76.67           C  
ANISOU  457  CA  ARG A  60    12620   9397   7114  -2474  -2862   2726       C  
ATOM    458  C   ARG A  60      17.910 -18.230  31.489  1.00 75.27           C  
ANISOU  458  C   ARG A  60    12428   9217   6955  -2727  -2799   2826       C  
ATOM    459  O   ARG A  60      17.060 -18.854  32.133  1.00 76.42           O  
ANISOU  459  O   ARG A  60    12587   9519   6930  -3120  -2831   3012       O  
ATOM    460  CB  ARG A  60      18.637 -16.565  33.215  1.00 85.79           C  
ANISOU  460  CB  ARG A  60    13518  11134   7943  -2609  -2561   2703       C  
ATOM    461  CG  ARG A  60      19.786 -15.861  33.935  1.00 95.06           C  
ANISOU  461  CG  ARG A  60    14683  12345   9089  -2346  -2626   2577       C  
ATOM    462  CD  ARG A  60      19.335 -15.215  35.240  1.00106.31           C  
ANISOU  462  CD  ARG A  60    15921  14312  10160  -2544  -2435   2584       C  
ATOM    463  NE  ARG A  60      18.136 -14.397  35.067  1.00113.81           N  
ANISOU  463  NE  ARG A  60    16548  15762  10931  -2685  -2051   2499       N  
ATOM    464  CZ  ARG A  60      18.140 -13.110  34.728  1.00116.69           C  
ANISOU  464  CZ  ARG A  60    16644  16412  11279  -2472  -1804   2256       C  
ATOM    465  NH1 ARG A  60      19.284 -12.471  34.517  1.00116.47           N  
ANISOU  465  NH1 ARG A  60    16538  16152  11563  -2041  -1823   1996       N  
ATOM    466  NH2 ARG A  60      16.992 -12.459  34.598  1.00117.88           N  
ANISOU  466  NH2 ARG A  60    16490  17004  11296  -2603  -1470   2153       N  
ATOM    467  N   LYS A  61      17.837 -18.068  30.167  1.00 73.66           N  
ANISOU  467  N   LYS A  61    12192   8840   6956  -2512  -2730   2707       N  
ATOM    468  CA  LYS A  61      16.766 -18.638  29.362  1.00 75.74           C  
ANISOU  468  CA  LYS A  61    12451   9060   7267  -2708  -2699   2776       C  
ATOM    469  C   LYS A  61      17.194 -19.988  28.798  1.00 79.85           C  
ANISOU  469  C   LYS A  61    13259   9041   8039  -2650  -3103   2804       C  
ATOM    470  O   LYS A  61      18.345 -20.165  28.385  1.00 79.09           O  
ANISOU  470  O   LYS A  61    13294   8588   8168  -2293  -3304   2661       O  
ATOM    471  CB  LYS A  61      16.394 -17.704  28.206  1.00 70.96           C  
ANISOU  471  CB  LYS A  61    11648   8579   6736  -2508  -2399   2621       C  
ATOM    472  CG  LYS A  61      16.001 -16.299  28.623  1.00 68.80           C  
ANISOU  472  CG  LYS A  61    11062   8833   6244  -2526  -2011   2529       C  
ATOM    473  CD  LYS A  61      14.608 -16.257  29.226  1.00 71.48           C  
ANISOU  473  CD  LYS A  61    11201   9618   6341  -2926  -1798   2613       C  
ATOM    474  CE  LYS A  61      14.237 -14.841  29.647  1.00 70.76           C  
ANISOU  474  CE  LYS A  61    10761  10068   6058  -2896  -1422   2442       C  
ATOM    475  NZ  LYS A  61      12.806 -14.723  30.041  1.00 74.57           N  
ANISOU  475  NZ  LYS A  61    10990  10988   6356  -3215  -1198   2450       N  
ATOM    476  N   SER A  62      16.259 -20.933  28.774  1.00 84.15           N  
ANISOU  476  N   SER A  62    13879   9546   8549  -2992  -3234   2963       N  
ATOM    477  CA  SER A  62      16.482 -22.246  28.187  1.00 88.19           C  
ANISOU  477  CA  SER A  62    14646   9577   9284  -2974  -3636   2975       C  
ATOM    478  C   SER A  62      15.571 -22.419  26.978  1.00 85.66           C  
ANISOU  478  C   SER A  62    14270   9217   9058  -2992  -3561   2939       C  
ATOM    479  O   SER A  62      14.589 -21.692  26.803  1.00 84.47           O  
ANISOU  479  O   SER A  62    13894   9432   8768  -3129  -3221   2962       O  
ATOM    480  CB  SER A  62      16.234 -23.366  29.205  1.00 95.67           C  
ANISOU  480  CB  SER A  62    15770  10451  10130  -3377  -3958   3207       C  
ATOM    481  OG  SER A  62      17.186 -23.323  30.257  1.00 97.76           O  
ANISOU  481  OG  SER A  62    16127  10681  10337  -3331  -4081   3229       O  
ATOM    482  N   ASN A  63      15.911 -23.403  26.141  1.00 83.14           N  
ANISOU  482  N   ASN A  63    14152   8456   8980  -2840  -3896   2857       N  
ATOM    483  CA  ASN A  63      15.205 -23.587  24.877  1.00 75.95           C  
ANISOU  483  CA  ASN A  63    13212   7459   8188  -2781  -3860   2785       C  
ATOM    484  C   ASN A  63      13.695 -23.634  25.072  1.00 73.62           C  
ANISOU  484  C   ASN A  63    12787   7480   7704  -3222  -3707   2980       C  
ATOM    485  O   ASN A  63      12.940 -23.091  24.257  1.00 73.43           O  
ANISOU  485  O   ASN A  63    12604   7616   7681  -3188  -3447   2921       O  
ATOM    486  CB  ASN A  63      15.694 -24.864  24.192  1.00 77.12           C  
ANISOU  486  CB  ASN A  63    13610   7112   8580  -2631  -4321   2685       C  
ATOM    487  CG  ASN A  63      17.152 -24.782  23.783  1.00 76.68           C  
ANISOU  487  CG  ASN A  63    13624   6780   8731  -2134  -4442   2418       C  
ATOM    488  OD1 ASN A  63      17.678 -23.696  23.535  1.00 72.69           O  
ANISOU  488  OD1 ASN A  63    12960   6422   8237  -1832  -4145   2281       O  
ATOM    489  ND2 ASN A  63      17.813 -25.932  23.709  1.00 80.55           N  
ANISOU  489  ND2 ASN A  63    14336   6884   9385  -2048  -4894   2330       N  
ATOM    490  N   HIS A  64      13.233 -24.269  26.146  1.00 73.56           N  
ANISOU  490  N   HIS A  64    12832   7583   7535  -3638  -3868   3207       N  
ATOM    491  CA  HIS A  64      11.802 -24.376  26.401  1.00 74.90           C  
ANISOU  491  CA  HIS A  64    12853   8087   7519  -4064  -3747   3387       C  
ATOM    492  C   HIS A  64      11.209 -23.115  27.025  1.00 73.43           C  
ANISOU  492  C   HIS A  64    12347   8474   7078  -4174  -3269   3388       C  
ATOM    493  O   HIS A  64      10.027 -23.120  27.381  1.00 74.84           O  
ANISOU  493  O   HIS A  64    12356   9004   7075  -4522  -3143   3511       O  
ATOM    494  CB  HIS A  64      11.512 -25.584  27.296  1.00 81.85           C  
ANISOU  494  CB  HIS A  64    13899   8885   8316  -4483  -4130   3639       C  
ATOM    495  CG  HIS A  64      12.349 -25.637  28.534  1.00 87.12           C  
ANISOU  495  CG  HIS A  64    14658   9562   8880  -4543  -4241   3723       C  
ATOM    496  ND1 HIS A  64      13.435 -26.476  28.660  1.00 90.21           N  
ANISOU  496  ND1 HIS A  64    15335   9496   9446  -4409  -4661   3699       N  
ATOM    497  CD2 HIS A  64      12.263 -24.953  29.699  1.00 88.83           C  
ANISOU  497  CD2 HIS A  64    14717  10196   8838  -4710  -3997   3812       C  
ATOM    498  CE1 HIS A  64      13.981 -26.309  29.852  1.00 92.23           C  
ANISOU  498  CE1 HIS A  64    15616   9870   9557  -4501  -4670   3789       C  
ATOM    499  NE2 HIS A  64      13.290 -25.389  30.501  1.00 91.46           N  
ANISOU  499  NE2 HIS A  64    15254  10305   9190  -4682  -4268   3863       N  
ATOM    500  N   ASN A  65      11.993 -22.045  27.170  1.00 72.91           N  
ANISOU  500  N   ASN A  65    12182   8525   6995  -3879  -3020   3237       N  
ATOM    501  CA  ASN A  65      11.445 -20.754  27.568  1.00 73.52           C  
ANISOU  501  CA  ASN A  65    11935   9136   6864  -3916  -2571   3169       C  
ATOM    502  C   ASN A  65      10.841 -19.988  26.396  1.00 73.30           C  
ANISOU  502  C   ASN A  65    11718   9214   6917  -3748  -2278   3005       C  
ATOM    503  O   ASN A  65      10.219 -18.943  26.614  1.00 74.86           O  
ANISOU  503  O   ASN A  65    11619   9862   6964  -3788  -1915   2914       O  
ATOM    504  CB  ASN A  65      12.530 -19.893  28.227  1.00 71.11           C  
ANISOU  504  CB  ASN A  65    11596   8922   6501  -3674  -2454   3071       C  
ATOM    505  CG  ASN A  65      12.966 -20.427  29.582  1.00 74.77           C  
ANISOU  505  CG  ASN A  65    12184   9406   6820  -3878  -2665   3232       C  
ATOM    506  OD1 ASN A  65      13.794 -21.334  29.668  1.00 77.08           O  
ANISOU  506  OD1 ASN A  65    12756   9277   7253  -3819  -3033   3292       O  
ATOM    507  ND2 ASN A  65      12.421 -19.852  30.650  1.00 75.21           N  
ANISOU  507  ND2 ASN A  65    12023   9959   6596  -4104  -2440   3279       N  
ATOM    508  N   PHE A  66      11.000 -20.479  25.169  1.00 72.09           N  
ANISOU  508  N   PHE A  66    11721   8668   7002  -3552  -2437   2944       N  
ATOM    509  CA  PHE A  66      10.547 -19.787  23.969  1.00 68.15           C  
ANISOU  509  CA  PHE A  66    11077   8215   6600  -3365  -2186   2791       C  
ATOM    510  C   PHE A  66       9.378 -20.547  23.357  1.00 70.93           C  
ANISOU  510  C   PHE A  66    11443   8519   6988  -3596  -2287   2869       C  
ATOM    511  O   PHE A  66       9.518 -21.720  22.993  1.00 72.95           O  
ANISOU  511  O   PHE A  66    11946   8390   7382  -3623  -2659   2943       O  
ATOM    512  CB  PHE A  66      11.687 -19.655  22.958  1.00 62.70           C  
ANISOU  512  CB  PHE A  66    10538   7135   6151  -2909  -2274   2635       C  
ATOM    513  CG  PHE A  66      12.836 -18.829  23.450  1.00 57.76           C  
ANISOU  513  CG  PHE A  66     9881   6561   5504  -2653  -2178   2548       C  
ATOM    514  CD1 PHE A  66      12.873 -17.465  23.217  1.00 55.48           C  
ANISOU  514  CD1 PHE A  66     9357   6559   5162  -2492  -1818   2420       C  
ATOM    515  CD2 PHE A  66      13.878 -19.413  24.148  1.00 57.02           C  
ANISOU  515  CD2 PHE A  66     9985   6230   5450  -2578  -2468   2586       C  
ATOM    516  CE1 PHE A  66      13.927 -16.701  23.670  1.00 53.45           C  
ANISOU  516  CE1 PHE A  66     9007   6362   4938  -2223  -1730   2274       C  
ATOM    517  CE2 PHE A  66      14.935 -18.655  24.601  1.00 55.46           C  
ANISOU  517  CE2 PHE A  66     9754   6079   5240  -2333  -2401   2500       C  
ATOM    518  CZ  PHE A  66      14.960 -17.297  24.363  1.00 52.72           C  
ANISOU  518  CZ  PHE A  66     9156   6024   4850  -2164  -2044   2363       C  
ATOM    519  N   LEU A  67       8.235 -19.874  23.238  1.00 71.69           N  
ANISOU  519  N   LEU A  67    11264   9007   6969  -3745  -1977   2829       N  
ATOM    520  CA  LEU A  67       7.014 -20.464  22.696  1.00 75.31           C  
ANISOU  520  CA  LEU A  67    11692   9484   7440  -3971  -2041   2897       C  
ATOM    521  C   LEU A  67       6.795 -19.914  21.291  1.00 70.61           C  
ANISOU  521  C   LEU A  67    11033   8785   7009  -3710  -1867   2724       C  
ATOM    522  O   LEU A  67       6.222 -18.833  21.119  1.00 67.28           O  
ANISOU  522  O   LEU A  67    10332   8707   6525  -3675  -1507   2589       O  
ATOM    523  CB  LEU A  67       5.819 -20.165  23.598  1.00 79.94           C  
ANISOU  523  CB  LEU A  67    12000  10599   7775  -4324  -1846   2960       C  
ATOM    524  CG  LEU A  67       4.453 -20.648  23.105  1.00 82.13           C  
ANISOU  524  CG  LEU A  67    12199  10970   8036  -4563  -1880   3024       C  
ATOM    525  CD1 LEU A  67       4.364 -22.166  23.142  1.00 86.43           C  
ANISOU  525  CD1 LEU A  67    13024  11183   8633  -4797  -2337   3256       C  
ATOM    526  CD2 LEU A  67       3.332 -20.024  23.926  1.00 83.35           C  
ANISOU  526  CD2 LEU A  67    12013  11715   7941  -4811  -1611   3004       C  
ATOM    527  N   VAL A  68       7.246 -20.662  20.291  1.00 69.12           N  
ANISOU  527  N   VAL A  68    11098   8126   7037  -3517  -2139   2707       N  
ATOM    528  CA  VAL A  68       7.010 -20.315  18.895  1.00 63.25           C  
ANISOU  528  CA  VAL A  68    10334   7245   6454  -3283  -2028   2562       C  
ATOM    529  C   VAL A  68       5.720 -20.986  18.445  1.00 64.79           C  
ANISOU  529  C   VAL A  68    10513   7452   6652  -3537  -2131   2640       C  
ATOM    530  O   VAL A  68       5.537 -22.195  18.634  1.00 64.70           O  
ANISOU  530  O   VAL A  68    10689   7230   6664  -3722  -2494   2785       O  
ATOM    531  CB  VAL A  68       8.193 -20.742  18.010  1.00 62.85           C  
ANISOU  531  CB  VAL A  68    10547   6703   6631  -2886  -2275   2457       C  
ATOM    532  CG1 VAL A  68       7.941 -20.362  16.554  1.00 61.30           C  
ANISOU  532  CG1 VAL A  68    10328   6380   6582  -2636  -2160   2306       C  
ATOM    533  CG2 VAL A  68       9.480 -20.108  18.512  1.00 61.59           C  
ANISOU  533  CG2 VAL A  68    10396   6542   6464  -2634  -2198   2389       C  
ATOM    534  N   GLN A  69       4.826 -20.200  17.848  1.00 67.12           N  
ANISOU  534  N   GLN A  69    10580   7990   6932  -3543  -1829   2540       N  
ATOM    535  CA  GLN A  69       3.525 -20.683  17.400  1.00 71.85           C  
ANISOU  535  CA  GLN A  69    11125   8647   7529  -3769  -1885   2596       C  
ATOM    536  C   GLN A  69       3.272 -20.181  15.987  1.00 68.25           C  
ANISOU  536  C   GLN A  69    10634   8064   7235  -3531  -1744   2430       C  
ATOM    537  O   GLN A  69       3.216 -18.969  15.757  1.00 65.13           O  
ANISOU  537  O   GLN A  69    10012   7912   6822  -3399  -1385   2275       O  
ATOM    538  CB  GLN A  69       2.416 -20.220  18.349  1.00 77.34           C  
ANISOU  538  CB  GLN A  69    11514   9878   7992  -4087  -1650   2638       C  
ATOM    539  CG  GLN A  69       1.022 -20.246  17.750  1.00 82.12           C  
ANISOU  539  CG  GLN A  69    11970  10638   8595  -4238  -1574   2620       C  
ATOM    540  CD  GLN A  69      -0.069 -20.243  18.805  1.00 88.46           C  
ANISOU  540  CD  GLN A  69    12543  11910   9158  -4587  -1487   2711       C  
ATOM    541  OE1 GLN A  69       0.105 -20.786  19.899  1.00 90.58           O  
ANISOU  541  OE1 GLN A  69    12868  12272   9278  -4811  -1643   2882       O  
ATOM    542  NE2 GLN A  69      -1.203 -19.628  18.484  1.00 89.92           N  
ANISOU  542  NE2 GLN A  69    12467  12397   9301  -4630  -1250   2590       N  
ATOM    543  N   ALA A  70       3.128 -21.112  15.046  1.00 66.26           N  
ANISOU  543  N   ALA A  70    10870   6722   7582  -2715  -1824   2283       N  
ATOM    544  CA  ALA A  70       2.829 -20.793  13.653  1.00 63.31           C  
ANISOU  544  CA  ALA A  70    10478   6181   7397  -2573  -1932   2089       C  
ATOM    545  C   ALA A  70       1.340 -21.027  13.422  1.00 65.69           C  
ANISOU  545  C   ALA A  70    10541   6471   7948  -2843  -1928   2203       C  
ATOM    546  O   ALA A  70       0.883 -22.175  13.391  1.00 66.34           O  
ANISOU  546  O   ALA A  70    10671   6332   8205  -2968  -2212   2333       O  
ATOM    547  CB  ALA A  70       3.675 -21.639  12.706  1.00 62.63           C  
ANISOU  547  CB  ALA A  70    10683   5713   7402  -2273  -2353   1920       C  
ATOM    548  N   GLY A  71       0.589 -19.943  13.256  1.00 67.11           N  
ANISOU  548  N   GLY A  71    10442   6888   8167  -2923  -1621   2150       N  
ATOM    549  CA  GLY A  71      -0.852 -20.043  13.154  1.00 72.19           C  
ANISOU  549  CA  GLY A  71    10786   7577   9066  -3165  -1567   2257       C  
ATOM    550  C   GLY A  71      -1.436 -20.728  14.370  1.00 81.08           C  
ANISOU  550  C   GLY A  71    11806   8835  10166  -3442  -1453   2547       C  
ATOM    551  O   GLY A  71      -1.670 -20.088  15.400  1.00 81.70           O  
ANISOU  551  O   GLY A  71    11704   9273  10065  -3552  -1051   2625       O  
ATOM    552  N   ASN A  72      -1.669 -22.033  14.263  1.00 89.03           N  
ANISOU  552  N   ASN A  72    12934   9554  11339  -3542  -1810   2697       N  
ATOM    553  CA  ASN A  72      -2.108 -22.845  15.388  1.00 96.95           C  
ANISOU  553  CA  ASN A  72    13892  10628  12316  -3810  -1764   3005       C  
ATOM    554  C   ASN A  72      -1.114 -23.927  15.776  1.00 99.00           C  
ANISOU  554  C   ASN A  72    14495  10655  12466  -3759  -2093   3093       C  
ATOM    555  O   ASN A  72      -1.019 -24.261  16.958  1.00103.95           O  
ANISOU  555  O   ASN A  72    15147  11428  12920  -3919  -1969   3314       O  
ATOM    556  CB  ASN A  72      -3.467 -23.498  15.083  1.00101.47           C  
ANISOU  556  CB  ASN A  72    14242  11082  13231  -4048  -1890   3172       C  
ATOM    557  CG  ASN A  72      -3.581 -23.968  13.646  1.00100.26           C  
ANISOU  557  CG  ASN A  72    14192  10549  13355  -3905  -2343   3000       C  
ATOM    558  OD1 ASN A  72      -2.594 -24.367  13.029  1.00 98.54           O  
ANISOU  558  OD1 ASN A  72    14293  10070  13079  -3662  -2670   2829       O  
ATOM    559  ND2 ASN A  72      -4.792 -23.912  13.102  1.00101.39           N  
ANISOU  559  ND2 ASN A  72    14063  10667  13793  -4031  -2364   3026       N  
ATOM    560  N   VAL A  73      -0.364 -24.477  14.819  1.00 94.85           N  
ANISOU  560  N   VAL A  73    14233   9775  12032  -3520  -2508   2910       N  
ATOM    561  CA  VAL A  73       0.655 -25.465  15.142  1.00 94.54           C  
ANISOU  561  CA  VAL A  73    14500   9504  11917  -3425  -2829   2946       C  
ATOM    562  C   VAL A  73       1.770 -24.800  15.942  1.00 90.87           C  
ANISOU  562  C   VAL A  73    14137   9262  11127  -3287  -2591   2894       C  
ATOM    563  O   VAL A  73       2.039 -23.599  15.804  1.00 88.46           O  
ANISOU  563  O   VAL A  73    13748   9188  10675  -3150  -2291   2727       O  
ATOM    564  CB  VAL A  73       1.191 -26.123  13.858  1.00 94.36           C  
ANISOU  564  CB  VAL A  73    14713   9077  12062  -3142  -3294   2696       C  
ATOM    565  CG1 VAL A  73       1.849 -25.091  12.947  1.00 89.65           C  
ANISOU  565  CG1 VAL A  73    14167   8527  11370  -2807  -3178   2365       C  
ATOM    566  CG2 VAL A  73       2.159 -27.245  14.198  1.00 97.80           C  
ANISOU  566  CG2 VAL A  73    15429   9256  12475  -3045  -3648   2723       C  
ATOM    567  N   GLN A  74       2.423 -25.585  16.796  1.00 90.20           N  
ANISOU  567  N   GLN A  74    14230   9101  10939  -3326  -2749   3040       N  
ATOM    568  CA  GLN A  74       3.501 -25.091  17.642  1.00 84.74           C  
ANISOU  568  CA  GLN A  74    13643   8598   9957  -3202  -2586   3008       C  
ATOM    569  C   GLN A  74       4.815 -25.757  17.261  1.00 77.99           C  
ANISOU  569  C   GLN A  74    13063   7426   9142  -2909  -2966   2848       C  
ATOM    570  O   GLN A  74       4.871 -26.971  17.043  1.00 75.13           O  
ANISOU  570  O   GLN A  74    12846   6734   8965  -2927  -3364   2904       O  
ATOM    571  CB  GLN A  74       3.201 -25.338  19.123  1.00 91.40           C  
ANISOU  571  CB  GLN A  74    14449   9667  10611  -3485  -2412   3313       C  
ATOM    572  CG  GLN A  74       1.947 -24.636  19.613  1.00 96.02           C  
ANISOU  572  CG  GLN A  74    14739  10614  11131  -3735  -1973   3447       C  
ATOM    573  CD  GLN A  74       1.947 -24.408  21.112  1.00102.35           C  
ANISOU  573  CD  GLN A  74    15524  11749  11614  -3891  -1676   3638       C  
ATOM    574  OE1 GLN A  74       2.958 -24.616  21.786  1.00104.04           O  
ANISOU  574  OE1 GLN A  74    15949  11945  11637  -3804  -1790   3653       O  
ATOM    575  NE2 GLN A  74       0.810 -23.974  21.643  1.00105.58           N  
ANISOU  575  NE2 GLN A  74    15679  12466  11969  -4106  -1295   3772       N  
ATOM    576  N   LEU A  75       5.867 -24.950  17.183  1.00 77.06           N  
ANISOU  576  N   LEU A  75    12996   7416   8866  -2628  -2842   2641       N  
ATOM    577  CA  LEU A  75       7.190 -25.430  16.822  1.00 80.61           C  
ANISOU  577  CA  LEU A  75    13654   7615   9360  -2300  -3137   2459       C  
ATOM    578  C   LEU A  75       7.983 -25.759  18.080  1.00 84.54           C  
ANISOU  578  C   LEU A  75    14249   8168   9704  -2348  -3183   2610       C  
ATOM    579  O   LEU A  75       7.729 -25.218  19.160  1.00 85.24           O  
ANISOU  579  O   LEU A  75    14251   8566   9571  -2548  -2903   2776       O  
ATOM    580  CB  LEU A  75       7.937 -24.385  15.989  1.00 78.68           C  
ANISOU  580  CB  LEU A  75    13383   7457   9055  -1945  -2984   2162       C  
ATOM    581  CG  LEU A  75       7.392 -24.077  14.589  1.00 78.72           C  
ANISOU  581  CG  LEU A  75    13348   7361   9200  -1815  -2995   1966       C  
ATOM    582  CD1 LEU A  75       6.034 -23.386  14.631  1.00 78.14           C  
ANISOU  582  CD1 LEU A  75    13059   7507   9124  -2113  -2714   2088       C  
ATOM    583  CD2 LEU A  75       8.386 -23.227  13.806  1.00 75.73           C  
ANISOU  583  CD2 LEU A  75    12988   7041   8746  -1412  -2895   1686       C  
ATOM    584  N   ARG A  76       8.946 -26.663  17.933  1.00 87.23           N  
ANISOU  584  N   ARG A  76    14772   8205  10165  -2147  -3548   2533       N  
ATOM    585  CA  ARG A  76       9.794 -27.092  19.036  1.00 90.06           C  
ANISOU  585  CA  ARG A  76    15243   8551  10426  -2167  -3673   2664       C  
ATOM    586  C   ARG A  76      11.144 -26.398  18.907  1.00 84.68           C  
ANISOU  586  C   ARG A  76    14562   7937   9674  -1802  -3616   2433       C  
ATOM    587  O   ARG A  76      11.837 -26.566  17.898  1.00 85.94           O  
ANISOU  587  O   ARG A  76    14763   7896   9993  -1460  -3778   2179       O  
ATOM    588  CB  ARG A  76       9.964 -28.611  19.035  1.00 96.32           C  
ANISOU  588  CB  ARG A  76    16217   8948  11432  -2203  -4145   2752       C  
ATOM    589  CG  ARG A  76      10.455 -29.191  20.353  1.00100.64           C  
ANISOU  589  CG  ARG A  76    16880   9482  11878  -2360  -4287   2996       C  
ATOM    590  CD  ARG A  76      10.768 -30.676  20.222  1.00107.49           C  
ANISOU  590  CD  ARG A  76    17932   9917  12992  -2343  -4800   3040       C  
ATOM    591  NE  ARG A  76       9.569 -31.475  19.977  1.00112.96           N  
ANISOU  591  NE  ARG A  76    18624  10458  13838  -2628  -4957   3217       N  
ATOM    592  CZ  ARG A  76       8.843 -32.056  20.930  1.00117.61           C  
ANISOU  592  CZ  ARG A  76    19230  11078  14378  -3017  -5001   3588       C  
ATOM    593  NH1 ARG A  76       9.186 -31.936  22.206  1.00119.02           N  
ANISOU  593  NH1 ARG A  76    19458  11439  14326  -3165  -4897   3810       N  
ATOM    594  NH2 ARG A  76       7.768 -32.761  20.603  1.00120.10           N  
ANISOU  594  NH2 ARG A  76    19512  11247  14874  -3255  -5155   3743       N  
ATOM    595  N   VAL A  77      11.504 -25.614  19.920  1.00 77.04           N  
ANISOU  595  N   VAL A  77    13539   7266   8467  -1862  -3384   2513       N  
ATOM    596  CA  VAL A  77      12.780 -24.905  19.928  1.00 68.50           C  
ANISOU  596  CA  VAL A  77    12422   6275   7328  -1547  -3339   2329       C  
ATOM    597  C   VAL A  77      13.848 -25.849  20.464  1.00 69.02           C  
ANISOU  597  C   VAL A  77    12637   6099   7487  -1440  -3699   2375       C  
ATOM    598  O   VAL A  77      13.762 -26.315  21.604  1.00 73.29           O  
ANISOU  598  O   VAL A  77    13275   6654   7918  -1682  -3788   2613       O  
ATOM    599  CB  VAL A  77      12.696 -23.627  20.777  1.00 67.09           C  
ANISOU  599  CB  VAL A  77    12119   6509   6863  -1654  -2973   2366       C  
ATOM    600  CG1 VAL A  77      14.007 -22.849  20.705  1.00 64.04           C  
ANISOU  600  CG1 VAL A  77    11666   6212   6455  -1333  -2955   2176       C  
ATOM    601  CG2 VAL A  77      11.526 -22.760  20.328  1.00 65.76           C  
ANISOU  601  CG2 VAL A  77    11794   6573   6619  -1790  -2625   2334       C  
ATOM    602  N   ILE A  78      14.855 -26.137  19.639  1.00 67.29           N  
ANISOU  602  N   ILE A  78    12433   5665   7470  -1067  -3903   2148       N  
ATOM    603  CA  ILE A  78      15.949 -27.020  20.015  1.00 73.51           C  
ANISOU  603  CA  ILE A  78    13332   6205   8394   -912  -4257   2149       C  
ATOM    604  C   ILE A  78      17.299 -26.319  19.941  1.00 79.05           C  
ANISOU  604  C   ILE A  78    13912   7012   9112   -562  -4218   1970       C  
ATOM    605  O   ILE A  78      18.340 -26.967  20.052  1.00 79.33           O  
ANISOU  605  O   ILE A  78    13991   6843   9308   -354  -4505   1916       O  
ATOM    606  CB  ILE A  78      15.947 -28.300  19.156  1.00 73.21           C  
ANISOU  606  CB  ILE A  78    13419   5764   8632   -775  -4614   2040       C  
ATOM    607  CG1 ILE A  78      16.507 -28.031  17.757  1.00 71.84           C  
ANISOU  607  CG1 ILE A  78    13161   5533   8601   -335  -4580   1689       C  
ATOM    608  CG2 ILE A  78      14.534 -28.845  19.034  1.00 72.46           C  
ANISOU  608  CG2 ILE A  78    13393   5587   8551  -1114  -4642   2198       C  
ATOM    609  CD1 ILE A  78      17.885 -28.622  17.525  1.00 75.08           C  
ANISOU  609  CD1 ILE A  78    13584   5739   9204     52  -4849   1504       C  
ATOM    610  N   GLY A  79      17.300 -25.002  19.761  1.00 83.15           N  
ANISOU  610  N   GLY A  79    14260   7846   9486   -499  -3881   1882       N  
ATOM    611  CA  GLY A  79      18.522 -24.232  19.669  1.00 84.14           C  
ANISOU  611  CA  GLY A  79    14229   8103   9638   -194  -3834   1734       C  
ATOM    612  C   GLY A  79      18.229 -22.750  19.740  1.00 77.60           C  
ANISOU  612  C   GLY A  79    13236   7646   8601   -258  -3465   1705       C  
ATOM    613  O   GLY A  79      17.189 -22.296  19.252  1.00 79.38           O  
ANISOU  613  O   GLY A  79    13431   7988   8740   -386  -3227   1690       O  
ATOM    614  N   HIS A  80      19.122 -21.985  20.362  1.00 69.06           N  
ANISOU  614  N   HIS A  80    12045   6743   7453   -180  -3439   1695       N  
ATOM    615  CA  HIS A  80      18.966 -20.541  20.471  1.00 61.40           C  
ANISOU  615  CA  HIS A  80    10916   6111   6302   -226  -3134   1642       C  
ATOM    616  C   HIS A  80      20.341 -19.907  20.364  1.00 63.10           C  
ANISOU  616  C   HIS A  80    10947   6397   6633     66  -3210   1525       C  
ATOM    617  O   HIS A  80      21.299 -20.383  20.981  1.00 64.57           O  
ANISOU  617  O   HIS A  80    11153   6463   6916    147  -3472   1571       O  
ATOM    618  CB  HIS A  80      18.289 -20.141  21.787  1.00 60.52           C  
ANISOU  618  CB  HIS A  80    10887   6206   5902   -581  -3001   1803       C  
ATOM    619  CG  HIS A  80      19.136 -20.370  22.998  1.00 64.30           C  
ANISOU  619  CG  HIS A  80    11451   6661   6319   -620  -3227   1907       C  
ATOM    620  ND1 HIS A  80      19.089 -21.536  23.731  1.00 68.04           N  
ANISOU  620  ND1 HIS A  80    12128   6934   6789   -769  -3473   2090       N  
ATOM    621  CD2 HIS A  80      20.056 -19.582  23.603  1.00 64.56           C  
ANISOU  621  CD2 HIS A  80    11400   6834   6297   -538  -3273   1860       C  
ATOM    622  CE1 HIS A  80      19.943 -21.457  24.736  1.00 71.12           C  
ANISOU  622  CE1 HIS A  80    12566   7345   7110   -768  -3652   2151       C  
ATOM    623  NE2 HIS A  80      20.543 -20.282  24.680  1.00 68.91           N  
ANISOU  623  NE2 HIS A  80    12113   7267   6803   -628  -3542   2007       N  
ATOM    624  N   SER A  81      20.438 -18.847  19.572  1.00 66.39           N  
ANISOU  624  N   SER A  81    11168   6999   7059    219  -2998   1387       N  
ATOM    625  CA  SER A  81      21.703 -18.172  19.342  1.00 70.24           C  
ANISOU  625  CA  SER A  81    11424   7571   7694    496  -3057   1288       C  
ATOM    626  C   SER A  81      21.413 -16.707  19.074  1.00 65.80           C  
ANISOU  626  C   SER A  81    10699   7295   7007    452  -2787   1218       C  
ATOM    627  O   SER A  81      20.410 -16.370  18.439  1.00 67.20           O  
ANISOU  627  O   SER A  81    10902   7552   7080    368  -2551   1177       O  
ATOM    628  CB  SER A  81      22.467 -18.790  18.168  1.00 73.95           C  
ANISOU  628  CB  SER A  81    11778   7872   8449    899  -3159   1152       C  
ATOM    629  OG  SER A  81      23.590 -18.000  17.819  1.00 74.97           O  
ANISOU  629  OG  SER A  81    11605   8139   8742   1172  -3144   1065       O  
ATOM    630  N   MET A  82      22.294 -15.844  19.561  1.00 59.41           N  
ANISOU  630  N   MET A  82     9722   6621   6230    499  -2850   1203       N  
ATOM    631  CA  MET A  82      22.151 -14.403  19.415  1.00 52.41           C  
ANISOU  631  CA  MET A  82     8635   5993   5285    437  -2602   1108       C  
ATOM    632  C   MET A  82      23.167 -13.912  18.396  1.00 50.09           C  
ANISOU  632  C   MET A  82     7954   5763   5316    744  -2499    976       C  
ATOM    633  O   MET A  82      24.377 -14.040  18.610  1.00 54.53           O  
ANISOU  633  O   MET A  82     8363   6270   6087    923  -2730    998       O  
ATOM    634  CB  MET A  82      22.347 -13.710  20.761  1.00 52.94           C  
ANISOU  634  CB  MET A  82     8779   6173   5164    227  -2733   1165       C  
ATOM    635  CG  MET A  82      22.169 -12.213  20.726  1.00 50.04           C  
ANISOU  635  CG  MET A  82     8195   6041   4778    141  -2474   1025       C  
ATOM    636  SD  MET A  82      22.036 -11.549  22.393  1.00 54.61           S  
ANISOU  636  SD  MET A  82     8994   6737   5017   -131  -2628   1053       S  
ATOM    637  CE  MET A  82      23.635 -11.974  23.081  1.00 55.14           C  
ANISOU  637  CE  MET A  82     8987   6657   5308     13  -3049   1121       C  
ATOM    638  N   GLN A  83      22.676 -13.368  17.287  1.00 47.80           N  
ANISOU  638  N   GLN A  83     7497   5595   5071    800  -2158    859       N  
ATOM    639  CA  GLN A  83      23.528 -12.745  16.276  1.00 48.33           C  
ANISOU  639  CA  GLN A  83     7184   5784   5394   1048  -1985    765       C  
ATOM    640  C   GLN A  83      23.232 -11.253  16.306  1.00 41.68           C  
ANISOU  640  C   GLN A  83     6154   5154   4530    871  -1752    725       C  
ATOM    641  O   GLN A  83      22.200 -10.804  15.803  1.00 39.36           O  
ANISOU  641  O   GLN A  83     5898   4938   4118    756  -1499    671       O  
ATOM    642  CB  GLN A  83      23.283 -13.317  14.887  1.00 53.75           C  
ANISOU  642  CB  GLN A  83     7849   6438   6134   1279  -1803    670       C  
ATOM    643  CG  GLN A  83      24.370 -12.934  13.888  1.00 61.94           C  
ANISOU  643  CG  GLN A  83     8508   7611   7417   1584  -1645    602       C  
ATOM    644  CD  GLN A  83      23.996 -13.250  12.453  1.00 68.67           C  
ANISOU  644  CD  GLN A  83     9357   8499   8234   1793  -1400    485       C  
ATOM    645  OE1 GLN A  83      22.843 -13.559  12.151  1.00 69.98           O  
ANISOU  645  OE1 GLN A  83     9779   8592   8217   1679  -1343    447       O  
ATOM    646  NE2 GLN A  83      24.974 -13.170  11.557  1.00 72.00           N  
ANISOU  646  NE2 GLN A  83     9484   9045   8826   2103  -1255    428       N  
ATOM    647  N   ASN A  84      24.134 -10.484  16.892  1.00 40.23           N  
ANISOU  647  N   ASN A  84     5763   5036   4488    850  -1871    749       N  
ATOM    648  CA  ASN A  84      23.946  -9.037  17.051  1.00 40.67           C  
ANISOU  648  CA  ASN A  84     5652   5241   4560    678  -1727    706       C  
ATOM    649  C   ASN A  84      22.638  -8.815  17.784  1.00 39.10           C  
ANISOU  649  C   ASN A  84     5752   5060   4044    408  -1668    668       C  
ATOM    650  O   ASN A  84      22.497  -9.272  18.942  1.00 39.02           O  
ANISOU  650  O   ASN A  84     6010   4989   3828    276  -1887    716       O  
ATOM    651  CB  ASN A  84      24.003  -8.364  15.684  1.00 42.92           C  
ANISOU  651  CB  ASN A  84     5635   5653   5020    798  -1411    672       C  
ATOM    652  CG  ASN A  84      25.291  -8.598  14.955  1.00 45.18           C  
ANISOU  652  CG  ASN A  84     5600   5973   5594   1073  -1413    717       C  
ATOM    653  OD1 ASN A  84      26.345  -8.111  15.365  1.00 43.88           O  
ANISOU  653  OD1 ASN A  84     5177   5832   5663   1091  -1564    775       O  
ATOM    654  ND2 ASN A  84      25.224  -9.347  13.858  1.00 46.64           N  
ANISOU  654  ND2 ASN A  84     5786   6165   5770   1300  -1247    683       N  
ATOM    655  N   CYS A  85      21.653  -8.151  17.195  1.00 36.96           N  
ANISOU  655  N   CYS A  85     5450   4880   3713    319  -1382    594       N  
ATOM    656  CA  CYS A  85      20.441  -7.787  17.897  1.00 37.59           C  
ANISOU  656  CA  CYS A  85     5739   5010   3535     81  -1293    538       C  
ATOM    657  C   CYS A  85      19.251  -8.672  17.550  1.00 38.09           C  
ANISOU  657  C   CYS A  85     6019   5031   3422     22  -1162    562       C  
ATOM    658  O   CYS A  85      18.132  -8.362  17.968  1.00 39.73           O  
ANISOU  658  O   CYS A  85     6342   5308   3446   -167  -1025    519       O  
ATOM    659  CB  CYS A  85      20.100  -6.323  17.622  1.00 36.97           C  
ANISOU  659  CB  CYS A  85     5457   5039   3551      8  -1106    428       C  
ATOM    660  SG  CYS A  85      21.238  -5.177  18.413  1.00 38.39           S  
ANISOU  660  SG  CYS A  85     5453   5232   3903    -21  -1328    390       S  
ATOM    661  N   VAL A  86      19.456  -9.769  16.826  1.00 38.83           N  
ANISOU  661  N   VAL A  86     6164   5008   3583    181  -1214    619       N  
ATOM    662  CA  VAL A  86      18.371 -10.695  16.519  1.00 42.06           C  
ANISOU  662  CA  VAL A  86     6791   5329   3862    110  -1160    653       C  
ATOM    663  C   VAL A  86      18.647 -12.027  17.203  1.00 43.52           C  
ANISOU  663  C   VAL A  86     7236   5338   3962    104  -1445    783       C  
ATOM    664  O   VAL A  86      19.802 -12.435  17.384  1.00 42.55           O  
ANISOU  664  O   VAL A  86     7081   5130   3957    271  -1671    820       O  
ATOM    665  CB  VAL A  86      18.169 -10.903  15.003  1.00 45.32           C  
ANISOU  665  CB  VAL A  86     7104   5710   4407    293  -1011    590       C  
ATOM    666  CG1 VAL A  86      17.704  -9.611  14.334  1.00 41.58           C  
ANISOU  666  CG1 VAL A  86     6413   5391   3994    258   -747    502       C  
ATOM    667  CG2 VAL A  86      19.442 -11.422  14.354  1.00 51.15           C  
ANISOU  667  CG2 VAL A  86     7729   6383   5323    599  -1121    583       C  
ATOM    668  N   LEU A  87      17.573 -12.704  17.589  1.00 44.74           N  
ANISOU  668  N   LEU A  87     7633   5430   3936    -99  -1448    871       N  
ATOM    669  CA  LEU A  87      17.646 -14.049  18.134  1.00 46.33           C  
ANISOU  669  CA  LEU A  87     8109   5426   4067   -142  -1729   1035       C  
ATOM    670  C   LEU A  87      17.363 -15.056  17.027  1.00 44.41           C  
ANISOU  670  C   LEU A  87     7932   4975   3965      1  -1780   1021       C  
ATOM    671  O   LEU A  87      16.426 -14.882  16.242  1.00 41.26           O  
ANISOU  671  O   LEU A  87     7491   4607   3579    -45  -1582    953       O  
ATOM    672  CB  LEU A  87      16.642 -14.250  19.267  1.00 50.55           C  
ANISOU  672  CB  LEU A  87     8858   6019   4331   -478  -1698   1176       C  
ATOM    673  CG  LEU A  87      17.169 -14.523  20.676  1.00 59.31           C  
ANISOU  673  CG  LEU A  87    10067   7135   5332   -581  -1864   1272       C  
ATOM    674  CD1 LEU A  87      16.012 -14.960  21.572  1.00 64.59           C  
ANISOU  674  CD1 LEU A  87    10871   7862   5807   -879  -1739   1394       C  
ATOM    675  CD2 LEU A  87      18.275 -15.563  20.688  1.00 62.64           C  
ANISOU  675  CD2 LEU A  87    10556   7314   5932   -398  -2203   1344       C  
ATOM    676  N   LYS A  88      18.167 -16.106  16.975  1.00 48.74           N  
ANISOU  676  N   LYS A  88     8594   5296   4629    187  -2077   1070       N  
ATOM    677  CA  LYS A  88      17.966 -17.204  16.038  1.00 52.45           C  
ANISOU  677  CA  LYS A  88     9186   5515   5228    346  -2202   1035       C  
ATOM    678  C   LYS A  88      17.560 -18.432  16.843  1.00 56.83           C  
ANISOU  678  C   LYS A  88     9987   5842   5764    139  -2438   1203       C  
ATOM    679  O   LYS A  88      18.341 -18.935  17.657  1.00 58.26           O  
ANISOU  679  O   LYS A  88    10209   5936   5993    153  -2648   1276       O  
ATOM    680  CB  LYS A  88      19.225 -17.449  15.209  1.00 56.65           C  
ANISOU  680  CB  LYS A  88     9569   5975   5981    765  -2291    885       C  
ATOM    681  CG  LYS A  88      19.495 -16.328  14.212  1.00 59.16           C  
ANISOU  681  CG  LYS A  88     9571   6545   6361    936  -1958    708       C  
ATOM    682  CD  LYS A  88      20.553 -16.699  13.189  1.00 62.74           C  
ANISOU  682  CD  LYS A  88     9882   6955   7003   1360  -1980    557       C  
ATOM    683  CE  LYS A  88      21.929 -16.792  13.815  1.00 66.73           C  
ANISOU  683  CE  LYS A  88    10245   7446   7665   1531  -2171    598       C  
ATOM    684  NZ  LYS A  88      22.997 -16.724  12.780  1.00 69.31           N  
ANISOU  684  NZ  LYS A  88    10293   7861   8179   1936  -2054    444       N  
ATOM    685  N   LEU A  89      16.331 -18.893  16.625  1.00 59.46           N  
ANISOU  685  N   LEU A  89    10437   6092   6062    -73  -2386   1259       N  
ATOM    686  CA  LEU A  89      15.767 -20.034  17.339  1.00 63.62           C  
ANISOU  686  CA  LEU A  89    11145   6427   6601   -322  -2561   1428       C  
ATOM    687  C   LEU A  89      15.684 -21.208  16.367  1.00 66.45           C  
ANISOU  687  C   LEU A  89    11633   6449   7167   -161  -2798   1351       C  
ATOM    688  O   LEU A  89      14.760 -21.287  15.553  1.00 65.60           O  
ANISOU  688  O   LEU A  89    11557   6280   7088   -211  -2738   1305       O  
ATOM    689  CB  LEU A  89      14.395 -19.693  17.909  1.00 63.18           C  
ANISOU  689  CB  LEU A  89    11092   6539   6374   -708  -2337   1566       C  
ATOM    690  CG  LEU A  89      14.302 -18.448  18.792  1.00 63.12           C  
ANISOU  690  CG  LEU A  89    10959   6883   6141   -851  -2063   1578       C  
ATOM    691  CD1 LEU A  89      12.869 -18.250  19.268  1.00 63.86           C  
ANISOU  691  CD1 LEU A  89    11035   7136   6092  -1194  -1827   1691       C  
ATOM    692  CD2 LEU A  89      15.256 -18.548  19.972  1.00 66.48           C  
ANISOU  692  CD2 LEU A  89    11433   7339   6487   -850  -2209   1650       C  
ATOM    693  N   LYS A  90      16.656 -22.113  16.451  1.00 68.84           N  
ANISOU  693  N   LYS A  90    12008   6526   7623     40  -3084   1316       N  
ATOM    694  CA  LYS A  90      16.616 -23.337  15.661  1.00 70.75           C  
ANISOU  694  CA  LYS A  90    12393   6428   8062    192  -3349   1213       C  
ATOM    695  C   LYS A  90      15.444 -24.192  16.125  1.00 68.34           C  
ANISOU  695  C   LYS A  90    12249   5961   7756   -190  -3474   1407       C  
ATOM    696  O   LYS A  90      15.333 -24.516  17.313  1.00 73.61           O  
ANISOU  696  O   LYS A  90    12975   6643   8351   -462  -3544   1629       O  
ATOM    697  CB  LYS A  90      17.931 -24.101  15.799  1.00 77.09           C  
