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***    ***

elNémo ID: 20053017162535919

Job options:

ID        	=	 20053017162535919
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 2017-08-09 Time 16:05:51 EEST +0300 (1502283951.32 s)
REMARK PHENIX refinement
REMARK 
REMARK ****************** INPUT FILES AND LABELS ******************************
REMARK Reflections:
REMARK   file name      : /corefiler/vol/crystaldata/scratch/apapageo/gst/CdGSTM1/hamb6jun17/ZOX/xds_CdGSTM1-ZOX-02_w1_4_1/XDS_ASCII_scaled1.mtz
REMARK   labels         : ['IMEAN_XDSdataset,SIGIMEAN_XDSdataset']
REMARK R-free flags:
REMARK   file name      : /corefiler/vol/crystaldata/scratch/apapageo/gst/CdGSTM1/hamb6jun17/ZOX/xds_CdGSTM1-ZOX-02_w1_4_1/XDS_ASCII_scaled1.mtz
REMARK   label          : FreeR_flag
REMARK   test_flag_value: 0
REMARK Model file name(s): 
REMARK   /corefiler/vol/crystaldata/scratch/apapageo/gst/CdGSTM1/hamb6jun17/ZOX/xds_CdGSTM1-ZOX-02_w1_4_1/reproc/Refine_3/CdGSTM1-ZOX_refine_3.pdb
REMARK 
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS *******************
REMARK Start: r_work = 0.2299 r_free = 0.2844 bonds = 0.008 angles = 1.002
REMARK Final: r_work = 0.2186 r_free = 0.2765 bonds = 0.008 angles = 1.009
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_bss: bulk solvent correction and/or (anisotropic) scaling             
REMARK 1_xyz: refinement of coordinates                                        
REMARK 1_adp: refinement of ADPs (Atomic Displacement Parameters)              
REMARK 1_sar: simulated annealing refinement of x,y,z                          
REMARK 1_wat: ordered solvent update (add / remove)                            
REMARK 1_occ: refinement of occupancies                                        
REMARK ------------------------------------------------------------------------
REMARK  stage       r-work r-free bonds angles b_min b_max b_ave n_water shift
REMARK       0    : 0.5304 0.5727 0.008  1.00  30.3 118.0  57.9 180      0.000
REMARK       1_bss: 0.2299 0.2844 0.008  1.00  30.3 118.0  57.9 180      0.000
REMARK 1_settarget: 0.2299 0.2844 0.008  1.00  30.3 118.0  57.9 180      0.000
REMARK       1_nqh: 0.2299 0.2844 0.008  1.00  30.3 118.0  57.9 180      0.000
REMARK    1_weight: 0.2299 0.2844 0.008  1.00  30.3 118.0  57.9 180      0.000
REMARK    1_xyzrec: 0.2273 0.2884 0.009  1.02  30.3 118.0  57.9 180      0.079
REMARK       1_adp: 0.2177 0.2839 0.009  1.02  24.8 134.9  60.7 180      0.079
REMARK       2_bss: 0.2179 0.2847 0.009  1.02  24.8 134.9  60.7 180      0.079
REMARK 2_settarget: 0.2179 0.2847 0.009  1.02  24.8 134.9  60.7 180      0.079
REMARK 2_updatecdl: 0.2179 0.2847 0.009  1.03  24.8 134.9  60.7 180      0.079
REMARK       2_nqh: 0.2179 0.2847 0.009  1.03  24.8 134.9  60.7 180      0.079
REMARK   2_realsrl: 0.2198 0.2844 0.009  1.05  24.8 134.9  60.7 180      0.092
REMARK    2_weight: 0.2198 0.2844 0.009  1.05  24.8 134.9  60.7 180      0.092
REMARK    2_sacart: 0.2231 0.2922 0.018  1.31  24.8 134.9  60.7 180      0.220
REMARK    2_xyzrec: 0.2216 0.2918 0.009  1.12  24.8 134.9  60.7 180      0.218
REMARK  2_realsrl2: 0.2224 0.2927 0.009  1.12  24.8 134.9  60.7 180      0.218
REMARK       2_adp: 0.2190 0.2910 0.009  1.12  23.1 147.5  62.2 180      0.218
REMARK       3_bss: 0.2188 0.2914 0.009  1.12  23.1 147.5  62.2 180      0.218
REMARK 3_settarget: 0.2188 0.2914 0.009  1.12  23.1 147.5  62.2 180      0.218
REMARK 3_updatecdl: 0.2188 0.2914 0.009  1.14  23.1 147.5  62.2 180      0.218
REMARK       3_sol: 0.2217 0.2879 0.009  1.14  23.1 147.5  62.2 174       n/a
REMARK       3_nqh: 0.2217 0.2877 0.009  1.14  23.1 147.5  62.2 174       n/a
REMARK   3_realsrl: 0.2238 0.2898 0.009  1.20  23.1 147.5  62.2 174       n/a
REMARK    3_weight: 0.2238 0.2898 0.009  1.20  23.1 147.5  62.2 174       n/a
REMARK    3_xyzrec: 0.2219 0.2849 0.008  1.06  23.1 147.5  62.2 174       n/a
REMARK  3_realsrl2: 0.2223 0.2846 0.008  1.06  23.1 147.5  62.2 174       n/a
REMARK       3_adp: 0.2218 0.2827 0.008  1.06  24.0 143.7  61.5 174       n/a
REMARK       4_bss: 0.2215 0.2820 0.008  1.06  24.0 143.7  61.5 174       n/a
REMARK 4_settarget: 0.2215 0.2820 0.008  1.06  24.0 143.7  61.5 174       n/a
REMARK 4_updatecdl: 0.2215 0.2820 0.008  1.07  24.0 143.7  61.5 174       n/a
REMARK       4_sol: 0.2218 0.2811 0.008  1.07  24.0 143.7  61.5 184       n/a
REMARK       4_nqh: 0.2218 0.2811 0.008  1.07  24.0 143.7  61.5 184       n/a
REMARK   4_realsrl: 0.2233 0.2822 0.008  1.11  24.0 143.7  61.5 184       n/a
REMARK    4_weight: 0.2233 0.2822 0.008  1.11  24.0 143.7  61.5 184       n/a
REMARK    4_sacart: 0.2198 0.2813 0.016  1.20  24.0 143.7  61.5 184       n/a
REMARK    4_xyzrec: 0.2179 0.2802 0.008  1.00  24.0 143.7  61.5 184       n/a
REMARK  4_realsrl2: 0.2185 0.2807 0.008  1.00  24.0 143.7  61.5 184       n/a
REMARK       4_adp: 0.2178 0.2795 0.008  1.00  23.1 151.0  60.9 184       n/a
REMARK       5_bss: 0.2176 0.2793 0.008  1.00  23.1 151.0  60.9 184       n/a
REMARK 5_settarget: 0.2176 0.2793 0.008  1.00  23.1 151.0  60.9 184       n/a
REMARK 5_updatecdl: 0.2176 0.2793 0.008  1.01  23.1 151.0  60.9 184       n/a
REMARK       5_sol: 0.2185 0.2790 0.008  1.01  23.1 151.0  60.8 188       n/a
REMARK       5_nqh: 0.2185 0.2790 0.008  1.01  23.1 151.0  60.8 188       n/a
REMARK   5_realsrl: 0.2194 0.2795 0.008  1.04  23.1 151.0  60.8 188       n/a
REMARK    5_weight: 0.2194 0.2795 0.008  1.04  23.1 151.0  60.8 188       n/a
REMARK    5_xyzrec: 0.2173 0.2787 0.008  1.01  23.1 151.0  60.8 188       n/a
REMARK  5_realsrl2: 0.2176 0.2788 0.008  1.01  23.1 151.0  60.8 188       n/a
REMARK       5_adp: 0.2177 0.2776 0.008  1.01  23.8 152.3  60.4 188       n/a
REMARK         end: 0.2186 0.2765 0.008  1.01  23.8 152.3  60.4 178       n/a
REMARK ------------------------------------------------------------------------
REMARK MODEL CONTENT.
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM
REMARK        C                     4698         4698.00
REMARK        S                       48           48.00
REMARK        O                     1478         1478.00
REMARK        N                     1200         1200.00
REMARK    TOTAL                     7424         7424.00
REMARK -----------------------------------------------------------------------
REMARK r_free_flags.md5.hexdigest 7b68487066b7b7d62b919c17cfb68444
REMARK 
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)
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  REFINEMENT TARGET : ML
REMARK   3  
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.411   
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.892  
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.33  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.74 
REMARK   3   NUMBER OF REFLECTIONS             : 55905     
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 55905     
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2214
REMARK   3   R VALUE            (WORKING SET) : 0.2186
REMARK   3   FREE R VALUE                     : 0.2765
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.92  
REMARK   3   FREE R VALUE TEST SET COUNT      : 2753      
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWORK CCFREE
REMARK   3     1 95.9684 -  6.5425    1.00     2999   136  0.2547 0.3135   0.865  0.771
REMARK   3     2  6.5425 -  5.1930    1.00     2831   143  0.2081 0.2195   0.895  0.847
REMARK   3     3  5.1930 -  4.5366    1.00     2818   121  0.1623 0.2220   0.938  0.892
REMARK   3     4  4.5366 -  4.1218    1.00     2787   147  0.1539 0.2230   0.941  0.888
REMARK   3     5  4.1218 -  3.8264    1.00     2743   156  0.1746 0.2152   0.926  0.859
REMARK   3     6  3.8264 -  3.6008    1.00     2749   131  0.1977 0.2821   0.905  0.748
REMARK   3     7  3.6008 -  3.4204    1.00     2719   157  0.2058 0.3047   0.896  0.797
REMARK   3     8  3.4204 -  3.2715    1.00     2750   165  0.2155 0.3180   0.886  0.780
REMARK   3     9  3.2715 -  3.1456    1.00     2664   163  0.2250 0.2570   0.880  0.857
REMARK   3    10  3.1456 -  3.0370    1.00     2752   154  0.2420 0.2946   0.858  0.792
REMARK   3    11  3.0370 -  2.9421    1.00     2720   143  0.2521 0.3422   0.845  0.707
REMARK   3    12  2.9421 -  2.8580    1.00     2721   127  0.2626 0.2917   0.823  0.758
REMARK   3    13  2.8580 -  2.7827    1.00     2717   130  0.2768 0.3193   0.794  0.639
REMARK   3    14  2.7827 -  2.7148    1.00     2714   155  0.2783 0.3218   0.761  0.603
REMARK   3    15  2.7148 -  2.6531    1.00     2722   128  0.2792 0.3641   0.757  0.406
REMARK   3    16  2.6531 -  2.5966    1.00     2722   126  0.2885 0.3517   0.727  0.557
REMARK   3    17  2.5966 -  2.5447    1.00     2680   125  0.2928 0.3497   0.705  0.680
REMARK   3    18  2.5447 -  2.4967    1.00     2714   160  0.3182 0.3544   0.645  0.519
REMARK   3    19  2.4967 -  2.4521    0.93     2513   136  0.3545 0.3745   0.542  0.574
REMARK   3    20  2.4521 -  2.4105    0.41     1117    50  0.3998 0.4256   0.298  0.078
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)     : 0.41    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.25   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  
REMARK   3  RESTRAINTS LIBRARY
REMARK   3    GEOSTD + MON.LIB. + CDL v1.2
REMARK   3  
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD     MAX  COUNT
REMARK   3   BOND      :  0.008   0.084   7430
REMARK   3   ANGLE     :  1.009  11.847   9992
REMARK   3   CHIRALITY :  0.049   0.225   1018
REMARK   3   PLANARITY :  0.007   0.087   1272
REMARK   3   DIHEDRAL  :  5.337  64.649   4504
REMARK   3   MIN NONBONDED DISTANCE : 1.899 
REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3   ALL-ATOM CLASHSCORE : 8.01
REMARK   3   RAMACHANDRAN PLOT:
REMARK   3     OUTLIERS : 1.51  %
REMARK   3     ALLOWED  : 4.07  %
REMARK   3     FAVORED  : 94.42 %
REMARK   3   ROTAMER OUTLIERS : 0.80 %
REMARK   3   CBETA DEVIATIONS : 0
REMARK   3   PEPTIDE PLANE:
REMARK   3     CIS-PROLINE     : 8
REMARK   3     CIS-GENERAL     : 0
REMARK   3     TWISTED PROLINE : 0
REMARK   3     TWISTED GENERAL : 1
REMARK   3  
REMARK   3  ATOMIC DISPLACEMENT PARAMETERS.
REMARK   3   WILSON B : None
REMARK   3   RMS(B_ISO_OR_EQUIVALENT_BONDED) : 5.83
REMARK   3   ATOMS          NUMBER OF ATOMS
REMARK   3                    ISO.  ANISO. 
REMARK   3    ALL         :   7424    7246
REMARK   3    ALL (NO H)  :   7424    7246
REMARK   3    SOLVENT     :    178       0
REMARK   3    NON-SOLVENT :   7246    7246
REMARK   3    HYDROGENS   :      0       0
REMARK   3  
REMARK   3  TLS DETAILS.
REMARK   3   NUMBER OF TLS GROUPS: 1     
REMARK   3   ORIGIN: CENTER OF MASS
REMARK   3   TLS GROUP : 1     
REMARK   3    SELECTION: all
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2688   8.2083 -45.5325
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.3029 T22:   0.2944                       
REMARK   3      T33:   0.3340 T12:  -0.0373                       
REMARK   3      T13:   0.0050 T23:  -0.0152                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   0.1192 L22:   0.5560                       
REMARK   3      L33:   1.1591 L12:  -0.1028                       
REMARK   3      L13:  -0.1467 L23:   0.7536                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0085 S12:   0.0411 S13:  -0.0096         
REMARK   3      S21:  -0.0043 S22:   0.0284 S23:  -0.0403         
REMARK   3      S31:   0.0577 S32:  -0.0048 S33:  -0.0013         
REMARK   3
CRYST1   50.832  150.151  191.785  90.00  90.00  90.00 P 21 21 21
SCALE1      0.019673  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006660  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005214        0.00000
ATOM      1  N   PRO C   1      -2.209  32.902 -44.587  1.00 77.09           N
ANISOU    1  N   PRO C   1    10139   9281   9869  -1485   1198   -800       N
ATOM      2  CA  PRO C   1      -3.448  32.141 -44.430  1.00 75.93           C
ANISOU    2  CA  PRO C   1     9986   9132   9731  -1351   1081   -696       C
ATOM      3  C   PRO C   1      -3.686  31.647 -43.016  1.00 71.93           C
ANISOU    3  C   PRO C   1     9354   8691   9285  -1270    989   -692       C
ATOM      4  O   PRO C   1      -2.742  31.442 -42.244  1.00 70.90           O
ANISOU    4  O   PRO C   1     9101   8636   9203  -1299    995   -780       O
ATOM      5  CB  PRO C   1      -3.256  30.942 -45.373  1.00 70.65           C
ANISOU    5  CB  PRO C   1     9269   8504   9071  -1333   1062   -702       C
ATOM      6  CG  PRO C   1      -1.805  30.846 -45.585  1.00 75.66           C
ANISOU    6  CG  PRO C   1     9823   9198   9727  -1436   1141   -825       C
ATOM      7  CD  PRO C   1      -1.325  32.273 -45.579  1.00 80.54           C
ANISOU    7  CD  PRO C   1    10536   9757  10307  -1549   1251   -868       C
ATOM      8  N   MET C   2      -4.963  31.448 -42.701  1.00 60.05           N
ANISOU    8  N   MET C   2     7882   7159   7774  -1168    904   -594       N
ATOM      9  CA  MET C   2      -5.345  30.822 -41.448  1.00 52.78           C
ANISOU    9  CA  MET C   2     6854   6295   6905  -1084    811   -579       C
ATOM     10  C   MET C   2      -4.743  29.429 -41.338  1.00 53.80           C
ANISOU   10  C   MET C   2     6847   6511   7082  -1054    767   -626       C
ATOM     11  O   MET C   2      -4.506  28.744 -42.338  1.00 56.55           O
ANISOU   11  O   MET C   2     7194   6871   7423  -1065    778   -635       O
ATOM     12  CB  MET C   2      -6.858  30.753 -41.356  1.00 52.55           C
ANISOU   12  CB  MET C   2     6888   6223   6854   -988    736   -472       C
ATOM     13  CG  MET C   2      -7.466  32.094 -41.555  1.00 66.84           C
ANISOU   13  CG  MET C   2     8841   7945   8609  -1003    773   -428       C
ATOM     14  SD  MET C   2      -9.181  32.123 -41.076  1.00 80.11           S
ANISOU   14  SD  MET C   2    10565   9598  10275   -885    677   -328       S
ATOM     15  CE  MET C   2      -9.801  33.365 -42.218  1.00 76.19           C
ANISOU   15  CE  MET C   2    10271   8991   9686   -896    728   -279       C
ATOM     16  N   ILE C   3      -4.467  29.009 -40.109  1.00 43.67           N
ANISOU   16  N   ILE C   3     5455   5290   5846  -1014    714   -659       N
ATOM     17  CA  ILE C   3      -4.005  27.650 -39.876  1.00 44.14           C
ANISOU   17  CA  ILE C   3     5399   5427   5944   -964    658   -697       C
ATOM     18  C   ILE C   3      -5.034  27.001 -38.977  1.00 42.98           C
ANISOU   18  C   ILE C   3     5233   5284   5814   -861    562   -626       C
ATOM     19  O   ILE C   3      -5.347  27.525 -37.905  1.00 52.32           O
ANISOU   19  O   ILE C   3     6411   6462   7006   -840    539   -612       O
ATOM     20  CB  ILE C   3      -2.588  27.595 -39.275  1.00 41.43           C
ANISOU   20  CB  ILE C   3     4941   5163   5637  -1005    683   -821       C
ATOM     21  CG1 ILE C   3      -1.575  28.214 -40.242  1.00 44.16           C
ANISOU   21  CG1 ILE C   3     5305   5508   5965  -1121    790   -902       C
ATOM     22  CG2 ILE C   3      -2.175  26.165 -39.003  1.00 37.11           C
ANISOU   22  CG2 ILE C   3     4287   4691   5122   -934    614   -857       C
ATOM     23  CD1 ILE C   3      -0.310  28.723 -39.555  1.00 50.08           C
ANISOU   23  CD1 ILE C   3     5964   6323   6742  -1186    838  -1030       C
ATOM     24  N   LEU C   4      -5.623  25.925 -39.454  1.00 41.65           N
ANISOU   24  N   LEU C   4     5064   5118   5642   -804    511   -578       N
ATOM     25  CA  LEU C   4      -6.542  25.116 -38.670  1.00 36.38           C
ANISOU   25  CA  LEU C   4     4376   4458   4988   -715    426   -520       C
ATOM     26  C   LEU C   4      -5.767  23.877 -38.284  1.00 39.07           C
ANISOU   26  C   LEU C   4     4620   4865   5359   -677    385   -576       C
ATOM     27  O   LEU C   4      -5.389  23.087 -39.158  1.00 45.39           O
ANISOU   27  O   LEU C   4     5404   5684   6157   -680    390   -596       O
ATOM     28  CB  LEU C   4      -7.798  24.754 -39.466  1.00 41.62           C
ANISOU   28  CB  LEU C   4     5111   5079   5624   -679    400   -433       C
ATOM     29  CG  LEU C   4      -8.747  23.768 -38.780  1.00 44.30           C
ANISOU   29  CG  LEU C   4     5427   5430   5974   -599    322   -383       C
ATOM     30  CD1 LEU C   4      -9.372  24.439 -37.564  1.00 41.81           C
ANISOU   30  CD1 LEU C   4     5119   5101   5664   -575    297   -356       C
ATOM     31  CD2 LEU C   4      -9.832  23.250 -39.700  1.00 48.74           C
ANISOU   31  CD2 LEU C   4     6043   5966   6512   -572    301   -319       C
ATOM     32  N   GLY C   5      -5.492  23.720 -36.992  1.00 36.31           N
ANISOU   32  N   GLY C   5     4212   4551   5034   -637    344   -605       N
ATOM     33  CA  GLY C   5      -4.803  22.536 -36.493  1.00 37.07           C
ANISOU   33  CA  GLY C   5     4229   4706   5151   -581    294   -658       C
ATOM     34  C   GLY C   5      -5.836  21.533 -36.009  1.00 39.72           C
ANISOU   34  C   GLY C   5     4587   5023   5481   -502    223   -585       C
ATOM     35  O   GLY C   5      -6.802  21.905 -35.352  1.00 46.60           O
ANISOU   35  O   GLY C   5     5497   5862   6347   -482    202   -524       O
ATOM     36  N   TYR C   6      -5.641  20.265 -36.363  1.00 46.81           N
ANISOU   36  N   TYR C   6     5465   5941   6378   -460    190   -595       N
ATOM     37  CA  TYR C   6      -6.534  19.204 -35.892  1.00 49.56           C
ANISOU   37  CA  TYR C   6     5842   6272   6718   -391    128   -536       C
ATOM     38  C   TYR C   6      -5.894  17.854 -36.189  1.00 43.85           C
ANISOU   38  C   TYR C   6     5088   5579   5994   -347     97   -575       C
ATOM     39  O   TYR C   6      -4.837  17.775 -36.817  1.00 47.84           O
ANISOU   39  O   TYR C   6     5547   6123   6507   -368    121   -646       O
ATOM     40  CB  TYR C   6      -7.931  19.283 -36.526  1.00 45.47           C
ANISOU   40  CB  TYR C   6     5395   5702   6181   -403    134   -445       C
ATOM     41  CG  TYR C   6      -8.953  18.451 -35.787  1.00 53.08           C
ANISOU   41  CG  TYR C   6     6386   6647   7137   -347     82   -391       C
ATOM     42  CD1 TYR C   6      -9.187  18.644 -34.429  1.00 45.25           C
ANISOU   42  CD1 TYR C   6     5391   5654   6149   -316     52   -384       C
ATOM     43  CD2 TYR C   6      -9.654  17.433 -36.437  1.00 58.71           C
ANISOU   43  CD2 TYR C   6     7129   7342   7834   -331     65   -351       C
ATOM     44  CE1 TYR C   6     -10.119  17.860 -33.735  1.00 42.98           C
ANISOU   44  CE1 TYR C   6     5136   5347   5849   -274     13   -339       C
ATOM     45  CE2 TYR C   6     -10.590  16.652 -35.757  1.00 46.34           C
ANISOU   45  CE2 TYR C   6     5593   5758   6257   -292     28   -309       C
ATOM     46  CZ  TYR C   6     -10.814  16.868 -34.412  1.00 49.76           C
ANISOU   46  CZ  TYR C   6     6027   6187   6691   -266      4   -304       C
ATOM     47  OH  TYR C   6     -11.737  16.085 -33.762  1.00 52.41           O
ANISOU   47  OH  TYR C   6     6400   6502   7013   -237    -25   -266       O
ATOM     48  N   TRP C   7      -6.534  16.793 -35.696  1.00 41.65           N
ANISOU   48  N   TRP C   7     4840   5283   5704   -285     45   -534       N
ATOM     49  CA  TRP C   7      -6.124  15.444 -36.032  1.00 44.63           C
ANISOU   49  CA  TRP C   7     5210   5674   6072   -238     13   -557       C
ATOM     50  C   TRP C   7      -6.521  15.142 -37.480  1.00 54.37           C
ANISOU   50  C   TRP C   7     6471   6890   7298   -276     43   -525       C
ATOM     51  O   TRP C   7      -7.290  15.881 -38.103  1.00 64.39           O
ANISOU   51  O   TRP C   7     7773   8129   8563   -327     79   -475       O
ATOM     52  CB  TRP C   7      -6.758  14.432 -35.076  1.00 47.91           C
ANISOU   52  CB  TRP C   7     5671   6064   6469   -168    -43   -519       C
ATOM     53  CG  TRP C   7      -6.445  14.603 -33.607  1.00 51.05           C
ANISOU   53  CG  TRP C   7     6056   6474   6866   -119    -79   -545       C
ATOM     54  CD1 TRP C   7      -7.275  15.133 -32.647  1.00 54.92           C
ANISOU   54  CD1 TRP C   7     6577   6937   7354   -120    -85   -498       C
ATOM     55  CD2 TRP C   7      -5.247  14.207 -32.919  1.00 50.53           C
ANISOU   55  CD2 TRP C   7     5945   6454   6799    -56   -117   -628       C
ATOM     56  NE1 TRP C   7      -6.661  15.104 -31.419  1.00 54.84           N
ANISOU   56  NE1 TRP C   7     6548   6948   7341    -65   -123   -542       N
ATOM     57  CE2 TRP C   7      -5.419  14.539 -31.553  1.00 54.73           C
ANISOU   57  CE2 TRP C   7     6489   6981   7327    -21   -145   -623       C
ATOM     58  CE3 TRP C   7      -4.044  13.615 -33.323  1.00 51.21           C
ANISOU   58  CE3 TRP C   7     5982   6590   6887    -21   -133   -712       C
ATOM     59  CZ2 TRP C   7      -4.421  14.308 -30.589  1.00 54.16           C
ANISOU   59  CZ2 TRP C   7     6380   6949   7248     51   -191   -699       C
ATOM     60  CZ3 TRP C   7      -3.050  13.381 -32.357  1.00 51.37           C
ANISOU   60  CZ3 TRP C   7     5961   6656   6901     54   -180   -793       C
ATOM     61  CH2 TRP C   7      -3.249  13.728 -31.012  1.00 51.89           C
ANISOU   61  CH2 TRP C   7     6041   6714   6960     91   -210   -785       C
ATOM     62  N   ASP C   8      -5.976  14.055 -38.030  1.00 59.44           N
ANISOU   62  N   ASP C   8     7100   7549   7934   -247     27   -557       N
ATOM     63  CA  ASP C   8      -6.325  13.646 -39.396  1.00 66.74           C
ANISOU   63  CA  ASP C   8     8050   8459   8851   -278     51   -530       C
ATOM     64  C   ASP C   8      -7.555  12.746 -39.390  1.00 71.95           C
ANISOU   64  C   ASP C   8     8772   9075   9492   -251     23   -456       C
ATOM     65  O   ASP C   8      -7.570  11.621 -39.886  1.00 76.03           O
ANISOU   65  O   ASP C   8     9305   9586   9996   -226      6   -455       O
ATOM     66  CB  ASP C   8      -5.141  12.987 -40.107  1.00 64.58           C
ANISOU   66  CB  ASP C   8     7728   8227   8581   -268     54   -604       C
ATOM     67  CG  ASP C   8      -4.619  11.752 -39.397  1.00 73.82           C
ANISOU   67  CG  ASP C   8     8890   9416   9743   -181     -7   -643       C
ATOM     68  OD1 ASP C   8      -5.058  11.479 -38.262  1.00 79.30           O
ANISOU   68  OD1 ASP C   8     9615  10089  10427   -132    -47   -616       O
ATOM     69  OD2 ASP C   8      -3.749  11.059 -39.978  1.00 79.05           O
ANISOU   69  OD2 ASP C   8     9518  10112  10404   -160    -14   -702       O
ATOM     70  N   ILE C   9      -8.608  13.273 -38.776  1.00 62.58           N
ANISOU   70  N   ILE C   9     7619   7858   8300   -260     21   -400       N
ATOM     71  CA  ILE C   9      -9.930  12.693 -38.781  1.00 55.42           C
ANISOU   71  CA  ILE C   9     6767   6915   7377   -254      8   -335       C
ATOM     72  C   ILE C   9     -10.928  13.820 -39.002  1.00 54.57           C
ANISOU   72  C   ILE C   9     6677   6790   7268   -296     34   -289       C
ATOM     73  O   ILE C   9     -10.571  14.998 -39.067  1.00 56.36           O
ANISOU   73  O   ILE C   9     6887   7024   7505   -326     61   -302       O
ATOM     74  CB  ILE C   9     -10.253  11.946 -37.470  1.00 51.22           C
ANISOU   74  CB  ILE C   9     6263   6365   6832   -203    -33   -324       C
ATOM     75  CG1 ILE C   9     -10.395  12.957 -36.315  1.00 49.06           C
ANISOU   75  CG1 ILE C   9     5981   6093   6568   -203    -37   -319       C
ATOM     76  CG2 ILE C   9      -9.198  10.896 -37.188  1.00 42.20           C
ANISOU   76  CG2 ILE C   9     5114   5238   5683   -146    -66   -375       C
ATOM     77  CD1 ILE C   9     -11.282  12.511 -35.182  1.00 37.08           C
ANISOU   77  CD1 ILE C   9     4509   4546   5033   -177    -62   -284       C
ATOM     78  N   ARG C  10     -12.199  13.443 -39.095  1.00 59.72           N
ANISOU   78  N   ARG C  10     7367   7419   7905   -297     26   -240       N
ATOM     79  CA  ARG C  10     -13.283  14.405 -39.269  1.00 55.79           C
ANISOU   79  CA  ARG C  10     6888   6909   7401   -322     40   -200       C
ATOM     80  C   ARG C  10     -13.561  15.148 -37.963  1.00 55.61           C
ANISOU   80  C   ARG C  10     6863   6883   7385   -313     30   -192       C
ATOM     81  O   ARG C  10     -13.317  16.354 -37.860  1.00 64.20           O
ANISOU   81  O   ARG C  10     7941   7972   8480   -331     47   -196       O
ATOM     82  CB  ARG C  10     -14.519  13.662 -39.778  1.00 54.86           C
ANISOU   82  CB  ARG C  10     6799   6782   7265   -324     33   -167       C
ATOM     83  CG  ARG C  10     -15.616  14.521 -40.279  1.00 55.20           C
ANISOU   83  CG  ARG C  10     6857   6822   7296   -340     43   -137       C
ATOM     84  CD  ARG C  10     -16.749  13.639 -40.749  1.00 54.62           C
ANISOU   84  CD  ARG C  10     6798   6749   7205   -341     35   -121       C
ATOM     85  NE  ARG C  10     -18.038  14.192 -40.378  1.00 50.33           N
ANISOU   85  NE  ARG C  10     6262   6211   6651   -341     27   -103       N
ATOM     86  CZ  ARG C  10     -19.160  13.939 -41.025  1.00 51.49           C
ANISOU   86  CZ  ARG C  10     6413   6370   6780   -345     24    -97       C
ATOM     87  NH1 ARG C  10     -19.143  13.128 -42.068  1.00 57.75           N
ANISOU   87  NH1 ARG C  10     7211   7167   7565   -352     29   -103       N
ATOM     88  NH2 ARG C  10     -20.296  14.493 -40.627  1.00 55.17           N
ANISOU   88  NH2 ARG C  10     6876   6849   7237   -340     15    -92       N
ATOM     89  N   GLY C  11     -14.083  14.437 -36.964  1.00 48.79           N
ANISOU   89  N   GLY C  11     6014   6009   6514   -289      4   -180       N
ATOM     90  CA  GLY C  11     -14.195  14.891 -35.585  1.00 49.55           C
ANISOU   90  CA  GLY C  11     6109   6102   6615   -273    -10   -178       C
ATOM     91  C   GLY C  11     -14.821  16.262 -35.448  1.00 52.09           C
ANISOU   91  C   GLY C  11     6427   6423   6941   -294      4   -158       C
ATOM     92  O   GLY C  11     -15.719  16.649 -36.201  1.00 53.27           O
ANISOU   92  O   GLY C  11     6590   6569   7080   -311     15   -133       O
ATOM     93  N   LEU C  12     -14.342  17.015 -34.446  1.00 51.16           N
ANISOU   93  N   LEU C  12     6294   6310   6836   -286     -0   -172       N
ATOM     94  CA  LEU C  12     -14.885  18.351 -34.196  1.00 52.40           C
ANISOU   94  CA  LEU C  12     6454   6461   6995   -302     12   -154       C
ATOM     95  C   LEU C  12     -14.429  19.397 -35.232  1.00 54.29           C
ANISOU   95  C   LEU C  12     6694   6698   7235   -332     45   -162       C
ATOM     96  O   LEU C  12     -14.741  20.604 -35.053  1.00 51.19           O
ANISOU   96  O   LEU C  12     6315   6294   6839   -343     58   -151       O
ATOM     97  CB  LEU C  12     -14.494  18.835 -32.805  1.00 48.29           C
ANISOU   97  CB  LEU C  12     5918   5944   6486   -287     -1   -169       C
ATOM     98  CG  LEU C  12     -15.123  18.180 -31.590  1.00 52.32           C
ANISOU   98  CG  LEU C  12     6443   6448   6988   -261    -28   -155       C
ATOM     99  CD1 LEU C  12     -14.223  18.484 -30.398  1.00 47.02           C
ANISOU   99  CD1 LEU C  12     5752   5785   6328   -239    -42   -185       C
ATOM    100  CD2 LEU C  12     -16.538  18.695 -31.356  1.00 48.45           C
ANISOU  100  CD2 LEU C  12     5970   5951   6488   -272    -26   -121       C
ATOM    101  N   ALA C  13     -13.700  19.035 -36.290  1.00 45.31           N
ANISOU  101  N   ALA C  13     5551   5566   6098   -347     63   -182       N
ATOM    102  CA  ALA C  13     -13.245  20.029 -37.249  1.00 42.54           C
ANISOU  102  CA  ALA C  13     5215   5207   5742   -383    102   -192       C
ATOM    103  C   ALA C  13     -14.077  20.065 -38.526  1.00 42.40           C
ANISOU  103  C   ALA C  13     5238   5172   5698   -390    112   -159       C
ATOM    104  O   ALA C  13     -13.877  20.969 -39.348  1.00 47.10           O
ANISOU  104  O   ALA C  13     5867   5750   6278   -416    146   -160       O
ATOM    105  CB  ALA C  13     -11.763  19.802 -37.581  1.00 35.13           C
ANISOU  105  CB  ALA C  13     4241   4289   4818   -403    125   -247       C
ATOM    106  N   HIS C  14     -15.011  19.125 -38.703  1.00 47.25           N
ANISOU  106  N   HIS C  14     5857   5792   6304   -368     85   -136       N
ATOM    107  CA  HIS C  14     -15.862  19.109 -39.895  1.00 45.67           C
ANISOU  107  CA  HIS C  14     5691   5585   6078   -367     88   -112       C
ATOM    108  C   HIS C  14     -16.596  20.433 -40.091  1.00 42.86           C
ANISOU  108  C   HIS C  14     5376   5210   5698   -362     95    -91       C
ATOM    109  O   HIS C  14     -16.520  21.036 -41.162  1.00 55.75           O
ANISOU  109  O   HIS C  14     7052   6824   7306   -372    118    -86       O
ATOM    110  CB  HIS C  14     -16.864  17.966 -39.803  1.00 45.12           C
ANISOU  110  CB  HIS C  14     5611   5528   6003   -347     59    -99       C
ATOM    111  CG  HIS C  14     -17.356  17.481 -41.131  1.00 48.38           C
ANISOU  111  CG  HIS C  14     6041   5944   6395   -348     62    -92       C
ATOM    112  ND1 HIS C  14     -16.511  17.003 -42.109  1.00 46.35           N
ANISOU  112  ND1 HIS C  14     5785   5686   6138   -363     80   -105       N
ATOM    113  CD2 HIS C  14     -18.611  17.358 -41.625  1.00 50.00           C
ANISOU  113  CD2 HIS C  14     6259   6161   6579   -334     46    -78       C
ATOM    114  CE1 HIS C  14     -17.225  16.616 -43.151  1.00 48.31           C
ANISOU  114  CE1 HIS C  14     6051   5940   6366   -358     76    -95       C
ATOM    115  NE2 HIS C  14     -18.501  16.822 -42.883  1.00 47.18           N
ANISOU  115  NE2 HIS C  14     5913   5806   6209   -339     54    -81       N
ATOM    116  N   ALA C  15     -17.320  20.905 -39.071  1.00 39.69           N
ANISOU  116  N   ALA C  15     4971   4811   5300   -343     75    -79       N
ATOM    117  CA  ALA C  15     -18.079  22.146 -39.247  1.00 39.40           C
ANISOU  117  CA  ALA C  15     4979   4757   5236   -328     75    -61       C
ATOM    118  C   ALA C  15     -17.170  23.343 -39.509  1.00 35.11           C
ANISOU  118  C   ALA C  15     4475   4180   4684   -354    114    -68       C
ATOM    119  O   ALA C  15     -17.558  24.267 -40.234  1.00 46.94           O
ANISOU  119  O   ALA C  15     6038   5650   6146   -345    125    -54       O
ATOM    120  CB  ALA C  15     -18.959  22.416 -38.019  1.00 43.98           C
ANISOU  120  CB  ALA C  15     5539   5348   5821   -304     47    -54       C
ATOM    121  N   ILE C  16     -15.974  23.359 -38.905  1.00 37.30           N
ANISOU  121  N   ILE C  16     4722   4461   4990   -385    136    -95       N
ATOM    122  CA  ILE C  16     -15.034  24.454 -39.114  1.00 41.08           C
ANISOU  122  CA  ILE C  16     5234   4913   5463   -425    183   -113       C
ATOM    123  C   ILE C  16     -14.517  24.439 -40.542  1.00 44.45           C
ANISOU  123  C   ILE C  16     5700   5322   5866   -454    221   -121       C
ATOM    124  O   ILE C  16     -14.411  25.488 -41.180  1.00 43.94           O
ANISOU  124  O   ILE C  16     5709   5217   5769   -475    258   -117       O
ATOM    125  CB  ILE C  16     -13.871  24.380 -38.103  1.00 43.71           C
ANISOU  125  CB  ILE C  16     5508   5266   5834   -450    195   -155       C
ATOM    126  CG1 ILE C  16     -14.376  24.373 -36.658  1.00 35.79           C
ANISOU  126  CG1 ILE C  16     4471   4277   4849   -419    157   -146       C
ATOM    127  CG2 ILE C  16     -12.894  25.527 -38.326  1.00 48.39           C
ANISOU  127  CG2 ILE C  16     6131   5836   6420   -503    252   -185       C
ATOM    128  CD1 ILE C  16     -13.327  23.861 -35.695  1.00 39.78           C
ANISOU  128  CD1 ILE C  16     4913   4813   5389   -424    152   -188       C
ATOM    129  N   ARG C  17     -14.181  23.254 -41.069  1.00 47.67           N
ANISOU  129  N   ARG C  17     6070   5754   6287   -457    214   -134       N
ATOM    130  CA  ARG C  17     -13.766  23.171 -42.468  1.00 46.39           C
ANISOU  130  CA  ARG C  17     5946   5578   6101   -484    248   -141       C
ATOM    131  C   ARG C  17     -14.878  23.652 -43.389  1.00 52.08           C
ANISOU  131  C   ARG C  17     6745   6269   6774   -454    239   -101       C
ATOM    132  O   ARG C  17     -14.656  24.519 -44.240  1.00 56.60           O
ANISOU  132  O   ARG C  17     7396   6801   7309   -476    279    -98       O
ATOM    133  CB  ARG C  17     -13.355  21.745 -42.832  1.00 38.86           C
ANISOU  133  CB  ARG C  17     4937   4658   5169   -482    235   -159       C
ATOM    134  CG  ARG C  17     -12.026  21.292 -42.238  1.00 38.49           C
ANISOU  134  CG  ARG C  17     4823   4642   5159   -506    248   -212       C
ATOM    135  CD  ARG C  17     -11.942  19.779 -42.169  1.00 38.06           C
ANISOU  135  CD  ARG C  17     4716   4620   5124   -478    212   -221       C
ATOM    136  NE  ARG C  17     -10.680  19.338 -41.591  1.00 41.15           N
ANISOU  136  NE  ARG C  17     5046   5044   5545   -486    215   -278       N
ATOM    137  CZ  ARG C  17     -10.547  18.270 -40.813  1.00 42.84           C
ANISOU  137  CZ  ARG C  17     5217   5282   5777   -447    173   -290       C
ATOM    138  NH1 ARG C  17     -11.605  17.536 -40.496  1.00 40.59           N
ANISOU  138  NH1 ARG C  17     4947   4989   5486   -410    134   -248       N
ATOM    139  NH2 ARG C  17      -9.355  17.953 -40.328  1.00 46.82           N
ANISOU  139  NH2 ARG C  17     5668   5819   6302   -444    172   -350       N
ATOM    140  N   LEU C  18     -16.094  23.113 -43.215  1.00 46.01           N
ANISOU  140  N   LEU C  18     5961   5519   6001   -403    188    -75       N
ATOM    141  CA  LEU C  18     -17.215  23.540 -44.052  1.00 36.41           C
ANISOU  141  CA  LEU C  18     4810   4286   4738   -362    170    -48       C
ATOM    142  C   LEU C  18     -17.453  25.045 -43.961  1.00 40.63           C
ANISOU  142  C   LEU C  18     5425   4777   5236   -352    184    -35       C
ATOM    143  O   LEU C  18     -17.796  25.689 -44.957  1.00 46.97           O
ANISOU  143  O   LEU C  18     6316   5545   5987   -333    193    -21       O
ATOM    144  CB  LEU C  18     -18.491  22.766 -43.696  1.00 33.86           C
ANISOU  144  CB  LEU C  18     4442   4002   4420   -315    114    -38       C
ATOM    145  CG  LEU C  18     -18.472  21.228 -43.807  1.00 39.65           C
ANISOU  145  CG  LEU C  18     5111   4772   5180   -322     99    -49       C
ATOM    146  CD1 LEU C  18     -19.626  20.488 -43.036  1.00 27.84           C
ANISOU  146  CD1 LEU C  18     3565   3314   3697   -294     56    -49       C
ATOM    147  CD2 LEU C  18     -18.370  20.841 -45.310  1.00 42.93           C
ANISOU  147  CD2 LEU C  18     5560   5182   5569   -325    111    -49       C
ATOM    148  N   LEU C  19     -17.280  25.633 -42.784  1.00 43.32           N
ANISOU  148  N   LEU C  19     5745   5114   5598   -359    185    -39       N
ATOM    149  CA  LEU C  19     -17.453  27.079 -42.697  1.00 47.03           C
ANISOU  149  CA  LEU C  19     6301   5537   6032   -351    203    -28       C
ATOM    150  C   LEU C  19     -16.286  27.804 -43.348  1.00 43.45           C
ANISOU  150  C   LEU C  19     5915   5035   5559   -413    273    -43       C
ATOM    151  O   LEU C  19     -16.475  28.826 -44.020  1.00 46.95           O
ANISOU  151  O   LEU C  19     6470   5422   5945   -406    297    -29       O
ATOM    152  CB  LEU C  19     -17.616  27.510 -41.243  1.00 45.52           C
ANISOU  152  CB  LEU C  19     6069   5358   5871   -344    185    -30       C
ATOM    153  CG  LEU C  19     -18.052  28.947 -41.011  1.00 47.74           C
ANISOU  153  CG  LEU C  19     6433   5593   6113   -321    190    -16       C
ATOM    154  CD1 LEU C  19     -19.429  29.132 -41.587  1.00 44.65           C
ANISOU  154  CD1 LEU C  19     6091   5202   5674   -244    143      5       C
ATOM    155  CD2 LEU C  19     -18.043  29.259 -39.515  1.00 51.47           C
ANISOU  155  CD2 LEU C  19     6852   6082   6622   -323    178    -23       C
ATOM    156  N   LEU C  20     -15.074  27.289 -43.166  1.00 36.78           N
ANISOU  156  N   LEU C  20     5009   4211   4754   -474    309    -77       N
ATOM    157  CA  LEU C  20     -13.928  27.893 -43.832  1.00 48.27           C
ANISOU  157  CA  LEU C  20     6519   5630   6192   -545    384   -105       C
ATOM    158  C   LEU C  20     -14.085  27.834 -45.353  1.00 54.01           C
ANISOU  158  C   LEU C  20     7329   6325   6867   -544    403    -90       C
ATOM    159  O   LEU C  20     -13.787  28.808 -46.051  1.00 52.25           O
ANISOU  159  O   LEU C  20     7217   6042   6594   -577    458    -90       O
ATOM    160  CB  LEU C  20     -12.636  27.205 -43.380  1.00 44.04           C
ANISOU  160  CB  LEU C  20     5885   5139   5711   -601    410   -158       C
ATOM    161  CG  LEU C  20     -12.079  27.531 -41.984  1.00 38.05           C
ANISOU  161  CG  LEU C  20     5061   4402   4994   -620    412   -188       C
ATOM    162  CD1 LEU C  20     -10.889  26.623 -41.690  1.00 42.06           C
ANISOU  162  CD1 LEU C  20     5466   4966   5550   -654    422   -246       C
ATOM    163  CD2 LEU C  20     -11.661  28.994 -41.870  1.00 39.44           C
ANISOU  163  CD2 LEU C  20     5314   4527   5143   -670    472   -202       C
ATOM    164  N   GLU C  21     -14.589  26.711 -45.882  1.00 51.75           N
ANISOU  164  N   GLU C  21     7000   6074   6588   -507    361    -78       N
ATOM    165  CA  GLU C  21     -14.807  26.618 -47.321  1.00 40.57           C
ANISOU  165  CA  GLU C  21     5662   4632   5122   -499    374    -64       C
ATOM    166  C   GLU C  21     -16.000  27.457 -47.768  1.00 44.25           C
ANISOU  166  C   GLU C  21     6235   5055   5522   -431    345    -26       C
ATOM    167  O   GLU C  21     -15.901  28.168 -48.776  1.00 42.01           O
ANISOU  167  O   GLU C  21     6072   4714   5176   -438    382    -17       O
ATOM    168  CB  GLU C  21     -14.964  25.163 -47.742  1.00 36.08           C
ANISOU  168  CB  GLU C  21     5013   4115   4581   -481    339    -68       C
ATOM    169  CG  GLU C  21     -13.647  24.421 -47.646  1.00 43.71           C
ANISOU  169  CG  GLU C  21     5901   5112   5594   -545    376   -111       C
ATOM    170  CD  GLU C  21     -12.800  24.531 -48.906  1.00 54.32           C
ANISOU  170  CD  GLU C  21     7302   6430   6908   -600    439   -132       C
ATOM    171  OE1 GLU C  21     -13.323  24.953 -49.945  1.00 58.74           O
ANISOU  171  OE1 GLU C  21     7961   6948   7410   -582    447   -105       O
ATOM    172  OE2 GLU C  21     -11.602  24.181 -48.867  1.00 64.84           O
ANISOU  172  OE2 GLU C  21     8579   7786   8273   -660    480   -180       O
ATOM    173  N   TYR C  22     -17.123  27.412 -47.031  1.00 43.07           N
ANISOU  173  N   TYR C  22     6050   4934   5381   -362    279     -9       N
ATOM    174  CA  TYR C  22     -18.283  28.223 -47.411  1.00 43.45           C
ANISOU  174  CA  TYR C  22     6193   4951   5365   -285    243     17       C
ATOM    175  C   TYR C  22     -17.918  29.702 -47.499  1.00 44.65           C
ANISOU  175  C   TYR C  22     6477   5024   5465   -302    291     25       C
ATOM    176  O   TYR C  22     -18.244  30.369 -48.485  1.00 49.98           O
ANISOU  176  O   TYR C  22     7282   5643   6064   -269    299     41       O
ATOM    177  CB  TYR C  22     -19.451  28.039 -46.434  1.00 52.86           C
ANISOU  177  CB  TYR C  22     7314   6191   6578   -219    173     22       C
ATOM    178  CG  TYR C  22     -20.623  28.984 -46.728  1.00 52.89           C
ANISOU  178  CG  TYR C  22     7412   6170   6514   -130    131     37       C
ATOM    179  CD1 TYR C  22     -20.745  30.212 -46.086  1.00 53.72           C
ANISOU  179  CD1 TYR C  22     7583   6233   6597   -113    136     45       C
ATOM    180  CD2 TYR C  22     -21.591  28.651 -47.664  1.00 52.85           C
ANISOU  180  CD2 TYR C  22     7430   6184   6465    -59     84     37       C
ATOM    181  CE1 TYR C  22     -21.790  31.079 -46.377  1.00 52.16           C
ANISOU  181  CE1 TYR C  22     7478   6011   6331    -22     94     54       C
ATOM    182  CE2 TYR C  22     -22.634  29.510 -47.961  1.00 49.81           C
ANISOU  182  CE2 TYR C  22     7132   5782   6014     33     40     42       C
ATOM    183  CZ  TYR C  22     -22.730  30.719 -47.314  1.00 54.69           C
ANISOU  183  CZ  TYR C  22     7818   6355   6607     54     43     51       C
ATOM    184  OH  TYR C  22     -23.785  31.558 -47.611  1.00 58.01           O
ANISOU  184  OH  TYR C  22     8327   6759   6955    159     -7     51       O
ATOM    185  N   THR C  23     -17.265  30.238 -46.464  1.00 50.26           N
ANISOU  185  N   THR C  23     7163   5725   6210   -352    324     12       N
ATOM    186  CA  THR C  23     -16.867  31.644 -46.450  1.00 52.64           C
ANISOU  186  CA  THR C  23     7589   5949   6464   -380    378     15       C
ATOM    187  C   THR C  23     -15.650  31.913 -47.326  1.00 54.41           C
ANISOU  187  C   THR C  23     7887   6123   6664   -471    468     -5       C
ATOM    188  O   THR C  23     -15.200  33.057 -47.400  1.00 51.62           O
ANISOU  188  O   THR C  23     7648   5698   6267   -512    529     -9       O
ATOM    189  CB  THR C  23     -16.580  32.118 -45.014  1.00 48.99           C
ANISOU  189  CB  THR C  23     7068   5497   6048   -406    383      2       C
ATOM    190  OG1 THR C  23     -15.408  31.469 -44.505  1.00 51.32           O
ANISOU  190  OG1 THR C  23     7254   5834   6411   -487    421    -35       O
ATOM    191  CG2 THR C  23     -17.758  31.806 -44.087  1.00 45.09           C
ANISOU  191  CG2 THR C  23     6495   5056   5580   -324    299     17       C
ATOM    192  N   GLY C  24     -15.106  30.889 -47.980  1.00 62.20           N
ANISOU  192  N   GLY C  24     8813   7145   7676   -507    483    -22       N
ATOM    193  CA  GLY C  24     -13.973  31.080 -48.869  1.00 57.83           C
ANISOU  193  CA  GLY C  24     8322   6551   7098   -596    571    -49       C
ATOM    194  C   GLY C  24     -12.730  31.583 -48.180  1.00 53.20           C
ANISOU  194  C   GLY C  24     7708   5960   6546   -697    646    -95       C
ATOM    195  O   GLY C  24     -11.901  32.236 -48.814  1.00 64.42           O
ANISOU  195  O   GLY C  24     9223   7327   7929   -777    733   -120       O
ATOM    196  N   SER C  25     -12.574  31.305 -46.896  1.00 54.40           N
ANISOU  196  N   SER C  25     7736   6167   6766   -698    617   -114       N
ATOM    197  CA  SER C  25     -11.389  31.769 -46.187  1.00 58.70           C
ANISOU  197  CA  SER C  25     8241   6716   7345   -789    683   -168       C
ATOM    198  C   SER C  25     -10.126  31.174 -46.802  1.00 57.36           C
ANISOU  198  C   SER C  25     8021   6577   7198   -877    747   -226       C
ATOM    199  O   SER C  25     -10.151  30.099 -47.405  1.00 57.77           O
ANISOU  199  O   SER C  25     8018   6668   7265   -857    719   -225       O
ATOM    200  CB  SER C  25     -11.485  31.401 -44.708  1.00 51.90           C
ANISOU  200  CB  SER C  25     7247   5919   6554   -761    629   -178       C
ATOM    201  OG  SER C  25     -12.558  32.097 -44.101  1.00 55.63           O