ANISOU  697  CB  LYS A  90    13215   7043   9034    476  -3626   1134       C  
ATOM    698  CG  LYS A  90      18.025 -25.386  14.972  1.00 82.37           C  
ANISOU  698  CG  LYS A  90    14028   7361   9907    683  -3919    971       C  
ATOM    699  CD  LYS A  90      18.523 -25.128  13.555  1.00 82.07           C  
ANISOU  699  CD  LYS A  90    13900   7348   9934   1134  -3821    656       C  
ATOM    700  CE  LYS A  90      19.388 -26.283  13.055  1.00 86.43           C  
ANISOU  700  CE  LYS A  90    14518   7630  10690   1478  -4114    448       C  
ATOM    701  NZ  LYS A  90      20.024 -25.985  11.741  1.00 86.83           N  
ANISOU  701  NZ  LYS A  90    14447   7780  10765   1956  -3963    128       N  
ATOM    702  N   VAL A  91      14.567 -24.557  15.192  1.00 61.48           N  
ANISOU  702  N   VAL A  91    11445   4949   6966   -212  -3512   1329       N  
ATOM    703  CA  VAL A  91      13.387 -25.351  15.512  1.00 60.19           C  
ANISOU  703  CA  VAL A  91    11390   4638   6843   -581  -3643   1520       C  
ATOM    704  C   VAL A  91      13.502 -26.718  14.846  1.00 62.07           C  
ANISOU  704  C   VAL A  91    11796   4484   7304   -439  -4040   1400       C  
ATOM    705  O   VAL A  91      14.457 -26.982  14.106  1.00 61.94           O  
ANISOU  705  O   VAL A  91    11809   4340   7386    -39  -4168   1144       O  
ATOM    706  CB  VAL A  91      12.100 -24.622  15.084  1.00 55.81           C  
ANISOU  706  CB  VAL A  91    10743   4248   6213   -794  -3386   1558       C  
ATOM    707  CG1 VAL A  91      11.848 -23.424  15.993  1.00 53.57           C  
ANISOU  707  CG1 VAL A  91    10304   4352   5700  -1003  -3020   1702       C  
ATOM    708  CG2 VAL A  91      12.186 -24.176  13.624  1.00 53.62           C  
ANISOU  708  CG2 VAL A  91    10443   3942   5987   -467  -3329   1273       C  
ATOM    709  N   ASP A  92      12.538 -27.597  15.107  1.00 66.23           N  
ANISOU  709  N   ASP A  92    12417   4837   7912   -759  -4236   1580       N  
ATOM    710  CA  ASP A  92      12.599 -28.966  14.614  1.00 75.28           C  
ANISOU  710  CA  ASP A  92    13730   5601   9272   -669  -4665   1489       C  
ATOM    711  C   ASP A  92      11.906 -29.153  13.271  1.00 78.23           C  
ANISOU  711  C   ASP A  92    14142   5840   9742   -557  -4753   1274       C  
ATOM    712  O   ASP A  92      11.966 -30.253  12.710  1.00 83.61           O  
ANISOU  712  O   ASP A  92    14968   6213  10587   -436  -5124   1143       O  
ATOM    713  CB  ASP A  92      11.982 -29.927  15.640  1.00 78.57           C  
ANISOU  713  CB  ASP A  92    14229   5881   9743  -1077  -4896   1821       C  
ATOM    714  CG  ASP A  92      10.495 -29.704  15.832  1.00 76.67           C  
ANISOU  714  CG  ASP A  92    13897   5775   9459  -1490  -4736   2058       C  
ATOM    715  OD1 ASP A  92       9.966 -28.711  15.292  1.00 72.56           O  
ANISOU  715  OD1 ASP A  92    13246   5467   8857  -1478  -4432   1974       O  
ATOM    716  OD2 ASP A  92       9.856 -30.524  16.526  1.00 79.41           O  
ANISOU  716  OD2 ASP A  92    14289   6019   9865  -1824  -4917   2338       O  
ATOM    717  N   THR A  93      11.258 -28.121  12.740  1.00 72.86           N  
ANISOU  717  N   THR A  93    13345   5379   8961   -588  -4447   1229       N  
ATOM    718  CA  THR A  93      10.540 -28.224  11.481  1.00 70.68           C  
ANISOU  718  CA  THR A  93    13106   4992   8756   -499  -4535   1036       C  
ATOM    719  C   THR A  93      11.029 -27.145  10.528  1.00 63.85           C  
ANISOU  719  C   THR A  93    12179   4315   7765   -138  -4261    761       C  
ATOM    720  O   THR A  93      11.219 -25.993  10.926  1.00 60.13           O  
ANISOU  720  O   THR A  93    11564   4132   7151   -161  -3911    836       O  
ATOM    721  CB  THR A  93       9.026 -28.086  11.685  1.00 72.04           C  
ANISOU  721  CB  THR A  93    13181   5227   8963   -937  -4467   1281       C  
ATOM    722  OG1 THR A  93       8.557 -29.143  12.532  1.00 79.48           O  
ANISOU  722  OG1 THR A  93    14168   6007  10022  -1266  -4722   1557       O  
ATOM    723  CG2 THR A  93       8.298 -28.153  10.354  1.00 70.63           C  
ANISOU  723  CG2 THR A  93    13035   4935   8868   -834  -4588   1076       C  
ATOM    724  N   ALA A  94      11.257 -27.536   9.276  1.00 61.68           N  
ANISOU  724  N   ALA A  94    12017   3895   7524    205  -4428    444       N  
ATOM    725  CA  ALA A  94      11.543 -26.578   8.220  1.00 58.87           C  
ANISOU  725  CA  ALA A  94    11616   3724   7029    536  -4179    190       C  
ATOM    726  C   ALA A  94      10.229 -26.047   7.664  1.00 59.51           C  
ANISOU  726  C   ALA A  94    11658   3857   7096    313  -4098    234       C  
ATOM    727  O   ALA A  94       9.287 -26.806   7.428  1.00 61.07           O  
ANISOU  727  O   ALA A  94    11924   3860   7419    107  -4369    283       O  
ATOM    728  CB  ALA A  94      12.362 -27.229   7.105  1.00 61.26           C  
ANISOU  728  CB  ALA A  94    12053   3903   7319   1021  -4365   -175       C  
ATOM    729  N   ASN A  95      10.159 -24.737   7.480  1.00 57.86           N  
ANISOU  729  N   ASN A  95    11319   3911   6754    347  -3742    234       N  
ATOM    730  CA  ASN A  95       8.951 -24.116   6.950  1.00 59.16           C  
ANISOU  730  CA  ASN A  95    11422   4134   6924    147  -3652    271       C  
ATOM    731  C   ASN A  95       8.731 -24.630   5.531  1.00 63.79           C  
ANISOU  731  C   ASN A  95    12165   4567   7506    404  -3891    -23       C  
ATOM    732  O   ASN A  95       9.549 -24.355   4.646  1.00 68.06           O  
ANISOU  732  O   ASN A  95    12773   5194   7892    829  -3804   -296       O  
ATOM    733  CB  ASN A  95       9.085 -22.591   6.989  1.00 56.19           C  
ANISOU  733  CB  ASN A  95    10885   4071   6394    189  -3244    312       C  
ATOM    734  CG  ASN A  95       7.811 -21.872   6.579  1.00 54.86           C  
ANISOU  734  CG  ASN A  95    10551   4040   6253    -65  -3099    347       C  
ATOM    735  OD1 ASN A  95       6.789 -22.496   6.291  1.00 57.47           O  
ANISOU  735  OD1 ASN A  95    10974   4114   6747   -273  -3368    400       O  
ATOM    736  ND2 ASN A  95       7.869 -20.543   6.559  1.00 48.75           N  
ANISOU  736  ND2 ASN A  95     9507   3666   5351    -54  -2695    320       N  
ATOM    737  N   PRO A  96       7.665 -25.396   5.274  1.00 62.10           N  
ANISOU  737  N   PRO A  96    11997   4158   7440    174  -4190     36       N  
ATOM    738  CA  PRO A  96       7.388 -25.825   3.895  1.00 61.07           C  
ANISOU  738  CA  PRO A  96    12013   3917   7273    420  -4432   -221       C  
ATOM    739  C   PRO A  96       6.965 -24.692   2.976  1.00 61.65           C  
ANISOU  739  C   PRO A  96    12030   4181   7215    514  -4208   -335       C  
ATOM    740  O   PRO A  96       6.745 -24.932   1.783  1.00 62.97           O  
ANISOU  740  O   PRO A  96    12318   4300   7307    737  -4377   -530       O  
ATOM    741  CB  PRO A  96       6.254 -26.846   4.066  1.00 64.21           C  
ANISOU  741  CB  PRO A  96    12420   4071   7906     83  -4806    -44       C  
ATOM    742  CG  PRO A  96       5.562 -26.420   5.305  1.00 62.82           C  
ANISOU  742  CG  PRO A  96    12022   3994   7854   -388  -4607    312       C  
ATOM    743  CD  PRO A  96       6.638 -25.884   6.215  1.00 61.55           C  
ANISOU  743  CD  PRO A  96    11823   3997   7567   -315  -4309    365       C  
ATOM    744  N   LYS A  97       6.837 -23.469   3.490  1.00 61.76           N  
ANISOU  744  N   LYS A  97    11866   4404   7195    353  -3847   -205       N  
ATOM    745  CA  LYS A  97       6.512 -22.306   2.676  1.00 62.00           C  
ANISOU  745  CA  LYS A  97    11834   4617   7107    435  -3627   -317       C  
ATOM    746  C   LYS A  97       7.695 -21.355   2.532  1.00 58.28           C  
ANISOU  746  C   LYS A  97    11278   4472   6394    760  -3240   -445       C  
ATOM    747  O   LYS A  97       7.512 -20.197   2.145  1.00 57.52           O  
ANISOU  747  O   LYS A  97    10978   4695   6183    756  -2940   -454       O  
ATOM    748  CB  LYS A  97       5.308 -21.570   3.267  1.00 65.32           C  
ANISOU  748  CB  LYS A  97    12009   5119   7691    -20  -3488    -69       C  
ATOM    749  CG  LYS A  97       3.992 -22.326   3.136  1.00 75.65           C  
ANISOU  749  CG  LYS A  97    13270   6241   9234   -321  -3802     57       C  
ATOM    750  CD  LYS A  97       2.804 -21.474   3.573  1.00 81.22           C  
ANISOU  750  CD  LYS A  97    13677   7076  10108   -720  -3618    265       C  
ATOM    751  CE  LYS A  97       2.361 -21.803   4.992  1.00 87.25           C  
ANISOU  751  CE  LYS A  97    14255   7863  11034  -1123  -3531    598       C  
ATOM    752  NZ  LYS A  97       1.229 -20.940   5.432  1.00 88.76           N  
ANISOU  752  NZ  LYS A  97    14105   8242  11377  -1478  -3291    783       N  
ATOM    753  N   THR A  98       8.905 -21.817   2.836  1.00 56.39           N  
ANISOU  753  N   THR A  98    11123   4208   6096   1031  -3234   -517       N  
ATOM    754  CA  THR A  98      10.085 -20.975   2.700  1.00 53.01           C  
ANISOU  754  CA  THR A  98    10525   4149   5468   1330  -2856   -608       C  
ATOM    755  C   THR A  98      10.291 -20.609   1.233  1.00 53.51           C  
ANISOU  755  C   THR A  98    10677   4351   5302   1679  -2773   -876       C  
ATOM    756  O   THR A  98      10.547 -21.505   0.414  1.00 52.82           O  
ANISOU  756  O   THR A  98    10829   4090   5152   1972  -3012  -1089       O  
ATOM    757  CB  THR A  98      11.333 -21.680   3.224  1.00 54.19           C  
ANISOU  757  CB  THR A  98    10746   4202   5642   1584  -2927   -652       C  
ATOM    758  OG1 THR A  98      11.150 -22.052   4.593  1.00 53.51           O  
ANISOU  758  OG1 THR A  98    10618   3982   5730   1251  -3033   -377       O  
ATOM    759  CG2 THR A  98      12.541 -20.763   3.114  1.00 53.59           C  
ANISOU  759  CG2 THR A  98    10431   4522   5407   1860  -2529   -713       C  
ATOM    760  N   PRO A  99      10.200 -19.338   0.858  1.00 52.53           N  
ANISOU  760  N   PRO A  99    10330   4586   5043   1649  -2431   -837       N  
ATOM    761  CA  PRO A  99      10.474 -18.957  -0.529  1.00 53.07           C  
ANISOU  761  CA  PRO A  99    10495   4825   4845   1976  -2330  -1052       C  
ATOM    762  C   PRO A  99      11.973 -18.889  -0.784  1.00 55.45           C  
ANISOU  762  C   PRO A  99    10744   5352   4972   2391  -2082  -1181       C  
ATOM    763  O   PRO A  99      12.797 -19.035   0.120  1.00 56.21           O  
ANISOU  763  O   PRO A  99    10699   5475   5183   2417  -1997  -1100       O  
ATOM    764  CB  PRO A  99       9.826 -17.575  -0.651  1.00 51.73           C  
ANISOU  764  CB  PRO A  99    10069   4937   4648   1737  -2067   -893       C  
ATOM    765  CG  PRO A  99       9.962 -16.996   0.735  1.00 50.12           C  
ANISOU  765  CG  PRO A  99     9556   4862   4624   1456  -1853   -652       C  
ATOM    766  CD  PRO A  99       9.864 -18.168   1.697  1.00 50.47           C  
ANISOU  766  CD  PRO A  99     9728   4591   4859   1322  -2128   -593       C  
ATOM    767  N   LYS A 100      12.319 -18.678  -2.049  1.00 58.76           N  
ANISOU  767  N   LYS A 100    11167   5975   5185   2672  -1938  -1294       N  
ATOM    768  CA  LYS A 100      13.683 -18.302  -2.393  1.00 63.47           C  
ANISOU  768  CA  LYS A 100    11591   6902   5621   3005  -1597  -1346       C  
ATOM    769  C   LYS A 100      13.947 -16.921  -1.808  1.00 58.58           C  
ANISOU  769  C   LYS A 100    10685   6597   4975   2843  -1240  -1167       C  
ATOM    770  O   LYS A 100      13.275 -15.950  -2.173  1.00 55.75           O  
ANISOU  770  O   LYS A 100    10230   6391   4563   2642  -1118  -1046       O  
ATOM    771  CB  LYS A 100      13.869 -18.306  -3.907  1.00 73.91           C  
ANISOU  771  CB  LYS A 100    12965   8399   6720   3264  -1506  -1454       C  
ATOM    772  CG  LYS A 100      15.272 -18.692  -4.374  1.00 85.27           C  
ANISOU  772  CG  LYS A 100    14326  10042   8030   3668  -1323  -1582       C  
ATOM    773  CD  LYS A 100      16.283 -17.568  -4.155  1.00 89.66           C  
ANISOU  773  CD  LYS A 100    14532  11002   8533   3714   -869  -1444       C  
ATOM    774  CE  LYS A 100      16.983 -17.164  -5.455  1.00 96.01           C  
ANISOU  774  CE  LYS A 100    15235  12158   9088   3953   -572  -1469       C  
ATOM    775  NZ  LYS A 100      18.468 -17.289  -5.372  1.00 99.44           N  
ANISOU  775  NZ  LYS A 100    15433  12829   9519   4234   -320  -1505       N  
ATOM    776  N   TYR A 101      14.890 -16.832  -0.875  1.00 57.26           N  
ANISOU  776  N   TYR A 101    10293   6517   4948   2867  -1096  -1076       N  
ATOM    777  CA  TYR A 101      15.087 -15.597  -0.134  1.00 52.07           C  
ANISOU  777  CA  TYR A 101     9272   6113   4401   2610   -816   -824       C  
ATOM    778  C   TYR A 101      16.570 -15.302   0.023  1.00 48.49           C  
ANISOU  778  C   TYR A 101     8556   5912   3955   2856   -549   -803       C  
ATOM    779  O   TYR A 101      17.431 -16.149  -0.223  1.00 48.93           O  
ANISOU  779  O   TYR A 101     8688   5925   3978   3209   -591   -974       O  
ATOM    780  CB  TYR A 101      14.426 -15.666   1.249  1.00 52.50           C  
ANISOU  780  CB  TYR A 101     9268   5974   4707   2216   -975   -652       C  
ATOM    781  CG  TYR A 101      15.107 -16.627   2.198  1.00 57.28           C  
ANISOU  781  CG  TYR A 101     9916   6387   5461   2284  -1150   -658       C  
ATOM    782  CD1 TYR A 101      14.727 -17.960   2.256  1.00 60.10           C  
ANISOU  782  CD1 TYR A 101    10581   6376   5880   2326  -1516   -763       C  
ATOM    783  CD2 TYR A 101      16.129 -16.199   3.037  1.00 58.02           C  
ANISOU  783  CD2 TYR A 101     9749   6642   5655   2297   -991   -545       C  
ATOM    784  CE1 TYR A 101      15.345 -18.841   3.122  1.00 61.24           C  
ANISOU  784  CE1 TYR A 101    10779   6316   6175   2384  -1714   -743       C  
ATOM    785  CE2 TYR A 101      16.754 -17.073   3.906  1.00 58.57           C  
ANISOU  785  CE2 TYR A 101     9868   6522   5864   2361  -1191   -536       C  
ATOM    786  CZ  TYR A 101      16.357 -18.392   3.945  1.00 60.38           C  
ANISOU  786  CZ  TYR A 101    10412   6384   6145   2405  -1549   -628       C  
ATOM    787  OH  TYR A 101      16.975 -19.266   4.809  1.00 61.73           O  
ANISOU  787  OH  TYR A 101    10647   6340   6469   2464  -1784   -594       O  
ATOM    788  N   LYS A 102      16.855 -14.078   0.455  1.00 46.97           N  
ANISOU  788  N   LYS A 102     8036   5970   3841   2667   -291   -596       N  
ATOM    789  CA  LYS A 102      18.211 -13.688   0.806  1.00 48.96           C  
ANISOU  789  CA  LYS A 102     7977   6444   4183   2815    -70   -521       C  
ATOM    790  C   LYS A 102      18.133 -12.446   1.677  1.00 41.56           C  
ANISOU  790  C   LYS A 102     6746   5632   3414   2469     58   -283       C  
ATOM    791  O   LYS A 102      17.168 -11.679   1.603  1.00 37.38           O  
ANISOU  791  O   LYS A 102     6220   5115   2869   2206     80   -196       O  
ATOM    792  CB  LYS A 102      19.067 -13.447  -0.440  1.00 58.37           C  
ANISOU  792  CB  LYS A 102     9078   7938   5161   3170    219   -594       C  
ATOM    793  CG  LYS A 102      18.690 -12.231  -1.260  1.00 64.87           C  
ANISOU  793  CG  LYS A 102     9804   9019   5825   3044    460   -454       C  
ATOM    794  CD  LYS A 102      19.269 -12.340  -2.669  1.00 74.47           C  
ANISOU  794  CD  LYS A 102    11042  10466   6788   3353    657   -533       C  
ATOM    795  CE  LYS A 102      19.424 -10.978  -3.325  1.00 79.98           C  
ANISOU  795  CE  LYS A 102    11488  11464   7437   3194    939   -287       C  
ATOM    796  NZ  LYS A 102      18.961 -10.980  -4.743  1.00 85.38           N  
ANISOU  796  NZ  LYS A 102    12359  12197   7883   3240    939   -328       N  
ATOM    797  N   PHE A 103      19.142 -12.281   2.530  1.00 42.37           N  
ANISOU  797  N   PHE A 103     6600   5801   3696   2482    105   -197       N  
ATOM    798  CA  PHE A 103      19.237 -11.139   3.428  1.00 38.74           C  
ANISOU  798  CA  PHE A 103     5870   5443   3407   2190    189     -4       C  
ATOM    799  C   PHE A 103      20.077 -10.053   2.768  1.00 38.91           C  
ANISOU  799  C   PHE A 103     5570   5776   3438   2272    492    115       C  
ATOM    800  O   PHE A 103      21.204 -10.314   2.333  1.00 40.23           O  
ANISOU  800  O   PHE A 103     5582   6097   3607   2560    627     92       O  
ATOM    801  CB  PHE A 103      19.866 -11.545   4.764  1.00 38.83           C  
ANISOU  801  CB  PHE A 103     5809   5335   3609   2136     18     35       C  
ATOM    802  CG  PHE A 103      19.046 -12.530   5.561  1.00 38.88           C  
ANISOU  802  CG  PHE A 103     6115   5043   3614   1991   -277    -11       C  
ATOM    803  CD1 PHE A 103      17.702 -12.731   5.286  1.00 39.21           C  
ANISOU  803  CD1 PHE A 103     6393   4952   3553   1823   -358    -47       C  
ATOM    804  CD2 PHE A 103      19.625 -13.249   6.601  1.00 37.82           C  
ANISOU  804  CD2 PHE A 103     6011   4760   3598   2007   -489     11       C  
ATOM    805  CE1 PHE A 103      16.955 -13.629   6.023  1.00 39.70           C  
ANISOU  805  CE1 PHE A 103     6695   4752   3636   1657   -616    -45       C  
ATOM    806  CE2 PHE A 103      18.884 -14.150   7.341  1.00 36.63           C  
ANISOU  806  CE2 PHE A 103     6138   4342   3438   1844   -758     20       C  
ATOM    807  CZ  PHE A 103      17.547 -14.341   7.052  1.00 39.58           C  
ANISOU  807  CZ  PHE A 103     6725   4599   3715   1660   -808      0       C  
ATOM    808  N   VAL A 104      19.535  -8.841   2.696  1.00 38.73           N  
ANISOU  808  N   VAL A 104     5431   5844   3441   2021    596    253       N  
ATOM    809  CA  VAL A 104      20.234  -7.711   2.096  1.00 41.76           C  
ANISOU  809  CA  VAL A 104     5511   6495   3860   2032    857    421       C  
ATOM    810  C   VAL A 104      20.173  -6.537   3.060  1.00 40.08           C  
ANISOU  810  C   VAL A 104     5074   6265   3891   1714    825    575       C  
ATOM    811  O   VAL A 104      19.161  -6.330   3.738  1.00 41.14           O  
ANISOU  811  O   VAL A 104     5336   6233   4064   1475    676    542       O  
ATOM    812  CB  VAL A 104      19.626  -7.313   0.735  1.00 44.28           C  
ANISOU  812  CB  VAL A 104     5947   6937   3940   2074   1000    446       C  
ATOM    813  CG1 VAL A 104      19.406  -8.540  -0.136  1.00 45.74           C  
ANISOU  813  CG1 VAL A 104     6452   7076   3851   2368    953    232       C  
ATOM    814  CG2 VAL A 104      18.324  -6.557   0.941  1.00 42.97           C  
ANISOU  814  CG2 VAL A 104     5870   6638   3817   1760    888    496       C  
ATOM    815  N   ARG A 105      21.249  -5.763   3.113  1.00 41.18           N  
ANISOU  815  N   ARG A 105     4868   6575   4202   1715    962    737       N  
ATOM    816  CA  ARG A 105      21.277  -4.520   3.877  1.00 42.31           C  
ANISOU  816  CA  ARG A 105     4790   6696   4589   1430    917    879       C  
ATOM    817  C   ARG A 105      21.146  -3.373   2.884  1.00 44.72           C  
ANISOU  817  C   ARG A 105     4956   7150   4886   1345   1101   1063       C  
ATOM    818  O   ARG A 105      22.081  -3.089   2.128  1.00 50.70           O  
ANISOU  818  O   ARG A 105     5481   8129   5652   1466   1311   1220       O  
ATOM    819  CB  ARG A 105      22.557  -4.403   4.699  1.00 44.23           C  
ANISOU  819  CB  ARG A 105     4739   6979   5087   1447    871    954       C  
ATOM    820  CG  ARG A 105      22.589  -3.176   5.595  1.00 41.79           C  
ANISOU  820  CG  ARG A 105     4242   6601   5036   1157    757   1060       C  
ATOM    821  CD  ARG A 105      23.865  -3.102   6.415  1.00 42.42           C  
ANISOU  821  CD  ARG A 105     4040   6697   5379   1170    653   1130       C  
ATOM    822  NE  ARG A 105      23.892  -1.890   7.229  1.00 43.44           N  
ANISOU  822  NE  ARG A 105     4015   6738   5752    898    508   1207       N  
ATOM    823  CZ  ARG A 105      23.315  -1.774   8.422  1.00 39.60           C  
ANISOU  823  CZ  ARG A 105     3704   6071   5271    730    276   1076       C  
ATOM    824  NH1 ARG A 105      22.663  -2.799   8.952  1.00 37.47           N  
ANISOU  824  NH1 ARG A 105     3750   5700   4786    773    178    907       N  
ATOM    825  NH2 ARG A 105      23.390  -0.628   9.083  1.00 38.60           N  
ANISOU  825  NH2 ARG A 105     3443   5863   5361    516    139   1117       N  
ATOM    826  N   ILE A 106      19.984  -2.721   2.875  1.00 42.03           N  
ANISOU  826  N   ILE A 106     4745   6691   4534   1139   1024   1058       N  
ATOM    827  CA  ILE A 106      19.717  -1.664   1.909  1.00 42.91           C  
ANISOU  827  CA  ILE A 106     4772   6897   4633   1050   1144   1242       C  
ATOM    828  C   ILE A 106      20.435  -0.387   2.327  1.00 42.50           C  
ANISOU  828  C   ILE A 106     4377   6872   4900    863   1150   1454       C  
ATOM    829  O   ILE A 106      20.904  -0.265   3.463  1.00 40.34           O  
ANISOU  829  O   ILE A 106     3971   6507   4848    777   1019   1414       O  
ATOM    830  CB  ILE A 106      18.208  -1.396   1.753  1.00 41.71           C  
ANISOU  830  CB  ILE A 106     4855   6581   4410    908   1019   1160       C  
ATOM    831  CG1 ILE A 106      17.573  -1.081   3.108  1.00 41.64           C  
ANISOU  831  CG1 ILE A 106     4852   6364   4607    700    826   1040       C  
ATOM    832  CG2 ILE A 106      17.523  -2.582   1.100  1.00 39.62           C  
ANISOU  832  CG2 ILE A 106     4915   6291   3846   1082    996    991       C  
ATOM    833  CD1 ILE A 106      16.304  -0.277   2.993  1.00 42.49           C  
ANISOU  833  CD1 ILE A 106     5024   6341   4780    527    737   1025       C  
ATOM    834  N   GLN A 107      20.512   0.561   1.417  1.00 45.01           N  
ANISOU  834  N   GLN A 107     4565   7297   5239    789   1271   1688       N  
ATOM    835  CA  GLN A 107      21.093   1.868   1.644  1.00 48.23           C  
ANISOU  835  CA  GLN A 107     4656   7695   5974    580   1248   1929       C  
ATOM    836  C   GLN A 107      19.996   2.895   1.898  1.00 43.21           C  
ANISOU  836  C   GLN A 107     4100   6829   5489    349   1057   1919       C  
ATOM    837  O   GLN A 107      18.857   2.720   1.450  1.00 37.69           O  
ANISOU  837  O   GLN A 107     3655   6059   4607    363   1020   1817       O  
ATOM    838  CB  GLN A 107      21.923   2.310   0.435  1.00 55.17           C  
ANISOU  838  CB  GLN A 107     5319   8843   6800    625   1508   2252       C  
ATOM    839  CG  GLN A 107      23.120   1.417   0.125  1.00 63.29           C  
ANISOU  839  CG  GLN A 107     6211  10118   7720    877   1720   2254       C  
ATOM    840  CD  GLN A 107      24.291   1.639   1.070  1.00 68.35           C  
ANISOU  840  CD  GLN A 107     6495  10746   8727    814   1654   2326       C  
ATOM    841  OE1 GLN A 107      24.877   2.723   1.111  1.00 70.83           O  
ANISOU  841  OE1 GLN A 107     6565  11019   9330    608   1594   2545       O  
ATOM    842  NE2 GLN A 107      24.640   0.606   1.832  1.00 68.86           N  
ANISOU  842  NE2 GLN A 107     6578  10795   8792    985   1598   2117       N  
ATOM    843  N   PRO A 108      20.302   3.977   2.612  1.00 44.59           N  
ANISOU  843  N   PRO A 108     4057   6868   6019    145    908   2009       N  
ATOM    844  CA  PRO A 108      19.303   5.037   2.786  1.00 42.50           C  
ANISOU  844  CA  PRO A 108     3847   6371   5929    -43    722   1989       C  
ATOM    845  C   PRO A 108      18.809   5.532   1.435  1.00 40.93           C  
ANISOU  845  C   PRO A 108     3705   6230   5615    -64    808   2210       C  
ATOM    846  O   PRO A 108      19.564   5.607   0.463  1.00 44.21           O  
ANISOU  846  O   PRO A 108     3999   6862   5935    -25   1003   2489       O  
ATOM    847  CB  PRO A 108      20.060   6.127   3.556  1.00 43.15           C  
ANISOU  847  CB  PRO A 108     3648   6325   6423   -230    559   2101       C  
ATOM    848  CG  PRO A 108      21.513   5.804   3.375  1.00 46.02           C  
ANISOU  848  CG  PRO A 108     3750   6904   6833   -167    711   2302       C  
ATOM    849  CD  PRO A 108      21.589   4.316   3.243  1.00 45.42           C  
ANISOU  849  CD  PRO A 108     3844   7005   6410     85    876   2131       C  
ATOM    850  N   GLY A 109      17.520   5.847   1.376  1.00 39.49           N  
ANISOU  850  N   GLY A 109     3708   5866   5430   -120    665   2086       N  
ATOM    851  CA  GLY A 109      16.884   6.283   0.159  1.00 43.82           C  
ANISOU  851  CA  GLY A 109     4357   6427   5864   -140    679   2269       C  
ATOM    852  C   GLY A 109      16.162   5.189  -0.600  1.00 47.05           C  
ANISOU  852  C   GLY A 109     5061   6944   5872     38    764   2140       C  
ATOM    853  O   GLY A 109      15.318   5.500  -1.449  1.00 49.35           O  
ANISOU  853  O   GLY A 109     5495   7186   6071     18    693   2215       O  
ATOM    854  N   GLN A 110      16.467   3.925  -0.317  1.00 48.09           N  
ANISOU  854  N   GLN A 110     5295   7194   5783    210    872   1948       N  
ATOM    855  CA  GLN A 110      15.797   2.813  -0.975  1.00 49.98           C  
ANISOU  855  CA  GLN A 110     5830   7492   5667    382    904   1795       C  
ATOM    856  C   GLN A 110      14.448   2.530  -0.324  1.00 44.70           C  
ANISOU  856  C   GLN A 110     5326   6594   5065    324    703   1527       C  
ATOM    857  O   GLN A 110      14.228   2.801   0.862  1.00 39.35           O  
ANISOU  857  O   GLN A 110     4552   5770   4628    215    603   1389       O  
ATOM    858  CB  GLN A 110      16.663   1.551  -0.935  1.00 55.51           C  
ANISOU  858  CB  GLN A 110     6577   8372   6142    600   1066   1689       C  
ATOM    859  CG  GLN A 110      17.433   1.273  -2.226  1.00 65.32           C  
ANISOU  859  CG  GLN A 110     7839   9902   7079    782   1304   1866       C  
ATOM    860  CD  GLN A 110      16.527   1.138  -3.444  1.00 70.99           C  
ANISOU  860  CD  GLN A 110     8848  10642   7484    846   1269   1879       C  
ATOM    861  OE1 GLN A 110      16.818   1.683  -4.512  1.00 75.03           O  
ANISOU  861  OE1 GLN A 110     9344  11292   7873    840   1365   2085       O  
ATOM    862  NE2 GLN A 110      15.427   0.407  -3.289  1.00 68.64           N  
ANISOU  862  NE2 GLN A 110     8814  10165   7102    880   1081   1622       N  
ATOM    863  N   THR A 111      13.540   1.973  -1.120  1.00 43.31           N  
ANISOU  863  N   THR A 111     5394   6399   4663    401    644   1457       N  
ATOM    864  CA  THR A 111      12.191   1.652  -0.685  1.00 37.84           C  
ANISOU  864  CA  THR A 111     4831   5509   4038    343    464   1239       C  
ATOM    865  C   THR A 111      12.038   0.146  -0.528  1.00 37.08           C  
ANISOU  865  C   THR A 111     4947   5427   3716    477    465   1032       C  
ATOM    866  O   THR A 111      12.774  -0.645  -1.124  1.00 37.20           O  
ANISOU  866  O   THR A 111     5075   5591   3470    657    575   1043       O  
ATOM    867  CB  THR A 111      11.153   2.167  -1.688  1.00 33.42           C  
ANISOU  867  CB  THR A 111     4378   4863   3458    302    318   1321       C  
ATOM    868  OG1 THR A 111      11.380   1.554  -2.962  1.00 32.35           O  
ANISOU  868  OG1 THR A 111     4460   4881   2951    459    375   1402       O  
ATOM    869  CG2 THR A 111      11.238   3.681  -1.819  1.00 30.80           C  
ANISOU  869  CG2 THR A 111     3847   4463   3392    158    266   1538       C  
ATOM    870  N   PHE A 112      11.056  -0.238   0.285  1.00 36.77           N  
ANISOU  870  N   PHE A 112     4952   5227   3792    389    341    845       N  
ATOM    871  CA  PHE A 112      10.751  -1.637   0.536  1.00 37.26           C  
ANISOU  871  CA  PHE A 112     5211   5245   3701    463    291    672       C  
ATOM    872  C   PHE A 112       9.356  -1.717   1.134  1.00 37.54           C  
ANISOU  872  C   PHE A 112     5252   5108   3902    310    147    543       C  
ATOM    873  O   PHE A 112       8.846  -0.748   1.702  1.00 37.04           O  
ANISOU  873  O   PHE A 112     5008   4982   4082    174    130    540       O  
ATOM    874  CB  PHE A 112      11.776  -2.283   1.472  1.00 34.30           C  
ANISOU  874  CB  PHE A 112     4797   4931   3304    520    384    618       C  
ATOM    875  CG  PHE A 112      11.944  -1.565   2.777  1.00 32.09           C  
ANISOU  875  CG  PHE A 112     4311   4618   3263    367    402    602       C  
ATOM    876  CD1 PHE A 112      12.842  -0.518   2.895  1.00 33.39           C  
ANISOU  876  CD1 PHE A 112     4261   4858   3568    337    479    733       C  
ATOM    877  CD2 PHE A 112      11.207  -1.935   3.887  1.00 30.87           C  
ANISOU  877  CD2 PHE A 112     4183   4361   3184    248    335    461       C  
ATOM    878  CE1 PHE A 112      13.001   0.144   4.094  1.00 32.40           C  
ANISOU  878  CE1 PHE A 112     3978   4679   3652    210    451    687       C  
ATOM    879  CE2 PHE A 112      11.362  -1.276   5.089  1.00 32.59           C  
ANISOU  879  CE2 PHE A 112     4250   4567   3565    130    351    419       C  
ATOM    880  CZ  PHE A 112      12.262  -0.235   5.192  1.00 32.10           C  
ANISOU  880  CZ  PHE A 112     4001   4554   3640    120    391    513       C  
ATOM    881  N   SER A 113       8.742  -2.886   0.989  1.00 36.41           N  
ANISOU  881  N   SER A 113     5308   4884   3643    341     38    435       N  
ATOM    882  CA  SER A 113       7.416  -3.126   1.533  1.00 32.04           C  
ANISOU  882  CA  SER A 113     4736   4186   3252    186    -84    337       C  
ATOM    883  C   SER A 113       7.533  -3.649   2.956  1.00 30.55           C  
ANISOU  883  C   SER A 113     4497   3991   3118     93    -17    260       C  
ATOM    884  O   SER A 113       8.431  -4.434   3.267  1.00 31.82           O  
ANISOU  884  O   SER A 113     4761   4192   3136    179     23    251       O  
ATOM    885  CB  SER A 113       6.652  -4.129   0.670  1.00 30.01           C  
ANISOU  885  CB  SER A 113     4710   3816   2875    231   -278    285       C  
ATOM    886  OG  SER A 113       6.375  -3.583  -0.603  1.00 32.82           O  
ANISOU  886  OG  SER A 113     5132   4174   3166    297   -373    356       O  
ATOM    887  N   VAL A 114       6.622  -3.200   3.815  1.00 29.59           N  
ANISOU  887  N   VAL A 114     4217   3827   3199    -73     -6    205       N  
ATOM    888  CA  VAL A 114       6.540  -3.656   5.196  1.00 32.86           C  
ANISOU  888  CA  VAL A 114     4598   4259   3629   -188     66    143       C  
ATOM    889  C   VAL A 114       5.250  -4.445   5.360  1.00 32.23           C  
ANISOU  889  C   VAL A 114     4549   4082   3615   -322    -23    109       C  
ATOM    890  O   VAL A 114       4.194  -4.038   4.865  1.00 30.50           O  
ANISOU  890  O   VAL A 114     4228   3800   3560   -377    -96     95       O  
ATOM    891  CB  VAL A 114       6.590  -2.487   6.200  1.00 34.64           C  
ANISOU  891  CB  VAL A 114     4608   4552   4003   -264    189     91       C  
ATOM    892  CG1 VAL A 114       6.332  -2.992   7.624  1.00 32.85           C  
ANISOU  892  CG1 VAL A 114     4377   4369   3734   -391    268     24       C  
ATOM    893  CG2 VAL A 114       7.926  -1.752   6.105  1.00 32.55           C  
ANISOU  893  CG2 VAL A 114     4294   4357   3715   -164    241    150       C  
ATOM    894  N   LEU A 115       5.340  -5.574   6.043  1.00 32.26           N  
ANISOU  894  N   LEU A 115     4680   4062   3515   -384    -38    118       N  
ATOM    895  CA  LEU A 115       4.176  -6.379   6.392  1.00 31.44           C  
ANISOU  895  CA  LEU A 115     4580   3873   3493   -559   -110    129       C  
ATOM    896  C   LEU A 115       4.019  -6.263   7.904  1.00 30.64           C  
ANISOU  896  C   LEU A 115     4362   3887   3394   -715     67    123       C  
ATOM    897  O   LEU A 115       4.767  -6.886   8.664  1.00 29.95           O  
ANISOU  897  O   LEU A 115     4405   3829   3145   -725     91    162       O  
ATOM    898  CB  LEU A 115       4.341  -7.826   5.944  1.00 30.45           C  
ANISOU  898  CB  LEU A 115     4720   3598   3250   -527   -304    170       C  
ATOM    899  CG  LEU A 115       3.154  -8.737   6.274  1.00 33.30           C  
ANISOU  899  CG  LEU A 115     5082   3837   3733   -745   -419    224       C  
ATOM    900  CD1 LEU A 115       1.901  -8.283   5.535  1.00 35.15           C  
ANISOU  900  CD1 LEU A 115     5159   4007   4189   -815   -513    204       C  
ATOM    901  CD2 LEU A 115       3.461 -10.194   5.952  1.00 35.82           C  
ANISOU  901  CD2 LEU A 115     5693   3965   3952   -710   -651    259       C  
ATOM    902  N   ALA A 116       3.063  -5.447   8.334  1.00 31.35           N  
ANISOU  902  N   ALA A 116     4210   4046   3654   -818    185     66       N  
ATOM    903  CA  ALA A 116       2.803  -5.259   9.753  1.00 33.34           C  
ANISOU  903  CA  ALA A 116     4352   4446   3871   -949    385     32       C  
ATOM    904  C   ALA A 116       2.042  -6.460  10.301  1.00 33.14           C  
ANISOU  904  C   ALA A 116     4372   4404   3816  -1153    379    144       C  
ATOM    905  O   ALA A 116       0.987  -6.830   9.778  1.00 32.98           O  
ANISOU  905  O   ALA A 116     4262   4294   3975  -1252    292    189       O  
ATOM    906  CB  ALA A 116       2.009  -3.974   9.981  1.00 36.17           C  
ANISOU  906  CB  ALA A 116     4424   4886   4433   -952    521   -100       C  
ATOM    907  N   CYS A 117       2.587  -7.068  11.355  1.00 36.97           N  
ANISOU  907  N   CYS A 117     4996   4963   4087  -1231    445    212       N  
ATOM    908  CA  CYS A 117       2.012  -8.255  11.967  1.00 43.86           C  
ANISOU  908  CA  CYS A 117     5943   5815   4906  -1451    429    373       C  
ATOM    909  C   CYS A 117       1.827  -8.023  13.460  1.00 44.12           C  
ANISOU  909  C   CYS A 117     5906   6082   4776  -1591    686    383       C  
ATOM    910  O   CYS A 117       2.522  -7.213  14.075  1.00 40.59           O  
ANISOU  910  O   CYS A 117     5464   5769   4190  -1489    802    262       O  
ATOM    911  CB  CYS A 117       2.901  -9.493  11.764  1.00 47.45           C  
ANISOU  911  CB  CYS A 117     6712   6097   5221  -1418    200    494       C  
ATOM    912  SG  CYS A 117       3.190  -9.983  10.051  1.00 45.82           S  
ANISOU  912  SG  CYS A 117     6659   5630   5120  -1224   -102    459       S  
ATOM    913  N   TYR A 118       0.880  -8.768  14.037  1.00 46.96           N  
ANISOU  913  N   TYR A 118     6207   6492   5144  -1837    763    537       N  
ATOM    914  CA  TYR A 118       0.620  -8.750  15.474  1.00 52.65           C  
ANISOU  914  CA  TYR A 118     6893   7465   5648  -1999   1025    590       C  
ATOM    915  C   TYR A 118       0.263 -10.164  15.906  1.00 58.49           C  
ANISOU  915  C   TYR A 118     7766   8142   6316  -2266    948    885       C  
ATOM    916  O   TYR A 118      -0.725 -10.730  15.426  1.00 57.35           O  
ANISOU  916  O   TYR A 118     7488   7896   6408  -2428    884   1012       O  
ATOM    917  CB  TYR A 118      -0.507  -7.776  15.825  1.00 56.66           C  
ANISOU  917  CB  TYR A 118     7048   8195   6286  -2032   1324    450       C  
ATOM    918  CG  TYR A 118      -0.199  -6.354  15.433  1.00 58.58           C  
ANISOU  918  CG  TYR A 118     7164   8458   6637  -1778   1361    167       C  
ATOM    919  CD1 TYR A 118      -0.473  -5.897  14.151  1.00 58.71           C  
ANISOU  919  CD1 TYR A 118     7051   8296   6962  -1654   1201     90       C  
ATOM    920  CD2 TYR A 118       0.381  -5.474  16.336  1.00 60.58           C  
ANISOU  920  CD2 TYR A 118     7450   8887   6682  -1670   1520    -11       C  
ATOM    921  CE1 TYR A 118      -0.184  -4.605  13.781  1.00 60.39           C  
ANISOU  921  CE1 TYR A 118     7156   8500   7288  -1446   1207   -125       C  
ATOM    922  CE2 TYR A 118       0.669  -4.179  15.977  1.00 61.81           C  
ANISOU  922  CE2 TYR A 118     7493   9016   6976  -1457   1511   -252       C  
ATOM    923  CZ  TYR A 118       0.387  -3.749  14.696  1.00 63.07           C  
ANISOU  923  CZ  TYR A 118     7512   8991   7459  -1352   1358   -292       C  
ATOM    924  OH  TYR A 118       0.674  -2.457  14.324  1.00 65.21           O  
ANISOU  924  OH  TYR A 118     7679   9212   7886  -1162   1323   -492       O  
ATOM    925  N   ASN A 119       1.069 -10.731  16.805  1.00 64.49           N  
ANISOU  925  N   ASN A 119     8790   8941   6774  -2323    920   1010       N  
ATOM    926  CA  ASN A 119       0.897 -12.108  17.272  1.00 70.79           C  
ANISOU  926  CA  ASN A 119     9767   9642   7489  -2581    797   1327       C  
ATOM    927  C   ASN A 119       1.153 -13.107  16.145  1.00 67.07           C  
ANISOU  927  C   ASN A 119     9463   8790   7231  -2540    406   1412       C  
ATOM    928  O   ASN A 119       0.451 -14.111  16.014  1.00 71.34           O  
ANISOU  928  O   ASN A 119    10017   9172   7916  -2768    267   1637       O  
ATOM    929  CB  ASN A 119      -0.491 -12.323  17.878  1.00 79.85           C  
ANISOU  929  CB  ASN A 119    10662  10967   8712  -2841   1036   1479       C  
ATOM    930  CG  ASN A 119      -0.801 -11.333  18.980  1.00 87.46           C  
ANISOU  930  CG  ASN A 119    11451  12290   9491  -2762   1408   1318       C  
ATOM    931  OD1 ASN A 119      -0.295 -11.451  20.097  1.00 91.03           O  
ANISOU  931  OD1 ASN A 119    12074  12870   9642  -2738   1467   1353       O  
ATOM    932  ND2 ASN A 119      -1.634 -10.346  18.669  1.00 90.18           N  
ANISOU  932  ND2 ASN A 119    11461  12775  10027  -2702   1632   1126       N  
ATOM    933  N   GLY A 120       2.171 -12.833  15.332  1.00 59.27           N  
ANISOU  933  N   GLY A 120     8603   7655   6263  -2245    224   1231       N  
ATOM    934  CA  GLY A 120       2.486 -13.689  14.209  1.00 55.91           C  
ANISOU  934  CA  GLY A 120     8351   6894   5997  -2139   -126   1247       C  
ATOM    935  C   GLY A 120       1.457 -13.703  13.102  1.00 56.53           C  
ANISOU  935  C   GLY A 120     8267   6837   6375  -2170   -221   1204       C  
ATOM    936  O   GLY A 120       1.547 -14.549  12.209  1.00 54.71           O  
ANISOU  936  O   GLY A 120     8208   6312   6267  -2115   -540   1222       O  
ATOM    937  N   SER A 121       0.488 -12.784  13.123  1.00 59.33           N  
ANISOU  937  N   SER A 121     8301   7383   6858  -2238     19   1129       N  