ANISOU  201  OG  SER C  25     7770   6364   7004   -693    582   -134       O
ATOM    202  N   ASP C  26      -9.016  31.901 -46.676  1.00 58.55           N
ANISOU  202  N   ASP C  26     8191   6708   7347   -977    835   -284       N
ATOM    203  CA  ASP C  26      -7.724  31.400 -47.146  1.00 50.66           C
ANISOU  203  CA  ASP C  26     7128   5749   6373  -1067    901   -358       C
ATOM    204  C   ASP C  26      -7.046  30.726 -45.967  1.00 49.31           C
ANISOU  204  C   ASP C  26     6782   5669   6284  -1073    871   -415       C
ATOM    205  O   ASP C  26      -6.499  31.388 -45.084  1.00 56.64           O
ANISOU  205  O   ASP C  26     7682   6605   7233  -1117    903   -459       O
ATOM    206  CB  ASP C  26      -6.848  32.509 -47.721  1.00 50.53           C
ANISOU  206  CB  ASP C  26     7225   5668   6307  -1183   1022   -405       C
ATOM    207  CG  ASP C  26      -5.467  31.997 -48.123  1.00 61.40           C
ANISOU  207  CG  ASP C  26     8517   7099   7714  -1283   1093   -498       C
ATOM    208  OD1 ASP C  26      -5.356  30.812 -48.513  1.00 65.37           O
ANISOU  208  OD1 ASP C  26     8928   7662   8248  -1253   1052   -506       O
ATOM    209  OD2 ASP C  26      -4.489  32.766 -48.052  1.00 69.65           O
ANISOU  209  OD2 ASP C  26     9583   8131   8751  -1392   1190   -570       O
ATOM    210  N   TYR C  27      -7.073  29.404 -45.958  1.00 48.65           N
ANISOU  210  N   TYR C  27     6588   5654   6244  -1024    810   -417       N
ATOM    211  CA  TYR C  27      -6.615  28.648 -44.811  1.00 46.76           C
ANISOU  211  CA  TYR C  27     6196   5496   6074  -1002    762   -460       C
ATOM    212  C   TYR C  27      -5.833  27.435 -45.277  1.00 53.26           C
ANISOU  212  C   TYR C  27     6923   6385   6929  -1012    758   -511       C
ATOM    213  O   TYR C  27      -6.013  26.927 -46.387  1.00 58.53           O
ANISOU  213  O   TYR C  27     7627   7039   7572  -1008    763   -490       O
ATOM    214  CB  TYR C  27      -7.788  28.194 -43.932  1.00 42.45           C
ANISOU  214  CB  TYR C  27     5618   4963   5549   -898    663   -393       C
ATOM    215  CG  TYR C  27      -8.503  27.011 -44.510  1.00 46.55           C
ANISOU  215  CG  TYR C  27     6117   5502   6069   -832    602   -349       C
ATOM    216  CD1 TYR C  27      -9.361  27.155 -45.594  1.00 44.45           C
ANISOU  216  CD1 TYR C  27     5953   5185   5750   -808    599   -293       C
ATOM    217  CD2 TYR C  27      -8.308  25.741 -43.990  1.00 51.13           C
ANISOU  217  CD2 TYR C  27     6582   6147   6697   -793    547   -368       C
ATOM    218  CE1 TYR C  27     -10.017  26.054 -46.134  1.00 50.99           C
ANISOU  218  CE1 TYR C  27     6758   6036   6581   -751    545   -259       C
ATOM    219  CE2 TYR C  27      -8.947  24.641 -44.530  1.00 52.06           C
ANISOU  219  CE2 TYR C  27     6687   6279   6814   -740    497   -331       C
ATOM    220  CZ  TYR C  27      -9.796  24.801 -45.604  1.00 51.01           C
ANISOU  220  CZ  TYR C  27     6645   6102   6634   -723    498   -279       C
ATOM    221  OH  TYR C  27     -10.441  23.703 -46.125  1.00 54.91           O
ANISOU  221  OH  TYR C  27     7120   6614   7128   -674    450   -249       O
ATOM    222  N   GLU C  28      -4.961  26.972 -44.404  1.00 53.37           N
ANISOU  222  N   GLU C  28     6813   6471   6995  -1019    746   -582       N
ATOM    223  CA  GLU C  28      -4.289  25.704 -44.595  1.00 56.10           C
ANISOU  223  CA  GLU C  28     7053   6886   7374  -1003    720   -632       C
ATOM    224  C   GLU C  28      -4.536  24.893 -43.340  1.00 47.00           C
ANISOU  224  C   GLU C  28     5806   5784   6266   -918    630   -625       C
ATOM    225  O   GLU C  28      -4.821  25.440 -42.278  1.00 58.31           O
ANISOU  225  O   GLU C  28     7234   7212   7710   -898    609   -612       O
ATOM    226  CB  GLU C  28      -2.781  25.880 -44.854  1.00 58.58           C
ANISOU  226  CB  GLU C  28     7307   7248   7701  -1095    798   -750       C
ATOM    227  CG  GLU C  28      -2.200  27.133 -44.199  1.00 80.89           C
ANISOU  227  CG  GLU C  28    10143  10066  10527  -1168    862   -805       C
ATOM    228  CD  GLU C  28      -0.677  27.193 -44.253  1.00 97.88           C
ANISOU  228  CD  GLU C  28    12204  12285  12700  -1256    932   -942       C
ATOM    229  OE1 GLU C  28      -0.104  27.031 -45.360  1.00104.17           O
ANISOU  229  OE1 GLU C  28    13016  13086  13479  -1319    993   -984       O
ATOM    230  OE2 GLU C  28      -0.057  27.412 -43.186  1.00 98.70           O
ANISOU  230  OE2 GLU C  28    12220  12443  12838  -1261    926  -1012       O
ATOM    231  N   GLU C  29      -4.443  23.585 -43.470  1.00 42.16           N
ANISOU  231  N   GLU C  29     5129   5216   5673   -866    579   -632       N
ATOM    232  CA  GLU C  29      -4.617  22.701 -42.337  1.00 42.50           C
ANISOU  232  CA  GLU C  29     5097   5301   5751   -785    497   -628       C
ATOM    233  C   GLU C  29      -3.265  22.189 -41.900  1.00 49.38           C
ANISOU  233  C   GLU C  29     5860   6250   6655   -790    497   -736       C
ATOM    234  O   GLU C  29      -2.380  21.959 -42.725  1.00 57.18           O
ANISOU  234  O   GLU C  29     6817   7268   7641   -835    540   -802       O
ATOM    235  CB  GLU C  29      -5.561  21.542 -42.659  1.00 38.14           C
ANISOU  235  CB  GLU C  29     4560   4739   5193   -714    434   -559       C
ATOM    236  CG  GLU C  29      -6.868  22.019 -43.247  1.00 41.40           C
ANISOU  236  CG  GLU C  29     5072   5087   5570   -707    434   -468       C
ATOM    237  CD  GLU C  29      -7.915  20.935 -43.359  1.00 54.51           C
ANISOU  237  CD  GLU C  29     6740   6744   7228   -639    369   -406       C
ATOM    238  OE1 GLU C  29      -8.210  20.290 -42.333  1.00 59.81           O
ANISOU  238  OE1 GLU C  29     7369   7435   7920   -585    313   -397       O
ATOM    239  OE2 GLU C  29      -8.452  20.737 -44.476  1.00 65.91           O
ANISOU  239  OE2 GLU C  29     8235   8162   8645   -641    378   -370       O
ATOM    240  N   LYS C  30      -3.107  22.067 -40.592  1.00 49.57           N
ANISOU  240  N   LYS C  30     5826   6307   6703   -742    450   -759       N
ATOM    241  CA  LYS C  30      -1.925  21.508 -39.957  1.00 46.29           C
ANISOU  241  CA  LYS C  30     5302   5970   6315   -719    428   -862       C
ATOM    242  C   LYS C  30      -2.368  20.172 -39.365  1.00 50.68           C
ANISOU  242  C   LYS C  30     5838   6539   6878   -613    336   -826       C
ATOM    243  O   LYS C  30      -2.947  20.125 -38.274  1.00 60.52           O
ANISOU  243  O   LYS C  30     7093   7774   8129   -558    285   -786       O
ATOM    244  CB  LYS C  30      -1.380  22.483 -38.914  1.00 44.77           C
ANISOU  244  CB  LYS C  30     5071   5803   6139   -746    448   -921       C
ATOM    245  CG  LYS C  30      -0.329  21.921 -37.974  1.00 46.56           C
ANISOU  245  CG  LYS C  30     5185   6115   6391   -697    405  -1024       C
ATOM    246  CD  LYS C  30       0.870  21.309 -38.696  1.00 46.34           C
ANISOU  246  CD  LYS C  30     5080   6157   6371   -715    426  -1132       C
ATOM    247  CE  LYS C  30       1.798  20.681 -37.653  1.00 51.70           C
ANISOU  247  CE  LYS C  30     5651   6922   7070   -639    364  -1234       C
ATOM    248  NZ  LYS C  30       2.640  19.597 -38.196  1.00 49.14           N
ANISOU  248  NZ  LYS C  30     5260   6661   6749   -601    341  -1313       N
ATOM    249  N   ILE C  31      -2.127  19.090 -40.103  1.00 54.22           N
ANISOU  249  N   ILE C  31     6271   7007   7323   -587    318   -840       N
ATOM    250  CA  ILE C  31      -2.635  17.774 -39.719  1.00 56.52           C
ANISOU  250  CA  ILE C  31     6567   7295   7612   -493    240   -798       C
ATOM    251  C   ILE C  31      -1.703  17.134 -38.700  1.00 60.70           C
ANISOU  251  C   ILE C  31     7019   7888   8155   -424    186   -882       C
ATOM    252  O   ILE C  31      -0.495  16.993 -38.943  1.00 59.46           O
ANISOU  252  O   ILE C  31     6788   7795   8009   -433    201   -987       O
ATOM    253  CB  ILE C  31      -2.804  16.871 -40.949  1.00 45.62           C
ANISOU  253  CB  ILE C  31     5210   5904   6218   -492    242   -776       C
ATOM    254  CG1 ILE C  31      -4.205  17.041 -41.530  1.00 47.82           C
ANISOU  254  CG1 ILE C  31     5578   6113   6477   -506    249   -665       C
ATOM    255  N   TYR C  32      -2.265  16.746 -37.553  1.00 60.95           N
ANISOU  255  N   TYR C  32     7070   7903   8184   -351    124   -840       N
ATOM    256  CA  TYR C  32      -1.611  15.858 -36.598  1.00 60.93           C
ANISOU  256  CA  TYR C  32     7024   7944   8181   -259     57   -899       C
ATOM    257  C   TYR C  32      -2.129  14.448 -36.809  1.00 61.25           C
ANISOU  257  C   TYR C  32     7114   7956   8201   -190      6   -850       C
ATOM    258  O   TYR C  32      -3.306  14.256 -37.115  1.00 57.40           O
ANISOU  258  O   TYR C  32     6699   7408   7701   -202      8   -753       O
ATOM    259  CB  TYR C  32      -1.856  16.303 -35.155  1.00 55.06           C
ANISOU  259  CB  TYR C  32     6284   7196   7439   -221     23   -888       C
ATOM    260  CG  TYR C  32      -1.349  17.693 -34.916  1.00 54.62           C
ANISOU  260  CG  TYR C  32     6182   7166   7403   -291     75   -939       C
ATOM    261  CD1 TYR C  32      -0.032  17.911 -34.527  1.00 55.56           C
ANISOU  261  CD1 TYR C  32     6209   7365   7537   -285     76  -1064       C
ATOM    262  CD2 TYR C  32      -2.166  18.796 -35.130  1.00 51.66           C
ANISOU  262  CD2 TYR C  32     5859   6740   7030   -364    126   -870       C
ATOM    263  CE1 TYR C  32       0.447  19.182 -34.335  1.00 53.32           C
ANISOU  263  CE1 TYR C  32     5884   7104   7269   -360    132  -1118       C
ATOM    264  CE2 TYR C  32      -1.692  20.075 -34.940  1.00 48.07           C
ANISOU  264  CE2 TYR C  32     5375   6302   6588   -433    179   -917       C
ATOM    265  CZ  TYR C  32      -0.392  20.257 -34.536  1.00 46.87           C
ANISOU  265  CZ  TYR C  32     5130   6225   6451   -435    185  -1040       C
ATOM    266  OH  TYR C  32       0.091  21.518 -34.346  1.00 42.43           O
ANISOU  266  OH  TYR C  32     4540   5680   5902   -512    245  -1094       O
ATOM    267  N   SER C  33      -1.241  13.469 -36.665  1.00 66.32           N
ANISOU  267  N   SER C  33     7717   8644   8837   -118    -40   -923       N
ATOM    268  CA  SER C  33      -1.564  12.071 -36.916  1.00 66.87           C
ANISOU  268  CA  SER C  33     7837   8686   8882    -51    -85   -890       C
ATOM    269  C   SER C  33      -1.333  11.264 -35.649  1.00 65.83           C
ANISOU  269  C   SER C  33     7724   8560   8730     61   -162   -913       C
ATOM    270  O   SER C  33      -0.273  11.355 -35.027  1.00 70.88           O
ANISOU  270  O   SER C  33     8297   9262   9372    109   -191  -1010       O
ATOM    271  CB  SER C  33      -0.730  11.509 -38.069  1.00 72.03           C
ANISOU  271  CB  SER C  33     8448   9382   9540    -58    -70   -955       C
ATOM    272  OG  SER C  33      -1.036  12.165 -39.291  1.00 74.31           O
ANISOU  272  OG  SER C  33     8739   9654   9839   -159      1   -924       O
ATOM    273  N   MET C  34      -2.329  10.480 -35.272  1.00 70.50           N
ANISOU  273  N   MET C  34     8407   9085   9294    100   -194   -829       N
ATOM    274  CA  MET C  34      -2.280   9.694 -34.054  1.00 69.19           C
ANISOU  274  CA  MET C  34     8289   8904   9096    203   -262   -834       C
ATOM    275  C   MET C  34      -1.719   8.316 -34.361  1.00 68.56           C
ANISOU  275  C   MET C  34     8233   8829   8986    287   -308   -874       C
ATOM    276  O   MET C  34      -2.148   7.666 -35.318  1.00 80.68           O
ANISOU  276  O   MET C  34     9806  10333  10515    263   -291   -834       O
ATOM    277  CB  MET C  34      -3.678   9.571 -33.446  1.00 72.79           C
ANISOU  277  CB  MET C  34     8843   9281   9533    193   -263   -726       C
ATOM    278  CG  MET C  34      -3.745   8.763 -32.159  1.00 72.82           C
ANISOU  278  CG  MET C  34     8919   9254   9495    291   -325   -722       C
ATOM    279  SD  MET C  34      -5.318   9.011 -31.338  1.00 65.74           S
ANISOU  279  SD  MET C  34     8113   8280   8584    253   -308   -613       S
ATOM    280  CE  MET C  34      -5.040  10.625 -30.627  1.00 62.03           C
ANISOU  280  CE  MET C  34     7562   7854   8151    216   -291   -639       C
ATOM    281  N   GLY C  35      -0.762   7.875 -33.550  1.00 61.01           N
ANISOU  281  N   GLY C  35     7257   7913   8009    391   -369   -957       N
ATOM    282  CA  GLY C  35      -0.252   6.526 -33.707  1.00 66.61           C
ANISOU  282  CA  GLY C  35     8005   8621   8681    489   -423   -996       C
ATOM    283  C   GLY C  35      -1.336   5.497 -33.442  1.00 77.33           C
ANISOU  283  C   GLY C  35     9505   9881   9995    518   -441   -898       C
ATOM    284  O   GLY C  35      -2.147   5.642 -32.525  1.00 74.43           O
ANISOU  284  O   GLY C  35     9209   9461   9611    518   -445   -833       O
ATOM    285  N   ASP C  36      -1.360   4.456 -34.271  1.00 89.74           N
ANISOU  285  N   ASP C  36    11120  11430  11547    537   -446   -889       N
ATOM    286  CA  ASP C  36      -2.255   3.333 -34.027  1.00 95.84           C
ANISOU  286  CA  ASP C  36    12034  12111  12271    570   -462   -813       C
ATOM    287  C   ASP C  36      -1.624   2.412 -32.991  1.00 93.18           C
ANISOU  287  C   ASP C  36    11770  11759  11874    713   -541   -861       C
ATOM    288  O   ASP C  36      -0.994   2.896 -32.044  1.00 90.99           O
ANISOU  288  O   ASP C  36    11454  11523  11593    772   -579   -917       O
ATOM    289  CB  ASP C  36      -2.574   2.588 -35.329  1.00101.51           C
ANISOU  289  CB  ASP C  36    12776  12805  12989    530   -434   -784       C
ATOM    290  CG  ASP C  36      -1.337   2.085 -36.035  1.00105.57           C
ANISOU  290  CG  ASP C  36    13227  13382  13504    590   -463   -880       C
ATOM    291  OD1 ASP C  36      -0.741   2.853 -36.822  1.00104.74           O
ANISOU  291  OD1 ASP C  36    13004  13348  13444    533   -430   -931       O
ATOM    292  OD2 ASP C  36      -0.965   0.918 -35.806  1.00108.88           O
ANISOU  292  OD2 ASP C  36    13719  13776  13873    693   -517   -907       O
ATOM    293  N   ALA C  37      -1.791   1.092 -33.151  1.00 96.52           N
ANISOU  293  N   ALA C  37    12306  12123  12246    773   -567   -842       N
ATOM    294  CA  ALA C  37      -1.200   0.096 -32.257  1.00 96.35           C
ANISOU  294  CA  ALA C  37    12380  12075  12155    921   -645   -886       C
ATOM    295  C   ALA C  37      -1.918   0.179 -30.911  1.00 88.45           C
ANISOU  295  C   ALA C  37    11485  11006  11116    939   -655   -828       C
ATOM    296  O   ALA C  37      -3.002   0.775 -30.848  1.00 83.61           O
ANISOU  296  O   ALA C  37    10883  10358  10529    831   -597   -747       O
ATOM    297  CB  ALA C  37       0.318   0.314 -32.138  1.00 95.31           C
ANISOU  297  CB  ALA C  37    12134  12047  12031   1018   -704  -1018       C
ATOM    298  N   PRO C  38      -1.409  -0.437 -29.832  1.00 83.29           N
ANISOU  298  N   PRO C  38    10921  10329  10396   1074   -727   -866       N
ATOM    299  CA  PRO C  38      -1.949  -0.095 -28.506  1.00 80.14           C
ANISOU  299  CA  PRO C  38    10596   9883   9968   1086   -734   -825       C
ATOM    300  C   PRO C  38      -1.578   1.303 -28.048  1.00 81.07           C
ANISOU  300  C   PRO C  38    10575  10085  10143   1054   -730   -863       C
ATOM    301  O   PRO C  38      -2.356   1.919 -27.312  1.00 77.51           O
ANISOU  301  O   PRO C  38    10151   9601   9698   1000   -702   -805       O
ATOM    302  CB  PRO C  38      -1.341  -1.162 -27.587  1.00 83.18           C
ANISOU  302  CB  PRO C  38    11117  10227  10262   1255   -818   -868       C
ATOM    303  CG  PRO C  38      -1.013  -2.290 -28.480  1.00 75.64           C
ANISOU  303  CG  PRO C  38    10211   9251   9277   1302   -835   -888       C
ATOM    304  CD  PRO C  38      -0.630  -1.693 -29.782  1.00 77.19           C
ANISOU  304  CD  PRO C  38    10234   9539   9556   1219   -798   -924       C
ATOM    305  N   ASP C  39      -0.411   1.819 -28.435  1.00 95.72           N
ANISOU  305  N   ASP C  39    12284  12048  12038   1084   -754   -966       N
ATOM    306  CA  ASP C  39       0.015   3.158 -28.018  1.00105.64           C
ANISOU  306  CA  ASP C  39    13406  13386  13347   1049   -745  -1014       C
ATOM    307  C   ASP C  39      -0.593   4.166 -28.980  1.00107.29           C
ANISOU  307  C   ASP C  39    13521  13613  13630    886   -656   -964       C
ATOM    308  O   ASP C  39      -0.011   4.508 -30.015  1.00114.11           O
ANISOU  308  O   ASP C  39    14273  14544  14538    839   -630  -1016       O
ATOM    309  CB  ASP C  39       1.533   3.278 -27.989  1.00109.67           C
ANISOU  309  CB  ASP C  39    13798  14008  13863   1145   -803  -1159       C
ATOM    310  CG  ASP C  39       2.204   2.047 -27.444  1.00114.46           C
ANISOU  310  CG  ASP C  39    14501  14599  14390   1319   -896  -1217       C
ATOM    311  OD1 ASP C  39       2.115   0.988 -28.102  1.00113.14           O
ANISOU  311  OD1 ASP C  39    14411  14387  14191   1350   -904  -1198       O
ATOM    312  OD2 ASP C  39       2.828   2.144 -26.364  1.00119.10           O
ANISOU  312  OD2 ASP C  39    15089  15220  14945   1430   -962  -1284       O
ATOM    313  N   TYR C  40      -1.780   4.654 -28.642  1.00 94.36           N
ANISOU  313  N   TYR C  40    11934  11916  12002    800   -610   -866       N
ATOM    314  CA  TYR C  40      -2.417   5.681 -29.457  1.00 86.11           C
ANISOU  314  CA  TYR C  40    10813  10885  11020    658   -532   -818       C
ATOM    315  C   TYR C  40      -1.598   6.952 -29.288  1.00 84.75           C
ANISOU  315  C   TYR C  40    10503  10803  10896    634   -525   -893       C
ATOM    316  O   TYR C  40      -1.959   7.877 -28.556  1.00 82.46           O
ANISOU  316  O   TYR C  40    10197  10512  10623    598   -509   -870       O
ATOM    317  CB  TYR C  40      -3.867   5.858 -29.054  1.00 83.87           C
ANISOU  317  CB  TYR C  40    10616  10522  10730    587   -493   -708       C
ATOM    318  CG  TYR C  40      -4.696   4.652 -29.400  1.00 79.60           C
ANISOU  318  CG  TYR C  40    10198   9899  10146    585   -484   -642       C
ATOM    319  CD1 TYR C  40      -4.874   4.274 -30.720  1.00 72.42           C
ANISOU  319  CD1 TYR C  40     9272   8989   9255    532   -451   -627       C
ATOM    320  CD2 TYR C  40      -5.281   3.876 -28.409  1.00 80.69           C
ANISOU  320  CD2 TYR C  40    10477   9958  10224    634   -506   -600       C
ATOM    321  CE1 TYR C  40      -5.625   3.178 -31.050  1.00 69.37           C
ANISOU  321  CE1 TYR C  40     8996   8531   8831    526   -440   -573       C
ATOM    322  CE2 TYR C  40      -6.036   2.768 -28.734  1.00 81.07           C
ANISOU  322  CE2 TYR C  40    10643   9929  10230    622   -489   -546       C
ATOM    323  CZ  TYR C  40      -6.206   2.429 -30.059  1.00 76.50           C
ANISOU  323  CZ  TYR C  40    10036   9356   9675    567   -456   -534       C
ATOM    324  OH  TYR C  40      -6.952   1.327 -30.398  1.00 83.76           O
ANISOU  324  OH  TYR C  40    11070  10200  10553    550   -437   -487       O
ATOM    325  N   ASP C  41      -0.462   6.980 -29.984  1.00 84.09           N
ANISOU  325  N   ASP C  41    10319  10798  10833    653   -533   -991       N
ATOM    326  CA  ASP C  41       0.602   7.933 -29.693  1.00 81.97           C
ANISOU  326  CA  ASP C  41     9923  10626  10597    657   -538  -1096       C
ATOM    327  C   ASP C  41       0.235   9.317 -30.204  1.00 82.78           C
ANISOU  327  C   ASP C  41     9951  10745  10757    517   -458  -1068       C
ATOM    328  O   ASP C  41      -0.036   9.496 -31.399  1.00 83.17           O
ANISOU  328  O   ASP C  41     9979  10788  10833    428   -401  -1039       O
ATOM    329  CB  ASP C  41       1.917   7.473 -30.309  1.00 79.43           C
ANISOU  329  CB  ASP C  41     9516  10388  10277    716   -568  -1220       C
ATOM    330  CG  ASP C  41       3.080   8.313 -29.855  1.00 80.26           C
ANISOU  330  CG  ASP C  41     9490  10600  10407    734   -581  -1349       C
ATOM    331  OD1 ASP C  41       3.482   8.190 -28.678  1.00 80.54           O
ANISOU  331  OD1 ASP C  41     9537  10654  10412    838   -647  -1397       O
ATOM    332  OD2 ASP C  41       3.585   9.108 -30.672  1.00 81.88           O
ANISOU  332  OD2 ASP C  41     9584  10869  10659    642   -523  -1405       O
ATOM    333  N   ARG C  42       0.251  10.293 -29.297  1.00 75.01           N
ANISOU  333  N   ARG C  42     8933   9780   9788    501   -454  -1080       N
ATOM    334  CA  ARG C  42      -0.122  11.668 -29.592  1.00 71.45           C
ANISOU  334  CA  ARG C  42     8428   9335   9383    378   -381  -1052       C
ATOM    335  C   ARG C  42       1.085  12.586 -29.709  1.00 73.41           C
ANISOU  335  C   ARG C  42     8545   9680   9666    348   -360  -1174       C
ATOM    336  O   ARG C  42       0.917  13.807 -29.808  1.00 73.63           O
ANISOU  336  O   ARG C  42     8533   9716   9727    251   -300  -1165       O
ATOM    337  CB  ARG C  42      -1.082  12.181 -28.514  1.00 71.09           C
ANISOU  337  CB  ARG C  42     8446   9236   9331    369   -383   -973       C
ATOM    338  CG  ARG C  42      -2.341  11.336 -28.397  1.00 63.29           C
ANISOU  338  CG  ARG C  42     7585   8154   8309    381   -392   -859       C
ATOM    339  CD  ARG C  42      -3.160  11.604 -27.151  1.00 58.63           C
ANISOU  339  CD  ARG C  42     7061   7515   7700    395   -406   -798       C
ATOM    340  NE  ARG C  42      -4.356  10.759 -27.154  1.00 68.59           N
ANISOU  340  NE  ARG C  42     8440   8693   8929    391   -403   -701       N
ATOM    341  CZ  ARG C  42      -5.612  11.206 -27.243  1.00 64.36           C
ANISOU  341  CZ  ARG C  42     7943   8109   8404    311   -358   -612       C
ATOM    342  NH1 ARG C  42      -5.861  12.507 -27.319  1.00 55.17           N
ANISOU  342  NH1 ARG C  42     6717   6964   7279    236   -317   -601       N
ATOM    343  NH2 ARG C  42      -6.625  10.343 -27.249  1.00 67.07           N
ANISOU  343  NH2 ARG C  42     8386   8383   8715    308   -354   -541       N
ATOM    344  N   SER C  43       2.298  12.025 -29.709  1.00 70.59           N
ANISOU  344  N   SER C  43     8122   9399   9299    428   -405  -1294       N
ATOM    345  CA  SER C  43       3.502  12.839 -29.615  1.00 72.23           C
ANISOU  345  CA  SER C  43     8198   9711   9535    409   -390  -1431       C
ATOM    346  C   SER C  43       3.611  13.833 -30.755  1.00 64.79           C
ANISOU  346  C   SER C  43     7191   8790   8636    262   -292  -1443       C
ATOM    347  O   SER C  43       4.293  14.850 -30.613  1.00 69.13           O
ANISOU  347  O   SER C  43     7649   9403   9213    204   -253  -1529       O
ATOM    348  CB  SER C  43       4.743  11.942 -29.584  1.00 84.35           C
ANISOU  348  CB  SER C  43     9671  11330  11049    523   -457  -1565       C
ATOM    349  OG  SER C  43       4.924  11.265 -30.821  1.00 85.48           O
ANISOU  349  OG  SER C  43     9809  11476  11193    506   -438  -1572       O
ATOM    350  N   GLN C  44       2.949  13.571 -31.880  1.00 57.45           N
ANISOU  350  N   GLN C  44     6314   7804   7709    200   -249  -1361       N
ATOM    351  CA  GLN C  44       3.019  14.507 -32.992  1.00 59.83           C
ANISOU  351  CA  GLN C  44     6574   8115   8043     64   -155  -1367       C
ATOM    352  C   GLN C  44       2.421  15.851 -32.623  1.00 61.69           C
ANISOU  352  C   GLN C  44     6825   8316   8297    -25   -101  -1314       C
ATOM    353  O   GLN C  44       2.865  16.892 -33.119  1.00 59.23           O
ANISOU  353  O   GLN C  44     6460   8035   8010   -126    -27  -1365       O
ATOM    354  CB  GLN C  44       2.312  13.926 -34.204  1.00 61.46           C
ANISOU  354  CB  GLN C  44     6847   8262   8243     27   -128  -1280       C
ATOM    355  CG  GLN C  44       2.781  14.548 -35.490  1.00 62.36           C
ANISOU  355  CG  GLN C  44     6909   8405   8379    -84    -45  -1325       C
ATOM    356  CD  GLN C  44       2.351  13.751 -36.668  1.00 64.73           C
ANISOU  356  CD  GLN C  44     7259   8667   8668    -96    -34  -1267       C
ATOM    357  OE1 GLN C  44       2.455  12.532 -36.665  1.00 66.64           O
ANISOU  357  OE1 GLN C  44     7519   8910   8890     -6    -93  -1272       O
ATOM    358  NE2 GLN C  44       1.843  14.428 -37.686  1.00 68.96           N
ANISOU  358  NE2 GLN C  44     7826   9163   9213   -203     42  -1212       N
ATOM    359  N   TRP C  45       1.422  15.843 -31.750  1.00 66.38           N
ANISOU  359  N   TRP C  45     7497   8847   8878     11   -134  -1216       N
ATOM    360  CA  TRP C  45       0.793  17.035 -31.211  1.00 55.14           C
ANISOU  360  CA  TRP C  45     6094   7389   7468    -53    -97  -1164       C
ATOM    361  C   TRP C  45       1.314  17.388 -29.830  1.00 58.53           C
ANISOU  361  C   TRP C  45     6478   7862   7898      3   -139  -1229       C
ATOM    362  O   TRP C  45       1.485  18.572 -29.523  1.00 66.86           O
ANISOU  362  O   TRP C  45     7496   8935   8974    -63    -95  -1258       O
ATOM    363  CB  TRP C  45      -0.719  16.825 -31.170  1.00 47.68           C
ANISOU  363  CB  TRP C  45     5261   6348   6508    -55   -103  -1018       C
ATOM    364  CG  TRP C  45      -1.440  17.572 -30.117  1.00 52.20           C
ANISOU  364  CG  TRP C  45     5867   6886   7081    -60   -107   -963       C
ATOM    365  CD1 TRP C  45      -2.050  17.051 -29.009  1.00 52.52           C
ANISOU  365  CD1 TRP C  45     5964   6893   7100     16   -165   -913       C
ATOM    366  CD2 TRP C  45      -1.672  18.982 -30.079  1.00 50.83           C
ANISOU  366  CD2 TRP C  45     5683   6702   6927   -147    -49   -950       C
ATOM    367  NE1 TRP C  45      -2.632  18.058 -28.277  1.00 52.10           N
ANISOU  367  NE1 TRP C  45     5925   6816   7055    -18   -148   -873       N
ATOM    368  CE2 TRP C  45      -2.419  19.252 -28.916  1.00 50.94           C
ANISOU  368  CE2 TRP C  45     5739   6682   6934   -115    -79   -894       C
ATOM    369  CE3 TRP C  45      -1.312  20.043 -30.907  1.00 52.09           C
ANISOU  369  CE3 TRP C  45     5812   6874   7106   -250     29   -982       C
ATOM    370  CZ2 TRP C  45      -2.815  20.536 -28.568  1.00 48.64           C
ANISOU  370  CZ2 TRP C  45     5453   6372   6657   -177    -38   -869       C
ATOM    371  CZ3 TRP C  45      -1.703  21.321 -30.553  1.00 52.95           C
ANISOU  371  CZ3 TRP C  45     5936   6957   7224   -312     71   -956       C
ATOM    372  CH2 TRP C  45      -2.442  21.555 -29.393  1.00 44.93           C
ANISOU  372  CH2 TRP C  45     4956   5911   6204   -273     35   -900       C
ATOM    373  N   LEU C  46       1.596  16.377 -29.001  1.00 54.13           N
ANISOU  373  N   LEU C  46     5931   7323   7314    127   -223  -1257       N
ATOM    374  CA  LEU C  46       2.171  16.607 -27.681  1.00 47.85           C
ANISOU  374  CA  LEU C  46     5093   6575   6513    198   -273  -1329       C
ATOM    375  C   LEU C  46       3.519  17.337 -27.739  1.00 53.05           C
ANISOU  375  C   LEU C  46     5618   7340   7198    164   -246  -1484       C
ATOM    376  O   LEU C  46       3.893  17.999 -26.766  1.00 59.44           O
ANISOU  376  O   LEU C  46     6381   8190   8015    178   -259  -1541       O
ATOM    377  CB  LEU C  46       2.287  15.265 -26.956  1.00 48.18           C
ANISOU  377  CB  LEU C  46     5183   6611   6510    346   -370  -1336       C
ATOM    378  CG  LEU C  46       0.954  14.799 -26.361  1.00 54.14           C
ANISOU  378  CG  LEU C  46     6070   7264   7235    376   -395  -1198       C
ATOM    379  CD1 LEU C  46       1.086  13.603 -25.401  1.00 44.30           C
ANISOU  379  CD1 LEU C  46     4892   6003   5935    523   -487  -1207       C
ATOM    380  CD2 LEU C  46       0.258  15.984 -25.663  1.00 50.47           C
ANISOU  380  CD2 LEU C  46     5617   6770   6790    311   -360  -1142       C
ATOM    381  N   SER C  47       4.238  17.250 -28.862  1.00 58.96           N
ANISOU  381  N   SER C  47     6303   8137   7961    115   -205  -1556       N
ATOM    382  CA  SER C  47       5.455  18.035 -29.069  1.00 60.93           C
ANISOU  382  CA  SER C  47     6425   8487   8238     53   -158  -1707       C
ATOM    383  C   SER C  47       5.147  19.516 -29.230  1.00 67.62           C
ANISOU  383  C   SER C  47     7270   9308   9112    -88    -63  -1681       C
ATOM    384  O   SER C  47       5.789  20.363 -28.600  1.00 82.67           O
ANISOU  384  O   SER C  47     9102  11274  11034   -117    -44  -1774       O
ATOM    385  CB  SER C  47       6.188  17.545 -30.311  1.00 59.63           C
ANISOU  385  CB  SER C  47     6205   8372   8079     25   -129  -1782       C
ATOM    386  OG  SER C  47       6.079  16.152 -30.431  1.00 75.39           O
ANISOU  386  OG  SER C  47     8247  10353  10047    139   -204  -1755       O
ATOM    387  N   GLU C  48       4.192  19.849 -30.104  1.00 53.37           N
ANISOU  387  N   GLU C  48     5551   7418   7311   -175     -3  -1561       N
ATOM    388  CA  GLU C  48       3.886  21.230 -30.464  1.00 54.87           C
ANISOU  388  CA  GLU C  48     5758   7572   7518   -309     92  -1533       C
ATOM    389  C   GLU C  48       2.972  21.949 -29.469  1.00 59.83           C
ANISOU  389  C   GLU C  48     6447   8140   8144   -308     82  -1444       C
ATOM    390  O   GLU C  48       2.881  23.183 -29.528  1.00 62.80           O
ANISOU  390  O   GLU C  48     6831   8498   8534   -406    154  -1443       O
ATOM    391  CB  GLU C  48       3.224  21.261 -31.842  1.00 60.23           C
ANISOU  391  CB  GLU C  48     6510   8182   8192   -389    154  -1445       C
ATOM    392  CG  GLU C  48       4.026  21.967 -32.911  1.00 65.21           C
ANISOU  392  CG  GLU C  48     7094   8847   8834   -511    252  -1531       C
ATOM    393  CD  GLU C  48       3.534  21.648 -34.303  1.00 62.82           C
ANISOU  393  CD  GLU C  48     6859   8490   8521   -559    293  -1459       C
ATOM    394  OE1 GLU C  48       2.334  21.853 -34.567  1.00 61.50           O
ANISOU  394  OE1 GLU C  48     6796   8231   8340   -574    301  -1324       O
ATOM    395  OE2 GLU C  48       4.347  21.191 -35.132  1.00 65.70           O
ANISOU  395  OE2 GLU C  48     7169   8908   8888   -579    315  -1541       O
ATOM    396  N   LYS C  49       2.333  21.220 -28.546  1.00 51.57           N
ANISOU  396  N   LYS C  49     5450   7064   7081   -200     -1  -1376       N
ATOM    397  CA  LYS C  49       1.104  21.698 -27.910  1.00 38.90           C
ANISOU  397  CA  LYS C  49     3932   5379   5471   -204     -6  -1254       C
ATOM    398  C   LYS C  49       1.331  22.950 -27.071  1.00 46.87           C
ANISOU  398  C   LYS C  49     4906   6407   6496   -249     23  -1295       C
ATOM    399  O   LYS C  49       0.496  23.861 -27.074  1.00 48.63           O
ANISOU  399  O   LYS C  49     5188   6567   6721   -314     66  -1215       O
ATOM    400  CB  LYS C  49       0.512  20.577 -27.064  1.00 41.97           C
ANISOU  400  CB  LYS C  49     4376   5738   5832    -83    -97  -1192       C
ATOM    401  CG  LYS C  49      -0.342  21.024 -25.924  1.00 44.10           C
ANISOU  401  CG  LYS C  49     4699   5962   6096    -61   -120  -1120       C
ATOM    402  CD  LYS C  49      -1.137  19.844 -25.380  1.00 47.66           C
ANISOU  402  CD  LYS C  49     5232   6364   6514     35   -189  -1039       C
ATOM    403  CE  LYS C  49      -1.961  20.211 -24.136  1.00 44.72           C
ANISOU  403  CE  LYS C  49     4911   5949   6131     61   -214   -975       C
ATOM    404  NZ  LYS C  49      -2.922  19.121 -23.857  1.00 47.57           N
ANISOU  404  NZ  LYS C  49     5369   6247   6458    123   -258   -884       N
ATOM    405  N   PHE C  50       2.457  23.029 -26.362  1.00 52.02           N
ANISOU  405  N   PHE C  50     5461   7148   7156   -214     -1  -1425       N
ATOM    406  CA  PHE C  50       2.780  24.193 -25.546  1.00 48.56           C
ANISOU  406  CA  PHE C  50     4980   6737   6734   -258     27  -1480       C
ATOM    407  C   PHE C  50       3.637  25.228 -26.276  1.00 50.06           C
ANISOU  407  C   PHE C  50     5103   6971   6946   -387    126  -1581       C
ATOM    408  O   PHE C  50       4.001  26.244 -25.670  1.00 51.29           O
ANISOU  408  O   PHE C  50     5219   7153   7115   -437    160  -1641       O
ATOM    409  CB  PHE C  50       3.435  23.731 -24.242  1.00 47.51           C
ANISOU  409  CB  PHE C  50     4783   6674   6592   -143    -58  -1565       C
ATOM    410  CG  PHE C  50       2.530  22.853 -23.437  1.00 50.57           C
ANISOU  410  CG  PHE C  50     5257   7005   6951    -30   -143  -1461       C
ATOM    411  CD1 PHE C  50       1.453  23.398 -22.753  1.00 45.67           C
ANISOU  411  CD1 PHE C  50     4713   6313   6328    -42   -141  -1354       C
ATOM    412  CD2 PHE C  50       2.688  21.474 -23.445  1.00 52.93           C
ANISOU  412  CD2 PHE C  50     5573   7314   7223     80   -216  -1465       C
ATOM    413  CE1 PHE C  50       0.575  22.577 -22.060  1.00 45.74           C
ANISOU  413  CE1 PHE C  50     4807   6266   6307     48   -208  -1259       C
ATOM    414  CE2 PHE C  50       1.821  20.652 -22.753  1.00 42.20           C
ANISOU  414  CE2 PHE C  50     4310   5891   5831    172   -282  -1367       C
ATOM    415  CZ  PHE C  50       0.763  21.196 -22.072  1.00 41.67           C
ANISOU  415  CZ  PHE C  50     4314   5757   5762    151   -275  -1266       C
ATOM    416  N   LYS C  51       3.888  25.036 -27.576  1.00 47.59           N
ANISOU  416  N   LYS C  51     4791   6657   6635   -449    179  -1595       N
ATOM    417  CA  LYS C  51       4.727  25.925 -28.372  1.00 48.74           C
ANISOU  417  CA  LYS C  51     4884   6840   6794   -579    281  -1695       C
ATOM    418  C   LYS C  51       3.930  26.788 -29.340  1.00 47.91           C
ANISOU  418  C   LYS C  51     4885   6638   6682   -695    372  -1595       C
ATOM    419  O   LYS C  51       4.517  27.394 -30.237  1.00 44.15           O
ANISOU  419  O   LYS C  51     4395   6174   6208   -808    464  -1660       O
ATOM    420  CB  LYS C  51       5.771  25.116 -29.151  1.00 47.53           C
ANISOU  420  CB  LYS C  51     4646   6770   6645   -570    282  -1809       C
ATOM    421  CG  LYS C  51       6.749  24.380 -28.255  1.00 51.76           C
ANISOU  421  CG  LYS C  51     5068   7417   7184   -456    197  -1939       C
ATOM    422  CD  LYS C  51       8.005  23.996 -28.990  1.00 59.54           C
ANISOU  422  CD  LYS C  51     5942   8505   8177   -479    221  -2095       C
ATOM    423  CE  LYS C  51       8.415  22.568 -28.695  1.00 60.62           C
ANISOU  423  CE  LYS C  51     6035   8701   8299   -322    110  -2140       C
ATOM    424  NZ  LYS C  51       8.918  21.926 -29.931  1.00 63.00           N
ANISOU  424  NZ  LYS C  51     6304   9033   8599   -347    137  -2189       N
ATOM    425  N   LEU C  52       2.619  26.894 -29.157  1.00 48.35           N
ANISOU  425  N   LEU C  52     5048   6599   6725   -669    348  -1445       N
ATOM    426  CA  LEU C  52       1.740  27.491 -30.154  1.00 46.88           C
ANISOU  426  CA  LEU C  52     4972   6317   6522   -748    414  -1341       C
ATOM    427  C   LEU C  52       1.074  28.773 -29.670  1.00 48.47           C
ANISOU  427  C   LEU C  52     5242   6455   6718   -800    453  -1283       C
ATOM    428  O   LEU C  52       0.184  29.290 -30.361  1.00 45.01           O
ANISOU  428  O   LEU C  52     4911   5932   6261   -844    493  -1185       O
ATOM    429  CB  LEU C  52       0.677  26.469 -30.582  1.00 41.78           C
ANISOU  429  CB  LEU C  52     4398   5615   5860   -674    356  -1216       C
ATOM    430  CG  LEU C  52       1.282  25.285 -31.363  1.00 49.41           C
ANISOU  430  CG  LEU C  52     5318   6628   6826   -641    335  -1264       C
ATOM    431  CD1 LEU C  52       0.325  24.066 -31.473  1.00 50.89           C
ANISOU  431  CD1 LEU C  52     5563   6774   7000   -547    260  -1157       C
ATOM    432  CD2 LEU C  52       1.689  25.749 -32.738  1.00 44.39           C
ANISOU  432  CD2 LEU C  52     4698   5982   6185   -751    429  -1296       C
ATOM    433  N   GLY C  53       1.480  29.289 -28.505  1.00 46.24           N
ANISOU  433  N   GLY C  53     4904   6214   6451   -789    439  -1344       N
ATOM    434  CA  GLY C  53       0.919  30.506 -27.942  1.00 44.91           C
ANISOU  434  CA  GLY C  53     4795   5991   6279   -834    473  -1299       C
ATOM    435  C   GLY C  53      -0.562  30.443 -27.651  1.00 50.12           C
ANISOU  435  C   GLY C  53     5553   6566   6923   -774    424  -1148       C
ATOM    436  O   GLY C  53      -1.221  31.487 -27.597  1.00 51.37           O
ANISOU  436  O   GLY C  53     5790   6659   7071   -821    464  -1090       O
ATOM    437  N   LEU C  54      -1.112  29.242 -27.500  1.00 48.00           N
ANISOU  437  N   LEU C  54     5288   6297   6652   -675    343  -1087       N
ATOM    438  CA  LEU C  54      -2.527  29.071 -27.205  1.00 49.75           C
ANISOU  438  CA  LEU C  54     5594   6450   6859   -620    297   -956       C
ATOM    439  C   LEU C  54      -2.761  29.167 -25.697  1.00 54.66           C
ANISOU  439  C   LEU C  54     6194   7087   7489   -557    240   -951       C
ATOM    440  O   LEU C  54      -1.962  28.673 -24.896  1.00 55.58           O
ANISOU  440  O   LEU C  54     6231   7271   7616   -505    196  -1030       O
ATOM    441  CB  LEU C  54      -3.013  27.719 -27.742  1.00 40.41           C
ANISOU  441  CB  LEU C  54     4429   5258   5666   -554    245   -899       C
ATOM    442  CG  LEU C  54      -2.734  27.451 -29.218  1.00 43.59           C
ANISOU  442  CG  LEU C  54     4848   5654   6062   -606    292   -907       C
ATOM    443  CD1 LEU C  54      -3.006  25.994 -29.625  1.00 39.74           C
ANISOU  443  CD1 LEU C  54     4361   5172   5567   -534    235   -872       C
ATOM    444  CD2 LEU C  54      -3.577  28.395 -30.042  1.00 49.27           C
ANISOU  444  CD2 LEU C  54     5665   6294   6760   -672    351   -830       C
ATOM    445  N   ASP C  55      -3.866  29.814 -25.319  1.00 47.32           N
ANISOU  445  N   ASP C  55     5336   6094   6549   -558    238   -861       N
ATOM    446  CA  ASP C  55      -4.204  30.004 -23.907  1.00 31.48           C
ANISOU  446  CA  ASP C  55     3319   4094   4548   -505    191   -848       C
ATOM    447  C   ASP C  55      -4.551  28.684 -23.215  1.00 48.17           C
ANISOU  447  C   ASP C  55     5424   6223   6655   -400    104   -817       C
ATOM    448  O   ASP C  55      -4.142  28.438 -22.072  1.00 48.85           O
ANISOU  448  O   ASP C  55     5466   6351   6745   -343     57   -861       O
ATOM    449  CB  ASP C  55      -5.382  30.962 -23.801  1.00 36.05           C
ANISOU  449  CB  ASP C  55     3982   4600   5114   -529    211   -758       C
ATOM    450  CG  ASP C  55      -5.010  32.370 -24.152  1.00 50.22           C
ANISOU  450  CG  ASP C  55     5799   6373   6909   -624    292   -793       C
ATOM    451  OD1 ASP C  55      -3.971  32.859 -23.645  1.00 49.65           O
ANISOU  451  OD1 ASP C  55     5662   6349   6853   -658    317   -890       O
ATOM    452  OD2 ASP C  55      -5.757  32.981 -24.946  1.00 49.05           O
ANISOU  452  OD2 ASP C  55     5737   6159   6741   -662    331   -728       O
ATOM    453  N   PHE C  56      -5.378  27.859 -23.850  1.00 52.10           N
ANISOU  453  N   PHE C  56     5974   6683   7138   -374     84   -739       N
ATOM    454  CA  PHE C  56      -5.711  26.531 -23.337  1.00 49.66           C
ANISOU  454  CA  PHE C  56     5672   6379   6816   -285     13   -710       C
ATOM    455  C   PHE C  56      -5.437  25.549 -24.463  1.00 47.91           C
ANISOU  455  C   PHE C  56     5449   6165   6588   -280     14   -716       C
ATOM    456  O   PHE C  56      -6.354  25.176 -25.204  1.00 57.02           O
ANISOU  456  O   PHE C  56     6661   7274   7730   -287     19   -639       O
ATOM    457  CB  PHE C  56      -7.167  26.430 -22.880  1.00 34.73           C
ANISOU  457  CB  PHE C  56     3854   4433   4910   -259    -12   -607       C
ATOM    458  CG  PHE C  56      -7.566  27.432 -21.855  1.00 41.73           C
ANISOU  458  CG  PHE C  56     4748   5307   5801   -266    -10   -593       C
ATOM    459  CD1 PHE C  56      -8.162  28.629 -22.233  1.00 45.95           C
ANISOU  459  CD1 PHE C  56     5319   5803   6337   -326     38   -556       C
ATOM    460  CD2 PHE C  56      -7.402  27.170 -20.498  1.00 48.08           C
ANISOU  460  CD2 PHE C  56     5534   6134   6601   -206    -58   -614       C
ATOM    461  CE1 PHE C  56      -8.553  29.577 -21.265  1.00 41.78           C
ANISOU  461  CE1 PHE C  56     4800   5262   5812   -330     39   -544       C
ATOM    462  CE2 PHE C  56      -7.799  28.109 -19.538  1.00 35.20           C
ANISOU  462  CE2 PHE C  56     3910   4490   4974   -213    -56   -600       C
ATOM    463  CZ  PHE C  56      -8.373  29.306 -19.932  1.00 33.00           C
ANISOU  463  CZ  PHE C  56     3661   4176   4701   -277     -7   -566       C
ATOM    464  N   PRO C  57      -4.194  25.102 -24.612  1.00 41.50           N
ANISOU  464  N   PRO C  57     4569   5415   5784   -265      7   -811       N
ATOM    465  CA  PRO C  57      -3.813  24.325 -25.803  1.00 43.04           C
ANISOU  465  CA  PRO C  57     4755   5621   5977   -273     18   -828       C
ATOM    466  C   PRO C  57      -4.692  23.099 -25.995  1.00 43.87           C
ANISOU  466  C   PRO C  57     4921   5687   6060   -216    -27   -748       C
ATOM    467  O   PRO C  57      -4.979  22.368 -25.048  1.00 47.08           O
ANISOU  467  O   PRO C  57     5348   6088   6451   -140    -85   -728       O
ATOM    468  CB  PRO C  57      -2.356  23.949 -25.518  1.00 36.78           C
ANISOU  468  CB  PRO C  57     3871   4911   5193   -240     -3   -955       C
ATOM    469  CG  PRO C  57      -1.870  25.047 -24.609  1.00 36.56           C
ANISOU  469  CG  PRO C  57     3796   4915   5180   -265     14  -1015       C
ATOM    470  CD  PRO C  57      -3.053  25.324 -23.711  1.00 40.58           C
ANISOU  470  CD  PRO C  57     4373   5367   5680   -240    -12   -918       C
ATOM    471  N   ASN C  58      -5.137  22.891 -27.236  1.00 42.71           N
ANISOU  471  N   ASN C  58     4808   5509   5909   -255      4   -703       N
ATOM    472  CA  ASN C  58      -6.212  21.953 -27.531  1.00 44.56           C
ANISOU  472  CA  ASN C  58     5109   5698   6124   -223    -23   -617       C
ATOM    473  C   ASN C  58      -6.389  21.871 -29.038  1.00 47.68           C
ANISOU  473  C   ASN C  58     5523   6075   6517   -274     19   -594       C
ATOM    474  O   ASN C  58      -5.948  22.752 -29.776  1.00 47.44           O
ANISOU  474  O   ASN C  58     5477   6051   6497   -342     75   -624       O
ATOM    475  CB  ASN C  58      -7.532  22.387 -26.882  1.00 53.29           C
ANISOU  475  CB  ASN C  58     6271   6755   7221   -223    -30   -533       C