ATOM    938  CA  SER A 121      -0.579 -12.742  12.132  1.00 61.59           C  
ANISOU  938  CA  SER A 121     8398   7545   7458  -2285    -90   1100       C  
ATOM    939  C   SER A 121      -0.489 -11.474  11.294  1.00 56.16           C  
ANISOU  939  C   SER A 121     7561   6923   6855  -2032    -26    850       C  
ATOM    940  O   SER A 121      -0.439 -10.372  11.856  1.00 52.14           O  
ANISOU  940  O   SER A 121     6874   6655   6281  -1969    252    730       O  
ATOM    941  CB  SER A 121      -1.943 -12.809  12.827  1.00 68.07           C  
ANISOU  941  CB  SER A 121     8914   8516   8432  -2600    112   1260       C  
ATOM    942  OG  SER A 121      -2.986 -12.893  11.877  1.00 71.48           O  
ANISOU  942  OG  SER A 121     9154   8792   9212  -2668    -54   1259       O  
ATOM    943  N   PRO A 122      -0.474 -11.575   9.962  1.00 52.75           N  
ANISOU  943  N   PRO A 122     7211   6275   6555  -1883   -292    766       N  
ATOM    944  CA  PRO A 122      -0.333 -10.365   9.139  1.00 47.63           C  
ANISOU  944  CA  PRO A 122     6448   5684   5964  -1655   -249    572       C  
ATOM    945  C   PRO A 122      -1.544  -9.450   9.230  1.00 44.85           C  
ANISOU  945  C   PRO A 122     5719   5460   5861  -1750    -84    524       C  
ATOM    946  O   PRO A 122      -2.693  -9.894   9.162  1.00 47.07           O  
ANISOU  946  O   PRO A 122     5831   5678   6377  -1949   -151    621       O  
ATOM    947  CB  PRO A 122      -0.164 -10.917   7.716  1.00 49.02           C  
ANISOU  947  CB  PRO A 122     6841   5599   6185  -1511   -595    532       C  
ATOM    948  CG  PRO A 122       0.299 -12.320   7.900  1.00 51.46           C  
ANISOU  948  CG  PRO A 122     7442   5722   6389  -1566   -799    642       C  
ATOM    949  CD  PRO A 122      -0.373 -12.803   9.151  1.00 53.41           C  
ANISOU  949  CD  PRO A 122     7560   6044   6688  -1880   -666    833       C  
ATOM    950  N   SER A 123      -1.267  -8.153   9.350  1.00 42.30           N  
ANISOU  950  N   SER A 123     5252   5299   5521  -1596    109    370       N  
ATOM    951  CA  SER A 123      -2.287  -7.124   9.508  1.00 43.78           C  
ANISOU  951  CA  SER A 123     5075   5611   5950  -1625    278    277       C  
ATOM    952  C   SER A 123      -2.446  -6.230   8.289  1.00 39.87           C  
ANISOU  952  C   SER A 123     4501   5003   5643  -1448    115    166       C  
ATOM    953  O   SER A 123      -3.573  -5.908   7.908  1.00 39.27           O  
ANISOU  953  O   SER A 123     4165   4888   5868  -1504     61    149       O  
ATOM    954  CB  SER A 123      -1.953  -6.248  10.722  1.00 46.54           C  
ANISOU  954  CB  SER A 123     5313   6215   6156  -1589    608    167       C  
ATOM    955  OG  SER A 123      -2.853  -5.159  10.833  1.00 50.78           O  
ANISOU  955  OG  SER A 123     5503   6856   6936  -1556    763     25       O  
ATOM    956  N   GLY A 124      -1.346  -5.807   7.678  1.00 35.40           N  
ANISOU  956  N   GLY A 124     4139   4393   4917  -1242     35    109       N  
ATOM    957  CA  GLY A 124      -1.408  -4.916   6.537  1.00 32.53           C  
ANISOU  957  CA  GLY A 124     3731   3940   4688  -1086   -111     44       C  
ATOM    958  C   GLY A 124      -0.037  -4.749   5.929  1.00 31.09           C  
ANISOU  958  C   GLY A 124     3812   3738   4264   -893   -171     43       C  
ATOM    959  O   GLY A 124       0.984  -5.060   6.552  1.00 31.70           O  
ANISOU  959  O   GLY A 124     4035   3893   4115   -860    -62     54       O  
ATOM    960  N   VAL A 125      -0.026  -4.256   4.694  1.00 31.69           N  
ANISOU  960  N   VAL A 125     3934   3718   4389   -769   -348     44       N  
ATOM    961  CA  VAL A 125       1.207  -4.077   3.937  1.00 34.25           C  
ANISOU  961  CA  VAL A 125     4480   4048   4484   -585   -389     70       C  
ATOM    962  C   VAL A 125       1.254  -2.652   3.406  1.00 34.68           C  
ANISOU  962  C   VAL A 125     4394   4116   4665   -495   -387     63       C  
ATOM    963  O   VAL A 125       0.250  -2.127   2.913  1.00 34.79           O  
ANISOU  963  O   VAL A 125     4260   4044   4915   -525   -516     54       O  
ATOM    964  CB  VAL A 125       1.316  -5.096   2.781  1.00 39.18           C  
ANISOU  964  CB  VAL A 125     5394   4543   4949   -510   -635    111       C  
ATOM    965  CG1 VAL A 125       0.253  -4.830   1.723  1.00 40.02           C  
ANISOU  965  CG1 VAL A 125     5458   4517   5229   -523   -880    119       C  
ATOM    966  CG2 VAL A 125       2.709  -5.061   2.170  1.00 40.97           C  
ANISOU  966  CG2 VAL A 125     5836   4837   4892   -305   -598    133       C  
ATOM    967  N   TYR A 126       2.426  -2.024   3.509  1.00 35.00           N  
ANISOU  967  N   TYR A 126     4470   4247   4581   -393   -267     83       N  
ATOM    968  CA  TYR A 126       2.608  -0.673   3.000  1.00 34.09           C  
ANISOU  968  CA  TYR A 126     4241   4121   4591   -325   -286    117       C  
ATOM    969  C   TYR A 126       4.050  -0.485   2.552  1.00 29.24           C  
ANISOU  969  C   TYR A 126     3766   3589   3754   -205   -226    218       C  
ATOM    970  O   TYR A 126       4.955  -1.211   2.974  1.00 28.56           O  
ANISOU  970  O   TYR A 126     3798   3586   3468   -168   -125    219       O  
ATOM    971  CB  TYR A 126       2.230   0.379   4.050  1.00 35.13           C  
ANISOU  971  CB  TYR A 126     4099   4273   4976   -382   -164      6       C  
ATOM    972  CG  TYR A 126       3.012   0.283   5.336  1.00 36.51           C  
ANISOU  972  CG  TYR A 126     4267   4570   5036   -405     36    -65       C  
ATOM    973  CD1 TYR A 126       2.540  -0.465   6.404  1.00 39.23           C  
ANISOU  973  CD1 TYR A 126     4586   4984   5335   -508    154   -147       C  
ATOM    974  CD2 TYR A 126       4.220   0.950   5.487  1.00 35.39           C  
ANISOU  974  CD2 TYR A 126     4142   4473   4833   -339     91    -30       C  
ATOM    975  CE1 TYR A 126       3.248  -0.551   7.584  1.00 39.18           C  
ANISOU  975  CE1 TYR A 126     4609   5091   5188   -531    308   -202       C  
ATOM    976  CE2 TYR A 126       4.935   0.867   6.662  1.00 36.31           C  
ANISOU  976  CE2 TYR A 126     4263   4683   4849   -361    224    -99       C  
ATOM    977  CZ  TYR A 126       4.444   0.115   7.707  1.00 39.08           C  
ANISOU  977  CZ  TYR A 126     4625   5104   5118   -450    326   -191       C  
ATOM    978  OH  TYR A 126       5.152   0.031   8.882  1.00 43.24           O  
ANISOU  978  OH  TYR A 126     5191   5728   5509   -473    431   -251       O  
ATOM    979  N   GLN A 127       4.248   0.506   1.687  1.00 26.91           N  
ANISOU  979  N   GLN A 127     3439   3269   3517   -150   -295    324       N  
ATOM    980  CA  GLN A 127       5.549   0.820   1.111  1.00 30.48           C  
ANISOU  980  CA  GLN A 127     3975   3819   3787    -54   -225    469       C  
ATOM    981  C   GLN A 127       6.129   2.051   1.791  1.00 36.32           C  
ANISOU  981  C   GLN A 127     4506   4568   4725    -95   -139    493       C  
ATOM    982  O   GLN A 127       5.427   3.041   2.012  1.00 44.79           O  
ANISOU  982  O   GLN A 127     5409   5529   6081   -153   -216    451       O  
ATOM    983  CB  GLN A 127       5.423   1.073  -0.394  1.00 33.29           C  
ANISOU  983  CB  GLN A 127     4463   4153   4034     15   -369    620       C  
ATOM    984  CG  GLN A 127       6.741   1.281  -1.128  1.00 36.96           C  
ANISOU  984  CG  GLN A 127     5017   4768   4259    118   -256    801       C  
ATOM    985  CD  GLN A 127       7.347  -0.018  -1.609  1.00 37.02           C  
ANISOU  985  CD  GLN A 127     5270   4890   3906    262   -196    770       C  
ATOM    986  OE1 GLN A 127       6.852  -1.099  -1.297  1.00 38.16           O  
ANISOU  986  OE1 GLN A 127     5530   4971   3998    269   -261    617       O  
ATOM    987  NE2 GLN A 127       8.422   0.079  -2.381  1.00 37.99           N  
ANISOU  987  NE2 GLN A 127     5465   5180   3790    381    -72    919       N  
ATOM    988  N   CYS A 128       7.420   1.995   2.105  1.00 35.20           N  
ANISOU  988  N   CYS A 128     4372   4541   4462    -55     -5    554       N  
ATOM    989  CA  CYS A 128       8.085   3.102   2.768  1.00 36.82           C  
ANISOU  989  CA  CYS A 128     4391   4735   4863   -104     37    580       C  
ATOM    990  C   CYS A 128       9.511   3.210   2.252  1.00 34.95           C  
ANISOU  990  C   CYS A 128     4161   4623   4494    -45    126    781       C  
ATOM    991  O   CYS A 128       9.963   2.409   1.427  1.00 32.83           O  
ANISOU  991  O   CYS A 128     4043   4472   3960     59    186    869       O  
ATOM    992  CB  CYS A 128       8.075   2.913   4.286  1.00 38.08           C  
ANISOU  992  CB  CYS A 128     4483   4903   5084   -157    109    381       C  
ATOM    993  SG  CYS A 128       9.034   1.490   4.780  1.00 39.51           S  
ANISOU  993  SG  CYS A 128     4820   5225   4968   -100    222    367       S  
ATOM    994  N   ALA A 129      10.231   4.205   2.755  1.00 34.29           N  
ANISOU  994  N   ALA A 129     3902   4515   4611   -105    131    843       N  
ATOM    995  CA  ALA A 129      11.617   4.421   2.375  1.00 32.04           C  
ANISOU  995  CA  ALA A 129     3548   4353   4274    -80    222   1058       C  
ATOM    996  C   ALA A 129      12.480   4.476   3.624  1.00 33.49           C  
ANISOU  996  C   ALA A 129     3614   4551   4561   -115    252    971       C  
ATOM    997  O   ALA A 129      12.055   4.985   4.666  1.00 36.07           O  
ANISOU  997  O   ALA A 129     3875   4754   5076   -190    167    794       O  
ATOM    998  CB  ALA A 129      11.784   5.713   1.563  1.00 31.30           C  
ANISOU  998  CB  ALA A 129     3334   4194   4365   -154    147   1309       C  
ATOM    999  N   MET A 130      13.681   3.920   3.518  1.00 34.01           N  
ANISOU  999  N   MET A 130     3659   4774   4491    -42    367   1078       N  
ATOM   1000  CA  MET A 130      14.720   4.140   4.516  1.00 37.30           C  
ANISOU 1000  CA  MET A 130     3926   5200   5045    -83    356   1066       C  
ATOM   1001  C   MET A 130      15.174   5.591   4.410  1.00 39.44           C  
ANISOU 1001  C   MET A 130     3978   5375   5631   -209    263   1242       C  
ATOM   1002  O   MET A 130      15.775   5.984   3.406  1.00 41.37           O  
ANISOU 1002  O   MET A 130     4123   5705   5891   -216    332   1522       O  
ATOM   1003  CB  MET A 130      15.877   3.178   4.278  1.00 41.28           C  
ANISOU 1003  CB  MET A 130     4427   5894   5364     48    492   1156       C  
ATOM   1004  CG  MET A 130      17.034   3.332   5.242  1.00 45.54           C  
ANISOU 1004  CG  MET A 130     4793   6447   6062     15    450   1167       C  
ATOM   1005  SD  MET A 130      16.581   2.814   6.903  1.00 47.39           S  
ANISOU 1005  SD  MET A 130     5165   6573   6269    -27    318    862       S  
ATOM   1006  CE  MET A 130      16.330   1.061   6.643  1.00 45.15           C  
ANISOU 1006  CE  MET A 130     5129   6386   5641    137    415    775       C  
ATOM   1007  N   ARG A 131      14.871   6.398   5.428  1.00 37.68           N  
ANISOU 1007  N   ARG A 131     3688   4972   5655   -310    103   1084       N  
ATOM   1008  CA  ARG A 131      15.242   7.804   5.393  1.00 36.53           C  
ANISOU 1008  CA  ARG A 131     3351   4670   5857   -437    -48   1227       C  
ATOM   1009  C   ARG A 131      16.765   7.949   5.399  1.00 34.52           C  
ANISOU 1009  C   ARG A 131     2898   4509   5708   -480    -24   1456       C  
ATOM   1010  O   ARG A 131      17.489   6.994   5.696  1.00 31.12           O  
ANISOU 1010  O   ARG A 131     2476   4242   5106   -394     84   1432       O  
ATOM   1011  CB  ARG A 131      14.634   8.546   6.584  1.00 36.71           C  
ANISOU 1011  CB  ARG A 131     3370   4475   6102   -496   -239    942       C  
ATOM   1012  CG  ARG A 131      13.113   8.426   6.716  1.00 34.51           C  
ANISOU 1012  CG  ARG A 131     3226   4122   5764   -448   -241    696       C  
ATOM   1013  CD  ARG A 131      12.387   8.855   5.452  1.00 35.38           C  
ANISOU 1013  CD  ARG A 131     3337   4167   5938   -452   -266    868       C  
ATOM   1014  NE  ARG A 131      12.837  10.158   4.975  1.00 38.70           N  
ANISOU 1014  NE  ARG A 131     3603   4421   6682   -555   -430   1097       N  
ATOM   1015  CZ  ARG A 131      12.450  10.707   3.828  1.00 37.80           C  
ANISOU 1015  CZ  ARG A 131     3478   4235   6649   -588   -492   1331       C  
ATOM   1016  NH1 ARG A 131      11.602  10.066   3.037  1.00 34.72           N  
ANISOU 1016  NH1 ARG A 131     3229   3929   6035   -512   -416   1338       N  
ATOM   1017  NH2 ARG A 131      12.919  11.895   3.467  1.00 39.20           N  
ANISOU 1017  NH2 ARG A 131     3514   4242   7137   -709   -661   1573       N  
ATOM   1018  N   PRO A 132      17.276   9.135   5.050  1.00 35.99           N  
ANISOU 1018  N   PRO A 132     2884   4582   6208   -617   -139   1699       N  
ATOM   1019  CA  PRO A 132      18.731   9.358   5.131  1.00 37.51           C  
ANISOU 1019  CA  PRO A 132     2828   4850   6573   -688   -137   1934       C  
ATOM   1020  C   PRO A 132      19.291   9.273   6.538  1.00 38.84           C  
ANISOU 1020  C   PRO A 132     2954   4938   6867   -708   -298   1712       C  
ATOM   1021  O   PRO A 132      20.494   9.024   6.690  1.00 41.32           O  
ANISOU 1021  O   PRO A 132     3083   5365   7252   -716   -271   1856       O  
ATOM   1022  CB  PRO A 132      18.907  10.771   4.555  1.00 38.85           C  
ANISOU 1022  CB  PRO A 132     2813   4845   7103   -874   -288   2232       C  
ATOM   1023  CG  PRO A 132      17.721  10.977   3.691  1.00 37.81           C  
ANISOU 1023  CG  PRO A 132     2849   4657   6859   -849   -270   2252       C  
ATOM   1024  CD  PRO A 132      16.591  10.239   4.356  1.00 36.14           C  
ANISOU 1024  CD  PRO A 132     2881   4416   6435   -713   -267   1836       C  
ATOM   1025  N   ASN A 133      18.476   9.494   7.568  1.00 40.20           N  
ANISOU 1025  N   ASN A 133     3279   4927   7067   -709   -468   1369       N  
ATOM   1026  CA  ASN A 133      18.918   9.328   8.947  1.00 42.31           C  
ANISOU 1026  CA  ASN A 133     3574   5139   7364   -713   -625   1130       C  
ATOM   1027  C   ASN A 133      18.714   7.904   9.455  1.00 40.68           C  
ANISOU 1027  C   ASN A 133     3572   5116   6770   -572   -475    936       C  
ATOM   1028  O   ASN A 133      18.809   7.667  10.663  1.00 40.97           O  
ANISOU 1028  O   ASN A 133     3708   5115   6745   -567   -600    705       O  
ATOM   1029  CB  ASN A 133      18.194  10.320   9.863  1.00 41.91           C  
ANISOU 1029  CB  ASN A 133     3599   4816   7507   -772   -879    841       C  
ATOM   1030  CG  ASN A 133      16.708  10.052   9.956  1.00 38.44           C  
ANISOU 1030  CG  ASN A 133     3377   4371   6859   -679   -779    573       C  
ATOM   1031  OD1 ASN A 133      16.202   9.088   9.382  1.00 34.78           O  
ANISOU 1031  OD1 ASN A 133     3021   4085   6109   -592   -553    605       O  
ATOM   1032  ND2 ASN A 133      15.999  10.902  10.690  1.00 39.75           N  
ANISOU 1032  ND2 ASN A 133     3595   4326   7181   -690   -959    294       N  
ATOM   1033  N   PHE A 134      18.421   6.964   8.555  1.00 39.92           N  
ANISOU 1033  N   PHE A 134     3560   5201   6405   -462   -234   1030       N  
ATOM   1034  CA  PHE A 134      18.323   5.537   8.868  1.00 41.67           C  
ANISOU 1034  CA  PHE A 134     3967   5574   6291   -333   -109    902       C  
ATOM   1035  C   PHE A 134      17.122   5.194   9.748  1.00 42.18           C  
ANISOU 1035  C   PHE A 134     4273   5577   6178   -328   -138    593       C  
ATOM   1036  O   PHE A 134      17.136   4.184  10.450  1.00 42.81           O  
ANISOU 1036  O   PHE A 134     4505   5729   6032   -275   -118    471       O  
ATOM   1037  CB  PHE A 134      19.606   5.024   9.522  1.00 40.51           C  
ANISOU 1037  CB  PHE A 134     3725   5499   6169   -303   -175    942       C  
ATOM   1038  CG  PHE A 134      20.758   4.911   8.574  1.00 39.72           C  
ANISOU 1038  CG  PHE A 134     3382   5547   6163   -252    -52   1241       C  
ATOM   1039  CD1 PHE A 134      20.839   3.846   7.696  1.00 38.03           C  
ANISOU 1039  CD1 PHE A 134     3230   5522   5697    -83    177   1316       C  
ATOM   1040  CD2 PHE A 134      21.756   5.870   8.554  1.00 42.23           C  
ANISOU 1040  CD2 PHE A 134     3399   5819   6829   -369   -163   1446       C  
ATOM   1041  CE1 PHE A 134      21.898   3.734   6.819  1.00 40.33           C  
ANISOU 1041  CE1 PHE A 134     3286   5992   6046     -6    335   1571       C  
ATOM   1042  CE2 PHE A 134      22.817   5.764   7.677  1.00 43.60           C  
ANISOU 1042  CE2 PHE A 134     3305   6170   7090   -327     -4   1745       C  
ATOM   1043  CZ  PHE A 134      22.888   4.694   6.808  1.00 42.33           C  
ANISOU 1043  CZ  PHE A 134     3208   6236   6641   -132    267   1799       C  
ATOM   1044  N   THR A 135      16.079   6.016   9.710  1.00 41.64           N  
ANISOU 1044  N   THR A 135     4227   5379   6216   -381   -182    480       N  
ATOM   1045  CA  THR A 135      14.800   5.694  10.326  1.00 38.67           C  
ANISOU 1045  CA  THR A 135     4030   4984   5677   -366   -143    215       C  
ATOM   1046  C   THR A 135      13.785   5.384   9.232  1.00 36.58           C  
ANISOU 1046  C   THR A 135     3819   4747   5333   -324    -15    276       C  
ATOM   1047  O   THR A 135      14.070   5.504   8.039  1.00 36.05           O  
ANISOU 1047  O   THR A 135     3683   4707   5308   -304     30    505       O  
ATOM   1048  CB  THR A 135      14.303   6.848  11.202  1.00 37.01           C  
ANISOU 1048  CB  THR A 135     3791   4606   5664   -424   -298    -15       C  
ATOM   1049  OG1 THR A 135      14.169   8.029  10.403  1.00 37.14           O  
ANISOU 1049  OG1 THR A 135     3654   4462   5995   -465   -393    100       O  
ATOM   1050  CG2 THR A 135      15.275   7.113  12.349  1.00 37.96           C  
ANISOU 1050  CG2 THR A 135     3903   4687   5832   -463   -472   -107       C  
ATOM   1051  N   ILE A 136      12.594   4.969   9.647  1.00 38.75           N  
ANISOU 1051  N   ILE A 136     4216   5027   5482   -316     43     78       N  
ATOM   1052  CA  ILE A 136      11.476   4.823   8.728  1.00 43.68           C  
ANISOU 1052  CA  ILE A 136     4869   5633   6093   -294    104    101       C  
ATOM   1053  C   ILE A 136      10.253   5.444   9.382  1.00 40.08           C  
ANISOU 1053  C   ILE A 136     4381   5085   5762   -321     79   -143       C  
ATOM   1054  O   ILE A 136      10.115   5.455  10.611  1.00 38.81           O  
ANISOU 1054  O   ILE A 136     4255   4948   5543   -338     91   -355       O  
ATOM   1055  CB  ILE A 136      11.209   3.355   8.324  1.00 50.99           C  
ANISOU 1055  CB  ILE A 136     5959   6680   6735   -242    217    144       C  
ATOM   1056  CG1 ILE A 136      10.602   2.557   9.475  1.00 54.95           C  
ANISOU 1056  CG1 ILE A 136     6579   7231   7069   -278    269    -45       C  
ATOM   1057  CG2 ILE A 136      12.502   2.685   7.857  1.00 53.74           C  
ANISOU 1057  CG2 ILE A 136     6335   7130   6953   -170    252    325       C  
ATOM   1058  CD1 ILE A 136      10.288   1.112   9.111  1.00 57.27           C  
ANISOU 1058  CD1 ILE A 136     7039   7590   7132   -250    329      7       C  
ATOM   1059  N   LYS A 137       9.378   5.993   8.547  1.00 38.06           N  
ANISOU 1059  N   LYS A 137     4055   4731   5676   -312     40   -113       N  
ATOM   1060  CA  LYS A 137       8.104   6.561   8.978  1.00 36.88           C  
ANISOU 1060  CA  LYS A 137     3831   4492   5689   -305     25   -342       C  
ATOM   1061  C   LYS A 137       7.047   5.520   8.636  1.00 38.92           C  
ANISOU 1061  C   LYS A 137     4153   4837   5796   -302    132   -353       C  
ATOM   1062  O   LYS A 137       6.491   5.510   7.538  1.00 42.28           O  
ANISOU 1062  O   LYS A 137     4564   5205   6296   -288     75   -233       O  
ATOM   1063  CB  LYS A 137       7.845   7.893   8.291  1.00 37.24           C  
ANISOU 1063  CB  LYS A 137     3737   4331   6082   -297   -145   -290       C  
ATOM   1064  CG  LYS A 137       8.822   8.978   8.685  1.00 43.26           C  
ANISOU 1064  CG  LYS A 137     4422   4962   7053   -326   -295   -280       C  
ATOM   1065  CD  LYS A 137       9.135   9.888   7.511  1.00 53.80           C  
ANISOU 1065  CD  LYS A 137     5666   6136   8640   -364   -456     -5       C  
ATOM   1066  CE  LYS A 137       9.769  11.194   7.969  1.00 59.07           C  
ANISOU 1066  CE  LYS A 137     6222   6587   9635   -410   -669    -32       C  
ATOM   1067  NZ  LYS A 137       8.814  12.031   8.747  1.00 59.66           N  
ANISOU 1067  NZ  LYS A 137     6241   6475   9951   -341   -784   -380       N  
ATOM   1068  N   GLY A 138       6.790   4.619   9.584  1.00 38.11           N  
ANISOU 1068  N   GLY A 138     4135   4868   5478   -329    264   -479       N  
ATOM   1069  CA  GLY A 138       5.888   3.521   9.380  1.00 39.78           C  
ANISOU 1069  CA  GLY A 138     4406   5153   5557   -361    350   -464       C  
ATOM   1070  C   GLY A 138       4.658   3.598  10.260  1.00 43.22           C  
ANISOU 1070  C   GLY A 138     4734   5636   6051   -392    463   -681       C  
ATOM   1071  O   GLY A 138       4.311   4.650  10.809  1.00 42.31           O  
ANISOU 1071  O   GLY A 138     4482   5475   6120   -349    464   -875       O  
ATOM   1072  N   SER A 139       3.984   2.458  10.389  1.00 47.35           N  
ANISOU 1072  N   SER A 139     5310   6253   6427   -464    559   -649       N  
ATOM   1073  CA  SER A 139       2.790   2.326  11.222  1.00 50.28           C  
ANISOU 1073  CA  SER A 139     5556   6723   6826   -519    717   -807       C  
ATOM   1074  C   SER A 139       2.988   1.069  12.065  1.00 46.65           C  
ANISOU 1074  C   SER A 139     5262   6418   6044   -628    842   -745       C  
ATOM   1075  O   SER A 139       2.812  -0.050  11.574  1.00 46.45           O  
ANISOU 1075  O   SER A 139     5335   6379   5934   -701    805   -580       O  
ATOM   1076  CB  SER A 139       1.528   2.248  10.374  1.00 54.70           C  
ANISOU 1076  CB  SER A 139     5954   7208   7621   -535    671   -776       C  
ATOM   1077  OG  SER A 139       0.368   2.404  11.173  1.00 59.99           O  
ANISOU 1077  OG  SER A 139     6415   7981   8396   -564    844   -948       O  
ATOM   1078  N   PHE A 140       3.364   1.260  13.327  1.00 43.46           N  
ANISOU 1078  N   PHE A 140     4911   6141   5460   -637    956   -874       N  
ATOM   1079  CA  PHE A 140       3.676   0.163  14.232  1.00 42.83           C  
ANISOU 1079  CA  PHE A 140     5019   6203   5051   -746   1047   -795       C  
ATOM   1080  C   PHE A 140       2.992   0.394  15.570  1.00 45.52           C  
ANISOU 1080  C   PHE A 140     5298   6742   5254   -791   1272   -978       C  
ATOM   1081  O   PHE A 140       3.072   1.493  16.130  1.00 47.03           O  
ANISOU 1081  O   PHE A 140     5420   6957   5491   -690   1305  -1211       O  
ATOM   1082  CB  PHE A 140       5.190   0.029  14.448  1.00 43.11           C  
ANISOU 1082  CB  PHE A 140     5257   6209   4912   -705    917   -725       C  
ATOM   1083  CG  PHE A 140       5.941  -0.504  13.258  1.00 42.63           C  
ANISOU 1083  CG  PHE A 140     5281   6018   4897   -659    754   -526       C  
ATOM   1084  CD1 PHE A 140       5.829  -1.835  12.890  1.00 41.81           C  
ANISOU 1084  CD1 PHE A 140     5312   5898   4676   -721    723   -359       C  
ATOM   1085  CD2 PHE A 140       6.782   0.321  12.525  1.00 42.05           C  
ANISOU 1085  CD2 PHE A 140     5157   5842   4979   -550    631   -506       C  
ATOM   1086  CE1 PHE A 140       6.529  -2.330  11.803  1.00 43.37           C  
ANISOU 1086  CE1 PHE A 140     5603   5990   4886   -638    585   -221       C  
ATOM   1087  CE2 PHE A 140       7.484  -0.169  11.438  1.00 42.51           C  
ANISOU 1087  CE2 PHE A 140     5286   5829   5036   -489    529   -330       C  
ATOM   1088  CZ  PHE A 140       7.358  -1.495  11.078  1.00 43.64           C  
ANISOU 1088  CZ  PHE A 140     5577   5970   5036   -514    511   -210       C  
ATOM   1089  N   LEU A 141       2.328  -0.639  16.077  1.00 45.55           N  
ANISOU 1089  N   LEU A 141     5333   6889   5085   -942   1424   -870       N  
ATOM   1090  CA  LEU A 141       1.774  -0.643  17.422  1.00 47.16           C  
ANISOU 1090  CA  LEU A 141     5521   7343   5054  -1010   1681   -987       C  
ATOM   1091  C   LEU A 141       2.492  -1.706  18.245  1.00 52.60           C  
ANISOU 1091  C   LEU A 141     6502   8130   5352  -1140   1672   -811       C  
ATOM   1092  O   LEU A 141       3.109  -2.626  17.701  1.00 49.06           O  
ANISOU 1092  O   LEU A 141     6217   7548   4877  -1194   1490   -585       O  
ATOM   1093  CB  LEU A 141       0.268  -0.914  17.409  1.00 46.56           C  
ANISOU 1093  CB  LEU A 141     5186   7387   5119  -1108   1899   -973       C  
ATOM   1094  CG  LEU A 141      -0.632   0.193  16.862  1.00 43.77           C  
ANISOU 1094  CG  LEU A 141     4504   6973   5152   -969   1936  -1186       C  
ATOM   1095  CD1 LEU A 141      -2.066  -0.290  16.844  1.00 42.24           C  
ANISOU 1095  CD1 LEU A 141     4034   6902   5112  -1093   2135  -1119       C  
ATOM   1096  CD2 LEU A 141      -0.509   1.460  17.687  1.00 45.84           C  
ANISOU 1096  CD2 LEU A 141     4716   7323   5379   -794   2041  -1527       C  
ATOM   1097  N   ASN A 142       2.414  -1.564  19.568  1.00 64.59           N  
ANISOU 1097  N   ASN A 142     8101   9881   6559  -1174   1859   -925       N  
ATOM   1098  CA  ASN A 142       3.060  -2.511  20.467  1.00 72.37           C  
ANISOU 1098  CA  ASN A 142     9384  10968   7145  -1305   1835   -750       C  
ATOM   1099  C   ASN A 142       2.724  -3.939  20.057  1.00 72.42           C  
ANISOU 1099  C   ASN A 142     9446  10918   7153  -1501   1797   -412       C  
ATOM   1100  O   ASN A 142       1.562  -4.272  19.807  1.00 75.62           O  
ANISOU 1100  O   ASN A 142     9651  11381   7702  -1615   1957   -334       O  
ATOM   1101  CB  ASN A 142       2.622  -2.245  21.908  1.00 81.08           C  
ANISOU 1101  CB  ASN A 142    10527  12297   7981  -1285   2022   -859       C  
ATOM   1102  CG  ASN A 142       2.990  -0.846  22.378  1.00 85.46           C  
ANISOU 1102  CG  ASN A 142    11072  12879   8521  -1084   2014  -1219       C  
ATOM   1103  OD1 ASN A 142       3.487  -0.029  21.604  1.00 83.73           O  
ANISOU 1103  OD1 ASN A 142    10774  12515   8523   -980   1890  -1395       O  
ATOM   1104  ND2 ASN A 142       2.738  -0.564  23.652  1.00 90.57           N  
ANISOU 1104  ND2 ASN A 142    11806  13702   8906  -1025   2138  -1333       N  
ATOM   1105  N   GLY A 143       3.753  -4.779  19.975  1.00 68.28           N  
ANISOU 1105  N   GLY A 143     9181  10256   6505  -1533   1558   -218       N  
ATOM   1106  CA  GLY A 143       3.602  -6.110  19.435  1.00 65.53           C  
ANISOU 1106  CA  GLY A 143     8917   9768   6212  -1677   1434     75       C  
ATOM   1107  C   GLY A 143       3.787  -6.206  17.937  1.00 60.71           C  
ANISOU 1107  C   GLY A 143     8234   8893   5939  -1564   1225     98       C  
ATOM   1108  O   GLY A 143       3.612  -7.295  17.375  1.00 62.11           O  
ANISOU 1108  O   GLY A 143     8488   8921   6191  -1658   1089    301       O  
ATOM   1109  N   SER A 144       4.124  -5.105  17.274  1.00 55.33           N  
ANISOU 1109  N   SER A 144     7423   8144   5456  -1369   1182    -99       N  
ATOM   1110  CA  SER A 144       4.408  -5.128  15.847  1.00 51.35           C  
ANISOU 1110  CA  SER A 144     6879   7422   5208  -1249    993    -69       C  
ATOM   1111  C   SER A 144       5.878  -5.459  15.617  1.00 51.91           C  
ANISOU 1111  C   SER A 144     7153   7377   5192  -1130    782     -4       C  
ATOM   1112  O   SER A 144       6.298  -5.695  14.485  1.00 51.19           O  
ANISOU 1112  O   SER A 144     7082   7130   5236  -1020    633     46       O  
ATOM   1113  CB  SER A 144       4.065  -3.788  15.201  1.00 49.45           C  
ANISOU 1113  CB  SER A 144     6400   7160   5227  -1114   1038   -263       C  
ATOM   1114  OG  SER A 144       4.931  -2.773  15.668  1.00 50.49           O  
ANISOU 1114  OG  SER A 144     6541   7328   5313   -993   1026   -419       O  
ATOM   1115  N   CSO A 145       6.663  -5.456  16.693  1.00 54.30           N  
ANISOU 1115  N   CSO A 145     7600   7770   5263  -1141    769    -12       N  
ATOM   1116  CA  CSO A 145       8.070  -5.835  16.602  1.00 54.29           C  
ANISOU 1116  CA  CSO A 145     7760   7666   5200  -1033    559     60       C  
ATOM   1117  C   CSO A 145       8.187  -7.238  16.019  1.00 56.31           C  
ANISOU 1117  C   CSO A 145     8170   7765   5459  -1054    405    254       C  
ATOM   1118  O   CSO A 145       7.396  -8.123  16.345  1.00 57.09           O  
ANISOU 1118  O   CSO A 145     8349   7862   5481  -1226    430    383       O  
ATOM   1119  CB  CSO A 145       8.751  -5.753  17.968  1.00 53.12           C  
ANISOU 1119  CB  CSO A 145     7762   7631   4790  -1075    531     41       C  
ATOM   1120  SG  CSO A 145       8.393  -4.159  18.748  1.00 52.47           S  
ANISOU 1120  SG  CSO A 145     7535   7721   4682  -1050    703   -239       S  
ATOM   1121  OD  CSO A 145       7.281  -4.351  20.123  1.00 53.34           O  
ANISOU 1121  OD  CSO A 145     7716   8085   4465  -1234    954   -271       O  
ATOM   1122  N   GLY A 146       9.168  -7.430  15.144  1.00 55.50           N  
ANISOU 1122  N   GLY A 146     8099   7530   5457   -876    245    273       N  
ATOM   1123  CA  GLY A 146       9.307  -8.679  14.422  1.00 53.45           C  
ANISOU 1123  CA  GLY A 146     7986   7096   5226   -833     80    396       C  
ATOM   1124  C   GLY A 146       8.855  -8.536  12.982  1.00 48.21           C  
ANISOU 1124  C   GLY A 146     7226   6343   4748   -731     79    346       C  
ATOM   1125  O   GLY A 146       9.311  -9.267  12.103  1.00 48.15           O  
ANISOU 1125  O   GLY A 146     7324   6196   4773   -592    -66    377       O  
ATOM   1126  N   SER A 147       7.941  -7.593  12.750  1.00 44.45           N  
ANISOU 1126  N   SER A 147     6559   5947   4384   -786    228    258       N  
ATOM   1127  CA  SER A 147       7.537  -7.252  11.392  1.00 39.85           C  
ANISOU 1127  CA  SER A 147     5883   5291   3969   -687    207    213       C  
ATOM   1128  C   SER A 147       8.766  -6.963  10.544  1.00 37.65           C  
ANISOU 1128  C   SER A 147     5615   4989   3702   -457    145    196       C  
ATOM   1129  O   SER A 147       9.737  -6.363  11.016  1.00 37.33           O  
ANISOU 1129  O   SER A 147     5518   5027   3638   -392    177    176       O  
ATOM   1130  CB  SER A 147       6.614  -6.036  11.404  1.00 38.25           C  
ANISOU 1130  CB  SER A 147     5445   5177   3910   -747    357    110       C  
ATOM   1131  OG  SER A 147       5.442  -6.292  12.154  1.00 39.17           O  
ANISOU 1131  OG  SER A 147     5503   5353   4027   -945    458    123       O  
ATOM   1132  N   VAL A 148       8.717  -7.380   9.283  1.00 33.32           N  
ANISOU 1132  N   VAL A 148     5132   4342   3187   -336     54    206       N  
ATOM   1133  CA  VAL A 148       9.883  -7.319   8.414  1.00 31.30           C  
ANISOU 1133  CA  VAL A 148     4901   4094   2897   -105     25    207       C  
ATOM   1134  C   VAL A 148       9.561  -6.514   7.164  1.00 33.69           C  
ANISOU 1134  C   VAL A 148     5109   4417   3275    -24     63    188       C  
ATOM   1135  O   VAL A 148       8.417  -6.470   6.699  1.00 33.15           O  
ANISOU 1135  O   VAL A 148     5034   4285   3275   -108     24    170       O  
ATOM   1136  CB  VAL A 148      10.380  -8.735   8.035  1.00 31.25           C  
ANISOU 1136  CB  VAL A 148     5123   3961   2788     27   -132    226       C  
ATOM   1137  CG1 VAL A 148      10.667  -9.560   9.289  1.00 32.95           C  
ANISOU 1137  CG1 VAL A 148     5452   4127   2941    -72   -213    282       C  
ATOM   1138  CG2 VAL A 148       9.363  -9.439   7.152  1.00 32.11           C  
ANISOU 1138  CG2 VAL A 148     5368   3923   2909      8   -259    205       C  
ATOM   1139  N   GLY A 149      10.591  -5.859   6.631  1.00 36.52           N  
ANISOU 1139  N   GLY A 149     5380   4866   3631    128    130    215       N  
ATOM   1140  CA  GLY A 149      10.515  -5.215   5.340  1.00 36.51           C  
ANISOU 1140  CA  GLY A 149     5332   4897   3644    225    158    244       C  
ATOM   1141  C   GLY A 149      11.177  -6.086   4.291  1.00 35.33           C  
ANISOU 1141  C   GLY A 149     5351   4749   3322    450    119    247       C  
ATOM   1142  O   GLY A 149      12.019  -6.926   4.602  1.00 33.75           O  
ANISOU 1142  O   GLY A 149     5234   4545   3043    565     97    229       O  
ATOM   1143  N   PHE A 150      10.787  -5.888   3.036  1.00 29.51           N  
ANISOU 1143  N   PHE A 150     4677   4018   2518    530     98    257       N  
ATOM   1144  CA  PHE A 150      11.220  -6.830   2.015  1.00 30.85           C  
ANISOU 1144  CA  PHE A 150     5061   4184   2477    761     47    210       C  
ATOM   1145  C   PHE A 150      10.994  -6.258   0.627  1.00 30.35           C  
ANISOU 1145  C   PHE A 150     5041   4195   2297    851     66    254       C  
ATOM   1146  O   PHE A 150      10.140  -5.391   0.413  1.00 31.07           O  
ANISOU 1146  O   PHE A 150     5048   4260   2499    706     33    308       O  
ATOM   1147  CB  PHE A 150      10.474  -8.164   2.149  1.00 34.55           C  
ANISOU 1147  CB  PHE A 150     5769   4447   2910    738   -165    103       C  
ATOM   1148  CG  PHE A 150       9.000  -8.051   1.884  1.00 34.78           C  
ANISOU 1148  CG  PHE A 150     5833   4348   3032    561   -307     90       C  
ATOM   1149  CD1 PHE A 150       8.124  -7.727   2.907  1.00 32.70           C  
ANISOU 1149  CD1 PHE A 150     5420   4035   2970    305   -305    118       C  
ATOM   1150  CD2 PHE A 150       8.492  -8.249   0.607  1.00 34.73           C  
ANISOU 1150  CD2 PHE A 150     6000   4284   2910    661   -443     46       C  
ATOM   1151  CE1 PHE A 150       6.766  -7.611   2.667  1.00 33.65           C  
ANISOU 1151  CE1 PHE A 150     5514   4050   3221    150   -425    110       C  
ATOM   1152  CE2 PHE A 150       7.135  -8.132   0.358  1.00 34.87           C  
ANISOU 1152  CE2 PHE A 150     6022   4171   3056    495   -610     41       C  
ATOM   1153  CZ  PHE A 150       6.269  -7.813   1.390  1.00 34.54           C  
ANISOU 1153  CZ  PHE A 150     5781   4080   3264    239   -596     78       C  
ATOM   1154  N   ASN A 151      11.776  -6.772  -0.315  1.00 29.03           N  
ANISOU 1154  N   ASN A 151     5013   4124   1894   1107    116    226       N  
ATOM   1155  CA  ASN A 151      11.589  -6.538  -1.734  1.00 31.26           C  
ANISOU 1155  CA  ASN A 151     5433   4487   1958   1234    114    248       C  
ATOM   1156  C   ASN A 151      11.454  -7.887  -2.426  1.00 38.85           C  
ANISOU 1156  C   ASN A 151     6730   5345   2687   1446    -49     62       C  
ATOM   1157  O   ASN A 151      11.974  -8.903  -1.952  1.00 37.82           O  
ANISOU 1157  O   ASN A 151     6681   5142   2546   1567    -87    -54       O  
ATOM   1158  CB  ASN A 151      12.759  -5.755  -2.339  1.00 33.29           C  
ANISOU 1158  CB  ASN A 151     5537   5017   2095   1368    376    400       C  
ATOM   1159  CG  ASN A 151      12.765  -4.295  -1.920  1.00 36.42           C  
ANISOU 1159  CG  ASN A 151     5637   5470   2730   1148    471    597       C  
ATOM   1160  OD1 ASN A 151      13.416  -3.919  -0.946  1.00 38.48           O  
ANISOU 1160  OD1 ASN A 151     5668   5762   3190   1069    564    648       O  
ATOM   1161  ND2 ASN A 151      12.043  -3.466  -2.659  1.00 37.73           N  
ANISOU 1161  ND2 ASN A 151     5821   5628   2888   1055    412    705       N  
ATOM   1162  N   ILE A 152      10.743  -7.896  -3.546  1.00 45.82           N  
ANISOU 1162  N   ILE A 152     7822   6195   3391   1495   -185     29       N  
ATOM   1163  CA  ILE A 152      10.579  -9.092  -4.359  1.00 50.18           C  
ANISOU 1163  CA  ILE A 152     8704   6628   3733   1699   -376   -171       C  
ATOM   1164  C   ILE A 152      11.125  -8.792  -5.745  1.00 57.11           C  
ANISOU 1164  C   ILE A 152     9613   7702   4384   1880   -231   -150       C  
ATOM   1165  O   ILE A 152      10.724  -7.808  -6.379  1.00 55.64           O  
ANISOU 1165  O   ILE A 152     9381   7611   4150   1776   -206     -6       O  
ATOM   1166  CB  ILE A 152       9.109  -9.544  -4.421  1.00 47.87           C  
ANISOU 1166  CB  ILE A 152     8604   6052   3533   1534   -737   -251       C  
ATOM   1167  CG1 ILE A 152       8.577  -9.771  -3.003  1.00 45.32           C  
ANISOU 1167  CG1 ILE A 152     8108   5551   3562   1267   -808   -222       C  
ATOM   1168  CG2 ILE A 152       8.977 -10.821  -5.235  1.00 48.81           C  
ANISOU 1168  CG2 ILE A 152     9008   5991   3548   1714   -955   -460       C  
ATOM   1169  CD1 ILE A 152       7.134 -10.223  -2.942  1.00 47.16           C  
ANISOU 1169  CD1 ILE A 152     8429   5512   3977   1056  -1130   -263       C  
ATOM   1170  N   ASP A 153      12.058  -9.624  -6.201  1.00 65.99           N  
ANISOU 1170  N   ASP A 153    10819   8892   5364   2153   -144   -283       N  
ATOM   1171  CA  ASP A 153      12.652  -9.513  -7.532  1.00 74.40           C  
ANISOU 1171  CA  ASP A 153    11936  10162   6172   2352      5   -285       C  
ATOM   1172  C   ASP A 153      12.432 -10.846  -8.242  1.00 76.47           C  
ANISOU 1172  C   ASP A 153    12519  10244   6292   2575   -220   -543       C  
ATOM   1173  O   ASP A 153      13.117 -11.831  -7.950  1.00 72.55           O  
ANISOU 1173  O   ASP A 153    12074   9693   5800   2791   -225   -696       O  
ATOM   1174  CB  ASP A 153      14.137  -9.168  -7.449  1.00 81.04           C  
ANISOU 1174  CB  ASP A 153    12522  11297   6974   2499    362   -184       C  
ATOM   1175  CG  ASP A 153      14.795  -9.086  -8.816  1.00 89.73           C  
ANISOU 1175  CG  ASP A 153    13666  12638   7790   2697    542   -176       C  
ATOM   1176  OD1 ASP A 153      14.766  -7.998  -9.430  1.00 91.43           O  
ANISOU 1176  OD1 ASP A 153    13785  13034   7921   2567    676     31       O  
ATOM   1177  OD2 ASP A 153      15.340 -10.111  -9.278  1.00 94.55           O  
ANISOU 1177  OD2 ASP A 153    14415  13255   8254   2981    540   -373       O  
ATOM   1178  N   TYR A 154      11.468 -10.870  -9.166  1.00 84.03           N  
ANISOU 1178  N   TYR A 154    13696  11093   7138   2530   -437   -590       N  
ATOM   1179  CA  TYR A 154      11.170 -12.060  -9.957  1.00 92.52           C  
ANISOU 1179  CA  TYR A 154    15094  11980   8079   2733   -687   -828       C  
ATOM   1180  C   TYR A 154      10.534 -13.132  -9.080  1.00 90.79           C  
ANISOU 1180  C   TYR A 154    15003  11390   8104   2674  -1013   -969       C  
ATOM   1181  O   TYR A 154       9.308 -13.279  -9.064  1.00 92.89           O  
ANISOU 1181  O   TYR A 154    15392  11400   8501   2483  -1324   -985       O  
ATOM   1182  CB  TYR A 154      12.440 -12.586 -10.629  1.00100.15           C  
ANISOU 1182  CB  TYR A 154    16092  13157   8802   3084   -469   -940       C  
ATOM   1183  CG  TYR A 154      12.232 -13.763 -11.567  1.00105.79           C  
ANISOU 1183  CG  TYR A 154    17152  13708   9337   3336   -715  -1196       C  
ATOM   1184  CD1 TYR A 154      10.962 -14.128 -11.999  1.00106.87           C  
ANISOU 1184  CD1 TYR A 154    17549  13556   9502   3232  -1095  -1282       C  
ATOM   1185  CD2 TYR A 154      13.313 -14.513 -12.011  1.00109.72           C  
ANISOU 1185  CD2 TYR A 154    17703  14335   9652   3685   -582  -1356       C  
ATOM   1186  CE1 TYR A 154      10.778 -15.204 -12.848  1.00111.56           C  
ANISOU 1186  CE1 TYR A 154    18465  13980   9944   3466  -1347  -1515       C  
ATOM   1187  CE2 TYR A 154      13.138 -15.589 -12.859  1.00114.55           C  
ANISOU 1187  CE2 TYR A 154    18637  14792  10093   3933   -821  -1605       C  
ATOM   1188  CZ  TYR A 154      11.871 -15.931 -13.275  1.00115.74           C  
ANISOU 1188  CZ  TYR A 154    19061  14642  10272   3822  -1210  -1683       C  
ATOM   1189  OH  TYR A 154      11.700 -17.003 -14.121  1.00121.27           O  
ANISOU 1189  OH  TYR A 154    20092  15172  10812   4073  -1476  -1932       O  
ATOM   1190  N   ASP A 155      11.352 -13.894  -8.356  1.00 86.65           N  
ANISOU 1190  N   ASP A 155    14443  10826   7653   2826   -965  -1056       N  
ATOM   1191  CA  ASP A 155      10.836 -14.942  -7.486  1.00 81.65           C  
ANISOU 1191  CA  ASP A 155    13940   9835   7247   2755  -1283  -1159       C  
ATOM   1192  C   ASP A 155      11.629 -15.032  -6.190  1.00 77.41           C  
ANISOU 1192  C   ASP A 155    13223   9334   6854   2745  -1143  -1111       C  
ATOM   1193  O   ASP A 155      11.480 -16.019  -5.454  1.00 77.98           O  
ANISOU 1193  O   ASP A 155    13417   9127   7085   2730  -1389  -1197       O  
ATOM   1194  CB  ASP A 155      10.845 -16.295  -8.212  1.00 82.67           C  
ANISOU 1194  CB  ASP A 155    14376   9744   7291   3018  -1560  -1391       C  
ATOM   1195  CG  ASP A 155      12.247 -16.784  -8.528  1.00 83.32           C  
ANISOU 1195  CG  ASP A 155    14443  10019   7196   3393  -1355  -1511       C  
ATOM   1196  OD1 ASP A 155      13.178 -15.954  -8.580  1.00 82.76           O  
ANISOU 1196  OD1 ASP A 155    14132  10301   7011   3462   -969  -1404       O  
ATOM   1197  OD2 ASP A 155      12.419 -18.005  -8.728  1.00 85.25           O  
ANISOU 1197  OD2 ASP A 155    14899  10059   7433   3614  -1595  -1705       O  
ATOM   1198  N   CYS A 156      12.447 -14.033  -5.880  1.00 73.70           N  
ANISOU 1198  N   CYS A 156    14746   7075   6183    874    339    135       N  
ATOM   1199  CA  CYS A 156      13.359 -14.072  -4.747  1.00 68.53           C  
ANISOU 1199  CA  CYS A 156    13849   6555   5634   1192    529    157       C  
ATOM   1200  C   CYS A 156      13.006 -12.948  -3.787  1.00 57.41           C  
ANISOU 1200  C   CYS A 156    11808   5524   4480    931    547    246       C  
ATOM   1201  O   CYS A 156      13.040 -11.770  -4.160  1.00 53.82           O  
ANISOU 1201  O   CYS A 156    10821   5363   4266    912    643    316       O  
ATOM   1202  CB  CYS A 156      14.808 -13.951  -5.218  1.00 72.30           C  
ANISOU 1202  CB  CYS A 156    14234   7151   6087   1844    856    213       C  
ATOM   1203  SG  CYS A 156      16.010 -13.914  -3.882  1.00 72.91           S  
ANISOU 1203  SG  CYS A 156    13917   7465   6319   2238   1084    295       S  
ATOM   1204  N   VAL A 157      12.671 -13.316  -2.555  1.00 51.43           N  
ANISOU 1204  N   VAL A 157    10973   4738   3831    713    430    228       N  
ATOM   1205  CA  VAL A 157      12.326 -12.356  -1.515  1.00 46.06           C  
ANISOU 1205  CA  VAL A 157     9547   4372   3580    463    421    271       C  
ATOM   1206  C   VAL A 157      13.609 -11.887  -0.843  1.00 45.28           C  
ANISOU 1206  C   VAL A 157     9018   4492   3694    874    677    308       C  
ATOM   1207  O   VAL A 157      14.310 -12.678  -0.204  1.00 47.96           O  
ANISOU 1207  O   VAL A 157     9578   4719   3927   1129    742    290       O  
ATOM   1208  CB  VAL A 157      11.365 -12.975  -0.490  1.00 45.96           C  
ANISOU 1208  CB  VAL A 157     9634   4258   3570     34    183    253       C  
ATOM   1209  CG1 VAL A 157      11.084 -11.996   0.640  1.00 45.72           C  
ANISOU 1209  CG1 VAL A 157     8877   4552   3944   -139    213    289       C  
ATOM   1210  CG2 VAL A 157      10.075 -13.407  -1.166  1.00 46.59           C  
ANISOU 1210  CG2 VAL A 157    10087   4177   3438   -436   -105    276       C  
ATOM   1211  N   SER A 158      13.917 -10.602  -0.979  1.00 44.42           N  
ANISOU 1211  N   SER A 158     8308   4692   3876    919    800    381       N  
ATOM   1212  CA  SER A 158      15.071  -9.999  -0.316  1.00 46.40           C  
ANISOU 1212  CA  SER A 158     8085   5191   4354   1205    991    461       C  
ATOM   1213  C   SER A 158      14.577  -9.356   0.977  1.00 43.31           C  
ANISOU 1213  C   SER A 158     7238   4937   4281    895    889    448       C  
ATOM   1214  O   SER A 158      13.947  -8.296   0.955  1.00 42.40           O  
ANISOU 1214  O   SER A 158     6748   4972   4389    649    830    463       O  
ATOM   1215  CB  SER A 158      15.753  -8.978  -1.220  1.00 50.07           C  
ANISOU 1215  CB  SER A 158     8212   5899   4915   1406   1158    576       C  
ATOM   1216  OG  SER A 158      16.306  -9.597  -2.371  1.00 55.90           O  
ANISOU 1216  OG  SER A 158     9375   6538   5325   1759   1293    598       O  
ATOM   1217  N   PHE A 159      14.852 -10.008   2.106  1.00 40.38           N  
ANISOU 1217  N   PHE A 159     6933   4502   3907    931    870    421       N  
ATOM   1218  CA  PHE A 159      14.535  -9.435   3.407  1.00 37.07           C  
ANISOU 1218  CA  PHE A 159     6116   4215   3755    698    801    411       C  
ATOM   1219  C   PHE A 159      15.610  -8.432   3.801  1.00 37.02           C  
ANISOU 1219  C   PHE A 159     5618   4460   3989    883    928    513       C  
ATOM   1220  O   PHE A 159      16.806  -8.745   3.769  1.00 40.62           O  
ANISOU 1220  O   PHE A 159     6078   4975   4381   1223   1060    604       O  
ATOM   1221  CB  PHE A 159      14.411 -10.529   4.464  1.00 38.73           C  
ANISOU 1221  CB  PHE A 159     6606   4258   3851    639    716    356       C  
ATOM   1222  CG  PHE A 159      13.270 -11.463   4.217  1.00 38.40           C  
ANISOU 1222  CG  PHE A 159     7030   3981   3579    350    536    291       C  
ATOM   1223  CD1 PHE A 159      11.982 -11.114   4.583  1.00 33.65           C  
ANISOU 1223  CD1 PHE A 159     6249   3458   3078    -75    385    283       C  
ATOM   1224  CD2 PHE A 159      13.480 -12.681   3.597  1.00 41.61           C  
ANISOU 1224  CD2 PHE A 159     8070   4096   3644    505    506    262       C  
ATOM   1225  CE1 PHE A 159      10.926 -11.966   4.343  1.00 34.73           C  
ANISOU 1225  CE1 PHE A 159     6775   3425   2995   -400    188    279       C  
ATOM   1226  CE2 PHE A 159      12.428 -13.539   3.357  1.00 44.49           C  
ANISOU 1226  CE2 PHE A 159     8910   4221   3772    171    288    227       C  
ATOM   1227  CZ  PHE A 159      11.149 -13.181   3.729  1.00 41.07           C  
ANISOU 1227  CZ  PHE A 159     8238   3908   3459   -312    119    252       C  
ATOM   1228  N   CYS A 160      15.177  -7.230   4.182  1.00 35.40           N  
ANISOU 1228  N   CYS A 160     5005   4407   4040    659    875    519       N  
ATOM   1229  CA  CYS A 160      16.085  -6.122   4.427  1.00 32.94           C  
ANISOU 1229  CA  CYS A 160     4265   4306   3943    746    938    632       C  
ATOM   1230  C   CYS A 160      15.827  -5.372   5.724  1.00 31.46           C  
ANISOU 1230  C   CYS A 160     3804   4181   3970    538    845    602       C  
ATOM   1231  O   CYS A 160      16.630  -4.500   6.074  1.00 32.63           O  
ANISOU 1231  O   CYS A 160     3655   4469   4274    567    852    704       O  
ATOM   1232  CB  CYS A 160      16.007  -5.109   3.273  1.00 33.57           C  
ANISOU 1232  CB  CYS A 160     4172   4490   4094    728    969    698       C  
ATOM   1233  SG  CYS A 160      14.377  -4.338   3.085  1.00 35.16           S  
ANISOU 1233  SG  CYS A 160     4312   4649   4400    386    829    596       S  
ATOM   1234  N   TYR A 161      14.741  -5.657   6.436  1.00 28.06           N  
ANISOU 1234  N   TYR A 161     3472   3659   3529    321    750    484       N  
ATOM   1235  CA  TYR A 161      14.410  -4.883   7.622  1.00 28.78           C  
ANISOU 1235  CA  TYR A 161     3340   3809   3787    162    683    446       C  
ATOM   1236  C   TYR A 161      13.615  -5.737   8.592  1.00 26.90           C  
ANISOU 1236  C   TYR A 161     3273   3492   3457     16    623    355       C  
ATOM   1237  O   TYR A 161      12.771  -6.537   8.182  1.00 30.58           O  
ANISOU 1237  O   TYR A 161     3968   3877   3774    -91    584    318       O  
ATOM   1238  CB  TYR A 161      13.610  -3.629   7.253  1.00 32.26           C  
ANISOU 1238  CB  TYR A 161     3582   4314   4362     32    646    430       C  
ATOM   1239  CG  TYR A 161      13.184  -2.774   8.427  1.00 30.80           C  
ANISOU 1239  CG  TYR A 161     3238   4162   4304    -78    589    378       C  
ATOM   1240  CD1 TYR A 161      14.031  -1.814   8.958  1.00 30.58           C  
ANISOU 1240  CD1 TYR A 161     3053   4162   4405    -51    557    428       C  
ATOM   1241  CD2 TYR A 161      11.923  -2.911   8.987  1.00 29.42           C  
ANISOU 1241  CD2 TYR A 161     3089   3999   4091   -210    560    299       C  
ATOM   1242  CE1 TYR A 161      13.639  -1.023  10.020  1.00 28.88           C  
ANISOU 1242  CE1 TYR A 161     2785   3929   4258   -130    496    365       C  
ATOM   1243  CE2 TYR A 161      11.522  -2.126  10.048  1.00 26.24           C  
ANISOU 1243  CE2 TYR A 161     2578   3630   3763   -247    538    250       C  
ATOM   1244  CZ  TYR A 161      12.383  -1.184  10.560  1.00 28.94           C  
ANISOU 1244  CZ  TYR A 161     2839   3943   4212   -195    505    265       C  
ATOM   1245  OH  TYR A 161      11.990  -0.397  11.617  1.00 32.61           O  
ANISOU 1245  OH  TYR A 161     3287   4396   4708   -211    474    200       O  
ATOM   1246  N   MET A 162      13.905  -5.563   9.877  1.00 25.10           N  
ANISOU 1246  N   MET A 162     2946   3291   3301    -13    596    339       N  
ATOM   1247  CA  MET A 162      13.105  -6.123  10.957  1.00 26.45           C  
ANISOU 1247  CA  MET A 162     3214   3432   3405   -174    544    268       C  
ATOM   1248  C   MET A 162      12.876  -5.009  11.965  1.00 25.18           C  
ANISOU 1248  C   MET A 162     2832   3356   3381   -242    523    233       C  
ATOM   1249  O   MET A 162      13.819  -4.297  12.325  1.00 24.26           O  
ANISOU 1249  O   MET A 162     2591   3257   3371   -166    511    271       O  
ATOM   1250  CB  MET A 162      13.793  -7.315  11.623  1.00 31.25           C  
ANISOU 1250  CB  MET A 162     4040   3943   3892    -99    533    278       C  
ATOM   1251  CG  MET A 162      13.060  -7.827  12.857  1.00 34.69           C  
ANISOU 1251  CG  MET A 162     4557   4364   4260   -284    473    224       C  
ATOM   1252  SD  MET A 162      13.742  -9.352  13.537  1.00 37.95           S  
ANISOU 1252  SD  MET A 162     5298   4621   4499   -213    436    242       S  
ATOM   1253  CE  MET A 162      13.082 -10.548  12.378  1.00 39.12           C  
ANISOU 1253  CE  MET A 162     5854   4595   4416   -274    392    238       C  
ATOM   1254  N   HIS A 163      11.639  -4.847  12.411  1.00 26.95           N  
ANISOU 1254  N   HIS A 163     3021   3639   3578   -382    512    181       N  
ATOM   1255  CA  HIS A 163      11.288  -3.733  13.275  1.00 28.03           C  
ANISOU 1255  CA  HIS A 163     3007   3843   3801   -387    515    137       C  
ATOM   1256  C   HIS A 163      11.579  -4.059  14.735  1.00 29.79           C  
ANISOU 1256  C   HIS A 163     3300   4044   3973   -417    493    100       C  
ATOM   1257  O   HIS A 163      11.195  -5.126  15.229  1.00 30.13           O  
ANISOU 1257  O   HIS A 163     3464   4092   3893   -511    488     98       O  
ATOM   1258  CB  HIS A 163       9.819  -3.361  13.120  1.00 28.83           C  
ANISOU 1258  CB  HIS A 163     3007   4071   3876   -456    545    128       C  
ATOM   1259  CG  HIS A 163       9.390  -2.286  14.058  1.00 29.43           C  
ANISOU 1259  CG  HIS A 163     2990   4205   3987   -389    574     75       C  
ATOM   1260  ND1 HIS A 163       9.824  -0.984  13.937  1.00 29.55           N  
ANISOU 1260  ND1 HIS A 163     2961   4152   4113   -273    556     51       N  
ATOM   1261  CD2 HIS A 163       8.601  -2.321  15.155  1.00 31.80           C  
ANISOU 1261  CD2 HIS A 163     3275   4611   4195   -405    619     48       C  
ATOM   1262  CE1 HIS A 163       9.301  -0.259  14.909  1.00 31.74           C  
ANISOU 1262  CE1 HIS A 163     3251   4456   4354   -199    584     -9       C  
ATOM   1263  NE2 HIS A 163       8.555  -1.046  15.662  1.00 30.94           N  
ANISOU 1263  NE2 HIS A 163     3148   4480   4129   -258    641    -11       N  
ATOM   1264  N   HIS A 164      12.225  -3.120  15.427  1.00 29.46           N  
ANISOU 1264  N   HIS A 164     3212   3970   4011   -365    458     81       N  
ATOM   1265  CA  HIS A 164      12.664  -3.338  16.798  1.00 27.51           C  
ANISOU 1265  CA  HIS A 164     3052   3688   3712   -398    414     55       C  
ATOM   1266  C   HIS A 164      12.051  -2.370  17.795  1.00 32.13           C  
ANISOU 1266  C   HIS A 164     3653   4286   4270   -393    418    -27       C  
ATOM   1267  O   HIS A 164      11.582  -2.805  18.853  1.00 34.13           O  
ANISOU 1267  O   HIS A 164     3985   4577   4407   -437    442    -70       O  
ATOM   1268  CB  HIS A 164      14.194  -3.242  16.884  1.00 23.56           C  
ANISOU 1268  CB  HIS A 164     2538   3128   3285   -358    331    139       C  
ATOM   1269  CG  HIS A 164      14.904  -4.475  16.428  1.00 23.97           C  
ANISOU 1269  CG  HIS A 164     2640   3174   3295   -295    348    220       C  
ATOM   1270  ND1 HIS A 164      15.573  -5.311  17.295  1.00 23.22           N  
ANISOU 1270  ND1 HIS A 164     2639   3051   3134   -288    305    257       N  
ATOM   1271  CD2 HIS A 164      15.056  -5.012  15.195  1.00 23.27           C  
ANISOU 1271  CD2 HIS A 164     2561   3087   3195   -203    405    272       C  
ATOM   1272  CE1 HIS A 164      16.107  -6.311  16.616  1.00 24.66           C  
ANISOU 1272  CE1 HIS A 164     2891   3213   3264   -164    343    329       C  
ATOM   1273  NE2 HIS A 164      15.808  -6.153  15.339  1.00 23.60           N  
ANISOU 1273  NE2 HIS A 164     2725   3091   3151   -107    407    333       N  
ATOM   1274  N   MET A 165      12.062  -1.066  17.521  1.00 34.14           N  
ANISOU 1274  N   MET A 165     3874   4496   4602   -328    393    -47       N  
ATOM   1275  C   MET A 165      10.982   1.106  17.831  1.00 36.40           C  
ANISOU 1275  C   MET A 165     4239   4723   4868   -150    416   -159       C  
ATOM   1276  O   MET A 165      11.209   1.370  16.648  1.00 35.59           O  
ANISOU 1276  O   MET A 165     4030   4613   4880   -152    395    -98       O  
ATOM   1277  CA  MET A 165      11.601  -0.106  18.509  1.00 36.91           C  
ANISOU 1277  CA  MET A 165     4334   4805   4885   -270    390   -135       C  
ATOM   1278  CB  MET A 165      12.756   0.347  19.410  1.00 39.72           C  
ANISOU 1278  CB  MET A 165     4842   5012   5238   -333    239   -132       C  
ATOM   1279  CG  MET A 165      13.721   1.283  18.709  1.00 40.53           C  
ANISOU 1279  CG  MET A 165     4920   5010   5468   -373    104    -49       C  
ATOM   1280  SD  MET A 165      15.393   1.199  19.370  1.00 43.52           S  
ANISOU 1280  SD  MET A 165     5335   5324   5876   -538   -101     81       S  
ATOM   1281  CE  MET A 165      15.146   1.821  21.030  1.00 43.50           C  
ANISOU 1281  CE  MET A 165     5659   5166   5703   -576   -197    -45       C  
ATOM   1282  N   GLU A 166      10.205   1.841  18.617  1.00 35.72           N  
ANISOU 1282  N   GLU A 166     4271   4629   4673    -19    468   -245       N  
ATOM   1283  CA  GLU A 166       9.730   3.170  18.266  1.00 41.58           C  
ANISOU 1283  CA  GLU A 166     5083   5293   5423    150    472   -282       C  
ATOM   1284  C   GLU A 166      10.502   4.177  19.111  1.00 43.68           C  
ANISOU 1284  C   GLU A 166     5664   5299   5632    151    319   -346       C  
ATOM   1285  O   GLU A 166      10.742   3.946  20.301  1.00 45.15           O  
ANISOU 1285  O   GLU A 166     6023   5435   5696    116    291   -400       O  
ATOM   1286  CB  GLU A 166       8.228   3.307  18.510  1.00 47.58           C  
ANISOU 1286  CB  GLU A 166     5775   6245   6059    362    656   -312       C  
ATOM   1287  CG  GLU A 166       7.675   4.692  18.204  1.00 54.54           C  
ANISOU 1287  CG  GLU A 166     6761   7040   6920    613    676   -349       C  
ATOM   1288  CD  GLU A 166       6.158   4.733  18.234  1.00 58.42           C  
ANISOU 1288  CD  GLU A 166     7083   7811   7303    859    882   -316       C  
ATOM   1289  OE1 GLU A 166       5.588   5.274  19.205  1.00 60.50           O  
ANISOU 1289  OE1 GLU A 166     7516   8087   7383   1113    984   -384       O  
ATOM   1290  OE2 GLU A 166       5.536   4.212  17.285  1.00 58.10           O  
ANISOU 1290  OE2 GLU A 166     6741   7994   7340    801    939   -205       O  
ATOM   1291  N   LEU A 167      10.907   5.271  18.500  1.00 43.81           N  
ANISOU 1291  N   LEU A 167     5784   5139   5721    158    196   -326       N  
ATOM   1292  CA  LEU A 167      11.657   6.264  19.251  1.00 46.35           C  
ANISOU 1292  CA  LEU A 167     6464   5180   5967     99     -4   -363       C  
ATOM   1293  C   LEU A 167      10.712   7.269  19.888  1.00 50.41           C  
ANISOU 1293  C   LEU A 167     7304   5559   6291    383     57   -499       C  
ATOM   1294  O   LEU A 167       9.564   7.421  19.458  1.00 46.97           O  
ANISOU 1294  O   LEU A 167     6752   5263   5831    638    243   -525       O  
ATOM   1295  CB  LEU A 167      12.647   6.982  18.340  1.00 45.54           C  
ANISOU 1295  CB  LEU A 167     6358   4937   6008    -78   -207   -241       C  
ATOM   1296  CG  LEU A 167      13.666   6.107  17.605  1.00 46.33           C  
ANISOU 1296  CG  LEU A 167     6135   5195   6275   -294   -248    -76       C  
ATOM   1297  CD1 LEU A 167      14.678   6.980  16.872  1.00 50.05           C  
ANISOU 1297  CD1 LEU A 167     6614   5553   6849   -477   -459     79       C  
ATOM   1298  CD2 LEU A 167      14.371   5.148  18.554  1.00 46.85           C  
ANISOU 1298  CD2 LEU A 167     6178   5323   6299   -426   -285    -48       C  
ATOM   1299  N   PRO A 168      11.165   7.980  20.927  1.00 55.73           N  
ANISOU 1299  N   PRO A 168     8410   5961   6803    361   -101   -575       N  
ATOM   1300  CA  PRO A 168      10.287   8.956  21.584  1.00 59.22           C  
ANISOU 1300  CA  PRO A 168     9252   6238   7010    697    -31   -718       C  
ATOM   1301  C   PRO A 168       9.682   9.985  20.633  1.00 59.87           C  
ANISOU 1301  C   PRO A 168     9395   6229   7125    926     -7   -718       C  
ATOM   1302  O   PRO A 168       8.660  10.586  20.963  1.00 61.16           O  
ANISOU 1302  O   PRO A 168     9764   6368   7105   1317    147   -814       O  
ATOM   1303  CB  PRO A 168      11.212   9.625  22.613  1.00 62.19           C  
ANISOU 1303  CB  PRO A 168    10152   6253   7223    530   -306   -770       C  
ATOM   1304  CG  PRO A 168      12.264   8.598  22.898  1.00 60.23           C  
ANISOU 1304  CG  PRO A 168     9673   6121   7090    164   -421   -664       C  
ATOM   1305  CD  PRO A 168      12.476   7.862  21.599  1.00 56.53           C  
ANISOU 1305  CD  PRO A 168     8669   5911   6898     43   -351   -519       C  
ATOM   1306  N   THR A 169      10.286  10.191  19.457  1.00 59.85           N  
ANISOU 1306  N   THR A 169     9212   6192   7336    718   -144   -597       N  
ATOM   1307  CA  THR A 169       9.741  11.140  18.490  1.00 60.26           C  
ANISOU 1307  CA  THR A 169     9311   6156   7428    912   -136   -581       C  
ATOM   1308  C   THR A 169       8.644  10.543  17.615  1.00 56.60           C  
ANISOU 1308  C   THR A 169     8380   6056   7068   1111    129   -533       C  
ATOM   1309  O   THR A 169       7.996  11.287  16.871  1.00 58.58           O  
ANISOU 1309  O   THR A 169     8645   6280   7333   1332    168   -516       O  
ATOM   1310  CB  THR A 169      10.852  11.672  17.583  1.00 62.58           C  
ANISOU 1310  CB  THR A 169     9619   6270   7887    584   -406   -447       C  
ATOM   1311  OG1 THR A 169      11.300  10.622  16.716  1.00 64.11           O  
ANISOU 1311  OG1 THR A 169     9297   6758   8303    359   -349   -311       O  
ATOM   1312  CG2 THR A 169      12.020  12.177  18.412  1.00 63.28           C  
ANISOU 1312  CG2 THR A 169    10115   6046   7881    290   -716   -431       C  
ATOM   1313  N   GLY A 170       8.429   9.231  17.670  1.00 52.22           N  
ANISOU 1313  N   GLY A 170     7440   5829   6574   1018    283   -494       N  
ATOM   1314  CA  GLY A 170       7.408   8.583  16.877  1.00 49.90           C  
ANISOU 1314  CA  GLY A 170     6725   5881   6355   1127    487   -419       C  
ATOM   1315  C   GLY A 170       7.915   7.882  15.634  1.00 49.23           C  
ANISOU 1315  C   GLY A 170     6307   5914   6485    855    435   -298       C  
ATOM   1316  O   GLY A 170       7.122   7.222  14.951  1.00 48.26           O  
ANISOU 1316  O   GLY A 170     5863   6064   6409    880    567   -225       O  
ATOM   1317  N   VAL A 171       9.204   8.010  15.316  1.00 50.50           N  
ANISOU 1317  N   VAL A 171     6542   5892   6753    596    242   -253       N  
ATOM   1318  CA  VAL A 171       9.787   7.321  14.170  1.00 46.96           C  
ANISOU 1318  CA  VAL A 171     5807   5563   6473    383    216   -132       C  
ATOM   1319  C   VAL A 171      10.244   5.938  14.611  1.00 38.48           C  
ANISOU 1319  C   VAL A 171     4588   4633   5400    221    261   -116       C  
ATOM   1320  O   VAL A 171      10.253   5.627  15.807  1.00 38.38           O  
ANISOU 1320  O   VAL A 171     4700   4605   5278    228    276   -189       O  
ATOM   1321  CB  VAL A 171      10.957   8.116  13.563  1.00 49.88           C  
ANISOU 1321  CB  VAL A 171     6277   5732   6943    205      7    -41       C  
ATOM   1322  CG1 VAL A 171      10.472   9.458  13.046  1.00 52.00           C  
ANISOU 1322  CG1 VAL A 171     6726   5828   7202    355    -55    -49       C  
ATOM   1323  CG2 VAL A 171      12.071   8.291  14.587  1.00 49.80           C  
ANISOU 1323  CG2 VAL A 171     6489   5548   6884     23   -170    -38       C  
ATOM   1324  N   HIS A 172      10.655   5.113  13.653  1.00 32.62           N  
ANISOU 1324  N   HIS A 172     3625   4012   4759     91    277    -21       N  
ATOM   1325  CA  HIS A 172      10.903   3.701  13.895  1.00 32.72           C  
ANISOU 1325  CA  HIS A 172     3529   4155   4749    -12    337     -4       C  
ATOM   1326  C   HIS A 172      12.320   3.319  13.503  1.00 33.38           C  
ANISOU 1326  C   HIS A 172     3563   4206   4913   -153    246    102       C  
ATOM   1327  O   HIS A 172      12.915   3.897  12.589  1.00 32.61           O  
ANISOU 1327  O   HIS A 172     3410   4076   4906   -190    180    197       O  
ATOM   1328  CB  HIS A 172       9.898   2.843  13.124  1.00 32.38           C  
ANISOU 1328  CB  HIS A 172     3310   4305   4689      6    462     22       C  
ATOM   1329  CG  HIS A 172       8.475   3.170  13.445  1.00 39.21           C  
ANISOU 1329  CG  HIS A 172     4134   5293   5472    149    563    -17       C  
ATOM   1330  ND1 HIS A 172       7.679   3.930  12.616  1.00 42.17           N  
ANISOU 1330  ND1 HIS A 172     4421   5721   5881    271    591     19       N  
ATOM   1331  CD2 HIS A 172       7.717   2.871  14.526  1.00 41.33           C  
ANISOU 1331  CD2 HIS A 172     4417   5673   5613    215    652    -63       C  
ATOM   1332  CE1 HIS A 172       6.484   4.067  13.163  1.00 44.32           C  
ANISOU 1332  CE1 HIS A 172     4632   6155   6051    426    700     10       C  
ATOM   1333  NE2 HIS A 172       6.481   3.436  14.323  1.00 43.11           N  
ANISOU 1333  NE2 HIS A 172     4535   6050   5794    394    747    -37       N  
ATOM   1334  N   ALA A 173      12.851   2.326  14.209  1.00 32.86           N  
ANISOU 1334  N   ALA A 173     3506   4177   4802   -217    250    107       N  
ATOM   1335  CA  ALA A 173      14.220   1.880  14.019  1.00 27.39           C  
ANISOU 1335  CA  ALA A 173     2747   3499   4161   -298    182    234       C  
ATOM   1336  C   ALA A 173      14.258   0.363  14.093  1.00 25.25           C  
ANISOU 1336  C   ALA A 173     2451   3317   3824   -280    273    236       C  
ATOM   1337  O   ALA A 173      13.493  -0.259  14.832  1.00 25.61           O  
ANISOU 1337  O   ALA A 173     2575   3379   3777   -282    327    142       O  
ATOM   1338  CB  ALA A 173      15.147   2.497  15.071  1.00 26.82           C  
ANISOU 1338  CB  ALA A 173     2778   3326   4085   -404     18    272       C  
ATOM   1339  N   GLY A 174      15.149  -0.227  13.304  1.00 24.75           N  
ANISOU 1339  N   GLY A 174     2299   3315   3789   -248    292    357       N  
ATOM   1340  CA  GLY A 174      15.294  -1.663  13.278  1.00 25.32           C  
ANISOU 1340  CA  GLY A 174     2425   3424   3773   -192    366    365       C  
ATOM   1341  C   GLY A 174      16.598  -2.070  12.632  1.00 28.29           C  
ANISOU 1341  C   GLY A 174     2711   3873   4165    -91    381    530       C  
ATOM   1342  O   GLY A 174      17.494  -1.249  12.425  1.00 29.75           O  
ANISOU 1342  O   GLY A 174     2745   4120   4439   -111    317    668       O  
ATOM   1343  N   THR A 175      16.686  -3.354  12.300  1.00 28.99           N  
ANISOU 1343  N   THR A 175     2909   3961   4144     26    465    535       N  
ATOM   1344  CA  THR A 175      17.938  -3.956  11.876  1.00 32.20           C  
ANISOU 1344  CA  THR A 175     3264   4454   4517    209    514    697       C  
ATOM   1345  C   THR A 175      17.766  -4.625  10.521  1.00 35.73           C  
ANISOU 1345  C   THR A 175     3828   4887   4859    372    634    701       C  
ATOM   1346  O   THR A 175      16.656  -4.756   9.999  1.00 36.14           O  
ANISOU 1346  O   THR A 175     4018   4851   4861    295    648    580       O  
ATOM   1347  CB  THR A 175      18.434  -5.001  12.891  1.00 31.70           C  
ANISOU 1347  CB  THR A 175     3311   4366   4367    274    497    712       C  
ATOM   1348  OG1 THR A 175      17.574  -6.150  12.858  1.00 29.51           O  
ANISOU 1348  OG1 THR A 175     3320   3952   3941    290    541    580       O  
ATOM   1349  CG2 THR A 175      18.455  -4.427  14.301  1.00 33.10           C  
ANISOU 1349  CG2 THR A 175     3439   4528   4610     90    367    682       C  
ATOM   1350  N   ASP A 176      18.889  -5.048   9.951  1.00 36.80           N  
ANISOU 1350  N   ASP A 176     3911   5130   4942    608    718    863       N  
ATOM   1351  CA  ASP A 176      18.852  -6.024   8.876  1.00 36.62           C  
ANISOU 1351  CA  ASP A 176     4125   5048   4740    833    841    854       C  
ATOM   1352  C   ASP A 176      18.583  -7.397   9.493  1.00 32.02           C  
ANISOU 1352  C   ASP A 176     3884   4293   3989    896    833    755       C  
ATOM   1353  O   ASP A 176      18.482  -7.545  10.715  1.00 29.54           O  
ANISOU 1353  O   ASP A 176     3567   3943   3713    769    747    712       O  
ATOM   1354  CB  ASP A 176      20.142  -5.974   8.058  1.00 39.77           C  
ANISOU 1354  CB  ASP A 176     4353   5650   5108   1123    965   1078       C  
ATOM   1355  CG  ASP A 176      21.383  -6.313   8.869  1.00 40.61           C  
ANISOU 1355  CG  ASP A 176     4296   5915   5220   1291    973   1262       C  
ATOM   1356  OD1 ASP A 176      21.265  -6.937   9.944  1.00 38.26           O  
ANISOU 1356  OD1 ASP A 176     4133   5508   4895   1248    902   1187       O  
ATOM   1357  OD2 ASP A 176      22.492  -5.956   8.422  1.00 43.76           O  
ANISOU 1357  OD2 ASP A 176     4406   6576   5643   1462   1046   1512       O  
ATOM   1358  N   LEU A 177      18.441  -8.415   8.653  1.00 33.08           N  
ANISOU 1358  N   LEU A 177     4364   4294   3911   1079    906    718       N  
ATOM   1359  CA  LEU A 177      18.164  -9.751   9.167  1.00 35.52           C  
ANISOU 1359  CA  LEU A 177     5077   4391   4028   1117    868    633       C  
ATOM   1360  C   LEU A 177      19.410 -10.430   9.717  1.00 41.49           C  
ANISOU 1360  C   LEU A 177     5850   5197   4717   1435    927    760       C  
ATOM   1361  O   LEU A 177      19.326 -11.578  10.163  1.00 45.13           O  
ANISOU 1361  O   LEU A 177     6680   5465   5003   1512    893    707       O  
ATOM   1362  CB  LEU A 177      17.520 -10.610   8.080  1.00 33.13           C  
ANISOU 1362  CB  LEU A 177     5235   3870   3482   1167    881    548       C  
ATOM   1363  CG  LEU A 177      15.990 -10.521   8.024  1.00 29.60           C  
ANISOU 1363  CG  LEU A 177     4903   3313   3032    765    746    417       C  
ATOM   1364  CD1 LEU A 177      15.379 -11.304   9.172  1.00 27.89           C  
ANISOU 1364  CD1 LEU A 177     4885   2965   2747    548    621    349       C  
ATOM   1365  CD2 LEU A 177      15.471  -9.075   8.051  1.00 25.81           C  
ANISOU 1365  CD2 LEU A 177     3975   3025   2806    542    727    416       C  
ATOM   1366  N   GLU A 178      20.551  -9.747   9.695  1.00 43.07           N  
ANISOU 1366  N   GLU A 178     5658   5665   5042   1608   1000    953       N  
ATOM   1367  CA  GLU A 178      21.741 -10.178  10.413  1.00 45.49           C  
ANISOU 1367  CA  GLU A 178     5845   6105   5333   1860   1029   1127       C  
ATOM   1368  C   GLU A 178      21.858  -9.522  11.783  1.00 43.34           C  
ANISOU 1368  C   GLU A 178     5279   5928   5259   1573    878   1157       C  
ATOM   1369  O   GLU A 178      22.809  -9.814  12.515  1.00 45.01           O  
ANISOU 1369  O   GLU A 178     5361   6265   5475   1719    862   1317       O  
ATOM   1370  CB  GLU A 178      22.991  -9.884   9.575  1.00 50.87           C  
ANISOU 1370  CB  GLU A 178     6239   7085   6004   2219   1192   1387       C  
ATOM   1371  CG  GLU A 178      23.519 -11.104   8.831  1.00 61.25           C  
ANISOU 1371  CG  GLU A 178     7912   8330   7029   2737   1370   1438       C  
ATOM   1372  CD  GLU A 178      24.453 -10.749   7.691  1.00 68.74           C  
ANISOU 1372  CD  GLU A 178     8638   9571   7909   3004   1543   1648       C  
ATOM   1373  OE1 GLU A 178      24.449  -9.579   7.252  1.00 68.93           O  
ANISOU 1373  OE1 GLU A 178     8303   9782   8106   2775   1519   1723       O  
ATOM   1374  OE2 GLU A 178      25.192 -11.645   7.230  1.00 73.52           O  
ANISOU 1374  OE2 GLU A 178     9477  10205   8251   3343   1663   1724       O  
ATOM   1375  N   GLY A 179      20.918  -8.650  12.142  1.00 42.11           N  
ANISOU 1375  N   GLY A 179     5038   5718   5245   1193    767   1018       N  
ATOM   1376  CA  GLY A 179      20.862  -8.075  13.470  1.00 41.74           C  
ANISOU 1376  CA  GLY A 179     4830   5698   5330    925    621   1002       C  
ATOM   1377  C   GLY A 179      21.618  -6.779  13.661  1.00 41.37           C  
ANISOU 1377  C   GLY A 179     4384   5869   5465    805    545   1172       C  
ATOM   1378  O   GLY A 179      21.761  -6.332  14.805  1.00 43.49           O  
ANISOU 1378  O   GLY A 179     4564   6150   5810    603    404   1185       O  
ATOM   1379  N   ASN A 180      22.104  -6.165  12.590  1.00 40.68           N  
ANISOU 1379  N   ASN A 180     4084   5944   5428    898    617   1314       N  
ATOM   1380  CA  ASN A 180      22.804  -4.891  12.685  1.00 41.62           C  
ANISOU 1380  CA  ASN A 180     3846   6262   5705    724    511   1507       C  
ATOM   1381  C   ASN A 180      21.824  -3.744  12.473  1.00 36.99           C  
ANISOU 1381  C   ASN A 180     3282   5551   5222    446    434   1349       C  
ATOM   1382  O   ASN A 180      21.110  -3.702  11.465  1.00 34.89           O  
ANISOU 1382  O   ASN A 180     3111   5215   4930    494    531   1242       O  
ATOM   1383  CB  ASN A 180      23.935  -4.829  11.661  1.00 46.99           C  
ANISOU 1383  CB  ASN A 180     4251   7233   6369    971    628   1800       C  
ATOM   1384  CG  ASN A 180      24.854  -6.030  11.744  1.00 48.73           C  
ANISOU 1384  CG  ASN A 180     4475   7589   6453   1354    749   1963       C  
ATOM   1385  OD1 ASN A 180      25.507  -6.253  12.763  1.00 48.23           O  
ANISOU 1385  OD1 ASN A 180     4300   7617   6408   1337    651   2093       O  
ATOM   1386  ND2 ASN A 180      24.906  -6.813  10.672  1.00 49.81           N  
ANISOU 1386  ND2 ASN A 180     4771   7727   6429   1722    959   1961       N  
ATOM   1387  N   PHE A 181      21.799  -2.816  13.426  1.00 34.81           N  
ANISOU 1387  N   PHE A 181     2948   5238   5042    171    252   1341       N  
ATOM   1388  CA  PHE A 181      20.865  -1.704  13.366  1.00 33.88           C  
ANISOU 1388  CA  PHE A 181     2900   4976   4996    -44    175   1188       C  
ATOM   1389  C   PHE A 181      21.168  -0.797  12.184  1.00 35.84           C  
ANISOU 1389  C   PHE A 181     2967   5331   5319    -64    185   1329       C  
ATOM   1390  O   PHE A 181      22.325  -0.475  11.899  1.00 36.64           O  
ANISOU 1390  O   PHE A 181     2815   5646   5459    -71    141   1606       O  
ATOM   1391  CB  PHE A 181      20.916  -0.887  14.662  1.00 33.25           C  
ANISOU 1391  CB  PHE A 181     2870   4808   4957   -296    -32   1164       C  
ATOM   1392  CG  PHE A 181      19.768  -1.156  15.590  1.00 32.08           C  
ANISOU 1392  CG  PHE A 181     2983   4466   4741   -342    -25    898       C  
ATOM   1393  CD1 PHE A 181      18.556  -0.509  15.417  1.00 30.50           C  
ANISOU 1393  CD1 PHE A 181     2911   4134   4545   -388      2    708       C  
ATOM   1394  CD2 PHE A 181      19.891  -2.066  16.623  1.00 30.46           C  
ANISOU 1394  CD2 PHE A 181     2877   4240   4455   -322    -37    864       C  
ATOM   1395  CE1 PHE A 181      17.491  -0.762  16.261  1.00 26.64           C  
ANISOU 1395  CE1 PHE A 181     2612   3536   3975   -405     34    507       C  
ATOM   1396  CE2 PHE A 181      18.828  -2.323  17.470  1.00 28.92           C  
ANISOU 1396  CE2 PHE A 181     2900   3908   4180   -372    -19    649       C  
ATOM   1397  CZ  PHE A 181      17.628  -1.669  17.287  1.00 25.85           C  
ANISOU 1397  CZ  PHE A 181     2603   3429   3789   -410     25    479       C  
ATOM   1398  N   TYR A 182      20.115  -0.386  11.491  1.00 36.18           N  
ANISOU 1398  N   TYR A 182     3120   5253   5375    -83    236   1164       N  
ATOM   1399  CA  TYR A 182      20.205   0.783  10.634  1.00 33.74           C  
ANISOU 1399  CA  TYR A 182     2691   4979   5149   -183    184   1263       C  
ATOM   1400  C   TYR A 182      20.309   2.021  11.518  1.00 36.55           C  
ANISOU 1400  C   TYR A 182     3083   5230   5575   -447    -45   1281       C  
ATOM   1401  O   TYR A 182      19.428   2.273  12.348  1.00 39.68           O  
ANISOU 1401  O   TYR A 182     3695   5431   5952   -512    -99   1070       O  
ATOM   1402  CB  TYR A 182      18.990   0.870   9.720  1.00 30.63           C  
ANISOU 1402  CB  TYR A 182     2422   4476   4741   -126    284   1085       C  
ATOM   1403  CG  TYR A 182      18.954  -0.202   8.656  1.00 30.40           C  
ANISOU 1403  CG  TYR A 182     2418   4520   4611     97    470   1092       C  
ATOM   1404  CD1 TYR A 182      19.808  -0.146   7.563  1.00 27.11           C  
ANISOU 1404  CD1 TYR A 182     1838   4283   4180    217    552   1297       C  
ATOM   1405  CD2 TYR A 182      18.063  -1.261   8.740  1.00 31.94           C  
ANISOU 1405  CD2 TYR A 182     2833   4603   4699    179    554    907       C  
ATOM   1406  CE1 TYR A 182      19.778  -1.115   6.589  1.00 29.37           C  
ANISOU 1406  CE1 TYR A 182     2225   4605   4330    455    726   1291       C  
ATOM   1407  CE2 TYR A 182      18.026  -2.238   7.767  1.00 33.60           C  
ANISOU 1407  CE2 TYR A 182     3164   4824   4778    364    688    907       C  
ATOM   1408  CZ  TYR A 182      18.886  -2.158   6.692  1.00 33.20           C  
ANISOU 1408  CZ  TYR A 182     2996   4922   4698    524    781   1085       C  
ATOM   1409  OH  TYR A 182      18.855  -3.126   5.716  1.00 35.60           O  
ANISOU 1409  OH  TYR A 182     3492   5206   4827    744    919   1072       O  
ATOM   1410  N   GLY A 183      21.389   2.777  11.361  1.00 37.74           N  
ANISOU 1410  N   GLY A 183     3044   5513   5781   -602   -186   1550       N  
ATOM   1411  CA  GLY A 183      21.582   3.984  12.127  1.00 40.27           C  
ANISOU 1411  CA  GLY A 183     3467   5698   6136   -893   -451   1595       C  
ATOM   1412  C   GLY A 183      22.339   3.736  13.413  1.00 43.24           C  
ANISOU 1412  C   GLY A 183     3844   6106   6481  -1025   -607   1690       C  
ATOM   1413  O   GLY A 183      22.782   2.619  13.697  1.00 44.45           O  
ANISOU 1413  O   GLY A 183     3876   6413   6601   -871   -500   1743       O  
ATOM   1414  N   PRO A 184      22.499   4.785  14.224  1.00 44.43           N  
ANISOU 1414  N   PRO A 184     4173   6086   6621  -1312   -880   1716       N  
ATOM   1415  CA  PRO A 184      23.284   4.653  15.458  1.00 45.40           C  
ANISOU 1415  CA  PRO A 184     4315   6234   6700  -1494  -1079   1837       C  
ATOM   1416  C   PRO A 184      22.469   4.173  16.647  1.00 47.03           C  
ANISOU 1416  C   PRO A 184     4827   6226   6817  -1413  -1044   1536       C  
ATOM   1417  O   PRO A 184      22.824   4.453  17.795  1.00 53.11           O  
ANISOU 1417  O   PRO A 184     5767   6894   7520  -1615  -1262   1562       O  
ATOM   1418  CB  PRO A 184      23.796   6.081  15.683  1.00 47.17           C  