ATOM    476  CG  ASN C  58      -8.500  21.229 -26.670  1.00 51.51           C
ANISOU  476  CG  ASN C  58     6101   6497   6973   -174    -70   -469       C
ATOM    477  OD1 ASN C  58      -8.220  20.080 -27.010  1.00 44.49           O
ANISOU  477  OD1 ASN C  58     5219   5614   6072   -138    -93   -480       O
ATOM    478  ND2 ASN C  58      -9.652  21.541 -26.119  1.00 55.95           N
ANISOU  478  ND2 ASN C  58     6706   7024   7526   -177    -74   -407       N
ATOM    479  N   LEU C  59      -7.070  20.810 -29.475  1.00 50.48           N
ANISOU  479  N   LEU C  59     5919   6404   6856   -244     -5   -542       N
ATOM    480  CA  LEU C  59      -7.433  20.559 -30.863  1.00 44.39           C
ANISOU  480  CA  LEU C  59     5176   5612   6079   -280     24   -509       C
ATOM    481  C   LEU C  59      -8.950  20.464 -30.984  1.00 46.67           C
ANISOU  481  C   LEU C  59     5530   5850   6351   -281     18   -417       C
ATOM    482  O   LEU C  59      -9.583  19.716 -30.225  1.00 54.49           O
ANISOU  482  O   LEU C  59     6546   6827   7330   -235    -22   -385       O
ATOM    483  CB  LEU C  59      -6.771  19.254 -31.390  1.00 37.42           C
ANISOU  483  CB  LEU C  59     4274   4754   5191   -243      0   -546       C
ATOM    484  CG  LEU C  59      -5.227  19.267 -31.386  1.00 36.51           C
ANISOU  484  CG  LEU C  59     4081   4701   5089   -238      4   -653       C
ATOM    485  CD1 LEU C  59      -4.684  17.878 -31.623  1.00 30.22           C
ANISOU  485  CD1 LEU C  59     3272   3928   4282   -176    -37   -687       C
ATOM    486  CD2 LEU C  59      -4.642  20.240 -32.405  1.00 36.48           C
ANISOU  486  CD2 LEU C  59     4049   4713   5100   -324     74   -693       C
ATOM    487  N   PRO C  60      -9.576  21.175 -31.937  1.00 47.45           N
ANISOU  487  N   PRO C  60     5661   5922   6445   -330     57   -378       N
ATOM    488  CA  PRO C  60      -8.906  21.968 -32.970  1.00 41.83           C
ANISOU  488  CA  PRO C  60     4942   5215   5738   -389    112   -410       C
ATOM    489  C   PRO C  60      -8.395  23.297 -32.454  1.00 46.01           C
ANISOU  489  C   PRO C  60     5456   5749   6278   -428    145   -445       C
ATOM    490  O   PRO C  60      -8.808  23.741 -31.383  1.00 51.91           O
ANISOU  490  O   PRO C  60     6206   6489   7027   -408    125   -428       O
ATOM    491  CB  PRO C  60     -10.017  22.187 -34.000  1.00 42.09           C
ANISOU  491  CB  PRO C  60     5036   5207   5750   -410    130   -344       C
ATOM    492  CG  PRO C  60     -11.263  22.239 -33.163  1.00 39.39           C
ANISOU  492  CG  PRO C  60     4723   4844   5401   -378     96   -288       C
ATOM    493  CD  PRO C  60     -11.041  21.173 -32.121  1.00 40.36           C
ANISOU  493  CD  PRO C  60     4817   4987   5531   -328     50   -303       C
ATOM    494  N   TYR C  61      -7.507  23.927 -33.213  1.00 40.79           N
ANISOU  494  N   TYR C  61     4782   5098   5620   -487    200   -496       N
ATOM    495  CA  TYR C  61      -7.121  25.302 -32.952  1.00 39.92           C
ANISOU  495  CA  TYR C  61     4676   4979   5512   -541    248   -526       C
ATOM    496  C   TYR C  61      -7.149  26.057 -34.270  1.00 42.83           C
ANISOU  496  C   TYR C  61     5104   5310   5860   -610    315   -515       C
ATOM    497  O   TYR C  61      -7.247  25.476 -35.347  1.00 50.13           O
ANISOU  497  O   TYR C  61     6049   6227   6772   -615    323   -499       O
ATOM    498  CB  TYR C  61      -5.739  25.410 -32.257  1.00 31.87           C
ANISOU  498  CB  TYR C  61     3572   4019   4516   -553    256   -628       C
ATOM    499  CG  TYR C  61      -4.534  24.962 -33.078  1.00 33.95           C
ANISOU  499  CG  TYR C  61     3782   4329   4787   -584    286   -711       C
ATOM    500  CD1 TYR C  61      -4.012  25.771 -34.077  1.00 37.65           C
ANISOU  500  CD1 TYR C  61     4271   4787   5249   -673    366   -747       C
ATOM    501  CD2 TYR C  61      -3.910  23.737 -32.830  1.00 34.58           C
ANISOU  501  CD2 TYR C  61     3798   4462   4878   -524    236   -759       C
ATOM    502  CE1 TYR C  61      -2.923  25.373 -34.821  1.00 49.63           C
ANISOU  502  CE1 TYR C  61     5736   6350   6772   -708    398   -829       C
ATOM    503  CE2 TYR C  61      -2.808  23.332 -33.558  1.00 42.87           C
ANISOU  503  CE2 TYR C  61     4793   5561   5935   -548    261   -843       C
ATOM    504  CZ  TYR C  61      -2.312  24.152 -34.568  1.00 52.29           C
ANISOU  504  CZ  TYR C  61     5996   6748   7124   -644    344   -880       C
ATOM    505  OH  TYR C  61      -1.206  23.766 -35.333  1.00 43.19           O
ANISOU  505  OH  TYR C  61     4785   5648   5978   -677    376   -972       O
ATOM    506  N   LEU C  62      -7.068  27.371 -34.173  1.00 43.31           N
ANISOU  506  N   LEU C  62     5202   5342   5912   -662    364   -523       N
ATOM    507  CA  LEU C  62      -7.116  28.222 -35.343  1.00 43.44           C
ANISOU  507  CA  LEU C  62     5298   5309   5897   -727    432   -511       C
ATOM    508  C   LEU C  62      -6.179  29.389 -35.108  1.00 50.82           C
ANISOU  508  C   LEU C  62     6231   6244   6834   -805    502   -580       C
ATOM    509  O   LEU C  62      -6.339  30.132 -34.135  1.00 47.67           O
ANISOU  509  O   LEU C  62     5835   5837   6442   -802    497   -579       O
ATOM    510  CB  LEU C  62      -8.532  28.725 -35.634  1.00 42.35           C
ANISOU  510  CB  LEU C  62     5258   5107   5726   -699    417   -418       C
ATOM    511  CG  LEU C  62      -8.577  29.555 -36.923  1.00 43.64           C
ANISOU  511  CG  LEU C  62     5523   5213   5847   -754    484   -404       C
ATOM    512  CD1 LEU C  62      -8.769  28.631 -38.146  1.00 43.27           C
ANISOU  512  CD1 LEU C  62     5489   5165   5784   -742    476   -383       C
ATOM    513  CD2 LEU C  62      -9.632  30.639 -36.858  1.00 41.40           C
ANISOU  513  CD2 LEU C  62     5339   4864   5526   -738    484   -343       C
ATOM    514  N   ILE C  63      -5.206  29.541 -36.000  1.00 55.28           N
ANISOU  514  N   ILE C  63     6794   6819   7393   -879    570   -644       N
ATOM    515  CA  ILE C  63      -4.302  30.679 -35.998  1.00 51.60           C
ANISOU  515  CA  ILE C  63     6338   6346   6921   -974    655   -717       C
ATOM    516  C   ILE C  63      -4.667  31.596 -37.157  1.00 48.46           C
ANISOU  516  C   ILE C  63     6077   5864   6472  -1037    728   -677       C
ATOM    517  O   ILE C  63      -4.719  31.166 -38.314  1.00 56.19           O
ANISOU  517  O   ILE C  63     7094   6826   7429  -1048    746   -660       O
ATOM    518  CB  ILE C  63      -2.839  30.218 -36.064  1.00 48.97           C
ANISOU  518  CB  ILE C  63     5897   6094   6617  -1021    687   -838       C
ATOM    519  CG1 ILE C  63      -2.525  29.408 -34.795  1.00 50.54           C
ANISOU  519  CG1 ILE C  63     5976   6370   6857   -943    606   -877       C
ATOM    520  CG2 ILE C  63      -1.926  31.428 -36.209  1.00 43.14           C
ANISOU  520  CG2 ILE C  63     5177   5348   5868  -1138    791   -922       C
ATOM    521  CD1 ILE C  63      -1.395  28.426 -34.921  1.00 55.74           C
ANISOU  521  CD1 ILE C  63     6523   7115   7540   -935    594   -975       C
ATOM    522  N   ASP C  64      -4.928  32.853 -36.842  1.00 44.40           N
ANISOU  522  N   ASP C  64     5642   5294   5934  -1072    768   -661       N
ATOM    523  CA  ASP C  64      -5.324  33.848 -37.828  1.00 38.72           C
ANISOU  523  CA  ASP C  64     5076   4482   5155  -1121    835   -621       C
ATOM    524  C   ASP C  64      -4.664  35.163 -37.418  1.00 49.75           C
ANISOU  524  C   ASP C  64     6513   5850   6540  -1213    919   -679       C
ATOM    525  O   ASP C  64      -5.208  35.924 -36.611  1.00 58.43           O
ANISOU  525  O   ASP C  64     7651   6917   7634  -1190    902   -647       O
ATOM    526  CB  ASP C  64      -6.833  33.977 -37.894  1.00 42.01           C
ANISOU  526  CB  ASP C  64     5582   4839   5539  -1033    773   -509       C
ATOM    527  CG  ASP C  64      -7.284  34.959 -38.958  1.00 56.77           C
ANISOU  527  CG  ASP C  64     7623   6610   7337  -1065    831   -466       C
ATOM    528  OD1 ASP C  64      -6.566  35.145 -39.970  1.00 57.70           O
ANISOU  528  OD1 ASP C  64     7792   6703   7427  -1145    911   -504       O
ATOM    529  OD2 ASP C  64      -8.371  35.552 -38.780  1.00 58.67           O
ANISOU  529  OD2 ASP C  64     7951   6796   7545  -1006    797   -396       O
ATOM    530  N   GLY C  65      -3.485  35.410 -37.973  1.00 54.04           N
ANISOU  530  N   GLY C  65     7045   6408   7079  -1321   1012   -771       N
ATOM    531  CA  GLY C  65      -2.759  36.634 -37.659  1.00 51.13           C
ANISOU  531  CA  GLY C  65     6715   6016   6698  -1427   1106   -842       C
ATOM    532  C   GLY C  65      -2.402  36.668 -36.185  1.00 55.57           C
ANISOU  532  C   GLY C  65     7153   6647   7313  -1406   1066   -894       C
ATOM    533  O   GLY C  65      -1.647  35.813 -35.695  1.00 58.80           O
ANISOU  533  O   GLY C  65     7411   7157   7773  -1390   1033   -969       O
ATOM    534  N   ALA C  66      -2.930  37.673 -35.471  1.00 54.12           N
ANISOU  534  N   ALA C  66     7038   6410   7114  -1401   1069   -858       N
ATOM    535  CA  ALA C  66      -2.665  37.850 -34.044  1.00 61.48           C
ANISOU  535  CA  ALA C  66     7870   7399   8091  -1381   1035   -902       C
ATOM    536  C   ALA C  66      -3.588  37.026 -33.155  1.00 60.33           C
ANISOU  536  C   ALA C  66     7659   7286   7976  -1246    908   -828       C
ATOM    537  O   ALA C  66      -3.364  36.977 -31.942  1.00 62.89           O
ANISOU  537  O   ALA C  66     7891   7666   8340  -1217    868   -864       O
ATOM    538  CB  ALA C  66      -2.794  39.322 -33.660  1.00 60.73           C
ANISOU  538  CB  ALA C  66     7881   7231   7964  -1441   1099   -901       C
ATOM    539  N   HIS C  67      -4.593  36.369 -33.733  1.00 59.02           N
ANISOU  539  N   HIS C  67     7540   7092   7794  -1168    849   -733       N
ATOM    540  CA  HIS C  67      -5.606  35.636 -32.992  1.00 51.44           C
ANISOU  540  CA  HIS C  67     6539   6151   6854  -1050    740   -658       C
ATOM    541  C   HIS C  67      -5.321  34.147 -33.053  1.00 50.34           C
ANISOU  541  C   HIS C  67     6289   6087   6750   -998    681   -676       C
ATOM    542  O   HIS C  67      -5.318  33.545 -34.128  1.00 55.34           O
ANISOU  542  O   HIS C  67     6942   6715   7369  -1003    690   -663       O
ATOM    543  CB  HIS C  67      -6.992  35.925 -33.546  1.00 46.19           C
ANISOU  543  CB  HIS C  67     6000   5407   6145   -996    713   -549       C
ATOM    544  CG  HIS C  67      -7.368  37.365 -33.464  1.00 51.09           C
ANISOU  544  CG  HIS C  67     6742   5946   6723  -1028    760   -525       C
ATOM    545  ND1 HIS C  67      -7.741  38.096 -34.569  1.00 51.51           N
ANISOU  545  ND1 HIS C  67     6946   5911   6713  -1056    813   -487       N
ATOM    546  CD2 HIS C  67      -7.418  38.214 -32.409  1.00 51.14           C
ANISOU  546  CD2 HIS C  67     6750   5942   6737  -1033    763   -536       C
ATOM    547  CE1 HIS C  67      -8.009  39.335 -34.198  1.00 58.20           C
ANISOU  547  CE1 HIS C  67     7889   6695   7529  -1075    845   -474       C
ATOM    548  NE2 HIS C  67      -7.827  39.432 -32.890  1.00 54.57           N
ANISOU  548  NE2 HIS C  67     7338   6283   7115  -1064    817   -503       N
ATOM    549  N   ARG C  68      -5.089  33.561 -31.898  1.00 57.33           N
ANISOU  549  N   ARG C  68     7067   7040   7677   -947    620   -706       N
ATOM    550  CA  ARG C  68      -4.959  32.128 -31.765  1.00 52.18           C
ANISOU  550  CA  ARG C  68     6324   6450   7051   -879    551   -713       C
ATOM    551  C   ARG C  68      -6.090  31.681 -30.858  1.00 49.91           C
ANISOU  551  C   ARG C  68     6038   6157   6770   -783    465   -634       C
ATOM    552  O   ARG C  68      -6.276  32.248 -29.773  1.00 57.12           O
ANISOU  552  O   ARG C  68     6941   7070   7693   -768    448   -633       O
ATOM    553  CB  ARG C  68      -3.585  31.775 -31.203  1.00 54.67           C
ANISOU  553  CB  ARG C  68     6518   6853   7401   -898    557   -832       C
ATOM    554  CG  ARG C  68      -2.454  32.548 -31.868  1.00 58.70           C
ANISOU  554  CG  ARG C  68     7025   7373   7905  -1014    659   -928       C
ATOM    555  CD  ARG C  68      -1.160  32.334 -31.135  1.00 69.34           C
ANISOU  555  CD  ARG C  68     8240   8817   9288  -1028    659  -1059       C
ATOM    556  NE  ARG C  68      -0.248  31.433 -31.840  1.00 76.36           N
ANISOU  556  NE  ARG C  68     9054   9770  10188  -1038    667  -1136       N
ATOM    557  CZ  ARG C  68       0.356  31.694 -32.996  1.00 76.99           C
ANISOU  557  CZ  ARG C  68     9157   9844  10253  -1132    752  -1185       C
ATOM    558  NH1 ARG C  68       0.181  32.855 -33.616  1.00 82.72           N
ANISOU  558  NH1 ARG C  68     9989  10494  10947  -1228    843  -1165       N
ATOM    559  NH2 ARG C  68       1.165  30.790 -33.522  1.00 78.21           N
ANISOU  559  NH2 ARG C  68     9230  10066  10420  -1129    748  -1259       N
ATOM    560  N   LEU C  69      -6.876  30.715 -31.327  1.00 39.11           N
ANISOU  560  N   LEU C  69     4686   4779   5394   -725    416   -569       N
ATOM    561  CA  LEU C  69      -8.056  30.242 -30.620  1.00 32.03           C
ANISOU  561  CA  LEU C  69     3800   3873   4498   -644    343   -494       C
ATOM    562  C   LEU C  69      -7.998  28.735 -30.443  1.00 37.64           C
ANISOU  562  C   LEU C  69     4449   4628   5225   -583    283   -496       C
ATOM    563  O   LEU C  69      -7.459  28.005 -31.279  1.00 43.75           O
ANISOU  563  O   LEU C  69     5201   5422   5999   -593    292   -523       O
ATOM    564  CB  LEU C  69      -9.360  30.571 -31.371  1.00 37.19           C
ANISOU  564  CB  LEU C  69     4551   4464   5117   -630    341   -407       C
ATOM    565  CG  LEU C  69      -9.770  32.015 -31.598  1.00 43.71           C
ANISOU  565  CG  LEU C  69     5469   5228   5912   -666    387   -383       C
ATOM    566  CD1 LEU C  69      -9.063  32.594 -32.845  1.00 42.47           C
ANISOU  566  CD1 LEU C  69     5370   5038   5729   -744    467   -414       C
ATOM    567  CD2 LEU C  69     -11.269  32.059 -31.759  1.00 39.18           C
ANISOU  567  CD2 LEU C  69     4959   4616   5312   -607    345   -300       C
ATOM    568  N   THR C  70      -8.607  28.269 -29.371  1.00 35.62           N
ANISOU  568  N   THR C  70     4175   4382   4977   -520    223   -465       N
ATOM    569  CA  THR C  70      -9.014  26.877 -29.295  1.00 35.62           C
ANISOU  569  CA  THR C  70     4158   4398   4977   -459    166   -438       C
ATOM    570  C   THR C  70     -10.527  26.867 -29.061  1.00 36.10           C
ANISOU  570  C   THR C  70     4273   4421   5021   -425    136   -354       C
ATOM    571  O   THR C  70     -11.172  27.917 -29.094  1.00 48.86           O
ANISOU  571  O   THR C  70     5935   6003   6625   -444    156   -322       O
ATOM    572  CB  THR C  70      -8.191  26.142 -28.229  1.00 36.09           C
ANISOU  572  CB  THR C  70     4148   4509   5054   -414    125   -495       C
ATOM    573  OG1 THR C  70      -8.536  26.615 -26.930  1.00 41.43           O
ANISOU  573  OG1 THR C  70     4822   5184   5736   -389    100   -484       O
ATOM    574  CG2 THR C  70      -6.713  26.402 -28.449  1.00 32.49           C
ANISOU  574  CG2 THR C  70     3631   4100   4615   -453    160   -593       C
ATOM    575  N   GLN C  71     -11.083  25.682 -28.826  1.00 40.10           N
ANISOU  575  N   GLN C  71     4775   4935   5525   -376     90   -325       N
ATOM    576  CA  GLN C  71     -12.518  25.456 -28.634  1.00 42.88           C
ANISOU  576  CA  GLN C  71     5167   5264   5862   -348     63   -259       C
ATOM    577  C   GLN C  71     -13.289  25.683 -29.932  1.00 44.90           C
ANISOU  577  C   GLN C  71     5471   5492   6097   -367     83   -220       C
ATOM    578  O   GLN C  71     -13.418  26.813 -30.418  1.00 48.25           O
ANISOU  578  O   GLN C  71     5932   5890   6510   -395    116   -212       O
ATOM    579  CB  GLN C  71     -13.075  26.318 -27.493  1.00 35.19           C
ANISOU  579  CB  GLN C  71     4201   4280   4889   -338     52   -244       C
ATOM    580  CG  GLN C  71     -12.453  26.038 -26.126  1.00 31.43           C
ANISOU  580  CG  GLN C  71     3684   3831   4428   -310     25   -279       C
ATOM    581  CD  GLN C  71     -12.939  24.732 -25.530  1.00 48.06           C
ANISOU  581  CD  GLN C  71     5793   5942   6524   -263    -19   -258       C
ATOM    582  OE1 GLN C  71     -14.010  24.230 -25.885  1.00 47.79           O
ANISOU  582  OE1 GLN C  71     5791   5891   6475   -257    -27   -214       O
ATOM    583  NE2 GLN C  71     -12.154  24.170 -24.624  1.00 50.35           N
ANISOU  583  NE2 GLN C  71     6057   6255   6820   -229    -46   -297       N
ATOM    584  N   SER C  72     -13.816  24.587 -30.485  1.00 41.99           N
ANISOU  584  N   SER C  72     5108   5126   5720   -347     64   -197       N
ATOM    585  CA  SER C  72     -14.395  24.607 -31.822  1.00 37.24           C
ANISOU  585  CA  SER C  72     4545   4506   5098   -360     79   -169       C
ATOM    586  C   SER C  72     -15.572  25.569 -31.918  1.00 41.63           C
ANISOU  586  C   SER C  72     5146   5038   5633   -352     79   -132       C
ATOM    587  O   SER C  72     -15.740  26.252 -32.937  1.00 41.37           O
ANISOU  587  O   SER C  72     5159   4982   5579   -367    103   -120       O
ATOM    588  CB  SER C  72     -14.816  23.196 -32.210  1.00 35.84           C
ANISOU  588  CB  SER C  72     4360   4340   4915   -338     55   -156       C
ATOM    589  OG  SER C  72     -15.618  22.630 -31.190  1.00 48.20           O
ANISOU  589  OG  SER C  72     5921   5912   6481   -310     21   -138       O
ATOM    590  N   ASN C  73     -16.393  25.652 -30.869  1.00 37.79           N
ANISOU  590  N   ASN C  73     4652   4557   5148   -327     51   -115       N
ATOM    591  CA  ASN C  73     -17.450  26.661 -30.875  1.00 34.73           C
ANISOU  591  CA  ASN C  73     4303   4153   4741   -313     47    -89       C
ATOM    592  C   ASN C  73     -16.871  28.062 -30.973  1.00 38.61           C
ANISOU  592  C   ASN C  73     4828   4615   5225   -336     81    -99       C
ATOM    593  O   ASN C  73     -17.380  28.897 -31.735  1.00 47.27           O
ANISOU  593  O   ASN C  73     5985   5684   6293   -331     93    -82       O
ATOM    594  CB  ASN C  73     -18.327  26.531 -29.633  1.00 44.62           C
ANISOU  594  CB  ASN C  73     5534   5421   5998   -287     16    -79       C
ATOM    595  CG  ASN C  73     -19.172  25.275 -29.656  1.00 39.56           C
ANISOU  595  CG  ASN C  73     4877   4801   5352   -273     -8    -69       C
ATOM    596  OD1 ASN C  73     -19.691  24.907 -30.689  1.00 35.66           O
ANISOU  596  OD1 ASN C  73     4396   4310   4842   -269     -8    -61       O
ATOM    597  ND2 ASN C  73     -19.283  24.599 -28.518  1.00 40.70           N
ANISOU  597  ND2 ASN C  73     4998   4958   5507   -266    -24    -74       N
ATOM    598  N   ALA C  74     -15.789  28.341 -30.232  1.00 38.55           N
ANISOU  598  N   ALA C  74     4793   4614   5242   -360     98   -132       N
ATOM    599  CA  ALA C  74     -15.206  29.682 -30.291  1.00 35.76           C
ANISOU  599  CA  ALA C  74     4475   4232   4882   -394    139   -148       C
ATOM    600  C   ALA C  74     -14.560  29.944 -31.641  1.00 42.34           C
ANISOU  600  C   ALA C  74     5350   5041   5697   -434    185   -160       C
ATOM    601  O   ALA C  74     -14.464  31.099 -32.071  1.00 41.57           O
ANISOU  601  O   ALA C  74     5317   4901   5574   -460    224   -159       O
ATOM    602  CB  ALA C  74     -14.184  29.888 -29.177  1.00 28.57           C
ANISOU  602  CB  ALA C  74     3514   3342   4001   -414    147   -191       C
ATOM    603  N   ILE C  75     -14.098  28.888 -32.310  1.00 40.44           N
ANISOU  603  N   ILE C  75     5079   4822   5465   -441    185   -173       N
ATOM    604  CA  ILE C  75     -13.557  29.039 -33.650  1.00 40.98           C
ANISOU  604  CA  ILE C  75     5188   4868   5513   -480    230   -184       C
ATOM    605  C   ILE C  75     -14.672  29.332 -34.650  1.00 43.40           C
ANISOU  605  C   ILE C  75     5572   5140   5778   -454    223   -136       C
ATOM    606  O   ILE C  75     -14.542  30.225 -35.492  1.00 44.51           O
ANISOU  606  O   ILE C  75     5791   5237   5885   -479    264   -133       O
ATOM    607  CB  ILE C  75     -12.746  27.787 -34.023  1.00 45.10           C
ANISOU  607  CB  ILE C  75     5651   5429   6058   -489    227   -215       C
ATOM    608  CG1 ILE C  75     -11.588  27.608 -33.021  1.00 39.83           C
ANISOU  608  CG1 ILE C  75     4909   4800   5426   -504    229   -273       C
ATOM    609  CG2 ILE C  75     -12.267  27.896 -35.439  1.00 43.51           C
ANISOU  609  CG2 ILE C  75     5491   5207   5835   -530    273   -225       C
ATOM    610  CD1 ILE C  75     -10.729  26.389 -33.251  1.00 36.66           C
ANISOU  610  CD1 ILE C  75     4446   4439   5043   -501    219   -314       C
ATOM    611  N   LEU C  76     -15.792  28.610 -34.562  1.00 40.48           N
ANISOU  611  N   LEU C  76     5186   4789   5405   -402    172   -104       N
ATOM    612  CA  LEU C  76     -16.886  28.861 -35.494  1.00 42.01           C
ANISOU  612  CA  LEU C  76     5443   4961   5557   -368    158    -70       C
ATOM    613  C   LEU C  76     -17.435  30.266 -35.321  1.00 47.64           C
ANISOU  613  C   LEU C  76     6230   5634   6238   -350    163    -55       C
ATOM    614  O   LEU C  76     -17.746  30.946 -36.306  1.00 46.83           O
ANISOU  614  O   LEU C  76     6214   5491   6089   -338    178    -40       O
ATOM    615  CB  LEU C  76     -18.004  27.836 -35.311  1.00 37.71           C
ANISOU  615  CB  LEU C  76     4856   4453   5017   -322    105    -53       C
ATOM    616  CG  LEU C  76     -17.670  26.411 -35.743  1.00 42.03           C
ANISOU  616  CG  LEU C  76     5356   5031   5584   -332     99    -62       C
ATOM    617  CD1 LEU C  76     -18.516  25.420 -34.960  1.00 49.90           C
ANISOU  617  CD1 LEU C  76     6301   6063   6596   -304     57    -56       C
ATOM    618  CD2 LEU C  76     -17.841  26.231 -37.239  1.00 43.49           C
ANISOU  618  CD2 LEU C  76     5584   5202   5738   -330    110    -53       C
ATOM    619  N   ARG C  77     -17.564  30.720 -34.074  1.00 53.16           N
ANISOU  619  N   ARG C  77     6901   6340   6956   -342    150    -58       N
ATOM    620  CA  ARG C  77     -18.069  32.067 -33.846  1.00 44.72           C
ANISOU  620  CA  ARG C  77     5903   5232   5856   -322    154    -46       C
ATOM    621  C   ARG C  77     -17.084  33.117 -34.352  1.00 44.85           C
ANISOU  621  C   ARG C  77     5997   5193   5850   -375    218    -60       C
ATOM    622  O   ARG C  77     -17.488  34.227 -34.707  1.00 52.11           O
ANISOU  622  O   ARG C  77     7015   6061   6723   -358    231    -44       O
ATOM    623  CB  ARG C  77     -18.376  32.264 -32.360  1.00 47.31           C
ANISOU  623  CB  ARG C  77     6180   5585   6213   -306    127    -49       C
ATOM    624  CG  ARG C  77     -19.668  31.599 -31.849  1.00 49.63           C
ANISOU  624  CG  ARG C  77     6426   5920   6510   -251     69    -35       C
ATOM    625  CD  ARG C  77     -19.875  31.774 -30.320  1.00 51.53           C
ANISOU  625  CD  ARG C  77     6617   6182   6778   -244     50    -41       C
ATOM    626  NE  ARG C  77     -19.691  30.493 -29.615  1.00 73.18           N
ANISOU  626  NE  ARG C  77     9280   8968   9558   -253     33    -51       N
ATOM    627  CZ  ARG C  77     -19.748  30.299 -28.287  1.00 75.07           C
ANISOU  627  CZ  ARG C  77     9473   9230   9822   -250     16    -58       C
ATOM    628  NH1 ARG C  77     -19.989  31.300 -27.447  1.00 73.05           N
ANISOU  628  NH1 ARG C  77     9229   8963   9564   -240     13    -58       N
ATOM    629  NH2 ARG C  77     -19.561  29.082 -27.790  1.00 70.12           N
ANISOU  629  NH2 ARG C  77     8794   8631   9216   -256      3    -65       N
ATOM    630  N   TYR C  78     -15.798  32.776 -34.422  1.00 42.95           N
ANISOU  630  N   TYR C  78     5718   4963   5638   -440    261    -95       N
ATOM    631  CA  TYR C  78     -14.795  33.732 -34.874  1.00 45.45           C
ANISOU  631  CA  TYR C  78     6102   5233   5936   -507    334   -121       C
ATOM    632  C   TYR C  78     -14.870  33.943 -36.382  1.00 49.33           C
ANISOU  632  C   TYR C  78     6693   5676   6374   -515    365   -105       C
ATOM    633  O   TYR C  78     -14.847  35.082 -36.871  1.00 44.49           O
ANISOU  633  O   TYR C  78     6196   4996   5710   -533    408    -99       O
ATOM    634  CB  TYR C  78     -13.399  33.247 -34.485  1.00 49.02           C
ANISOU  634  CB  TYR C  78     6467   5724   6434   -571    368   -178       C
ATOM    635  CG  TYR C  78     -12.330  34.082 -35.125  1.00 51.23           C
ANISOU  635  CG  TYR C  78     6808   5963   6693   -654    453   -217       C
ATOM    636  CD1 TYR C  78     -12.139  35.390 -34.729  1.00 44.41           C
ANISOU  636  CD1 TYR C  78     6011   5053   5809   -689    496   -229       C
ATOM    637  CD2 TYR C  78     -11.547  33.585 -36.167  1.00 51.47           C
ANISOU  637  CD2 TYR C  78     6839   5999   6720   -702    495   -245       C
ATOM    638  CE1 TYR C  78     -11.187  36.167 -35.311  1.00 54.14           C
ANISOU  638  CE1 TYR C  78     7308   6244   7018   -775    583   -270       C
ATOM    639  CE2 TYR C  78     -10.588  34.372 -36.765  1.00 42.35           C
ANISOU  639  CE2 TYR C  78     5743   4806   5541   -789    581   -288       C
ATOM    640  CZ  TYR C  78     -10.414  35.663 -36.325  1.00 53.71           C
ANISOU  640  CZ  TYR C  78     7250   6198   6960   -828    628   -301       C
ATOM    641  OH  TYR C  78      -9.469  36.483 -36.890  1.00 66.32           O
ANISOU  641  OH  TYR C  78     8917   7753   8530   -925    724   -348       O
ATOM    642  N   ILE C  79     -14.912  32.844 -37.136  1.00 48.87           N
ANISOU  642  N   ILE C  79     6598   5648   6323   -505    348   -101       N
ATOM    643  CA  ILE C  79     -15.140  32.907 -38.573  1.00 47.49           C
ANISOU  643  CA  ILE C  79     6514   5434   6096   -500    366    -82       C
ATOM    644  C   ILE C  79     -16.515  33.486 -38.891  1.00 52.10           C
ANISOU  644  C   ILE C  79     7185   5985   6626   -419    322    -38       C
ATOM    645  O   ILE C  79     -16.670  34.223 -39.868  1.00 51.70           O
ANISOU  645  O   ILE C  79     7258   5873   6512   -412    348    -23       O
ATOM    646  CB  ILE C  79     -14.951  31.501 -39.154  1.00 47.09           C
ANISOU  646  CB  ILE C  79     6389   5432   6071   -500    348    -89       C
ATOM    647  CG1 ILE C  79     -13.566  30.977 -38.751  1.00 41.76           C
ANISOU  647  CG1 ILE C  79     5626   4795   5446   -568    385   -141       C
ATOM    648  CG2 ILE C  79     -15.182  31.492 -40.669  1.00 39.43           C
ANISOU  648  CG2 ILE C  79     5509   4426   5048   -493    365    -70       C
ATOM    649  CD1 ILE C  79     -13.548  29.481 -38.526  1.00 41.53           C
ANISOU  649  CD1 ILE C  79     5489   4830   5461   -544    339   -148       C
ATOM    650  N   ALA C  80     -17.519  33.198 -38.058  1.00 54.56           N
ANISOU  650  N   ALA C  80     7437   6337   6957   -355    256    -22       N
ATOM    651  CA  ALA C  80     -18.878  33.681 -38.302  1.00 45.75           C
ANISOU  651  CA  ALA C  80     6384   5206   5792   -269    206      6       C
ATOM    652  C   ALA C  80     -18.964  35.200 -38.193  1.00 49.58           C
ANISOU  652  C   ALA C  80     6989   5621   6228   -259    230     14       C
ATOM    653  O   ALA C  80     -19.579  35.851 -39.038  1.00 49.23           O
ANISOU  653  O   ALA C  80     7061   5529   6115   -208    221     33       O
ATOM    654  CB  ALA C  80     -19.853  33.014 -37.327  1.00 33.87           C
ANISOU  654  CB  ALA C  80     4777   3768   4323   -218    139      8       C
ATOM    655  N   ARG C  81     -18.383  35.782 -37.141  1.00 56.26           N
ANISOU  655  N   ARG C  81     7815   6460   7104   -302    257     -1       N
ATOM    656  CA  ARG C  81     -18.334  37.239 -37.018  1.00 40.44           C
ANISOU  656  CA  ARG C  81     5931   4382   5053   -304    291      4       C
ATOM    657  C   ARG C  81     -17.662  37.874 -38.230  1.00 50.59           C
ANISOU  657  C   ARG C  81     7355   5589   6279   -351    361      4       C
ATOM    658  O   ARG C  81     -18.111  38.913 -38.729  1.00 56.63           O
ANISOU  658  O   ARG C  81     8266   6280   6970   -313    369     23       O
ATOM    659  CB  ARG C  81     -17.550  37.635 -35.772  1.00 41.77           C
ANISOU  659  CB  ARG C  81     6043   4559   5269   -364    322    -22       C
ATOM    660  CG  ARG C  81     -18.275  37.767 -34.460  1.00 43.46           C
ANISOU  660  CG  ARG C  81     6191   4810   5512   -316    269    -17       C
ATOM    661  CD  ARG C  81     -17.249  38.147 -33.371  1.00 43.14           C
ANISOU  661  CD  ARG C  81     6101   4774   5516   -388    311    -49       C
ATOM    662  NE  ARG C  81     -17.128  37.088 -32.366  1.00 56.20           N
ANISOU  662  NE  ARG C  81     7608   6508   7239   -389    275    -64       N
ATOM    663  CZ  ARG C  81     -15.989  36.497 -32.020  1.00 56.28           C
ANISOU  663  CZ  ARG C  81     7535   6552   7296   -451    304   -101       C
ATOM    664  NH1 ARG C  81     -14.849  36.841 -32.587  1.00 55.65           N
ANISOU  664  NH1 ARG C  81     7490   6445   7210   -527    374   -134       N
ATOM    665  NH2 ARG C  81     -15.990  35.547 -31.106  1.00 67.06           N
ANISOU  665  NH2 ARG C  81     8786   7981   8711   -437    263   -111       N
ATOM    666  N   LYS C  82     -16.551  37.280 -38.678  1.00 44.15           N
ANISOU  666  N   LYS C  82     6499   4785   5491   -434    415    -22       N
ATOM    667  CA  LYS C  82     -15.755  37.820 -39.777  1.00 42.98           C
ANISOU  667  CA  LYS C  82     6472   4566   5292   -500    496    -32       C
ATOM    668  C   LYS C  82     -16.582  37.965 -41.045  1.00 56.29           C
ANISOU  668  C   LYS C  82     8284   6205   6899   -431    474      4       C
ATOM    669  O   LYS C  82     -16.370  38.892 -41.834  1.00 66.75           O
ANISOU  669  O   LYS C  82     9771   7440   8150   -451    528     11       O
ATOM    670  CB  LYS C  82     -14.577  36.884 -40.055  1.00 47.34           C
ANISOU  670  CB  LYS C  82     6929   5164   5894   -586    541    -72       C
ATOM    671  CG  LYS C  82     -13.208  37.365 -39.751  1.00 45.34           C
ANISOU  671  CG  LYS C  82     6668   4897   5662   -700    629   -127       C
ATOM    672  CD  LYS C  82     -12.219  36.623 -40.660  1.00 55.39           C
ANISOU  672  CD  LYS C  82     7909   6191   6947   -772    681   -163       C
ATOM    673  CE  LYS C  82     -10.758  37.011 -40.368  1.00 63.88           C
ANISOU  673  CE  LYS C  82     8954   7271   8048   -893    773   -237       C
ATOM    674  NZ  LYS C  82      -9.763  36.431 -41.326  1.00 63.12           N
ANISOU  674  NZ  LYS C  82     8837   7191   7954   -970    834   -283       N
ATOM    675  N   HIS C  83     -17.510  37.044 -41.275  1.00 51.33           N
ANISOU  675  N   HIS C  83     7588   5633   6282   -351    396     23       N
ATOM    676  CA  HIS C  83     -18.204  36.949 -42.549  1.00 44.20           C
ANISOU  676  CA  HIS C  83     6780   4703   5312   -286    371     47       C
ATOM    677  C   HIS C  83     -19.697  37.178 -42.399  1.00 53.70           C
ANISOU  677  C   HIS C  83     8004   5921   6480   -160    282     69       C
ATOM    678  O   HIS C  83     -20.487  36.710 -43.227  1.00 64.34           O
ANISOU  678  O   HIS C  83     9365   7287   7793    -88    232     79       O
ATOM    679  CB  HIS C  83     -17.922  35.603 -43.208  1.00 42.42           C
ANISOU  679  CB  HIS C  83     6460   4534   5121   -309    364     39       C
ATOM    680  CG  HIS C  83     -16.495  35.448 -43.619  1.00 49.90           C
ANISOU  680  CG  HIS C  83     7408   5464   6087   -423    452     10       C
ATOM    681  ND1 HIS C  83     -15.613  34.627 -42.954  1.00 53.96           N
ANISOU  681  ND1 HIS C  83     7778   6043   6683   -491    469    -24       N
ATOM    682  CD2 HIS C  83     -15.783  36.053 -44.600  1.00 51.73           C
ANISOU  682  CD2 HIS C  83     7770   5621   6263   -483    531      4       C
ATOM    683  CE1 HIS C  83     -14.419  34.717 -43.517  1.00 56.06           C
ANISOU  683  CE1 HIS C  83     8072   6284   6945   -585    552    -56       C
ATOM    684  NE2 HIS C  83     -14.496  35.580 -44.515  1.00 54.31           N
ANISOU  684  NE2 HIS C  83     8017   5976   6641   -589    595    -40       N
ATOM    685  N   ASN C  84     -20.077  37.929 -41.362  1.00 55.67           N
ANISOU  685  N   ASN C  84     8254   6163   6734   -132    262     70       N
ATOM    686  CA  ASN C  84     -21.466  38.216 -41.020  1.00 68.12           C
ANISOU  686  CA  ASN C  84     9835   7764   8284    -14    178     79       C
ATOM    687  C   ASN C  84     -22.336  36.968 -41.172  1.00 71.09           C
ANISOU  687  C   ASN C  84    10085   8233   8691     42    106     72       C
ATOM    688  O   ASN C  84     -23.174  36.879 -42.073  1.00 79.62           O
ANISOU  688  O   ASN C  84    11217   9318   9717    124     60     76       O
ATOM    689  CB  ASN C  84     -21.981  39.380 -41.869  1.00 84.45           C
ANISOU  689  CB  ASN C  84    12100   9743  10243     61    173     96       C
ATOM    690  CG  ASN C  84     -23.474  39.579 -41.739  1.00102.06           C
ANISOU  690  CG  ASN C  84    14332  12008  12436    200     76     95       C
ATOM    691  OD1 ASN C  84     -24.059  39.303 -40.685  1.00106.50           O
ANISOU  691  OD1 ASN C  84    14771  12642  13052    226     28     81       O
ATOM    692  ND2 ASN C  84     -24.105  40.055 -42.810  1.00107.15           N
ANISOU  692  ND2 ASN C  84    15118  12607  12987    292     47    103       N
ATOM    693  N   LEU C  85     -22.117  35.978 -40.308  1.00 68.03           N
ANISOU  693  N   LEU C  85     9539   7922   8389     -4     98     59       N
ATOM    694  CA  LEU C  85     -22.895  34.745 -40.301  1.00 65.81           C
ANISOU  694  CA  LEU C  85     9135   7727   8142     32     40     48       C
ATOM    695  C   LEU C  85     -23.477  34.476 -38.923  1.00 65.51           C
ANISOU  695  C   LEU C  85     8981   7753   8157     47      0     34       C
ATOM    696  O   LEU C  85     -23.608  33.317 -38.514  1.00 74.00           O
ANISOU  696  O   LEU C  85     9934   8895   9286     26    -18     22       O
ATOM    697  CB  LEU C  85     -22.053  33.556 -40.758  1.00 63.41           C
ANISOU  697  CB  LEU C  85     8761   7451   7882    -41     73     43       C
ATOM    698  CG  LEU C  85     -21.847  33.461 -42.258  1.00 63.76           C
ANISOU  698  CG  LEU C  85     8894   7458   7875    -37     93     52       C
ATOM    699  CD1 LEU C  85     -21.095  32.192 -42.584  1.00 66.68           C
ANISOU  699  CD1 LEU C  85     9174   7865   8294   -103    117     43       C
ATOM    700  CD2 LEU C  85     -23.192  33.487 -42.953  1.00 69.03           C
ANISOU  700  CD2 LEU C  85     9599   8144   8484     71     25     51       C
ATOM    701  N   CYS C  86     -23.814  35.537 -38.196  1.00 66.74           N
ANISOU  701  N   CYS C  86     9181   7884   8294     80    -11     36       N
ATOM    702  CA  CYS C  86     -24.382  35.443 -36.861  1.00 73.24           C
ANISOU  702  CA  CYS C  86     9907   8761   9161     94    -45     22       C
ATOM    703  C   CYS C  86     -25.847  35.868 -36.888  1.00 76.64           C
ANISOU  703  C   CYS C  86    10354   9220   9546    203   -114      7       C
ATOM    704  O   CYS C  86     -26.309  36.519 -37.828  1.00 91.69           O
ANISOU  704  O   CYS C  86    12369  11089  11380    274   -135     10       O
ATOM    705  CB  CYS C  86     -23.584  36.303 -35.876  1.00 75.18           C
ANISOU  705  CB  CYS C  86    10175   8963   9427     43     -3     28       C
ATOM    706  SG  CYS C  86     -22.024  35.532 -35.349  1.00 81.99           S
ANISOU  706  SG  CYS C  86    10952   9835  10365    -77     59     22       S
ATOM    707  N   GLY C  87     -26.581  35.474 -35.851  1.00 63.93           N
ANISOU  707  N   GLY C  87     8636   7680   7975    219   -152    -15       N
ATOM    708  CA  GLY C  87     -27.974  35.868 -35.750  1.00 53.30           C
ANISOU  708  CA  GLY C  87     7286   6375   6591    319   -217    -43       C
ATOM    709  C   GLY C  87     -28.151  37.373 -35.818  1.00 48.76           C
ANISOU  709  C   GLY C  87     6841   5733   5952    385   -227    -34       C
ATOM    710  O   GLY C  87     -27.303  38.150 -35.384  1.00 44.39           O
ANISOU  710  O   GLY C  87     6351   5113   5403    340   -181    -11       O
ATOM    711  N   GLU C  88     -29.269  37.793 -36.398  1.00 62.93           N
ANISOU  711  N   GLU C  88     8681   7545   7683    497   -287    -59       N
ATOM    712  CA  GLU C  88     -29.522  39.213 -36.612  1.00 67.46           C
ANISOU  712  CA  GLU C  88     9401   8049   8180    579   -304    -52       C
ATOM    713  C   GLU C  88     -30.403  39.793 -35.516  1.00 75.57           C
ANISOU  713  C   GLU C  88    10384   9117   9211    638   -350    -82       C
ATOM    714  O   GLU C  88     -30.025  40.761 -34.855  1.00 88.20           O
ANISOU  714  O   GLU C  88    12049  10659  10805    628   -328    -64       O
ATOM    715  CB  GLU C  88     -30.168  39.436 -37.979  1.00 69.98           C
ANISOU  715  CB  GLU C  88     9821   8354   8413    683   -349    -63       C
ATOM    716  CG  GLU C  88     -29.220  39.316 -39.157  1.00 84.15           C
ANISOU  716  CG  GLU C  88    11719  10075  10179    635   -296    -27       C
ATOM    717  CD  GLU C  88     -29.899  39.682 -40.466  1.00 96.23           C
ANISOU  717  CD  GLU C  88    13370  11582  11612    752   -344    -37       C
ATOM    718  OE1 GLU C  88     -30.902  39.025 -40.823  1.00 98.17           O
ANISOU  718  OE1 GLU C  88    13535  11916  11851    824   -409    -79       O
ATOM    719  OE2 GLU C  88     -29.440  40.634 -41.130  1.00 98.89           O
ANISOU  719  OE2 GLU C  88    13888  11812  11875    772   -316     -8       O
ATOM    720  N   THR C  89     -31.572  39.203 -35.302  1.00 68.96           N
ANISOU  720  N   THR C  89     9435   8383   8385    695   -411   -132       N
ATOM    721  CA  THR C  89     -32.481  39.651 -34.269  1.00 60.35           C
ANISOU  721  CA  THR C  89     8286   7345   7300    749   -455   -171       C
ATOM    722  C   THR C  89     -32.186  38.928 -32.948  1.00 61.65           C
ANISOU  722  C   THR C  89     8311   7558   7554    647   -422   -172       C
ATOM    723  O   THR C  89     -31.403  37.973 -32.887  1.00 64.84           O
ANISOU  723  O   THR C  89     8657   7966   8014    548   -376   -149       O
ATOM    724  CB  THR C  89     -33.925  39.420 -34.697  1.00 60.78           C
ANISOU  724  CB  THR C  89     8285   7492   7315    862   -535   -240       C
ATOM    725  OG1 THR C  89     -34.790  39.767 -33.609  1.00 86.14           O
ANISOU  725  OG1 THR C  89    11422  10768  10540    903   -573   -286       O
ATOM    726  CG2 THR C  89     -34.133  37.966 -35.032  1.00 51.83           C
ANISOU  726  CG2 THR C  89     7026   6441   6226    810   -532   -265       C
ATOM    727  N   GLU C  90     -32.801  39.434 -31.872  1.00 51.35           N
ANISOU  727  N   GLU C  90     6963   6287   6259    678   -448   -199       N
ATOM    728  CA  GLU C  90     -32.801  38.731 -30.595  1.00 47.24           C
ANISOU  728  CA  GLU C  90     6310   5825   5814    599   -428   -212       C
ATOM    729  C   GLU C  90     -33.249  37.280 -30.752  1.00 51.25           C
ANISOU  729  C   GLU C  90     6694   6420   6358    560   -432   -244       C
ATOM    730  O   GLU C  90     -32.572  36.354 -30.294  1.00 59.63           O
ANISOU  730  O   GLU C  90     7693   7486   7478    461   -387   -223       O
ATOM    731  CB  GLU C  90     -33.708  39.459 -29.603  1.00 42.58           C
ANISOU  731  CB  GLU C  90     5689   5276   5216    660   -468   -252       C
ATOM    732  CG  GLU C  90     -33.638  38.915 -28.191  1.00 48.99           C
ANISOU  732  CG  GLU C  90     6385   6132   6096    579   -442   -259       C
ATOM    733  CD  GLU C  90     -32.214  38.929 -27.643  1.00 54.20           C
ANISOU  733  CD  GLU C  90     7074   6718   6801    479   -378   -199       C
ATOM    734  OE1 GLU C  90     -31.431  39.812 -28.036  1.00 66.64           O
ANISOU  734  OE1 GLU C  90     8764   8206   8349    483   -356   -160       O
ATOM    735  OE2 GLU C  90     -31.867  38.055 -26.834  1.00 57.36           O
ANISOU  735  OE2 GLU C  90     7387   7148   7259    397   -348   -195       O
ATOM    736  N   GLU C  91     -34.394  37.064 -31.399  1.00 51.64           N
ANISOU  736  N   GLU C  91     6710   6539   6370    639   -485   -301       N
ATOM    737  CA  GLU C  91     -34.897  35.706 -31.551  1.00 55.31           C
ANISOU  737  CA  GLU C  91     7059   7090   6867    597   -485   -341       C
ATOM    738  C   GLU C  91     -33.906  34.842 -32.322  1.00 62.57           C
ANISOU  738  C   GLU C  91     7999   7968   7807    524   -441   -294       C
ATOM    739  O   GLU C  91     -33.739  33.659 -32.017  1.00 71.63           O
ANISOU  739  O   GLU C  91     9061   9150   9003    442   -411   -298       O
ATOM    740  CB  GLU C  91     -36.261  35.743 -32.234  1.00 57.78           C
ANISOU  740  CB  GLU C  91     7338   7486   7128    703   -552   -420       C
ATOM    741  CG  GLU C  91     -37.024  34.432 -32.195  1.00 69.79           C
ANISOU  741  CG  GLU C  91     8723   9112   8680    659   -552   -483       C
ATOM    742  CD  GLU C  91     -37.971  34.280 -33.375  1.00 83.63           C
ANISOU  742  CD  GLU C  91    10464  10930  10380    751   -608   -549       C
ATOM    743  OE1 GLU C  91     -37.757  34.966 -34.408  1.00 81.28           O
ANISOU  743  OE1 GLU C  91    10279  10577  10025    833   -636   -524       O
ATOM    744  OE2 GLU C  91     -38.927  33.478 -33.268  1.00 90.79           O
ANISOU  744  OE2 GLU C  91    11254  11943  11300    740   -621   -629       O
ATOM    745  N   GLU C  92     -33.224  35.426 -33.310  1.00 54.72           N
ANISOU  745  N   GLU C  92     7124   6895   6774    551   -434   -251       N
ATOM    746  CA  GLU C  92     -32.184  34.707 -34.031  1.00 55.24           C
ANISOU  746  CA  GLU C  92     7214   6917   6858    480   -388   -208       C
ATOM    747  C   GLU C  92     -31.047  34.312 -33.099  1.00 51.36           C
ANISOU  747  C   GLU C  92     6691   6391   6432    370   -329   -167       C
ATOM    748  O   GLU C  92     -30.584  33.164 -33.112  1.00 47.31           O
ANISOU  748  O   GLU C  92     6118   5896   5961    297   -299   -159       O
ATOM    749  CB  GLU C  92     -31.649  35.572 -35.164  1.00 64.42           C
ANISOU  749  CB  GLU C  92     8523   7993   7959    526   -385   -172       C