ANISOU 1418  CB  PRO A 184     4690   6330   6902  -1852  -1412   1995       C  
ATOM   1419  CG  PRO A 184      22.679   6.933  15.164  1.00 45.96           C  
ANISOU 1419  CG  PRO A 184     4798   5901   6763  -1825  -1386   1768       C  
ATOM   1420  CD  PRO A 184      22.079   6.181  13.987  1.00 44.34           C  
ANISOU 1420  CD  PRO A 184     4383   5844   6620  -1496  -1050   1671       C  
ATOM   1421  N   PHE A 185      21.388   3.444  16.400  1.00 42.44           N  
ANISOU 1421  N   PHE A 185     4321   5589   6215  -1145   -787   1275       N  
ATOM   1422  CA  PHE A 185      20.440   3.126  17.456  1.00 39.11           C  
ANISOU 1422  CA  PHE A 185     4184   4982   5695  -1080   -741    999       C  
ATOM   1423  C   PHE A 185      20.804   1.824  18.157  1.00 39.45           C  
ANISOU 1423  C   PHE A 185     4156   5142   5690   -997   -673   1020       C  
ATOM   1424  O   PHE A 185      21.451   0.944  17.587  1.00 42.58           O  
ANISOU 1424  O   PHE A 185     4307   5748   6125   -869   -569   1176       O  
ATOM   1425  CB  PHE A 185      19.023   3.044  16.886  1.00 36.45           C  
ANISOU 1425  CB  PHE A 185     3946   4559   5346   -879   -526    751       C  
ATOM   1426  CG  PHE A 185      18.644   4.236  16.056  1.00 36.00           C  
ANISOU 1426  CG  PHE A 185     3939   4400   5339   -909   -571    743       C  
ATOM   1427  CD1 PHE A 185      18.520   5.488  16.638  1.00 36.18           C  
ANISOU 1427  CD1 PHE A 185     4247   4190   5308  -1045   -769    694       C  
ATOM   1428  CD2 PHE A 185      18.430   4.110  14.693  1.00 34.00           C  
ANISOU 1428  CD2 PHE A 185     3497   4258   5162   -796   -429    787       C  
ATOM   1429  CE1 PHE A 185      18.183   6.591  15.879  1.00 37.37           C  
ANISOU 1429  CE1 PHE A 185     4489   4219   5492  -1060   -825    693       C  
ATOM   1430  CE2 PHE A 185      18.093   5.209  13.925  1.00 37.84           C  
ANISOU 1430  CE2 PHE A 185     4036   4650   5693   -828   -481    792       C  
ATOM   1431  CZ  PHE A 185      17.969   6.452  14.519  1.00 38.99           C  
ANISOU 1431  CZ  PHE A 185     4460   4560   5796   -955   -680    747       C  
ATOM   1432  N   VAL A 186      20.394   1.727  19.420  1.00 38.34           N  
ANISOU 1432  N   VAL A 186     4264   4859   5445  -1049   -732    866       N  
ATOM   1433  CA  VAL A 186      20.560   0.523  20.219  1.00 38.91           C  
ANISOU 1433  CA  VAL A 186     4336   4997   5451   -982   -679    852       C  
ATOM   1434  C   VAL A 186      19.177   0.076  20.676  1.00 36.07           C  
ANISOU 1434  C   VAL A 186     4192   4521   4991   -862   -513    570       C  
ATOM   1435  O   VAL A 186      18.206   0.837  20.631  1.00 35.52           O  
ANISOU 1435  O   VAL A 186     4279   4328   4888   -840   -473    405       O  
ATOM   1436  CB  VAL A 186      21.495   0.744  21.428  1.00 41.57           C  
ANISOU 1436  CB  VAL A 186     4744   5317   5732  -1200   -935    989       C  
ATOM   1437  CG1 VAL A 186      22.935   0.936  20.961  1.00 41.05           C  
ANISOU 1437  CG1 VAL A 186     4365   5471   5763  -1321  -1089   1348       C  
ATOM   1438  CG2 VAL A 186      21.037   1.941  22.255  1.00 43.24           C  
ANISOU 1438  CG2 VAL A 186     5313   5272   5846  -1379  -1112    848       C  
ATOM   1439  N   ASP A 187      19.090  -1.180  21.109  1.00 33.76           N  
ANISOU 1439  N   ASP A 187     3903   4288   4637   -776   -418    542       N  
ATOM   1440  CA  ASP A 187      17.818  -1.732  21.571  1.00 33.45           C  
ANISOU 1440  CA  ASP A 187     4030   4193   4488   -706   -272    330       C  
ATOM   1441  C   ASP A 187      17.755  -1.681  23.097  1.00 34.17           C  
ANISOU 1441  C   ASP A 187     4342   4197   4444   -809   -371    257       C  
ATOM   1442  O   ASP A 187      17.824  -2.688  23.802  1.00 33.10           O  
ANISOU 1442  O   ASP A 187     4258   4091   4229   -810   -355    259       O  
ATOM   1443  CB  ASP A 187      17.613  -3.149  21.031  1.00 33.50           C  
ANISOU 1443  CB  ASP A 187     3970   4282   4477   -580   -120    341       C  
ATOM   1444  CG  ASP A 187      18.835  -4.040  21.196  1.00 34.18           C  
ANISOU 1444  CG  ASP A 187     3976   4440   4569   -535   -180    517       C  
ATOM   1445  OD1 ASP A 187      19.892  -3.555  21.650  1.00 35.86           O  
ANISOU 1445  OD1 ASP A 187     4108   4695   4824   -622   -342    669       O  
ATOM   1446  OD2 ASP A 187      18.730  -5.238  20.858  1.00 32.43           O  
ANISOU 1446  OD2 ASP A 187     3790   4236   4295   -411    -77    521       O  
ATOM   1447  N   ARG A 188      17.634  -0.452  23.597  1.00 38.27           N  
ANISOU 1447  N   ARG A 188     5039   4585   4917   -893   -488    194       N  
ATOM   1448  CA  ARG A 188      17.247  -0.204  24.978  1.00 44.54           C  
ANISOU 1448  CA  ARG A 188     6126   5264   5533   -946   -544     70       C  
ATOM   1449  C   ARG A 188      16.351   1.027  25.018  1.00 43.17           C  
ANISOU 1449  C   ARG A 188     6173   4951   5279   -868   -512    -88       C  
ATOM   1450  O   ARG A 188      16.442   1.909  24.158  1.00 41.54           O  
ANISOU 1450  O   ARG A 188     5929   4687   5167   -861   -557    -57       O  
ATOM   1451  CB  ARG A 188      18.463  -0.028  25.897  1.00 52.37           C  
ANISOU 1451  CB  ARG A 188     7218   6194   6485  -1150   -810    204       C  
ATOM   1452  CG  ARG A 188      19.500   0.964  25.417  1.00 59.26           C  
ANISOU 1452  CG  ARG A 188     8030   7026   7460  -1319  -1043    384       C  
ATOM   1453  CD  ARG A 188      20.701   0.984  26.361  1.00 65.69           C  
ANISOU 1453  CD  ARG A 188     8900   7834   8225  -1564  -1331    569       C  
ATOM   1454  NE  ARG A 188      20.367   1.547  27.669  1.00 70.52           N  
ANISOU 1454  NE  ARG A 188     9950   8225   8621  -1669  -1464    421       N  
ATOM   1455  CZ  ARG A 188      20.824   2.707  28.138  1.00 75.46           C  
ANISOU 1455  CZ  ARG A 188    10872   8647   9151  -1898  -1753    464       C  
ATOM   1456  NH1 ARG A 188      21.659   3.450  27.423  1.00 76.34           N  
ANISOU 1456  NH1 ARG A 188    10853   8772   9382  -2092  -1960    677       N  
ATOM   1457  NH2 ARG A 188      20.451   3.123  29.341  1.00 78.73           N  
ANISOU 1457  NH2 ARG A 188    11749   8840   9326  -1946  -1849    304       N  
ATOM   1458  N   GLN A 189      15.482   1.070  26.029  1.00 42.82           N  
ANISOU 1458  N   GLN A 189     6370   4860   5038   -784   -425   -245       N  
ATOM   1459  CA  GLN A 189      14.523   2.162  26.200  1.00 45.94           C  
ANISOU 1459  CA  GLN A 189     7013   5138   5304   -619   -350   -400       C  
ATOM   1460  C   GLN A 189      15.252   3.359  26.806  1.00 46.59           C  
ANISOU 1460  C   GLN A 189     7471   4943   5289   -744   -621   -406       C  
ATOM   1461  O   GLN A 189      15.231   3.602  28.014  1.00 50.40           O  
ANISOU 1461  O   GLN A 189     8306   5289   5553   -763   -699   -492       O  
ATOM   1462  CB  GLN A 189      13.358   1.714  27.077  1.00 43.73           C  
ANISOU 1462  CB  GLN A 189     6832   4963   4819   -452   -135   -530       C  
ATOM   1463  CG  GLN A 189      12.164   2.662  27.074  1.00 44.90           C  
ANISOU 1463  CG  GLN A 189     7142   5088   4829   -172     30   -662       C  
ATOM   1464  CD  GLN A 189      11.116   2.305  28.119  1.00 43.29           C  
ANISOU 1464  CD  GLN A 189     7043   5029   4377      4    242   -751       C  
ATOM   1465  OE1 GLN A 189      10.580   3.181  28.794  1.00 43.67           O  
ANISOU 1465  OE1 GLN A 189     7419   4972   4200    223    300   -867       O  
ATOM   1466  NE2 GLN A 189      10.814   1.017  28.248  1.00 41.00           N  
ANISOU 1466  NE2 GLN A 189     6498   4980   4101    -81    358   -684       N  
ATOM   1467  N   THR A 190      15.915   4.123  25.939  1.00 47.41           N  
ANISOU 1467  N   THR A 190     7525   4953   5535   -856   -786   -301       N  
ATOM   1468  CA  THR A 190      16.585   5.350  26.351  1.00 51.19           C  
ANISOU 1468  CA  THR A 190     8389   5143   5917  -1031  -1090   -275       C  
ATOM   1469  C   THR A 190      16.425   6.385  25.248  1.00 50.93           C  
ANISOU 1469  C   THR A 190     8368   5002   5981   -983  -1123   -259       C  
ATOM   1470  O   THR A 190      16.260   6.041  24.074  1.00 43.08           O  
ANISOU 1470  O   THR A 190     6990   4195   5184   -909   -976   -192       O  
ATOM   1471  CB  THR A 190      18.075   5.137  26.653  1.00 53.78           C  
ANISOU 1471  CB  THR A 190     8637   5484   6312  -1390  -1396    -45       C  
ATOM   1472  OG1 THR A 190      18.652   6.371  27.101  1.00 58.78           O  
ANISOU 1472  OG1 THR A 190     9699   5818   6817  -1619  -1735     -5       O  
ATOM   1473  CG2 THR A 190      18.818   4.656  25.417  1.00 51.78           C  
ANISOU 1473  CG2 THR A 190     7877   5470   6328  -1473  -1387    182       C  
ATOM   1474  N   ALA A 191      16.466   7.658  25.632  1.00 60.60           N  
ANISOU 1474  N   ALA A 191    10083   5899   7043  -1025  -1330   -320       N  
ATOM   1475  CA  ALA A 191      16.282   8.735  24.668  1.00 66.06           C  
ANISOU 1475  CA  ALA A 191    10870   6436   7793   -977  -1388   -309       C  
ATOM   1476  C   ALA A 191      17.386   8.690  23.620  1.00 65.94           C  
ANISOU 1476  C   ALA A 191    10475   6553   8028  -1277  -1559    -39       C  
ATOM   1477  O   ALA A 191      18.568   8.847  23.942  1.00 69.22           O  
ANISOU 1477  O   ALA A 191    10925   6925   8449  -1635  -1866    157       O  
ATOM   1478  CB  ALA A 191      16.268  10.087  25.378  1.00 71.54           C  
ANISOU 1478  CB  ALA A 191    12263   6693   8225  -1003  -1638   -410       C  
ATOM   1479  N   GLN A 192      16.996   8.469  22.367  1.00 61.12           N  
ANISOU 1479  N   GLN A 192     9487   6129   7605  -1132  -1358     -6       N  
ATOM   1480  CA  GLN A 192      17.934   8.335  21.262  1.00 55.95           C  
ANISOU 1480  CA  GLN A 192     8431   5655   7171  -1341  -1446    249       C  
ATOM   1481  C   GLN A 192      17.572   9.332  20.174  1.00 52.24           C  
ANISOU 1481  C   GLN A 192     8015   5069   6763  -1282  -1461    258       C  
ATOM   1482  O   GLN A 192      16.403   9.446  19.791  1.00 48.83           O  
ANISOU 1482  O   GLN A 192     7616   4623   6314   -969  -1232     82       O  
ATOM   1483  CB  GLN A 192      17.927   6.913  20.698  1.00 54.52           C  
ANISOU 1483  CB  GLN A 192     7737   5832   7145  -1225  -1186    303       C  
ATOM   1484  CG  GLN A 192      18.619   5.898  21.584  1.00 59.13           C  
ANISOU 1484  CG  GLN A 192     8213   6551   7703  -1335  -1224    379       C  
ATOM   1485  CD  GLN A 192      18.536   4.494  21.024  1.00 62.47           C  
ANISOU 1485  CD  GLN A 192     8233   7264   8239  -1181   -972    412       C  
ATOM   1486  OE1 GLN A 192      19.250   4.143  20.087  1.00 61.60           O  
ANISOU 1486  OE1 GLN A 192     7794   7342   8270  -1216   -957    606       O  
ATOM   1487  NE2 GLN A 192      17.653   3.684  21.593  1.00 65.63           N  
ANISOU 1487  NE2 GLN A 192     8685   7699   8553  -1007   -774    233       N  
ATOM   1488  N   ALA A 193      18.579  10.042  19.679  1.00 55.02           N  
ANISOU 1488  N   ALA A 193     8357   5366   7182  -1596  -1739    492       N  
ATOM   1489  CA  ALA A 193      18.393  11.081  18.680  1.00 59.56           C  
ANISOU 1489  CA  ALA A 193     9025   5801   7803  -1605  -1814    538       C  
ATOM   1490  C   ALA A 193      18.704  10.528  17.296  1.00 58.21           C  
ANISOU 1490  C   ALA A 193     8300   5964   7855  -1601  -1660    719       C  
ATOM   1491  O   ALA A 193      19.740   9.883  17.097  1.00 53.97           O  
ANISOU 1491  O   ALA A 193     7394   5693   7418  -1790  -1703    957       O  
ATOM   1492  CB  ALA A 193      19.289  12.285  18.978  1.00 64.37           C  
ANISOU 1492  CB  ALA A 193    10022   6122   8315  -2001  -2253    710       C  
ATOM   1493  N   ALA A 194      17.802  10.772  16.352  1.00 59.40           N  
ANISOU 1493  N   ALA A 194     8400   6109   8061  -1361  -1476    617       N  
ATOM   1494  CA  ALA A 194      18.064  10.514  14.947  1.00 56.15           C  
ANISOU 1494  CA  ALA A 194     7571   5944   7821  -1370  -1370    785       C  
ATOM   1495  C   ALA A 194      18.580  11.789  14.291  1.00 57.33           C  
ANISOU 1495  C   ALA A 194     7869   5929   7986  -1614  -1636    968       C  
ATOM   1496  O   ALA A 194      18.209  12.903  14.672  1.00 61.13           O  
ANISOU 1496  O   ALA A 194     8830   6052   8345  -1635  -1819    872       O  
ATOM   1497  CB  ALA A 194      16.802  10.028  14.234  1.00 53.16           C  
ANISOU 1497  CB  ALA A 194     7046   5667   7485  -1016  -1049    602       C  
ATOM   1498  N   GLY A 195      19.453  11.616  13.310  1.00 53.47           N  
ANISOU 1498  N   GLY A 195     6992   5699   7624  -1788  -1657   1246       N  
ATOM   1499  CA  GLY A 195      20.029  12.754  12.625  1.00 53.15           C  
ANISOU 1499  CA  GLY A 195     7036   5559   7601  -2071  -1916   1475       C  
ATOM   1500  C   GLY A 195      18.981  13.575  11.896  1.00 51.19           C  
ANISOU 1500  C   GLY A 195     7028   5080   7343  -1873  -1861   1318       C  
ATOM   1501  O   GLY A 195      17.804  13.228  11.803  1.00 47.91           O  
ANISOU 1501  O   GLY A 195     6640   4643   6922  -1506  -1603   1060       O  
ATOM   1502  N   THR A 196      19.436  14.707  11.370  1.00 52.38           N  
ANISOU 1502  N   THR A 196     7352   5069   7482  -2143  -2132   1510       N  
ATOM   1503  CA  THR A 196      18.573  15.533  10.542  1.00 50.83           C  
ANISOU 1503  CA  THR A 196     7362   4667   7283  -1973  -2107   1414       C  
ATOM   1504  C   THR A 196      18.082  14.718   9.351  1.00 50.08           C  
ANISOU 1504  C   THR A 196     6799   4904   7327  -1713  -1763   1397       C  
ATOM   1505  O   THR A 196      18.873  14.088   8.642  1.00 48.44           O  
ANISOU 1505  O   THR A 196     6146   5043   7215  -1835  -1684   1622       O  
ATOM   1506  CB  THR A 196      19.325  16.781  10.080  1.00 50.67           C  
ANISOU 1506  CB  THR A 196     7519   4553   7179  -2279  -2424   1634       C  
ATOM   1507  OG1 THR A 196      19.810  17.496  11.226  1.00 54.37           O  
ANISOU 1507  OG1 THR A 196     8410   4815   7432  -2449  -2714   1609       O  
ATOM   1508  CG2 THR A 196      18.417  17.699   9.286  1.00 51.15           C  
ANISOU 1508  CG2 THR A 196     7863   4333   7237  -2122  -2436   1544       C  
ATOM   1509  N   ASP A 197      16.767  14.699   9.158  1.00 51.41           N  
ANISOU 1509  N   ASP A 197     7075   4979   7480  -1341  -1558   1143       N  
ATOM   1510  CA  ASP A 197      16.159  13.990   8.041  1.00 50.56           C  
ANISOU 1510  CA  ASP A 197     6599   5138   7472  -1117  -1272   1117       C  
ATOM   1511  C   ASP A 197      16.160  14.908   6.824  1.00 53.27           C  
ANISOU 1511  C   ASP A 197     6969   5414   7857  -1199  -1374   1265       C  
ATOM   1512  O   ASP A 197      15.589  16.003   6.868  1.00 59.33           O  
ANISOU 1512  O   ASP A 197     8125   5859   8559  -1131  -1517   1191       O  
ATOM   1513  CB  ASP A 197      14.738  13.549   8.385  1.00 49.82           C  
ANISOU 1513  CB  ASP A 197     6565   5028   7338   -725  -1032    833       C  
ATOM   1514  CG  ASP A 197      14.215  12.488   7.439  1.00 52.09           C  
ANISOU 1514  CG  ASP A 197     6456   5629   7706   -564   -758    820       C  
ATOM   1515  OD1 ASP A 197      15.007  11.994   6.611  1.00 53.02           O  
ANISOU 1515  OD1 ASP A 197     6285   5966   7895   -710   -725    998       O  
ATOM   1516  OD2 ASP A 197      13.017  12.146   7.521  1.00 52.57           O  
ANISOU 1516  OD2 ASP A 197     6506   5729   7738   -293   -581    651       O  
ATOM   1517  N   THR A 198      16.815  14.473   5.752  1.00 49.71           N  
ANISOU 1517  N   THR A 198     6135   5260   7494  -1323  -1301   1479       N  
ATOM   1518  CA  THR A 198      16.859  15.222   4.505  1.00 47.98           C  
ANISOU 1518  CA  THR A 198     5889   5031   7310  -1412  -1373   1643       C  
ATOM   1519  C   THR A 198      15.949  14.559   3.476  1.00 41.91           C  
ANISOU 1519  C   THR A 198     4888   4448   6586  -1127  -1093   1542       C  
ATOM   1520  O   THR A 198      15.487  13.428   3.651  1.00 39.59           O  
ANISOU 1520  O   THR A 198     4415   4329   6298   -924   -859   1396       O  
ATOM   1521  CB  THR A 198      18.295  15.327   3.972  1.00 50.37           C  
ANISOU 1521  CB  THR A 198     5936   5560   7644  -1776  -1507   2008       C  
ATOM   1522  OG1 THR A 198      18.841  14.019   3.763  1.00 51.21           O  
ANISOU 1522  OG1 THR A 198     5608   6062   7786  -1702  -1266   2083       O  
ATOM   1523  CG2 THR A 198      19.174  16.088   4.956  1.00 51.23           C  
ANISOU 1523  CG2 THR A 198     6295   5506   7665  -2088  -1834   2121       C  
ATOM   1524  N   THR A 199      15.680  15.290   2.397  1.00 41.06           N  
ANISOU 1524  N   THR A 199     4818   4285   6497  -1142  -1147   1634       N  
ATOM   1525  CA  THR A 199      14.807  14.806   1.338  1.00 41.04           C  
ANISOU 1525  CA  THR A 199     4636   4436   6522   -917   -934   1568       C  
ATOM   1526  C   THR A 199      15.611  14.059   0.281  1.00 40.51           C  
ANISOU 1526  C   THR A 199     4212   4706   6473  -1018   -803   1768       C  
ATOM   1527  O   THR A 199      16.691  14.497  -0.124  1.00 42.13           O  
ANISOU 1527  O   THR A 199     4328   4998   6682  -1272   -924   2031       O  
ATOM   1528  CB  THR A 199      14.047  15.965   0.692  1.00 42.73           C  
ANISOU 1528  CB  THR A 199     5086   4418   6730   -847  -1055   1567       C  
ATOM   1529  OG1 THR A 199      13.253  16.629   1.683  1.00 40.98           O  
ANISOU 1529  OG1 THR A 199     5228   3887   6454   -663  -1141   1375       O  
ATOM   1530  CG2 THR A 199      13.148  15.455  -0.422  1.00 43.30           C  
ANISOU 1530  CG2 THR A 199     4957   4671   6823   -648   -861   1527       C  
ATOM   1531  N   ILE A 200      15.062  12.933  -0.175  1.00 36.23           N  
ANISOU 1531  N   ILE A 200     3488   4360   5918   -815   -559   1659       N  
ATOM   1532  CA  ILE A 200      15.747  12.055  -1.118  1.00 34.76           C  
ANISOU 1532  CA  ILE A 200     3033   4475   5699   -825   -395   1806       C  
ATOM   1533  C   ILE A 200      15.612  12.619  -2.527  1.00 33.04           C  
ANISOU 1533  C   ILE A 200     2789   4296   5469   -862   -410   1945       C  
ATOM   1534  O   ILE A 200      14.696  12.253  -3.275  1.00 31.35           O  
ANISOU 1534  O   ILE A 200     2580   4106   5225   -710   -301   1844       O  
ATOM   1535  CB  ILE A 200      15.192  10.622  -1.035  1.00 36.32           C  
ANISOU 1535  CB  ILE A 200     3152   4802   5845   -613   -166   1628       C  
ATOM   1536  CG1 ILE A 200      15.191  10.133   0.415  1.00 37.34           C  
ANISOU 1536  CG1 ILE A 200     3335   4868   5983   -578   -165   1481       C  
ATOM   1537  CG2 ILE A 200      16.037   9.688  -1.885  1.00 38.98           C  
ANISOU 1537  CG2 ILE A 200     3297   5410   6103   -576      4   1774       C  
ATOM   1538  CD1 ILE A 200      14.282   8.946   0.664  1.00 36.83           C  
ANISOU 1538  CD1 ILE A 200     3276   4850   5868   -398      1   1276       C  
ATOM   1539  N   THR A 201      16.555  13.488  -2.904  1.00 35.40           N  
ANISOU 1539  N   THR A 201     3052   4620   5779  -1097   -561   2206       N  
ATOM   1540  CA  THR A 201      16.438  14.253  -4.140  1.00 35.80           C  
ANISOU 1540  CA  THR A 201     3120   4665   5817  -1173   -624   2357       C  
ATOM   1541  C   THR A 201      16.254  13.354  -5.354  1.00 33.93           C  
ANISOU 1541  C   THR A 201     2721   4669   5500  -1017   -389   2370       C  
ATOM   1542  O   THR A 201      15.433  13.648  -6.232  1.00 32.67           O  
ANISOU 1542  O   THR A 201     2645   4444   5326   -953   -392   2331       O  
ATOM   1543  CB  THR A 201      17.680  15.127  -4.324  1.00 41.78           C  
ANISOU 1543  CB  THR A 201     3849   5496   6530  -1434   -813   2622       C  
ATOM   1544  OG1 THR A 201      17.936  15.854  -3.116  1.00 47.04           O  
ANISOU 1544  OG1 THR A 201     4711   5928   7234  -1612  -1054   2612       O  
ATOM   1545  CG2 THR A 201      17.492  16.100  -5.488  1.00 41.83           C  
ANISOU 1545  CG2 THR A 201     3934   5444   6515  -1531   -926   2755       C  
ATOM   1546  N   VAL A 202      17.027  12.271  -5.442  1.00 35.72           N  
ANISOU 1546  N   VAL A 202     2792   5156   5624   -905   -204   2390       N  
ATOM   1547  CA  VAL A 202      16.953  11.412  -6.620  1.00 38.88           C  
ANISOU 1547  CA  VAL A 202     3138   5744   5891   -735      4   2393       C  
ATOM   1548  C   VAL A 202      15.557  10.821  -6.760  1.00 39.31           C  
ANISOU 1548  C   VAL A 202     3297   5682   5956   -606     85   2179       C  
ATOM   1549  O   VAL A 202      15.046  10.657  -7.875  1.00 39.05           O  
ANISOU 1549  O   VAL A 202     3318   5683   5836   -549    143   2181       O  
ATOM   1550  CB  VAL A 202      18.033  10.315  -6.554  1.00 41.18           C  
ANISOU 1550  CB  VAL A 202     3331   6274   6042   -573    174   2422       C  
ATOM   1551  CG1 VAL A 202      17.720   9.313  -5.454  1.00 40.40           C  
ANISOU 1551  CG1 VAL A 202     3273   6114   5965   -456    258   2222       C  
ATOM   1552  CG2 VAL A 202      18.153   9.614  -7.901  1.00 44.41           C  
ANISOU 1552  CG2 VAL A 202     3727   6865   6282   -406    370   2482       C  
ATOM   1553  N   ASN A 203      14.910  10.502  -5.634  1.00 36.99           N  
ANISOU 1553  N   ASN A 203     3083   5245   5725   -543     60   1962       N  
ATOM   1554  CA  ASN A 203      13.563   9.943  -5.685  1.00 34.55           C  
ANISOU 1554  CA  ASN A 203     2883   4854   5389   -419     99   1748       C  
ATOM   1555  C   ASN A 203      12.544  10.984  -6.134  1.00 32.49           C  
ANISOU 1555  C   ASN A 203     2706   4448   5190   -440    -44   1738       C  
ATOM   1556  O   ASN A 203      11.622  10.669  -6.895  1.00 29.47           O  
ANISOU 1556  O   ASN A 203     2358   4092   4749   -383    -18   1692       O  
ATOM   1557  CB  ASN A 203      13.177   9.374  -4.320  1.00 34.25           C  
ANISOU 1557  CB  ASN A 203     2877   4745   5391   -354    115   1559       C  
ATOM   1558  CG  ASN A 203      13.899   8.081  -4.001  1.00 33.42           C  
ANISOU 1558  CG  ASN A 203     2729   4773   5195   -285    270   1538       C  
ATOM   1559  OD1 ASN A 203      14.812   7.672  -4.719  1.00 30.72           O  
ANISOU 1559  OD1 ASN A 203     2325   4589   4760   -253    377   1679       O  
ATOM   1560  ND2 ASN A 203      13.496   7.429  -2.916  1.00 34.92           N  
ANISOU 1560  ND2 ASN A 203     2962   4911   5396   -235    293   1375       N  
ATOM   1561  N   VAL A 204      12.684  12.229  -5.668  1.00 34.82           N  
ANISOU 1561  N   VAL A 204     3064   4581   5586   -520   -212   1791       N  
ATOM   1562  CA  VAL A 204      11.788  13.292  -6.113  1.00 34.63           C  
ANISOU 1562  CA  VAL A 204     3154   4399   5605   -495   -351   1800       C  
ATOM   1563  C   VAL A 204      11.832  13.417  -7.631  1.00 33.34           C  
ANISOU 1563  C   VAL A 204     2953   4339   5377   -553   -340   1954       C  
ATOM   1564  O   VAL A 204      10.793  13.488  -8.298  1.00 33.68           O  
ANISOU 1564  O   VAL A 204     3026   4370   5400   -475   -359   1921       O  
ATOM   1565  CB  VAL A 204      12.149  14.627  -5.433  1.00 35.32           C  
ANISOU 1565  CB  VAL A 204     3406   4247   5768   -585   -556   1854       C  
ATOM   1566  CG1 VAL A 204      11.255  15.754  -5.969  1.00 36.46           C  
ANISOU 1566  CG1 VAL A 204     3714   4204   5934   -514   -701   1876       C  
ATOM   1567  CG2 VAL A 204      12.041  14.509  -3.917  1.00 31.11           C  
ANISOU 1567  CG2 VAL A 204     2961   3593   5265   -511   -569   1688       C  
ATOM   1568  N   LEU A 205      13.041  13.444  -8.201  1.00 32.21           N  
ANISOU 1568  N   LEU A 205     2725   4327   5186   -691   -309   2148       N  
ATOM   1569  CA  LEU A 205      13.176  13.554  -9.651  1.00 35.91           C  
ANISOU 1569  CA  LEU A 205     3167   4914   5562   -741   -279   2309       C  
ATOM   1570  C   LEU A 205      12.463  12.410 -10.363  1.00 36.98           C  
ANISOU 1570  C   LEU A 205     3315   5162   5572   -608   -129   2199       C  
ATOM   1571  O   LEU A 205      11.761  12.629 -11.358  1.00 36.46           O  
ANISOU 1571  O   LEU A 205     3311   5087   5455   -608   -174   2231       O  
ATOM   1572  CB  LEU A 205      14.655  13.584 -10.040  1.00 37.19           C  
ANISOU 1572  CB  LEU A 205     3187   5279   5663   -875   -219   2558       C  
ATOM   1573  CG  LEU A 205      15.474  14.758  -9.505  1.00 43.11           C  
ANISOU 1573  CG  LEU A 205     3930   5943   6507  -1105   -420   2745       C  
ATOM   1574  CD1 LEU A 205      16.951  14.573  -9.806  1.00 47.93           C  
ANISOU 1574  CD1 LEU A 205     4377   6840   6995  -1143   -363   2900       C  
ATOM   1575  CD2 LEU A 205      14.978  16.061 -10.092  1.00 47.25           C  
ANISOU 1575  CD2 LEU A 205     4620   6260   7071  -1222   -637   2833       C  
ATOM   1576  N   ALA A 206      12.636  11.178  -9.878  1.00 35.32           N  
ANISOU 1576  N   ALA A 206     3082   5045   5294   -513     25   2080       N  
ATOM   1577  CA  ALA A 206      11.942  10.049 -10.488  1.00 35.33           C  
ANISOU 1577  CA  ALA A 206     3176   5104   5143   -426    124   1974       C  
ATOM   1578  C   ALA A 206      10.434  10.247 -10.435  1.00 35.09           C  
ANISOU 1578  C   ALA A 206     3195   4970   5169   -421     -1   1865       C  
ATOM   1579  O   ALA A 206       9.721   9.931 -11.395  1.00 34.47           O  
ANISOU 1579  O   ALA A 206     3193   4924   4979   -440    -23   1879       O  
ATOM   1580  CB  ALA A 206      12.340   8.752  -9.788  1.00 32.46           C  
ANISOU 1580  CB  ALA A 206     2833   4801   4700   -329    274   1857       C  
ATOM   1581  N   TRP A 207       9.933  10.777  -9.317  1.00 35.83           N  
ANISOU 1581  N   TRP A 207     3243   4955   5414   -386    -84   1776       N  
ATOM   1582  CA  TRP A 207       8.505  11.041  -9.172  1.00 36.88           C  
ANISOU 1582  CA  TRP A 207     3368   5048   5598   -327   -180   1713       C  
ATOM   1583  C   TRP A 207       8.043  12.108 -10.151  1.00 36.40           C  
ANISOU 1583  C   TRP A 207     3329   4940   5562   -343   -310   1844       C  
ATOM   1584  O   TRP A 207       6.964  11.988 -10.745  1.00 38.38           O  
ANISOU 1584  O   TRP A 207     3561   5252   5771   -329   -367   1866       O  
ATOM   1585  CB  TRP A 207       8.226  11.455  -7.727  1.00 36.49           C  
ANISOU 1585  CB  TRP A 207     3291   4901   5673   -228   -208   1603       C  
ATOM   1586  CG  TRP A 207       6.814  11.832  -7.403  1.00 33.69           C  
ANISOU 1586  CG  TRP A 207     2891   4546   5364    -96   -274   1565       C  
ATOM   1587  CD1 TRP A 207       5.740  10.999  -7.311  1.00 30.64           C  
ANISOU 1587  CD1 TRP A 207     2408   4312   4923    -73   -244   1527       C  
ATOM   1588  CD2 TRP A 207       6.335  13.142  -7.082  1.00 34.48           C  
ANISOU 1588  CD2 TRP A 207     3041   4504   5555     49   -380   1588       C  
ATOM   1589  NE1 TRP A 207       4.618  11.710  -6.965  1.00 32.86           N  
ANISOU 1589  NE1 TRP A 207     2609   4613   5262     95   -303   1549       N  
ATOM   1590  CE2 TRP A 207       4.957  13.030  -6.818  1.00 35.01           C  
ANISOU 1590  CE2 TRP A 207     2995   4688   5618    207   -377   1570       C  
ATOM   1591  CE3 TRP A 207       6.937  14.400  -6.996  1.00 35.69           C  
ANISOU 1591  CE3 TRP A 207     3350   4440   5772     57   -492   1640       C  
ATOM   1592  CZ2 TRP A 207       4.172  14.126  -6.478  1.00 37.21           C  
ANISOU 1592  CZ2 TRP A 207     3306   4883   5948    448   -444   1593       C  
ATOM   1593  CZ3 TRP A 207       6.155  15.488  -6.661  1.00 39.02           C  
ANISOU 1593  CZ3 TRP A 207     3876   4715   6236    266   -588   1639       C  
ATOM   1594  CH2 TRP A 207       4.788  15.344  -6.406  1.00 38.50           C  
ANISOU 1594  CH2 TRP A 207     3690   4779   6160    494   -546   1609       C  
ATOM   1595  N   LEU A 208       8.848  13.155 -10.340  1.00 35.32           N  
ANISOU 1595  N   LEU A 208     3234   4703   5484   -397   -379   1957       N  
ATOM   1596  CA  LEU A 208       8.501  14.184 -11.314  1.00 38.51           C  
ANISOU 1596  CA  LEU A 208     3692   5041   5899   -426   -514   2096       C  
ATOM   1597  C   LEU A 208       8.417  13.597 -12.716  1.00 39.33           C  
ANISOU 1597  C   LEU A 208     3802   5291   5852   -506   -472   2185       C  
ATOM   1598  O   LEU A 208       7.580  14.017 -13.524  1.00 43.13           O  
ANISOU 1598  O   LEU A 208     4305   5768   6315   -502   -577   2258       O  
ATOM   1599  CB  LEU A 208       9.523  15.317 -11.261  1.00 39.55           C  
ANISOU 1599  CB  LEU A 208     3898   5038   6092   -534   -615   2228       C  
ATOM   1600  CG  LEU A 208       9.497  16.180 -10.000  1.00 39.24           C  
ANISOU 1600  CG  LEU A 208     3968   4772   6169   -470   -728   2157       C  
ATOM   1601  CD1 LEU A 208      10.544  17.281 -10.089  1.00 40.59           C  
ANISOU 1601  CD1 LEU A 208     4261   4796   6365   -663   -882   2330       C  
ATOM   1602  CD2 LEU A 208       8.123  16.781  -9.772  1.00 39.93           C  
ANISOU 1602  CD2 LEU A 208     4133   4735   6304   -250   -817   2082       C  
ATOM   1603  N   TYR A 209       9.277  12.621 -13.024  1.00 36.49           N  
ANISOU 1603  N   TYR A 209     3446   5057   5361   -556   -318   2187       N  
ATOM   1604  CA  TYR A 209       9.199  11.942 -14.313  1.00 38.53           C  
ANISOU 1604  CA  TYR A 209     3791   5428   5421   -600   -264   2245       C  
ATOM   1605  C   TYR A 209       7.906  11.147 -14.434  1.00 36.88           C  
ANISOU 1605  C   TYR A 209     3628   5244   5142   -592   -312   2146       C  
ATOM   1606  O   TYR A 209       7.252  11.167 -15.482  1.00 36.61           O  
ANISOU 1606  O   TYR A 209     3666   5241   5005   -658   -400   2223       O  
ATOM   1607  CB  TYR A 209      10.406  11.023 -14.502  1.00 39.73           C  
ANISOU 1607  CB  TYR A 209     3979   5703   5415   -577    -63   2260       C  
ATOM   1608  CG  TYR A 209      11.628  11.721 -15.051  1.00 40.47           C  
ANISOU 1608  CG  TYR A 209     4009   5881   5485   -630    -16   2468       C  
ATOM   1609  CD1 TYR A 209      11.717  12.043 -16.398  1.00 41.64           C  
ANISOU 1609  CD1 TYR A 209     4227   6097   5496   -687    -25   2625       C  
ATOM   1610  CD2 TYR A 209      12.694  12.051 -14.227  1.00 40.70           C  
ANISOU 1610  CD2 TYR A 209     3899   5951   5616   -652     24   2538       C  
ATOM   1611  CE1 TYR A 209      12.830  12.679 -16.909  1.00 42.54           C  
ANISOU 1611  CE1 TYR A 209     4254   6336   5575   -757     21   2855       C  
ATOM   1612  CE2 TYR A 209      13.814  12.688 -14.730  1.00 44.98           C  
ANISOU 1612  CE2 TYR A 209     4340   6623   6127   -748     48   2785       C  
ATOM   1613  CZ  TYR A 209      13.876  12.997 -16.072  1.00 43.34           C  
ANISOU 1613  CZ  TYR A 209     4185   6502   5782   -797     55   2947       C  
ATOM   1614  OH  TYR A 209      14.983  13.629 -16.580  1.00 44.42           O  
ANISOU 1614  OH  TYR A 209     4208   6794   5875   -879     63   3150       O  
ATOM   1615  N   ALA A 210       7.528  10.431 -13.373  1.00 37.80           N  
ANISOU 1615  N   ALA A 210     3702   5363   5297   -544   -273   2000       N  
ATOM   1616  CA  ALA A 210       6.244   9.745 -13.376  1.00 39.66           C  
ANISOU 1616  CA  ALA A 210     3939   5655   5474   -585   -351   1953       C  
ATOM   1617  C   ALA A 210       5.120  10.722 -13.681  1.00 39.18           C  
ANISOU 1617  C   ALA A 210     3762   5609   5514   -570   -519   2057       C  
ATOM   1618  O   ALA A 210       4.206  10.409 -14.452  1.00 40.07           O  
ANISOU 1618  O   ALA A 210     3891   5809   5525   -667   -628   2134       O  
ATOM   1619  CB  ALA A 210       6.015   9.055 -12.032  1.00 41.03           C  
ANISOU 1619  CB  ALA A 210     4043   5841   5705   -538   -293   1810       C  
ATOM   1620  N   ALA A 211       5.184  11.926 -13.106  1.00 38.35           N  
ANISOU 1620  N   ALA A 211     3568   5412   5591   -445   -557   2076       N  
ATOM   1621  CA  ALA A 211       4.135  12.912 -13.333  1.00 37.46           C  
ANISOU 1621  CA  ALA A 211     3369   5299   5564   -354   -703   2179       C  
ATOM   1622  C   ALA A 211       4.053  13.291 -14.806  1.00 38.12           C  
ANISOU 1622  C   ALA A 211     3531   5395   5559   -460   -808   2336       C  
ATOM   1623  O   ALA A 211       2.963  13.340 -15.387  1.00 39.11           O  
ANISOU 1623  O   ALA A 211     3586   5624   5650   -474   -930   2440       O  
ATOM   1624  CB  ALA A 211       4.378  14.150 -12.470  1.00 35.55           C  
ANISOU 1624  CB  ALA A 211     3137   4884   5488   -178   -730   2156       C  
ATOM   1625  N   VAL A 212       5.201  13.562 -15.430  1.00 39.75           N  
ANISOU 1625  N   VAL A 212     3864   5525   5714   -544   -764   2384       N  
ATOM   1626  CA  VAL A 212       5.209  13.881 -16.855  1.00 43.83           C  
ANISOU 1626  CA  VAL A 212     4474   6062   6118   -653   -846   2538       C  
ATOM   1627  C   VAL A 212       4.593  12.740 -17.654  1.00 43.48           C  
ANISOU 1627  C   VAL A 212     4501   6150   5871   -776   -863   2543       C  
ATOM   1628  O   VAL A 212       3.827  12.965 -18.599  1.00 41.79           O  
ANISOU 1628  O   VAL A 212     4307   5984   5588   -849  -1009   2669       O  
ATOM   1629  CB  VAL A 212       6.641  14.192 -17.325  1.00 46.16           C  
ANISOU 1629  CB  VAL A 212     4864   6316   6358   -729   -757   2609       C  
ATOM   1630  CG1 VAL A 212       6.674  14.394 -18.835  1.00 47.13           C  
ANISOU 1630  CG1 VAL A 212     5098   6486   6323   -842   -816   2770       C  
ATOM   1631  CG2 VAL A 212       7.184  15.422 -16.608  1.00 48.10           C  
ANISOU 1631  CG2 VAL A 212     5083   6406   6786   -685   -816   2648       C  
ATOM   1632  N   ILE A 213       4.913  11.499 -17.284  1.00 45.29           N  
ANISOU 1632  N   ILE A 213     4804   6421   5984   -814   -739   2415       N  
ATOM   1633  CA  ILE A 213       4.361  10.346 -17.987  1.00 47.24           C  
ANISOU 1633  CA  ILE A 213     5214   6738   5997   -960   -787   2411       C  
ATOM   1634  C   ILE A 213       2.844  10.312 -17.849  1.00 47.58           C  
ANISOU 1634  C   ILE A 213     5102   6888   6088  -1028   -977   2480       C  
ATOM   1635  O   ILE A 213       2.132   9.907 -18.774  1.00 48.12           O  
ANISOU 1635  O   ILE A 213     5271   7024   5990  -1202  -1127   2582       O  
ATOM   1636  CB  ILE A 213       5.004   9.047 -17.470  1.00 46.44           C  
ANISOU 1636  CB  ILE A 213     5268   6617   5759   -957   -627   2254       C  
ATOM   1637  CG1 ILE A 213       6.500   9.032 -17.793  1.00 46.48           C  
ANISOU 1637  CG1 ILE A 213     5398   6588   5674   -864   -429   2245       C  
ATOM   1638  CG2 ILE A 213       4.305   7.837 -18.076  1.00 46.49           C  
ANISOU 1638  CG2 ILE A 213     5518   6642   5503  -1136   -728   2245       C  
ATOM   1639  CD1 ILE A 213       7.280   7.935 -17.089  1.00 45.91           C  
ANISOU 1639  CD1 ILE A 213     5432   6501   5510   -776   -246   2103       C  
ATOM   1640  N   ASN A 214       2.325  10.733 -16.692  1.00 48.74           N  
ANISOU 1640  N   ASN A 214     5000   7075   6445   -891   -975   2449       N  
ATOM   1641  CA  ASN A 214       0.896  10.696 -16.414  1.00 51.15           C  
ANISOU 1641  CA  ASN A 214     5082   7557   6797   -908  -1119   2551       C  
ATOM   1642  C   ASN A 214       0.179  11.993 -16.774  1.00 52.25           C  
ANISOU 1642  C   ASN A 214     5047   7740   7065   -768  -1246   2720       C  
ATOM   1643  O   ASN A 214      -0.995  12.154 -16.422  1.00 54.87           O  
ANISOU 1643  O   ASN A 214     5126   8260   7461   -695  -1336   2836       O  
ATOM   1644  CB  ASN A 214       0.652  10.375 -14.936  1.00 52.92           C  
ANISOU 1644  CB  ASN A 214     5129   7842   7138   -790  -1021   2441       C  
ATOM   1645  CG  ASN A 214       0.860   8.909 -14.615  1.00 54.59           C  
ANISOU 1645  CG  ASN A 214     5483   8067   7192   -971   -968   2329       C  
ATOM   1646  OD1 ASN A 214      -0.022   8.080 -14.848  1.00 56.78           O  
ANISOU 1646  OD1 ASN A 214     5751   8486   7335  -1183  -1101   2418       O  
ATOM   1647  ND2 ASN A 214       2.028   8.580 -14.073  1.00 52.96           N  
ANISOU 1647  ND2 ASN A 214     5420   7712   6989   -902   -795   2157       N  
ATOM   1648  N   GLY A 215       0.851  12.922 -17.449  1.00 50.43           N  
ANISOU 1648  N   GLY A 215     4502   8512   6146   1473    340   -208       N  
ATOM   1649  CA  GLY A 215       0.203  14.101 -17.981  1.00 54.17           C  
ANISOU 1649  CA  GLY A 215     5228   8963   6390   1467      1    241       C  
ATOM   1650  C   GLY A 215       0.411  15.375 -17.192  1.00 54.48           C  
ANISOU 1650  C   GLY A 215     5753   8365   6581   1530   -301    658       C  
ATOM   1651  O   GLY A 215       0.077  16.455 -17.699  1.00 57.03           O  
ANISOU 1651  O   GLY A 215     6275   8636   6757   1468   -589   1104       O  
ATOM   1652  N   ASP A 216       0.935  15.293 -15.972  1.00 52.25           N  
ANISOU 1652  N   ASP A 216     5646   7606   6600   1638   -242    532       N  
ATOM   1653  CA  ASP A 216       1.230  16.487 -15.180  1.00 54.96           C  
ANISOU 1653  CA  ASP A 216     6424   7365   7092   1644   -490    853       C  
ATOM   1654  C   ASP A 216       2.543  17.080 -15.674  1.00 56.51           C  
ANISOU 1654  C   ASP A 216     6661   7725   7084   1186   -568   1158       C  
ATOM   1655  O   ASP A 216       3.623  16.562 -15.380  1.00 54.72           O  
ANISOU 1655  O   ASP A 216     6303   7608   6880    993   -402    998       O  
ATOM   1656  CB  ASP A 216       1.310  16.148 -13.697  1.00 56.23           C  
ANISOU 1656  CB  ASP A 216     6720   7054   7591   1883   -390    586       C  
ATOM   1657  CG  ASP A 216      -0.006  16.359 -12.978  1.00 59.32           C  
ANISOU 1657  CG  ASP A 216     7303   7023   8212   2306   -467    480       C  
ATOM   1658  OD1 ASP A 216      -0.810  17.206 -13.423  1.00 63.82           O  
ANISOU 1658  OD1 ASP A 216     8031   7461   8757   2404   -682    728       O  
ATOM   1659  OD2 ASP A 216      -0.232  15.681 -11.955  1.00 58.88           O  
ANISOU 1659  OD2 ASP A 216     7196   6803   8374   2209   -269    166       O  
ATOM   1660  N   ARG A 217       2.452  18.187 -16.419  1.00 60.99           N  
ANISOU 1660  N   ARG A 217     7400   8302   7472   1011   -827   1624       N  
ATOM   1661  CA  ARG A 217       3.629  18.811 -17.011  1.00 66.41           C  
ANISOU 1661  CA  ARG A 217     8121   9180   7930    545   -910   1954       C  
ATOM   1662  C   ARG A 217       3.763  20.296 -16.689  1.00 67.23           C  
ANISOU 1662  C   ARG A 217     8650   8727   8169    477  -1203   2419       C  
ATOM   1663  O   ARG A 217       4.675  20.945 -17.215  1.00 72.22           O  
ANISOU 1663  O   ARG A 217     9340   9481   8619     81  -1297   2751       O  
ATOM   1664  CB  ARG A 217       3.614  18.640 -18.535  1.00 74.91           C  
ANISOU 1664  CB  ARG A 217     8899  10990   8574    247   -906   2117       C  
ATOM   1665  CG  ARG A 217       3.229  17.248 -19.007  1.00 80.98           C  
ANISOU 1665  CG  ARG A 217     9221  12322   9224    321   -614   1635       C  
ATOM   1666  CD  ARG A 217       3.472  17.076 -20.500  1.00 92.87           C  
ANISOU 1666  CD  ARG A 217    10394  14643  10249    -90   -573   1739       C  
ATOM   1667  NE  ARG A 217       3.651  15.671 -20.866  1.00 98.45           N  
ANISOU 1667  NE  ARG A 217    10626  15891  10888   -163   -201   1170       N  
ATOM   1668  CZ  ARG A 217       2.674  14.855 -21.255  1.00101.98           C  
ANISOU 1668  CZ  ARG A 217    10789  16671  11286     23    -51    840       C  
ATOM   1669  NH1 ARG A 217       1.422  15.288 -21.339  1.00104.89           N  
ANISOU 1669  NH1 ARG A 217    11295  16922  11637    308   -259   1037       N  
ATOM   1670  NH2 ARG A 217       2.953  13.595 -21.563  1.00100.83           N  
ANISOU 1670  NH2 ARG A 217    10199  16968  11145    -79    321    294       N  
ATOM   1671  N   TRP A 218       2.893  20.856 -15.845  1.00 62.16           N  
ANISOU 1671  N   TRP A 218     8288   7468   7861    835  -1332   2431       N  
ATOM   1672  CA  TRP A 218       2.891  22.302 -15.644  1.00 59.90           C  
ANISOU 1672  CA  TRP A 218     8369   6622   7767    781  -1594   2860       C  
ATOM   1673  C   TRP A 218       4.193  22.796 -15.028  1.00 57.94           C  
ANISOU 1673  C   TRP A 218     8305   6125   7585    469  -1582   2896       C  
ATOM   1674  O   TRP A 218       4.586  23.949 -15.249  1.00 59.20           O  
ANISOU 1674  O   TRP A 218     8690   6009   7795    237  -1767   3311       O  
ATOM   1675  CB  TRP A 218       1.706  22.702 -14.765  1.00 56.91           C  
ANISOU 1675  CB  TRP A 218     8210   5623   7791   1234  -1681   2750       C  
ATOM   1676  CG  TRP A 218       1.722  22.098 -13.389  1.00 50.98           C  
ANISOU 1676  CG  TRP A 218     7512   4589   7269   1454  -1498   2240       C  
ATOM   1677  CD1 TRP A 218       1.080  20.965 -12.982  1.00 48.02           C  
ANISOU 1677  CD1 TRP A 218     6944   4379   6922   1755  -1309   1807       C  
ATOM   1678  CD2 TRP A 218       2.408  22.605 -12.239  1.00 51.62           C  
ANISOU 1678  CD2 TRP A 218     7841   4205   7569   1363  -1490   2129       C  
ATOM   1679  NE1 TRP A 218       1.324  20.734 -11.649  1.00 48.29           N  
ANISOU 1679  NE1 TRP A 218     7085   4101   7162   1850  -1187   1474       N  
ATOM   1680  CE2 TRP A 218       2.139  21.726 -11.170  1.00 49.77           C  
ANISOU 1680  CE2 TRP A 218     7517   3960   7432   1594  -1267   1635       C  
ATOM   1681  CE3 TRP A 218       3.227  23.715 -12.009  1.00 52.85           C  
ANISOU 1681  CE3 TRP A 218     8231   4047   7803   1065  -1578   2351       C  
ATOM   1682  CZ2 TRP A 218       2.659  21.924  -9.892  1.00 48.06           C  
ANISOU 1682  CZ2 TRP A 218     7409   3515   7337   1504  -1138   1388       C  
ATOM   1683  CZ3 TRP A 218       3.742  23.908 -10.742  1.00 51.70           C  
ANISOU 1683  CZ3 TRP A 218     8215   3619   7810   1010  -1461   2052       C  
ATOM   1684  CH2 TRP A 218       3.455  23.018  -9.699  1.00 49.40           C  
ANISOU 1684  CH2 TRP A 218     7814   3385   7570   1227  -1261   1592       C  
ATOM   1685  N   PHE A 219       4.876  21.949 -14.258  1.00 55.13           N  
ANISOU 1685  N   PHE A 219     7839   5863   7246    451  -1369   2487       N  
ATOM   1686  CA  PHE A 219       6.094  22.353 -13.568  1.00 56.00           C  
ANISOU 1686  CA  PHE A 219     8094   5770   7415    169  -1355   2483       C  
ATOM   1687  C   PHE A 219       7.297  22.456 -14.494  1.00 57.38           C  
ANISOU 1687  C   PHE A 219     8134   6392   7275   -318  -1345   2723       C  
ATOM   1688  O   PHE A 219       8.316  23.033 -14.098  1.00 58.10           O  
ANISOU 1688  O   PHE A 219     8370   6308   7396   -606  -1377   2813       O  
ATOM   1689  CB  PHE A 219       6.402  21.365 -12.434  1.00 52.00           C  
ANISOU 1689  CB  PHE A 219     7470   5263   7025    319  -1149   2014       C  
ATOM   1690  CG  PHE A 219       6.482  19.931 -12.882  1.00 51.57           C  
ANISOU 1690  CG  PHE A 219     7001   5779   6815    369   -915   1737       C  
ATOM   1691  CD1 PHE A 219       7.681  19.391 -13.317  1.00 54.19           C  
ANISOU 1691  CD1 PHE A 219     7072   6554   6963     35   -779   1699       C  
ATOM   1692  CD2 PHE A 219       5.356  19.123 -12.869  1.00 49.25           C  
ANISOU 1692  CD2 PHE A 219     6556   5561   6596    743   -815   1487       C  
ATOM   1693  CE1 PHE A 219       7.753  18.074 -13.733  1.00 53.18           C  
ANISOU 1693  CE1 PHE A 219     6530   6905   6770     79   -534   1405       C  
ATOM   1694  CE2 PHE A 219       5.423  17.808 -13.285  1.00 48.32           C  
ANISOU 1694  CE2 PHE A 219     6039   5928   6393    777   -572   1201       C  
ATOM   1695  CZ  PHE A 219       6.621  17.283 -13.716  1.00 50.01           C  
ANISOU 1695  CZ  PHE A 219     5985   6551   6465    447   -425   1153       C  
ATOM   1696  N   LEU A 220       7.208  21.924 -15.708  1.00 56.17           N  
ANISOU 1696  N   LEU A 220     7693   6838   6810   -442  -1292   2803       N  
ATOM   1697  CA  LEU A 220       8.351  21.927 -16.604  1.00 57.69           C  
ANISOU 1697  CA  LEU A 220     7713   7530   6678   -929  -1249   2971       C  
ATOM   1698  C   LEU A 220       8.705  23.347 -17.034  1.00 65.61           C  
ANISOU 1698  C   LEU A 220     9002   8293   7633  -1238  -1493   3524       C  
ATOM   1699  O   LEU A 220       7.888  24.272 -16.985  1.00 63.97           O  
ANISOU 1699  O   LEU A 220     9058   7631   7617  -1066  -1704   3835       O  
ATOM   1700  CB  LEU A 220       8.066  21.071 -17.838  1.00 57.46           C  
ANISOU 1700  CB  LEU A 220     7291   8236   6306  -1015  -1126   2898       C  
ATOM   1701  CG  LEU A 220       7.916  19.566 -17.607  1.00 54.07           C  
ANISOU 1701  CG  LEU A 220     6497   8120   5927   -801   -827   2334       C  
ATOM   1702  CD1 LEU A 220       7.519  18.871 -18.906  1.00 54.73           C  
ANISOU 1702  CD1 LEU A 220     6198   8924   5673   -919   -710   2251       C  
ATOM   1703  CD2 LEU A 220       9.199  18.962 -17.041  1.00 51.57           C  
ANISOU 1703  CD2 LEU A 220     6023   7877   5694   -984   -627   2054       C  
ATOM   1704  N   ASN A 221       9.954  23.510 -17.459  1.00 71.28           N  
ANISOU 1704  N   ASN A 221     9646   9307   8129  -1705  -1452   3644       N  
ATOM   1705  CA  ASN A 221      10.413  24.749 -18.067  1.00 79.93           C  
ANISOU 1705  CA  ASN A 221    10950  10296   9122  -2081  -1653   4194       C  
ATOM   1706  C   ASN A 221      11.625  24.415 -18.920  1.00 86.48           C  
ANISOU 1706  C   ASN A 221    11513  11791   9554  -2596  -1529   4219       C  
ATOM   1707  O   ASN A 221      12.286  23.394 -18.716  1.00 83.52           O  
ANISOU 1707  O   ASN A 221    10858  11764   9112  -2648  -1293   3780       O  
ATOM   1708  CB  ASN A 221      10.740  25.822 -17.019  1.00 79.72           C  
ANISOU 1708  CB  ASN A 221    11319   9505   9467  -2086  -1771   4298       C  
ATOM   1709  CG  ASN A 221      11.859  25.415 -16.073  1.00 78.32           C  
ANISOU 1709  CG  ASN A 221    11106   9299   9353  -2220  -1605   3911       C  
ATOM   1710  OD1 ASN A 221      12.689  24.563 -16.390  1.00 78.35           O  
ANISOU 1710  OD1 ASN A 221    10804   9853   9113  -2432  -1430   3698       O  
ATOM   1711  ND2 ASN A 221      11.888  26.039 -14.901  1.00 77.54           N  
ANISOU 1711  ND2 ASN A 221    11296   8570   9596  -2108  -1658   3811       N  
ATOM   1712  N   ARG A 222      11.901  25.278 -19.896  1.00 97.17           N  
ANISOU 1712  N   ARG A 222    12931  13323  10665  -2981  -1686   4747       N  
ATOM   1713  CA  ARG A 222      13.013  25.049 -20.804  1.00101.01           C  
ANISOU 1713  CA  ARG A 222    13161  14485  10734  -3518  -1574   4797       C  
ATOM   1714  C   ARG A 222      14.291  25.743 -20.349  1.00 98.45           C  
ANISOU 1714  C   ARG A 222    13001  13889  10515  -3844  -1576   4831       C  
ATOM   1715  O   ARG A 222      15.162  26.026 -21.181  1.00 99.05           O  
ANISOU 1715  O   ARG A 222    12935  14364  10336  -4250  -1560   4920       O  
ATOM   1716  CB  ARG A 222      12.642  25.476 -22.227  1.00107.33           C  
ANISOU 1716  CB  ARG A 222    13817  15745  11220  -3708  -1696   5144       C  
ATOM   1717  CG  ARG A 222      12.312  24.283 -23.123  1.00107.84           C  
ANISOU 1717  CG  ARG A 222    13442  16671  10861  -3784  -1523   4921       C  
ATOM   1718  CD  ARG A 222      12.348  24.624 -24.606  1.00115.53           C  
ANISOU 1718  CD  ARG A 222    14181  18246  11468  -4121  -1602   5156       C  
ATOM   1719  NE  ARG A 222      13.706  24.614 -25.147  1.00119.41           N  
ANISOU 1719  NE  ARG A 222    14485  19167  11717  -4626  -1494   5046       N  
ATOM   1720  CZ  ARG A 222      13.998  24.591 -26.446  1.00122.52           C  
ANISOU 1720  CZ  ARG A 222    14572  20255  11724  -5005  -1496   5098       C  
ATOM   1721  NH1 ARG A 222      13.028  24.568 -27.351  1.00124.41           N  
ANISOU 1721  NH1 ARG A 222    14640  20870  11760  -4962  -1591   5278       N  
ATOM   1722  NH2 ARG A 222      15.265  24.585 -26.840  1.00123.13           N  
ANISOU 1722  NH2 ARG A 222    14500  20667  11618  -5430  -1412   4953       N  
ATOM   1723  N   PHE A 223      14.425  26.013 -19.053  1.00 95.16           N  
ANISOU 1723  N   PHE A 223    12853  12829  10475  -3660  -1593   4693       N  
ATOM   1724  CA  PHE A 223      15.731  26.364 -18.530  1.00 96.79           C  
ANISOU 1724  CA  PHE A 223    13121  12914  10740  -3971  -1535   4582       C  
ATOM   1725  C   PHE A 223      16.501  25.076 -18.240  1.00 91.37           C  
ANISOU 1725  C   PHE A 223    12074  12688   9954  -4017  -1275   4082       C  
ATOM   1726  O   PHE A 223      15.930  23.984 -18.155  1.00 89.67           O  
ANISOU 1726  O   PHE A 223    11612  12693   9767  -3687  -1135   3729       O  
ATOM   1727  CB  PHE A 223      15.677  27.189 -17.236  1.00 99.64           C  
ANISOU 1727  CB  PHE A 223    13854  12466  11540  -3782  -1630   4530       C  
ATOM   1728  CG  PHE A 223      14.488  28.111 -17.103  1.00105.88           C  
ANISOU 1728  CG  PHE A 223    14925  12663  12643  -3427  -1807   4738       C  
ATOM   1729  CD1 PHE A 223      13.792  28.592 -18.202  1.00111.07           C  
ANISOU 1729  CD1 PHE A 223    15547  13452  13201  -3387  -1927   5088       C  
ATOM   1730  CD2 PHE A 223      14.085  28.511 -15.839  1.00106.09           C  
ANISOU 1730  CD2 PHE A 223    15214  12014  13081  -3142  -1835   4546       C  
ATOM   1731  CE1 PHE A 223      12.704  29.434 -18.035  1.00113.83           C  
ANISOU 1731  CE1 PHE A 223    16110  13248  13892  -3040  -2061   5253       C  
ATOM   1732  CE2 PHE A 223      13.006  29.352 -15.668  1.00109.16           C  
ANISOU 1732  CE2 PHE A 223    15811  11861  13803  -2804  -1947   4656       C  
ATOM   1733  CZ  PHE A 223      12.315  29.815 -16.766  1.00112.73           C  
ANISOU 1733  CZ  PHE A 223    16218  12426  14188  -2742  -2056   5018       C  
ATOM   1734  N   THR A 224      17.810  25.212 -18.079  1.00 89.75           N  
ANISOU 1734  N   THR A 224    11812  12607   9682  -4403  -1203   4024       N  
ATOM   1735  CA  THR A 224      18.634  24.136 -17.555  1.00 85.24           C  
ANISOU 1735  CA  THR A 224    10912  12323   9151  -4394   -979   3544       C  
ATOM   1736  C   THR A 224      19.432  24.693 -16.387  1.00 83.29           C  
ANISOU 1736  C   THR A 224    10878  11638   9131  -4483  -1028   3484       C  
ATOM   1737  O   THR A 224      19.386  25.889 -16.082  1.00 86.66           O  
ANISOU 1737  O   THR A 224    11683  11573   9669  -4585  -1203   3766       O  
ATOM   1738  CB  THR A 224      19.549  23.530 -18.633  1.00 86.98           C  
ANISOU 1738  CB  THR A 224    10718  13302   9029  -4817   -795   3454       C  
ATOM   1739  OG1 THR A 224      19.583  22.103 -18.471  1.00 82.64           O  
ANISOU 1739  OG1 THR A 224     9743  13087   8570  -4586   -549   2958       O  
ATOM   1740  CG2 THR A 224      20.978  24.076 -18.554  1.00 88.54           C  
ANISOU 1740  CG2 THR A 224    10933  13524   9184  -5127   -814   3396       C  
ATOM   1741  N   THR A 225      20.154  23.810 -15.715  1.00 77.87           N  
ANISOU 1741  N   THR A 225     9918  11132   8538  -4435   -867   3105       N  
ATOM   1742  CA  THR A 225      20.999  24.209 -14.608  1.00 74.69           C  
ANISOU 1742  CA  THR A 225     9637  10444   8296  -4552   -903   3017       C  
ATOM   1743  C   THR A 225      22.252  23.353 -14.638  1.00 71.71           C  
ANISOU 1743  C   THR A 225     8830  10568   7847  -4769   -720   2758       C  
ATOM   1744  O   THR A 225      22.373  22.410 -15.424  1.00 67.57           O  
ANISOU 1744  O   THR A 225     7927  10531   7215  -4739   -550   2575       O  
ATOM   1745  CB  THR A 225      20.276  24.067 -13.263  1.00 71.86           C  
ANISOU 1745  CB  THR A 225     9448   9613   8244  -4099   -952   2817       C  
ATOM   1746  OG1 THR A 225      21.095  24.605 -12.217  1.00 71.27           O  
ANISOU 1746  OG1 THR A 225     9506   9302   8272  -4281  -1004   2753       O  
ATOM   1747  CG2 THR A 225      19.976  22.607 -12.974  1.00 69.02           C  
ANISOU 1747  CG2 THR A 225     8716   9521   7986  -3728   -782   2475       C  
ATOM   1748  N   THR A 226      23.191  23.705 -13.777  1.00 73.95           N  
ANISOU 1748  N   THR A 226     9171  10712   8215  -4874   -756   2658       N  
ATOM   1749  CA  THR A 226      24.392  22.917 -13.572  1.00 71.97           C  
ANISOU 1749  CA  THR A 226     8539  10835   7970  -4898   -613   2364       C  
ATOM   1750  C   THR A 226      24.183  22.023 -12.357  1.00 65.03           C  
ANISOU 1750  C   THR A 226     7480   9864   7364  -4600   -561   2158       C  
ATOM   1751  O   THR A 226      23.469  22.383 -11.418  1.00 62.99           O  
ANISOU 1751  O   THR A 226     7490   9195   7249  -4451   -679   2215       O  
ATOM   1752  CB  THR A 226      25.609  23.820 -13.373  1.00 76.04           C  
ANISOU 1752  CB  THR A 226     9188  11317   8386  -5199   -685   2399       C  
ATOM   1753  OG1 THR A 226      25.591  24.379 -12.056  1.00 76.72           O  
ANISOU 1753  OG1 THR A 226     9513  10999   8637  -5180   -800   2400       O  
ATOM   1754  CG2 THR A 226      25.594  24.956 -14.388  1.00 79.20           C  
ANISOU 1754  CG2 THR A 226     9858  11663   8570  -5484   -789   2685       C  
ATOM   1755  N   LEU A 227      24.789  20.836 -12.397  1.00 63.34           N  
ANISOU 1755  N   LEU A 227     6823  10000   7245  -4428   -382   1888       N  
ATOM   1756  CA  LEU A 227      24.770  19.966 -11.226  1.00 59.34           C  
ANISOU 1756  CA  LEU A 227     6098   9436   7014  -4137   -342   1729       C  
ATOM   1757  C   LEU A 227      25.263  20.715  -9.995  1.00 60.14           C  
ANISOU 1757  C   LEU A 227     6415   9307   7129  -4279   -506   1804       C  
ATOM   1758  O   LEU A 227      24.737  20.530  -8.892  1.00 58.31           O  
ANISOU 1758  O   LEU A 227     6220   8880   7054  -4122   -578   1801       O  
ATOM   1759  CB  LEU A 227      25.625  18.727 -11.484  1.00 59.05           C  
ANISOU 1759  CB  LEU A 227     5593   9717   7125  -3934   -131   1454       C  
ATOM   1760  CG  LEU A 227      25.423  17.548 -10.531  1.00 60.04           C  
ANISOU 1760  CG  LEU A 227     5425   9793   7595  -3538    -48   1308       C  
ATOM   1761  CD1 LEU A 227      23.994  17.040 -10.613  1.00 59.70           C  
ANISOU 1761  CD1 LEU A 227     5366   9648   7670  -3272      2   1290       C  
ATOM   1762  CD2 LEU A 227      26.411  16.432 -10.839  1.00 58.79           C  
ANISOU 1762  CD2 LEU A 227     4868   9809   7659  -3351    153   1063       C  
ATOM   1763  N   ASN A 228      26.264  21.581 -10.173  1.00 63.16           N  
ANISOU 1763  N   ASN A 228     6936   9728   7334  -4590   -565   1856       N  
ATOM   1764  CA  ASN A 228      26.809  22.347  -9.059  1.00 64.48           C  
ANISOU 1764  CA  ASN A 228     7293   9718   7488  -4758   -700   1878       C  
ATOM   1765  C   ASN A 228      25.803  23.374  -8.553  1.00 65.01           C  
ANISOU 1765  C   ASN A 228     7831   9294   7577  -4824   -857   2011       C  
ATOM   1766  O   ASN A 228      25.477  23.405  -7.361  1.00 65.04           O  
ANISOU 1766  O   ASN A 228     7920   9104   7688  -4750   -935   1950       O  
ATOM   1767  CB  ASN A 228      28.105  23.037  -9.495  1.00 68.70           C  
ANISOU 1767  CB  ASN A 228     7849  10417   7836  -5078   -701   1885       C  
ATOM   1768  CG  ASN A 228      29.227  22.878  -8.486  1.00 68.76           C  
ANISOU 1768  CG  ASN A 228     7671  10585   7871  -5126   -715   1770       C  
ATOM   1769  OD1 ASN A 228      29.384  21.825  -7.870  1.00 67.11           O  
ANISOU 1769  OD1 ASN A 228     7135  10539   7824  -4872   -661   1669       O  
ATOM   1770  ND2 ASN A 228      30.020  23.928  -8.319  1.00 72.33           N  
ANISOU 1770  ND2 ASN A 228     8318  10989   8175  -5448   -789   1802       N  
ATOM   1771  N   ASP A 229      25.304  24.230  -9.448  1.00 69.98           N  
ANISOU 1771  N   ASP A 229     8769   9703   8116  -4949   -904   2192       N  
ATOM   1772  CA  ASP A 229      24.405  25.297  -9.023  1.00 73.71           C  
ANISOU 1772  CA  ASP A 229     9713   9615   8678  -4960  -1043   2310       C  
ATOM   1773  C   ASP A 229      23.121  24.739  -8.430  1.00 71.87           C  
ANISOU 1773  C   ASP A 229     9539   9148   8619  -4479  -1053   2203       C  
ATOM   1774  O   ASP A 229      22.507  25.380  -7.570  1.00 73.57           O  
ANISOU 1774  O   ASP A 229    10061   8934   8960  -4361  -1141   2137       O  
ATOM   1775  CB  ASP A 229      24.098  26.224 -10.200  1.00 77.00           C  
ANISOU 1775  CB  ASP A 229    10390   9863   9004  -5087  -1091   2564       C  
ATOM   1776  CG  ASP A 229      25.285  27.094 -10.580  1.00 83.18           C  
ANISOU 1776  CG  ASP A 229    11216  10751   9639  -5437  -1101   2613       C  
ATOM   1777  OD1 ASP A 229      26.340  26.537 -10.951  1.00 84.17           O  
ANISOU 1777  OD1 ASP A 229    11020  11350   9609  -5561  -1007   2513       O  
ATOM   1778  OD2 ASP A 229      25.161  28.335 -10.509  1.00 87.32           O  
ANISOU 1778  OD2 ASP A 229    12082  10861  10233  -5569  -1190   2737       O  
ATOM   1779  N   PHE A 230      22.706  23.545  -8.862  1.00 68.95           N  
ANISOU 1779  N   PHE A 230     8863   9061   8275  -4165   -940   2130       N  
ATOM   1780  CA  PHE A 230      21.493  22.948  -8.319  1.00 65.90           C  
ANISOU 1780  CA  PHE A 230     8508   8481   8051  -3662   -930   1998       C  
ATOM   1781  C   PHE A 230      21.707  22.449  -6.894  1.00 62.99           C  
ANISOU 1781  C   PHE A 230     8012   8133   7787  -3515   -934   1807       C  
ATOM   1782  O   PHE A 230      20.834  22.616  -6.036  1.00 64.11           O  
ANISOU 1782  O   PHE A 230     8365   7962   8032  -3257   -991   1708       O  
ATOM   1783  CB  PHE A 230      21.019  21.802  -9.213  1.00 64.62           C  
ANISOU 1783  CB  PHE A 230     8029   8623   7900  -3402   -785   1951       C  
ATOM   1784  CG  PHE A 230      19.978  20.936  -8.569  1.00 60.98           C  
ANISOU 1784  CG  PHE A 230     7496   8049   7624  -2900   -735   1778       C  
ATOM   1785  CD1 PHE A 230      18.647  21.318  -8.565  1.00 60.80           C  
ANISOU 1785  CD1 PHE A 230     7779   7658   7664  -2609   -805   1796       C  
ATOM   1786  CD2 PHE A 230      20.332  19.748  -7.950  1.00 57.13           C  
ANISOU 1786  CD2 PHE A 230     6619   7812   7275  -2721   -620   1618       C  
ATOM   1787  CE1 PHE A 230      17.690  20.528  -7.963  1.00 59.25           C  
ANISOU 1787  CE1 PHE A 230     7515   7369   7629  -2166   -751   1624       C  
ATOM   1788  CE2 PHE A 230      19.381  18.955  -7.344  1.00 53.61           C  
ANISOU 1788  CE2 PHE A 230     6106   7257   7006  -2279   -569   1485       C  
ATOM   1789  CZ  PHE A 230      18.058  19.345  -7.350  1.00 55.90           C  
ANISOU 1789  CZ  PHE A 230     6717   7201   7321  -2010   -630   1471       C  
ATOM   1790  N   ASN A 231      22.857  21.825  -6.625  1.00 60.33           N  
ANISOU 1790  N   ASN A 231     7306   8191   7425  -3684   -876   1764       N  
ATOM   1791  CA  ASN A 231      23.127  21.335  -5.278  1.00 58.13           C  
ANISOU 1791  CA  ASN A 231     6863   8006   7219  -3575   -902   1652       C  
ATOM   1792  C   ASN A 231      23.197  22.475  -4.269  1.00 60.32           C  
ANISOU 1792  C   ASN A 231     7489   8012   7419  -3790  -1043   1603       C  
ATOM   1793  O   ASN A 231      22.793  22.303  -3.112  1.00 59.33           O  
ANISOU 1793  O   ASN A 231     7387   7823   7331  -3617  -1085   1485       O  
ATOM   1794  CB  ASN A 231      24.423  20.523  -5.261  1.00 58.12           C  
ANISOU 1794  CB  ASN A 231     6368   8483   7231  -3742   -829   1664       C  
ATOM   1795  CG  ASN A 231      24.229  19.106  -5.772  1.00 54.87           C  
ANISOU 1795  CG  ASN A 231     5521   8311   7016  -3421   -658   1620       C  
ATOM   1796  OD1 ASN A 231      23.139  18.541  -5.676  1.00 51.69           O  
ANISOU 1796  OD1 ASN A 231     5143   7751   6745  -3022   -609   1558       O  
ATOM   1797  ND2 ASN A 231      25.291  18.523  -6.315  1.00 55.28           N  
ANISOU 1797  ND2 ASN A 231     5165   8726   7114  -3578   -546   1614       N  
ATOM   1798  N   LEU A 232      23.704  23.642  -4.677  1.00 65.34           N  
ANISOU 1798  N   LEU A 232     8380   8495   7951  -4190  -1101   1678       N  
ATOM   1799  CA  LEU A 232      23.673  24.801  -3.793  1.00 70.73           C  
ANISOU 1799  CA  LEU A 232     9407   8852   8616  -4407  -1201   1581       C  
ATOM   1800  C   LEU A 232      22.258  25.076  -3.303  1.00 73.38           C  
ANISOU 1800  C   LEU A 232    10048   8738   9094  -4060  -1230   1464       C  
ATOM   1801  O   LEU A 232      22.051  25.424  -2.135  1.00 72.95           O  
ANISOU 1801  O   LEU A 232    10113   8554   9052  -4075  -1271   1268       O  
ATOM   1802  CB  LEU A 232      24.230  26.028  -4.514  1.00 74.56           C  
ANISOU 1802  CB  LEU A 232    10147   9139   9044  -4848  -1235   1709       C  
ATOM   1803  CG  LEU A 232      25.690  26.374  -4.222  1.00 78.93           C  
ANISOU 1803  CG  LEU A 232    10550   9993   9446  -5298  -1243   1678       C  
ATOM   1804  CD1 LEU A 232      26.472  26.581  -5.514  1.00 80.18           C  
ANISOU 1804  CD1 LEU A 232    10634  10338   9492  -5441  -1181   1833       C  
ATOM   1805  CD2 LEU A 232      25.773  27.609  -3.326  1.00 82.63           C  
ANISOU 1805  CD2 LEU A 232    11334  10130   9932  -5534  -1298   1510       C  
ATOM   1806  N   VAL A 233      21.269  24.918  -4.186  1.00 75.94           N  
ANISOU 1806  N   VAL A 233    10478   8857   9517  -3762  -1203   1565       N  
ATOM   1807  CA  VAL A 233      19.883  25.170  -3.814  1.00 76.93           C  
ANISOU 1807  CA  VAL A 233    10875   8551   9805  -3415  -1227   1457       C  
ATOM   1808  C   VAL A 233      19.309  23.998  -3.030  1.00 74.89           C  
ANISOU 1808  C   VAL A 233    10389   8486   9579  -3019  -1174   1299       C  
ATOM   1809  O   VAL A 233      18.444  24.187  -2.169  1.00 76.21           O  
ANISOU 1809  O   VAL A 233    10729   8394   9835  -2820  -1193   1116       O  
ATOM   1810  CB  VAL A 233      19.034  25.462  -5.063  1.00 76.50           C  
ANISOU 1810  CB  VAL A 233    10995   8238   9833  -3253  -1236   1656       C  
ATOM   1811  CG1 VAL A 233      17.682  26.039  -4.661  1.00 76.81           C  
ANISOU 1811  CG1 VAL A 233    11356   7744  10086  -2960  -1281   1555       C  
ATOM   1812  CG2 VAL A 233      19.772  26.400  -6.004  1.00 78.71           C  
ANISOU 1812  CG2 VAL A 233    11407   8458  10043  -3674  -1280   1904       C  
ATOM   1813  N   ALA A 234      19.766  22.776  -3.314  1.00 72.69           N  
ANISOU 1813  N   ALA A 234     9707   8650   9261  -2907  -1094   1359       N  
ATOM   1814  CA  ALA A 234      19.294  21.620  -2.564  1.00 69.03           C  
ANISOU 1814  CA  ALA A 234     8995   8363   8869  -2548  -1037   1255       C  
ATOM   1815  C   ALA A 234      19.716  21.705  -1.102  1.00 70.32           C  
ANISOU 1815  C   ALA A 234     9115   8652   8951  -2681  -1100   1138       C  
ATOM   1816  O   ALA A 234      18.917  21.423  -0.201  1.00 69.96           O  
ANISOU 1816  O   ALA A 234     9109   8531   8942  -2438  -1101   1004       O  
ATOM   1817  CB  ALA A 234      19.816  20.334  -3.204  1.00 66.66           C  
ANISOU 1817  CB  ALA A 234     8234   8475   8618  -2439   -918   1347       C  
ATOM   1818  N   MET A 235      20.965  22.098  -0.846  1.00 72.76           N  
ANISOU 1818  N   MET A 235     9327   9195   9123  -3092  -1152   1180       N  
ATOM   1819  CA  MET A 235      21.444  22.188   0.529  1.00 74.64           C  
ANISOU 1819  CA  MET A 235     9483   9647   9231  -3274  -1222   1076       C  
ATOM   1820  C   MET A 235      20.573  23.128   1.351  1.00 64.97           C  
ANISOU 1820  C   MET A 235     8643   8049   7995  -3288  -1262    832       C  
ATOM   1821  O   MET A 235      20.179  22.804   2.477  1.00 64.70           O  
ANISOU 1821  O   MET A 235     8547   8139   7898  -3182  -1277    699       O  
ATOM   1822  CB  MET A 235      22.900  22.655   0.552  1.00 91.27           C  
ANISOU 1822  CB  MET A 235    11462  12032  11183  -3757  -1274   1139       C  
ATOM   1823  CG  MET A 235      23.925  21.534   0.647  1.00103.23           C  
ANISOU 1823  CG  MET A 235    12453  14087  12684  -3768  -1261   1308       C  
ATOM   1824  SD  MET A 235      24.131  20.611  -0.888  1.00110.14           S  
ANISOU 1824  SD  MET A 235    13043  15062  13745  -3578  -1125   1476       S  
ATOM   1825  CE  MET A 235      25.918  20.589  -1.018  1.00115.95           C  
ANISOU 1825  CE  MET A 235    13411  16261  14384  -4024  -1148   1587       C  
ATOM   1826  N   LYS A 236      20.260  24.305   0.800  1.00 60.30           N  
ANISOU 1826  N   LYS A 236     8432   6997   7482  -3428  -1273    772       N  
ATOM   1827  CA  LYS A 236      19.490  25.293   1.547  1.00 62.54           C  
ANISOU 1827  CA  LYS A 236     9062   6868   7832  -3471  -1287    499       C  
ATOM   1828  C   LYS A 236      18.144  24.738   1.987  1.00 60.95           C  
ANISOU 1828  C   LYS A 236     8903   6522   7735  -3018  -1248    366       C  
ATOM   1829  O   LYS A 236      17.660  25.074   3.075  1.00 59.95           O  
ANISOU 1829  O   LYS A 236     8883   6314   7582  -3043  -1243     87       O  
ATOM   1830  CB  LYS A 236      19.307  26.551   0.692  1.00 67.78           C  
ANISOU 1830  CB  LYS A 236    10090   6994   8668  -3631  -1297    534       C  
ATOM   1831  CG  LYS A 236      18.207  27.494   1.159  1.00 74.59           C  
ANISOU 1831  CG  LYS A 236    11306   7283   9750  -3541  -1282    274       C  
ATOM   1832  CD  LYS A 236      18.556  28.948   0.845  1.00 84.29           C  
ANISOU 1832  CD  LYS A 236    12831   8055  11139  -3917  -1294    253       C  
ATOM   1833  CE  LYS A 236      17.343  29.864   0.955  1.00 89.78           C  
ANISOU 1833  CE  LYS A 236    13861   8065  12185  -3747  -1268     68       C  
ATOM   1834  NZ  LYS A 236      16.812  30.266  -0.380  1.00 91.82           N  
ANISOU 1834  NZ  LYS A 236    14299   7904  12683  -3574  -1308    405       N  
ATOM   1835  N   TYR A 237      17.535  23.880   1.172  1.00 49.78           N  
ANISOU 1835  N   TYR A 237     5035   5431   8450  -2043    -66    582       N  
ATOM   1836  CA  TYR A 237      16.223  23.322   1.463  1.00 50.18           C  
ANISOU 1836  CA  TYR A 237     5160   5364   8543  -1723   -108    635       C  
ATOM   1837  C   TYR A 237      16.298  21.899   2.003  1.00 50.64           C  
ANISOU 1837  C   TYR A 237     5082   5711   8447  -1499    -93    543       C  
ATOM   1838  O   TYR A 237      15.317  21.153   1.913  1.00 45.45           O  
ANISOU 1838  O   TYR A 237     4478   5027   7763  -1309    -87    614       O  
ATOM   1839  CB  TYR A 237      15.350  23.374   0.209  1.00 52.59           C  
ANISOU 1839  CB  TYR A 237     5595   5513   8872  -1686   -119    882       C  
ATOM   1840  CG  TYR A 237      15.023  24.781  -0.240  1.00 60.30           C  
ANISOU 1840  CG  TYR A 237     6816   6121   9976  -1809   -158    990       C  
ATOM   1841  CD1 TYR A 237      13.893  25.436   0.233  1.00 64.54           C  
ANISOU 1841  CD1 TYR A 237     7511   6373  10640  -1603   -239    962       C  
ATOM   1842  CD2 TYR A 237      15.846  25.455  -1.131  1.00 64.93           C  
ANISOU 1842  CD2 TYR A 237     7504   6642  10526  -2124   -113   1109       C  
ATOM   1843  CE1 TYR A 237      13.592  26.722  -0.172  1.00 69.34           C  
ANISOU 1843  CE1 TYR A 237     8412   6599  11334  -1653   -297   1057       C  
ATOM   1844  CE2 TYR A 237      15.553  26.742  -1.543  1.00 70.44           C  
ANISOU 1844  CE2 TYR A 237     8526   6935  11303  -2236   -145   1226       C  
ATOM   1845  CZ  TYR A 237      14.426  27.370  -1.061  1.00 72.70           C  
ANISOU 1845  CZ  TYR A 237     9007   6901  11713  -1972   -249   1204       C  
ATOM   1846  OH  TYR A 237      14.135  28.649  -1.472  1.00 77.37           O  
ANISOU 1846  OH  TYR A 237     9989   7051  12356  -2025   -302   1318       O  
ATOM   1847  N   ASN A 238      17.439  21.506   2.565  1.00 58.27           N  
ANISOU 1847  N   ASN A 238     5897   6958   9286  -1516    -86    372       N  
ATOM   1848  CA  ASN A 238      17.580  20.204   3.215  1.00 60.73           C  
ANISOU 1848  CA  ASN A 238     6164   7497   9413  -1255    -90    273       C  
ATOM   1849  C   ASN A 238      17.320  19.067   2.226  1.00 54.66           C  
ANISOU 1849  C   ASN A 238     5432   6821   8517  -1154    -58    433       C  
ATOM   1850  O   ASN A 238      16.570  18.128   2.499  1.00 53.66           O  
ANISOU 1850  O   ASN A 238     5424   6652   8311   -963    -38    458       O  
ATOM   1851  CB  ASN A 238      16.647  20.104   4.424  1.00 66.72           C  
ANISOU 1851  CB  ASN A 238     7037   8099  10214  -1067   -101    186       C  
ATOM   1852  CG  ASN A 238      17.248  19.308   5.566  1.00 71.04           C  
ANISOU 1852  CG  ASN A 238     7563   8863  10565   -862   -121     -2       C  
ATOM   1853  OD1 ASN A 238      18.414  19.491   5.923  1.00 74.42           O  
ANISOU 1853  OD1 ASN A 238     7841   9523  10911   -886   -162   -167       O  
ATOM   1854  ND2 ASN A 238      16.454  18.412   6.147  1.00 70.16           N  
ANISOU 1854  ND2 ASN A 238     7614   8695  10350   -663    -89      9       N  
ATOM   1855  N   TYR A 239      17.954  19.159   1.060  1.00 49.28           N  
ANISOU 1855  N   TYR A 239     4658   6268   7799  -1314    -41    529       N  
ATOM   1856  CA  TYR A 239      17.836  18.151   0.016  1.00 42.81           C  
ANISOU 1856  CA  TYR A 239     3853   5560   6851  -1237    -15    664       C  
ATOM   1857  C   TYR A 239      19.164  17.429  -0.149  1.00 43.82           C  
ANISOU 1857  C   TYR A 239     3819   6073   6758  -1172    -27    540       C  
ATOM   1858  O   TYR A 239      20.228  18.057  -0.149  1.00 45.96           O  
ANISOU 1858  O   TYR A 239     3900   6555   7007  -1343    -30    419       O  
ATOM   1859  CB  TYR A 239      17.405  18.780  -1.315  1.00 39.56           C  
ANISOU 1859  CB  TYR A 239     3472   5017   6543  -1435      8    881       C  
ATOM   1860  CG  TYR A 239      15.909  18.752  -1.527  1.00 38.34           C  
ANISOU 1860  CG  TYR A 239     3468   4608   6493  -1340      3   1012       C  
ATOM   1861  CD1 TYR A 239      15.063  19.485  -0.708  1.00 38.28           C  
ANISOU 1861  CD1 TYR A 239     3546   4359   6641  -1298    -25    964       C  
ATOM   1862  CD2 TYR A 239      15.344  17.985  -2.540  1.00 38.75           C  
ANISOU 1862  CD2 TYR A 239     3548   4705   6469  -1285     24   1145       C  
ATOM   1863  CE1 TYR A 239      13.693  19.456  -0.890  1.00 37.72           C  
ANISOU 1863  CE1 TYR A 239     3555   4138   6638  -1192    -35   1031       C  
ATOM   1864  CE2 TYR A 239      13.975  17.951  -2.730  1.00 38.39           C  
ANISOU 1864  CE2 TYR A 239     3586   4504   6495  -1205     18   1213       C  
ATOM   1865  CZ  TYR A 239      13.154  18.689  -1.901  1.00 38.19           C  
ANISOU 1865  CZ  TYR A 239     3614   4282   6614  -1153    -12   1148       C  
ATOM   1866  OH  TYR A 239      11.792  18.658  -2.083  1.00 38.86           O  
ANISOU 1866  OH  TYR A 239     3728   4293   6745  -1057    -22   1167       O  
ATOM   1867  N   GLU A 240      19.101  16.109  -0.274  1.00 44.21           N  
ANISOU 1867  N   GLU A 240     3951   6224   6623   -924    -32    543       N  
ATOM   1868  CA  GLU A 240      20.315  15.325  -0.430  1.00 46.72           C  
ANISOU 1868  CA  GLU A 240     4138   6919   6695   -767    -68    402       C  
ATOM   1869  C   GLU A 240      21.070  15.782  -1.676  1.00 44.26           C  
ANISOU 1869  C   GLU A 240     3602   6845   6370  -1012    -37    447       C  
ATOM   1870  O   GLU A 240      20.456  16.002  -2.727  1.00 40.71           O  
ANISOU 1870  O   GLU A 240     3208   6247   6014  -1177     11    656       O  
ATOM   1871  CB  GLU A 240      19.984  13.836  -0.536  1.00 49.85           C  
ANISOU 1871  CB  GLU A 240     4754   7296   6891   -463    -75    432       C  
ATOM   1872  CG  GLU A 240      19.745  13.160   0.798  1.00 54.22           C  
ANISOU 1872  CG  GLU A 240     5541   7738   7324   -184   -105    323       C  
ATOM   1873  CD  GLU A 240      21.016  13.030   1.611  1.00 60.18           C  
ANISOU 1873  CD  GLU A 240     6168   8816   7881     47   -201     75       C  
ATOM   1874  OE1 GLU A 240      22.078  12.772   1.004  1.00 66.08           O  
ANISOU 1874  OE1 GLU A 240     6713   9925   8471    127   -249    -30       O  
ATOM   1875  OE2 GLU A 240      20.959  13.196   2.851  1.00 58.21           O  
ANISOU 1875  OE2 GLU A 240     5998   8503   7618    159   -233    -37       O  
ATOM   1876  N   PRO A 241      22.393  15.926  -1.603  1.00 45.04           N  
ANISOU 1876  N   PRO A 241     3434   7349   6329  -1047    -60    239       N  
ATOM   1877  CA  PRO A 241      23.146  16.309  -2.804  1.00 49.18           C  
ANISOU 1877  CA  PRO A 241     3734   8152   6800  -1323     -4    262       C  
ATOM   1878  C   PRO A 241      22.981  15.263  -3.895  1.00 51.49           C  
ANISOU 1878  C   PRO A 241     4081   8530   6951  -1162      2    382       C  
ATOM   1879  O   PRO A 241      22.940  14.059  -3.630  1.00 50.45           O  
ANISOU 1879  O   PRO A 241     4066   8449   6655   -786    -59    317       O  
ATOM   1880  CB  PRO A 241      24.597  16.393  -2.313  1.00 52.34           C  
ANISOU 1880  CB  PRO A 241     3802   9069   7016  -1314    -38    -69       C  
ATOM   1881  CG  PRO A 241      24.519  16.416  -0.808  1.00 51.05           C  
ANISOU 1881  CG  PRO A 241     3705   8816   6874  -1100   -115   -236       C  
ATOM   1882  CD  PRO A 241      23.276  15.666  -0.451  1.00 45.18           C  
ANISOU 1882  CD  PRO A 241     3329   7650   6189   -818   -140    -52       C  
ATOM   1883  N   LEU A 242      22.874  15.735  -5.133  1.00 54.91           N  
ANISOU 1883  N   LEU A 242     4472   8958   7435  -1451     76    560       N  
ATOM   1884  CA  LEU A 242      22.700  14.871  -6.293  1.00 54.69           C  
ANISOU 1884  CA  LEU A 242     4476   9021   7281  -1348     88    678       C  
ATOM   1885  C   LEU A 242      24.056  14.640  -6.949  1.00 56.68           C  
ANISOU 1885  C   LEU A 242     4411   9829   7296  -1390    104    500       C  
ATOM   1886  O   LEU A 242      24.827  15.586  -7.137  1.00 61.28           O  
ANISOU 1886  O   LEU A 242     4767  10637   7878  -1740    171    425       O  
ATOM   1887  CB  LEU A 242      21.724  15.497  -7.288  1.00 53.29           C  
ANISOU 1887  CB  LEU A 242     4446   8536   7265  -1598    149    974       C  
ATOM   1888  CG  LEU A 242      20.981  14.523  -8.203  1.00 52.00           C  
ANISOU 1888  CG  LEU A 242     4415   8309   7035  -1429    144   1118       C  
ATOM   1889  CD1 LEU A 242      19.941  13.729  -7.421  1.00 48.15           C  
ANISOU 1889  CD1 LEU A 242     4171   7525   6598  -1157    103   1118       C  
ATOM   1890  CD2 LEU A 242      20.341  15.278  -9.354  1.00 53.55           C  
ANISOU 1890  CD2 LEU A 242     4676   8344   7326  -1688    193   1374       C  
ATOM   1891  N   THR A 243      24.340  13.388  -7.294  1.00 52.63           N  
ANISOU 1891  N   THR A 243     3890   9543   6565  -1047     49    412       N  
ATOM   1892  CA  THR A 243      25.624  13.005  -7.860  1.00 51.90           C  
ANISOU 1892  CA  THR A 243     3473  10041   6206   -989     42    189       C  
ATOM   1893  C   THR A 243      25.434  12.428  -9.258  1.00 49.61           C  
ANISOU 1893  C   THR A 243     3204   9832   5815   -990     79    329       C  
ATOM   1894  O   THR A 243      24.314  12.183  -9.712  1.00 47.60           O  
ANISOU 1894  O   THR A 243     3223   9185   5679   -985     95    574       O  
ATOM   1895  CB  THR A 243      26.340  11.981  -6.965  1.00 54.46           C  
ANISOU 1895  CB  THR A 243     3758  10643   6293   -478    -92   -113       C  
ATOM   1896  OG1 THR A 243      25.627  10.739  -6.989  1.00 55.79           O  
ANISOU 1896  OG1 THR A 243     4285  10528   6385    -84   -155    -25       O  
ATOM   1897  CG2 THR A 243      26.416  12.487  -5.536  1.00 53.96           C  
ANISOU 1897  CG2 THR A 243     3707  10478   6319   -440   -140   -243       C  
ATOM   1898  N   GLN A 244      26.560  12.215  -9.944  1.00 52.96           N  
ANISOU 1898  N   GLN A 244     3301  10823   5999   -999     94    138       N  
ATOM   1899  CA  GLN A 244      26.513  11.649 -11.288  1.00 53.22           C  