ATOM    750  CG  GLU C  92     -31.947  35.052 -36.526  1.00 75.68           C
ANISOU  750  CG  GLU C  92     9971   9436   9348    564   -406   -185       C
ATOM    751  CD  GLU C  92     -31.719  36.097 -37.593  1.00 75.87           C
ANISOU  751  CD  GLU C  92    10158   9378   9293    636   -414   -160       C
ATOM    752  OE1 GLU C  92     -32.384  37.146 -37.521  1.00 66.24           O
ANISOU  752  OE1 GLU C  92     9004   8145   8017    733   -458   -178       O
ATOM    753  OE2 GLU C  92     -30.880  35.868 -38.494  1.00 82.14           O
ANISOU  753  OE2 GLU C  92    11017  10117  10077    596   -376   -124       O
ATOM    754  N   LYS C  93     -30.571  35.266 -32.299  1.00 44.14           N
ANISOU  754  N   LYS C  93     5822   5427   5523    362   -313   -144       N
ATOM    755  CA  LYS C  93     -29.485  34.998 -31.369  1.00 43.97           C
ANISOU  755  CA  LYS C  93     5771   5377   5558    269   -262   -113       C
ATOM    756  C   LYS C  93     -29.856  33.912 -30.366  1.00 51.30           C
ANISOU  756  C   LYS C  93     6577   6376   6539    221   -261   -137       C
ATOM    757  O   LYS C  93     -29.027  33.052 -30.040  1.00 53.75           O
ANISOU  757  O   LYS C  93     6849   6679   6892    145   -225   -118       O
ATOM    758  CB  LYS C  93     -29.113  36.286 -30.652  1.00 51.30           C
ANISOU  758  CB  LYS C  93     6763   6250   6477    279   -251    -95       C
ATOM    759  CG  LYS C  93     -28.600  37.365 -31.586  1.00 50.33           C
ANISOU  759  CG  LYS C  93     6782   6042   6299    310   -237    -69       C
ATOM    760  CD  LYS C  93     -27.913  38.453 -30.808  1.00 58.15           C
ANISOU  760  CD  LYS C  93     7832   6971   7293    285   -206    -49       C
ATOM    761  CE  LYS C  93     -27.204  39.408 -31.728  1.00 66.47           C
ANISOU  761  CE  LYS C  93     9033   7929   8294    289   -172    -22       C
ATOM    762  NZ  LYS C  93     -28.181  40.349 -32.319  1.00 74.37           N
ANISOU  762  NZ  LYS C  93    10134   8907   9216    401   -220    -33       N
ATOM    763  N   ILE C  94     -31.101  33.919 -29.877  1.00 47.86           N
ANISOU  763  N   ILE C  94     6082   6007   6095    265   -300   -183       N
ATOM    764  CA  ILE C  94     -31.504  32.908 -28.903  1.00 43.96           C
ANISOU  764  CA  ILE C  94     5484   5575   5643    212   -291   -210       C
ATOM    765  C   ILE C  94     -31.566  31.534 -29.553  1.00 49.71           C
ANISOU  765  C   ILE C  94     6166   6338   6385    172   -279   -221       C
ATOM    766  O   ILE C  94     -31.190  30.528 -28.934  1.00 52.28           O
ANISOU  766  O   ILE C  94     6444   6672   6749    100   -248   -215       O
ATOM    767  CB  ILE C  94     -32.844  33.289 -28.250  1.00 40.51           C
ANISOU  767  CB  ILE C  94     4994   5206   5191    263   -329   -267       C
ATOM    768  CG1 ILE C  94     -32.659  34.432 -27.260  1.00 41.31           C
ANISOU  768  CG1 ILE C  94     5127   5274   5295    281   -331   -252       C
ATOM    769  CG2 ILE C  94     -33.488  32.099 -27.588  1.00 34.62           C
ANISOU  769  CG2 ILE C  94     4147   4533   4476    208   -317   -309       C
ATOM    770  CD1 ILE C  94     -33.937  35.170 -27.024  1.00 47.26           C
ANISOU  770  CD1 ILE C  94     5860   6082   6015    363   -380   -308       C
ATOM    771  N   ARG C  95     -32.033  31.460 -30.814  1.00 46.05           N
ANISOU  771  N   ARG C  95     5722   5891   5884    220   -304   -239       N
ATOM    772  CA  ARG C  95     -32.069  30.166 -31.508  1.00 39.77           C
ANISOU  772  CA  ARG C  95     4886   5126   5100    181   -292   -250       C
ATOM    773  C   ARG C  95     -30.671  29.642 -31.759  1.00 34.17           C
ANISOU  773  C   ARG C  95     4211   4353   4417    116   -249   -195       C
ATOM    774  O   ARG C  95     -30.437  28.430 -31.705  1.00 43.87           O
ANISOU  774  O   ARG C  95     5396   5598   5674     57   -225   -196       O
ATOM    775  CB  ARG C  95     -32.784  30.266 -32.846  1.00 44.90           C
ANISOU  775  CB  ARG C  95     5554   5804   5701    253   -330   -281       C
ATOM    776  CG  ARG C  95     -34.161  30.851 -32.806  1.00 45.86           C
ANISOU  776  CG  ARG C  95     5645   5994   5786    336   -382   -347       C
ATOM    777  CD  ARG C  95     -34.865  30.542 -34.094  1.00 45.68           C
ANISOU  777  CD  ARG C  95     5618   6016   5723    394   -418   -389       C
ATOM    778  NE  ARG C  95     -35.959  29.648 -33.788  1.00 52.31           N
ANISOU  778  NE  ARG C  95     6343   6957   6576    374   -426   -466       N
ATOM    779  CZ  ARG C  95     -36.061  28.432 -34.272  1.00 50.24           C
ANISOU  779  CZ  ARG C  95     6030   6729   6328    321   -406   -487       C
ATOM    780  NH1 ARG C  95     -35.135  27.992 -35.096  1.00 39.39           N
ANISOU  780  NH1 ARG C  95     4709   5300   4959    292   -383   -433       N
ATOM    781  NH2 ARG C  95     -37.084  27.670 -33.920  1.00 61.39           N
ANISOU  781  NH2 ARG C  95     7341   8234   7751    293   -405   -565       N
ATOM    782  N   VAL C  96     -29.747  30.542 -32.097  1.00 36.50           N
ANISOU  782  N   VAL C  96     4589   4578   4701    128   -237   -153       N
ATOM    783  CA  VAL C  96     -28.371  30.164 -32.389  1.00 38.76           C
ANISOU  783  CA  VAL C  96     4906   4810   5011     69   -195   -112       C
ATOM    784  C   VAL C  96     -27.670  29.667 -31.122  1.00 50.05           C
ANISOU  784  C   VAL C  96     6291   6236   6491      4   -166   -100       C
ATOM    785  O   VAL C  96     -27.018  28.611 -31.128  1.00 48.12           O
ANISOU  785  O   VAL C  96     6019   5990   6273    -48   -143    -91       O
ATOM    786  CB  VAL C  96     -27.649  31.359 -33.040  1.00 36.85           C
ANISOU  786  CB  VAL C  96     4766   4497   4737     93   -183    -82       C
ATOM    787  CG1 VAL C  96     -26.161  31.098 -33.234  1.00 34.88           C
ANISOU  787  CG1 VAL C  96     4542   4198   4514     25   -134    -50       C
ATOM    788  CG2 VAL C  96     -28.283  31.657 -34.346  1.00 32.47           C
ANISOU  788  CG2 VAL C  96     4267   3944   4128    159   -211    -92       C
ATOM    789  N   ASP C  97     -27.838  30.390 -30.007  1.00 41.43           N
ANISOU  789  N   ASP C  97     5191   5142   5406     12   -172   -103       N
ATOM    790  CA  ASP C  97     -27.263  29.968 -28.728  1.00 32.96           C
ANISOU  790  CA  ASP C  97     4080   4069   4375    -40   -150    -96       C
ATOM    791  C   ASP C  97     -27.811  28.620 -28.259  1.00 44.03           C
ANISOU  791  C   ASP C  97     5415   5518   5794    -73   -149   -117       C
ATOM    792  O   ASP C  97     -27.072  27.806 -27.681  1.00 36.33           O
ANISOU  792  O   ASP C  97     4426   4532   4848   -120   -127   -106       O
ATOM    793  CB  ASP C  97     -27.544  31.019 -27.672  1.00 32.67           C
ANISOU  793  CB  ASP C  97     4047   4027   4338    -18   -161   -100       C
ATOM    794  CG  ASP C  97     -26.652  32.224 -27.792  1.00 49.55           C
ANISOU  794  CG  ASP C  97     6254   6104   6468    -12   -145    -75       C
ATOM    795  OD1 ASP C  97     -25.717  32.209 -28.637  1.00 46.19           O
ANISOU  795  OD1 ASP C  97     5871   5639   6040    -33   -121    -56       O
ATOM    796  OD2 ASP C  97     -26.891  33.189 -27.021  1.00 50.29           O
ANISOU  796  OD2 ASP C  97     6362   6190   6557     10   -154    -78       O
ATOM    797  N   VAL C  98     -29.113  28.380 -28.447  1.00 39.64           N
ANISOU  797  N   VAL C  98     4824   5017   5220    -49   -171   -156       N
ATOM    798  CA  VAL C  98     -29.695  27.150 -27.915  1.00 40.84           C
ANISOU  798  CA  VAL C  98     4920   5213   5385    -92   -160   -183       C
ATOM    799  C   VAL C  98     -29.218  25.955 -28.712  1.00 37.92           C
ANISOU  799  C   VAL C  98     4552   4835   5021   -128   -141   -174       C
ATOM    800  O   VAL C  98     -28.937  24.886 -28.148  1.00 38.69           O
ANISOU  800  O   VAL C  98     4635   4929   5136   -178   -118   -172       O
ATOM    801  CB  VAL C  98     -31.236  27.207 -27.890  1.00 38.42           C
ANISOU  801  CB  VAL C  98     4564   4977   5057    -65   -183   -242       C
ATOM    802  CG1 VAL C  98     -31.783  25.802 -27.746  1.00 34.05           C
ANISOU  802  CG1 VAL C  98     3963   4464   4509   -122   -160   -276       C
ATOM    803  CG2 VAL C  98     -31.721  28.023 -26.714  1.00 25.23           C
ANISOU  803  CG2 VAL C  98     2876   3321   3388    -50   -192   -258       C
ATOM    804  N   LEU C  99     -29.144  26.113 -30.035  1.00 40.33           N
ANISOU  804  N   LEU C  99     4882   5135   5308    -99   -153   -169       N
ATOM    805  CA  LEU C  99     -28.819  25.012 -30.934  1.00 36.75           C
ANISOU  805  CA  LEU C  99     4428   4680   4857   -126   -139   -165       C
ATOM    806  C   LEU C  99     -27.333  24.729 -30.919  1.00 44.85           C
ANISOU  806  C   LEU C  99     5486   5650   5905   -158   -114   -124       C
ATOM    807  O   LEU C  99     -26.928  23.562 -30.994  1.00 48.67           O
ANISOU  807  O   LEU C  99     5961   6130   6401   -196    -96   -121       O
ATOM    808  CB  LEU C  99     -29.278  25.329 -32.355  1.00 29.81           C
ANISOU  808  CB  LEU C  99     3567   3815   3945    -79   -162   -177       C
ATOM    809  CG  LEU C  99     -29.610  24.257 -33.403  1.00 36.38           C
ANISOU  809  CG  LEU C  99     4379   4675   4767    -91   -160   -197       C
ATOM    810  CD1 LEU C  99     -28.912  24.606 -34.687  1.00 45.31           C
ANISOU  810  CD1 LEU C  99     5567   5769   5882    -65   -163   -169       C
ATOM    811  CD2 LEU C  99     -29.311  22.815 -33.013  1.00 39.38           C
ANISOU  811  CD2 LEU C  99     4733   5056   5172   -159   -129   -198       C
ATOM    812  N   GLU C 100     -26.508  25.779 -30.803  1.00 36.35           N
ANISOU  812  N   GLU C 100     4448   4533   4832   -144   -111    -98       N
ATOM    813  CA  GLU C 100     -25.085  25.540 -30.645  1.00 26.63           C
ANISOU  813  CA  GLU C 100     3233   3260   3624   -176    -87    -74       C
ATOM    814  C   GLU C 100     -24.818  24.639 -29.452  1.00 32.91           C
ANISOU  814  C   GLU C 100     4001   4061   4444   -210    -78    -77       C
ATOM    815  O   GLU C 100     -23.993  23.726 -29.534  1.00 39.80           O
ANISOU  815  O   GLU C 100     4874   4920   5330   -234    -64    -71       O
ATOM    816  CB  GLU C 100     -24.314  26.841 -30.490  1.00 34.71           C
ANISOU  816  CB  GLU C 100     4296   4245   4649   -166    -79    -57       C
ATOM    817  CG  GLU C 100     -22.817  26.587 -30.404  1.00 36.79           C
ANISOU  817  CG  GLU C 100     4565   4478   4937   -201    -52    -48       C
ATOM    818  CD  GLU C 100     -22.055  27.699 -29.739  1.00 51.64           C
ANISOU  818  CD  GLU C 100     6464   6330   6827   -207    -39    -44       C
ATOM    819  OE1 GLU C 100     -22.108  28.843 -30.239  1.00 52.68           O
ANISOU  819  OE1 GLU C 100     6643   6436   6936   -191    -33    -38       O
ATOM    820  OE2 GLU C 100     -21.386  27.427 -28.724  1.00 56.99           O
ANISOU  820  OE2 GLU C 100     7114   7009   7529   -226    -34    -50       O
ATOM    821  N   ASN C 101     -25.513  24.872 -28.332  1.00 43.06           N
ANISOU  821  N   ASN C 101     5266   5364   5731   -207    -85    -88       N
ATOM    822  CA  ASN C 101     -25.241  24.104 -27.117  1.00 40.33           C
ANISOU  822  CA  ASN C 101     4909   5015   5400   -236    -75    -89       C
ATOM    823  C   ASN C 101     -25.920  22.751 -27.159  1.00 45.82           C
ANISOU  823  C   ASN C 101     5592   5732   6086   -264    -66   -107       C
ATOM    824  O   ASN C 101     -25.355  21.752 -26.698  1.00 54.16           O
ANISOU  824  O   ASN C 101     6663   6769   7148   -288    -53   -101       O
ATOM    825  CB  ASN C 101     -25.682  24.890 -25.890  1.00 38.99           C
ANISOU  825  CB  ASN C 101     4728   4852   5232   -227    -82    -95       C
ATOM    826  CG  ASN C 101     -24.721  26.017 -25.555  1.00 48.65           C
ANISOU  826  CG  ASN C 101     5970   6046   6470   -212    -83    -78       C
ATOM    827  OD1 ASN C 101     -23.723  25.821 -24.853  1.00 51.90           O
ANISOU  827  OD1 ASN C 101     6386   6436   6898   -224    -76    -72       O
ATOM    828  ND2 ASN C 101     -25.015  27.206 -26.060  1.00 49.71           N
ANISOU  828  ND2 ASN C 101     6120   6177   6593   -183    -92    -77       N
ATOM    829  N   GLN C 102     -27.125  22.708 -27.724  1.00 36.31           N
ANISOU  829  N   GLN C 102     4364   4566   4864   -260    -72   -133       N
ATOM    830  CA  GLN C 102     -27.834  21.452 -27.889  1.00 35.63           C
ANISOU  830  CA  GLN C 102     4265   4505   4768   -296    -56   -158       C
ATOM    831  C   GLN C 102     -27.104  20.530 -28.850  1.00 43.70           C
ANISOU  831  C   GLN C 102     5308   5506   5792   -308    -47   -144       C
ATOM    832  O   GLN C 102     -27.083  19.312 -28.652  1.00 41.17           O
ANISOU  832  O   GLN C 102     4999   5176   5467   -344    -28   -150       O
ATOM    833  CB  GLN C 102     -29.243  21.725 -28.395  1.00 45.88           C
ANISOU  833  CB  GLN C 102     5524   5861   6048   -283    -68   -202       C
ATOM    834  CG  GLN C 102     -30.022  20.467 -28.653  1.00 51.31           C
ANISOU  834  CG  GLN C 102     6192   6580   6724   -328    -46   -239       C
ATOM    835  CD  GLN C 102     -30.390  19.804 -27.361  1.00 54.69           C
ANISOU  835  CD  GLN C 102     6623   7008   7150   -379    -16   -257       C
ATOM    836  OE1 GLN C 102     -30.819  20.477 -26.421  1.00 55.79           O
ANISOU  836  OE1 GLN C 102     6746   7161   7289   -374    -20   -269       O
ATOM    837  NE2 GLN C 102     -30.201  18.490 -27.282  1.00 52.50           N
ANISOU  837  NE2 GLN C 102     6374   6707   6865   -429     15   -257       N
ATOM    838  N   ALA C 103     -26.507  21.097 -29.904  1.00 42.48           N
ANISOU  838  N   ALA C 103     5163   5338   5639   -279    -59   -126       N
ATOM    839  CA  ALA C 103     -25.795  20.282 -30.882  1.00 44.01           C
ANISOU  839  CA  ALA C 103     5374   5515   5835   -290    -51   -115       C
ATOM    840  C   ALA C 103     -24.569  19.619 -30.265  1.00 44.96           C
ANISOU  840  C   ALA C 103     5516   5596   5970   -305    -39    -96       C
ATOM    841  O   ALA C 103     -24.241  18.472 -30.602  1.00 42.79           O
ANISOU  841  O   ALA C 103     5255   5311   5693   -324    -29    -97       O
ATOM    842  CB  ALA C 103     -25.393  21.132 -32.087  1.00 44.52           C
ANISOU  842  CB  ALA C 103     5451   5570   5894   -259    -61   -102       C
ATOM    843  N   MET C 104     -23.874  20.324 -29.364  1.00 38.10           N
ANISOU  843  N   MET C 104     4654   4708   5115   -294    -44    -84       N
ATOM    844  CA  MET C 104     -22.744  19.701 -28.682  1.00 39.95           C
ANISOU  844  CA  MET C 104     4906   4913   5359   -297    -40    -77       C
ATOM    845  C   MET C 104     -23.219  18.626 -27.714  1.00 38.37           C
ANISOU  845  C   MET C 104     4725   4708   5146   -318    -32    -85       C
ATOM    846  O   MET C 104     -22.586  17.573 -27.595  1.00 45.57           O
ANISOU  846  O   MET C 104     5666   5597   6052   -321    -28    -84       O
ATOM    847  CB  MET C 104     -21.901  20.748 -27.956  1.00 48.93           C
ANISOU  847  CB  MET C 104     6040   6038   6513   -280    -47    -71       C
ATOM    848  CG  MET C 104     -20.710  20.156 -27.181  1.00 48.12           C
ANISOU  848  CG  MET C 104     5950   5915   6419   -272    -51    -75       C
ATOM    849  SD  MET C 104     -19.466  19.357 -28.236  1.00 57.50           S
ANISOU  849  SD  MET C 104     7141   7094   7612   -268    -48    -83       S
ATOM    850  CE  MET C 104     -18.788  20.795 -29.071  1.00 49.11           C
ANISOU  850  CE  MET C 104     6058   6035   6566   -269    -38    -85       C
ATOM    851  N   ASP C 105     -24.335  18.867 -27.022  1.00 41.86           N
ANISOU  851  N   ASP C 105     5157   5168   5578   -331    -27    -96       N
ATOM    852  CA  ASP C 105     -24.946  17.819 -26.209  1.00 34.92           C
ANISOU  852  CA  ASP C 105     4305   4283   4679   -364     -8   -109       C
ATOM    853  C   ASP C 105     -25.261  16.581 -27.053  1.00 44.80           C
ANISOU  853  C   ASP C 105     5572   5534   5915   -393     10   -120       C
ATOM    854  O   ASP C 105     -24.920  15.448 -26.679  1.00 44.37           O
ANISOU  854  O   ASP C 105     5568   5446   5845   -408     23   -118       O
ATOM    855  CB  ASP C 105     -26.222  18.344 -25.551  1.00 34.18           C
ANISOU  855  CB  ASP C 105     4186   4223   4579   -382     -0   -131       C
ATOM    856  CG  ASP C 105     -25.956  19.190 -24.326  1.00 53.35           C
ANISOU  856  CG  ASP C 105     6616   6641   7015   -364    -10   -122       C
ATOM    857  OD1 ASP C 105     -24.779  19.499 -24.026  1.00 50.39           O
ANISOU  857  OD1 ASP C 105     6256   6238   6653   -336    -25   -101       O
ATOM    858  OD2 ASP C 105     -26.951  19.559 -23.663  1.00 69.63           O
ANISOU  858  OD2 ASP C 105     8659   8728   9069   -379     -3   -142       O
ATOM    859  N   THR C 106     -25.902  16.785 -28.211  1.00 45.80           N
ANISOU  859  N   THR C 106     5663   5695   6043   -396      8   -134       N
ATOM    860  CA  THR C 106     -26.338  15.657 -29.029  1.00 47.33           C
ANISOU  860  CA  THR C 106     5865   5896   6223   -427     26   -151       C
ATOM    861  C   THR C 106     -25.156  14.885 -29.586  1.00 45.92           C
ANISOU  861  C   THR C 106     5721   5679   6046   -415     23   -129       C
ATOM    862  O   THR C 106     -25.173  13.645 -29.619  1.00 44.96           O
ANISOU  862  O   THR C 106     5639   5537   5908   -442     43   -136       O
ATOM    863  CB  THR C 106     -27.233  16.132 -30.168  1.00 49.64           C
ANISOU  863  CB  THR C 106     6108   6239   6514   -421     18   -174       C
ATOM    864  OG1 THR C 106     -28.418  16.737 -29.620  1.00 53.05           O
ANISOU  864  OG1 THR C 106     6504   6714   6940   -429     18   -207       O
ATOM    865  CG2 THR C 106     -27.620  14.934 -31.043  1.00 42.88           C
ANISOU  865  CG2 THR C 106     5257   5392   5644   -455     37   -195       C
ATOM    866  N   ARG C 107     -24.114  15.600 -30.008  1.00 37.23           N
ANISOU  866  N   ARG C 107     4610   4570   4965   -377      2   -108       N
ATOM    867  CA  ARG C 107     -22.905  14.937 -30.481  1.00 41.39           C
ANISOU  867  CA  ARG C 107     5162   5068   5497   -362     -2    -97       C
ATOM    868  C   ARG C 107     -22.271  14.055 -29.397  1.00 48.96           C
ANISOU  868  C   ARG C 107     6172   5988   6443   -357     -1    -94       C
ATOM    869  O   ARG C 107     -21.916  12.893 -29.661  1.00 37.83           O
ANISOU  869  O   ARG C 107     4801   4553   5017   -361      5    -96       O
ATOM    870  CB  ARG C 107     -21.928  15.991 -30.983  1.00 39.43           C
ANISOU  870  CB  ARG C 107     4889   4822   5271   -332    -18    -86       C
ATOM    871  CG  ARG C 107     -20.601  15.460 -31.390  1.00 42.94           C
ANISOU  871  CG  ARG C 107     5346   5247   5722   -316    -22    -85       C
ATOM    872  CD  ARG C 107     -19.571  16.579 -31.273  1.00 51.78           C
ANISOU  872  CD  ARG C 107     6444   6368   6863   -294    -30    -85       C
ATOM    873  NE  ARG C 107     -19.948  17.751 -32.065  1.00 46.33           N
ANISOU  873  NE  ARG C 107     5733   5692   6177   -299    -25    -79       N
ATOM    874  CZ  ARG C 107     -19.793  17.829 -33.381  1.00 42.78           C
ANISOU  874  CZ  ARG C 107     5282   5247   5726   -303    -18    -78       C
ATOM    875  NH1 ARG C 107     -19.257  16.807 -34.027  1.00 49.66           N
ANISOU  875  NH1 ARG C 107     6159   6113   6596   -307    -14    -84       N
ATOM    876  NH2 ARG C 107     -20.151  18.920 -34.047  1.00 40.74           N
ANISOU  876  NH2 ARG C 107     5022   4994   5462   -300    -14    -71       N
ATOM    877  N   LEU C 108     -22.128  14.589 -28.158  1.00 39.28           N
ANISOU  877  N   LEU C 108     4953   4753   5218   -344     -8    -90       N
ATOM    878  CA  LEU C 108     -21.438  13.839 -27.097  1.00 38.70           C
ANISOU  878  CA  LEU C 108     4937   4641   5127   -325    -14    -88       C
ATOM    879  C   LEU C 108     -22.280  12.690 -26.579  1.00 46.81           C
ANISOU  879  C   LEU C 108     6026   5641   6117   -362     13    -94       C
ATOM    880  O   LEU C 108     -21.728  11.676 -26.145  1.00 53.00           O
ANISOU  880  O   LEU C 108     6881   6383   6875   -346     12    -93       O
ATOM    881  CB  LEU C 108     -21.041  14.745 -25.930  1.00 30.77           C
ANISOU  881  CB  LEU C 108     3924   3636   4132   -299    -31    -85       C
ATOM    882  CG  LEU C 108     -20.053  15.846 -26.345  1.00 42.82           C
ANISOU  882  CG  LEU C 108     5398   5182   5691   -269    -50    -86       C
ATOM    883  CD1 LEU C 108     -19.617  16.707 -25.186  1.00 45.80           C
ANISOU  883  CD1 LEU C 108     5765   5559   6077   -245    -65    -89       C
ATOM    884  CD2 LEU C 108     -18.843  15.236 -27.020  1.00 43.42           C
ANISOU  884  CD2 LEU C 108     5479   5250   5771   -242    -63    -96       C
ATOM    885  N   ASP C 109     -23.606  12.827 -26.607  1.00 53.10           N
ANISOU  885  N   ASP C 109     6804   6464   6909   -410     39   -107       N
ATOM    886  CA  ASP C 109     -24.468  11.692 -26.301  1.00 53.17           C
ANISOU  886  CA  ASP C 109     6869   6451   6881   -462     77   -123       C
ATOM    887  C   ASP C 109     -24.039  10.471 -27.094  1.00 51.03           C
ANISOU  887  C   ASP C 109     6645   6151   6594   -465     85   -122       C
ATOM    888  O   ASP C 109     -23.925   9.370 -26.546  1.00 52.79           O
ANISOU  888  O   ASP C 109     6956   6322   6778   -477    103   -122       O
ATOM    889  CB  ASP C 109     -25.921  12.035 -26.610  1.00 55.56           C
ANISOU  889  CB  ASP C 109     7119   6805   7187   -514    103   -152       C
ATOM    890  CG  ASP C 109     -26.606  12.728 -25.469  1.00 63.77           C
ANISOU  890  CG  ASP C 109     8146   7859   8223   -530    112   -163       C
ATOM    891  OD1 ASP C 109     -26.044  12.741 -24.350  1.00 75.43           O
ANISOU  891  OD1 ASP C 109     9673   9298   9689   -510    106   -146       O
ATOM    892  OD2 ASP C 109     -27.715  13.255 -25.687  1.00 67.73           O
ANISOU  892  OD2 ASP C 109     8589   8414   8731   -557    122   -193       O
ATOM    893  N   PHE C 110     -23.766  10.669 -28.390  1.00 52.62           N
ANISOU  893  N   PHE C 110     6795   6380   6819   -452     70   -121       N
ATOM    894  CA  PHE C 110     -23.374   9.591 -29.286  1.00 46.45           C
ANISOU  894  CA  PHE C 110     6046   5578   6026   -454     76   -122       C
ATOM    895  C   PHE C 110     -21.892   9.259 -29.156  1.00 51.22           C
ANISOU  895  C   PHE C 110     6687   6146   6629   -394     45   -107       C
ATOM    896  O   PHE C 110     -21.507   8.095 -29.288  1.00 56.40           O
ANISOU  896  O   PHE C 110     7409   6762   7258   -387     50   -109       O
ATOM    897  CB  PHE C 110     -23.707   9.981 -30.729  1.00 47.18           C
ANISOU  897  CB  PHE C 110     6067   5717   6142   -463     73   -130       C
ATOM    898  CG  PHE C 110     -23.312   8.950 -31.756  1.00 50.77           C
ANISOU  898  CG  PHE C 110     6547   6157   6589   -465     77   -132       C
ATOM    899  CD1 PHE C 110     -23.760   7.631 -31.658  1.00 56.30           C
ANISOU  899  CD1 PHE C 110     7314   6824   7254   -506    110   -145       C
ATOM    900  CD2 PHE C 110     -22.497   9.290 -32.810  1.00 52.30           C
ANISOU  900  CD2 PHE C 110     6702   6364   6804   -431     54   -123       C
ATOM    901  CE1 PHE C 110     -23.412   6.669 -32.603  1.00 56.01           C
ANISOU  901  CE1 PHE C 110     7302   6770   7208   -507    114   -148       C
ATOM    902  CE2 PHE C 110     -22.137   8.327 -33.778  1.00 56.46           C
ANISOU  902  CE2 PHE C 110     7249   6879   7324   -433     59   -127       C
ATOM    903  CZ  PHE C 110     -22.597   7.016 -33.669  1.00 54.41           C
ANISOU  903  CZ  PHE C 110     7054   6588   7032   -468     86   -139       C
ATOM    904  N   ALA C 111     -21.038  10.267 -28.946  1.00 40.96           N
ANISOU  904  N   ALA C 111     5343   4862   5357   -348     13   -100       N
ATOM    905  CA  ALA C 111     -19.612   9.995 -28.787  1.00 40.51           C
ANISOU  905  CA  ALA C 111     5307   4784   5299   -288    -18   -101       C
ATOM    906  C   ALA C 111     -19.313   9.234 -27.499  1.00 52.88           C
ANISOU  906  C   ALA C 111     6964   6301   6827   -260    -25   -101       C
ATOM    907  O   ALA C 111     -18.372   8.433 -27.460  1.00 55.41           O
ANISOU  907  O   ALA C 111     7334   6593   7127   -212    -46   -109       O
ATOM    908  CB  ALA C 111     -18.824  11.299 -28.808  1.00 31.23           C
ANISOU  908  CB  ALA C 111     4062   3643   4162   -257    -42   -103       C
ATOM    909  N   ARG C 112     -20.087   9.490 -26.437  1.00 44.28           N
ANISOU  909  N   ARG C 112     5901   5202   5723   -285     -8    -96       N
ATOM    910  CA  ARG C 112     -19.905   8.774 -25.179  1.00 43.36           C
ANISOU  910  CA  ARG C 112     5885   5031   5560   -261    -11    -94       C
ATOM    911  C   ARG C 112     -20.053   7.269 -25.368  1.00 50.89           C
ANISOU  911  C   ARG C 112     6942   5929   6464   -274     11    -96       C
ATOM    912  O   ARG C 112     -19.322   6.485 -24.747  1.00 51.15           O
ANISOU  912  O   ARG C 112     7068   5911   6456   -220     -9    -97       O
ATOM    913  CB  ARG C 112     -20.911   9.277 -24.134  1.00 48.10           C
ANISOU  913  CB  ARG C 112     6494   5631   6150   -303     15    -90       C
ATOM    914  CG  ARG C 112     -20.446  10.478 -23.283  1.00 46.29           C
ANISOU  914  CG  ARG C 112     6218   5425   5945   -264    -15    -88       C
ATOM    915  CD  ARG C 112     -21.366  10.673 -22.063  1.00 46.38           C
ANISOU  915  CD  ARG C 112     6267   5421   5932   -300     11    -85       C
ATOM    916  NE  ARG C 112     -22.691  11.190 -22.424  1.00 46.35           N
ANISOU  916  NE  ARG C 112     6205   5459   5948   -370     46    -92       N
ATOM    917  CZ  ARG C 112     -22.932  12.468 -22.736  1.00 56.55           C
ANISOU  917  CZ  ARG C 112     7399   6804   7283   -372     34    -93       C
ATOM    918  NH1 ARG C 112     -21.937  13.364 -22.724  1.00 49.88           N
ANISOU  918  NH1 ARG C 112     6507   5976   6470   -318     -4    -86       N
ATOM    919  NH2 ARG C 112     -24.165  12.858 -23.068  1.00 57.74           N
ANISOU  919  NH2 ARG C 112     7501   6994   7443   -425     61   -107       N
ATOM    920  N   VAL C 113     -21.002   6.842 -26.210  1.00 54.14           N
ANISOU  920  N   VAL C 113     7344   6349   6876   -342     51   -100       N
ATOM    921  CA  VAL C 113     -21.212   5.409 -26.399  1.00 59.68           C
ANISOU  921  CA  VAL C 113     8150   6996   7530   -365     80   -104       C
ATOM    922  C   VAL C 113     -20.194   4.830 -27.383  1.00 59.74           C
ANISOU  922  C   VAL C 113     8158   6999   7543   -315     50   -106       C
ATOM    923  O   VAL C 113     -19.714   3.698 -27.203  1.00 58.51           O
ANISOU  923  O   VAL C 113     8108   6783   7340   -283     46   -108       O
ATOM    924  CB  VAL C 113     -22.673   5.116 -26.811  1.00 60.44           C
ANISOU  924  CB  VAL C 113     8238   7106   7620   -465    140   -119       C
ATOM    925  CG1 VAL C 113     -23.111   6.028 -27.902  1.00 65.20           C
ANISOU  925  CG1 VAL C 113     8710   7786   8276   -487    135   -127       C
ATOM    926  CG2 VAL C 113     -22.833   3.665 -27.272  1.00 63.37           C
ANISOU  926  CG2 VAL C 113     8706   7425   7947   -496    173   -127       C
ATOM    927  N   CYS C 114     -19.813   5.590 -28.415  1.00 56.60           N
ANISOU  927  N   CYS C 114     7649   6659   7197   -302     28   -108       N
ATOM    928  CA  CYS C 114     -18.817   5.065 -29.351  1.00 61.03           C
ANISOU  928  CA  CYS C 114     8204   7220   7763   -257      2   -116       C
ATOM    929  C   CYS C 114     -17.463   4.881 -28.680  1.00 61.38           C
ANISOU  929  C   CYS C 114     8288   7242   7792   -165    -46   -125       C
ATOM    930  O   CYS C 114     -16.759   3.904 -28.961  1.00 60.78           O
ANISOU  930  O   CYS C 114     8271   7135   7689   -120    -64   -136       O
ATOM    931  CB  CYS C 114     -18.689   5.968 -30.571  1.00 61.99           C
ANISOU  931  CB  CYS C 114     8208   7406   7940   -268     -5   -118       C
ATOM    932  SG  CYS C 114     -20.108   5.808 -31.637  1.00 69.05           S
ANISOU  932  SG  CYS C 114     9070   8325   8841   -353     40   -119       S
ATOM    933  N   TYR C 115     -17.092   5.793 -27.775  1.00 57.50           N
ANISOU  933  N   TYR C 115     7765   6768   7314   -132    -70   -126       N
ATOM    934  CA  TYR C 115     -15.818   5.717 -27.072  1.00 52.48           C
ANISOU  934  CA  TYR C 115     7154   6123   6664    -40   -121   -146       C
ATOM    935  C   TYR C 115     -15.855   4.766 -25.881  1.00 67.35           C
ANISOU  935  C   TYR C 115     9178   7934   8479     -3   -126   -142       C
ATOM    936  O   TYR C 115     -14.843   4.619 -25.180  1.00 69.31           O
ANISOU  936  O   TYR C 115     9460   8170   8702     86   -174   -163       O
ATOM    937  CB  TYR C 115     -15.388   7.115 -26.633  1.00 50.50           C
ANISOU  937  CB  TYR C 115     6807   5924   6456    -23   -142   -155       C
ATOM    938  CG  TYR C 115     -14.733   7.902 -27.745  1.00 52.39           C
ANISOU  938  CG  TYR C 115     6932   6225   6750    -25   -151   -172       C
ATOM    939  CD1 TYR C 115     -13.479   7.538 -28.220  1.00 43.20           C
ANISOU  939  CD1 TYR C 115     5749   5078   5589     35   -184   -208       C
ATOM    940  CD2 TYR C 115     -15.369   9.006 -28.322  1.00 48.03           C
ANISOU  940  CD2 TYR C 115     6296   5712   6240    -86   -124   -158       C
ATOM    941  CE1 TYR C 115     -12.868   8.240 -29.232  1.00 38.51           C
ANISOU  941  CE1 TYR C 115     5057   4537   5040     24   -183   -229       C
ATOM    942  CE2 TYR C 115     -14.764   9.725 -29.348  1.00 44.42           C
ANISOU  942  CE2 TYR C 115     5753   5301   5824    -92   -126   -173       C
ATOM    943  CZ  TYR C 115     -13.510   9.333 -29.806  1.00 50.95           C
ANISOU  943  CZ  TYR C 115     6563   6142   6654    -43   -151   -209       C
ATOM    944  OH  TYR C 115     -12.872  10.028 -30.830  1.00 56.70           O
ANISOU  944  OH  TYR C 115     7210   6915   7419    -57   -145   -229       O
ATOM    945  N   ASN C 116     -16.965   4.094 -25.668  1.00 71.06           N
ANISOU  945  N   ASN C 116     9734   8356   8912    -67    -78   -123       N
ATOM    946  CA  ASN C 116     -17.197   3.229 -24.526  1.00 69.60           C
ANISOU  946  CA  ASN C 116     9700   8091   8653    -51    -68   -115       C
ATOM    947  C   ASN C 116     -16.893   1.781 -24.886  1.00 65.99           C
ANISOU  947  C   ASN C 116     9364   7568   8140    -22    -67   -120       C
ATOM    948  O   ASN C 116     -17.413   1.274 -25.894  1.00 68.26           O
ANISOU  948  O   ASN C 116     9644   7856   8436    -82    -31   -118       O
ATOM    949  CB  ASN C 116     -18.649   3.372 -24.076  1.00 75.01           C
ANISOU  949  CB  ASN C 116    10409   8762   9328   -154     -4    -99       C
ATOM    950  CG  ASN C 116     -18.874   2.892 -22.677  1.00 72.42           C
ANISOU  950  CG  ASN C 116    10222   8362   8933   -143      9    -92       C
ATOM    951  OD1 ASN C 116     -18.292   1.905 -22.258  1.00 69.64           O
ANISOU  951  OD1 ASN C 116    10003   7941   8517    -81     -9    -94       O
ATOM    952  ND2 ASN C 116     -19.733   3.591 -21.940  1.00 73.69           N
ANISOU  952  ND2 ASN C 116    10360   8537   9102   -200     41    -86       N
ATOM    953  N   PRO C 117     -16.060   1.094 -24.101  1.00 62.09           N
ANISOU  953  N   PRO C 117     8986   7019   7586     73   -108   -130       N
ATOM    954  CA  PRO C 117     -15.792  -0.331 -24.364  1.00 63.90           C
ANISOU  954  CA  PRO C 117     9354   7174   7750    109   -108   -134       C
ATOM    955  C   PRO C 117     -17.039  -1.194 -24.500  1.00 66.52           C
ANISOU  955  C   PRO C 117     9791   7442   8041      3    -29   -115       C
ATOM    956  O   PRO C 117     -17.003  -2.180 -25.246  1.00 70.70           O
ANISOU  956  O   PRO C 117    10383   7936   8545     -3    -15   -119       O
ATOM    957  CB  PRO C 117     -14.963  -0.759 -23.146  1.00 65.57           C
ANISOU  957  CB  PRO C 117     9693   7329   7891    225   -160   -144       C
ATOM    958  CG  PRO C 117     -14.342   0.490 -22.645  1.00 59.85           C
ANISOU  958  CG  PRO C 117     8847   6679   7217    274   -208   -160       C
ATOM    959  CD  PRO C 117     -15.291   1.608 -22.956  1.00 60.52           C
ANISOU  959  CD  PRO C 117     8798   6824   7373    162   -161   -141       C
ATOM    960  N   ASP C 118     -18.138  -0.868 -23.811  1.00 69.66           N
ANISOU  960  N   ASP C 118    10211   7827   8430    -85     26   -101       N
ATOM    961  CA  ASP C 118     -19.373  -1.634 -23.950  1.00 73.53           C
ANISOU  961  CA  ASP C 118    10786   8267   8884   -200    111    -97       C
ATOM    962  C   ASP C 118     -20.266  -1.084 -25.057  1.00 65.78           C
ANISOU  962  C   ASP C 118     9654   7364   7973   -302    151   -104       C
ATOM    963  O   ASP C 118     -21.495  -1.169 -24.969  1.00 61.49           O
ANISOU  963  O   ASP C 118     9123   6818   7423   -412    221   -111       O
ATOM    964  CB  ASP C 118     -20.139  -1.666 -22.626  1.00 75.73           C
ANISOU  964  CB  ASP C 118    11175   8491   9110   -248    157    -89       C
ATOM    965  CG  ASP C 118     -19.244  -1.925 -21.446  1.00 89.67           C
ANISOU  965  CG  ASP C 118    13070  10190  10809   -135    107    -82       C
ATOM    966  OD1 ASP C 118     -19.247  -1.098 -20.511  1.00 95.38           O
ANISOU  966  OD1 ASP C 118    13763  10934  11542   -118     91    -77       O
ATOM    967  OD2 ASP C 118     -18.515  -2.950 -21.463  1.00 93.38           O
ANISOU  967  OD2 ASP C 118    13672  10590  11217    -56     79    -84       O
ATOM    968  N   PHE C 119     -19.662  -0.488 -26.084  1.00 70.06           N
ANISOU  968  N   PHE C 119    10056   7981   8582   -265    107   -108       N
ATOM    969  CA  PHE C 119     -20.401  -0.006 -27.249  1.00 65.04           C
ANISOU  969  CA  PHE C 119     9288   7418   8007   -344    135   -115       C
ATOM    970  C   PHE C 119     -21.487  -0.993 -27.678  1.00 58.86           C
ANISOU  970  C   PHE C 119     8574   6599   7190   -445    208   -127       C
ATOM    971  O   PHE C 119     -22.631  -0.590 -27.911  1.00 54.02           O
ANISOU  971  O   PHE C 119     7892   6031   6602   -538    255   -142       O
ATOM    972  CB  PHE C 119     -19.432   0.267 -28.404  1.00 58.20           C
ANISOU  972  CB  PHE C 119     8319   6603   7189   -284     84   -119       C
ATOM    973  CG  PHE C 119     -20.102   0.531 -29.721  1.00 62.52           C
ANISOU  973  CG  PHE C 119     8759   7211   7785   -353    111   -127       C
ATOM    974  CD1 PHE C 119     -20.579   1.795 -30.029  1.00 60.60           C
ANISOU  974  CD1 PHE C 119     8381   7044   7599   -385    110   -127       C
ATOM    975  CD2 PHE C 119     -20.263  -0.488 -30.650  1.00 60.98           C
ANISOU  975  CD2 PHE C 119     8605   6994   7572   -382    135   -135       C
ATOM    976  CE1 PHE C 119     -21.203   2.039 -31.240  1.00 67.01           C
ANISOU  976  CE1 PHE C 119     9103   7910   8446   -437    129   -136       C
ATOM    977  CE2 PHE C 119     -20.883  -0.244 -31.866  1.00 65.73           C
ANISOU  977  CE2 PHE C 119     9108   7653   8214   -440    156   -145       C
ATOM    978  CZ  PHE C 119     -21.352   1.018 -32.164  1.00 66.56           C
ANISOU  978  CZ  PHE C 119     9082   7835   8373   -464    151   -146       C
ATOM    979  N   GLU C 120     -21.159  -2.292 -27.726  1.00 60.55           N
ANISOU  979  N   GLU C 120     8930   6733   7343   -427    219   -128       N
ATOM    980  CA  GLU C 120     -22.085  -3.259 -28.313  1.00 63.54           C
ANISOU  980  CA  GLU C 120     9368   7081   7693   -524    290   -145       C
ATOM    981  C   GLU C 120     -23.330  -3.456 -27.458  1.00 67.61           C
ANISOU  981  C   GLU C 120     9957   7563   8168   -632    369   -159       C
ATOM    982  O   GLU C 120     -24.439  -3.549 -27.993  1.00 67.15           O
ANISOU  982  O   GLU C 120     9851   7540   8124   -740    430   -188       O
ATOM    983  CB  GLU C 120     -21.387  -4.594 -28.549  1.00 63.38           C
ANISOU  983  CB  GLU C 120     9493   6975   7612   -475    282   -142       C
ATOM    984  CG  GLU C 120     -21.774  -5.227 -29.884  1.00 72.91           C
ANISOU  984  CG  GLU C 120    10669   8200   8835   -534    314   -159       C
ATOM    985  CD  GLU C 120     -20.997  -4.650 -31.032  1.00 74.86           C
ANISOU  985  CD  GLU C 120    10769   8525   9150   -472    253   -157       C
ATOM    986  OE1 GLU C 120     -19.754  -4.602 -30.930  1.00 77.55           O
ANISOU  986  OE1 GLU C 120    11118   8858   9491   -360    186   -148       O
ATOM    987  OE2 GLU C 120     -21.623  -4.224 -32.024  1.00 77.02           O
ANISOU  987  OE2 GLU C 120    10918   8870   9475   -534    272   -170       O
ATOM    988  N   LYS C 121     -23.170  -3.546 -26.132  1.00 71.28           N
ANISOU  988  N   LYS C 121    10540   7964   8580   -605    371   -146       N
ATOM    989  CA  LYS C 121     -24.331  -3.697 -25.261  1.00 68.64           C
ANISOU  989  CA  LYS C 121    10278   7597   8204   -712    452   -163       C
ATOM    990  C   LYS C 121     -25.112  -2.396 -25.136  1.00 59.29           C
ANISOU  990  C   LYS C 121     8930   6513   7085   -763    459   -177       C
ATOM    991  O   LYS C 121     -26.340  -2.416 -24.968  1.00 55.34           O
ANISOU  991  O   LYS C 121     8419   6030   6577   -879    533   -211       O
ATOM    992  CB  LYS C 121     -23.894  -4.202 -23.883  1.00 73.59           C
ANISOU  992  CB  LYS C 121    11095   8119   8747   -663    452   -144       C
ATOM    993  CG  LYS C 121     -22.935  -5.387 -23.948  1.00 83.30           C
ANISOU  993  CG  LYS C 121    12493   9250   9909   -578    425   -129       C
ATOM    994  CD  LYS C 121     -22.530  -5.881 -22.561  1.00 88.86           C
ANISOU  994  CD  LYS C 121    13399   9844  10518   -519    421   -111       C
ATOM    995  CE  LYS C 121     -21.028  -5.707 -22.313  1.00 89.68           C
ANISOU  995  CE  LYS C 121    13512   9942  10618   -345    311    -92       C
ATOM    996  NZ  LYS C 121     -20.364  -6.993 -21.915  1.00 91.95           N
ANISOU  996  NZ  LYS C 121    14032  10105  10800   -263    298    -85       N
ATOM    997  N   LEU C 122     -24.418  -1.265 -25.231  1.00 56.47           N
ANISOU  997  N   LEU C 122     8444   6221   6789   -679    384   -158       N
ATOM    998  CA  LEU C 122     -25.063   0.037 -25.213  1.00 60.23           C
ANISOU  998  CA  LEU C 122     8765   6792   7329   -712    381   -169       C
ATOM    999  C   LEU C 122     -25.778   0.379 -26.525  1.00 66.96           C
ANISOU  999  C   LEU C 122     9473   7731   8237   -770    395   -196       C
ATOM   1000  O   LEU C 122     -26.697   1.209 -26.518  1.00 67.82           O
ANISOU 1000  O   LEU C 122     9477   7911   8380   -823    413   -220       O
ATOM   1001  CB  LEU C 122     -24.012   1.087 -24.886  1.00 54.15           C
ANISOU 1001  CB  LEU C 122     7922   6054   6599   -604    300   -140       C
ATOM   1002  CG  LEU C 122     -23.487   0.902 -23.466  1.00 53.58           C
ANISOU 1002  CG  LEU C 122     7978   5910   6472   -551    286   -122       C
ATOM   1003  CD1 LEU C 122     -22.260   1.746 -23.195  1.00 57.06           C
ANISOU 1003  CD1 LEU C 122     8357   6377   6945   -434    202   -103       C
ATOM   1004  CD2 LEU C 122     -24.602   1.211 -22.482  1.00 37.88           C
ANISOU 1004  CD2 LEU C 122     6010   3918   4463   -635    344   -137       C
ATOM   1005  N   LYS C 123     -25.397  -0.243 -27.644  1.00 62.52           N
ANISOU 1005  N   LYS C 123     8907   7167   7681   -755    384   -196       N
ATOM   1006  CA  LYS C 123     -25.877   0.208 -28.945  1.00 59.33           C
ANISOU 1006  CA  LYS C 123     8361   6849   7332   -785    380   -217       C
ATOM   1007  C   LYS C 123     -27.375  -0.020 -29.153  1.00 62.97           C
ANISOU 1007  C   LYS C 123     8794   7347   7786   -906    454   -269       C
ATOM   1008  O   LYS C 123     -28.044   0.848 -29.737  1.00 56.19           O
ANISOU 1008  O   LYS C 123     7796   6578   6974   -927    447   -294       O
ATOM   1009  CB  LYS C 123     -25.085  -0.459 -30.070  1.00 64.37           C
ANISOU 1009  CB  LYS C 123     9010   7473   7976   -741    353   -206       C
ATOM   1010  CG  LYS C 123     -25.453   0.056 -31.458  1.00 63.66           C
ANISOU 1010  CG  LYS C 123     8778   7470   7940   -758    342   -224       C
ATOM   1011  CD  LYS C 123     -24.473  -0.426 -32.515  1.00 62.26           C
ANISOU 1011  CD  LYS C 123     8602   7282   7773   -701    305   -208       C
ATOM   1012  CE  LYS C 123     -23.938  -1.829 -32.218  1.00 55.52           C
ANISOU 1012  CE  LYS C 123     7905   6330   6858   -688    322   -201       C
ATOM   1013  NZ  LYS C 123     -23.580  -2.556 -33.480  1.00 54.65           N
ANISOU 1013  NZ  LYS C 123     7791   6220   6752   -679    316   -207       N
ATOM   1014  N   PRO C 124     -27.945  -1.163 -28.740  1.00 66.81           N
ANISOU 1014  N   PRO C 124     9406   7769   8212   -986    526   -294       N
ATOM   1015  CA  PRO C 124     -29.399  -1.321 -28.910  1.00 65.88           C
ANISOU 1015  CA  PRO C 124     9244   7698   8088  -1110    601   -359       C
ATOM   1016  C   PRO C 124     -30.208  -0.275 -28.173  1.00 65.30           C
ANISOU 1016  C   PRO C 124     9086   7688   8036  -1142    611   -384       C
ATOM   1017  O   PRO C 124     -31.158   0.279 -28.747  1.00 63.73           O
ANISOU 1017  O   PRO C 124     8758   7585   7873  -1188    623   -434       O
ATOM   1018  CB  PRO C 124     -29.652  -2.735 -28.376  1.00 66.41           C
ANISOU 1018  CB  PRO C 124     9493   7662   8076  -1186    681   -375       C
ATOM   1019  CG  PRO C 124     -28.395  -3.459 -28.687  1.00 59.82           C
ANISOU 1019  CG  PRO C 124     8759   6750   7219  -1098    637   -326       C
ATOM   1020  CD  PRO C 124     -27.314  -2.453 -28.400  1.00 64.13           C
ANISOU 1020  CD  PRO C 124     9247   7315   7805   -972    545   -274       C
ATOM   1021  N   GLY C 125     -29.854   0.007 -26.915  1.00 70.82           N
ANISOU 1021  N   GLY C 125     9857   8338   8713  -1112    604   -354       N
ATOM   1022  CA  GLY C 125     -30.503   1.090 -26.193  1.00 63.23           C
ANISOU 1022  CA  GLY C 125     8811   7437   7775  -1129    605   -373       C
ATOM   1023  C   GLY C 125     -30.346   2.425 -26.893  1.00 66.52           C
ANISOU 1023  C   GLY C 125     9059   7950   8265  -1059    532   -363       C
ATOM   1024  O   GLY C 125     -31.317   3.169 -27.068  1.00 64.19           O