ANISOU 1899  CA  GLN A 244     3315  11006   5900   -987    128    232       C  
ATOM   1900  C   GLN A 244      25.893  10.260 -11.282  1.00 50.79           C  
ANISOU 1900  C   GLN A 244     3313  10475   5510   -511     30    251       C  
ATOM   1901  O   GLN A 244      25.234   9.870 -12.253  1.00 49.26           O  
ANISOU 1901  O   GLN A 244     3263  10132   5323   -539     61    431       O  
ATOM   1902  CB  GLN A 244      27.920  11.602 -11.886  1.00 59.07           C  
ANISOU 1902  CB  GLN A 244     3775  12309   6360  -1003    148    -43       C  
ATOM   1903  CG  GLN A 244      27.971  11.086 -13.320  1.00 63.30           C  
ANISOU 1903  CG  GLN A 244     4304  13013   6736  -1003    186     27       C  
ATOM   1904  CD  GLN A 244      27.213  11.972 -14.296  1.00 65.41           C  
ANISOU 1904  CD  GLN A 244     4756  12923   7172  -1437    300    365       C  
ATOM   1905  OE1 GLN A 244      27.174  13.193 -14.142  1.00 66.67           O  
ANISOU 1905  OE1 GLN A 244     5004  12841   7485  -1799    375    463       O  
ATOM   1906  NE2 GLN A 244      26.606  11.357 -15.304  1.00 65.47           N  
ANISOU 1906  NE2 GLN A 244     4852  12890   7135  -1363    304    529       N  
ATOM   1907  N   ASP A 245      26.097   9.495 -10.208  1.00 51.77           N  
ANISOU 1907  N   ASP A 245     3569  10568   5532    -80    -86     60       N  
ATOM   1908  CA  ASP A 245      25.445   8.195 -10.098  1.00 52.71           C  
ANISOU 1908  CA  ASP A 245     4087  10379   5561    326   -159     90       C  
ATOM   1909  C   ASP A 245      23.932   8.347 -10.117  1.00 49.85           C  
ANISOU 1909  C   ASP A 245     4061   9420   5458    121    -91    392       C  
ATOM   1910  O   ASP A 245      23.225   7.535 -10.724  1.00 50.23           O  
ANISOU 1910  O   ASP A 245     4355   9263   5469    210    -81    491       O  
ATOM   1911  CB  ASP A 245      25.896   7.491  -8.822  1.00 56.60           C  
ANISOU 1911  CB  ASP A 245     4740  10881   5886    800   -289   -140       C  
ATOM   1912  CG  ASP A 245      27.352   7.093  -8.866  1.00 63.69           C  
ANISOU 1912  CG  ASP A 245     5316  12421   6461   1136   -394   -491       C  
ATOM   1913  OD1 ASP A 245      27.689   6.155  -9.618  1.00 66.46           O  
ANISOU 1913  OD1 ASP A 245     5701  12972   6578   1429   -446   -589       O  
ATOM   1914  OD2 ASP A 245      28.164   7.730  -8.165  1.00 68.00           O  
ANISOU 1914  OD2 ASP A 245     5554  13307   6975   1110   -427   -696       O  
ATOM   1915  N   HIS A 246      23.416   9.385  -9.455  1.00 48.28           N  
ANISOU 1915  N   HIS A 246     3866   8968   5511   -152    -47    511       N  
ATOM   1916  CA  HIS A 246      21.981   9.635  -9.475  1.00 46.88           C  
ANISOU 1916  CA  HIS A 246     3944   8302   5568   -334      9    758       C  
ATOM   1917  C   HIS A 246      21.501  10.014 -10.869  1.00 45.61           C  
ANISOU 1917  C   HIS A 246     3706   8150   5473   -608     77    961       C  
ATOM   1918  O   HIS A 246      20.383   9.654 -11.256  1.00 45.84           O  
ANISOU 1918  O   HIS A 246     3942   7903   5574   -625     99   1103       O  
ATOM   1919  CB  HIS A 246      21.635  10.734  -8.471  1.00 47.89           C  
ANISOU 1919  CB  HIS A 246     4066   8203   5928   -527     26    805       C  
ATOM   1920  CG  HIS A 246      21.857  10.336  -7.046  1.00 49.22           C  
ANISOU 1920  CG  HIS A 246     4367   8299   6037   -252    -39    634       C  
ATOM   1921  ND1 HIS A 246      22.102  11.251  -6.046  1.00 50.28           N  
ANISOU 1921  ND1 HIS A 246     4397   8414   6293   -356    -50    564       N  
ATOM   1922  CD2 HIS A 246      21.869   9.119  -6.452  1.00 49.32           C  
ANISOU 1922  CD2 HIS A 246     4647   8236   5856    128    -98    521       C  
ATOM   1923  CE1 HIS A 246      22.255  10.615  -4.897  1.00 50.09           C  
ANISOU 1923  CE1 HIS A 246     4539   8340   6152    -38   -117    414       C  
ATOM   1924  NE2 HIS A 246      22.118   9.320  -5.118  1.00 49.68           N  
ANISOU 1924  NE2 HIS A 246     4740   8237   5900    262   -147    396       N  
ATOM   1925  N   VAL A 247      22.323  10.731 -11.635  1.00 44.29           N  
ANISOU 1925  N   VAL A 247     3247   8324   5259   -837    117    964       N  
ATOM   1926  CA  VAL A 247      21.940  11.091 -12.995  1.00 43.21           C  
ANISOU 1926  CA  VAL A 247     3066   8214   5138  -1080    179   1165       C  
ATOM   1927  C   VAL A 247      21.866   9.848 -13.871  1.00 42.78           C  
ANISOU 1927  C   VAL A 247     3069   8295   4889   -853    157   1125       C  
ATOM   1928  O   VAL A 247      20.964   9.714 -14.707  1.00 40.88           O  
ANISOU 1928  O   VAL A 247     2944   7899   4691   -926    179   1293       O  
ATOM   1929  CB  VAL A 247      22.925  12.131 -13.561  1.00 47.80           C  
ANISOU 1929  CB  VAL A 247     3361   9133   5667  -1420    253   1167       C  
ATOM   1930  CG1 VAL A 247      22.681  12.350 -15.052  1.00 48.68           C  
ANISOU 1930  CG1 VAL A 247     3462   9321   5715  -1624    315   1361       C  
ATOM   1931  CG2 VAL A 247      22.810  13.437 -12.786  1.00 45.92           C  
ANISOU 1931  CG2 VAL A 247     3148   8661   5640  -1696    286   1236       C  
ATOM   1932  N   ASP A 248      22.798   8.912 -13.682  1.00 44.87           N  
ANISOU 1932  N   ASP A 248     3266   8857   4924   -544    100    880       N  
ATOM   1933  CA  ASP A 248      22.860   7.735 -14.543  1.00 47.96           C  
ANISOU 1933  CA  ASP A 248     3726   9393   5104   -308     73    809       C  
ATOM   1934  C   ASP A 248      21.615   6.866 -14.391  1.00 50.83           C  
ANISOU 1934  C   ASP A 248     4481   9306   5527   -175     61    890       C  
ATOM   1935  O   ASP A 248      21.015   6.449 -15.388  1.00 50.62           O  
ANISOU 1935  O   ASP A 248     4525   9242   5467   -226     87    977       O  
ATOM   1936  CB  ASP A 248      24.126   6.932 -14.235  1.00 47.78           C  
ANISOU 1936  CB  ASP A 248     3584   9767   4802     70    -12    498       C  
ATOM   1937  CG  ASP A 248      25.385   7.594 -14.776  1.00 49.08           C  
ANISOU 1937  CG  ASP A 248     3286  10530   4832    -95     24    365       C  
ATOM   1938  OD1 ASP A 248      25.272   8.571 -15.546  1.00 49.52           O  
ANISOU 1938  OD1 ASP A 248     3175  10656   4986   -524    130    545       O  
ATOM   1939  OD2 ASP A 248      26.494   7.137 -14.430  1.00 50.37           O  
ANISOU 1939  OD2 ASP A 248     3262  11110   4765    204    -52     66       O  
ATOM   1940  N   ILE A 249      21.209   6.575 -13.152  1.00 53.02           N  
ANISOU 1940  N   ILE A 249     5016   9257   5871    -29     32    846       N  
ATOM   1941  CA  ILE A 249      20.029   5.738 -12.955  1.00 54.67           C  
ANISOU 1941  CA  ILE A 249     5608   9056   6109     28     54    896       C  
ATOM   1942  C   ILE A 249      18.776   6.414 -13.496  1.00 49.18           C  
ANISOU 1942  C   ILE A 249     4888   8164   5634   -305    123   1110       C  
ATOM   1943  O   ILE A 249      17.803   5.733 -13.836  1.00 49.76           O  
ANISOU 1943  O   ILE A 249     5168   8040   5697   -332    158   1135       O  
ATOM   1944  CB  ILE A 249      19.855   5.375 -11.465  1.00 59.93           C  
ANISOU 1944  CB  ILE A 249     6569   9424   6779    209     31    813       C  
ATOM   1945  CG1 ILE A 249      19.559   6.635 -10.650  1.00 63.09           C  
ANISOU 1945  CG1 ILE A 249     6827   9713   7432    -18     55    908       C  
ATOM   1946  CG2 ILE A 249      21.089   4.651 -10.952  1.00 62.02           C  
ANISOU 1946  CG2 ILE A 249     6889   9898   6776    623    -69    584       C  
ATOM   1947  CD1 ILE A 249      20.054   6.578  -9.219  1.00 65.84           C  
ANISOU 1947  CD1 ILE A 249     7286   9994   7735    195      3    774       C  
ATOM   1948  N   LEU A 250      18.772   7.743 -13.585  1.00 44.67           N  
ANISOU 1948  N   LEU A 250     4083   7647   5242   -552    141   1247       N  
ATOM   1949  CA  LEU A 250      17.655   8.466 -14.178  1.00 42.09           C  
ANISOU 1949  CA  LEU A 250     3734   7171   5087   -795    175   1443       C  
ATOM   1950  C   LEU A 250      17.687   8.459 -15.702  1.00 44.67           C  
ANISOU 1950  C   LEU A 250     3927   7735   5312   -886    186   1535       C  
ATOM   1951  O   LEU A 250      16.747   8.960 -16.325  1.00 47.83           O  
ANISOU 1951  O   LEU A 250     4322   8046   5806  -1031    194   1688       O  
ATOM   1952  CB  LEU A 250      17.635   9.913 -13.672  1.00 39.43           C  
ANISOU 1952  CB  LEU A 250     3285   6742   4955   -987    177   1558       C  
ATOM   1953  CG  LEU A 250      17.167  10.103 -12.227  1.00 37.04           C  
ANISOU 1953  CG  LEU A 250     3121   6152   4802   -941    170   1503       C  
ATOM   1954  CD1 LEU A 250      17.445  11.512 -11.731  1.00 38.28           C  
ANISOU 1954  CD1 LEU A 250     3163   6255   5128  -1111    165   1573       C  
ATOM   1955  CD2 LEU A 250      15.686   9.791 -12.101  1.00 36.64           C  
ANISOU 1955  CD2 LEU A 250     3240   5839   4842   -959    192   1541       C  
ATOM   1956  N   GLY A 251      18.731   7.902 -16.312  1.00 46.06           N  
ANISOU 1956  N   GLY A 251     3989   8236   5276   -776    177   1430       N  
ATOM   1957  CA  GLY A 251      18.863   7.884 -17.749  1.00 48.52           C  
ANISOU 1957  CA  GLY A 251     4162   8814   5461   -862    194   1502       C  
ATOM   1958  C   GLY A 251      17.653   7.308 -18.459  1.00 48.87           C  
ANISOU 1958  C   GLY A 251     4346   8718   5504   -867    196   1558       C  
ATOM   1959  O   GLY A 251      17.093   7.922 -19.373  1.00 51.38           O  
ANISOU 1959  O   GLY A 251     4585   9083   5854  -1027    203   1724       O  
ATOM   1960  N   PRO A 252      17.236   6.103 -18.061  1.00 46.55           N  
ANISOU 1960  N   PRO A 252     4284   8255   5148   -697    191   1407       N  
ATOM   1961  CA  PRO A 252      16.060   5.495 -18.710  1.00 44.41           C  
ANISOU 1961  CA  PRO A 252     4133   7880   4862   -752    209   1410       C  
ATOM   1962  C   PRO A 252      14.821   6.373 -18.671  1.00 40.86           C  
ANISOU 1962  C   PRO A 252     3643   7272   4611   -942    216   1555       C  
ATOM   1963  O   PRO A 252      14.092   6.453 -19.669  1.00 39.09           O  
ANISOU 1963  O   PRO A 252     3343   7151   4360  -1023    207   1617       O  
ATOM   1964  CB  PRO A 252      15.862   4.194 -17.919  1.00 44.24           C  
ANISOU 1964  CB  PRO A 252     4444   7612   4754   -595    229   1218       C  
ATOM   1965  CG  PRO A 252      17.235   3.864 -17.396  1.00 46.56           C  
ANISOU 1965  CG  PRO A 252     4760   8021   4911   -343    185   1098       C  
ATOM   1966  CD  PRO A 252      17.890   5.187 -17.107  1.00 46.96           C  
ANISOU 1966  CD  PRO A 252     4522   8232   5090   -441    169   1210       C  
ATOM   1967  N   LEU A 253      14.550   7.032 -17.541  1.00 38.13           N  
ANISOU 1967  N   LEU A 253     3339   6703   4447   -981    218   1591       N  
ATOM   1968  CA  LEU A 253      13.390   7.911 -17.476  1.00 37.23           C  
ANISOU 1968  CA  LEU A 253     3176   6463   4505  -1104    205   1700       C  
ATOM   1969  C   LEU A 253      13.580   9.129 -18.368  1.00 37.63           C  
ANISOU 1969  C   LEU A 253     3059   6658   4582  -1186    160   1910       C  
ATOM   1970  O   LEU A 253      12.641   9.562 -19.047  1.00 37.89           O  
ANISOU 1970  O   LEU A 253     3046   6715   4634  -1219    122   1998       O  
ATOM   1971  CB  LEU A 253      13.132   8.346 -16.036  1.00 37.36           C  
ANISOU 1971  CB  LEU A 253     3279   6222   4693  -1109    216   1672       C  
ATOM   1972  CG  LEU A 253      12.680   7.249 -15.075  1.00 37.05           C  
ANISOU 1972  CG  LEU A 253     3470   5987   4620  -1070    278   1490       C  
ATOM   1973  CD1 LEU A 253      12.487   7.827 -13.680  1.00 38.30           C  
ANISOU 1973  CD1 LEU A 253     3687   5928   4936  -1077    288   1478       C  
ATOM   1974  CD2 LEU A 253      11.408   6.586 -15.574  1.00 35.85           C  
ANISOU 1974  CD2 LEU A 253     3363   5837   4422  -1172    322   1403       C  
ATOM   1975  N   SER A 254      14.789   9.695 -18.380  1.00 39.86           N  
ANISOU 1975  N   SER A 254     3263   7047   4836  -1223    167   1978       N  
ATOM   1976  CA  SER A 254      15.079  10.805 -19.278  1.00 44.53           C  
ANISOU 1976  CA  SER A 254     3763   7755   5401  -1355    155   2185       C  
ATOM   1977  C   SER A 254      14.851  10.410 -20.731  1.00 46.29           C  
ANISOU 1977  C   SER A 254     3927   8219   5443  -1350    145   2238       C  
ATOM   1978  O   SER A 254      14.319  11.197 -21.523  1.00 42.51           O  
ANISOU 1978  O   SER A 254     3455   7748   4947  -1404    108   2418       O  
ATOM   1979  CB  SER A 254      16.517  11.278 -19.074  1.00 49.16           C  
ANISOU 1979  CB  SER A 254     4254   8487   5938  -1458    200   2188       C  
ATOM   1980  OG  SER A 254      16.898  12.191 -20.087  1.00 55.15           O  
ANISOU 1980  OG  SER A 254     4997   9350   6607  -1612    210   2343       O  
ATOM   1981  N   ALA A 255      15.242   9.189 -21.100  1.00 51.61           N  
ANISOU 1981  N   ALA A 255     4570   9082   5958  -1257    167   2077       N  
ATOM   1982  CA  ALA A 255      15.092   8.751 -22.482  1.00 55.53           C  
ANISOU 1982  CA  ALA A 255     4998   9833   6266  -1248    159   2099       C  
ATOM   1983  C   ALA A 255      13.626   8.599 -22.861  1.00 57.63           C  
ANISOU 1983  C   ALA A 255     5307  10019   6569  -1221    111   2101       C  
ATOM   1984  O   ALA A 255      13.240   8.873 -24.003  1.00 60.05           O  
ANISOU 1984  O   ALA A 255     5552  10501   6764  -1235     74   2208       O  
ATOM   1985  CB  ALA A 255      15.832   7.433 -22.697  1.00 55.52           C  
ANISOU 1985  CB  ALA A 255     4985  10026   6085  -1121    184   1887       C  
ATOM   1986  N   GLN A 256      12.792   8.159 -21.918  1.00 55.92           N  
ANISOU 1986  N   GLN A 256     5187   9577   6484  -1188    115   1966       N  
ATOM   1987  CA  GLN A 256      11.387   7.915 -22.211  1.00 53.12           C  
ANISOU 1987  CA  GLN A 256     4821   9220   6142  -1188     85   1895       C  
ATOM   1988  C   GLN A 256      10.566   9.193 -22.301  1.00 50.09           C  
ANISOU 1988  C   GLN A 256     4383   8786   5864  -1175      3   2057       C  
ATOM   1989  O   GLN A 256       9.505   9.183 -22.933  1.00 55.21           O  
ANISOU 1989  O   GLN A 256     4953   9565   6458  -1134    -54   2018       O  
ATOM   1990  CB  GLN A 256      10.793   6.996 -21.143  1.00 55.27           C  
ANISOU 1990  CB  GLN A 256     5223   9291   6486  -1210    146   1672       C  
ATOM   1991  CG  GLN A 256       9.340   6.633 -21.367  1.00 60.04           C  
ANISOU 1991  CG  GLN A 256     5779   9951   7081  -1273    145   1529       C  
ATOM   1992  CD  GLN A 256       8.819   5.662 -20.329  1.00 63.32           C  
ANISOU 1992  CD  GLN A 256     6366  10167   7525  -1373    247   1302       C  
ATOM   1993  OE1 GLN A 256       9.590   5.078 -19.567  1.00 63.18           O  
ANISOU 1993  OE1 GLN A 256     6554   9957   7496  -1349    307   1256       O  
ATOM   1994  NE2 GLN A 256       7.504   5.486 -20.291  1.00 66.09           N  
ANISOU 1994  NE2 GLN A 256     6642  10584   7885  -1485    271   1144       N  
ATOM   1995  N   THR A 257      11.022  10.289 -21.693  1.00 45.26           N  
ANISOU 1995  N   THR A 257     3819   7997   5379  -1191    -12   2215       N  
ATOM   1996  CA  THR A 257      10.251  11.524 -21.667  1.00 46.68           C  
ANISOU 1996  CA  THR A 257     4021   8062   5652  -1133   -102   2358       C  
ATOM   1997  C   THR A 257      10.869  12.638 -22.496  1.00 49.81           C  
ANISOU 1997  C   THR A 257     4486   8477   5962  -1164   -139   2632       C  
ATOM   1998  O   THR A 257      10.276  13.718 -22.593  1.00 53.73           O  
ANISOU 1998  O   THR A 257     5079   8842   6495  -1079   -229   2777       O  
ATOM   1999  CB  THR A 257      10.077  12.019 -20.223  1.00 46.78           C  
ANISOU 1999  CB  THR A 257     4102   7788   5884  -1133    -94   2313       C  
ATOM   2000  OG1 THR A 257      11.363  12.238 -19.629  1.00 43.73           O  
ANISOU 2000  OG1 THR A 257     3773   7296   5546  -1230    -29   2368       O  
ATOM   2001  CG2 THR A 257       9.289  11.008 -19.395  1.00 48.43           C  
ANISOU 2001  CG2 THR A 257     4284   7967   6152  -1133    -44   2054       C  
ATOM   2002  N   GLY A 258      12.037  12.415 -23.091  1.00 49.29           N  
ANISOU 2002  N   GLY A 258     4397   8573   5758  -1280    -68   2697       N  
ATOM   2003  CA  GLY A 258      12.698  13.461 -23.840  1.00 49.22           C  
ANISOU 2003  CA  GLY A 258     4481   8584   5638  -1389    -62   2952       C  
ATOM   2004  C   GLY A 258      13.228  14.600 -23.005  1.00 50.22           C  
ANISOU 2004  C   GLY A 258     4749   8429   5903  -1516    -35   3072       C  
ATOM   2005  O   GLY A 258      13.693  15.596 -23.567  1.00 51.08           O  
ANISOU 2005  O   GLY A 258     5007   8486   5915  -1655    -15   3295       O  
ATOM   2006  N   ILE A 259      13.186  14.488 -21.683  1.00 50.92           N  
ANISOU 2006  N   ILE A 259     4824   8326   6199  -1497    -22   2928       N  
ATOM   2007  CA  ILE A 259      13.612  15.561 -20.793  1.00 52.59           C  
ANISOU 2007  CA  ILE A 259     5163   8261   6557  -1612     -4   3005       C  
ATOM   2008  C   ILE A 259      14.910  15.140 -20.124  1.00 52.52           C  
ANISOU 2008  C   ILE A 259     5040   8355   6559  -1752     98   2850       C  
ATOM   2009  O   ILE A 259      14.941  14.169 -19.357  1.00 48.20           O  
ANISOU 2009  O   ILE A 259     4386   7855   6073  -1656    113   2650       O  
ATOM   2010  CB  ILE A 259      12.534  15.900 -19.752  1.00 50.56           C  
ANISOU 2010  CB  ILE A 259     4975   7723   6512  -1448    -86   2932       C  
ATOM   2011  CG1 ILE A 259      11.241  16.311 -20.460  1.00 52.05           C  
ANISOU 2011  CG1 ILE A 259     5241   7884   6651  -1240   -215   3022       C  
ATOM   2012  CG2 ILE A 259      13.027  17.010 -18.826  1.00 48.72           C  
ANISOU 2012  CG2 ILE A 259     4887   7197   6426  -1570    -68   2994       C  
ATOM   2013  CD1 ILE A 259      10.064  16.481 -19.533  1.00 52.75           C  
ANISOU 2013  CD1 ILE A 259     5322   7810   6910  -1045   -300   2886       C  
ATOM   2014  N   ALA A 260      15.982  15.872 -20.420  1.00 56.71           N  
ANISOU 2014  N   ALA A 260     5637   8906   7006  -1931    153   2870       N  
ATOM   2015  CA  ALA A 260      17.267  15.615 -19.790  1.00 57.56           C  
ANISOU 2015  CA  ALA A 260     5630   9143   7096  -2017    225   2652       C  
ATOM   2016  C   ALA A 260      17.156  15.774 -18.278  1.00 53.45           C  
ANISOU 2016  C   ALA A 260     5124   8396   6788  -1971    211   2540       C  
ATOM   2017  O   ALA A 260      16.310  16.511 -17.765  1.00 53.81           O  
ANISOU 2017  O   ALA A 260     5312   8136   6997  -1952    163   2648       O  
ATOM   2018  CB  ALA A 260      18.325  16.566 -20.348  1.00 62.29           C  
ANISOU 2018  CB  ALA A 260     6297   9800   7571  -2278    307   2689       C  
ATOM   2019  N   VAL A 261      18.027  15.063 -17.559  1.00 49.85           N  
ANISOU 2019  N   VAL A 261     4513   8117   6311  -1938    247   2325       N  
ATOM   2020  CA  VAL A 261      17.995  15.110 -16.101  1.00 47.58           C  
ANISOU 2020  CA  VAL A 261     4223   7659   6195  -1886    235   2211       C  
ATOM   2021  C   VAL A 261      18.220  16.534 -15.611  1.00 47.00           C  
ANISOU 2021  C   VAL A 261     4277   7344   6235  -2074    253   2258       C  
ATOM   2022  O   VAL A 261      17.543  17.004 -14.689  1.00 46.72           O  
ANISOU 2022  O   VAL A 261     4342   7023   6388  -2031    213   2278       O  
ATOM   2023  CB  VAL A 261      19.039  14.145 -15.514  1.00 49.16           C  
ANISOU 2023  CB  VAL A 261     4219   8162   6299  -1812    264   1995       C  
ATOM   2024  CG1 VAL A 261      19.115  14.308 -14.008  1.00 49.88           C  
ANISOU 2024  CG1 VAL A 261     4298   8111   6545  -1779    251   1890       C  
ATOM   2025  CG2 VAL A 261      18.704  12.710 -15.886  1.00 47.82           C  
ANISOU 2025  CG2 VAL A 261     3982   8167   6019  -1611    250   1955       C  
ATOM   2026  N   LEU A 262      19.174  17.241 -16.215  1.00 48.28           N  
ANISOU 2026  N   LEU A 262     4449   7618   6279  -2304    326   2263       N  
ATOM   2027  CA  LEU A 262      19.478  18.595 -15.766  1.00 50.33           C  
ANISOU 2027  CA  LEU A 262     4864   7635   6624  -2531    372   2288       C  
ATOM   2028  C   LEU A 262      18.327  19.550 -16.043  1.00 52.70           C  
ANISOU 2028  C   LEU A 262     5461   7537   7025  -2526    317   2536       C  
ATOM   2029  O   LEU A 262      18.122  20.503 -15.282  1.00 49.87           O  
ANISOU 2029  O   LEU A 262     5271   6868   6810  -2600    310   2557       O  
ATOM   2030  CB  LEU A 262      20.764  19.081 -16.429  1.00 53.57           C  
ANISOU 2030  CB  LEU A 262     5225   8271   6857  -2815    490   2222       C  
ATOM   2031  CG  LEU A 262      22.017  18.527 -15.749  1.00 56.63           C  
ANISOU 2031  CG  LEU A 262     5314   9025   7178  -2843    534   1933       C  
ATOM   2032  CD1 LEU A 262      23.222  18.562 -16.668  1.00 59.03           C  
ANISOU 2032  CD1 LEU A 262     5477   9705   7247  -3051    631   1839       C  
ATOM   2033  CD2 LEU A 262      22.300  19.309 -14.470  1.00 59.71           C  
ANISOU 2033  CD2 LEU A 262     5727   9233   7726  -2961    554   1814       C  
ATOM   2034  N   ASP A 263      17.566  19.316 -17.115  1.00 56.32           N  
ANISOU 2034  N   ASP A 263     5988   8013   7399  -2423    266   2722       N  
ATOM   2035  CA  ASP A 263      16.355  20.095 -17.347  1.00 60.27           C  
ANISOU 2035  CA  ASP A 263     6746   8176   7978  -2337    176   2967       C  
ATOM   2036  C   ASP A 263      15.356  19.882 -16.218  1.00 58.44           C  
ANISOU 2036  C   ASP A 263     6472   7759   7972  -2127     82   2930       C  
ATOM   2037  O   ASP A 263      14.787  20.840 -15.683  1.00 58.40           O  
ANISOU 2037  O   ASP A 263     6674   7409   8106  -2106     23   3027       O  
ATOM   2038  CB  ASP A 263      15.726  19.716 -18.686  1.00 62.61           C  
ANISOU 2038  CB  ASP A 263     7061   8613   8116  -2231    128   3156       C  
ATOM   2039  CG  ASP A 263      16.601  20.077 -19.864  1.00 66.53           C  
ANISOU 2039  CG  ASP A 263     7646   9252   8380  -2446    222   3221       C  
ATOM   2040  OD1 ASP A 263      17.444  20.987 -19.722  1.00 69.37           O  
ANISOU 2040  OD1 ASP A 263     8158   9486   8713  -2699    323   3193       O  
ATOM   2041  OD2 ASP A 263      16.439  19.453 -20.934  1.00 66.93           O  
ANISOU 2041  OD2 ASP A 263     7613   9551   8267  -2379    208   3292       O  
ATOM   2042  N   MET A 264      15.125  18.623 -15.846  1.00 57.36           N  
ANISOU 2042  N   MET A 264     6095   7835   7865  -1968     72   2783       N  
ATOM   2043  CA  MET A 264      14.225  18.350 -14.733  1.00 54.50           C  
ANISOU 2043  CA  MET A 264     5697   7321   7691  -1781     12   2681       C  
ATOM   2044  C   MET A 264      14.759  18.971 -13.451  1.00 52.94           C  
ANISOU 2044  C   MET A 264     5531   6941   7641  -1884     38   2577       C  
ATOM   2045  O   MET A 264      13.990  19.489 -12.634  1.00 53.55           O  
ANISOU 2045  O   MET A 264     5710   6761   7876  -1759    -27   2538       O  
ATOM   2046  CB  MET A 264      14.034  16.844 -14.568  1.00 50.91           C  
ANISOU 2046  CB  MET A 264     5054   7101   7188  -1631     29   2501       C  
ATOM   2047  CG  MET A 264      12.868  16.481 -13.664  1.00 50.10           C  
ANISOU 2047  CG  MET A 264     4956   6866   7215  -1435    -19   2364       C  
ATOM   2048  SD  MET A 264      11.281  16.992 -14.356  1.00 52.92           S  
ANISOU 2048  SD  MET A 264     5383   7139   7587  -1252   -133   2456       S  
ATOM   2049  CE  MET A 264      10.924  15.620 -15.451  1.00 51.37           C  
ANISOU 2049  CE  MET A 264     5044   7269   7205  -1204   -111   2405       C  
ATOM   2050  N   CYS A 265      16.080  18.947 -13.263  1.00 50.92           N  
ANISOU 2050  N   CYS A 265     5203   6846   7298  -2042    120   2433       N  
ATOM   2051  CA  CYS A 265      16.664  19.595 -12.094  1.00 50.06           C  
ANISOU 2051  CA  CYS A 265     5112   6608   7301  -2153    146   2300       C  
ATOM   2052  C   CYS A 265      16.282  21.068 -12.050  1.00 52.80           C  
ANISOU 2052  C   CYS A 265     5738   6574   7750  -2270    120   2445       C  
ATOM   2053  O   CYS A 265      15.811  21.566 -11.021  1.00 54.04           O  
ANISOU 2053  O   CYS A 265     5967   6477   8090  -2218     70   2411       O  
ATOM   2054  CB  CYS A 265      18.181  19.422 -12.105  1.00 50.60           C  
ANISOU 2054  CB  CYS A 265     5022   6977   7226  -2333    243   2129       C  
ATOM   2055  SG  CYS A 265      18.721  17.765 -11.626  1.00 50.74           S  
ANISOU 2055  SG  CYS A 265     4742   7383   7154  -2141    240   1926       S  
ATOM   2056  N   ALA A 266      16.452  21.773 -13.172  1.00 56.31           N  
ANISOU 2056  N   ALA A 266     6378   6953   8066  -2414    151   2614       N  
ATOM   2057  CA  ALA A 266      16.061  23.176 -13.241  1.00 59.05           C  
ANISOU 2057  CA  ALA A 266     7091   6880   8467  -2498    120   2778       C  
ATOM   2058  C   ALA A 266      14.589  23.369 -12.904  1.00 57.77           C  
ANISOU 2058  C   ALA A 266     7047   6427   8476  -2210    -42   2921       C  
ATOM   2059  O   ALA A 266      14.206  24.420 -12.376  1.00 60.23           O  
ANISOU 2059  O   ALA A 266     7628   6354   8902  -2185   -104   2963       O  
ATOM   2060  CB  ALA A 266      16.355  23.733 -14.635  1.00 61.70           C  
ANISOU 2060  CB  ALA A 266     7658   7195   8591  -2652    179   2962       C  
ATOM   2061  N   SER A 267      13.747  22.381 -13.207  1.00 53.97           N  
ANISOU 2061  N   SER A 267     6382   6148   7978  -1931   -109   2900       N  
ATOM   2062  CA  SER A 267      12.341  22.473 -12.829  1.00 51.61           C  
ANISOU 2062  CA  SER A 267     6130   5699   7781  -1569   -247   2849       C  
ATOM   2063  C   SER A 267      12.176  22.320 -11.323  1.00 48.92           C  
ANISOU 2063  C   SER A 267     5666   5297   7625  -1495   -248   2613       C  
ATOM   2064  O   SER A 267      11.450  23.093 -10.685  1.00 47.23           O  
ANISOU 2064  O   SER A 267     5598   4818   7528  -1326   -339   2570       O  
ATOM   2065  CB  SER A 267      11.529  21.414 -13.576  1.00 50.93           C  
ANISOU 2065  CB  SER A 267     5850   5905   7595  -1351   -291   2830       C  
ATOM   2066  OG  SER A 267      11.508  21.684 -14.968  1.00 56.50           O  
ANISOU 2066  OG  SER A 267     6698   6649   8119  -1361   -318   3052       O  
ATOM   2067  N   LEU A 268      12.857  21.333 -10.735  1.00 47.13           N  
ANISOU 2067  N   LEU A 268     5191   5316   7402  -1593   -156   2452       N  
ATOM   2068  CA  LEU A 268      12.755  21.117  -9.295  1.00 44.72           C  
ANISOU 2068  CA  LEU A 268     4790   4969   7233  -1522   -150   2236       C  
ATOM   2069  C   LEU A 268      13.298  22.310  -8.525  1.00 47.68           C  
ANISOU 2069  C   LEU A 268     5324   5071   7722  -1672   -149   2212       C  
ATOM   2070  O   LEU A 268      12.720  22.722  -7.514  1.00 49.07           O  
ANISOU 2070  O   LEU A 268     5547   5065   8034  -1535   -203   2092       O  
ATOM   2071  CB  LEU A 268      13.502  19.842  -8.906  1.00 42.57           C  
ANISOU 2071  CB  LEU A 268     4293   4995   6888  -1570    -63   2089       C  
ATOM   2072  CG  LEU A 268      13.605  19.541  -7.411  1.00 39.13           C  
ANISOU 2072  CG  LEU A 268     3789   4540   6540  -1508    -47   1875       C  
ATOM   2073  CD1 LEU A 268      12.217  19.462  -6.804  1.00 39.49           C  
ANISOU 2073  CD1 LEU A 268     3859   4468   6676  -1291    -98   1792       C  
ATOM   2074  CD2 LEU A 268      14.385  18.252  -7.172  1.00 37.43           C  
ANISOU 2074  CD2 LEU A 268     3425   4604   6194  -1497     18   1752       C  
ATOM   2075  N   LYS A 269      14.416  22.876  -8.989  1.00 51.58           N  
ANISOU 2075  N   LYS A 269     5898   5552   8149  -1981    -77   2304       N  
ATOM   2076  CA  LYS A 269      14.947  24.095  -8.389  1.00 58.46           C  
ANISOU 2076  CA  LYS A 269     6964   6141   9108  -2196    -59   2281       C  
ATOM   2077  C   LYS A 269      13.862  25.155  -8.250  1.00 63.66           C  
ANISOU 2077  C   LYS A 269     7944   6374   9871  -1993   -180   2358       C  
ATOM   2078  O   LYS A 269      13.678  25.736  -7.174  1.00 65.66           O  
ANISOU 2078  O   LYS A 269     8271   6413  10264  -1940   -218   2219       O  
ATOM   2079  CB  LYS A 269      16.112  24.616  -9.233  1.00 61.57           C  
ANISOU 2079  CB  LYS A 269     7462   6602   9331  -2551     61   2345       C  
ATOM   2080  CG  LYS A 269      16.593  26.009  -8.862  1.00 66.08           C  
ANISOU 2080  CG  LYS A 269     8332   6843   9933  -2800    114   2309       C  
ATOM   2081  CD  LYS A 269      17.906  26.332  -9.560  1.00 70.76           C  
ANISOU 2081  CD  LYS A 269     8934   7617  10334  -3158    296   2256       C  
ATOM   2082  CE  LYS A 269      18.320  27.777  -9.336  1.00 79.04           C  
ANISOU 2082  CE  LYS A 269    10326   8296  11410  -3431    381   2238       C  
ATOM   2083  NZ  LYS A 269      17.331  28.750  -9.890  1.00 83.02           N  
ANISOU 2083  NZ  LYS A 269    11333   8294  11917  -3301    296   2492       N  
ATOM   2084  N   GLU A 270      13.125  25.414  -9.333  1.00 66.80           N  
ANISOU 2084  N   GLU A 270     8537   6663  10181  -1837   -256   2562       N  
ATOM   2085  CA  GLU A 270      12.045  26.393  -9.280  1.00 72.25           C  
ANISOU 2085  CA  GLU A 270     9544   6979  10928  -1550   -404   2620       C  
ATOM   2086  C   GLU A 270      11.025  26.040  -8.204  1.00 67.76           C  
ANISOU 2086  C   GLU A 270     8779   6466  10499  -1209   -492   2390       C  
ATOM   2087  O   GLU A 270      10.575  26.915  -7.455  1.00 72.15           O  
ANISOU 2087  O   GLU A 270     9522   6726  11164  -1064   -575   2305       O  
ATOM   2088  CB  GLU A 270      11.365  26.493 -10.646  1.00 80.35           C  
ANISOU 2088  CB  GLU A 270    10746   7989  11793  -1357   -491   2846       C  
ATOM   2089  CG  GLU A 270      11.986  27.519 -11.572  1.00 90.09           C  
ANISOU 2089  CG  GLU A 270    12426   8917  12886  -1609   -456   3110       C  
ATOM   2090  CD  GLU A 270      11.376  28.895 -11.396  1.00 99.27           C  
ANISOU 2090  CD  GLU A 270    14101   9543  14073  -1410   -591   3187       C  
ATOM   2091  OE1 GLU A 270      10.300  29.146 -11.980  1.00102.91           O  
ANISOU 2091  OE1 GLU A 270    14742   9912  14448   -986   -762   3278       O  
ATOM   2092  OE2 GLU A 270      11.963  29.720 -10.664  1.00102.65           O  
ANISOU 2092  OE2 GLU A 270    14757   9653  14592  -1654   -536   3133       O  
ATOM   2093  N   LEU A 271      10.652  24.760  -8.109  1.00 58.60           N  
ANISOU 2093  N   LEU A 271     7265   5681   9320  -1096   -463   2275       N  
ATOM   2094  CA  LEU A 271       9.618  24.360  -7.158  1.00 54.75           C  
ANISOU 2094  CA  LEU A 271     6593   5285   8923   -822   -517   2053       C  
ATOM   2095  C   LEU A 271      10.048  24.629  -5.719  1.00 56.53           C  
ANISOU 2095  C   LEU A 271     6792   5398   9287   -909   -476   1865       C  
ATOM   2096  O   LEU A 271       9.227  25.027  -4.885  1.00 58.78           O  
ANISOU 2096  O   LEU A 271     7088   5579   9665   -687   -551   1711       O  
ATOM   2097  CB  LEU A 271       9.272  22.883  -7.349  1.00 49.48           C  
ANISOU 2097  CB  LEU A 271     5611   5013   8176   -784   -454   1969       C  
ATOM   2098  CG  LEU A 271       8.359  22.546  -8.529  1.00 47.76           C  
ANISOU 2098  CG  LEU A 271     5348   4964   7835   -596   -525   2053       C  
ATOM   2099  CD1 LEU A 271       8.326  21.050  -8.784  1.00 42.49           C  
ANISOU 2099  CD1 LEU A 271     4418   4653   7074   -670   -426   1978       C  
ATOM   2100  CD2 LEU A 271       6.950  23.064  -8.291  1.00 49.19           C  
ANISOU 2100  CD2 LEU A 271     5530   5113   8048   -243   -666   1930       C  
ATOM   2101  N   LEU A 272      11.328  24.414  -5.402  1.00 56.94           N  
ANISOU 2101  N   LEU A 272     6784   5513   9336  -1212   -364   1848       N  
ATOM   2102  CA  LEU A 272      11.798  24.682  -4.046  1.00 59.57           C  
ANISOU 2102  CA  LEU A 272     7081   5773   9778  -1290   -334   1654       C  
ATOM   2103  C   LEU A 272      11.795  26.177  -3.749  1.00 65.33           C  
ANISOU 2103  C   LEU A 272     8122   6090  10610  -1322   -402   1665       C  
ATOM   2104  O   LEU A 272      11.365  26.603  -2.672  1.00 65.52           O  
ANISOU 2104  O   LEU A 272     8168   5980  10746  -1183   -451   1490       O  
ATOM   2105  CB  LEU A 272      13.201  24.107  -3.850  1.00 56.44           C  
ANISOU 2105  CB  LEU A 272     6522   5605   9317  -1573   -217   1602       C  
ATOM   2106  CG  LEU A 272      13.382  22.632  -4.205  1.00 51.49           C  
ANISOU 2106  CG  LEU A 272     5658   5346   8558  -1534   -156   1594       C  
ATOM   2107  CD1 LEU A 272      14.859  22.278  -4.258  1.00 50.64           C  
ANISOU 2107  CD1 LEU A 272     5418   5472   8351  -1777    -70   1551       C  
ATOM   2108  CD2 LEU A 272      12.653  21.736  -3.218  1.00 48.47           C  
ANISOU 2108  CD2 LEU A 272     5149   5078   8190  -1316   -154   1421       C  
ATOM   2109  N   GLN A 273      12.269  26.987  -4.698  1.00 70.70           N  
ANISOU 2109  N   GLN A 273     9082   6548  11233  -1512   -397   1867       N  
ATOM   2110  CA  GLN A 273      12.334  28.428  -4.487  1.00 76.39           C  
ANISOU 2110  CA  GLN A 273    10198   6805  12020  -1583   -448   1894       C  
ATOM   2111  C   GLN A 273      10.945  29.055  -4.455  1.00 77.97           C  
ANISOU 2111  C   GLN A 273    10617   6743  12265  -1139   -623   1895       C  
ATOM   2112  O   GLN A 273      10.692  29.971  -3.662  1.00 81.01           O  
ANISOU 2112  O   GLN A 273    11215   6812  12752  -1040   -694   1776       O  
ATOM   2113  CB  GLN A 273      13.179  29.073  -5.584  1.00 79.84           C  
ANISOU 2113  CB  GLN A 273    10936   7062  12337  -1940   -374   2127       C  
ATOM   2114  CG  GLN A 273      14.672  28.867  -5.419  1.00 79.98           C  
ANISOU 2114  CG  GLN A 273    10777   7298  12314  -2430   -202   2053       C  
ATOM   2115  CD  GLN A 273      15.451  29.216  -6.673  1.00 83.39           C  
ANISOU 2115  CD  GLN A 273    11405   7742  12538  -2754    -74   2229       C  
ATOM   2116  OE1 GLN A 273      14.874  29.571  -7.700  1.00 84.96           O  
ANISOU 2116  OE1 GLN A 273    11901   7743  12636  -2624   -127   2459       O  
ATOM   2117  NE2 GLN A 273      16.772  29.114  -6.593  1.00 85.06           N  
ANISOU 2117  NE2 GLN A 273    11428   8241  12649  -3118    111   2067       N  
ATOM   2118  N   ASN A 274      10.037  28.583  -5.309  1.00 75.65           N  
ANISOU 2118  N   ASN A 274    10261   6604  11880   -849   -703   1998       N  
ATOM   2119  CA  ASN A 274       8.733  29.207  -5.469  1.00 76.15           C  
ANISOU 2119  CA  ASN A 274    10516   6484  11934   -387   -890   1988       C  
ATOM   2120  C   ASN A 274       7.578  28.365  -4.947  1.00 74.79           C  
ANISOU 2120  C   ASN A 274     9949   6680  11789    -43   -945   1765       C  
ATOM   2121  O   ASN A 274       6.475  28.898  -4.782  1.00 76.74           O  
ANISOU 2121  O   ASN A 274    10270   6848  12038    366  -1103   1658       O  
ATOM   2122  CB  ASN A 274       8.487  29.532  -6.951  1.00 78.28           C  
ANISOU 2122  CB  ASN A 274    11071   6641  12031   -282   -967   2265       C  
ATOM   2123  CG  ASN A 274       9.566  30.422  -7.540  1.00 82.40           C  
ANISOU 2123  CG  ASN A 274    12047   6777  12483   -664   -890   2499       C  
ATOM   2124  OD1 ASN A 274      10.108  30.137  -8.607  1.00 82.48           O  
ANISOU 2124  OD1 ASN A 274    12098   6889  12350   -889   -810   2713       O  
ATOM   2125  ND2 ASN A 274       9.884  31.505  -6.840  1.00 86.31           N  
ANISOU 2125  ND2 ASN A 274    12892   6836  13064   -769   -900   2445       N  
ATOM   2126  N   GLY A 275       7.792  27.082  -4.683  1.00 75.80           N  
ANISOU 2126  N   GLY A 275     8512   6685  13602     77   -533   2047       N  
ATOM   2127  CA  GLY A 275       6.732  26.236  -4.185  1.00 75.71           C  
ANISOU 2127  CA  GLY A 275     8560   7133  13075    227   -662   1738       C  
ATOM   2128  C   GLY A 275       5.753  25.833  -5.272  1.00 78.91           C  
ANISOU 2128  C   GLY A 275     9170   7783  13028    397   -575   1964       C  
ATOM   2129  O   GLY A 275       5.946  26.085  -6.465  1.00 79.45           O  
ANISOU 2129  O   GLY A 275     9387   7733  13067    440   -411   2397       O  
ATOM   2130  N   MET A 276       4.672  25.186  -4.834  1.00 82.02           N  
ANISOU 2130  N   MET A 276     9564   8540  13059    513   -678   1636       N  
ATOM   2131  CA  MET A 276       3.627  24.737  -5.743  1.00 85.18           C  
ANISOU 2131  CA  MET A 276    10082   9218  13064    697   -656   1693       C  
ATOM   2132  C   MET A 276       2.543  25.782  -5.957  1.00 86.81           C  
ANISOU 2132  C   MET A 276    10334   9276  13373    968   -897   1596       C  
ATOM   2133  O   MET A 276       1.787  25.681  -6.930  1.00 85.45           O  
ANISOU 2133  O   MET A 276    10275   9261  12932   1193   -930   1692       O  
ATOM   2134  CB  MET A 276       2.985  23.453  -5.212  1.00 85.40           C  
ANISOU 2134  CB  MET A 276    10040   9686  12721    653   -601   1357       C  
ATOM   2135  CG  MET A 276       3.991  22.412  -4.767  1.00 85.19           C  
ANISOU 2135  CG  MET A 276     9994   9776  12597    431   -415   1393       C  
ATOM   2136  SD  MET A 276       3.652  20.778  -5.441  1.00 84.46           S  
ANISOU 2136  SD  MET A 276     9955  10092  12044    394   -202   1405       S  
ATOM   2137  CE  MET A 276       5.076  19.881  -4.833  1.00 83.07           C  
ANISOU 2137  CE  MET A 276     9784   9913  11864    184    -51   1487       C  
ATOM   2138  N   ASN A 277       2.447  26.773  -5.074  1.00 89.71           N  
ANISOU 2138  N   ASN A 277    10609   9356  14119    995  -1102   1365       N  
ATOM   2139  CA  ASN A 277       1.490  27.865  -5.229  1.00 93.58           C  