ANISOU 1024  O   GLY C 125     8649   7743   7999  -1097    541   -408       O
ATOM   1025  N   PHE C 126     -29.120   2.737 -27.334  1.00 66.16           N
ANISOU 1025  N   PHE C 126     9001   7891   8246   -956    460   -308       N
ATOM   1026  CA  PHE C 126     -28.890   4.030 -27.969  1.00 47.41           C
ANISOU 1026  CA  PHE C 126     6486   5595   5934   -891    397   -296       C
ATOM   1027  C   PHE C 126     -29.673   4.162 -29.266  1.00 45.02           C
ANISOU 1027  C   PHE C 126     6076   5372   5658   -925    403   -338       C
ATOM   1028  O   PHE C 126     -30.190   5.240 -29.580  1.00 50.24           O
ANISOU 1028  O   PHE C 126     6622   6112   6356   -911    378   -356       O
ATOM   1029  CB  PHE C 126     -27.412   4.267 -28.242  1.00 50.88           C
ANISOU 1029  CB  PHE C 126     6934   6005   6393   -787    329   -240       C
ATOM   1030  CG  PHE C 126     -27.154   5.623 -28.808  1.00 53.60           C
ANISOU 1030  CG  PHE C 126     7152   6419   6793   -730    274   -227       C
ATOM   1031  CD1 PHE C 126     -27.177   6.736 -27.989  1.00 57.00           C
ANISOU 1031  CD1 PHE C 126     7542   6874   7244   -704    253   -218       C
ATOM   1032  CD2 PHE C 126     -26.994   5.799 -30.158  1.00 47.64           C
ANISOU 1032  CD2 PHE C 126     6326   5707   6069   -709    250   -229       C
ATOM   1033  CE1 PHE C 126     -26.986   7.990 -28.501  1.00 61.29           C
ANISOU 1033  CE1 PHE C 126     7983   7473   7831   -656    208   -207       C
ATOM   1034  CE2 PHE C 126     -26.806   7.052 -30.681  1.00 57.47           C
ANISOU 1034  CE2 PHE C 126     7473   7007   7357   -662    207   -218       C
ATOM   1035  CZ  PHE C 126     -26.790   8.149 -29.850  1.00 66.46           C
ANISOU 1035  CZ  PHE C 126     8578   8161   8511   -635    186   -207       C
ATOM   1036  N   LEU C 127     -29.778   3.079 -30.034  1.00 48.08           N
ANISOU 1036  N   LEU C 127     6504   5739   6026   -964    433   -355       N
ATOM   1037  CA  LEU C 127     -30.547   3.152 -31.266  1.00 52.87           C
ANISOU 1037  CA  LEU C 127     7010   6423   6654   -995    438   -401       C
ATOM   1038  C   LEU C 127     -31.988   3.548 -30.978  1.00 58.24           C
ANISOU 1038  C   LEU C 127     7616   7178   7334  -1069    478   -473       C
ATOM   1039  O   LEU C 127     -32.591   4.315 -31.741  1.00 61.87           O
ANISOU 1039  O   LEU C 127     7956   7727   7824  -1054    452   -507       O
ATOM   1040  CB  LEU C 127     -30.468   1.823 -32.021  1.00 49.49           C
ANISOU 1040  CB  LEU C 127     6648   5956   6200  -1036    473   -414       C
ATOM   1041  CG  LEU C 127     -29.201   1.683 -32.875  1.00 53.78           C
ANISOU 1041  CG  LEU C 127     7204   6470   6761   -952    418   -361       C
ATOM   1042  CD1 LEU C 127     -29.054   0.296 -33.436  1.00 43.34           C
ANISOU 1042  CD1 LEU C 127     5967   5094   5405   -988    453   -370       C
ATOM   1043  CD2 LEU C 127     -29.161   2.702 -34.002  1.00 64.32           C
ANISOU 1043  CD2 LEU C 127     8408   7885   8144   -899    364   -360       C
ATOM   1044  N   LYS C 128     -32.547   3.070 -29.858  1.00 57.41           N
ANISOU 1044  N   LYS C 128     7584   7039   7192  -1144    540   -500       N
ATOM   1045  CA  LYS C 128     -33.922   3.419 -29.516  1.00 51.89           C
ANISOU 1045  CA  LYS C 128     6810   6416   6490  -1221    584   -580       C
ATOM   1046  C   LYS C 128     -34.075   4.896 -29.170  1.00 52.60           C
ANISOU 1046  C   LYS C 128     6797   6571   6617  -1160    531   -574       C
ATOM   1047  O   LYS C 128     -35.180   5.438 -29.281  1.00 50.58           O
ANISOU 1047  O   LYS C 128     6439   6406   6372  -1192    541   -645       O
ATOM   1048  CB  LYS C 128     -34.407   2.550 -28.360  1.00 53.81           C
ANISOU 1048  CB  LYS C 128     7167   6598   6679  -1322    670   -609       C
ATOM   1049  CG  LYS C 128     -34.625   1.094 -28.736  1.00 64.14           C
ANISOU 1049  CG  LYS C 128     8570   7855   7943  -1409    741   -640       C
ATOM   1050  N   GLU C 129     -32.991   5.571 -28.777  1.00 55.31           N
ANISOU 1050  N   GLU C 129     7164   6873   6978  -1069    473   -498       N
ATOM   1051  CA  GLU C 129     -33.096   6.975 -28.410  1.00 45.32           C
ANISOU 1051  CA  GLU C 129     5814   5660   5745  -1013    426   -490       C
ATOM   1052  C   GLU C 129     -33.065   7.914 -29.597  1.00 44.78           C
ANISOU 1052  C   GLU C 129     5636   5663   5717   -942    363   -488       C
ATOM   1053  O   GLU C 129     -33.360   9.102 -29.424  1.00 56.54           O
ANISOU 1053  O   GLU C 129     7051   7204   7228   -900    328   -495       O
ATOM   1054  CB  GLU C 129     -31.960   7.383 -27.488  1.00 53.18           C
ANISOU 1054  CB  GLU C 129     6875   6587   6744   -948    392   -416       C
ATOM   1055  CG  GLU C 129     -31.926   6.723 -26.159  1.00 58.84           C
ANISOU 1055  CG  GLU C 129     7706   7232   7418   -996    440   -410       C
ATOM   1056  CD  GLU C 129     -30.659   7.098 -25.417  1.00 72.72           C
ANISOU 1056  CD  GLU C 129     9524   8927   9179   -913    394   -339       C
ATOM   1057  OE1 GLU C 129     -29.969   6.183 -24.909  1.00 76.18           O
ANISOU 1057  OE1 GLU C 129    10086   9280   9580   -910    408   -309       O
ATOM   1058  OE2 GLU C 129     -30.339   8.310 -25.375  1.00 75.61           O
ANISOU 1058  OE2 GLU C 129     9814   9330   9583   -849    341   -317       O
ATOM   1059  N   ILE C 130     -32.682   7.438 -30.779  1.00 46.88           N
ANISOU 1059  N   ILE C 130     5899   5926   5989   -925    349   -478       N
ATOM   1060  CA  ILE C 130     -32.385   8.342 -31.891  1.00 46.35           C
ANISOU 1060  CA  ILE C 130     5753   5904   5953   -846    287   -460       C
ATOM   1061  C   ILE C 130     -33.643   9.021 -32.428  1.00 54.79           C
ANISOU 1061  C   ILE C 130     6713   7076   7028   -849    276   -532       C
ATOM   1062  O   ILE C 130     -33.601  10.230 -32.706  1.00 55.97           O
ANISOU 1062  O   ILE C 130     6805   7263   7197   -778    224   -519       O
ATOM   1063  CB  ILE C 130     -31.632   7.623 -33.021  1.00 41.85           C
ANISOU 1063  CB  ILE C 130     5212   5303   5385   -828    276   -432       C
ATOM   1064  CG1 ILE C 130     -30.418   6.883 -32.468  1.00 36.10           C
ANISOU 1064  CG1 ILE C 130     4592   4479   4645   -817    282   -373       C
ATOM   1065  CG2 ILE C 130     -31.200   8.631 -34.049  1.00 45.39           C
ANISOU 1065  CG2 ILE C 130     5599   5786   5861   -746    215   -407       C
ATOM   1066  CD1 ILE C 130     -29.385   6.495 -33.494  1.00 29.40           C
ANISOU 1066  CD1 ILE C 130     3764   3600   3806   -773    255   -335       C
ATOM   1067  N   PRO C 131     -34.769   8.312 -32.607  1.00 58.00           N
ANISOU 1067  N   PRO C 131     7089   7532   7416   -927    324   -614       N
ATOM   1068  CA  PRO C 131     -35.973   8.989 -33.126  1.00 52.57           C
ANISOU 1068  CA  PRO C 131     6288   6955   6732   -918    306   -695       C
ATOM   1069  C   PRO C 131     -36.383  10.230 -32.355  1.00 50.63           C
ANISOU 1069  C   PRO C 131     5990   6750   6495   -878    278   -706       C
ATOM   1070  O   PRO C 131     -36.700  11.245 -32.984  1.00 56.62           O
ANISOU 1070  O   PRO C 131     6676   7571   7265   -805    222   -723       O
ATOM   1071  CB  PRO C 131     -37.044   7.891 -33.044  1.00 45.78           C
ANISOU 1071  CB  PRO C 131     5417   6132   5847  -1031    380   -788       C
ATOM   1072  CG  PRO C 131     -36.309   6.668 -33.227  1.00 54.35           C
ANISOU 1072  CG  PRO C 131     6601   7132   6918  -1072    417   -747       C
ATOM   1073  CD  PRO C 131     -34.994   6.858 -32.507  1.00 57.51           C
ANISOU 1073  CD  PRO C 131     7093   7433   7324  -1022    394   -643       C
ATOM   1074  N   GLU C 132     -36.392  10.182 -31.013  1.00 53.01           N
ANISOU 1074  N   GLU C 132     6335   7015   6790   -921    313   -698       N
ATOM   1075  CA  GLU C 132     -36.820  11.346 -30.235  1.00 54.20           C
ANISOU 1075  CA  GLU C 132     6436   7207   6950   -887    289   -713       C
ATOM   1076  C   GLU C 132     -35.812  12.488 -30.341  1.00 47.95           C
ANISOU 1076  C   GLU C 132     5655   6381   6182   -782    220   -629       C
ATOM   1077  O   GLU C 132     -36.201  13.660 -30.416  1.00 45.42           O
ANISOU 1077  O   GLU C 132     5273   6114   5872   -720    175   -645       O
ATOM   1078  CB  GLU C 132     -37.050  10.956 -28.774  1.00 64.27           C
ANISOU 1078  CB  GLU C 132     7764   8448   8208   -964    348   -724       C
ATOM   1079  CG  GLU C 132     -38.354  10.186 -28.518  1.00 75.33           C
ANISOU 1079  CG  GLU C 132     9131   9907   9583  -1075    421   -833       C
ATOM   1080  CD  GLU C 132     -39.596  10.834 -29.160  1.00 85.59           C
ANISOU 1080  CD  GLU C 132    10294  11338  10888  -1058    397   -937       C
ATOM   1081  OE1 GLU C 132     -39.898  10.559 -30.349  1.00 83.43           O
ANISOU 1081  OE1 GLU C 132     9971  11114  10615  -1046    382   -976       O
ATOM   1082  OE2 GLU C 132     -40.284  11.610 -28.458  1.00 89.21           O
ANISOU 1082  OE2 GLU C 132    10695  11854  11349  -1052    392   -984       O
ATOM   1083  N   LYS C 133     -34.516  12.163 -30.340  1.00 43.11           N
ANISOU 1083  N   LYS C 133     5122   5680   5576   -761    213   -545       N
ATOM   1084  CA  LYS C 133     -33.490  13.142 -30.681  1.00 51.83           C
ANISOU 1084  CA  LYS C 133     6235   6756   6704   -671    155   -474       C
ATOM   1085  C   LYS C 133     -33.794  13.825 -32.009  1.00 58.70           C
ANISOU 1085  C   LYS C 133     7042   7683   7579   -610    109   -492       C
ATOM   1086  O   LYS C 133     -33.794  15.058 -32.105  1.00 59.58           O
ANISOU 1086  O   LYS C 133     7124   7815   7698   -542     64   -481       O
ATOM   1087  CB  LYS C 133     -32.117  12.466 -30.755  1.00 52.97           C
ANISOU 1087  CB  LYS C 133     6460   6813   6851   -664    158   -403       C
ATOM   1088  CG  LYS C 133     -31.634  11.817 -29.481  1.00 40.27           C
ANISOU 1088  CG  LYS C 133     4932   5137   5231   -703    192   -377       C
ATOM   1089  CD  LYS C 133     -30.211  12.242 -29.200  1.00 47.20           C
ANISOU 1089  CD  LYS C 133     5854   5954   6125   -642    158   -305       C
ATOM   1090  CE  LYS C 133     -29.718  11.709 -27.870  1.00 52.20           C
ANISOU 1090  CE  LYS C 133     6569   6524   6742   -663    181   -282       C
ATOM   1091  NZ  LYS C 133     -29.454  10.254 -27.997  1.00 70.13           N
ANISOU 1091  NZ  LYS C 133     8918   8743   8985   -703    216   -281       N
ATOM   1092  N   MET C 134     -34.035  13.032 -33.057  1.00 58.31           N
ANISOU 1092  N   MET C 134     6981   7654   7520   -630    119   -520       N
ATOM   1093  CA  MET C 134     -34.244  13.609 -34.385  1.00 51.38           C
ANISOU 1093  CA  MET C 134     6058   6823   6642   -566     73   -534       C
ATOM   1094  C   MET C 134     -35.551  14.405 -34.466  1.00 53.46           C
ANISOU 1094  C   MET C 134     6238   7182   6894   -538     49   -613       C
ATOM   1095  O   MET C 134     -35.601  15.459 -35.110  1.00 57.70           O
ANISOU 1095  O   MET C 134     6754   7744   7427   -454     -5   -607       O
ATOM   1096  CB  MET C 134     -34.198  12.502 -35.430  1.00 44.62           C
ANISOU 1096  CB  MET C 134     5210   5967   5778   -598     92   -549       C
ATOM   1097  CG  MET C 134     -32.836  11.825 -35.517  1.00 41.66           C
ANISOU 1097  CG  MET C 134     4915   5503   5412   -606    104   -473       C
ATOM   1098  SD  MET C 134     -31.495  12.981 -35.904  1.00 49.38           S
ANISOU 1098  SD  MET C 134     5922   6432   6409   -517     53   -389       S
ATOM   1099  CE  MET C 134     -30.555  12.986 -34.378  1.00 56.75           C
ANISOU 1099  CE  MET C 134     6914   7294   7356   -532     69   -337       C
ATOM   1100  N   LYS C 135     -36.610  13.939 -33.796  1.00 52.66           N
ANISOU 1100  N   LYS C 135     6094   7133   6782   -604     88   -690       N
ATOM   1101  CA  LYS C 135     -37.862  14.694 -33.761  1.00 56.21           C
ANISOU 1101  CA  LYS C 135     6455   7682   7220   -575     63   -777       C
ATOM   1102  C   LYS C 135     -37.699  16.071 -33.114  1.00 52.12           C
ANISOU 1102  C   LYS C 135     5937   7157   6709   -503     21   -745       C
ATOM   1103  O   LYS C 135     -38.358  17.031 -33.521  1.00 57.55           O
ANISOU 1103  O   LYS C 135     6573   7910   7385   -428    -30   -787       O
ATOM   1104  CB  LYS C 135     -38.931  13.898 -33.022  1.00 50.41           C
ANISOU 1104  CB  LYS C 135     5678   7001   6475   -676    125   -870       C
ATOM   1105  CG  LYS C 135     -40.228  14.647 -32.856  1.00 62.17           C
ANISOU 1105  CG  LYS C 135     7067   8602   7953   -650    103   -973       C
ATOM   1106  CD  LYS C 135     -41.139  13.938 -31.856  1.00 70.48           C
ANISOU 1106  CD  LYS C 135     8086   9695   8996   -764    176  -1060       C
ATOM   1107  CE  LYS C 135     -42.531  14.554 -31.820  1.00 70.19           C
ANISOU 1107  CE  LYS C 135     7931   9791   8948   -743    156  -1187       C
ATOM   1108  NZ  LYS C 135     -43.359  13.966 -30.723  1.00 69.97           N
ANISOU 1108  NZ  LYS C 135     7875   9800   8911   -862    235  -1271       N
ATOM   1109  N   LEU C 136     -36.840  16.193 -32.107  1.00 48.13           N
ANISOU 1109  N   LEU C 136     5494   6575   6220   -520     38   -673       N
ATOM   1110  CA  LEU C 136     -36.619  17.503 -31.500  1.00 48.50           C
ANISOU 1110  CA  LEU C 136     5545   6610   6274   -455     -0   -640       C
ATOM   1111  C   LEU C 136     -36.009  18.467 -32.511  1.00 48.85           C
ANISOU 1111  C   LEU C 136     5610   6634   6316   -357    -58   -591       C
ATOM   1112  O   LEU C 136     -36.457  19.612 -32.643  1.00 52.28           O
ANISOU 1112  O   LEU C 136     6019   7104   6739   -283   -104   -610       O
ATOM   1113  CB  LEU C 136     -35.725  17.372 -30.258  1.00 43.62           C
ANISOU 1113  CB  LEU C 136     4990   5911   5671   -492     29   -574       C
ATOM   1114  CG  LEU C 136     -36.338  16.722 -29.014  1.00 45.12           C
ANISOU 1114  CG  LEU C 136     5176   6111   5855   -579     85   -617       C
ATOM   1115  CD1 LEU C 136     -35.256  16.226 -28.027  1.00 42.53           C
ANISOU 1115  CD1 LEU C 136     4936   5688   5534   -615    116   -544       C
ATOM   1116  CD2 LEU C 136     -37.266  17.681 -28.320  1.00 42.43           C
ANISOU 1116  CD2 LEU C 136     4776   5835   5511   -557     69   -671       C
ATOM   1117  N   PHE C 137     -34.980  18.011 -33.234  1.00 44.69           N
ANISOU 1117  N   PHE C 137     5137   6046   5797   -358    -55   -530       N
ATOM   1118  CA  PHE C 137     -34.363  18.833 -34.270  1.00 44.37           C
ANISOU 1118  CA  PHE C 137     5127   5982   5751   -278    -99   -485       C
ATOM   1119  C   PHE C 137     -35.364  19.163 -35.364  1.00 47.51           C
ANISOU 1119  C   PHE C 137     5478   6454   6120   -221   -138   -549       C
ATOM   1120  O   PHE C 137     -35.385  20.284 -35.884  1.00 46.29           O
ANISOU 1120  O   PHE C 137     5339   6302   5946   -135   -185   -539       O
ATOM   1121  CB  PHE C 137     -33.153  18.105 -34.865  1.00 43.06           C
ANISOU 1121  CB  PHE C 137     5017   5747   5597   -302    -81   -423       C
ATOM   1122  CG  PHE C 137     -31.907  18.205 -34.031  1.00 41.34           C
ANISOU 1122  CG  PHE C 137     4853   5451   5402   -318    -65   -353       C
ATOM   1123  CD1 PHE C 137     -31.151  19.359 -34.033  1.00 43.56           C
ANISOU 1123  CD1 PHE C 137     5168   5694   5688   -265    -89   -305       C
ATOM   1124  CD2 PHE C 137     -31.499  17.147 -33.242  1.00 44.80           C
ANISOU 1124  CD2 PHE C 137     5315   5856   5853   -384    -24   -340       C
ATOM   1125  CE1 PHE C 137     -30.011  19.456 -33.253  1.00 54.90           C
ANISOU 1125  CE1 PHE C 137     6644   7069   7146   -281    -75   -253       C
ATOM   1126  CE2 PHE C 137     -30.355  17.238 -32.458  1.00 45.92           C
ANISOU 1126  CE2 PHE C 137     5504   5933   6012   -388    -16   -284       C
ATOM   1127  CZ  PHE C 137     -29.617  18.390 -32.458  1.00 50.70           C
ANISOU 1127  CZ  PHE C 137     6126   6511   6627   -337    -42   -244       C
ATOM   1128  N   SER C 138     -36.200  18.187 -35.723  1.00 49.06           N
ANISOU 1128  N   SER C 138     5621   6712   6308   -265   -119   -620       N
ATOM   1129  CA  SER C 138     -37.188  18.368 -36.786  1.00 47.63           C
ANISOU 1129  CA  SER C 138     5387   6614   6098   -210   -158   -694       C
ATOM   1130  C   SER C 138     -38.196  19.452 -36.425  1.00 51.70           C
ANISOU 1130  C   SER C 138     5851   7200   6593   -142   -201   -757       C
ATOM   1131  O   SER C 138     -38.459  20.357 -37.223  1.00 45.65           O
ANISOU 1131  O   SER C 138     5090   6457   5798    -42   -259   -769       O
ATOM   1132  CB  SER C 138     -37.894  17.034 -37.052  1.00 43.63           C
ANISOU 1132  CB  SER C 138     4826   6163   5590   -289   -118   -768       C
ATOM   1133  OG  SER C 138     -38.714  17.080 -38.180  1.00 50.66           O
ANISOU 1133  OG  SER C 138     5664   7132   6452   -237   -156   -840       O
ATOM   1134  N   GLU C 139     -38.762  19.392 -35.210  1.00 49.92           N
ANISOU 1134  N   GLU C 139     5582   7005   6379   -193   -173   -798       N
ATOM   1135  CA  GLU C 139     -39.734  20.413 -34.837  1.00 46.59           C
ANISOU 1135  CA  GLU C 139     5106   6656   5939   -126   -215   -865       C
ATOM   1136  C   GLU C 139     -39.092  21.771 -34.610  1.00 41.49           C
ANISOU 1136  C   GLU C 139     4525   5949   5289    -42   -257   -792       C
ATOM   1137  O   GLU C 139     -39.787  22.789 -34.667  1.00 44.43           O
ANISOU 1137  O   GLU C 139     4874   6372   5637     46   -309   -837       O
ATOM   1138  CB  GLU C 139     -40.486  20.032 -33.571  1.00 56.61           C
ANISOU 1138  CB  GLU C 139     6315   7974   7221   -207   -170   -930       C
ATOM   1139  CG  GLU C 139     -40.878  18.603 -33.427  1.00 70.91           C
ANISOU 1139  CG  GLU C 139     8091   9813   9040   -324   -103   -984       C
ATOM   1140  CD  GLU C 139     -41.452  18.350 -32.055  1.00 88.10           C
ANISOU 1140  CD  GLU C 139    10233  12016  11226   -408    -51  -1033       C
ATOM   1141  OE1 GLU C 139     -41.035  17.374 -31.395  1.00 89.30           O
ANISOU 1141  OE1 GLU C 139    10428  12112  11391   -511     17  -1003       O
ATOM   1142  OE2 GLU C 139     -42.309  19.157 -31.628  1.00 96.92           O
ANISOU 1142  OE2 GLU C 139    11286  13206  12332   -365    -79  -1102       O
ATOM   1143  N   PHE C 140     -37.797  21.816 -34.315  1.00 48.49           N
ANISOU 1143  N   PHE C 140     5492   6733   6199    -67   -234   -688       N
ATOM   1144  CA  PHE C 140     -37.168  23.101 -34.037  1.00 51.42           C
ANISOU 1144  CA  PHE C 140     5924   7046   6567     -1   -264   -625       C
ATOM   1145  C   PHE C 140     -36.954  23.871 -35.324  1.00 49.26           C
ANISOU 1145  C   PHE C 140     5703   6754   6260     96   -314   -603       C
ATOM   1146  O   PHE C 140     -37.141  25.092 -35.369  1.00 50.18           O
ANISOU 1146  O   PHE C 140     5850   6866   6349    183   -358   -602       O
ATOM   1147  CB  PHE C 140     -35.845  22.889 -33.301  1.00 48.82           C
ANISOU 1147  CB  PHE C 140     5657   6621   6273    -61   -222   -534       C
ATOM   1148  CG  PHE C 140     -35.154  24.162 -32.908  1.00 45.90           C
ANISOU 1148  CG  PHE C 140     5345   6191   5903    -10   -243   -475       C
ATOM   1149  CD1 PHE C 140     -35.778  25.084 -32.076  1.00 44.80           C
ANISOU 1149  CD1 PHE C 140     5184   6080   5757     27   -264   -503       C
ATOM   1150  CD2 PHE C 140     -33.877  24.430 -33.347  1.00 40.49           C
ANISOU 1150  CD2 PHE C 140     4736   5423   5225     -4   -236   -396       C
ATOM   1151  CE1 PHE C 140     -35.138  26.259 -31.695  1.00 31.99           C
ANISOU 1151  CE1 PHE C 140     3622   4400   4134     71   -279   -450       C
ATOM   1152  CE2 PHE C 140     -33.225  25.602 -32.959  1.00 42.87           C
ANISOU 1152  CE2 PHE C 140     5093   5669   5526     33   -247   -348       C
ATOM   1153  CZ  PHE C 140     -33.858  26.516 -32.131  1.00 32.46           C
ANISOU 1153  CZ  PHE C 140     3758   4375   4200     70   -268   -374       C
ATOM   1154  N   LEU C 141     -36.559  23.157 -36.374  1.00 51.34           N
ANISOU 1154  N   LEU C 141     5986   7001   6519     82   -305   -586       N
ATOM   1155  CA  LEU C 141     -36.422  23.769 -37.683  1.00 47.43           C
ANISOU 1155  CA  LEU C 141     5546   6491   5985    169   -349   -572       C
ATOM   1156  C   LEU C 141     -37.786  24.160 -38.242  1.00 52.77           C
ANISOU 1156  C   LEU C 141     6170   7264   6617    257   -406   -667       C
ATOM   1157  O   LEU C 141     -37.951  25.261 -38.778  1.00 45.38           O
ANISOU 1157  O   LEU C 141     5286   6319   5637    364   -459   -666       O
ATOM   1158  CB  LEU C 141     -35.701  22.802 -38.613  1.00 40.35           C
ANISOU 1158  CB  LEU C 141     4675   5560   5097    125   -322   -536       C
ATOM   1159  CG  LEU C 141     -35.708  23.232 -40.077  1.00 41.84           C
ANISOU 1159  CG  LEU C 141     4914   5743   5240    209   -363   -534       C
ATOM   1160  CD1 LEU C 141     -34.731  24.404 -40.284  1.00 36.49           C
ANISOU 1160  CD1 LEU C 141     4347   4972   4544    257   -372   -455       C
ATOM   1161  CD2 LEU C 141     -35.355  22.049 -40.948  1.00 39.99           C
ANISOU 1161  CD2 LEU C 141     4673   5506   5015    158   -337   -528       C
ATOM   1162  N   GLY C 142     -38.774  23.274 -38.109  1.00 58.33           N
ANISOU 1162  N   GLY C 142     6774   8062   7328    215   -396   -757       N
ATOM   1163  CA  GLY C 142     -40.117  23.584 -38.566  1.00 59.57           C
ANISOU 1163  CA  GLY C 142     6862   8328   7445    297   -451   -867       C
ATOM   1164  C   GLY C 142     -40.158  23.799 -40.066  1.00 63.73           C
ANISOU 1164  C   GLY C 142     7431   8859   7924    389   -500   -873       C
ATOM   1165  O   GLY C 142     -39.612  23.013 -40.847  1.00 56.00           O
ANISOU 1165  O   GLY C 142     6475   7850   6953    348   -476   -840       O
ATOM   1166  N   LYS C 143     -40.805  24.890 -40.481  1.00 62.60           N
ANISOU 1166  N   LYS C 143     7306   8751   7728    520   -572   -915       N
ATOM   1167  CA  LYS C 143     -40.883  25.256 -41.886  1.00 59.48           C
ANISOU 1167  CA  LYS C 143     6970   8354   7275    627   -628   -920       C
ATOM   1168  C   LYS C 143     -39.813  26.267 -42.277  1.00 55.02           C
ANISOU 1168  C   LYS C 143     6557   7665   6684    682   -637   -810       C
ATOM   1169  O   LYS C 143     -39.932  26.907 -43.321  1.00 60.54           O
ANISOU 1169  O   LYS C 143     7332   8351   7320    793   -690   -812       O
ATOM   1170  CB  LYS C 143     -42.272  25.808 -42.221  1.00 66.92           C
ANISOU 1170  CB  LYS C 143     7851   9412   8162    752   -707  -1043       C
ATOM   1171  CG  LYS C 143     -43.431  25.139 -41.482  1.00 81.24           C
ANISOU 1171  CG  LYS C 143     9507  11358  10001    699   -696  -1168       C
ATOM   1172  CD  LYS C 143     -44.717  26.001 -41.472  1.00 86.71           C
ANISOU 1172  CD  LYS C 143    10142  12161  10643    833   -778  -1288       C
ATOM   1173  CE  LYS C 143     -44.926  26.743 -40.144  1.00 87.06           C
ANISOU 1173  CE  LYS C 143    10167  12207  10704    831   -774  -1293       C
ATOM   1174  NZ  LYS C 143     -46.084  27.690 -40.175  1.00 85.45           N
ANISOU 1174  NZ  LYS C 143     9921  12102  10445    977   -861  -1405       N
ATOM   1175  N   ARG C 144     -38.785  26.438 -41.459  1.00 53.52           N
ANISOU 1175  N   ARG C 144     6416   7383   6535    607   -586   -720       N
ATOM   1176  CA  ARG C 144     -37.773  27.456 -41.712  1.00 52.69           C
ANISOU 1176  CA  ARG C 144     6450   7163   6406    646   -585   -625       C
ATOM   1177  C   ARG C 144     -36.781  26.999 -42.773  1.00 49.48           C
ANISOU 1177  C   ARG C 144     6118   6686   5996    614   -556   -560       C
ATOM   1178  O   ARG C 144     -36.527  25.802 -42.933  1.00 55.71           O
ANISOU 1178  O   ARG C 144     6851   7492   6825    527   -517   -560       O
ATOM   1179  CB  ARG C 144     -37.020  27.788 -40.422  1.00 49.70           C
ANISOU 1179  CB  ARG C 144     6087   6722   6076    574   -539   -563       C
ATOM   1180  CG  ARG C 144     -37.838  28.561 -39.396  1.00 44.12           C
ANISOU 1180  CG  ARG C 144     5339   6061   5363    621   -570   -612       C
ATOM   1181  CD  ARG C 144     -37.054  28.733 -38.107  1.00 43.43           C
ANISOU 1181  CD  ARG C 144     5259   5915   5328    538   -519   -552       C
ATOM   1182  NE  ARG C 144     -37.862  29.323 -37.043  1.00 48.17           N
ANISOU 1182  NE  ARG C 144     5806   6566   5929    568   -542   -602       N
ATOM   1183  CZ  ARG C 144     -38.765  28.650 -36.330  1.00 48.37           C
ANISOU 1183  CZ  ARG C 144     5711   6686   5981    526   -536   -679       C
ATOM   1184  NH1 ARG C 144     -38.990  27.360 -36.573  1.00 35.79           N
ANISOU 1184  NH1 ARG C 144     4043   5143   4412    452   -507   -715       N
ATOM   1185  NH2 ARG C 144     -39.447  29.267 -35.369  1.00 42.51           N
ANISOU 1185  NH2 ARG C 144     4927   5988   5239    555   -556   -724       N
ATOM   1186  N   THR C 145     -36.205  27.967 -43.502  1.00 46.16           N
ANISOU 1186  N   THR C 145     5832   6182   5525    682   -571   -505       N
ATOM   1187  CA  THR C 145     -35.176  27.613 -44.482  1.00 49.70           C
ANISOU 1187  CA  THR C 145     6358   6558   5969    644   -536   -442       C
ATOM   1188  C   THR C 145     -33.906  27.155 -43.792  1.00 53.28           C
ANISOU 1188  C   THR C 145     6811   6944   6489    519   -462   -370       C
ATOM   1189  O   THR C 145     -33.244  26.216 -44.253  1.00 48.06           O
ANISOU 1189  O   THR C 145     6137   6267   5856    448   -424   -345       O
ATOM   1190  CB  THR C 145     -34.856  28.791 -45.405  1.00 55.03           C
ANISOU 1190  CB  THR C 145     7190   7154   6567    739   -562   -404       C
ATOM   1191  OG1 THR C 145     -36.050  29.231 -46.054  1.00 65.27           O
ANISOU 1191  OG1 THR C 145     8494   8514   7793    873   -641   -476       O
ATOM   1192  N   TRP C 146     -33.537  27.828 -42.701  1.00 53.49           N
ANISOU 1192  N   TRP C 146     6852   6932   6539    497   -443   -340       N
ATOM   1193  CA  TRP C 146     -32.370  27.493 -41.901  1.00 47.73           C
ANISOU 1193  CA  TRP C 146     6118   6147   5871    389   -380   -282       C
ATOM   1194  C   TRP C 146     -32.786  27.500 -40.436  1.00 46.66           C
ANISOU 1194  C   TRP C 146     5903   6049   5776    359   -377   -304       C
ATOM   1195  O   TRP C 146     -33.900  27.907 -40.093  1.00 48.05           O
ANISOU 1195  O   TRP C 146     6039   6287   5931    421   -421   -360       O
ATOM   1196  CB  TRP C 146     -31.217  28.470 -42.180  1.00 43.71           C
ANISOU 1196  CB  TRP C 146     5736   5532   5341    389   -351   -213       C
ATOM   1197  CG  TRP C 146     -30.867  28.559 -43.642  1.00 45.57           C
ANISOU 1197  CG  TRP C 146     6063   5726   5526    421   -352   -195       C
ATOM   1198  CD1 TRP C 146     -31.025  29.640 -44.462  1.00 45.53           C
ANISOU 1198  CD1 TRP C 146     6181   5674   5445    510   -379   -186       C
ATOM   1199  CD2 TRP C 146     -30.304  27.517 -44.460  1.00 46.78           C
ANISOU 1199  CD2 TRP C 146     6201   5878   5697    366   -323   -182       C
ATOM   1200  NE1 TRP C 146     -30.575  29.342 -45.731  1.00 39.02           N
ANISOU 1200  NE1 TRP C 146     5420   4817   4588    510   -366   -168       N
ATOM   1201  CE2 TRP C 146     -30.138  28.045 -45.757  1.00 37.23           C
ANISOU 1201  CE2 TRP C 146     5104   4621   4420    422   -333   -167       C
ATOM   1202  CE3 TRP C 146     -29.909  26.194 -44.214  1.00 50.64           C
ANISOU 1202  CE3 TRP C 146     6600   6395   6247    277   -290   -182       C
ATOM   1203  CZ2 TRP C 146     -29.615  27.300 -46.800  1.00 42.51           C
ANISOU 1203  CZ2 TRP C 146     5789   5277   5087    390   -310   -153       C
ATOM   1204  CZ3 TRP C 146     -29.373  25.453 -45.255  1.00 39.71           C
ANISOU 1204  CZ3 TRP C 146     5232   4997   4860    248   -269   -169       C
ATOM   1205  CH2 TRP C 146     -29.235  26.011 -46.536  1.00 51.46           C
ANISOU 1205  CH2 TRP C 146     6823   6443   6285    303   -279   -156       C
ATOM   1206  N   PHE C 147     -31.894  27.041 -39.554  1.00 43.93           N
ANISOU 1206  N   PHE C 147     5534   5670   5487    266   -327   -265       N
ATOM   1207  CA  PHE C 147     -32.338  26.830 -38.181  1.00 42.10           C
ANISOU 1207  CA  PHE C 147     5224   5480   5294    230   -321   -290       C
ATOM   1208  C   PHE C 147     -32.616  28.134 -37.459  1.00 47.55           C
ANISOU 1208  C   PHE C 147     5946   6155   5966    285   -344   -289       C
ATOM   1209  O   PHE C 147     -33.514  28.184 -36.620  1.00 58.66           O
ANISOU 1209  O   PHE C 147     7286   7621   7380    296   -363   -337       O
ATOM   1210  CB  PHE C 147     -31.334  25.991 -37.418  1.00 36.31           C
ANISOU 1210  CB  PHE C 147     4465   4713   4617    130   -267   -251       C
ATOM   1211  CG  PHE C 147     -31.519  24.528 -37.641  1.00 38.48           C
ANISOU 1211  CG  PHE C 147     4677   5028   4914     73   -249   -275       C
ATOM   1212  CD1 PHE C 147     -32.364  23.798 -36.832  1.00 35.62           C
ANISOU 1212  CD1 PHE C 147     4234   4727   4571     36   -243   -324       C
ATOM   1213  CD2 PHE C 147     -30.893  23.898 -38.699  1.00 37.37           C
ANISOU 1213  CD2 PHE C 147     4564   4863   4771     54   -234   -253       C
ATOM   1214  CE1 PHE C 147     -32.547  22.456 -37.048  1.00 41.37           C
ANISOU 1214  CE1 PHE C 147     4918   5487   5315    -21   -220   -348       C
ATOM   1215  CE2 PHE C 147     -31.065  22.563 -38.921  1.00 39.17           C
ANISOU 1215  CE2 PHE C 147     4741   5124   5017      4   -216   -276       C
ATOM   1216  CZ  PHE C 147     -31.897  21.836 -38.093  1.00 47.19           C
ANISOU 1216  CZ  PHE C 147     5684   6197   6050    -35   -209   -323       C
ATOM   1217  N   ALA C 148     -31.876  29.192 -37.763  1.00 49.90           N
ANISOU 1217  N   ALA C 148     6347   6375   6237    315   -340   -241       N
ATOM   1218  CA  ALA C 148     -32.162  30.491 -37.175  1.00 46.64           C
ANISOU 1218  CA  ALA C 148     5979   5941   5799    374   -363   -242       C
ATOM   1219  C   ALA C 148     -33.186  31.290 -37.978  1.00 57.88           C
ANISOU 1219  C   ALA C 148     7451   7391   7152    496   -426   -282       C
ATOM   1220  O   ALA C 148     -33.566  32.379 -37.543  1.00 56.97           O
ANISOU 1220  O   ALA C 148     7376   7263   7007    560   -454   -290       O
ATOM   1221  CB  ALA C 148     -30.871  31.303 -37.021  1.00 38.68           C
ANISOU 1221  CB  ALA C 148     5067   4834   4795    342   -323   -177       C
ATOM   1222  N   GLY C 149     -33.641  30.780 -39.131  1.00 55.15           N
ANISOU 1222  N   GLY C 149     7101   7079   6773    534   -451   -311       N
ATOM   1223  CA  GLY C 149     -34.597  31.491 -39.964  1.00 50.78           C
ANISOU 1223  CA  GLY C 149     6597   6552   6145    662   -517   -355       C
ATOM   1224  C   GLY C 149     -34.256  31.528 -41.445  1.00 53.10           C
ANISOU 1224  C   GLY C 149     6989   6802   6386    703   -524   -333       C
ATOM   1225  O   GLY C 149     -33.762  30.535 -41.985  1.00 61.82           O
ANISOU 1225  O   GLY C 149     8064   7906   7517    637   -491   -317       O
ATOM   1226  N   ASP C 150     -34.517  32.667 -42.109  1.00 46.48           N
ANISOU 1226  N   ASP C 150     6273   5920   5467    816   -566   -331       N
ATOM   1227  CA  ASP C 150     -34.283  32.788 -43.550  1.00 48.13           C
ANISOU 1227  CA  ASP C 150     6592   6083   5611    867   -576   -313       C
ATOM   1228  C   ASP C 150     -32.797  32.700 -43.893  1.00 52.16           C
ANISOU 1228  C   ASP C 150     7186   6491   6142    769   -499   -232       C
ATOM   1229  O   ASP C 150     -32.430  32.102 -44.910  1.00 58.24           O
ANISOU 1229  O   ASP C 150     7979   7248   6901    749   -484   -220       O
ATOM   1230  CB  ASP C 150     -34.862  34.110 -44.090  1.00 46.37           C
ANISOU 1230  CB  ASP C 150     6506   5824   5288   1015   -637   -328       C
ATOM   1231  CG  ASP C 150     -36.364  34.050 -44.326  1.00 42.53           C
ANISOU 1231  CG  ASP C 150     5948   5451   4760   1140   -727   -424       C
ATOM   1232  N   LYS C 151     -31.932  33.287 -43.068  1.00 54.08           N
ANISOU 1232  N   LYS C 151     7470   6665   6415    706   -450   -184       N
ATOM   1233  CA  LYS C 151     -30.515  33.422 -43.391  1.00 57.04           C
ANISOU 1233  CA  LYS C 151     7933   6942   6798    620   -377   -120       C
ATOM   1234  C   LYS C 151     -29.716  32.249 -42.842  1.00 56.90           C
ANISOU 1234  C   LYS C 151     7798   6948   6871    492   -323   -105       C
ATOM   1235  O   LYS C 151     -29.929  31.807 -41.708  1.00 56.98           O
ANISOU 1235  O   LYS C 151     7697   7011   6942    452   -323   -121       O
ATOM   1236  CB  LYS C 151     -29.936  34.730 -42.840  1.00 58.78           C
ANISOU 1236  CB  LYS C 151     8266   7072   6997    617   -347    -84       C
ATOM   1237  CG  LYS C 151     -30.477  35.987 -43.502  1.00 75.47           C
ANISOU 1237  CG  LYS C 151    10539   9130   9007    740   -389    -86       C
ATOM   1238  CD  LYS C 151     -31.889  36.355 -43.020  1.00 90.44           C
ANISOU 1238  CD  LYS C 151    12385  11100  10876    858   -473   -143       C
ATOM   1239  CE  LYS C 151     -32.028  36.212 -41.500  1.00 97.58           C
ANISOU 1239  CE  LYS C 151    13161  12058  11858    805   -467   -157       C
ATOM   1240  NZ  LYS C 151     -33.449  36.260 -41.035  1.00100.16           N
ANISOU 1240  NZ  LYS C 151    13400  12483  12173    902   -545   -228       N
ATOM   1241  N   LEU C 152     -28.794  31.755 -43.661  1.00 57.84           N
ANISOU 1241  N   LEU C 152     7953   7027   6995    433   -278    -75       N
ATOM   1242  CA  LEU C 152     -27.875  30.715 -43.237  1.00 55.81           C
ANISOU 1242  CA  LEU C 152     7607   6781   6815    319   -226    -60       C
ATOM   1243  C   LEU C 152     -26.910  31.251 -42.184  1.00 57.15           C
ANISOU 1243  C   LEU C 152     7786   6902   7025    250   -177    -31       C
ATOM   1244  O   LEU C 152     -26.518  32.422 -42.203  1.00 54.80           O
ANISOU 1244  O   LEU C 152     7599   6534   6690    263   -158    -10       O
ATOM   1245  CB  LEU C 152     -27.104  30.170 -44.433  1.00 49.88           C
ANISOU 1245  CB  LEU C 152     6900   5999   6053    281   -191    -40       C
ATOM   1246  CG  LEU C 152     -25.918  29.246 -44.170  1.00 44.72           C
ANISOU 1246  CG  LEU C 152     6183   5339   5467    169   -133    -23       C
ATOM   1247  CD1 LEU C 152     -26.392  27.805 -44.006  1.00 39.97           C
ANISOU 1247  CD1 LEU C 152     5454   4819   4914    148   -153    -49       C
ATOM   1248  CD2 LEU C 152     -24.954  29.364 -45.333  1.00 28.02           C
ANISOU 1248  CD2 LEU C 152     4164   3162   3322    137    -87      1       C
ATOM   1249  N   ASN C 153     -26.502  30.352 -41.288  1.00 44.38           N
ANISOU 1249  N   ASN C 153     6059   5323   5482    175   -156    -34       N
ATOM   1250  CA  ASN C 153     -25.893  30.685 -40.021  1.00 36.21           C
ANISOU 1250  CA  ASN C 153     4994   4271   4492    124   -128    -23       C
ATOM   1251  C   ASN C 153     -24.833  29.640 -39.701  1.00 42.24           C
ANISOU 1251  C   ASN C 153     5688   5042   5318     32    -86    -15       C
ATOM   1252  O   ASN C 153     -24.900  28.507 -40.182  1.00 49.10           O
ANISOU 1252  O   ASN C 153     6504   5947   6203     15    -90    -24       O
ATOM   1253  CB  ASN C 153     -26.984  30.716 -38.947  1.00 47.88           C
ANISOU 1253  CB  ASN C 153     6398   5808   5985    163   -173    -50       C
ATOM   1254  CG  ASN C 153     -26.706  31.702 -37.884  1.00 60.13           C
ANISOU 1254  CG  ASN C 153     7972   7327   7546    156   -161    -39       C
ATOM   1255  OD1 ASN C 153     -25.866  31.461 -37.022  1.00 68.12           O
ANISOU 1255  OD1 ASN C 153     8942   8330   8609     87   -126    -27       O
ATOM   1256  ND2 ASN C 153     -27.394  32.843 -37.931  1.00 67.52           N
ANISOU 1256  ND2 ASN C 153     8979   8243   8430    233   -192    -45       N
ATOM   1257  N   TYR C 154     -23.864  30.005 -38.853  1.00 40.24           N
ANISOU 1257  N   TYR C 154     5432   4757   5098    -23    -47     -3       N
ATOM   1258  CA  TYR C 154     -22.873  29.006 -38.459  1.00 36.24           C
ANISOU 1258  CA  TYR C 154     4856   4265   4649    -96    -16     -4       C
ATOM   1259  C   TYR C 154     -23.495  27.835 -37.699  1.00 38.35           C
ANISOU 1259  C   TYR C 154     5020   4598   4956    -99    -45    -20       C
ATOM   1260  O   TYR C 154     -22.929  26.741 -37.738  1.00 41.33           O
ANISOU 1260  O   TYR C 154     5349   4990   5364   -141    -30    -23       O
ATOM   1261  CB  TYR C 154     -21.718  29.625 -37.641  1.00 38.94           C
ANISOU 1261  CB  TYR C 154     5207   4571   5018   -149     26     -1       C
ATOM   1262  CG  TYR C 154     -22.011  29.849 -36.176  1.00 40.68           C
ANISOU 1262  CG  TYR C 154     5375   4813   5269   -145      9     -6       C
ATOM   1263  CD1 TYR C 154     -21.782  28.845 -35.232  1.00 35.65           C
ANISOU 1263  CD1 TYR C 154     4648   4216   4681   -175      4    -16       C
ATOM   1264  CD2 TYR C 154     -22.533  31.071 -35.734  1.00 38.64           C
ANISOU 1264  CD2 TYR C 154     5166   4532   4984   -107     -3     -2       C
ATOM   1265  CE1 TYR C 154     -22.082  29.040 -33.886  1.00 33.19           C
ANISOU 1265  CE1 TYR C 154     4296   3922   4393   -170    -12    -21       C
ATOM   1266  CE2 TYR C 154     -22.816  31.286 -34.393  1.00 35.23           C
ANISOU 1266  CE2 TYR C 154     4686   4120   4579   -104    -19     -8       C
ATOM   1267  CZ  TYR C 154     -22.585  30.276 -33.467  1.00 38.47           C
ANISOU 1267  CZ  TYR C 154     5007   4572   5039   -137    -22    -17       C
ATOM   1268  OH  TYR C 154     -22.884  30.501 -32.134  1.00 37.88           O
ANISOU 1268  OH  TYR C 154     4892   4515   4987   -133    -36    -23       O
ATOM   1269  N   VAL C 155     -24.656  28.004 -37.048  1.00 50.24           N
ANISOU 1269  N   VAL C 155     6495   6140   6456    -56    -83    -35       N
ATOM   1270  CA  VAL C 155     -25.267  26.835 -36.396  1.00 47.41           C
ANISOU 1270  CA  VAL C 155     6047   5839   6128    -71   -100    -55       C
ATOM   1271  C   VAL C 155     -25.778  25.833 -37.413  1.00 38.70           C
ANISOU 1271  C   VAL C 155     4923   4769   5012    -64   -112    -69       C
ATOM   1272  O   VAL C 155     -25.920  24.649 -37.083  1.00 41.58           O
ANISOU 1272  O   VAL C 155     5227   5166   5404    -97   -109    -83       O
ATOM   1273  CB  VAL C 155     -26.440  27.153 -35.437  1.00 41.13           C
ANISOU 1273  CB  VAL C 155     5213   5085   5330    -37   -132    -77       C
ATOM   1274  CG1 VAL C 155     -25.920  27.651 -34.125  1.00 37.05           C
ANISOU 1274  CG1 VAL C 155     4687   4549   4842    -62   -118    -66       C
ATOM   1275  CG2 VAL C 155     -27.470  28.087 -36.070  1.00 40.67           C
ANISOU 1275  CG2 VAL C 155     5195   5037   5220     40   -169    -94       C
ATOM   1276  N   ASP C 156     -26.076  26.268 -38.642  1.00 39.01           N
ANISOU 1276  N   ASP C 156     5017   4799   5008    -21   -125    -70       N
ATOM   1277  CA  ASP C 156     -26.483  25.296 -39.650  1.00 36.97           C
ANISOU 1277  CA  ASP C 156     4737   4572   4737    -16   -135    -86       C
ATOM   1278  C   ASP C 156     -25.335  24.380 -40.012  1.00 40.67           C
ANISOU 1278  C   ASP C 156     5200   5019   5236    -77    -98    -68       C
ATOM   1279  O   ASP C 156     -25.562  23.242 -40.444  1.00 41.26           O
ANISOU 1279  O   ASP C 156     5234   5124   5318    -94   -100    -82       O
ATOM   1280  CB  ASP C 156     -27.002  25.990 -40.898  1.00 50.01           C
ANISOU 1280  CB  ASP C 156     6458   6215   6330     51   -160    -90       C
ATOM   1281  CG  ASP C 156     -28.231  26.810 -40.630  1.00 48.92           C
ANISOU 1281  CG  ASP C 156     6322   6108   6156    127   -207   -119       C
ATOM   1282  OD1 ASP C 156     -29.301  26.204 -40.381  1.00 49.74           O
ANISOU 1282  OD1 ASP C 156     6350   6284   6266    143   -236   -162       O
ATOM   1283  OD2 ASP C 156     -28.105  28.057 -40.660  1.00 36.69           O
ANISOU 1283  OD2 ASP C 156     4854   4513   4573    168   -212   -102       O
ATOM   1284  N   PHE C 157     -24.095  24.847 -39.828  1.00 39.09           N
ANISOU 1284  N   PHE C 157     5035   4768   5050   -112    -63    -44       N
ATOM   1285  CA  PHE C 157     -22.974  23.959 -40.069  1.00 32.78           C
ANISOU 1285  CA  PHE C 157     4219   3957   4280   -166    -31    -38       C
ATOM   1286  C   PHE C 157     -22.876  22.938 -38.950  1.00 40.14           C
ANISOU 1286  C   PHE C 157     5080   4916   5255   -198    -32    -47       C
ATOM   1287  O   PHE C 157     -22.716  21.739 -39.215  1.00 40.78           O
ANISOU 1287  O   PHE C 157     5130   5013   5351   -220    -28    -54       O
ATOM   1288  CB  PHE C 157     -21.683  24.770 -40.250  1.00 39.77           C
ANISOU 1288  CB  PHE C 157     5157   4789   5165   -195      9    -23       C
ATOM   1289  CG  PHE C 157     -21.675  25.616 -41.523  1.00 40.45           C
ANISOU 1289  CG  PHE C 157     5333   4837   5199   -173     20    -13       C
ATOM   1290  CD1 PHE C 157     -22.546  26.686 -41.670  1.00 40.52           C
ANISOU 1290  CD1 PHE C 157     5402   4831   5162   -116     -4     -8       C
ATOM   1291  CD2 PHE C 157     -20.825  25.313 -42.582  1.00 38.98           C
ANISOU 1291  CD2 PHE C 157     5178   4628   5004   -205     53    -11       C
ATOM   1292  CE1 PHE C 157     -22.557  27.446 -42.849  1.00 47.29           C
ANISOU 1292  CE1 PHE C 157     6361   5645   5961    -87      5      2       C
ATOM   1293  CE2 PHE C 157     -20.831  26.071 -43.761  1.00 37.61           C
ANISOU 1293  CE2 PHE C 157     5102   4414   4776   -186     67     -1       C
ATOM   1294  CZ  PHE C 157     -21.695  27.128 -43.895  1.00 40.69           C
ANISOU 1294  CZ  PHE C 157     5562   4782   5116   -125     43      8       C
ATOM   1295  N   LEU C 158     -23.049  23.385 -37.699  1.00 41.45           N
ANISOU 1295  N   LEU C 158     5227   5086   5438   -196    -39    -48       N
ATOM   1296  CA  LEU C 158     -23.094  22.461 -36.568  1.00 37.35           C
ANISOU 1296  CA  LEU C 158     4655   4587   4950   -221    -41    -56       C
ATOM   1297  C   LEU C 158     -24.269  21.482 -36.691  1.00 41.51           C
ANISOU 1297  C   LEU C 158     5147   5158   5469   -218    -58    -77       C
ATOM   1298  O   LEU C 158     -24.117  20.273 -36.472  1.00 41.60           O