ANISOU 2139  CA  ASN A 277    11141   9644  14772   1279  -1365   1254       C  
ATOM   2140  C   ASN A 277       0.054  27.349  -5.251  1.00 88.94           C  
ANISOU 2140  C   ASN A 277    10483   9482  13827   1491  -1483    878       C  
ATOM   2141  O   ASN A 277      -0.810  27.912  -5.925  1.00 93.59           O  
ANISOU 2141  O   ASN A 277    11152  10033  14376   1802  -1674    872       O  
ATOM   2142  CB  ASN A 277       1.791  28.673  -6.495  1.00101.70           C  
ANISOU 2142  CB  ASN A 277    12421  10304  15918   1424  -1328   1794       C  
ATOM   2143  CG  ASN A 277       1.723  30.174  -6.266  1.00108.89           C  
ANISOU 2143  CG  ASN A 277    13375  10652  17348   1555  -1547   1806       C  
ATOM   2144  OD1 ASN A 277       1.521  30.639  -5.144  1.00109.49           O  
ANISOU 2144  OD1 ASN A 277    13256  10623  17722   1534  -1755   1368       O  
ATOM   2145  ND2 ASN A 277       1.908  30.941  -7.334  1.00114.08           N  
ANISOU 2145  ND2 ASN A 277    14309  10928  18107   1710  -1491   2315       N  
ATOM   2146  N   GLY A 278      -0.211  26.269  -4.516  1.00 80.97           N  
ANISOU 2146  N   GLY A 278     9323   8867  12576   1335  -1361    552       N  
ATOM   2147  CA  GLY A 278      -1.548  25.734  -4.394  1.00 77.94           C  
ANISOU 2147  CA  GLY A 278     8797   8870  11946   1461  -1405    130       C  
ATOM   2148  C   GLY A 278      -1.908  24.639  -5.374  1.00 75.52           C  
ANISOU 2148  C   GLY A 278     8512   8900  11282   1474  -1259    205       C  
ATOM   2149  O   GLY A 278      -3.005  24.074  -5.269  1.00 72.18           O  
ANISOU 2149  O   GLY A 278     7910   8801  10713   1532  -1260   -200       O  
ATOM   2150  N   ARG A 279      -1.030  24.320  -6.320  1.00 77.50           N  
ANISOU 2150  N   ARG A 279     8943   9089  11413   1424  -1125    665       N  
ATOM   2151  CA  ARG A 279      -1.305  23.266  -7.279  1.00 77.58           C  
ANISOU 2151  CA  ARG A 279     8969   9427  11081   1466  -1014    699       C  
ATOM   2152  C   ARG A 279      -0.881  21.911  -6.718  1.00 68.92           C  
ANISOU 2152  C   ARG A 279     7792   8545   9851   1142   -733    608       C  
ATOM   2153  O   ARG A 279      -0.446  21.786  -5.570  1.00 68.75           O  
ANISOU 2153  O   ARG A 279     7728   8449   9944    927   -637    519       O  
ATOM   2154  CB  ARG A 279      -0.596  23.537  -8.603  1.00 83.57           C  
ANISOU 2154  CB  ARG A 279     9978  10062  11714   1614   -983   1226       C  
ATOM   2155  CG  ARG A 279      -1.092  24.771  -9.320  1.00 91.04           C  
ANISOU 2155  CG  ARG A 279    11089  10791  12711   2000  -1240   1380       C  
ATOM   2156  CD  ARG A 279      -0.912  24.644 -10.820  1.00 96.85           C  
ANISOU 2156  CD  ARG A 279    12075  11626  13097   2267  -1206   1770       C  
ATOM   2157  NE  ARG A 279       0.162  25.490 -11.328  1.00102.91           N  
ANISOU 2157  NE  ARG A 279    13126  11985  13989   2258  -1057   2393       N  
ATOM   2158  CZ  ARG A 279       0.496  25.578 -12.611  1.00108.51           C  
ANISOU 2158  CZ  ARG A 279    14127  12712  14389   2497   -955   2854       C  
ATOM   2159  NH1 ARG A 279      -0.162  24.867 -13.517  1.00109.12           N  
ANISOU 2159  NH1 ARG A 279    14244  13224  13991   2805  -1056   2714       N  
ATOM   2160  NH2 ARG A 279       1.486  26.375 -12.988  1.00112.82           N  
ANISOU 2160  NH2 ARG A 279    14915  12844  15109   2434   -737   3434       N  
ATOM   2161  N   THR A 280      -1.002  20.883  -7.553  1.00 59.17           N  
ANISOU 2161  N   THR A 280     6557   7568   8357   1147   -621    622       N  
ATOM   2162  CA  THR A 280      -0.670  19.523  -7.166  1.00 48.06           C  
ANISOU 2162  CA  THR A 280     5100   6327   6832    873   -361    542       C  
ATOM   2163  C   THR A 280       0.111  18.863  -8.290  1.00 45.24           C  
ANISOU 2163  C   THR A 280     4868   6051   6272    888   -254    860       C  
ATOM   2164  O   THR A 280       0.067  19.290  -9.446  1.00 44.92           O  
ANISOU 2164  O   THR A 280     4924   6044   6098   1145   -368   1052       O  
ATOM   2165  CB  THR A 280      -1.927  18.699  -6.855  1.00 44.38           C  
ANISOU 2165  CB  THR A 280     4411   6128   6323    827   -299     39       C  
ATOM   2166  OG1 THR A 280      -2.702  18.535  -8.049  1.00 45.62           O  
ANISOU 2166  OG1 THR A 280     4481   6496   6357   1076   -447   -123       O  
ATOM   2167  CG2 THR A 280      -2.772  19.392  -5.805  1.00 42.59           C  
ANISOU 2167  CG2 THR A 280     4038   5873   6273    845   -379   -306       C  
ATOM   2168  N   ILE A 281       0.838  17.812  -7.930  1.00 44.28           N  
ANISOU 2168  N   ILE A 281     4763   5965   6095    645    -33    914       N  
ATOM   2169  CA  ILE A 281       1.515  16.951  -8.889  1.00 43.87           C  
ANISOU 2169  CA  ILE A 281     4783   6039   5847    644     89   1111       C  
ATOM   2170  C   ILE A 281       1.168  15.522  -8.506  1.00 43.16           C  
ANISOU 2170  C   ILE A 281     4599   6100   5699    461    253    814       C  
ATOM   2171  O   ILE A 281       1.476  15.085  -7.390  1.00 42.49           O  
ANISOU 2171  O   ILE A 281     4539   5911   5694    243    393    773       O  
ATOM   2172  CB  ILE A 281       3.036  17.169  -8.901  1.00 42.78           C  
ANISOU 2172  CB  ILE A 281     4770   5715   5768    538    200   1529       C  
ATOM   2173  CG1 ILE A 281       3.353  18.599  -9.347  1.00 41.34           C  
ANISOU 2173  CG1 ILE A 281     4680   5314   5715    685    100   1845       C  
ATOM   2174  CG2 ILE A 281       3.708  16.158  -9.819  1.00 45.36           C  
ANISOU 2174  CG2 ILE A 281     5138   6215   5881    540    347   1667       C  
ATOM   2175  CD1 ILE A 281       4.822  18.952  -9.301  1.00 41.34           C  
ANISOU 2175  CD1 ILE A 281     4729   5088   5892    539    242   2208       C  
ATOM   2176  N   LEU A 282       0.503  14.809  -9.410  1.00 44.50           N  
ANISOU 2176  N   LEU A 282     4671   6499   5738    571    231    591       N  
ATOM   2177  CA  LEU A 282       0.036  13.454  -9.139  1.00 45.36           C  
ANISOU 2177  CA  LEU A 282     4660   6698   5877    385    400    264       C  
ATOM   2178  C   LEU A 282      -0.786  13.412  -7.851  1.00 46.92           C  
ANISOU 2178  C   LEU A 282     4752   6817   6258    188    518    -19       C  
ATOM   2179  O   LEU A 282      -0.565  12.582  -6.966  1.00 47.99           O  
ANISOU 2179  O   LEU A 282     4949   6847   6437    -56    762    -32       O  
ATOM   2180  CB  LEU A 282       1.212  12.481  -9.073  1.00 45.39           C  
ANISOU 2180  CB  LEU A 282     4801   6627   5817    226    587    491       C  
ATOM   2181  CG  LEU A 282       1.954  12.250 -10.391  1.00 45.83           C  
ANISOU 2181  CG  LEU A 282     4915   6824   5673    406    538    689       C  
ATOM   2182  CD1 LEU A 282       3.211  11.422 -10.162  1.00 46.65           C  
ANISOU 2182  CD1 LEU A 282     5135   6832   5757    257    705    899       C  
ATOM   2183  CD2 LEU A 282       1.043  11.579 -11.411  1.00 44.13           C  
ANISOU 2183  CD2 LEU A 282     4539   6864   5365    571    447    318       C  
ATOM   2184  N   GLY A 283      -1.742  14.335  -7.750  1.00 47.67           N  
ANISOU 2184  N   GLY A 283     4708   6965   6440    327    352   -239       N  
ATOM   2185  CA  GLY A 283      -2.655  14.387  -6.627  1.00 48.28           C  
ANISOU 2185  CA  GLY A 283     4639   7029   6677    179    474   -563       C  
ATOM   2186  C   GLY A 283      -2.064  14.858  -5.318  1.00 48.40           C  
ANISOU 2186  C   GLY A 283     4821   6860   6708     56    568   -365       C  
ATOM   2187  O   GLY A 283      -2.791  14.922  -4.319  1.00 52.39           O  
ANISOU 2187  O   GLY A 283     5233   7382   7291    -43    701   -621       O  
ATOM   2188  N   SER A 284      -0.781  15.200  -5.284  1.00 46.20           N  
ANISOU 2188  N   SER A 284     4761   6429   6364     77    504     39       N  
ATOM   2189  CA  SER A 284      -0.104  15.594  -4.059  1.00 44.20           C  
ANISOU 2189  CA  SER A 284     4649   6017   6128      1    539    171       C  
ATOM   2190  C   SER A 284       0.274  17.066  -4.111  1.00 42.16           C  
ANISOU 2190  C   SER A 284     4400   5617   6000    171    265    311       C  
ATOM   2191  O   SER A 284       0.649  17.584  -5.168  1.00 41.71           O  
ANISOU 2191  O   SER A 284     4366   5512   5970    302    122    535       O  
ATOM   2192  CB  SER A 284       1.155  14.752  -3.835  1.00 41.81           C  
ANISOU 2192  CB  SER A 284     4547   5620   5720   -115    672    448       C  
ATOM   2193  OG  SER A 284       1.917  15.266  -2.758  1.00 42.45           O  
ANISOU 2193  OG  SER A 284     4748   5566   5816   -108    614    545       O  
ATOM   2194  N   ALA A 285       0.185  17.732  -2.959  1.00 42.02           N  
ANISOU 2194  N   ALA A 285     4382   5520   6064    177    212    182       N  
ATOM   2195  CA  ALA A 285       0.598  19.122  -2.835  1.00 43.10           C  
ANISOU 2195  CA  ALA A 285     4516   5454   6406    313    -47    268       C  
ATOM   2196  C   ALA A 285       2.031  19.274  -2.341  1.00 47.16           C  
ANISOU 2196  C   ALA A 285     5145   5778   6997    248    -76    500       C  
ATOM   2197  O   ALA A 285       2.561  20.389  -2.365  1.00 49.47           O  
ANISOU 2197  O   ALA A 285     5412   5841   7545    319   -268    596       O  
ATOM   2198  CB  ALA A 285      -0.345  19.871  -1.889  1.00 39.54           C  
ANISOU 2198  CB  ALA A 285     3948   5031   6044    402   -146    -96       C  
ATOM   2199  N   LEU A 286       2.658  18.187  -1.897  1.00 48.90           N  
ANISOU 2199  N   LEU A 286     5477   6063   7040    128     99    564       N  
ATOM   2200  CA  LEU A 286       4.039  18.180  -1.447  1.00 50.84           C  
ANISOU 2200  CA  LEU A 286     5799   6170   7347    103     45    719       C  
ATOM   2201  C   LEU A 286       4.905  17.401  -2.432  1.00 47.54           C  
ANISOU 2201  C   LEU A 286     5426   5761   6876     28    158   1004       C  
ATOM   2202  O   LEU A 286       4.403  16.643  -3.267  1.00 49.46           O  
ANISOU 2202  O   LEU A 286     5680   6144   6968     -5    297   1048       O  
ATOM   2203  CB  LEU A 286       4.157  17.551  -0.055  1.00 56.21           C  
ANISOU 2203  CB  LEU A 286     6614   6928   7816    110    114    549       C  
ATOM   2204  CG  LEU A 286       3.222  18.063   1.043  1.00 61.73           C  
ANISOU 2204  CG  LEU A 286     7296   7706   8454    198     83    233       C  
ATOM   2205  CD1 LEU A 286       3.044  16.986   2.107  1.00 64.84           C  
ANISOU 2205  CD1 LEU A 286     7906   8245   8487    189    321    158       C  
ATOM   2206  CD2 LEU A 286       3.751  19.347   1.664  1.00 62.40           C  
ANISOU 2206  CD2 LEU A 286     7289   7631   8788    333   -226     93       C  
ATOM   2207  N   LEU A 287       6.215  17.590  -2.325  1.00 43.35           N  
ANISOU 2207  N   LEU A 287     4884   5092   6494     14     87   1141       N  
ATOM   2208  CA  LEU A 287       7.155  16.833  -3.140  1.00 43.52           C  
ANISOU 2208  CA  LEU A 287     4922   5144   6471    -44    203   1370       C  
ATOM   2209  C   LEU A 287       7.373  15.463  -2.510  1.00 40.24           C  
ANISOU 2209  C   LEU A 287     4660   4840   5790    -58    311   1297       C  
ATOM   2210  O   LEU A 287       7.715  15.356  -1.329  1.00 40.92           O  
ANISOU 2210  O   LEU A 287     4832   4894   5822      2    229   1162       O  
ATOM   2211  CB  LEU A 287       8.476  17.590  -3.275  1.00 50.28           C  
ANISOU 2211  CB  LEU A 287     5649   5803   7654    -68    113   1501       C  
ATOM   2212  CG  LEU A 287       8.399  18.906  -4.057  1.00 55.74           C  
ANISOU 2212  CG  LEU A 287     6235   6299   8643    -74     79   1673       C  
ATOM   2213  CD1 LEU A 287       9.701  19.679  -3.937  1.00 58.37           C  
ANISOU 2213  CD1 LEU A 287     6398   6374   9407   -151     30   1738       C  
ATOM   2214  CD2 LEU A 287       8.075  18.654  -5.522  1.00 57.40           C  
ANISOU 2214  CD2 LEU A 287     6503   6626   8680    -52    248   1944       C  
ATOM   2215  N   GLU A 288       7.150  14.414  -3.296  1.00 38.07           N  
ANISOU 2215  N   GLU A 288     4439   4685   5340   -105    482   1376       N  
ATOM   2216  CA  GLU A 288       7.179  13.041  -2.805  1.00 37.72           C  
ANISOU 2216  CA  GLU A 288     4573   4689   5071   -126    620   1326       C  
ATOM   2217  C   GLU A 288       8.532  12.410  -3.102  1.00 34.63           C  
ANISOU 2217  C   GLU A 288     4200   4271   4686    -92    602   1456       C  
ATOM   2218  O   GLU A 288       9.009  12.461  -4.239  1.00 34.30           O  
ANISOU 2218  O   GLU A 288     4031   4277   4724   -108    629   1590       O  
ATOM   2219  CB  GLU A 288       6.059  12.227  -3.455  1.00 45.72           C  
ANISOU 2219  CB  GLU A 288     5591   5812   5968   -204    808   1251       C  
ATOM   2220  CG  GLU A 288       5.942  10.809  -2.942  1.00 55.96           C  
ANISOU 2220  CG  GLU A 288     7086   7077   7101   -262   1004   1206       C  
ATOM   2221  CD  GLU A 288       5.575  10.750  -1.474  1.00 61.12           C  
ANISOU 2221  CD  GLU A 288     7931   7664   7627   -253   1081   1123       C  
ATOM   2222  OE1 GLU A 288       4.757  11.584  -1.030  1.00 63.08           O  
ANISOU 2222  OE1 GLU A 288     8096   7961   7910   -257   1062    985       O  
ATOM   2223  OE2 GLU A 288       6.114   9.876  -0.765  1.00 62.40           O  
ANISOU 2223  OE2 GLU A 288     8347   7735   7628   -205   1158   1196       O  
ATOM   2224  N   ASP A 289       9.137  11.791  -2.083  1.00 33.32           N  
ANISOU 2224  N   ASP A 289     4205   4048   4406    -10    559   1405       N  
ATOM   2225  CA  ASP A 289      10.473  11.226  -2.236  1.00 33.85           C  
ANISOU 2225  CA  ASP A 289     4266   4093   4502     70    488   1463       C  
ATOM   2226  C   ASP A 289      10.554   9.765  -1.797  1.00 35.95           C  
ANISOU 2226  C   ASP A 289     4813   4326   4520    143    582   1462       C  
ATOM   2227  O   ASP A 289      11.644   9.289  -1.460  1.00 37.91           O  
ANISOU 2227  O   ASP A 289     5124   4536   4744    293    455   1450       O  
ATOM   2228  CB  ASP A 289      11.492  12.066  -1.458  1.00 34.66           C  
ANISOU 2228  CB  ASP A 289     4260   4124   4787    184    237   1366       C  
ATOM   2229  CG  ASP A 289      11.415  11.841   0.040  1.00 38.22           C  
ANISOU 2229  CG  ASP A 289     4959   4546   5015    362    114   1215       C  
ATOM   2230  OD1 ASP A 289      10.360  11.386   0.533  1.00 38.89           O  
ANISOU 2230  OD1 ASP A 289     5284   4651   4842    346    276   1220       O  
ATOM   2231  OD2 ASP A 289      12.418  12.121   0.728  1.00 41.47           O  
ANISOU 2231  OD2 ASP A 289     5319   4929   5508    536   -136   1072       O  
ATOM   2232  N   GLU A 290       9.438   9.035  -1.804  1.00 36.30           N  
ANISOU 2232  N   GLU A 290     5017   4360   4417     45    803   1458       N  
ATOM   2233  CA  GLU A 290       9.448   7.613  -1.478  1.00 35.51           C  
ANISOU 2233  CA  GLU A 290     5205   4148   4139     81    949   1491       C  
ATOM   2234  C   GLU A 290       9.166   6.738  -2.698  1.00 33.28           C  
ANISOU 2234  C   GLU A 290     4832   3883   3928    -35   1102   1487       C  
ATOM   2235  O   GLU A 290       8.639   5.630  -2.569  1.00 34.35           O  
ANISOU 2235  O   GLU A 290     5160   3887   4004    -98   1302   1471       O  
ATOM   2236  CB  GLU A 290       8.459   7.309  -0.353  1.00 35.24           C  
ANISOU 2236  CB  GLU A 290     5453   4024   3911     51   1146   1475       C  
ATOM   2237  CG  GLU A 290       8.910   7.867   0.990  1.00 38.09           C  
ANISOU 2237  CG  GLU A 290     5997   4381   4093    266    974   1458       C  
ATOM   2238  CD  GLU A 290       8.344   7.113   2.177  1.00 42.81           C  
ANISOU 2238  CD  GLU A 290     7026   4868   4370    335   1209   1524       C  
ATOM   2239  OE1 GLU A 290       7.325   6.406   2.014  1.00 45.25           O  
ANISOU 2239  OE1 GLU A 290     7423   5090   4681    127   1565   1561       O  
ATOM   2240  OE2 GLU A 290       8.925   7.232   3.279  1.00 41.17           O  
ANISOU 2240  OE2 GLU A 290     7070   4661   3913    612   1046   1528       O  
ATOM   2241  N   PHE A 291       9.513   7.227  -3.886  1.00 32.38           N  
ANISOU 2241  N   PHE A 291     4434   3921   3947    -51   1022   1493       N  
ATOM   2242  CA  PHE A 291       9.554   6.416  -5.096  1.00 34.33           C  
ANISOU 2242  CA  PHE A 291     4584   4242   4219    -70   1099   1457       C  
ATOM   2243  C   PHE A 291      10.963   6.495  -5.668  1.00 34.33           C  
ANISOU 2243  C   PHE A 291     4449   4328   4267     57    971   1525       C  
ATOM   2244  O   PHE A 291      11.411   7.577  -6.065  1.00 32.95           O  
ANISOU 2244  O   PHE A 291     4069   4262   4189     60    900   1604       O  
ATOM   2245  CB  PHE A 291       8.550   6.897  -6.146  1.00 31.77           C  
ANISOU 2245  CB  PHE A 291     4046   4087   3937   -155   1153   1379       C  
ATOM   2246  CG  PHE A 291       7.118   6.705  -5.762  1.00 32.50           C  
ANISOU 2246  CG  PHE A 291     4177   4126   4046   -290   1294   1222       C  
ATOM   2247  CD1 PHE A 291       6.482   5.501  -5.998  1.00 36.60           C  
ANISOU 2247  CD1 PHE A 291     4734   4562   4609   -381   1459   1055       C  
ATOM   2248  CD2 PHE A 291       6.400   7.739  -5.189  1.00 34.95           C  
ANISOU 2248  CD2 PHE A 291     4444   4458   4377   -334   1271   1200       C  
ATOM   2249  CE1 PHE A 291       5.158   5.325  -5.655  1.00 38.63           C  
ANISOU 2249  CE1 PHE A 291     4962   4762   4955   -542   1636    869       C  
ATOM   2250  CE2 PHE A 291       5.078   7.569  -4.843  1.00 36.22           C  
ANISOU 2250  CE2 PHE A 291     4585   4597   4579   -462   1429   1011       C  
ATOM   2251  CZ  PHE A 291       4.455   6.360  -5.078  1.00 38.79           C  
ANISOU 2251  CZ  PHE A 291     4922   4843   4972   -582   1629    845       C  
ATOM   2252  N   THR A 292      11.654   5.359  -5.721  1.00 35.39           N  
ANISOU 2252  N   THR A 292     4686   4394   4365    157    964   1488       N  
ATOM   2253  CA  THR A 292      12.954   5.321  -6.366  1.00 37.43           C  
ANISOU 2253  CA  THR A 292     4763   4771   4686    279    874   1494       C  
ATOM   2254  C   THR A 292      12.787   5.370  -7.883  1.00 38.72           C  
ANISOU 2254  C   THR A 292     4703   5170   4840    251    977   1482       C  
ATOM   2255  O   THR A 292      11.704   5.103  -8.409  1.00 36.07           O  
ANISOU 2255  O   THR A 292     4382   4881   4443    184   1067   1407       O  
ATOM   2256  CB  THR A 292      13.717   4.057  -5.984  1.00 39.15           C  
ANISOU 2256  CB  THR A 292     5162   4849   4864    445    804   1419       C  
ATOM   2257  OG1 THR A 292      13.037   2.911  -6.511  1.00 43.35           O  
ANISOU 2257  OG1 THR A 292     5806   5308   5358    406    936   1331       O  
ATOM   2258  CG2 THR A 292      13.831   3.932  -4.477  1.00 39.85           C  
ANISOU 2258  CG2 THR A 292     5556   4720   4867    551    695   1450       C  
ATOM   2259  N   PRO A 293      13.854   5.704  -8.613  1.00 42.16           N  
ANISOU 2259  N   PRO A 293     4917   5774   5329    324    973   1529       N  
ATOM   2260  CA  PRO A 293      13.772   5.625 -10.079  1.00 41.25           C  
ANISOU 2260  CA  PRO A 293     4641   5921   5111    366   1094   1527       C  
ATOM   2261  C   PRO A 293      13.366   4.247 -10.568  1.00 42.41           C  
ANISOU 2261  C   PRO A 293     4870   6085   5157    442   1106   1314       C  
ATOM   2262  O   PRO A 293      12.714   4.133 -11.614  1.00 39.47           O  
ANISOU 2262  O   PRO A 293     4425   5911   4660    480   1164   1232       O  
ATOM   2263  CB  PRO A 293      15.191   5.999 -10.534  1.00 40.92           C  
ANISOU 2263  CB  PRO A 293     4366   6018   5162    432   1137   1600       C  
ATOM   2264  CG  PRO A 293      15.780   6.764  -9.385  1.00 41.66           C  
ANISOU 2264  CG  PRO A 293     4428   5923   5477    371   1024   1650       C  
ATOM   2265  CD  PRO A 293      15.180   6.152  -8.149  1.00 42.59           C  
ANISOU 2265  CD  PRO A 293     4833   5805   5543    386    876   1552       C  
ATOM   2266  N   PHE A 294      13.728   3.189  -9.835  1.00 44.77           N  
ANISOU 2266  N   PHE A 294     5333   6164   5514    495   1034   1203       N  
ATOM   2267  CA  PHE A 294      13.324   1.843 -10.226  1.00 47.57           C  
ANISOU 2267  CA  PHE A 294     5777   6443   5856    546   1053    985       C  
ATOM   2268  C   PHE A 294      11.838   1.618  -9.976  1.00 42.37           C  
ANISOU 2268  C   PHE A 294     5240   5630   5228    381   1133    901       C  
ATOM   2269  O   PHE A 294      11.149   1.013 -10.805  1.00 41.40           O  
ANISOU 2269  O   PHE A 294     5032   5580   5117    382   1170    675       O  
ATOM   2270  CB  PHE A 294      14.156   0.805  -9.474  1.00 56.81           C  
ANISOU 2270  CB  PHE A 294     7133   7357   7096    675    956    927       C  
ATOM   2271  CG  PHE A 294      15.628   0.883  -9.766  1.00 66.82           C  
ANISOU 2271  CG  PHE A 294     8212   8793   8382    859    860    907       C  
ATOM   2272  CD1 PHE A 294      16.168   0.221 -10.859  1.00 71.38           C  
ANISOU 2272  CD1 PHE A 294     8610   9575   8935   1006    873    722       C  
ATOM   2273  CD2 PHE A 294      16.471   1.616  -8.948  1.00 69.10           C  
ANISOU 2273  CD2 PHE A 294     8464   9054   8737    895    756   1016       C  
ATOM   2274  CE1 PHE A 294      17.524   0.291 -11.130  1.00 72.46           C  
ANISOU 2274  CE1 PHE A 294     8525   9890   9115   1167    823    668       C  
ATOM   2275  CE2 PHE A 294      17.825   1.690  -9.215  1.00 70.48           C  
ANISOU 2275  CE2 PHE A 294     8392   9387   9001   1047    681    932       C  
ATOM   2276  CZ  PHE A 294      18.352   1.027 -10.307  1.00 71.88           C  
ANISOU 2276  CZ  PHE A 294     8383   9773   9156   1172    736    769       C  
ATOM   2277  N   ASP A 295      11.324   2.088  -8.838  1.00 41.04           N  
ANISOU 2277  N   ASP A 295     5240   5264   5091    250   1163   1031       N  
ATOM   2278  CA  ASP A 295       9.896   1.969  -8.565  1.00 40.80           C  
ANISOU 2278  CA  ASP A 295     5270   5110   5121     69   1287    931       C  
ATOM   2279  C   ASP A 295       9.078   2.578  -9.696  1.00 40.96           C  
ANISOU 2279  C   ASP A 295     5028   5427   5108     55   1280    798       C  
ATOM   2280  O   ASP A 295       8.120   1.971 -10.187  1.00 42.23           O  
ANISOU 2280  O   ASP A 295     5106   5585   5356     -2   1332    530       O  
ATOM   2281  CB  ASP A 295       9.567   2.640  -7.233  1.00 38.78           C  
ANISOU 2281  CB  ASP A 295     5194   4693   4846    -31   1326   1100       C  
ATOM   2282  CG  ASP A 295      10.237   1.958  -6.065  1.00 39.05           C  
ANISOU 2282  CG  ASP A 295     5557   4440   4841     50   1320   1217       C  
ATOM   2283  OD1 ASP A 295      10.747   0.832  -6.254  1.00 41.08           O  
ANISOU 2283  OD1 ASP A 295     5925   4551   5134    147   1313   1156       O  
ATOM   2284  OD2 ASP A 295      10.264   2.546  -4.963  1.00 37.07           O  
ANISOU 2284  OD2 ASP A 295     5466   4114   4505     59   1299   1352       O  
ATOM   2285  N   VAL A 296       9.458   3.782 -10.131  1.00 39.01           N  
ANISOU 2285  N   VAL A 296     4649   5422   4750    130   1208    969       N  
ATOM   2286  CA  VAL A 296       8.734   4.464 -11.200  1.00 38.40           C  
ANISOU 2286  CA  VAL A 296     4391   5627   4571    195   1178    899       C  
ATOM   2287  C   VAL A 296       8.783   3.644 -12.484  1.00 40.09           C  
ANISOU 2287  C   VAL A 296     4482   6063   4686    361   1150    665       C  
ATOM   2288  O   VAL A 296       7.763   3.445 -13.154  1.00 41.34           O  
ANISOU 2288  O   VAL A 296     4527   6354   4825    408   1107    390       O  
ATOM   2289  CB  VAL A 296       9.307   5.878 -11.405  1.00 35.61           C  
ANISOU 2289  CB  VAL A 296     3981   5416   4132    254   1148   1199       C  
ATOM   2290  CG1 VAL A 296       8.799   6.486 -12.696  1.00 35.80           C  
ANISOU 2290  CG1 VAL A 296     3891   5744   3968    418   1118   1192       C  
ATOM   2291  CG2 VAL A 296       8.949   6.769 -10.220  1.00 34.20           C  
ANISOU 2291  CG2 VAL A 296     3882   5041   4071    114   1128   1323       C  
ATOM   2292  N   VAL A 297       9.971   3.155 -12.847  1.00 40.99           N  
ANISOU 2292  N   VAL A 297     4587   6243   4743    481   1154    714       N  
ATOM   2293  CA  VAL A 297      10.100   2.344 -14.056  1.00 44.27           C  
ANISOU 2293  CA  VAL A 297     4882   6897   5043    676   1121    456       C  
ATOM   2294  C   VAL A 297       9.247   1.086 -13.946  1.00 48.42           C  
ANISOU 2294  C   VAL A 297     5415   7215   5769    604   1098     67       C  
ATOM   2295  O   VAL A 297       8.623   0.652 -14.923  1.00 48.15           O  
ANISOU 2295  O   VAL A 297     5227   7379   5687    733   1024   -275       O  
ATOM   2296  CB  VAL A 297      11.579   2.001 -14.317  1.00 43.71           C  
ANISOU 2296  CB  VAL A 297     4781   6912   4916    808   1147    547       C  
ATOM   2297  CG1 VAL A 297      11.691   0.853 -15.306  1.00 45.47           C  
ANISOU 2297  CG1 VAL A 297     4906   7300   5072   1005   1098    195       C  
ATOM   2298  CG2 VAL A 297      12.330   3.214 -14.841  1.00 43.21           C  
ANISOU 2298  CG2 VAL A 297     4625   7118   4675    886   1234    864       C  
ATOM   2299  N   ARG A 298       9.213   0.476 -12.758  1.00 51.62           N  
ANISOU 2299  N   ARG A 298     6002   7205   6408    412   1168    101       N  
ATOM   2300  CA  ARG A 298       8.416  -0.730 -12.564  1.00 55.75           C  
ANISOU 2300  CA  ARG A 298     6553   7431   7197    289   1223   -223       C  
ATOM   2301  C   ARG A 298       6.939  -0.452 -12.803  1.00 54.55           C  
ANISOU 2301  C   ARG A 298     6230   7345   7151    170   1242   -486       C  
ATOM   2302  O   ARG A 298       6.274  -1.159 -13.569  1.00 56.86           O  
ANISOU 2302  O   ARG A 298     6332   7690   7582    209   1189   -918       O  
ATOM   2303  CB  ARG A 298       8.623  -1.281 -11.153  1.00 61.78           C  
ANISOU 2303  CB  ARG A 298     7622   7717   8133    119   1352    -33       C  
ATOM   2304  CG  ARG A 298       9.632  -2.413 -11.065  1.00 71.25           C  
ANISOU 2304  CG  ARG A 298     8975   8695   9401    249   1313    -57       C  
ATOM   2305  CD  ARG A 298       9.537  -3.153  -9.732  1.00 80.35           C  
ANISOU 2305  CD  ARG A 298    10494   9315  10719    113   1461     95       C  
ATOM   2306  NE  ARG A 298      10.783  -3.084  -8.972  1.00 85.48           N  
ANISOU 2306  NE  ARG A 298    11382   9878  11217    289   1360    380       N  
ATOM   2307  CZ  ARG A 298      10.995  -2.289  -7.925  1.00 87.94           C  
ANISOU 2307  CZ  ARG A 298    11870  10160  11384    273   1363    676       C  
ATOM   2308  NH1 ARG A 298      10.040  -1.479  -7.481  1.00 87.77           N  
ANISOU 2308  NH1 ARG A 298    11831  10177  11339     75   1488    758       N  
ATOM   2309  NH2 ARG A 298      12.171  -2.310  -7.313  1.00 89.72           N  
ANISOU 2309  NH2 ARG A 298    12265  10329  11495    487   1213    837       N  
ATOM   2310  N   GLN A 299       6.407   0.581 -12.151  1.00 52.27           N  
ANISOU 2310  N   GLN A 299     5976   7060   6825     46   1291   -286       N  
ATOM   2311  CA  GLN A 299       4.973   0.832 -12.219  1.00 50.45           C  
ANISOU 2311  CA  GLN A 299     5563   6865   6740    -71   1312   -571       C  
ATOM   2312  C   GLN A 299       4.552   1.266 -13.616  1.00 50.39           C  
ANISOU 2312  C   GLN A 299     5296   7301   6548    195   1096   -838       C  
ATOM   2313  O   GLN A 299       3.465   0.908 -14.081  1.00 51.19           O  
ANISOU 2313  O   GLN A 299     5164   7463   6823    190   1037  -1300       O  
ATOM   2314  CB  GLN A 299       4.577   1.882 -11.185  1.00 45.96           C  
ANISOU 2314  CB  GLN A 299     5091   6221   6152   -221   1395   -307       C  
ATOM   2315  CG  GLN A 299       3.122   1.790 -10.766  1.00 47.17           C  
ANISOU 2315  CG  GLN A 299     5097   6253   6571   -439   1525   -614       C  
ATOM   2316  CD  GLN A 299       2.738   2.808  -9.711  1.00 46.21           C  
ANISOU 2316  CD  GLN A 299     5065   6079   6412   -560   1612   -388       C  
ATOM   2317  OE1 GLN A 299       1.698   3.453  -9.817  1.00 48.74           O  
ANISOU 2317  OE1 GLN A 299     5178   6544   6798   -578   1572   -602       O  
ATOM   2318  NE2 GLN A 299       3.566   2.945  -8.680  1.00 43.67           N  
ANISOU 2318  NE2 GLN A 299     5040   5565   5989   -608   1701     -6       N  
ATOM   2319  N   CYS A 300       5.397   2.028 -14.308  1.00 51.79           N  
ANISOU 2319  N   CYS A 300     5509   7792   6375    447    986   -570       N  
ATOM   2320  CA  CYS A 300       5.049   2.563 -15.618  1.00 57.76           C  
ANISOU 2320  CA  CYS A 300     6111   8990   6845    767    799   -728       C  
ATOM   2321  C   CYS A 300       5.362   1.604 -16.761  1.00 65.12           C  
ANISOU 2321  C   CYS A 300     6928  10151   7665   1018    694  -1067       C  
ATOM   2322  O   CYS A 300       5.137   1.959 -17.923  1.00 65.88           O  
ANISOU 2322  O   CYS A 300     6928  10661   7441   1359    528  -1215       O  
ATOM   2323  CB  CYS A 300       5.769   3.898 -15.837  1.00 57.27           C  
ANISOU 2323  CB  CYS A 300     6176   9126   6457    915    800   -230       C  
ATOM   2324  SG  CYS A 300       5.377   5.141 -14.574  1.00 56.51           S  
ANISOU 2324  SG  CYS A 300     6186   8784   6503    677    862     99       S  
ATOM   2325  N   SER A 301       5.856   0.400 -16.462  1.00 71.19           N  
ANISOU 2325  N   SER A 301     7722  10660   8668    897    772  -1208       N  
ATOM   2326  CA  SER A 301       6.128  -0.619 -17.473  1.00 79.14           C  
ANISOU 2326  CA  SER A 301     8598  11840   9633   1130    657  -1607       C  
ATOM   2327  C   SER A 301       5.322  -1.894 -17.273  1.00 86.05           C  
ANISOU 2327  C   SER A 301     9325  12384  10986    952    651  -2147       C  
ATOM   2328  O   SER A 301       4.881  -2.496 -18.256  1.00 91.13           O  
ANISOU 2328  O   SER A 301     9737  13236  11652   1165    469  -2687       O  
ATOM   2329  CB  SER A 301       7.628  -0.965 -17.494  1.00 78.62           C  
ANISOU 2329  CB  SER A 301     8667  11771   9434   1215    734  -1335       C  
ATOM   2330  OG  SER A 301       7.952  -1.954 -16.532  1.00 78.32           O  
ANISOU 2330  OG  SER A 301     8751  11242   9764    977    835  -1345       O  
ATOM   2331  N   GLY A 302       5.121  -2.328 -16.028  1.00 87.72           N  
ANISOU 2331  N   GLY A 302     9671  12073  11585    578    858  -2027       N  
ATOM   2332  CA  GLY A 302       4.290  -3.484 -15.746  1.00 93.55           C  
ANISOU 2332  CA  GLY A 302    10285  12409  12849    341    944  -2484       C  
ATOM   2333  C   GLY A 302       5.064  -4.738 -15.396  1.00 98.24           C  
ANISOU 2333  C   GLY A 302    11056  12580  13691    267   1043  -2479       C  
ATOM   2334  O   GLY A 302       4.822  -5.804 -15.969  1.00100.04           O  
ANISOU 2334  O   GLY A 302    11109  12683  14218    307    969  -2985       O  
ATOM   2335  N   VAL A 303       5.990  -4.625 -14.445  1.00100.37           N  
ANISOU 2335  N   VAL A 303    11667  12612  13858    189   1181  -1947       N  
ATOM   2336  CA  VAL A 303       6.833  -5.746 -14.044  1.00103.34           C  
ANISOU 2336  CA  VAL A 303    12269  12579  14415    189   1238  -1888       C  
ATOM   2337  C   VAL A 303       6.097  -6.600 -13.021  1.00107.53           C  
ANISOU 2337  C   VAL A 303    12970  12456  15431   -167   1515  -1919       C  
ATOM   2338  O   VAL A 303       5.445  -6.081 -12.107  1.00107.79           O  
ANISOU 2338  O   VAL A 303    13111  12330  15513   -423   1731  -1684       O  
ATOM   2339  CB  VAL A 303       8.174  -5.232 -13.488  1.00 98.20           C  
ANISOU 2339  CB  VAL A 303    11891  11991  13430    324   1220  -1355       C  
ATOM   2340  CG1 VAL A 303       8.859  -6.295 -12.638  1.00 98.89           C  
ANISOU 2340  CG1 VAL A 303    12308  11542  13724    296   1300  -1214       C  
ATOM   2341  CG2 VAL A 303       9.085  -4.791 -14.627  1.00 96.00           C  
ANISOU 2341  CG2 VAL A 303    11431  12265  12778    669   1018  -1390       C  
ATOM   2342  N   THR A 304       6.203  -7.919 -13.175  1.00110.01           N  
ANISOU 2342  N   THR A 304    13315  12369  16114   -181   1537  -2206       N  
ATOM   2343  CA  THR A 304       5.573  -8.885 -12.287  1.00109.95           C  
ANISOU 2343  CA  THR A 304    13503  11653  16621   -520   1857  -2222       C  
ATOM   2344  C   THR A 304       6.636  -9.769 -11.642  1.00106.54           C  
ANISOU 2344  C   THR A 304    13517  10746  16216   -414   1898  -1911       C  
ATOM   2345  O   THR A 304       7.823  -9.697 -11.974  1.00108.84           O  
ANISOU 2345  O   THR A 304    13880  11289  16186    -78   1646  -1795       O  
ATOM   2346  CB  THR A 304       4.557  -9.751 -13.047  1.00114.37           C  
ANISOU 2346  CB  THR A 304    13674  12038  17743   -665   1867  -2923       C  
ATOM   2347  OG1 THR A 304       5.165 -10.278 -14.234  1.00115.25           O  
ANISOU 2347  OG1 THR A 304    13575  12405  17808   -319   1526  -3343       O  
ATOM   2348  CG2 THR A 304       3.328  -8.934 -13.422  1.00113.51           C  
ANISOU 2348  CG2 THR A 304    13153  12298  17678   -796   1858  -3242       C  
ATOM   2349  N   PHE A 305       6.198 -10.610 -10.708  1.00100.81           N  
ANISOU 2349  N   PHE A 305    13098   9321  15885   -690   2237  -1777       N  
ATOM   2350  CA  PHE A 305       7.103 -11.517 -10.006  1.00 95.00           C  
ANISOU 2350  CA  PHE A 305    12865   8047  15185   -560   2286  -1459       C  
ATOM   2351  C   PHE A 305       6.526 -12.930  -9.946  1.00 97.72           C  
ANISOU 2351  C   PHE A 305    13291   7636  16201   -789   2534  -1731       C  
ATOM   2352  O   PHE A 305       5.369 -13.124  -9.576  1.00100.14           O  
ANISOU 2352  O   PHE A 305    13531   7596  16921  -1197   2913  -1822       O  
ATOM   2353  CB  PHE A 305       7.385 -11.008  -8.589  1.00 90.71           C  
ANISOU 2353  CB  PHE A 305    12832   7331  14302   -590   2491   -793       C  
ATOM   2354  CG  PHE A 305       7.426  -9.512  -8.482  1.00 84.81           C  
ANISOU 2354  CG  PHE A 305    11933   7213  13077   -544   2379   -586       C  
ATOM   2355  CD1 PHE A 305       8.475  -8.789  -9.028  1.00 81.70           C  
ANISOU 2355  CD1 PHE A 305    11398   7370  12276   -209   2012   -544       C  
ATOM   2356  CD2 PHE A 305       6.412  -8.826  -7.835  1.00 84.60           C  
ANISOU 2356  CD2 PHE A 305    11892   7203  13049   -844   2667   -448       C  
ATOM   2357  CE1 PHE A 305       8.509  -7.410  -8.932  1.00 78.27           C  
ANISOU 2357  CE1 PHE A 305    10830   7436  11473   -188   1932   -349       C  
ATOM   2358  CE2 PHE A 305       6.440  -7.450  -7.736  1.00 81.32           C  
ANISOU 2358  CE2 PHE A 305    11342   7319  12238   -788   2544   -282       C  
ATOM   2359  CZ  PHE A 305       7.490  -6.741  -8.285  1.00 77.91           C  
ANISOU 2359  CZ  PHE A 305    10790   7377  11434   -466   2176   -221       C  
ATOM   2360  O   DMS B 801       6.343  -0.880  -7.746  1.00 76.80           O  
ATOM   2361  C1  DMS B 801       6.770  -1.439  -5.130  1.00 74.82           C  
ATOM   2362  C2  DMS B 801       5.560  -3.290  -6.785  1.00 73.48           C  
ATOM   2363  S   DMS B 801       6.819  -1.986  -6.857  1.00 75.77           S  
ATOM   2364  O   DMS B 901       7.325   0.087  17.463  1.00 83.38           O  
ATOM   2365  C1  DMS B 901       7.183  -0.544  20.093  1.00 85.95           C  
ATOM   2366  C2  DMS B 901       5.237   1.044  18.874  1.00 83.72           C  
ATOM   2367  S   DMS B 901       6.339  -0.349  18.498  1.00 84.68           S  
ATOM   2368  O   HOH C   1      -1.332   6.126  -2.678  1.00 37.22           O  
ATOM   2369  O   HOH C   2      -2.174   3.825  -2.449  1.00 51.96           O  
ATOM   2370  O   HOH C   3       5.915   1.786  -7.878  1.00 41.00           O  
ATOM   2371  O   HOH C   4       7.799   3.119  -3.514  1.00 31.41           O  
ATOM   2372  O   HOH C   5       4.148 -12.508  -2.510  1.00 42.39           O  
ATOM   2373  O   HOH C   7      21.563 -19.364  26.787  1.00 46.41           O  
ATOM   2374  O   HOH C   8      16.245 -26.627  27.418  1.00 41.22           O  
ATOM   2375  O   HOH C   9      23.311  -3.011  15.883  1.00 40.65           O  
ATOM   2376  O   HOH C  10      27.991  -7.985  12.073  1.00 39.72           O  
ATOM   2377  O   HOH C  11      17.047   5.910  -4.226  1.00 47.75           O  
ATOM   2378  O   HOH C  12      19.910   0.096  -1.044  1.00 43.66           O  
ATOM   2379  O   HOH C  13      10.035   6.192   5.561  1.00 30.07           O  
ATOM   2380  O   HOH C  14      16.809   1.951  11.900  1.00 33.40           O  
ATOM   2381  O   HOH C  15      13.104  10.418  10.867  1.00 44.71           O  
ATOM   2382  O   HOH C  16      22.355   8.955   4.323  1.00 56.54           O  
ATOM   2383  O   HOH C  17       9.961   0.556  21.268  1.00 41.87           O  
ATOM   2384  O   HOH C  18      12.961   6.559  25.835  1.00 42.28           O  
ATOM   2385  O   HOH C  19      23.198   3.543  25.397  1.00 43.40           O  
ATOM   2386  O   HOH C  21       9.623   9.818  -4.915  1.00 37.88           O  
ATOM   2387  O   HOH C  22      21.234  16.209 -18.279  1.00 36.12           O  
ATOM   2388  O   HOH C  23      -0.038  16.361   0.010  1.00 33.15           O  
ATOM   2389  O   HOH C  24       5.764   2.026  -5.019  1.00 32.39           O  
ATOM   2390  O   HOH C  25      16.165  -6.024  20.239  1.00 37.43           O  
ATOM   2391  O   HOH C  26       6.974  -5.086  22.261  1.00 46.42           O  
ATOM   2392  O   HOH C  27       8.204   2.311  29.926  1.00 51.89           O  
ATOM   2393  O   HOH C  28      15.111 -10.030  -4.458  1.00 58.95           O  
ATOM   2394  O   HOH C  29      10.680  -0.987  -3.576  1.00 43.31           O  
ATOM   2395  O   HOH C  30       6.351  -9.256   8.776  1.00 55.02           O  
ATOM   2396  O   HOH C  31      20.226   9.329  12.366  1.00 39.07           O  
ATOM   2397  O   HOH C  32       6.688  26.341 -15.072  1.00 45.06           O  
END



If you find results from this site helpful for your research, please cite one of our papers:

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