ANISOU 1298  O   LEU C 158     5135   5177   5495   -247    -49    -83       O
ATOM   1299  CB  LEU C 158     -23.182  23.246 -35.263  1.00 33.48           C
ANISOU 1299  CB  LEU C 158     4157   4093   4471   -215    -46    -54       C
ATOM   1300  CG  LEU C 158     -21.921  23.939 -34.764  1.00 39.73           C
ANISOU 1300  CG  LEU C 158     4966   4849   5281   -233    -24    -44       C
ATOM   1301  CD1 LEU C 158     -22.220  24.867 -33.548  1.00 32.59           C
ANISOU 1301  CD1 LEU C 158     4058   3942   4381   -221    -33    -44       C
ATOM   1302  CD2 LEU C 158     -20.869  22.902 -34.406  1.00 29.52           C
ANISOU 1302  CD2 LEU C 158     3646   3554   4016   -265    -10    -50       C
ATOM   1303  N   ALA C 159     -25.456  21.982 -37.025  1.00 34.05           N
ANISOU 1303  N   ALA C 159     4199   4242   4497   -181    -82    -94       N
ATOM   1304  CA  ALA C 159     -26.585  21.071 -37.165  1.00 39.19           C
ANISOU 1304  CA  ALA C 159     4807   4943   5139   -184    -93   -127       C
ATOM   1305  C   ALA C 159     -26.346  20.081 -38.302  1.00 47.28           C
ANISOU 1305  C   ALA C 159     5835   5971   6160   -200    -85   -130       C
ATOM   1306  O   ALA C 159     -26.564  18.874 -38.144  1.00 43.39           O
ANISOU 1306  O   ALA C 159     5314   5496   5678   -236    -73   -146       O
ATOM   1307  CB  ALA C 159     -27.872  21.852 -37.384  1.00 32.62           C
ANISOU 1307  CB  ALA C 159     3965   4152   4276   -132   -126   -158       C
ATOM   1308  N   TYR C 160     -25.872  20.572 -39.453  1.00 42.14           N
ANISOU 1308  N   TYR C 160     5225   5297   5489   -177    -86   -114       N
ATOM   1309  CA  TYR C 160     -25.582  19.667 -40.557  1.00 48.57           C
ANISOU 1309  CA  TYR C 160     6044   6112   6299   -192    -77   -115       C
ATOM   1310  C   TYR C 160     -24.616  18.565 -40.123  1.00 51.18           C
ANISOU 1310  C   TYR C 160     6362   6423   6663   -242    -50   -104       C
ATOM   1311  O   TYR C 160     -24.887  17.371 -40.304  1.00 53.42           O
ANISOU 1311  O   TYR C 160     6623   6724   6951   -266    -45   -120       O
ATOM   1312  CB  TYR C 160     -25.015  20.428 -41.766  1.00 45.63           C
ANISOU 1312  CB  TYR C 160     5730   5707   5900   -166    -74    -95       C
ATOM   1313  CG  TYR C 160     -24.508  19.465 -42.804  1.00 43.17           C
ANISOU 1313  CG  TYR C 160     5422   5392   5589   -188    -59    -94       C
ATOM   1314  CD1 TYR C 160     -25.392  18.826 -43.681  1.00 42.60           C
ANISOU 1314  CD1 TYR C 160     5332   5358   5495   -172    -77   -119       C
ATOM   1315  CD2 TYR C 160     -23.160  19.142 -42.884  1.00 46.36           C
ANISOU 1315  CD2 TYR C 160     5839   5760   6016   -225    -29    -76       C
ATOM   1316  CE1 TYR C 160     -24.942  17.917 -44.621  1.00 41.36           C
ANISOU 1316  CE1 TYR C 160     5177   5197   5338   -193    -63   -119       C
ATOM   1317  CE2 TYR C 160     -22.699  18.212 -43.826  1.00 48.01           C
ANISOU 1317  CE2 TYR C 160     6048   5969   6226   -245    -16    -78       C
ATOM   1318  CZ  TYR C 160     -23.597  17.604 -44.685  1.00 48.52           C
ANISOU 1318  CZ  TYR C 160     6101   6065   6268   -229    -33    -96       C
ATOM   1319  OH  TYR C 160     -23.140  16.679 -45.603  1.00 45.15           O
ANISOU 1319  OH  TYR C 160     5675   5638   5843   -249    -20    -98       O
ATOM   1320  N   ASP C 161     -23.479  18.952 -39.544  1.00 42.98           N
ANISOU 1320  N   ASP C 161     5340   5347   5645   -255    -34    -83       N
ATOM   1321  CA  ASP C 161     -22.479  17.965 -39.152  1.00 38.78           C
ANISOU 1321  CA  ASP C 161     4798   4798   5139   -288    -17    -79       C
ATOM   1322  C   ASP C 161     -23.036  16.961 -38.142  1.00 45.39           C
ANISOU 1322  C   ASP C 161     5611   5650   5985   -308    -19    -92       C
ATOM   1323  O   ASP C 161     -22.738  15.766 -38.216  1.00 40.47           O
ANISOU 1323  O   ASP C 161     4989   5022   5368   -329    -10    -97       O
ATOM   1324  CB  ASP C 161     -21.261  18.664 -38.566  1.00 33.42           C
ANISOU 1324  CB  ASP C 161     4131   4089   4479   -293     -4    -67       C
ATOM   1325  CG  ASP C 161     -20.304  17.698 -37.944  1.00 44.80           C
ANISOU 1325  CG  ASP C 161     5559   5521   5943   -312      3    -73       C
ATOM   1326  OD1 ASP C 161     -19.927  16.715 -38.616  1.00 55.17           O
ANISOU 1326  OD1 ASP C 161     6872   6833   7256   -322      9    -79       O
ATOM   1327  OD2 ASP C 161     -19.932  17.900 -36.779  1.00 55.55           O
ANISOU 1327  OD2 ASP C 161     6912   6875   7320   -312      1    -73       O
ATOM   1328  N   VAL C 162     -23.831  17.428 -37.177  1.00 43.54           N
ANISOU 1328  N   VAL C 162     5362   5431   5750   -302    -28    -99       N
ATOM   1329  CA  VAL C 162     -24.342  16.521 -36.158  1.00 39.00           C
ANISOU 1329  CA  VAL C 162     4776   4864   5179   -329    -21   -113       C
ATOM   1330  C   VAL C 162     -25.436  15.621 -36.733  1.00 47.08           C
ANISOU 1330  C   VAL C 162     5782   5921   6185   -349    -17   -142       C
ATOM   1331  O   VAL C 162     -25.447  14.410 -36.480  1.00 45.77           O
ANISOU 1331  O   VAL C 162     5625   5746   6018   -382      1   -151       O
ATOM   1332  CB  VAL C 162     -24.819  17.315 -34.926  1.00 27.32           C
ANISOU 1332  CB  VAL C 162     3286   3392   3704   -322    -28   -115       C
ATOM   1333  CG1 VAL C 162     -25.634  16.433 -34.033  1.00 24.14           C
ANISOU 1333  CG1 VAL C 162     2875   3002   3295   -355    -16   -137       C
ATOM   1334  CG2 VAL C 162     -23.609  17.843 -34.151  1.00 31.71           C
ANISOU 1334  CG2 VAL C 162     3858   3913   4279   -314    -27    -92       C
ATOM   1335  N   LEU C 163     -26.360  16.183 -37.528  1.00 35.25           N
ANISOU 1335  N   LEU C 163     4263   4461   4669   -326    -32   -162       N
ATOM   1336  CA  LEU C 163     -27.327  15.343 -38.219  1.00 36.12           C
ANISOU 1336  CA  LEU C 163     4349   4611   4764   -343    -29   -200       C
ATOM   1337  C   LEU C 163     -26.640  14.394 -39.186  1.00 42.28           C
ANISOU 1337  C   LEU C 163     5149   5371   5545   -358    -17   -189       C
ATOM   1338  O   LEU C 163     -27.139  13.289 -39.427  1.00 41.49           O
ANISOU 1338  O   LEU C 163     5039   5286   5437   -392     -2   -216       O
ATOM   1339  CB  LEU C 163     -28.344  16.194 -38.967  1.00 35.94           C
ANISOU 1339  CB  LEU C 163     4301   4638   4718   -300    -57   -228       C
ATOM   1340  CG  LEU C 163     -29.177  17.149 -38.123  1.00 43.54           C
ANISOU 1340  CG  LEU C 163     5239   5630   5675   -277    -74   -249       C
ATOM   1341  CD1 LEU C 163     -30.146  17.920 -38.998  1.00 49.09           C
ANISOU 1341  CD1 LEU C 163     5923   6383   6348   -219   -109   -284       C
ATOM   1342  CD2 LEU C 163     -29.908  16.356 -37.062  1.00 41.11           C
ANISOU 1342  CD2 LEU C 163     4899   5346   5373   -330    -50   -285       C
ATOM   1343  N   ASP C 164     -25.494  14.795 -39.744  1.00 39.51           N
ANISOU 1343  N   ASP C 164     4825   4986   5201   -338    -20   -156       N
ATOM   1344  CA  ASP C 164     -24.804  13.892 -40.653  1.00 48.08           C
ANISOU 1344  CA  ASP C 164     5925   6054   6287   -351     -9   -149       C
ATOM   1345  C   ASP C 164     -24.267  12.673 -39.918  1.00 51.11           C
ANISOU 1345  C   ASP C 164     6325   6410   6683   -385     10   -147       C
ATOM   1346  O   ASP C 164     -24.373  11.553 -40.422  1.00 61.04           O
ANISOU 1346  O   ASP C 164     7590   7668   7934   -408     22   -159       O
ATOM   1347  CB  ASP C 164     -23.673  14.600 -41.394  1.00 42.18           C
ANISOU 1347  CB  ASP C 164     5202   5279   5544   -328    -11   -122       C
ATOM   1348  CG  ASP C 164     -23.069  13.734 -42.486  1.00 47.31           C
ANISOU 1348  CG  ASP C 164     5864   5921   6192   -339     -0   -122       C
ATOM   1349  OD1 ASP C 164     -23.817  13.199 -43.339  1.00 51.60           O
ANISOU 1349  OD1 ASP C 164     6397   6489   6718   -342     -4   -140       O
ATOM   1350  OD2 ASP C 164     -21.836  13.574 -42.490  1.00 54.30           O
ANISOU 1350  OD2 ASP C 164     6763   6777   7093   -345     11   -108       O
ATOM   1351  N   VAL C 165     -23.680  12.860 -38.733  1.00 41.53           N
ANISOU 1351  N   VAL C 165     5125   5170   5483   -384     11   -132       N
ATOM   1352  CA  VAL C 165     -23.097  11.723 -38.012  1.00 47.19           C
ANISOU 1352  CA  VAL C 165     5872   5854   6202   -403     24   -130       C
ATOM   1353  C   VAL C 165     -24.175  10.713 -37.646  1.00 52.86           C
ANISOU 1353  C   VAL C 165     6600   6581   6903   -443     43   -154       C
ATOM   1354  O   VAL C 165     -23.949   9.494 -37.690  1.00 55.25           O
ANISOU 1354  O   VAL C 165     6938   6859   7196   -464     59   -159       O
ATOM   1355  CB  VAL C 165     -22.314  12.193 -36.766  1.00 36.88           C
ANISOU 1355  CB  VAL C 165     4579   4523   4910   -386     17   -114       C
ATOM   1356  CG1 VAL C 165     -21.035  12.835 -37.187  1.00 30.58           C
ANISOU 1356  CG1 VAL C 165     3776   3715   4129   -359      8   -102       C
ATOM   1357  N   TYR C 166     -25.369  11.200 -37.308  1.00 48.16           N
ANISOU 1357  N   TYR C 166     5976   6022   6301   -456     45   -176       N
ATOM   1358  CA  TYR C 166     -26.426  10.282 -36.924  1.00 39.03           C
ANISOU 1358  CA  TYR C 166     4824   4879   5127   -507     73   -211       C
ATOM   1359  C   TYR C 166     -26.902   9.475 -38.118  1.00 49.79           C
ANISOU 1359  C   TYR C 166     6176   6265   6478   -529     83   -238       C
ATOM   1360  O   TYR C 166     -27.082   8.254 -38.009  1.00 53.15           O
ANISOU 1360  O   TYR C 166     6635   6671   6889   -574    113   -254       O
ATOM   1361  CB  TYR C 166     -27.568  11.047 -36.266  1.00 37.33           C
ANISOU 1361  CB  TYR C 166     4570   4707   4908   -515     72   -239       C
ATOM   1362  CG  TYR C 166     -27.346  11.222 -34.778  1.00 38.70           C
ANISOU 1362  CG  TYR C 166     4770   4849   5083   -523     80   -225       C
ATOM   1363  CD1 TYR C 166     -26.412  12.138 -34.299  1.00 40.93           C
ANISOU 1363  CD1 TYR C 166     5059   5108   5384   -479     56   -187       C
ATOM   1364  CD2 TYR C 166     -28.058  10.456 -33.848  1.00 51.68           C
ANISOU 1364  CD2 TYR C 166     6439   6487   6709   -577    116   -252       C
ATOM   1365  CE1 TYR C 166     -26.184  12.294 -32.923  1.00 45.50           C
ANISOU 1365  CE1 TYR C 166     5664   5661   5964   -481     60   -176       C
ATOM   1366  CE2 TYR C 166     -27.858  10.606 -32.477  1.00 50.25           C
ANISOU 1366  CE2 TYR C 166     6292   6274   6525   -582    123   -238       C
ATOM   1367  CZ  TYR C 166     -26.929  11.521 -32.018  1.00 53.20           C
ANISOU 1367  CZ  TYR C 166     6667   6628   6917   -530     92   -199       C
ATOM   1368  OH  TYR C 166     -26.744  11.643 -30.660  1.00 52.51           O
ANISOU 1368  OH  TYR C 166     6614   6512   6826   -532     98   -188       O
ATOM   1369  N   ARG C 167     -27.061  10.128 -39.278  1.00 57.42           N
ANISOU 1369  N   ARG C 167     7103   7267   7446   -497     61   -242       N
ATOM   1370  CA  ARG C 167     -27.540   9.416 -40.459  1.00 50.68           C
ANISOU 1370  CA  ARG C 167     6235   6441   6580   -513     67   -271       C
ATOM   1371  C   ARG C 167     -26.496   8.436 -40.975  1.00 49.30           C
ANISOU 1371  C   ARG C 167     6104   6220   6408   -519     77   -246       C
ATOM   1372  O   ARG C 167     -26.862   7.403 -41.523  1.00 50.41           O
ANISOU 1372  O   ARG C 167     6251   6367   6536   -554     97   -271       O
ATOM   1373  CB  ARG C 167     -27.973  10.405 -41.542  1.00 42.06           C
ANISOU 1373  CB  ARG C 167     5103   5397   5483   -467     36   -281       C
ATOM   1374  CG  ARG C 167     -27.115  10.408 -42.782  1.00 54.92           C
ANISOU 1374  CG  ARG C 167     6748   7008   7112   -439     24   -255       C
ATOM   1375  CD  ARG C 167     -26.570  11.807 -43.127  1.00 54.65           C
ANISOU 1375  CD  ARG C 167     6721   6965   7079   -383     -3   -223       C
ATOM   1376  NE  ARG C 167     -27.435  12.487 -44.072  1.00 50.02           N
ANISOU 1376  NE  ARG C 167     6112   6424   6468   -345    -28   -248       N
ATOM   1377  CZ  ARG C 167     -27.023  13.190 -45.121  1.00 51.60           C
ANISOU 1377  CZ  ARG C 167     6335   6615   6654   -303    -45   -229       C
ATOM   1378  NH1 ARG C 167     -25.736  13.348 -45.375  1.00 43.57           N
ANISOU 1378  NH1 ARG C 167     5356   5549   5649   -303    -34   -188       N
ATOM   1379  NH2 ARG C 167     -27.916  13.753 -45.918  1.00 61.43           N
ANISOU 1379  NH2 ARG C 167     7569   7903   7870   -259    -73   -257       N
ATOM   1380  N   ILE C 168     -25.205   8.695 -40.754  1.00 47.28           N
ANISOU 1380  N   ILE C 168     5877   5921   6167   -489     66   -205       N
ATOM   1381  CA  ILE C 168     -24.192   7.699 -41.110  1.00 43.58           C
ANISOU 1381  CA  ILE C 168     5448   5412   5699   -490     73   -191       C
ATOM   1382  C   ILE C 168     -24.309   6.468 -40.213  1.00 49.71           C
ANISOU 1382  C   ILE C 168     6278   6152   6460   -527     99   -200       C
ATOM   1383  O   ILE C 168     -24.201   5.328 -40.669  1.00 63.36           O
ANISOU 1383  O   ILE C 168     8039   7859   8174   -548    115   -210       O
ATOM   1384  CB  ILE C 168     -22.786   8.323 -41.039  1.00 35.33           C
ANISOU 1384  CB  ILE C 168     4411   4341   4673   -448     54   -159       C
ATOM   1385  CG1 ILE C 168     -22.568   9.321 -42.181  1.00 34.53           C
ANISOU 1385  CG1 ILE C 168     4279   4264   4578   -422     40   -151       C
ATOM   1386  CG2 ILE C 168     -21.705   7.262 -41.049  1.00 31.84           C
ANISOU 1386  CG2 ILE C 168     4010   3858   4229   -442     58   -153       C
ATOM   1387  CD1 ILE C 168     -21.425  10.339 -41.916  1.00 36.23           C
ANISOU 1387  CD1 ILE C 168     4493   4461   4810   -392     30   -129       C
ATOM   1388  N   PHE C 169     -24.528   6.675 -38.923  1.00 52.46           N
ANISOU 1388  N   PHE C 169     6644   6485   6805   -536    106   -198       N
ATOM   1389  CA  PHE C 169     -24.642   5.548 -38.011  1.00 45.83           C
ANISOU 1389  CA  PHE C 169     5873   5600   5941   -571    134   -205       C
ATOM   1390  C   PHE C 169     -25.969   4.819 -38.216  1.00 44.87           C
ANISOU 1390  C   PHE C 169     5750   5502   5798   -639    173   -249       C
ATOM   1391  O   PHE C 169     -26.006   3.589 -38.320  1.00 53.37           O
ANISOU 1391  O   PHE C 169     6884   6543   6851   -674    202   -261       O
ATOM   1392  CB  PHE C 169     -24.475   6.058 -36.572  1.00 39.84           C
ANISOU 1392  CB  PHE C 169     5137   4819   5182   -559    130   -190       C
ATOM   1393  CG  PHE C 169     -24.601   4.997 -35.522  1.00 40.53           C
ANISOU 1393  CG  PHE C 169     5312   4852   5236   -591    160   -196       C
ATOM   1394  CD1 PHE C 169     -23.590   4.075 -35.318  1.00 46.94           C
ANISOU 1394  CD1 PHE C 169     6202   5603   6029   -563    155   -179       C
ATOM   1395  CD2 PHE C 169     -25.733   4.927 -34.718  1.00 43.30           C
ANISOU 1395  CD2 PHE C 169     5672   5211   5569   -647    195   -221       C
ATOM   1396  CE1 PHE C 169     -23.713   3.086 -34.338  1.00 44.86           C
ANISOU 1396  CE1 PHE C 169     6041   5279   5724   -587    183   -182       C
ATOM   1397  CE2 PHE C 169     -25.852   3.934 -33.726  1.00 39.94           C
ANISOU 1397  CE2 PHE C 169     5346   4725   5104   -683    231   -226       C
ATOM   1398  CZ  PHE C 169     -24.848   3.023 -33.552  1.00 36.70           C
ANISOU 1398  CZ  PHE C 169     5027   4246   4670   -651    225   -204       C
ATOM   1399  N   GLU C 170     -27.067   5.567 -38.305  1.00 42.49           N
ANISOU 1399  N   GLU C 170     5382   5261   5502   -656    175   -279       N
ATOM   1400  CA  GLU C 170     -28.410   5.038 -38.540  1.00 42.63           C
ANISOU 1400  CA  GLU C 170     5374   5321   5502   -721    210   -337       C
ATOM   1401  C   GLU C 170     -28.953   5.647 -39.830  1.00 51.41           C
ANISOU 1401  C   GLU C 170     6405   6504   6624   -698    185   -363       C
ATOM   1402  O   GLU C 170     -29.563   6.727 -39.793  1.00 52.05           O
ANISOU 1402  O   GLU C 170     6426   6638   6713   -673    162   -379       O
ATOM   1403  CB  GLU C 170     -29.327   5.369 -37.362  1.00 49.81           C
ANISOU 1403  CB  GLU C 170     6274   6248   6402   -760    234   -367       C
ATOM   1404  CG  GLU C 170     -30.693   4.771 -37.492  1.00 64.79           C
ANISOU 1404  CG  GLU C 170     8144   8194   8281   -837    279   -440       C
ATOM   1405  CD  GLU C 170     -30.597   3.347 -37.955  1.00 87.25           C
ANISOU 1405  CD  GLU C 170    11050  11000  11103   -889    318   -453       C
ATOM   1406  OE1 GLU C 170     -30.375   2.483 -37.077  1.00 95.53           O
ANISOU 1406  OE1 GLU C 170    12192  11979  12125   -931    359   -444       O
ATOM   1407  OE2 GLU C 170     -30.713   3.094 -39.187  1.00 90.90           O
ANISOU 1407  OE2 GLU C 170    11474  11494  11569   -883    309   -472       O
ATOM   1408  N   PRO C 171     -28.782   4.984 -40.989  1.00 54.14           N
ANISOU 1408  N   PRO C 171     6752   6853   6967   -701    186   -369       N
ATOM   1409  CA  PRO C 171     -29.054   5.662 -42.273  1.00 52.08           C
ANISOU 1409  CA  PRO C 171     6427   6649   6711   -660    152   -382       C
ATOM   1410  C   PRO C 171     -30.498   6.014 -42.518  1.00 55.83           C
ANISOU 1410  C   PRO C 171     6831   7207   7176   -677    152   -451       C
ATOM   1411  O   PRO C 171     -30.755   6.859 -43.384  1.00 59.12           O
ANISOU 1411  O   PRO C 171     7199   7672   7593   -624    114   -460       O
ATOM   1412  CB  PRO C 171     -28.539   4.665 -43.315  1.00 38.99           C
ANISOU 1412  CB  PRO C 171     4797   4970   5049   -669    160   -377       C
ATOM   1413  CG  PRO C 171     -27.461   3.938 -42.586  1.00 45.84           C
ANISOU 1413  CG  PRO C 171     5744   5758   5917   -675    176   -336       C
ATOM   1414  CD  PRO C 171     -28.048   3.729 -41.207  1.00 52.08           C
ANISOU 1414  CD  PRO C 171     6561   6532   6694   -720    207   -353       C
ATOM   1415  N   LYS C 172     -31.442   5.433 -41.785  1.00 51.05           N
ANISOU 1415  N   LYS C 172     6218   6621   6557   -746    194   -504       N
ATOM   1416  CA  LYS C 172     -32.850   5.770 -41.944  1.00 51.24           C
ANISOU 1416  CA  LYS C 172     6161   6736   6571   -763    195   -586       C
ATOM   1417  C   LYS C 172     -33.359   6.799 -40.936  1.00 56.88           C
ANISOU 1417  C   LYS C 172     6842   7480   7291   -747    183   -597       C
ATOM   1418  O   LYS C 172     -34.548   7.131 -40.975  1.00 56.22           O
ANISOU 1418  O   LYS C 172     6685   7478   7198   -756    181   -673       O
ATOM   1419  CB  LYS C 172     -33.706   4.503 -41.849  1.00 48.65           C
ANISOU 1419  CB  LYS C 172     5835   6426   6224   -862    257   -657       C
ATOM   1420  CG  LYS C 172     -33.574   3.596 -43.050  1.00 54.15           C
ANISOU 1420  CG  LYS C 172     6539   7123   6914   -877    265   -670       C
ATOM   1421  CD  LYS C 172     -34.095   2.184 -42.804  1.00 61.28           C
ANISOU 1421  CD  LYS C 172     7478   8009   7795   -984    337   -723       C
ATOM   1422  CE  LYS C 172     -33.468   1.207 -43.803  1.00 67.30           C
ANISOU 1422  CE  LYS C 172     8285   8732   8552   -989    345   -702       C
ATOM   1423  NZ  LYS C 172     -31.949   1.283 -43.813  1.00 58.74           N
ANISOU 1423  NZ  LYS C 172     7275   7563   7482   -926    314   -603       N
ATOM   1424  N   CYS C 173     -32.501   7.333 -40.053  1.00 59.15           N
ANISOU 1424  N   CYS C 173     7176   7708   7592   -719    172   -531       N
ATOM   1425  CA  CYS C 173     -33.001   8.141 -38.934  1.00 53.76           C
ANISOU 1425  CA  CYS C 173     6470   7046   6912   -717    170   -545       C
ATOM   1426  C   CYS C 173     -33.634   9.458 -39.371  1.00 45.90           C
ANISOU 1426  C   CYS C 173     5399   6122   5917   -648    119   -571       C
ATOM   1427  O   CYS C 173     -34.362  10.061 -38.582  1.00 52.78           O
ANISOU 1427  O   CYS C 173     6234   7034   6787   -650    118   -607       O
ATOM   1428  CB  CYS C 173     -31.889   8.426 -37.911  1.00 50.13           C
ANISOU 1428  CB  CYS C 173     6076   6507   6465   -698    166   -469       C
ATOM   1429  SG  CYS C 173     -30.485   9.368 -38.513  1.00 49.96           S
ANISOU 1429  SG  CYS C 173     6074   6445   6465   -607    113   -388       S
ATOM   1430  N   LEU C 174     -33.410   9.908 -40.603  1.00 49.43           N
ANISOU 1430  N   LEU C 174     5831   6588   6363   -584     77   -559       N
ATOM   1431  CA  LEU C 174     -34.017  11.147 -41.078  1.00 52.44           C
ANISOU 1431  CA  LEU C 174     6159   7031   6733   -508     25   -585       C
ATOM   1432  C   LEU C 174     -35.285  10.916 -41.908  1.00 55.50           C
ANISOU 1432  C   LEU C 174     6472   7515   7099   -507     15   -681       C
ATOM   1433  O   LEU C 174     -35.971  11.892 -42.234  1.00 58.15           O
ANISOU 1433  O   LEU C 174     6762   7913   7420   -438    -32   -719       O
ATOM   1434  CB  LEU C 174     -32.981  11.961 -41.894  1.00 40.31           C
ANISOU 1434  CB  LEU C 174     4664   5450   5200   -430    -17   -514       C
ATOM   1435  CG  LEU C 174     -32.044  12.934 -41.151  1.00 41.26           C
ANISOU 1435  CG  LEU C 174     4829   5512   5336   -395    -30   -443       C
ATOM   1436  CD1 LEU C 174     -31.652  12.365 -39.833  1.00 41.98           C
ANISOU 1436  CD1 LEU C 174     4947   5558   5445   -455      9   -422       C
ATOM   1437  CD2 LEU C 174     -30.759  13.209 -41.935  1.00 37.62           C
ANISOU 1437  CD2 LEU C 174     4423   4991   4881   -359    -43   -375       C
ATOM   1438  N   ASP C 175     -35.634   9.656 -42.215  1.00 54.55           N
ANISOU 1438  N   ASP C 175     6342   7411   6975   -580     57   -726       N
ATOM   1439  CA  ASP C 175     -36.697   9.374 -43.189  1.00 58.64           C
ANISOU 1439  CA  ASP C 175     6788   8021   7472   -577     46   -819       C
ATOM   1440  C   ASP C 175     -38.049   9.901 -42.734  1.00 56.64           C
ANISOU 1440  C   ASP C 175     6447   7869   7207   -572     35   -919       C
ATOM   1441  O   ASP C 175     -38.832  10.406 -43.546  1.00 64.18           O
ANISOU 1441  O   ASP C 175     7337   8908   8141   -507    -12   -985       O
ATOM   1442  CB  ASP C 175     -36.829   7.871 -43.444  1.00 58.74           C
ANISOU 1442  CB  ASP C 175     6808   8027   7482   -672    104   -854       C
ATOM   1443  CG  ASP C 175     -35.652   7.289 -44.185  1.00 61.45           C
ANISOU 1443  CG  ASP C 175     7223   8292   7833   -666    106   -776       C
ATOM   1444  OD1 ASP C 175     -34.830   8.062 -44.743  1.00 54.75           O
ANISOU 1444  OD1 ASP C 175     6404   7410   6988   -586     60   -708       O
ATOM   1445  OD2 ASP C 175     -35.565   6.039 -44.202  1.00 67.83           O
ANISOU 1445  OD2 ASP C 175     8060   9072   8639   -745    157   -788       O
ATOM   1446  N   GLU C 176     -38.372   9.737 -41.456  1.00 50.46           N
ANISOU 1446  N   GLU C 176     5659   7082   6432   -639     79   -939       N
ATOM   1447  CA  GLU C 176     -39.664  10.212 -40.997  1.00 47.87           C
ANISOU 1447  CA  GLU C 176     5241   6855   6093   -640     73  -1044       C
ATOM   1448  C   GLU C 176     -39.741  11.731 -40.932  1.00 51.66           C
ANISOU 1448  C   GLU C 176     5702   7359   6567   -525      1  -1027       C
ATOM   1449  O   GLU C 176     -40.826  12.258 -40.683  1.00 65.74           O
ANISOU 1449  O   GLU C 176     7404   9236   8338   -503    -18  -1119       O
ATOM   1450  CB  GLU C 176     -39.990   9.604 -39.637  1.00 52.46           C
ANISOU 1450  CB  GLU C 176     5830   7422   6680   -751    146  -1072       C
ATOM   1451  N   PHE C 177     -38.641  12.454 -41.164  1.00 47.87           N
ANISOU 1451  N   PHE C 177     5294   6800   6095   -453    -37   -919       N
ATOM   1452  CA  PHE C 177     -38.623  13.915 -41.070  1.00 48.88           C
ANISOU 1452  CA  PHE C 177     5425   6933   6214   -348    -98   -895       C
ATOM   1453  C   PHE C 177     -38.142  14.493 -42.394  1.00 57.24           C
ANISOU 1453  C   PHE C 177     6521   7975   7253   -251   -154   -854       C
ATOM   1454  O   PHE C 177     -36.940  14.737 -42.590  1.00 57.70           O
ANISOU 1454  O   PHE C 177     6660   7942   7321   -232   -157   -754       O
ATOM   1455  CB  PHE C 177     -37.764  14.391 -39.898  1.00 48.04           C
ANISOU 1455  CB  PHE C 177     5379   6743   6131   -361    -82   -809       C
ATOM   1456  CG  PHE C 177     -37.904  13.542 -38.664  1.00 48.69           C
ANISOU 1456  CG  PHE C 177     5459   6810   6230   -471    -15   -825       C
ATOM   1457  CD1 PHE C 177     -38.960  13.744 -37.793  1.00 42.66           C
ANISOU 1457  CD1 PHE C 177     4632   6116   5463   -499     -1   -906       C
ATOM   1458  CD2 PHE C 177     -36.983  12.552 -38.373  1.00 46.51           C
ANISOU 1458  CD2 PHE C 177     5252   6449   5970   -541     34   -763       C
ATOM   1459  CE1 PHE C 177     -39.111  12.950 -36.660  1.00 32.84           C
ANISOU 1459  CE1 PHE C 177     3399   4852   4227   -605     68   -922       C
ATOM   1460  CE2 PHE C 177     -37.126  11.770 -37.249  1.00 44.86           C
ANISOU 1460  CE2 PHE C 177     5060   6218   5767   -636     96   -778       C
ATOM   1461  CZ  PHE C 177     -38.204  11.978 -36.390  1.00 42.37           C
ANISOU 1461  CZ  PHE C 177     4686   5967   5444   -672    116   -856       C
ATOM   1462  N   PRO C 178     -39.054  14.742 -43.332  1.00 66.44           N
ANISOU 1462  N   PRO C 178     7632   9228   8386   -185   -200   -934       N
ATOM   1463  CA  PRO C 178     -38.624  15.213 -44.666  1.00 61.86           C
ANISOU 1463  CA  PRO C 178     7099   8627   7778    -94   -251   -896       C
ATOM   1464  C   PRO C 178     -37.915  16.556 -44.601  1.00 62.48           C
ANISOU 1464  C   PRO C 178     7256   8638   7845     -7   -290   -814       C
ATOM   1465  O   PRO C 178     -36.912  16.784 -45.295  1.00 69.03           O
ANISOU 1465  O   PRO C 178     8167   9392   8670     21   -296   -734       O
ATOM   1466  CB  PRO C 178     -39.945  15.282 -45.442  1.00 52.22           C
ANISOU 1466  CB  PRO C 178     5793   7528   6519    -34   -297  -1018       C
ATOM   1467  CG  PRO C 178     -40.962  14.518 -44.578  1.00 54.61           C
ANISOU 1467  CG  PRO C 178     5996   7913   6838   -127   -251  -1122       C
ATOM   1468  CD  PRO C 178     -40.516  14.697 -43.184  1.00 58.93           C
ANISOU 1468  CD  PRO C 178     6573   8400   7417   -185   -211  -1067       C
ATOM   1469  N   ASN C 179     -38.505  17.479 -43.856  1.00 54.36           N
ANISOU 1469  N   ASN C 179     6204   7644   6809     39   -318   -845       N
ATOM   1470  CA  ASN C 179     -37.879  18.546 -43.091  1.00 59.80           C
ANISOU 1470  CA  ASN C 179     6952   8264   7504     71   -326   -773       C
ATOM   1471  C   ASN C 179     -36.354  18.535 -42.986  1.00 58.80           C
ANISOU 1471  C   ASN C 179     6918   8019   7403     34   -293   -655       C
ATOM   1472  O   ASN C 179     -35.668  19.453 -43.449  1.00 58.09           O
ANISOU 1472  O   ASN C 179     6908   7870   7295     98   -317   -594       O
ATOM   1473  CB  ASN C 179     -38.448  18.453 -41.679  1.00 64.02           C
ANISOU 1473  CB  ASN C 179     7426   8834   8064     13   -298   -815       C
ATOM   1474  CG  ASN C 179     -38.484  19.743 -41.019  1.00 61.19           C
ANISOU 1474  CG  ASN C 179     7091   8461   7696     79   -332   -795       C
ATOM   1475  OD1 ASN C 179     -38.350  20.778 -41.673  1.00 77.37           O
ANISOU 1475  OD1 ASN C 179     9195  10490   9710    182   -383   -771       O
ATOM   1476  ND2 ASN C 179     -38.691  19.730 -39.723  1.00 45.92           N
ANISOU 1476  ND2 ASN C 179     5124   6535   5788     25   -302   -807       N
ATOM   1477  N   LEU C 180     -35.827  17.527 -42.299  1.00 50.52           N
ANISOU 1477  N   LEU C 180     5863   6936   6395    -69   -235   -628       N
ATOM   1478  CA  LEU C 180     -34.405  17.490 -42.015  1.00 41.26           C
ANISOU 1478  CA  LEU C 180     4764   5662   5249   -103   -204   -531       C
ATOM   1479  C   LEU C 180     -33.632  16.970 -43.209  1.00 52.92           C
ANISOU 1479  C   LEU C 180     6285   7101   6721   -104   -198   -493       C
ATOM   1480  O   LEU C 180     -32.550  17.478 -43.518  1.00 63.89           O
ANISOU 1480  O   LEU C 180     7744   8419   8112    -84   -198   -423       O
ATOM   1481  CB  LEU C 180     -34.130  16.613 -40.799  1.00 37.19           C
ANISOU 1481  CB  LEU C 180     4236   5123   4771   -199   -151   -520       C
ATOM   1482  CG  LEU C 180     -34.676  17.051 -39.450  1.00 43.03           C
ANISOU 1482  CG  LEU C 180     4944   5885   5521   -214   -145   -544       C
ATOM   1483  CD1 LEU C 180     -34.292  16.025 -38.395  1.00 49.10           C
ANISOU 1483  CD1 LEU C 180     5721   6618   6318   -310    -88   -528       C
ATOM   1484  CD2 LEU C 180     -34.150  18.437 -39.100  1.00 42.13           C
ANISOU 1484  CD2 LEU C 180     4874   5728   5404   -149   -174   -492       C
ATOM   1485  N   LYS C 181     -34.164  15.965 -43.903  1.00 48.34           N
ANISOU 1485  N   LYS C 181     5664   6568   6135   -132   -190   -544       N
ATOM   1486  CA  LYS C 181     -33.420  15.483 -45.057  1.00 51.19           C
ANISOU 1486  CA  LYS C 181     6067   6892   6489   -131   -186   -508       C
ATOM   1487  C   LYS C 181     -33.461  16.486 -46.199  1.00 47.49           C
ANISOU 1487  C   LYS C 181     5641   6426   5979    -33   -235   -500       C
ATOM   1488  O   LYS C 181     -32.543  16.511 -47.027  1.00 41.41           O
ANISOU 1488  O   LYS C 181     4933   5600   5202    -23   -230   -447       O
ATOM   1489  CB  LYS C 181     -33.919  14.103 -45.476  1.00 48.09           C
ANISOU 1489  CB  LYS C 181     5626   6544   6102   -191   -160   -561       C
ATOM   1490  CG  LYS C 181     -35.382  13.998 -45.762  1.00 54.28           C
ANISOU 1490  CG  LYS C 181     6330   7433   6861   -172   -183   -665       C
ATOM   1491  CD  LYS C 181     -35.767  12.529 -45.738  1.00 62.90           C
ANISOU 1491  CD  LYS C 181     7377   8554   7966   -266   -136   -716       C
ATOM   1492  CE  LYS C 181     -34.781  11.682 -46.533  1.00 73.47           C
ANISOU 1492  CE  LYS C 181     8768   9834   9315   -296   -112   -662       C
ATOM   1493  NZ  LYS C 181     -35.249  11.358 -47.915  1.00 84.59           N
ANISOU 1493  NZ  LYS C 181    10152  11294  10696   -263   -137   -709       N
ATOM   1494  N   ASP C 182     -34.465  17.356 -46.215  1.00 42.81           N
ANISOU 1494  N   ASP C 182     5023   5890   5353     42   -282   -552       N
ATOM   1495  CA  ASP C 182     -34.467  18.463 -47.156  1.00 41.53           C
ANISOU 1495  CA  ASP C 182     4925   5714   5141    147   -331   -539       C
ATOM   1496  C   ASP C 182     -33.420  19.504 -46.768  1.00 46.30           C
ANISOU 1496  C   ASP C 182     5618   6226   5747    162   -323   -455       C
ATOM   1497  O   ASP C 182     -32.649  19.965 -47.619  1.00 47.61           O
ANISOU 1497  O   ASP C 182     5870   6332   5889    193   -324   -405       O
ATOM   1498  CB  ASP C 182     -35.875  19.058 -47.217  1.00 54.79           C
ANISOU 1498  CB  ASP C 182     6552   7486   6780    231   -389   -627       C
ATOM   1499  CG  ASP C 182     -36.002  20.164 -48.228  1.00 72.07           C
ANISOU 1499  CG  ASP C 182     8819   9662   8904    354   -447   -622       C
ATOM   1500  OD1 ASP C 182     -35.425  20.038 -49.326  1.00 80.30           O
ANISOU 1500  OD1 ASP C 182     9924  10663   9923    370   -447   -586       O
ATOM   1501  OD2 ASP C 182     -36.690  21.164 -47.923  1.00 79.94           O
ANISOU 1501  OD2 ASP C 182     9818  10688   9868    437   -494   -656       O
ATOM   1502  N   PHE C 183     -33.375  19.885 -45.478  1.00 44.02           N
ANISOU 1502  N   PHE C 183     5313   5926   5486    136   -309   -443       N
ATOM   1503  CA  PHE C 183     -32.317  20.771 -44.993  1.00 38.30           C
ANISOU 1503  CA  PHE C 183     4665   5117   4772    135   -292   -369       C
ATOM   1504  C   PHE C 183     -30.939  20.192 -45.307  1.00 46.46           C
ANISOU 1504  C   PHE C 183     5741   6079   5832     71   -246   -306       C
ATOM   1505  O   PHE C 183     -30.009  20.929 -45.667  1.00 47.65           O
ANISOU 1505  O   PHE C 183     5972   6162   5970     85   -236   -253       O
ATOM   1506  CB  PHE C 183     -32.474  21.019 -43.482  1.00 41.64           C
ANISOU 1506  CB  PHE C 183     5048   5544   5227    103   -280   -372       C
ATOM   1507  CG  PHE C 183     -31.187  21.412 -42.796  1.00 38.55           C
ANISOU 1507  CG  PHE C 183     4710   5070   4865     63   -245   -299       C
ATOM   1508  CD1 PHE C 183     -30.825  22.753 -42.687  1.00 35.91           C
ANISOU 1508  CD1 PHE C 183     4446   4687   4509    112   -257   -265       C
ATOM   1509  CD2 PHE C 183     -30.317  20.441 -42.304  1.00 36.35           C
ANISOU 1509  CD2 PHE C 183     4417   4761   4633    -21   -199   -269       C
ATOM   1510  CE1 PHE C 183     -29.623  23.124 -42.094  1.00 43.26           C
ANISOU 1510  CE1 PHE C 183     5421   5548   5467     71   -222   -208       C
ATOM   1511  CE2 PHE C 183     -29.114  20.798 -41.718  1.00 35.12           C
ANISOU 1511  CE2 PHE C 183     4302   4538   4502    -51   -171   -214       C
ATOM   1512  CZ  PHE C 183     -28.768  22.151 -41.596  1.00 39.97           C
ANISOU 1512  CZ  PHE C 183     4976   5112   5099     -9   -181   -186       C
ATOM   1513  N   MET C 184     -30.785  18.870 -45.185  1.00 45.17           N
ANISOU 1513  N   MET C 184     5528   5932   5704     -2   -215   -316       N
ATOM   1514  CA  MET C 184     -29.501  18.260 -45.522  1.00 54.23           C
ANISOU 1514  CA  MET C 184     6710   7020   6875    -54   -177   -265       C
ATOM   1515  C   MET C 184     -29.166  18.464 -46.996  1.00 62.02           C
ANISOU 1515  C   MET C 184     7754   7987   7825    -16   -186   -251       C
ATOM   1516  O   MET C 184     -28.010  18.722 -47.349  1.00 60.89           O
ANISOU 1516  O   MET C 184     7671   7781   7686    -31   -162   -202       O
ATOM   1517  CB  MET C 184     -29.507  16.768 -45.175  1.00 51.31           C
ANISOU 1517  CB  MET C 184     6286   6669   6539   -128   -146   -283       C
ATOM   1518  CG  MET C 184     -29.639  16.440 -43.701  1.00 40.44           C
ANISOU 1518  CG  MET C 184     4873   5297   5195   -177   -126   -289       C
ATOM   1519  SD  MET C 184     -28.407  17.265 -42.679  1.00 40.53           S
ANISOU 1519  SD  MET C 184     4930   5237   5232   -185   -110   -227       S
ATOM   1520  CE  MET C 184     -27.158  15.987 -42.503  1.00 43.73           C
ANISOU 1520  CE  MET C 184     5346   5596   5672   -252    -70   -197       C
ATOM   1521  N   SER C 185     -30.175  18.375 -47.866  1.00 62.24           N
ANISOU 1521  N   SER C 185     7764   8069   7815     35   -222   -298       N
ATOM   1522  CA  SER C 185     -29.945  18.511 -49.302  1.00 52.67           C
ANISOU 1522  CA  SER C 185     6609   6840   6561     76   -234   -289       C
ATOM   1523  C   SER C 185     -29.625  19.948 -49.688  1.00 48.29           C
ANISOU 1523  C   SER C 185     6155   6232   5961    143   -250   -254       C
ATOM   1524  O   SER C 185     -28.742  20.195 -50.523  1.00 39.03           O
ANISOU 1524  O   SER C 185     5060   5001   4768    141   -230   -214       O
ATOM   1525  CB  SER C 185     -31.168  18.016 -50.070  1.00 49.93           C
ANISOU 1525  CB  SER C 185     6213   6574   6184    118   -272   -358       C
ATOM   1526  OG  SER C 185     -30.833  17.742 -51.415  1.00 55.65           O
ANISOU 1526  OG  SER C 185     6982   7284   6880    136   -274   -348       O
ATOM   1527  N   ARG C 186     -30.347  20.916 -49.118  1.00 49.47           N
ANISOU 1527  N   ARG C 186     6309   6398   6087    201   -284   -273       N
ATOM   1528  CA  ARG C 186     -30.052  22.296 -49.468  1.00 45.99           C
ANISOU 1528  CA  ARG C 186     5980   5897   5597    265   -297   -240       C
ATOM   1529  C   ARG C 186     -28.696  22.723 -48.925  1.00 53.10           C
ANISOU 1529  C   ARG C 186     6934   6715   6528    202   -243   -177       C
ATOM   1530  O   ARG C 186     -27.995  23.508 -49.573  1.00 60.27           O
ANISOU 1530  O   ARG C 186     7948   7554   7398    217   -226   -140       O
ATOM   1531  CB  ARG C 186     -31.182  23.199 -48.998  1.00 56.81           C
ANISOU 1531  CB  ARG C 186     7345   7308   6933    351   -350   -280       C
ATOM   1532  CG  ARG C 186     -32.557  22.575 -49.289  1.00 70.68           C
ANISOU 1532  CG  ARG C 186     9011   9170   8675    397   -399   -363       C
ATOM   1533  CD  ARG C 186     -33.708  23.541 -49.028  1.00 66.38           C
ANISOU 1533  CD  ARG C 186     8463   8673   8084    501   -462   -415       C
ATOM   1534  NE  ARG C 186     -34.217  23.339 -47.686  1.00 55.22           N
ANISOU 1534  NE  ARG C 186     6952   7310   6718    460   -456   -448       N
ATOM   1535  CZ  ARG C 186     -33.905  24.154 -46.708  1.00 54.99           C
ANISOU 1535  CZ  ARG C 186     6951   7239   6703    455   -445   -415       C
ATOM   1536  NH1 ARG C 186     -33.107  25.171 -47.004  1.00 55.32           N
ANISOU 1536  NH1 ARG C 186     7116   7191   6713    486   -438   -353       N
ATOM   1537  NH2 ARG C 186     -34.357  23.952 -45.469  1.00 52.87           N
ANISOU 1537  NH2 ARG C 186     6597   7016   6477    415   -438   -445       N
ATOM   1538  N   PHE C 187     -28.270  22.169 -47.788  1.00 47.70           N
ANISOU 1538  N   PHE C 187     6181   6035   5907    128   -213   -168       N
ATOM   1539  CA  PHE C 187     -26.931  22.473 -47.306  1.00 44.35           C
ANISOU 1539  CA  PHE C 187     5795   5543   5513     68   -163   -120       C
ATOM   1540  C   PHE C 187     -25.869  21.918 -48.246  1.00 38.95           C
ANISOU 1540  C   PHE C 187     5144   4823   4833     23   -125    -96       C
ATOM   1541  O   PHE C 187     -24.904  22.611 -48.586  1.00 45.49           O
ANISOU 1541  O   PHE C 187     6050   5587   5646      7    -91    -65       O
ATOM   1542  CB  PHE C 187     -26.725  21.950 -45.876  1.00 46.43           C
ANISOU 1542  CB  PHE C 187     5980   5822   5838      9   -146   -120       C
ATOM   1543  CG  PHE C 187     -25.418  22.372 -45.295  1.00 43.24           C
ANISOU 1543  CG  PHE C 187     5608   5359   5463    -40   -103    -83       C
ATOM   1544  CD1 PHE C 187     -25.303  23.582 -44.651  1.00 41.93           C
ANISOU 1544  CD1 PHE C 187     5484   5160   5286    -21   -102    -68       C
ATOM   1545  CD2 PHE C 187     -24.279  21.600 -45.475  1.00 37.43           C
ANISOU 1545  CD2 PHE C 187     4861   4601   4759   -102    -64    -68       C
ATOM   1546  CE1 PHE C 187     -24.087  23.996 -44.149  1.00 47.36           C
ANISOU 1546  CE1 PHE C 187     6198   5798   6000    -70    -60    -42       C
ATOM   1547  CE2 PHE C 187     -23.076  22.008 -44.980  1.00 40.49           C
ANISOU 1547  CE2 PHE C 187     5270   4944   5170   -144    -27    -46       C
ATOM   1548  CZ  PHE C 187     -22.973  23.211 -44.318  1.00 41.57           C
ANISOU 1548  CZ  PHE C 187     5444   5051   5298   -132    -23    -35       C
ATOM   1549  N   GLU C 188     -26.024  20.665 -48.677  1.00 48.69           N
ANISOU 1549  N   GLU C 188     6320   6096   6086     -2   -125   -115       N
ATOM   1550  CA  GLU C 188     -25.082  20.071 -49.630  1.00 45.50           C
ANISOU 1550  CA  GLU C 188     5941   5663   5683    -41    -93    -99       C
ATOM   1551  C   GLU C 188     -25.180  20.689 -51.027  1.00 47.33           C
ANISOU 1551  C   GLU C 188     6264   5869   5850     11   -102    -93       C
ATOM   1552  O   GLU C 188     -24.220  20.621 -51.806  1.00 42.42           O
ANISOU 1552  O   GLU C 188     5693   5206   5221    -21    -65    -72       O
ATOM   1553  CB  GLU C 188     -25.311  18.557 -49.695  1.00 45.58           C
ANISOU 1553  CB  GLU C 188     5870   5720   5727    -77    -93   -123       C
ATOM   1554  CG  GLU C 188     -24.781  17.819 -48.448  1.00 45.23           C
ANISOU 1554  CG  GLU C 188     5765   5677   5742   -139    -69   -118       C
ATOM   1555  CD  GLU C 188     -25.200  16.370 -48.426  1.00 49.67           C
ANISOU 1555  CD  GLU C 188     6264   6282   6328   -170    -70   -145       C
ATOM   1556  OE1 GLU C 188     -25.800  15.917 -49.411  1.00 54.49           O
ANISOU 1556  OE1 GLU C 188     6868   6921   6913   -151    -85   -168       O
ATOM   1557  OE2 GLU C 188     -24.952  15.686 -47.423  1.00 53.99           O
ANISOU 1557  OE2 GLU C 188     6772   6829   6914   -213    -55   -146       O
ATOM   1558  N   GLY C 189     -26.307  21.304 -51.357  1.00 49.65           N
ANISOU 1558  N   GLY C 189     6584   6188   6093     93   -150   -115       N
ATOM   1559  CA  GLY C 189     -26.400  21.998 -52.612  1.00 44.80           C
ANISOU 1559  CA  GLY C 189     6076   5541   5406    153   -163   -108       C
ATOM   1560  C   GLY C 189     -25.858  23.409 -52.636  1.00 47.44           C
ANISOU 1560  C   GLY C 189     6532   5796   5697    172   -142    -73       C
ATOM   1561  O   GLY C 189     -25.836  24.016 -53.707  1.00 55.16           O
ANISOU 1561  O   GLY C 189     7620   6731   6606    219   -145    -63       O
ATOM   1562  N   LEU C 190     -25.434  23.971 -51.512  1.00 52.36           N
ANISOU 1562  N   LEU C 190     7149   6394   6353    139   -121    -56       N
ATOM   1563  CA  LEU C 190     -24.783  25.272 -51.596  1.00 59.26           C
ANISOU 1563  CA  LEU C 190     8147   7184   7185    141    -88    -25       C
ATOM   1564  C   LEU C 190     -23.519  25.171 -52.451  1.00 56.08           C
ANISOU 1564  C   LEU C 190     7809   6724   6775     75    -24     -2       C
ATOM   1565  O   LEU C 190     -22.722  24.238 -52.300  1.00 46.95           O
ANISOU 1565  O   LEU C 190     6578   5584   5678     -2     11     -3       O
ATOM   1566  CB  LEU C 190     -24.459  25.814 -50.199  1.00 51.50           C
ANISOU 1566  CB  LEU C 190     7134   6188   6245    107    -71    -15       C
ATOM   1567  CG  LEU C 190     -25.632  26.071 -49.248  1.00 43.42           C
ANISOU 1567  CG  LEU C 190     6054   5216   5228    166   -127    -39       C
ATOM   1568  CD1 LEU C 190     -25.214  25.953 -47.791  1.00 37.14           C
ANISOU 1568  CD1 LEU C 190     5180   4431   4502    106   -106    -34       C
ATOM   1569  CD2 LEU C 190     -26.240  27.411 -49.489  1.00 39.00           C
ANISOU 1569  CD2 LEU C 190     5606   4618   4593    256   -158    -36       C
ATOM   1570  N   LYS C 191     -23.348  26.152 -53.349  1.00 49.85           N
ANISOU 1570  N   LYS C 191     7167   5865   5909    106     -7     15       N
ATOM   1571  CA  LYS C 191     -22.307  26.115 -54.378  1.00 49.87           C
ANISOU 1571  CA  LYS C 191     7248   5812   5887     50     54     30       C
ATOM   1572  C   LYS C 191     -20.935  25.771 -53.807  1.00 55.87           C
ANISOU 1572  C   LYS C 191     7952   6560   6716    -65    124     32       C
ATOM   1573  O   LYS C 191     -20.304  24.781 -54.205  1.00 52.35           O
ANISOU 1573  O   LYS C 191     7446   6138   6306   -120    149     23       O
ATOM   1574  CB  LYS C 191     -22.255  27.461 -55.100  1.00 57.44           C
ANISOU 1574  CB  LYS C 191     8393   6681   6750     91     74     50       C
ATOM   1575  CG  LYS C 191     -21.313  27.497 -56.295  1.00 60.94           C
ANISOU 1575  CG  LYS C 191     8939   7063   7152     37    139     62       C
ATOM   1576  N   LYS C 192     -20.457  26.578 -52.859  1.00 58.63           N
ANISOU 1576  N   LYS C 192     8316   6877   7083   -100    154     39       N
ATOM   1577  CA  LYS C 192     -19.113  26.351 -52.353  1.00 54.81           C
ANISOU 1577  CA  LYS C 192     7782   6385   6657   -204    220     31       C
ATOM   1578  C   LYS C 192     -19.017  25.101 -51.482  1.00 54.97           C
ANISOU 1578  C   LYS C 192     7641   6480   6764   -231    197     14       C
ATOM   1579  O   LYS C 192     -17.923  24.541 -51.355  1.00 57.58           O
ANISOU 1579  O   LYS C 192     7918   6819   7140   -304    241     -2       O
ATOM   1580  CB  LYS C 192     -18.630  27.585 -51.608  1.00 48.77           C
ANISOU 1580  CB  LYS C 192     7081   5566   5884   -234    260     36       C
ATOM   1581  CG  LYS C 192     -17.975  28.598 -52.544  1.00 48.49           C
ANISOU 1581  CG  LYS C 192     7207   5441   5776   -267    328     44       C
ATOM   1582  CD  LYS C 192     -17.264  29.698 -51.779  1.00 61.35           C
ANISOU 1582  CD  LYS C 192     8888   7018   7405   -324    385     41       C
ATOM   1583  CE  LYS C 192     -15.930  30.020 -52.409  1.00 75.28           C
ANISOU 1583  CE  LYS C 192    10721   8728   9152   -428    485     22       C
ATOM   1584  NZ  LYS C 192     -16.110  31.014 -53.508  1.00 80.59           N
ANISOU 1584  NZ  LYS C 192    11593   9309   9720   -407    518     43       N
ATOM   1585  N   ILE C 193     -20.126  24.638 -50.896  1.00 50.57           N
ANISOU 1585  N   ILE C 193     7011   5977   6225   -173    133     11       N
ATOM   1586  CA  ILE C 193     -20.075  23.372 -50.169  1.00 46.32           C
ANISOU 1586  CA  ILE C 193     6340   5501   5759   -200    115     -5       C
ATOM   1587  C   ILE C 193     -20.033  22.217 -51.153  1.00 43.01           C
ANISOU 1587  C   ILE C 193     5891   5110   5342   -208    112    -14       C
ATOM   1588  O   ILE C 193     -19.254  21.272 -50.985  1.00 43.96           O
ANISOU 1588  O   ILE C 193     5943   5249   5510   -260    133    -25       O
ATOM   1589  CB  ILE C 193     -21.255  23.228 -49.180  1.00 41.55           C
ANISOU 1589  CB  ILE C 193     5670   4944   5172   -151     58    -11       C
ATOM   1590  CG1 ILE C 193     -21.237  24.324 -48.110  1.00 45.98           C
ANISOU 1590  CG1 ILE C 193     6253   5481   5737   -146     62     -3       C
ATOM   1591  CG2 ILE C 193     -21.188  21.881 -48.499  1.00 44.08           C
ANISOU 1591  CG2 ILE C 193     5876   5318   5556   -183     48    -26       C
ATOM   1592  CD1 ILE C 193     -19.879  24.476 -47.404  1.00 51.61           C
ANISOU 1592  CD1 ILE C 193     6948   6169   6494   -222    115     -3       C
ATOM   1593  N   SER C 194     -20.853  22.288 -52.207  1.00 48.53           N
ANISOU 1593  N   SER C 194     6644   5810   5986   -151     84    -12       N
ATOM   1594  CA  SER C 194     -20.864  21.239 -53.222  1.00 49.64           C
ANISOU 1594  CA  SER C 194     6761   5976   6124   -156     80    -22       C
ATOM   1595  C   SER C 194     -19.499  21.084 -53.889  1.00 48.65           C
ANISOU 1595  C   SER C 194     6667   5815   6003   -225    143    -20       C
ATOM   1596  O   SER C 194     -19.008  19.964 -54.063  1.00 51.19           O
ANISOU 1596  O   SER C 194     6922   6165   6364   -262    153    -33       O
ATOM   1597  CB  SER C 194     -21.924  21.535 -54.269  1.00 50.79           C
ANISOU 1597  CB  SER C 194     6972   6125   6200    -77     39    -24       C
ATOM   1598  OG  SER C 194     -21.815  20.603 -55.328  1.00 57.60           O
ANISOU 1598  OG  SER C 194     7822   7006   7056    -86     42    -33       O
ATOM   1599  N   ALA C 195     -18.872  22.195 -54.284  1.00 45.31           N
ANISOU 1599  N   ALA C 195     6349   5328   5538   -244    188     -8       N
ATOM   1600  CA  ALA C 195     -17.548  22.095 -54.893  1.00 43.62           C
ANISOU 1600  CA  ALA C 195     6160   5084   5328   -319    257    -18       C
ATOM   1601  C   ALA C 195     -16.536  21.487 -53.925  1.00 56.59           C
ANISOU 1601  C   ALA C 195     7698   6755   7047   -385    282    -40       C
ATOM   1602  O   ALA C 195     -15.693  20.669 -54.325  1.00 55.42           O
ANISOU 1602  O   ALA C 195     7506   6625   6926   -431    310    -61       O
ATOM   1603  CB  ALA C 195     -17.076  23.469 -55.364  1.00 38.98           C
ANISOU 1603  CB  ALA C 195     5712   4419   4679   -339    310     -7       C
ATOM   1604  N   TYR C 196     -16.608  21.873 -52.644  1.00 49.52           N
ANISOU 1604  N   TYR C 196     6763   5868   6185   -384    270    -40       N
ATOM   1605  CA  TYR C 196     -15.672  21.350 -51.654  1.00 50.22           C
ANISOU 1605  CA  TYR C 196     6757   5984   6339   -434    287    -64       C
ATOM   1606  C   TYR C 196     -15.818  19.841 -51.511  1.00 53.05           C
ANISOU 1606  C   TYR C 196     7017   6396   6741   -424    252    -75       C
ATOM   1607  O   TYR C 196     -14.824  19.117 -51.355  1.00 41.97           O
ANISOU 1607  O   TYR C 196     5556   5013   5377   -465    273   -102       O
ATOM   1608  CB  TYR C 196     -15.900  22.062 -50.318  1.00 42.79           C
ANISOU 1608  CB  TYR C 196     5799   5041   5419   -424    273    -59       C
ATOM   1609  CG  TYR C 196     -15.104  21.546 -49.140  1.00 46.37           C
ANISOU 1609  CG  TYR C 196     6156   5526   5936   -458    277    -84       C
ATOM   1610  CD1 TYR C 196     -13.750  21.309 -49.235  1.00 50.04           C
ANISOU 1610  CD1 TYR C 196     6591   5997   6426   -517    324   -121       C
ATOM   1611  CD2 TYR C 196     -15.711  21.327 -47.915  1.00 52.69           C
ANISOU 1611  CD2 TYR C 196     6899   6353   6768   -427    234    -77       C
ATOM   1612  CE1 TYR C 196     -13.014  20.860 -48.132  1.00 45.13           C
ANISOU 1612  CE1 TYR C 196     5882   5407   5856   -535    321   -152       C
ATOM   1613  CE2 TYR C 196     -14.993  20.887 -46.819  1.00 56.08           C
ANISOU 1613  CE2 TYR C 196     7253   6808   7247   -449    234   -100       C
ATOM   1614  CZ  TYR C 196     -13.644  20.649 -46.928  1.00 52.82           C
ANISOU 1614  CZ  TYR C 196     6811   6402   6857   -498    274   -138       C
ATOM   1615  OH  TYR C 196     -12.936  20.204 -45.816  1.00 53.30           O
ANISOU 1615  OH  TYR C 196     6797   6492   6963   -506    266   -168       O
ATOM   1616  N   MET C 197     -17.055  19.345 -51.581  1.00 52.15           N
ANISOU 1616  N   MET C 197     6888   6308   6617   -370    199    -60       N
ATOM   1617  CA  MET C 197     -17.259  17.911 -51.431  1.00 54.84           C
ANISOU 1617  CA  MET C 197     7149   6694   6994   -367    171    -71       C
ATOM   1618  C   MET C 197     -16.763  17.148 -52.647  1.00 50.70           C
ANISOU 1618  C   MET C 197     6630   6172   6460   -386    190    -82       C
ATOM   1619  O   MET C 197     -16.318  16.003 -52.510  1.00 51.80           O
ANISOU 1619  O   MET C 197     6709   6337   6635   -404    187    -99       O
ATOM   1620  CB  MET C 197     -18.730  17.612 -51.162  1.00 51.24           C
ANISOU 1620  CB  MET C 197     6671   6268   6529   -315    118    -64       C
ATOM   1621  CG  MET C 197     -19.227  18.204 -49.858  1.00 55.29           C
ANISOU 1621  CG  MET C 197     7165   6785   7057   -299     97    -58       C
ATOM   1622  SD  MET C 197     -20.867  17.621 -49.390  1.00 57.71           S
ANISOU 1622  SD  MET C 197     7422   7141   7363   -254     43    -66       S
ATOM   1623  CE  MET C 197     -21.837  18.778 -50.308  1.00 62.95           C
ANISOU 1623  CE  MET C 197     8162   7796   7960   -191     19    -60       C
ATOM   1624  N   LYS C 198     -16.828  17.762 -53.833  1.00 50.31           N
ANISOU 1624  N   LYS C 198     6662   6095   6360   -380    209    -73       N
ATOM   1625  CA  LYS C 198     -16.299  17.192 -55.070  1.00 44.83           C
ANISOU 1625  CA  LYS C 198     5985   5397   5650   -402    234    -84       C
ATOM   1626  C   LYS C 198     -14.837  17.543 -55.290  1.00 51.39           C
ANISOU 1626  C   LYS C 198     6833   6205   6489   -468    299   -105       C
ATOM   1627  O   LYS C 198     -14.389  17.619 -56.437  1.00 65.31           O
ANISOU 1627  O   LYS C 198     8649   7948   8220   -491    334   -111       O
ATOM   1628  CB  LYS C 198     -17.139  17.643 -56.262  1.00 34.84           C
ANISOU 1628  CB  LYS C 198     4805   4114   4319   -359    221    -67       C
ATOM   1629  CG  LYS C 198     -18.552  17.070 -56.241  1.00 46.68           C
ANISOU 1629  CG  LYS C 198     6269   5655   5812   -298    157    -64       C
ATOM   1630  CD  LYS C 198     -19.385  17.427 -57.458  1.00 42.78           C
ANISOU 1630  CD  LYS C 198     5851   5153   5250   -243    135    -57       C
ATOM   1631  CE  LYS C 198     -20.702  18.007 -57.032  1.00 50.81           C
ANISOU 1631  CE  LYS C 198     6877   6188   6241   -172     82    -55       C
ATOM   1632  NZ  LYS C 198     -20.989  17.684 -55.603  1.00 67.67           N
ANISOU 1632  NZ  LYS C 198     8923   8357   8433   -183     62    -62       N
ATOM   1633  N   SER C 199     -14.086  17.745 -54.209  1.00 49.25           N
ANISOU 1633  N   SER C 199     6515   5938   6258   -499    315   -123       N
ATOM   1634  CA  SER C 199     -12.699  18.169 -54.243  1.00 33.61           C
ANISOU 1634  CA  SER C 199     4537   3945   4289   -564    378   -158       C
ATOM   1635  C   SER C 199     -11.877  17.228 -53.384  1.00 37.94           C
ANISOU 1635  C   SER C 199     4979   4538   4898   -580    369   -195       C
ATOM   1636  O   SER C 199     -12.398  16.611 -52.450  1.00 51.36           O
ANISOU 1636  O   SER C 199     6623   6262   6628   -542    320   -185       O
ATOM   1637  CB  SER C 199     -12.544  19.608 -53.732  1.00 36.50           C
ANISOU 1637  CB  SER C 199     4962   4271   4636   -585    410   -153       C
ATOM   1638  OG  SER C 199     -12.107  19.641 -52.394  1.00 45.35           O
ANISOU 1638  OG  SER C 199     6012   5415   5805   -596    403   -173       O
ATOM   1639  N   SER C 200     -10.583  17.121 -53.705  1.00 40.19           N
ANISOU 1639  N   SER C 200     5240   4834   5196   -633    418   -244       N
ATOM   1640  CA  SER C 200      -9.680  16.272 -52.929  1.00 43.68           C
ANISOU 1640  CA  SER C 200     5585   5322   5691   -639    407   -291       C
ATOM   1641  C   SER C 200      -9.440  16.772 -51.504  1.00 45.56           C
ANISOU 1641  C   SER C 200     5784   5569   5958   -636    397   -304       C
ATOM   1642  O   SER C 200      -8.874  16.029 -50.707  1.00 58.76           O
ANISOU 1642  O   SER C 200     7380   7277   7668   -620    372   -338       O
ATOM   1643  CB  SER C 200      -8.336  16.149 -53.627  1.00 47.90           C
ANISOU 1643  CB  SER C 200     6097   5874   6229   -696    463   -353       C
ATOM   1644  OG  SER C 200      -7.696  17.418 -53.685  1.00 49.22           O
ANISOU 1644  OG  SER C 200     6306   6017   6379   -758    529   -378       O
ATOM   1645  N   ARG C 201      -9.846  17.993 -51.157  1.00 44.03           N
ANISOU 1645  N   ARG C 201     5644   5341   5745   -644    412   -280       N
ATOM   1646  CA  ARG C 201      -9.644  18.484 -49.799  1.00 45.48           C
ANISOU 1646  CA  ARG C 201     5791   5533   5956   -641    402   -292       C
ATOM   1647  C   ARG C 201     -10.611  17.863 -48.798  1.00 56.02           C
ANISOU 1647  C   ARG C 201     7092   6882   7311   -578    333   -257       C
ATOM   1648  O   ARG C 201     -10.360  17.954 -47.594  1.00 59.31           O
ANISOU 1648  O   ARG C 201     7465   7314   7757   -569    316   -272       O
ATOM   1649  CB  ARG C 201      -9.785  20.013 -49.754  1.00 48.14           C
ANISOU 1649  CB  ARG C 201     6205   5825   6263   -672    443   -277       C
ATOM   1650  CG  ARG C 201      -8.874  20.797 -50.707  1.00 42.58           C
ANISOU 1650  CG  ARG C 201     5556   5093   5528   -747    525   -313       C
ATOM   1651  CD  ARG C 201      -8.993  22.310 -50.522  1.00 49.63           C
ANISOU 1651  CD  ARG C 201     6536   5933   6387   -778    568   -300       C
ATOM   1652  NE  ARG C 201     -10.350  22.825 -50.741  1.00 56.06           N
ANISOU 1652  NE  ARG C 201     7440   6702   7158   -722    533   -230       N
ATOM   1653  CZ  ARG C 201     -10.960  22.890 -51.923  1.00 52.84           C
ANISOU 1653  CZ  ARG C 201     7118   6259   6698   -703    535   -197       C
ATOM   1654  NH1 ARG C 201     -10.350  22.466 -53.013  1.00 50.96           N
ANISOU 1654  NH1 ARG C 201     6895   6023   6446   -742    574   -220       N
ATOM   1655  NH2 ARG C 201     -12.192  23.372 -52.021  1.00 51.09           N
ANISOU 1655  NH2 ARG C 201     6969   6006   6436   -641    495   -144       N
ATOM   1656  N   PHE C 202     -11.706  17.242 -49.256  1.00 56.18           N
ANISOU 1656  N   PHE C 202     7132   6898   7315   -539    296   -215       N
ATOM   1657  CA  PHE C 202     -12.781  16.815 -48.360  1.00 55.92           C
ANISOU 1657  CA  PHE C 202     7080   6873   7293   -491    241   -183       C
ATOM   1658  C   PHE C 202     -12.399  15.558 -47.564  1.00 57.51           C
ANISOU 1658  C   PHE C 202     7215   7106   7531   -472    210   -206       C
ATOM   1659  O   PHE C 202     -12.004  14.539 -48.143  1.00 58.05           O
ANISOU 1659  O   PHE C 202     7263   7189   7604   -471    207   -224       O
ATOM   1660  CB  PHE C 202     -14.056  16.561 -49.167  1.00 57.19           C
ANISOU 1660  CB  PHE C 202     7280   7027   7422   -461    216   -146       C
ATOM   1661  CG  PHE C 202     -15.300  16.564 -48.342  1.00 54.72           C
ANISOU 1661  CG  PHE C 202     6960   6720   7109   -422    173   -119       C
ATOM   1662  CD1 PHE C 202     -15.827  17.755 -47.867  1.00 59.97           C
ANISOU 1662  CD1 PHE C 202     7660   7368   7760   -410    171   -101       C
ATOM   1663  CD2 PHE C 202     -15.924  15.375 -48.003  1.00 58.93           C
ANISOU 1663  CD2 PHE C 202     7456   7278   7657   -401    139   -117       C
ATOM   1664  CE1 PHE C 202     -16.971  17.771 -47.072  1.00 59.00           C
ANISOU 1664  CE1 PHE C 202     7523   7256   7637   -376    133    -84       C
ATOM   1665  CE2 PHE C 202     -17.078  15.379 -47.212  1.00 59.12           C
ANISOU 1665  CE2 PHE C 202     7471   7312   7681   -375    106   -101       C
ATOM   1666  CZ  PHE C 202     -17.598  16.587 -46.744  1.00 59.41           C
ANISOU 1666  CZ  PHE C 202     7532   7336   7704   -362    102    -86       C
ATOM   1667  N   LEU C 203     -12.546  15.618 -46.239  1.00 51.65           N
ANISOU 1667  N   LEU C 203     6447   6370   6809   -453    185   -204       N
ATOM   1668  CA  LEU C 203     -12.204  14.502 -45.349  1.00 56.87           C
ANISOU 1668  CA  LEU C 203     7063   7051   7495   -426    154   -223       C
ATOM   1669  C   LEU C 203     -13.497  13.895 -44.792  1.00 60.18           C
ANISOU 1669  C   LEU C 203     7494   7465   7908   -397    116   -186       C
ATOM   1670  O   LEU C 203     -14.014  14.335 -43.768  1.00 59.79           O
ANISOU 1670  O   LEU C 203     7445   7411   7863   -385    101   -171       O
ATOM   1671  CB  LEU C 203     -11.255  14.961 -44.219  1.00 58.72           C
ANISOU 1671  CB  LEU C 203     7261   7297   7752   -427    156   -259       C
ATOM   1672  CG  LEU C 203     -10.864  13.940 -43.129  1.00 52.17           C
ANISOU 1672  CG  LEU C 203     6397   6484   6940   -387    118   -281       C
ATOM   1673  CD1 LEU C 203     -10.432  12.633 -43.754  1.00 53.95           C
ANISOU 1673  CD1 LEU C 203     6613   6722   7164   -370    106   -302       C
ATOM   1674  CD2 LEU C 203      -9.756  14.469 -42.257  1.00 40.60           C
ANISOU 1674  CD2 LEU C 203     4891   5040   5495   -386    122   -331       C
ATOM   1675  N   ARG C 204     -13.991  12.848 -45.467  1.00 66.88           N
ANISOU 1675  N   ARG C 204     8350   8316   8746   -389    105   -178       N
ATOM   1676  CA  ARG C 204     -15.286  12.248 -45.141  1.00 65.92           C
ANISOU 1676  CA  ARG C 204     8240   8192   8614   -374     80   -152       C
ATOM   1677  C   ARG C 204     -15.241  11.472 -43.826  1.00 69.33           C
ANISOU 1677  C   ARG C 204     8663   8621   9058   -356     58   -158       C
ATOM   1678  O   ARG C 204     -16.197  11.502 -43.040  1.00 65.29           O
ANISOU 1678  O   ARG C 204     8160   8105   8542   -351     45   -141       O
ATOM   1679  CB  ARG C 204     -15.710  11.313 -46.276  1.00 71.31           C
ANISOU 1679  CB  ARG C 204     8933   8879   9282   -378     80   -151       C
ATOM   1680  CG  ARG C 204     -16.763  11.880 -47.203  1.00 79.34           C
ANISOU 1680  CG  ARG C 204     9971   9901  10274   -380     83   -132       C
ATOM   1681  CD  ARG C 204     -17.019  10.973 -48.396  1.00 79.47           C
ANISOU 1681  CD  ARG C 204     9993   9926  10276   -385     84   -136       C
ATOM   1682  NE  ARG C 204     -16.994   9.551 -48.047  1.00 84.63           N
ANISOU 1682  NE  ARG C 204    10636  10580  10938   -385     74   -148       N
ATOM   1683  CZ  ARG C 204     -18.060   8.840 -47.672  1.00 82.39           C
ANISOU 1683  CZ  ARG C 204    10355  10302  10648   -387     62   -146       C
ATOM   1684  NH1 ARG C 204     -19.261   9.408 -47.578  1.00 77.80           N
ANISOU 1684  NH1 ARG C 204     9771   9736  10053   -385     54   -138       N
ATOM   1685  NH2 ARG C 204     -17.924   7.551 -47.390  1.00 78.57           N
ANISOU 1685  NH2 ARG C 204     9879   9808  10166   -390     60   -156       N
ATOM   1686  N   SER C 205     -14.152  10.747 -43.590  1.00 64.73           N
ANISOU 1686  N   SER C 205     8069   8040   8487   -342     53   -186       N
ATOM   1687  CA  SER C 205     -14.016   9.850 -42.455  1.00 56.87           C
ANISOU 1687  CA  SER C 205     7083   7034   7492   -314     29   -194       C
ATOM   1688  C   SER C 205     -12.524   9.620 -42.219  1.00 57.43           C
ANISOU 1688  C   SER C 205     7130   7116   7575   -289     21   -238       C
ATOM   1689  O   SER C 205     -11.698   9.953 -43.082  1.00 65.08           O
ANISOU 1689  O   SER C 205     8072   8104   8553   -303     39   -264       O
ATOM   1690  CB  SER C 205     -14.777   8.528 -42.700  1.00 59.87           C
ANISOU 1690  CB  SER C 205     7496   7398   7853   -314     22   -183       C
ATOM   1691  OG  SER C 205     -13.968   7.507 -43.269  1.00 66.80           O
ANISOU 1691  OG  SER C 205     8379   8275   8728   -298     17   -207       O
ATOM   1692  N   PRO C 206     -12.132   9.098 -41.043  1.00 49.05           N
ANISOU 1692  N   PRO C 206     6077   6046   6511   -250     -6   -253       N
ATOM   1693  CA  PRO C 206     -12.859   8.604 -39.857  1.00 48.44           C
ANISOU 1693  CA  PRO C 206     6042   5943   6419   -231    -25   -231       C
ATOM   1694  C   PRO C 206     -13.631   9.677 -39.111  1.00 52.08           C
ANISOU 1694  C   PRO C 206     6499   6403   6888   -250    -19   -205       C
ATOM   1695  O   PRO C 206     -13.177  10.809 -39.009  1.00 55.98           O
ANISOU 1695  O   PRO C 206     6957   6914   7398   -258    -11   -215       O
ATOM   1696  CB  PRO C 206     -11.748   8.053 -38.955  1.00 43.79           C
ANISOU 1696  CB  PRO C 206     5458   5354   5827   -175    -56   -269       C
ATOM   1697  CG  PRO C 206     -10.456   8.101 -39.810  1.00 43.28           C
ANISOU 1697  CG  PRO C 206     5343   5324   5777   -165    -53   -319       C
ATOM   1698  CD  PRO C 206     -10.677   9.152 -40.820  1.00 42.14           C
ANISOU 1698  CD  PRO C 206     5165   5197   5649   -221    -16   -307       C
ATOM   1699  N   LEU C 207     -14.795   9.295 -38.593  1.00 54.52           N
ANISOU 1699  N   LEU C 207     6845   6692   7180   -261    -20   -177       N
ATOM   1700  CA  LEU C 207     -15.580  10.186 -37.746  1.00 52.55           C
ANISOU 1700  CA  LEU C 207     6592   6442   6934   -274    -18   -157       C
ATOM   1701  C   LEU C 207     -14.896  10.464 -36.406  1.00 48.87           C
ANISOU 1701  C   LEU C 207     6126   5970   6472   -241    -37   -170       C
ATOM   1702  O   LEU C 207     -14.983  11.579 -35.879  1.00 49.99           O
ANISOU 1702  O   LEU C 207     6244   6123   6627   -247    -35   -165       O
ATOM   1703  CB  LEU C 207     -16.964   9.579 -37.522  1.00 50.46           C
ANISOU 1703  CB  LEU C 207     6362   6163   6649   -298    -10   -136       C
ATOM   1704  CG  LEU C 207     -18.037  10.176 -38.435  1.00 52.24           C
ANISOU 1704  CG  LEU C 207     6565   6410   6875   -331      6   -123       C
ATOM   1705  CD1 LEU C 207     -17.664   9.942 -39.874  1.00 57.27           C
ANISOU 1705  CD1 LEU C 207     7189   7057   7513   -336     13   -130       C
ATOM   1706  CD2 LEU C 207     -19.375   9.584 -38.135  1.00 48.28           C
ANISOU 1706  CD2 LEU C 207     6085   5905   6355   -358     16   -120       C
ATOM   1707  N   PHE C 208     -14.210   9.475 -35.848  1.00 42.64           N
ANISOU 1707  N   PHE C 208     5368   5165   5669   -200    -58   -189       N
ATOM   1708  CA  PHE C 208     -13.727   9.498 -34.480  1.00 47.41           C
ANISOU 1708  CA  PHE C 208     5989   5759   6266   -159    -83   -202       C
ATOM   1709  C   PHE C 208     -12.264   9.080 -34.459  1.00 56.96           C
ANISOU 1709  C   PHE C 208     7185   6983   7477   -105   -109   -250       C
ATOM   1710  O   PHE C 208     -11.688   8.733 -35.492  1.00 56.20           O
ANISOU 1710  O   PHE C 208     7066   6903   7387   -104   -106   -271       O
ATOM   1711  CB  PHE C 208     -14.557   8.562 -33.592  1.00 51.31           C
ANISOU 1711  CB  PHE C 208     6561   6209   6725   -155    -86   -181       C
ATOM   1712  CG  PHE C 208     -15.966   9.020 -33.382  1.00 50.87           C
ANISOU 1712  CG  PHE C 208     6510   6150   6668   -206    -61   -150       C
ATOM   1713  CD1 PHE C 208     -16.235  10.191 -32.681  1.00 47.27           C
ANISOU 1713  CD1 PHE C 208     6023   5710   6229   -215    -60   -142       C
ATOM   1714  CD2 PHE C 208     -17.029   8.281 -33.881  1.00 47.72           C
ANISOU 1714  CD2 PHE C 208     6143   5736   6251   -247    -37   -135       C
ATOM   1715  CE1 PHE C 208     -17.545  10.619 -32.478  1.00 44.97           C
ANISOU 1715  CE1 PHE C 208     5730   5421   5934   -256    -40   -121       C
ATOM   1716  CE2 PHE C 208     -18.340   8.712 -33.688  1.00 49.94           C
ANISOU 1716  CE2 PHE C 208     6418   6025   6531   -293    -15   -120       C
ATOM   1717  CZ  PHE C 208     -18.597   9.882 -32.981  1.00 41.21           C
ANISOU 1717  CZ  PHE C 208     5280   4938   5442   -295    -19   -113       C
ATOM   1718  N   LEU C 209     -11.658   9.095 -33.270  1.00 55.96           N
ANISOU 1718  N   LEU C 209     7068   6854   7341    -54   -139   -272       N
ATOM   1719  CA  LEU C 209     -10.250   8.747 -33.194  1.00 58.15           C
ANISOU 1719  CA  LEU C 209     7322   7156   7617      8   -171   -331       C
ATOM   1720  C   LEU C 209     -10.080   7.230 -33.191  1.00 66.16           C
ANISOU 1720  C   LEU C 209     8410   8135   8591     60   -196   -338       C
ATOM   1721  O   LEU C 209     -11.039   6.468 -33.048  1.00 67.73           O
ANISOU 1721  O   LEU C 209     8687   8285   8761     44   -186   -297       O
ATOM   1722  CB  LEU C 209      -9.594   9.356 -31.958  1.00 60.75           C
ANISOU 1722  CB  LEU C 209     7629   7503   7948     52   -198   -363       C
ATOM   1723  CG  LEU C 209      -9.445  10.870 -31.875  1.00 63.42           C
ANISOU 1723  CG  LEU C 209     7894   7879   8325     10   -177   -372       C
ATOM   1724  CD1 LEU C 209      -9.375  11.221 -30.406  1.00 67.71           C
ANISOU 1724  CD1 LEU C 209     8450   8417   8859     48   -203   -379       C
ATOM   1725  CD2 LEU C 209      -8.226  11.382 -32.618  1.00 71.58           C
ANISOU 1725  CD2 LEU C 209     8845   8967   9386      5   -168   -436       C
ATOM   1726  N   LYS C 210      -8.820   6.797 -33.315  1.00 71.52           N
ANISOU 1726  N   LYS C 210     9067   8842   9267    123   -229   -398       N
ATOM   1727  CA  LYS C 210      -8.522   5.414 -33.681  1.00 70.65           C
ANISOU 1727  CA  LYS C 210     9017   8705   9122    172   -251   -411       C
ATOM   1728  C   LYS C 210      -9.021   4.403 -32.656  1.00 64.29           C
ANISOU 1728  C   LYS C 210     8335   7833   8261    218   -273   -385       C
ATOM   1729  O   LYS C 210      -9.245   3.239 -33.009  1.00 63.22           O
ANISOU 1729  O   LYS C 210     8277   7653   8091    233   -274   -373       O
ATOM   1730  CB  LYS C 210      -7.017   5.242 -33.894  1.00 69.54           C
ANISOU 1730  CB  LYS C 210     8820   8616   8986    242   -288   -493       C
ATOM   1731  CG  LYS C 210      -6.571   5.340 -35.348  1.00 73.67           C
ANISOU 1731  CG  LYS C 210     9272   9180   9539    202   -262   -518       C
ATOM   1732  CD  LYS C 210      -5.054   5.408 -35.453  1.00 77.77           C
ANISOU 1732  CD  LYS C 210     9714   9767  10069    261   -292   -614       C
ATOM   1733  CE  LYS C 210      -4.626   5.826 -36.848  1.00 85.80           C
ANISOU 1733  CE  LYS C 210    10649  10830  11122    200   -253   -642       C
ATOM   1734  NZ  LYS C 210      -3.891   7.135 -36.872  1.00 89.26           N
ANISOU 1734  NZ  LYS C 210    10983  11332  11598    161   -229   -695       N
ATOM   1735  N   MET C 211      -9.213   4.828 -31.413  1.00 63.05           N
ANISOU 1735  N   MET C 211     8203   7661   8092    237   -286   -376       N
ATOM   1736  CA  MET C 211      -9.631   4.000 -30.287  1.00 57.80           C
ANISOU 1736  CA  MET C 211     7664   6929   7369    281   -303   -354       C
ATOM   1737  C   MET C 211     -11.145   3.854 -30.167  1.00 57.86           C
ANISOU 1737  C   MET C 211     7737   6885   7363    198   -254   -288       C
ATOM   1738  O   MET C 211     -11.611   3.170 -29.250  1.00 59.66           O
ANISOU 1738  O   MET C 211     8079   7050   7540    217   -255   -268       O
ATOM   1739  CB  MET C 211      -9.126   4.627 -28.988  1.00 55.87           C
ANISOU 1739  CB  MET C 211     7410   6699   7118    337   -339   -378       C
ATOM   1740  CG  MET C 211      -9.936   5.872 -28.744  1.00 60.36           C
ANISOU 1740  CG  MET C 211     7921   7286   7727    256   -301   -343       C
ATOM   1741  SD  MET C 211      -8.988   7.287 -28.265  1.00 77.73           S
ANISOU 1741  SD  MET C 211    10002   9560   9971    277   -322   -393       S
ATOM   1742  CE  MET C 211      -7.876   7.425 -29.641  1.00 78.69           C
ANISOU 1742  CE  MET C 211    10019   9748  10131    277   -322   -452       C
ATOM   1743  N   ALA C 212     -11.931   4.526 -31.005  1.00 52.68           N
ANISOU 1743  N   ALA C 212     7013   6253   6749    109   -210   -261       N
ATOM   1744  CA  ALA C 212     -13.378   4.408 -30.867  1.00 62.08           C
ANISOU 1744  CA  ALA C 212     8253   7408   7928     33   -165   -213       C
ATOM   1745  C   ALA C 212     -13.843   3.013 -31.288  1.00 59.38           C
ANISOU 1745  C   ALA C 212     8008   7010   7542     20   -147   -202       C
ATOM   1746  O   ALA C 212     -13.160   2.297 -32.025  1.00 57.70           O
ANISOU 1746  O   ALA C 212     7805   6797   7322     57   -163   -223       O
ATOM   1747  CB  ALA C 212     -14.095   5.483 -31.686  1.00 56.81           C
ANISOU 1747  CB  ALA C 212     7490   6787   7310    -46   -130   -194       C
ATOM   1748  N   MET C 213     -15.007   2.614 -30.773  1.00 58.34           N
ANISOU 1748  N   MET C 213     7955   6832   7379    -33   -110   -173       N
ATOM   1749  CA  MET C 213     -15.589   1.319 -31.107  1.00 65.08           C
ANISOU 1749  CA  MET C 213     8910   7628   8188    -63    -80   -164       C
ATOM   1750  C   MET C 213     -16.441   1.372 -32.362  1.00 65.32           C
ANISOU 1750  C   MET C 213     8880   7689   8249   -146    -39   -156       C
ATOM   1751  O   MET C 213     -16.917   0.326 -32.817  1.00 67.88           O
ANISOU 1751  O   MET C 213     9273   7975   8543   -179    -10   -154       O
ATOM   1752  CB  MET C 213     -16.435   0.782 -29.945  1.00 75.66           C
ANISOU 1752  CB  MET C 213    10372   8900   9473    -91    -50   -147       C
ATOM   1753  CG  MET C 213     -15.736   0.781 -28.579  1.00 77.72           C
ANISOU 1753  CG  MET C 213    10707   9128   9697     -8    -90   -153       C
ATOM   1754  SD  MET C 213     -14.480  -0.499 -28.402  1.00 78.66           S
ANISOU 1754  SD  MET C 213    10947   9189   9753    112   -142   -177       S
ATOM   1755  CE  MET C 213     -15.314  -1.913 -29.118  1.00 83.51           C
ANISOU 1755  CE  MET C 213    11677   9733  10321     46    -87   -163       C
ATOM   1756  N   TRP C 214     -16.640   2.564 -32.919  1.00 64.74           N
ANISOU 1756  N   TRP C 214     8686   7681   8231   -178    -35   -153       N
ATOM   1757  CA  TRP C 214     -17.305   2.745 -34.196  1.00 62.49           C
ANISOU 1757  CA  TRP C 214     8335   7433   7974   -239     -7   -149       C
ATOM   1758  C   TRP C 214     -16.733   4.002 -34.829  1.00 59.64           C
ANISOU 1758  C   TRP C 214     7859   7135   7665   -225    -27   -154       C
ATOM   1759  O   TRP C 214     -16.316   4.918 -34.120  1.00 68.53           O
ANISOU 1759  O   TRP C 214     8950   8280   8809   -199    -46   -155       O
ATOM   1760  CB  TRP C 214     -18.822   2.850 -34.014  1.00 58.50           C
ANISOU 1760  CB  TRP C 214     7835   6928   7462   -320     38   -139       C
ATOM   1761  CG  TRP C 214     -19.582   2.974 -35.300  1.00 60.83           C
ANISOU 1761  CG  TRP C 214     8067   7265   7779   -375     62   -144       C
ATOM   1762  CD1 TRP C 214     -20.094   1.951 -36.053  1.00 50.07           C
ANISOU 1762  CD1 TRP C 214     6741   5887   6397   -415     90   -153       C
ATOM   1763  CD2 TRP C 214     -19.931   4.193 -35.984  1.00 60.88           C
ANISOU 1763  CD2 TRP C 214     7971   7334   7828   -392     59   -141       C
ATOM   1764  NE1 TRP C 214     -20.739   2.461 -37.156  1.00 44.54           N
ANISOU 1764  NE1 TRP C 214     5957   5240   5724   -452    101   -160       N
ATOM   1765  CE2 TRP C 214     -20.652   3.829 -37.142  1.00 50.23           C
ANISOU 1765  CE2 TRP C 214     6597   6007   6480   -436     81   -151       C
ATOM   1766  CE3 TRP C 214     -19.697   5.554 -35.733  1.00 64.30           C
ANISOU 1766  CE3 TRP C 214     8336   7803   8292   -372     40   -134       C
ATOM   1767  CZ2 TRP C 214     -21.153   4.778 -38.044  1.00 49.03           C
ANISOU 1767  CZ2 TRP C 214     6362   5912   6356   -452     80   -153       C
ATOM   1768  CZ3 TRP C 214     -20.195   6.496 -36.636  1.00 60.31           C
ANISOU 1768  CZ3 TRP C 214     7755   7347   7814   -392     43   -133       C
ATOM   1769  CH2 TRP C 214     -20.915   6.098 -37.773  1.00 54.87           C
ANISOU 1769  CH2 TRP C 214     7049   6678   7120   -427     61   -142       C
ATOM   1770  N   GLY C 215     -16.695   4.037 -36.161  1.00 46.20           N
ANISOU 1770  N   GLY C 215     6105   5463   5984   -245    -19   -158       N
ATOM   1771  CA  GLY C 215     -16.290   5.263 -36.828  1.00 32.51           C
ANISOU 1771  CA  GLY C 215     4278   3782   4293   -245    -26   -161       C
ATOM   1772  C   GLY C 215     -14.812   5.581 -36.738  1.00 49.87           C
ANISOU 1772  C   GLY C 215     6445   5997   6506   -187    -57   -186       C
ATOM   1773  O   GLY C 215     -14.426   6.736 -36.917  1.00 56.93           O
ANISOU 1773  O   GLY C 215     7272   6928   7431   -190    -58   -192       O
ATOM   1774  N   ASN C 216     -13.972   4.591 -36.450  1.00 48.64           N
ANISOU 1774  N   ASN C 216     6338   5816   6327   -133    -81   -208       N
ATOM   1775  CA  ASN C 216     -12.526   4.709 -36.544  1.00 59.29           C
ANISOU 1775  CA  ASN C 216     7648   7191   7688    -74   -112   -248       C
ATOM   1776  C   ASN C 216     -12.040   4.154 -37.882  1.00 78.95           C
ANISOU 1776  C   ASN C 216    10116   9696  10183    -76   -108   -267       C
ATOM   1777  O   ASN C 216     -12.629   3.219 -38.434  1.00 83.51           O
ANISOU 1777  O   ASN C 216    10743  10247  10742    -96    -94   -252       O
ATOM   1778  CB  ASN C 216     -11.876   3.939 -35.404  1.00 60.91           C
ANISOU 1778  CB  ASN C 216     7922   7364   7857      1   -150   -269       C
ATOM   1779  CG  ASN C 216     -12.156   2.437 -35.489  1.00 61.04           C
ANISOU 1779  CG  ASN C 216     8042   7323   7826     18   -150   -262       C
ATOM   1780  OD1 ASN C 216     -13.317   2.009 -35.498  1.00 52.54           O
ANISOU 1780  OD1 ASN C 216     7021   6211   6732    -37   -117   -228       O
ATOM   1781  ND2 ASN C 216     -11.091   1.634 -35.577  1.00 63.59           N
ANISOU 1781  ND2 ASN C 216     8392   7642   8129     93   -187   -300       N
ATOM   1782  N   LYS C 217     -10.963   4.733 -38.414  1.00 94.03           N
ANISOU 1782  N   LYS C 217    11954  11654  12122    -59   -116   -305       N
ATOM   1783  CA  LYS C 217     -10.358   4.160 -39.632  1.00102.53           C
ANISOU 1783  CA  LYS C 217    13010  12747  13202    -55   -113   -331       C
ATOM   1784  C   LYS C 217      -8.823   4.181 -39.623  1.00105.38           C
ANISOU 1784  C   LYS C 217    13321  13148  13572      3   -142   -398       C
ATOM   1785  O   LYS C 217      -8.168   4.843 -38.813  1.00103.61           O
ANISOU 1785  O   LYS C 217    13060  12949  13357     32   -159   -429       O
ATOM   1786  CB  LYS C 217     -10.853   4.862 -40.918  1.00 96.89           C
ANISOU 1786  CB  LYS C 217    12245  12056  12511   -124    -74   -311       C
ATOM   1787  CG  LYS C 217     -12.322   5.259 -40.966  1.00 87.81           C
ANISOU 1787  CG  LYS C 217    11115  10890  11360   -180    -48   -259       C
ATOM   1788  CD  LYS C 217     -13.200   4.118 -41.405  1.00 85.47           C
ANISOU 1788  CD  LYS C 217    10874  10561  11038   -199    -38   -238       C
ATOM   1789  CE  LYS C 217     -14.622   4.287 -40.884  1.00 79.99           C
ANISOU 1789  CE  LYS C 217    10208   9849  10334   -240    -21   -203       C
ATOM   1790  NZ  LYS C 217     -15.579   3.311 -41.511  1.00 68.48           N
ANISOU 1790  NZ  LYS C 217     8791   8372   8855   -275     -1   -192       N
ATOM   1791  OXT LYS C 217      -8.203   3.506 -40.453  1.00105.18           O
ANISOU 1791  OXT LYS C 217    13286  13135  13542     22   -147   -429       O
TER
HETATM 1792  CB1 GSH C 701     -13.046  19.812 -27.033  1.00 71.44           C
ANISOU 1792  CB1 GSH C 701     8806   8898   9440   -184    -81   -239       C
HETATM 1793  CB2 GSH C 701      -9.737  15.664 -29.756  1.00 86.88           C
ANISOU 1793  CB2 GSH C 701    10734  10904  11374    -89   -125   -371       C
HETATM 1794  CG1 GSH C 701     -11.651  19.523 -27.551  1.00 73.56           C
ANISOU 1794  CG1 GSH C 701     9038   9194   9719   -173    -82   -294       C
HETATM 1795  SG2 GSH C 701     -11.428  15.327 -30.245  1.00 93.92           S
ANISOU 1795  SG2 GSH C 701    11686  11748  12249   -127   -107   -289       S
HETATM 1796  CD1 GSH C 701     -11.132  18.103 -27.603  1.00 75.22           C
ANISOU 1796  CD1 GSH C 701     9261   9407   9913   -128   -111   -315       C
HETATM 1797  OE1 GSH C 701     -11.686  17.211 -26.968  1.00 70.93           O
ANISOU 1797  OE1 GSH C 701     8766   8840   9346    -96   -135   -290       O
HETATM 1798  C1  GSH C 701     -13.732  21.984 -28.320  1.00 63.64           C
ANISOU 1798  C1  GSH C 701     7812   7901   8468   -260    -22   -210       C
HETATM 1799  C2  GSH C 701      -7.904  16.572 -28.243  1.00 72.97           C
ANISOU 1799  C2  GSH C 701     8887   9207   9630    -36   -157   -482       C
HETATM 1800  C3  GSH C 701      -5.104  17.104 -26.240  1.00 84.11           C
ANISOU 1800  C3  GSH C 701    10167  10738  11053     78   -227   -682       C
HETATM 1801  CA1 GSH C 701     -13.540  21.258 -26.980  1.00 67.80           C
ANISOU 1801  CA1 GSH C 701     8337   8434   8991   -218    -57   -222       C
HETATM 1802  CA2 GSH C 701      -9.385  16.488 -28.552  1.00 75.43           C
ANISOU 1802  CA2 GSH C 701     9259   9468   9931    -73   -138   -395       C
HETATM 1803  CA3 GSH C 701      -6.028  17.894 -27.140  1.00 83.70           C
ANISOU 1803  CA3 GSH C 701    10131  10653  11020    -17   -166   -615       C
HETATM 1804  N1  GSH C 701     -14.649  21.434 -26.039  1.00 66.05           N
ANISOU 1804  N1  GSH C 701     8140   8197   8758   -211    -69   -187       N
HETATM 1805  N2  GSH C 701     -10.045  17.799 -28.502  1.00 72.75           N
ANISOU 1805  N2  GSH C 701     8911   9122   9610   -127   -105   -364       N
HETATM 1806  N3  GSH C 701      -7.432  17.575 -27.288  1.00 79.89           N
ANISOU 1806  N3  GSH C 701     9723  10110  10522    -34   -159   -519       N
HETATM 1807  O11 GSH C 701     -14.948  21.832 -28.964  1.00 58.34           O
ANISOU 1807  O11 GSH C 701     7172   7214   7782   -270    -18   -166       O
HETATM 1808  O12 GSH C 701     -12.672  21.946 -29.205  1.00 67.49           O
ANISOU 1808  O12 GSH C 701     8277   8401   8963   -278     -2   -246       O
HETATM 1809  O2  GSH C 701      -7.143  15.683 -28.575  1.00 62.65           O
ANISOU 1809  O2  GSH C 701     7571   7919   8314      5   -179   -524       O
HETATM 1810  O31 GSH C 701      -4.123  17.899 -25.670  1.00 69.82           O
ANISOU 1810  O31 GSH C 701     8282   8986   9261     83   -229   -765       O
HETATM 1811  O32 GSH C 701      -4.602  15.941 -26.842  1.00 90.61           O
ANISOU 1811  O32 GSH C 701    10997  11572  11860    124   -252   -711       O
TER
ATOM   1812  N   PRO A   1     -42.307  38.695 -13.805  1.00 87.33           N
ANISOU 1812  N   PRO A   1    10267  11754  11162    359   -426   -869       N
ATOM   1813  CA  PRO A   1     -40.999  38.206 -13.355  1.00 83.51           C
ANISOU 1813  CA  PRO A   1     9845  11173  10710    273   -376   -768       C
ATOM   1814  C   PRO A   1     -40.500  37.018 -14.181  1.00 70.72           C
ANISOU 1814  C   PRO A   1     8238   9532   9101    214   -346   -736       C
ATOM   1815  O   PRO A   1     -41.299  36.131 -14.474  1.00 65.67           O
ANISOU 1815  O   PRO A   1     7530   8966   8455    178   -331   -804       O
ATOM   1816  CB  PRO A   1     -41.274  37.783 -11.911  1.00 80.62           C
ANISOU 1816  CB  PRO A   1     9432  10837  10364    190   -329   -795       C
ATOM   1817  CG  PRO A   1     -42.721  37.303 -11.953  1.00 78.92           C
ANISOU 1817  CG  PRO A   1     9111  10743  10132    180   -328   -915       C
ATOM   1818  CD  PRO A   1     -43.418  38.113 -13.024  1.00 82.21           C
ANISOU 1818  CD  PRO A   1     9512  11209  10515    304   -399   -969       C
ATOM   1819  N   MET A   2     -39.216  36.990 -14.541  1.00 65.73           N
ANISOU 1819  N   MET A   2     7686   8805   8484    200   -335   -643       N
ATOM   1820  CA  MET A   2     -38.672  35.809 -15.197  1.00 59.70           C
ANISOU 1820  CA  MET A   2     6934   8018   7731    139   -303   -611       C
ATOM   1821  C   MET A   2     -38.691  34.613 -14.248  1.00 64.76           C
ANISOU 1821  C   MET A   2     7542   8673   8392     31   -244   -620       C
ATOM   1822  O   MET A   2     -38.607  34.754 -13.024  1.00 71.85           O
ANISOU 1822  O   MET A   2     8438   9561   9300     -4   -223   -615       O
ATOM   1823  CB  MET A   2     -37.240  36.037 -15.673  1.00 53.13           C
ANISOU 1823  CB  MET A   2     6190   7085   6912    142   -300   -516       C
ATOM   1824  CG  MET A   2     -36.824  37.461 -15.872  1.00 62.16           C
ANISOU 1824  CG  MET A   2     7398   8178   8043    221   -335   -483       C
ATOM   1825  SD  MET A   2     -35.043  37.517 -16.159  1.00 72.53           S
ANISOU 1825  SD  MET A   2     8801   9379   9378    188   -309   -384       S
ATOM   1826  CE  MET A   2     -34.790  39.288 -16.188  1.00 72.16           C
ANISOU 1826  CE  MET A   2     8829   9278   9308    270   -341   -363       C
ATOM   1827  N   ILE A   3     -38.791  33.424 -14.830  1.00 54.48           N
ANISOU 1827  N   ILE A   3     6224   7388   7090    -23   -217   -633       N
ATOM   1828  CA  ILE A   3     -38.807  32.166 -14.095  1.00 49.58           C
ANISOU 1828  CA  ILE A   3     5591   6770   6477   -127   -157   -641       C
ATOM   1829  C   ILE A   3     -37.534  31.416 -14.436  1.00 50.30           C
ANISOU 1829  C   ILE A   3     5750   6779   6583   -163   -136   -560       C
ATOM   1830  O   ILE A   3     -37.262  31.144 -15.612  1.00 59.95           O
ANISOU 1830  O   ILE A   3     6985   7990   7803   -143   -149   -543       O
ATOM   1831  CB  ILE A   3     -40.040  31.321 -14.449  1.00 52.14           C
ANISOU 1831  CB  ILE A   3     5840   7184   6784   -168   -136   -736       C
ATOM   1832  CG1 ILE A   3     -41.311  31.963 -13.913  1.00 54.79           C
ANISOU 1832  CG1 ILE A   3     6098   7612   7106   -143   -150   -832       C
ATOM   1833  CG2 ILE A   3     -39.903  29.938 -13.887  1.00 56.21           C
ANISOU 1833  CG2 ILE A   3     6373   7683   7303   -281    -67   -734       C
ATOM   1834  CD1 ILE A   3     -41.986  32.825 -14.915  1.00 67.15           C
ANISOU 1834  CD1 ILE A   3     7624   9236   8653    -37   -215   -883       C
ATOM   1835  N   LEU A   4     -36.753  31.078 -13.421  1.00 49.15           N
ANISOU 1835  N   LEU A   4     5648   6578   6450   -212   -105   -513       N
ATOM   1836  CA  LEU A   4     -35.627  30.167 -13.581  1.00 47.97           C
ANISOU 1836  CA  LEU A   4     5556   6360   6309   -251    -81   -451       C
ATOM   1837  C   LEU A   4     -36.004  28.830 -12.958  1.00 40.49           C
ANISOU 1837  C   LEU A   4     4614   5422   5350   -340    -26   -477       C
ATOM   1838  O   LEU A   4     -36.248  28.753 -11.755  1.00 55.67           O
ANISOU 1838  O   LEU A   4     6542   7345   7264   -377      1   -492       O
ATOM   1839  CB  LEU A   4     -34.365  30.719 -12.924  1.00 49.68           C
ANISOU 1839  CB  LEU A   4     5828   6505   6543   -233    -90   -382       C
ATOM   1840  CG  LEU A   4     -33.252  29.675 -12.760  1.00 50.25           C
ANISOU 1840  CG  LEU A   4     5956   6516   6621   -274    -65   -333       C
ATOM   1841  CD1 LEU A   4     -32.650  29.309 -14.105  1.00 48.48           C
ANISOU 1841  CD1 LEU A   4     5747   6271   6403   -259    -76   -306       C
ATOM   1842  CD2 LEU A   4     -32.175  30.165 -11.810  1.00 49.75           C
ANISOU 1842  CD2 LEU A   4     5932   6401   6571   -261    -71   -287       C
ATOM   1843  N   GLY A   5     -36.033  27.777 -13.762  1.00 40.02           N
ANISOU 1843  N   GLY A   5     4561   5363   5283   -375     -6   -483       N
ATOM   1844  CA  GLY A   5     -36.389  26.449 -13.289  1.00 55.68           C
ANISOU 1844  CA  GLY A   5     6563   7345   7247   -464     53   -510       C
ATOM   1845  C   GLY A   5     -35.184  25.526 -13.257  1.00 52.20           C
ANISOU 1845  C   GLY A   5     6206   6823   6806   -487     70   -442       C
ATOM   1846  O   GLY A   5     -34.495  25.350 -14.261  1.00 43.41           O
ANISOU 1846  O   GLY A   5     5107   5683   5703   -458     49   -406       O
ATOM   1847  N   TYR A   6     -34.961  24.913 -12.099  1.00 49.74           N
ANISOU 1847  N   TYR A   6     5952   6471   6477   -536    108   -431       N
ATOM   1848  CA  TYR A   6     -33.831  24.012 -11.938  1.00 47.20           C
ANISOU 1848  CA  TYR A   6     5717   6072   6147   -547    119   -374       C
ATOM   1849  C   TYR A   6     -34.113  23.093 -10.759  1.00 45.03           C
ANISOU 1849  C   TYR A   6     5508   5768   5835   -618    175   -389       C
ATOM   1850  O   TYR A   6     -35.019  23.343  -9.964  1.00 54.48           O
ANISOU 1850  O   TYR A   6     6680   7000   7018   -656    203   -435       O
ATOM   1851  CB  TYR A   6     -32.530  24.800 -11.744  1.00 39.38           C
ANISOU 1851  CB  TYR A   6     4750   5035   5180   -478     73   -311       C
ATOM   1852  CG  TYR A   6     -31.277  23.963 -11.864  1.00 46.25           C
ANISOU 1852  CG  TYR A   6     5692   5837   6044   -470     71   -261       C
ATOM   1853  CD1 TYR A   6     -30.982  23.286 -13.034  1.00 43.45           C
ANISOU 1853  CD1 TYR A   6     5342   5474   5692   -471     69   -251       C
ATOM   1854  CD2 TYR A   6     -30.394  23.839 -10.791  1.00 51.43           C
ANISOU 1854  CD2 TYR A   6     6410   6441   6690   -456     67   -229       C
ATOM   1855  CE1 TYR A   6     -29.827  22.523 -13.149  1.00 44.11           C
ANISOU 1855  CE1 TYR A   6     5489   5500   5770   -457     63   -212       C
ATOM   1856  CE2 TYR A   6     -29.246  23.074 -10.892  1.00 48.01           C
ANISOU 1856  CE2 TYR A   6     6041   5953   6248   -436     58   -193       C
ATOM   1857  CZ  TYR A   6     -28.967  22.422 -12.075  1.00 50.72           C
ANISOU 1857  CZ  TYR A   6     6385   6290   6596   -437     56   -185       C
ATOM   1858  OH  TYR A   6     -27.829  21.665 -12.187  1.00 53.96           O
ANISOU 1858  OH  TYR A   6     6854   6650   6996   -412     44   -156       O
ATOM   1859  N   TRP A   7     -33.332  22.016 -10.664  1.00 46.65           N
ANISOU 1859  N   TRP A   7     5802   5904   6017   -636    194   -352       N
ATOM   1860  CA  TRP A   7     -33.318  21.186  -9.463  1.00 51.52           C
ANISOU 1860  CA  TRP A   7     6515   6470   6590   -687    241   -350       C
ATOM   1861  C   TRP A   7     -32.994  22.029  -8.229  1.00 54.48           C
ANISOU 1861  C   TRP A   7     6901   6831   6967   -654    221   -332       C
ATOM   1862  O   TRP A   7     -32.538  23.170  -8.321  1.00 60.77           O
ANISOU 1862  O   TRP A   7     7643   7646   7800   -588    170   -311       O
ATOM   1863  CB  TRP A   7     -32.285  20.056  -9.596  1.00 44.19           C
ANISOU 1863  CB  TRP A   7     5690   5462   5636   -680    244   -304       C
ATOM   1864  CG  TRP A   7     -32.524  19.125 -10.768  1.00 42.18           C
ANISOU 1864  CG  TRP A   7     5437   5212   5377   -714    266   -318       C
ATOM   1865  CD1 TRP A   7     -31.789  19.046 -11.921  1.00 46.54           C
ANISOU 1865  CD1 TRP A   7     5970   5758   5954   -668    228   -288       C
ATOM   1866  CD2 TRP A   7     -33.562  18.141 -10.891  1.00 49.15           C
ANISOU 1866  CD2 TRP A   7     6342   6107   6226   -808    334   -370       C
ATOM   1867  NE1 TRP A   7     -32.307  18.088 -12.751  1.00 47.61           N
ANISOU 1867  NE1 TRP A   7     6113   5902   6076   -721    263   -315       N
ATOM   1868  CE2 TRP A   7     -33.399  17.519 -12.148  1.00 49.63           C
ANISOU 1868  CE2 TRP A   7     6393   6169   6295   -809    330   -367       C
ATOM   1869  CE3 TRP A   7     -34.621  17.734 -10.067  1.00 45.29           C
ANISOU 1869  CE3 TRP A   7     5880   5630   5700   -898    404   -425       C
ATOM   1870  CZ2 TRP A   7     -34.244  16.509 -12.593  1.00 47.00           C
ANISOU 1870  CZ2 TRP A   7     6074   5848   5935   -894    390   -417       C
ATOM   1871  CZ3 TRP A   7     -35.463  16.746 -10.513  1.00 45.24           C
ANISOU 1871  CZ3 TRP A   7     5887   5637   5666   -988    468   -478       C
ATOM   1872  CH2 TRP A   7     -35.269  16.138 -11.768  1.00 50.93           C
ANISOU 1872  CH2 TRP A   7     6597   6359   6397   -984    460   -473       C
ATOM   1873  N   ASP A   8     -33.236  21.453  -7.055  1.00 57.65           N
ANISOU 1873  N   ASP A   8     7382   7198   7325   -703    267   -341       N
ATOM   1874  CA  ASP A   8     -32.877  22.110  -5.795  1.00 57.73           C
ANISOU 1874  CA  ASP A   8     7418   7188   7329   -673    252   -323       C
ATOM   1875  C   ASP A   8     -31.426  21.872  -5.389  1.00 59.01           C
ANISOU 1875  C   ASP A   8     7664   7277   7482   -608    214   -262       C
ATOM   1876  O   ASP A   8     -31.145  21.661  -4.214  1.00 68.09           O
ANISOU 1876  O   ASP A   8     8894   8381   8595   -607    225   -250       O
ATOM   1877  CB  ASP A   8     -33.823  21.662  -4.683  1.00 65.82           C
ANISOU 1877  CB  ASP A   8     8493   8209   8307   -755    319   -365       C
ATOM   1878  CG  ASP A   8     -33.979  20.134  -4.605  1.00 81.56           C
ANISOU 1878  CG  ASP A   8    10602  10144  10241   -828    384   -372       C
ATOM   1879  OD1 ASP A   8     -33.262  19.390  -5.320  1.00 83.17           O
ANISOU 1879  OD1 ASP A   8    10855  10305  10440   -806    371   -339       O
ATOM   1880  OD2 ASP A   8     -34.833  19.673  -3.812  1.00 86.82           O
ANISOU 1880  OD2 ASP A   8    11317  10807  10864   -912    454   -414       O
ATOM   1881  N   ILE A   9     -30.484  21.895  -6.331  1.00 60.33           N
ANISOU 1881  N   ILE A   9     7813   7433   7677   -552    169   -229       N
ATOM   1882  CA  ILE A   9     -29.062  21.867  -5.997  1.00 56.89           C
ANISOU 1882  CA  ILE A   9     7429   6946   7239   -479    124   -186       C
ATOM   1883  C   ILE A   9     -28.414  23.121  -6.565  1.00 59.15           C
ANISOU 1883  C   ILE A   9     7622   7268   7583   -416     68   -171       C
ATOM   1884  O   ILE A   9     -29.093  23.984  -7.138  1.00 47.90           O
ANISOU 1884  O   ILE A   9     6110   5898   6193   -424     64   -190       O
ATOM   1885  CB  ILE A   9     -28.364  20.612  -6.542  1.00 51.95           C
ANISOU 1885  CB  ILE A   9     6884   6269   6586   -471    126   -165       C
ATOM   1886  CG1 ILE A   9     -28.512  20.564  -8.072  1.00 48.25           C
ANISOU 1886  CG1 ILE A   9     6345   5835   6154   -479    120   -170       C
ATOM   1887  CG2 ILE A   9     -28.908  19.347  -5.863  1.00 48.04           C
ANISOU 1887  CG2 ILE A   9     6510   5721   6022   -532    185   -176       C
ATOM   1888  CD1 ILE A   9     -27.282  20.074  -8.823  1.00 39.86           C
ANISOU 1888  CD1 ILE A   9     5307   4741   5098   -425     84   -141       C
ATOM   1889  N   ARG A  10     -27.098  23.229  -6.396  1.00 58.24           N
ANISOU 1889  N   ARG A  10     7530   7123   7475   -352     26   -144       N
ATOM   1890  CA  ARG A  10     -26.310  24.282  -7.022  1.00 54.44           C
ANISOU 1890  CA  ARG A  10     6974   6667   7045   -301    -18   -134       C
ATOM   1891  C   ARG A  10     -26.222  24.068  -8.532  1.00 50.40           C
ANISOU 1891  C   ARG A  10     6424   6169   6557   -304    -22   -130       C
ATOM   1892  O   ARG A  10     -26.853  24.797  -9.305  1.00 47.99           O
ANISOU 1892  O   ARG A  10     6049   5904   6279   -316    -22   -141       O
ATOM   1893  CB  ARG A  10     -24.917  24.308  -6.414  1.00 52.98           C
ANISOU 1893  CB  ARG A  10     6823   6451   6856   -239    -57   -121       C
ATOM   1894  CG  ARG A  10     -24.257  25.646  -6.444  1.00 53.48           C
ANISOU 1894  CG  ARG A  10     6815   6541   6964   -200    -91   -122       C
ATOM   1895  CD  ARG A  10     -22.895  25.505  -5.855  1.00 57.83           C
ANISOU 1895  CD  ARG A  10     7396   7071   7507   -142   -126   -122       C
ATOM   1896  NE  ARG A  10     -21.853  26.038  -6.716  1.00 61.05           N
ANISOU 1896  NE  ARG A  10     7746   7495   7954   -112   -152   -128       N
ATOM   1897  CZ  ARG A  10     -20.726  26.528  -6.233  1.00 53.70           C
ANISOU 1897  CZ  ARG A  10     6798   6569   7035    -66   -184   -143       C
ATOM   1898  NH1 ARG A  10     -20.559  26.527  -4.926  1.00 41.22           N
ANISOU 1898  NH1 ARG A  10     5255   4978   5428    -39   -197   -151       N
ATOM   1899  NH2 ARG A  10     -19.795  27.020  -7.034  1.00 59.23           N
ANISOU 1899  NH2 ARG A  10     7446   7289   7771    -50   -199   -157       N
ATOM   1900  N   GLY A  11     -25.428  23.080  -8.949  1.00 49.28           N
ANISOU 1900  N   GLY A  11     6332   5994   6400   -288    -29   -118       N
ATOM   1901  CA  GLY A  11     -25.408  22.627 -10.334  1.00 45.85           C
ANISOU 1901  CA  GLY A  11     5875   5567   5979   -299    -26   -115       C
ATOM   1902  C   GLY A  11     -25.126  23.722 -11.340  1.00 46.43           C
ANISOU 1902  C   GLY A  11     5866   5675   6099   -276    -49   -113       C
ATOM   1903  O   GLY A  11     -24.265  24.591 -11.131  1.00 44.48           O
ANISOU 1903  O   GLY A  11     5593   5430   5876   -237    -77   -108       O
ATOM   1904  N   LEU A  12     -25.875  23.695 -12.449  1.00 45.08           N
ANISOU 1904  N   LEU A  12     5659   5531   5939   -303    -36   -120       N
ATOM   1905  CA  LEU A  12     -25.636  24.589 -13.579  1.00 45.96           C
ANISOU 1905  CA  LEU A  12     5712   5666   6085   -282    -55   -116       C
ATOM   1906  C   LEU A  12     -26.358  25.914 -13.454  1.00 48.35           C
ANISOU 1906  C   LEU A  12     5965   6002   6404   -276    -61   -127       C
ATOM   1907  O   LEU A  12     -26.271  26.737 -14.369  1.00 45.61           O
ANISOU 1907  O   LEU A  12     5584   5669   6078   -257    -75   -124       O
ATOM   1908  CB  LEU A  12     -26.056  23.930 -14.893  1.00 35.88           C
ANISOU 1908  CB  LEU A  12     4426   4401   4807   -303    -43   -120       C
ATOM   1909  CG  LEU A  12     -25.052  22.864 -15.303  1.00 43.34           C
ANISOU 1909  CG  LEU A  12     5412   5311   5743   -294    -46   -106       C
ATOM   1910  CD1 LEU A  12     -25.630  22.037 -16.444  1.00 40.13           C
ANISOU 1910  CD1 LEU A  12     5005   4914   5329   -323    -28   -112       C
ATOM   1911  CD2 LEU A  12     -23.750  23.558 -15.693  1.00 35.79           C
ANISOU 1911  CD2 LEU A  12     4434   4348   4814   -252    -74    -95       C
ATOM   1912  N   ALA A  13     -27.079  26.132 -12.368  1.00 47.86           N
ANISOU 1912  N   ALA A  13     5904   5951   6330   -291    -51   -141       N
ATOM   1913  CA  ALA A  13     -27.819  27.366 -12.180  1.00 54.16           C
ANISOU 1913  CA  ALA A  13     6656   6782   7139   -280    -59   -157       C
ATOM   1914  C   ALA A  13     -27.051  28.363 -11.328  1.00 57.11           C
ANISOU 1914  C   ALA A  13     7030   7141   7529   -248    -78   -145       C
ATOM   1915  O   ALA A  13     -27.521  29.493 -11.139  1.00 60.72           O
ANISOU 1915  O   ALA A  13     7456   7619   7996   -233    -88   -154       O
ATOM   1916  CB  ALA A  13     -29.197  27.067 -11.556  1.00 51.26           C
ANISOU 1916  CB  ALA A  13     6279   6448   6751   -320    -32   -191       C
ATOM   1917  N   HIS A  14     -25.875  27.976 -10.823  1.00 50.67           N
ANISOU 1917  N   HIS A  14     6248   6292   6713   -234    -86   -129       N
ATOM   1918  CA  HIS A  14     -25.146  28.840  -9.899  1.00 37.12           C
ANISOU 1918  CA  HIS A  14     4529   4566   5009   -207   -104   -127       C
ATOM   1919  C   HIS A  14     -24.700  30.134 -10.580  1.00 43.72           C
ANISOU 1919  C   HIS A  14     5329   5408   5875   -185   -117   -124       C
ATOM   1920  O   HIS A  14     -24.872  31.227 -10.036  1.00 49.74           O
ANISOU 1920  O   HIS A  14     6075   6177   6646   -174   -124   -130       O
ATOM   1921  CB  HIS A  14     -23.956  28.084  -9.323  1.00 39.25           C
ANISOU 1921  CB  HIS A  14     4839   4807   5269   -188   -114   -121       C
ATOM   1922  CG  HIS A  14     -23.342  28.752  -8.131  1.00 48.45           C
ANISOU 1922  CG  HIS A  14     6005   5967   6438   -163   -131   -127       C
ATOM   1923  ND1 HIS A  14     -23.985  28.837  -6.915  1.00 45.39           N
ANISOU 1923  ND1 HIS A  14     5637   5580   6031   -170   -124   -132       N
ATOM   1924  CD2 HIS A  14     -22.148  29.370  -7.970  1.00 48.78           C
ANISOU 1924  CD2 HIS A  14     6028   6006   6500   -132   -151   -136       C
ATOM   1925  CE1 HIS A  14     -23.217  29.486  -6.059  1.00 48.48           C
ANISOU 1925  CE1 HIS A  14     6022   5968   6430   -141   -144   -139       C
ATOM   1926  NE2 HIS A  14     -22.099  29.826  -6.674  1.00 48.54           N
ANISOU 1926  NE2 HIS A  14     6004   5976   6462   -118   -160   -144       N
ATOM   1927  N   ALA A  15     -24.113  30.037 -11.771  1.00 46.83           N
ANISOU 1927  N   ALA A  15     5718   5794   6280   -182   -119   -117       N
ATOM   1928  CA  ALA A  15     -23.699  31.264 -12.440  1.00 39.94           C
ANISOU 1928  CA  ALA A  15     4829   4918   5428   -169   -123   -116       C
ATOM   1929  C   ALA A  15     -24.911  32.062 -12.895  1.00 43.24           C
ANISOU 1929  C   ALA A  15     5234   5354   5840   -163   -124   -119       C
ATOM   1930  O   ALA A  15     -24.878  33.306 -12.873  1.00 38.47           O
ANISOU 1930  O   ALA A  15     4628   4744   5243   -147   -128   -120       O
ATOM   1931  CB  ALA A  15     -22.764  30.950 -13.607  1.00 37.58           C
ANISOU 1931  CB  ALA A  15     4533   4607   5139   -171   -120   -111       C
ATOM   1932  N   ILE A  16     -26.004  31.367 -13.243  1.00 35.86           N
ANISOU 1932  N   ILE A  16     4292   4443   4889   -175   -119   -126       N
ATOM   1933  CA  ILE A  16     -27.229  32.048 -13.661  1.00 37.75           C
ANISOU 1933  CA  ILE A  16     4513   4712   5119   -160   -126   -141       C
ATOM   1934  C   ILE A  16     -27.854  32.820 -12.504  1.00 42.62           C
ANISOU 1934  C   ILE A  16     5116   5345   5733   -151   -131   -157       C
ATOM   1935  O   ILE A  16     -28.240  33.981 -12.663  1.00 47.26           O
ANISOU 1935  O   ILE A  16     5698   5938   6320   -120   -145   -164       O
ATOM   1936  CB  ILE A  16     -28.227  31.052 -14.260  1.00 40.77           C
ANISOU 1936  CB  ILE A  16     4881   5126   5485   -179   -118   -159       C
ATOM   1937  CG1 ILE A  16     -27.615  30.359 -15.479  1.00 40.77           C
ANISOU 1937  CG1 ILE A  16     4894   5109   5487   -185   -114   -143       C
ATOM   1938  CG2 ILE A  16     -29.493  31.786 -14.636  1.00 38.59           C
ANISOU 1938  CG2 ILE A  16     4575   4890   5196   -154   -132   -188       C
ATOM   1939  CD1 ILE A  16     -28.300  29.057 -15.836  1.00 40.72           C
ANISOU 1939  CD1 ILE A  16     4881   5124   5466   -216    -99   -158       C
ATOM   1940  N   ARG A  17     -27.996  32.185 -11.333  1.00 43.82           N
ANISOU 1940  N   ARG A  17     5269   5502   5880   -175   -120   -164       N
ATOM   1941  CA  ARG A  17     -28.526  32.905 -10.172  1.00 42.09           C
ANISOU 1941  CA  ARG A  17     5037   5298   5658   -169   -123   -180       C
ATOM   1942  C   ARG A  17     -27.677  34.130  -9.869  1.00 45.95           C
ANISOU 1942  C   ARG A  17     5534   5761   6164   -141   -137   -166       C
ATOM   1943  O   ARG A  17     -28.193  35.245  -9.718  1.00 44.13           O
ANISOU 1943  O   ARG A  17     5293   5540   5933   -116   -149   -177       O
ATOM   1944  CB  ARG A  17     -28.580  31.997  -8.947  1.00 44.41           C
ANISOU 1944  CB  ARG A  17     5347   5589   5938   -201   -105   -184       C
ATOM   1945  CG  ARG A  17     -29.539  30.834  -9.064  1.00 40.55           C
ANISOU 1945  CG  ARG A  17     4858   5123   5426   -242    -80   -206       C
ATOM   1946  CD  ARG A  17     -29.449  29.959  -7.830  1.00 30.43           C
ANISOU 1946  CD  ARG A  17     3616   3822   4122   -275    -57   -206       C
ATOM   1947  NE  ARG A  17     -30.325  28.805  -7.962  1.00 40.80           N
ANISOU 1947  NE  ARG A  17     4941   5151   5410   -326    -23   -230       N
ATOM   1948  CZ  ARG A  17     -29.917  27.543  -7.928  1.00 46.30           C
ANISOU 1948  CZ  ARG A  17     5694   5813   6086   -353     -2   -216       C
ATOM   1949  NH1 ARG A  17     -28.632  27.266  -7.762  1.00 52.99           N
ANISOU 1949  NH1 ARG A  17     6585   6615   6935   -324    -20   -183       N
ATOM   1950  NH2 ARG A  17     -30.797  26.557  -8.083  1.00 52.23           N
ANISOU 1950  NH2 ARG A  17     6457   6576   6810   -407     36   -243       N
ATOM   1951  N   LEU A  18     -26.361  33.940  -9.820  1.00 48.45           N
ANISOU 1951  N   LEU A  18     5870   6045   6494   -144   -136   -148       N
ATOM   1952  CA  LEU A  18     -25.456  35.053  -9.573  1.00 49.63           C
ANISOU 1952  CA  LEU A  18     6024   6173   6661   -128   -142   -144       C
ATOM   1953  C   LEU A  18     -25.660  36.165 -10.587  1.00 50.93           C
ANISOU 1953  C   LEU A  18     6197   6328   6826   -108   -145   -142       C
ATOM   1954  O   LEU A  18     -25.734  37.340 -10.219  1.00 62.81           O
ANISOU 1954  O   LEU A  18     7708   7824   8333    -91   -150   -146       O
ATOM   1955  CB  LEU A  18     -24.011  34.558  -9.592  1.00 46.24           C
ANISOU 1955  CB  LEU A  18     5604   5721   6244   -135   -139   -139       C
ATOM   1956  CG  LEU A  18     -23.618  33.808  -8.320  1.00 43.76           C
ANISOU 1956  CG  LEU A  18     5296   5408   5923   -137   -144   -144       C
ATOM   1957  CD1 LEU A  18     -22.381  32.945  -8.544  1.00 41.96           C
ANISOU 1957  CD1 LEU A  18     5077   5167   5698   -134   -148   -146       C
ATOM   1958  CD2 LEU A  18     -23.386  34.829  -7.228  1.00 40.32           C
ANISOU 1958  CD2 LEU A  18     4852   4971   5495   -125   -151   -155       C
ATOM   1959  N   LEU A  19     -25.782  35.819 -11.868  1.00 46.49           N
ANISOU 1959  N   LEU A  19     5642   5763   6257   -108   -143   -135       N
ATOM   1960  CA  LEU A  19     -25.933  36.865 -12.872  1.00 48.45           C
ANISOU 1960  CA  LEU A  19     5917   5995   6498    -83   -146   -131       C
ATOM   1961  C   LEU A  19     -27.301  37.526 -12.772  1.00 49.86           C
ANISOU 1961  C   LEU A  19     6089   6200   6657    -48   -165   -147       C
ATOM   1962  O   LEU A  19     -27.424  38.740 -12.974  1.00 52.42           O
ANISOU 1962  O   LEU A  19     6443   6503   6970    -17   -173   -148       O
ATOM   1963  CB  LEU A  19     -25.708  36.304 -14.276  1.00 43.06           C
ANISOU 1963  CB  LEU A  19     5249   5303   5810    -88   -140   -121       C
ATOM   1964  CG  LEU A  19     -25.673  37.342 -15.386  1.00 45.05           C
ANISOU 1964  CG  LEU A  19     5547   5525   6046    -64   -139   -114       C
ATOM   1965  CD1 LEU A  19     -24.497  38.274 -15.198  1.00 42.84           C
ANISOU 1965  CD1 LEU A  19     5299   5202   5777    -81   -118   -110       C
ATOM   1966  CD2 LEU A  19     -25.602  36.653 -16.732  1.00 48.76           C
ANISOU 1966  CD2 LEU A  19     6028   5992   6506    -68   -135   -105       C
ATOM   1967  N   LEU A  20     -28.344  36.753 -12.468  1.00 46.92           N
ANISOU 1967  N   LEU A  20     5680   5872   6276    -52   -171   -167       N
ATOM   1968  CA  LEU A  20     -29.645  37.372 -12.251  1.00 51.13           C
ANISOU 1968  CA  LEU A  20     6195   6442   6791    -17   -190   -196       C
ATOM   1969  C   LEU A  20     -29.570  38.365 -11.099  1.00 56.57           C
ANISOU 1969  C   LEU A  20     6887   7122   7486     -6   -195   -200       C
ATOM   1970  O   LEU A  20     -30.050  39.501 -11.215  1.00 59.58           O
ANISOU 1970  O   LEU A  20     7284   7500   7853     39   -213   -211       O
ATOM   1971  CB  LEU A  20     -30.707  36.308 -11.987  1.00 47.34           C
ANISOU 1971  CB  LEU A  20     5667   6017   6302    -40   -186   -228       C
ATOM   1972  CG  LEU A  20     -31.167  35.407 -13.133  1.00 43.05           C
ANISOU 1972  CG  LEU A  20     5111   5498   5748    -46   -185   -239       C
ATOM   1973  CD1 LEU A  20     -31.874  34.180 -12.561  1.00 36.08           C
ANISOU 1973  CD1 LEU A  20     4192   4657   4860    -95   -163   -267       C
ATOM   1974  CD2 LEU A  20     -32.079  36.117 -14.137  1.00 35.38           C
ANISOU 1974  CD2 LEU A  20     4135   4554   4753     12   -214   -265       C
ATOM   1975  N   GLU A  21     -28.926  37.963  -9.991  1.00 46.23           N
ANISOU 1975  N   GLU A  21     5569   5804   6193    -40   -180   -192       N
ATOM   1976  CA  GLU A  21     -28.743  38.847  -8.837  1.00 41.18           C
ANISOU 1976  CA  GLU A  21     4930   5155   5561    -33   -182   -195       C
ATOM   1977  C   GLU A  21     -27.968  40.109  -9.212  1.00 49.78           C
ANISOU 1977  C   GLU A  21     6062   6199   6655    -12   -184   -181       C
ATOM   1978  O   GLU A  21     -28.437  41.235  -9.001  1.00 55.29           O
ANISOU 1978  O   GLU A  21     6774   6892   7342     22   -196   -191       O
ATOM   1979  CB  GLU A  21     -28.016  38.102  -7.717  1.00 39.65           C
ANISOU 1979  CB  GLU A  21     4729   4955   5380    -69   -169   -188       C
ATOM   1980  CG  GLU A  21     -28.805  36.941  -7.073  1.00 47.60           C
ANISOU 1980  CG  GLU A  21     5714   5997   6374    -97   -159   -204       C
ATOM   1981  CD  GLU A  21     -30.032  37.404  -6.279  1.00 59.10           C
ANISOU 1981  CD  GLU A  21     7143   7492   7818    -89   -163   -236       C
ATOM   1982  OE1 GLU A  21     -29.984  38.493  -5.654  1.00 56.90           O
ANISOU 1982  OE1 GLU A  21     6866   7208   7546    -65   -174   -239       O
ATOM   1983  OE2 GLU A  21     -31.049  36.672  -6.277  1.00 61.35           O
ANISOU 1983  OE2 GLU A  21     7404   7818   8089   -109   -152   -263       O
ATOM   1984  N   TYR A  22     -26.772  39.936  -9.775  1.00 49.86           N
ANISOU 1984  N   TYR A  22     6095   6174   6678    -34   -168   -162       N
ATOM   1985  CA  TYR A  22     -25.926  41.079 -10.118  1.00 46.88           C
ANISOU 1985  CA  TYR A  22     5761   5749   6302    -31   -156   -155       C
ATOM   1986  C   TYR A  22     -26.633  42.062 -11.045  1.00 51.48           C
ANISOU 1986  C   TYR A  22     6391   6313   6857     11   -167   -155       C
ATOM   1987  O   TYR A  22     -26.415  43.277 -10.947  1.00 53.84           O
ANISOU 1987  O   TYR A  22     6735   6575   7147     26   -161   -155       O
ATOM   1988  CB  TYR A  22     -24.631  40.601 -10.769  1.00 38.29           C
ANISOU 1988  CB  TYR A  22     4683   4637   5229    -67   -133   -146       C
ATOM   1989  CG  TYR A  22     -23.782  41.731 -11.254  1.00 39.60           C
ANISOU 1989  CG  TYR A  22     4899   4755   5394    -77   -110   -146       C
ATOM   1990  CD1 TYR A  22     -23.895  42.218 -12.557  1.00 44.44           C
ANISOU 1990  CD1 TYR A  22     5568   5334   5984    -66   -101   -136       C
ATOM   1991  CD2 TYR A  22     -22.840  42.309 -10.420  1.00 35.00           C
ANISOU 1991  CD2 TYR A  22     4311   4158   4829   -102    -94   -161       C
ATOM   1992  CE1 TYR A  22     -23.100  43.268 -13.005  1.00 38.56           C
ANISOU 1992  CE1 TYR A  22     4884   4536   5231    -85    -69   -138       C
ATOM   1993  CE2 TYR A  22     -22.051  43.347 -10.860  1.00 35.05           C
ANISOU 1993  CE2 TYR A  22     4365   4118   4832   -124    -62   -169       C
ATOM   1994  CZ  TYR A  22     -22.189  43.832 -12.138  1.00 39.23           C
ANISOU 1994  CZ  TYR A  22     4961   4609   5336   -119    -47   -157       C
ATOM   1995  OH  TYR A  22     -21.379  44.867 -12.533  1.00 47.17           O
ANISOU 1995  OH  TYR A  22     6027   5562   6333   -150     -7   -167       O
ATOM   1996  N   THR A  23     -27.442  41.567 -11.986  1.00 46.50           N
ANISOU 1996  N   THR A  23     5758   5703   6206     35   -182   -156       N
ATOM   1997  CA  THR A  23     -28.138  42.478 -12.880  1.00 45.51           C
ANISOU 1997  CA  THR A  23     5684   5561   6046     90   -199   -159       C
ATOM   1998  C   THR A  23     -29.439  42.993 -12.285  1.00 52.55           C
ANISOU 1998  C   THR A  23     6554   6492   6919    143   -232   -188       C
ATOM   1999  O   THR A  23     -30.176  43.719 -12.973  1.00 55.70           O
ANISOU 1999  O   THR A  23     6994   6886   7283    205   -257   -199       O
ATOM   2000  CB  THR A  23     -28.411  41.833 -14.264  1.00 52.86           C
ANISOU 2000  CB  THR A  23     6628   6499   6960    103   -206   -154       C
ATOM   2001  OG1 THR A  23     -29.240  40.660 -14.152  1.00 44.24           O
ANISOU 2001  OG1 THR A  23     5467   5470   5873     98   -219   -173       O
ATOM   2002  CG2 THR A  23     -27.101  41.543 -15.014  1.00 48.37           C
ANISOU 2002  CG2 THR A  23     6092   5884   6403     58   -172   -129       C
ATOM   2003  N   GLY A  24     -29.724  42.657 -11.030  1.00 57.12           N
ANISOU 2003  N   GLY A  24     7075   7109   7518    122   -233   -203       N
ATOM   2004  CA  GLY A  24     -30.954  43.098 -10.390  1.00 56.44           C
ANISOU 2004  CA  GLY A  24     6960   7069   7417    165   -260   -238       C
ATOM   2005  C   GLY A  24     -32.192  42.700 -11.157  1.00 55.25           C
ANISOU 2005  C   GLY A  24     6780   6972   7241    207   -287   -272       C
ATOM   2006  O   GLY A  24     -33.131  43.495 -11.279  1.00 59.10           O
ANISOU 2006  O   GLY A  24     7274   7481   7700    273   -320   -304       O
ATOM   2007  N   SER A  25     -32.196  41.496 -11.710  1.00 52.70           N
ANISOU 2007  N   SER A  25     6426   6672   6925    173   -276   -271       N
ATOM   2008  CA  SER A  25     -33.322  40.996 -12.476  1.00 44.59           C
ANISOU 2008  CA  SER A  25     5363   5703   5876    203   -298   -310       C
ATOM   2009  C   SER A  25     -34.451  40.550 -11.549  1.00 50.94           C
ANISOU 2009  C   SER A  25     6089   6584   6681    192   -301   -364       C
ATOM   2010  O   SER A  25     -34.225  40.108 -10.421  1.00 52.65           O
ANISOU 2010  O   SER A  25     6279   6806   6919    137   -276   -360       O
ATOM   2011  CB  SER A  25     -32.872  39.830 -13.357  1.00 48.46           C
ANISOU 2011  CB  SER A  25     5849   6188   6374    162   -279   -290       C
ATOM   2012  OG  SER A  25     -31.801  40.201 -14.221  1.00 56.04           O
ANISOU 2012  OG  SER A  25     6879   7080   7333    165   -271   -246       O
ATOM   2013  N   ASP A  26     -35.681  40.663 -12.034  1.00 56.39           N
ANISOU 2013  N   ASP A  26     6743   7337   7345    244   -332   -420       N
ATOM   2014  CA  ASP A  26     -36.836  40.228 -11.247  1.00 58.81           C
ANISOU 2014  CA  ASP A  26     6967   7727   7650    227   -330   -487       C
ATOM   2015  C   ASP A  26     -37.177  38.799 -11.649  1.00 59.14           C
ANISOU 2015  C   ASP A  26     6960   7813   7696    168   -305   -510       C
ATOM   2016  O   ASP A  26     -37.922  38.551 -12.602  1.00 57.22           O
ANISOU 2016  O   ASP A  26     6689   7619   7433    200   -325   -554       O
ATOM   2017  CB  ASP A  26     -38.021  41.162 -11.454  1.00 60.45           C
ANISOU 2017  CB  ASP A  26     7151   7992   7825    318   -378   -553       C
ATOM   2018  CG  ASP A  26     -39.117  40.922 -10.453  1.00 67.50           C
ANISOU 2018  CG  ASP A  26     7957   8970   8719    297   -372   -627       C
ATOM   2019  OD1 ASP A  26     -38.791  40.897  -9.255  1.00 71.37           O
ANISOU 2019  OD1 ASP A  26     8443   9445   9230    245   -343   -610       O
ATOM   2020  OD2 ASP A  26     -40.291  40.747 -10.856  1.00 69.30           O
ANISOU 2020  OD2 ASP A  26     8121   9285   8926    330   -394   -708       O
ATOM   2021  N   TYR A  27     -36.631  37.836 -10.922  1.00 52.19           N
ANISOU 2021  N   TYR A  27     6076   6915   6839     83   -260   -485       N
ATOM   2022  CA  TYR A  27     -36.916  36.446 -11.230  1.00 57.63           C
ANISOU 2022  CA  TYR A  27     6732   7635   7528     21   -229   -505       C
ATOM   2023  C   TYR A  27     -37.474  35.737 -10.009  1.00 61.49           C
ANISOU 2023  C   TYR A  27     7182   8163   8019    -51   -189   -543       C
ATOM   2024  O   TYR A  27     -37.290  36.162  -8.868  1.00 62.48           O
ANISOU 2024  O   TYR A  27     7315   8273   8152    -62   -181   -533       O
ATOM   2025  CB  TYR A  27     -35.674  35.699 -11.714  1.00 49.80           C
ANISOU 2025  CB  TYR A  27     5793   6576   6552    -18   -208   -437       C
ATOM   2026  CG  TYR A  27     -34.678  35.457 -10.607  1.00 47.04           C
ANISOU 2026  CG  TYR A  27     5477   6173   6222    -65   -180   -390       C
ATOM   2027  CD1 TYR A  27     -33.968  36.520 -10.049  1.00 38.97           C
ANISOU 2027  CD1 TYR A  27     4488   5107   5210    -35   -194   -357       C
ATOM   2028  CD2 TYR A  27     -34.465  34.179 -10.105  1.00 41.40           C
ANISOU 2028  CD2 TYR A  27     4767   5452   5509   -136   -141   -384       C
ATOM   2029  CE1 TYR A  27     -33.064  36.324  -9.054  1.00 30.09           C
ANISOU 2029  CE1 TYR A  27     3390   3942   4101    -70   -174   -322       C
ATOM   2030  CE2 TYR A  27     -33.554  33.962  -9.093  1.00 40.45           C
ANISOU 2030  CE2 TYR A  27     4685   5284   5400   -166   -123   -345       C
ATOM   2031  CZ  TYR A  27     -32.852  35.042  -8.578  1.00 39.06           C
ANISOU 2031  CZ  TYR A  27     4530   5073   5237   -131   -142   -316       C
ATOM   2032  OH  TYR A  27     -31.945  34.852  -7.574  1.00 36.24           O
ANISOU 2032  OH  TYR A  27     4205   4676   4889   -153   -129   -286       O
ATOM   2033  N   GLU A  28     -38.170  34.646 -10.273  1.00 57.69           N
ANISOU 2033  N   GLU A  28     6660   7731   7528   -103   -161   -590       N
ATOM   2034  CA  GLU A  28     -38.507  33.668  -9.258  1.00 56.71           C
ANISOU 2034  CA  GLU A  28     6522   7624   7401   -192   -107   -617       C
ATOM   2035  C   GLU A  28     -37.983  32.319  -9.727  1.00 55.02           C
ANISOU 2035  C   GLU A  28     6343   7375   7186   -255    -71   -587       C
ATOM   2036  O   GLU A  28     -37.703  32.126 -10.912  1.00 62.05           O
ANISOU 2036  O   GLU A  28     7241   8256   8079   -229    -89   -569       O
ATOM   2037  CB  GLU A  28     -40.015  33.615  -9.019  1.00 58.05           C
ANISOU 2037  CB  GLU A  28     6609   7895   7553   -209    -96   -723       C
ATOM   2038  CG  GLU A  28     -40.817  33.910 -10.268  1.00 77.81           C
ANISOU 2038  CG  GLU A  28     9056  10465  10043   -147   -136   -781       C
ATOM   2039  CD  GLU A  28     -42.303  33.635 -10.102  1.00 94.83           C
ANISOU 2039  CD  GLU A  28    11116  12733  12180   -174   -120   -903       C
ATOM   2040  OE1 GLU A  28     -42.665  32.726  -9.321  1.00 98.98           O
ANISOU 2040  OE1 GLU A  28    11628  13279  12702   -274    -56   -938       O
ATOM   2041  OE2 GLU A  28     -43.107  34.310 -10.782  1.00102.58           O
ANISOU 2041  OE2 GLU A  28    12041  13785  13148    -95   -169   -968       O
ATOM   2042  N   GLU A  29     -37.849  31.381  -8.800  1.00 51.27           N
ANISOU 2042  N   GLU A  29     5898   6878   6704   -334    -19   -582       N
ATOM   2043  CA  GLU A  29     -37.354  30.053  -9.124  1.00 51.43           C
ANISOU 2043  CA  GLU A  29     5965   6859   6718   -393     17   -554       C
ATOM   2044  C   GLU A  29     -38.457  29.017  -9.008  1.00 50.61           C
ANISOU 2044  C   GLU A  29     5831   6810   6591   -476     72   -630       C
ATOM   2045  O   GLU A  29     -39.209  29.002  -8.034  1.00 62.18           O
ANISOU 2045  O   GLU A  29     7275   8310   8041   -521    106   -681       O
ATOM   2046  CB  GLU A  29     -36.158  29.672  -8.253  1.00 62.33           C
ANISOU 2046  CB  GLU A  29     7427   8155   8100   -413     33   -484       C
ATOM   2047  CG  GLU A  29     -35.209  30.830  -7.980  1.00 71.91           C
ANISOU 2047  CG  GLU A  29     8659   9328   9336   -345    -11   -430       C
ATOM   2048  CD  GLU A  29     -33.816  30.378  -7.566  1.00 73.46           C
ANISOU 2048  CD  GLU A  29     8929   9447   9537   -349     -8   -363       C
ATOM   2049  OE1 GLU A  29     -33.335  29.341  -8.074  1.00 74.46           O
ANISOU 2049  OE1 GLU A  29     9093   9543   9657   -373      8   -342       O
ATOM   2050  OE2 GLU A  29     -33.212  31.061  -6.711  1.00 79.24           O
ANISOU 2050  OE2 GLU A  29     9680  10151  10278   -324    -22   -337       O
ATOM   2051  N   LYS A  30     -38.581  28.201 -10.045  1.00 51.78           N
ANISOU 2051  N   LYS A  30     5972   6968   6733   -497     83   -642       N
ATOM   2052  CA  LYS A  30     -39.373  26.986 -10.014  1.00 46.58           C
ANISOU 2052  CA  LYS A  30     5306   6341   6051   -591    146   -704       C
ATOM   2053  C   LYS A  30     -38.406  25.868  -9.657  1.00 53.37           C
ANISOU 2053  C   LYS A  30     6270   7110   6899   -643    185   -638       C
ATOM   2054  O   LYS A  30     -37.538  25.517 -10.470  1.00 56.36           O
ANISOU 2054  O   LYS A  30     6686   7441   7287   -616    164   -582       O
ATOM   2055  CB  LYS A  30     -40.037  26.746 -11.367  1.00 45.96           C
ANISOU 2055  CB  LYS A  30     5163   6326   5972   -580    133   -757       C
ATOM   2056  CG  LYS A  30     -40.785  25.416 -11.459  1.00 46.96           C
ANISOU 2056  CG  LYS A  30     5283   6484   6075   -685    203   -824       C
ATOM   2057  CD  LYS A  30     -42.045  25.452 -10.595  1.00 46.56           C
ANISOU 2057  CD  LYS A  30     5172   6512   6005   -749    249   -927       C
ATOM   2058  CE  LYS A  30     -42.784  24.102 -10.591  1.00 57.33           C
ANISOU 2058  CE  LYS A  30     6539   7903   7341   -873    334  -1000       C
ATOM   2059  NZ  LYS A  30     -43.428  23.808  -9.271  1.00 65.14           N
ANISOU 2059  NZ  LYS A  30     7542   8905   8304   -968    407  -1055       N
ATOM   2060  N   ILE A  31     -38.519  25.349  -8.424  1.00 48.27           N
ANISOU 2060  N   ILE A  31     5677   6437   6227   -711    238   -645       N
ATOM   2061  CA  ILE A  31     -37.611  24.331  -7.903  1.00 40.37           C
ANISOU 2061  CA  ILE A  31     4792   5342   5203   -749    271   -586       C
ATOM   2062  C   ILE A  31     -38.252  22.969  -8.085  1.00 44.47           C
ANISOU 2062  C   ILE A  31     5344   5865   5688   -849    344   -633       C
ATOM   2063  O   ILE A  31     -39.391  22.754  -7.664  1.00 58.68           O
ANISOU 2063  O   ILE A  31     7109   7720   7467   -924    398   -715       O
ATOM   2064  CB  ILE A  31     -37.254  24.569  -6.423  1.00 38.58           C
ANISOU 2064  CB  ILE A  31     4627   5071   4961   -756    285   -559       C
ATOM   2065  CG1 ILE A  31     -36.796  26.025  -6.180  1.00 39.87           C
ANISOU 2065  CG1 ILE A  31     4746   5244   5159   -666    219   -527       C
ATOM   2066  N   TYR A  32     -37.531  22.058  -8.726  1.00 43.72           N
ANISOU 2066  N   TYR A  32     5314   5713   5586   -854    348   -589       N
ATOM   2067  CA  TYR A  32     -37.910  20.657  -8.787  1.00 50.50           C
ANISOU 2067  CA  TYR A  32     6236   6547   6405   -950    421   -619       C
ATOM   2068  C   TYR A  32     -37.049  19.871  -7.816  1.00 60.07           C
ANISOU 2068  C   TYR A  32     7594   7654   7577   -969    450   -559       C
ATOM   2069  O   TYR A  32     -35.834  20.080  -7.737  1.00 64.10           O
ANISOU 2069  O   TYR A  32     8153   8103   8098   -893    398   -483       O
ATOM   2070  CB  TYR A  32     -37.744  20.090 -10.197  1.00 55.43           C
ANISOU 2070  CB  TYR A  32     6842   7178   7041   -941    408   -614       C
ATOM   2071  CG  TYR A  32     -38.517  20.859 -11.222  1.00 52.92           C
ANISOU 2071  CG  TYR A  32     6392   6960   6756   -906    371   -670       C
ATOM   2072  CD1 TYR A  32     -39.779  20.449 -11.615  1.00 53.28           C
ANISOU 2072  CD1 TYR A  32     6369   7085   6789   -976    416   -769       C
ATOM   2073  CD2 TYR A  32     -37.990  22.011 -11.782  1.00 55.54           C
ANISOU 2073  CD2 TYR A  32     6671   7306   7127   -800    291   -630       C
ATOM   2074  CE1 TYR A  32     -40.503  21.163 -12.538  1.00 49.57           C
ANISOU 2074  CE1 TYR A  32     5779   6712   6343   -931    374   -828       C
ATOM   2075  CE2 TYR A  32     -38.698  22.724 -12.701  1.00 55.90           C
ANISOU 2075  CE2 TYR A  32     6611   7435   7192   -758    254   -680       C
ATOM   2076  CZ  TYR A  32     -39.953  22.298 -13.070  1.00 53.64           C
ANISOU 2076  CZ  TYR A  32     6257   7232   6892   -817    291   -779       C
ATOM   2077  OH  TYR A  32     -40.645  23.028 -13.975  1.00 57.18           O
ANISOU 2077  OH  TYR A  32     6604   7768   7356   -761    245   -834       O
ATOM   2078  N   SER A  33     -37.680  18.953  -7.095  1.00 62.88           N
ANISOU 2078  N   SER A  33     8023   7987   7881  -1071    533   -601       N
ATOM   2079  CA  SER A  33     -37.002  18.141  -6.101  1.00 65.61           C
ANISOU 2079  CA  SER A  33     8526   8228   8175  -1092    566   -553       C
ATOM   2080  C   SER A  33     -36.979  16.693  -6.558  1.00 61.91           C
ANISOU 2080  C   SER A  33     8158   7704   7663  -1159    623   -556       C
ATOM   2081  O   SER A  33     -37.952  16.199  -7.131  1.00 65.28           O
ANISOU 2081  O   SER A  33     8541   8180   8083  -1243    678   -627       O
ATOM   2082  CB  SER A  33     -37.683  18.270  -4.732  1.00 67.64           C
ANISOU 2082  CB  SER A  33     8819   8486   8395  -1157    623   -592       C
ATOM   2083  OG  SER A  33     -37.689  19.634  -4.304  1.00 65.96           O
ANISOU 2083  OG  SER A  33     8515   8324   8223  -1091    568   -589       O
ATOM   2084  N   MET A  34     -35.858  16.028  -6.303  1.00 67.47           N
ANISOU 2084  N   MET A  34     8994   8307   8336  -1117    608   -485       N
ATOM   2085  CA  MET A  34     -35.600  14.654  -6.707  1.00 66.34           C
ANISOU 2085  CA  MET A  34     8968   8092   8147  -1159    650   -473       C
ATOM   2086  C   MET A  34     -35.729  13.725  -5.508  1.00 69.83           C
ANISOU 2086  C   MET A  34     9583   8443   8505  -1230    727   -475       C
ATOM   2087  O   MET A  34     -35.492  14.125  -4.369  1.00 79.38           O
ANISOU 2087  O   MET A  34    10845   9622   9693  -1206    720   -454       O
ATOM   2088  CB  MET A  34     -34.193  14.541  -7.303  1.00 64.47           C
ANISOU 2088  CB  MET A  34     8764   7802   7928  -1050    572   -395       C
ATOM   2089  CG  MET A  34     -33.885  13.263  -8.030  1.00 68.53           C
ANISOU 2089  CG  MET A  34     9370   8259   8410  -1073    598   -383       C
ATOM   2090  SD  MET A  34     -32.220  13.306  -8.733  1.00 66.62           S
ANISOU 2090  SD  MET A  34     9140   7974   8197   -936    499   -302       S
ATOM   2091  CE  MET A  34     -32.520  14.094 -10.302  1.00 70.84           C
ANISOU 2091  CE  MET A  34     9488   8613   8814   -915    456   -323       C
ATOM   2092  N   GLY A  35     -36.094  12.477  -5.774  1.00 71.75           N
ANISOU 2092  N   GLY A  35     9924   8640   8696  -1318    802   -501       N
ATOM   2093  CA  GLY A  35     -36.153  11.492  -4.722  1.00 73.32           C
ANISOU 2093  CA  GLY A  35    10318   8737   8804  -1386    881   -499       C
ATOM   2094  C   GLY A  35     -34.788  10.951  -4.336  1.00 83.21           C
ANISOU 2094  C   GLY A  35    11730   9873  10013  -1288    832   -414       C
ATOM   2095  O   GLY A  35     -33.825  11.004  -5.098  1.00 86.37           O
ANISOU 2095  O   GLY A  35    12102  10267  10448  -1189    754   -364       O
ATOM   2096  N   ASP A  36     -34.712  10.425  -3.110  1.00 88.63           N
ANISOU 2096  N   ASP A  36    12591  10468  10617  -1315    880   -401       N
ATOM   2097  CA  ASP A  36     -33.500   9.789  -2.604  1.00 85.94           C
ANISOU 2097  CA  ASP A  36    12429  10009  10215  -1221    840   -332       C
ATOM   2098  C   ASP A  36     -33.482   8.336  -3.039  1.00 83.25           C
ANISOU 2098  C   ASP A  36    12246   9579   9805  -1274    899   -332       C
ATOM   2099  O   ASP A  36     -33.830   8.030  -4.181  1.00 81.57           O
ANISOU 2099  O   ASP A  36    11955   9409   9628  -1318    915   -358       O
ATOM   2100  CB  ASP A  36     -33.432   9.861  -1.078  1.00 86.23           C
ANISOU 2100  CB  ASP A  36    12599   9981  10184  -1218    862   -319       C
ATOM   2101  CG  ASP A  36     -33.906  11.178  -0.537  1.00 86.55           C
ANISOU 2101  CG  ASP A  36    12492  10113  10281  -1218    843   -342       C
ATOM   2102  OD1 ASP A  36     -34.454  11.179   0.577  1.00 88.43           O
ANISOU 2102  OD1 ASP A  36    12810  10324  10466  -1281    904   -365       O
ATOM   2103  OD2 ASP A  36     -33.735  12.210  -1.215  1.00 87.58           O
ANISOU 2103  OD2 ASP A  36    12435  10338  10503  -1157    770   -339       O
ATOM   2104  N   ALA A  37     -33.089   7.437  -2.120  1.00 93.67           N
ANISOU 2104  N   ALA A  37    13797  10771  11021  -1268    933   -304       N
ATOM   2105  CA  ALA A  37     -33.357   6.001  -2.204  1.00 95.41           C
ANISOU 2105  CA  ALA A  37    14212  10889  11151  -1353   1022   -316       C
ATOM   2106  C   ALA A  37     -32.589   5.415  -3.383  1.00 91.18           C
ANISOU 2106  C   ALA A  37    13673  10335  10635  -1283    968   -285       C
ATOM   2107  O   ALA A  37     -31.651   6.062  -3.868  1.00 80.00           O
ANISOU 2107  O   ALA A  37    12146   8964   9285  -1152    857   -245       O
ATOM   2108  CB  ALA A  37     -34.869   5.759  -2.316  1.00 95.15           C
ANISOU 2108  CB  ALA A  37    14141  10902  11111  -1540   1150   -402       C
ATOM   2109  N   PRO A  38     -32.890   4.188  -3.833  1.00103.60           N
ANISOU 2109  N   PRO A  38    15376  11839  12149  -1363   1043   -303       N
ATOM   2110  CA  PRO A  38     -32.470   3.812  -5.193  1.00107.26           C
ANISOU 2110  CA  PRO A  38    15772  12326  12658  -1325   1002   -292       C
ATOM   2111  C   PRO A  38     -33.264   4.534  -6.258  1.00108.73           C
ANISOU 2111  C   PRO A  38    15712  12654  12947  -1387   1004   -342       C
ATOM   2112  O   PRO A  38     -32.735   4.790  -7.346  1.00109.85           O
ANISOU 2112  O   PRO A  38    15731  12848  13157  -1313    930   -322       O
ATOM   2113  CB  PRO A  38     -32.714   2.297  -5.244  1.00107.28           C
ANISOU 2113  CB  PRO A  38    15996  12209  12558  -1410   1096   -304       C
ATOM   2114  CG  PRO A  38     -32.705   1.856  -3.833  1.00109.93           C
ANISOU 2114  CG  PRO A  38    16557  12427  12782  -1426   1148   -291       C
ATOM   2115  CD  PRO A  38     -33.273   3.000  -3.043  1.00109.68           C
ANISOU 2115  CD  PRO A  38    16404  12477  12792  -1456   1153   -315       C
ATOM   2116  N   ASP A  39     -34.520   4.878  -5.970  1.00111.08           N
ANISOU 2116  N   ASP A  39    15934  13016  13254  -1516   1086   -411       N
ATOM   2117  CA  ASP A  39     -35.392   5.544  -6.935  1.00115.21           C
ANISOU 2117  CA  ASP A  39    16229  13679  13866  -1573   1090   -473       C
ATOM   2118  C   ASP A  39     -35.203   7.055  -6.819  1.00113.63           C
ANISOU 2118  C   ASP A  39    15844  13579  13751  -1483    999   -458       C
ATOM   2119  O   ASP A  39     -35.968   7.769  -6.162  1.00117.55           O
ANISOU 2119  O   ASP A  39    16269  14134  14260  -1534   1029   -501       O
ATOM   2120  CB  ASP A  39     -36.839   5.133  -6.707  1.00115.69           C
ANISOU 2120  CB  ASP A  39    16295  13768  13892  -1754   1222   -569       C
ATOM   2121  CG  ASP A  39     -37.176   3.831  -7.387  1.00117.95           C
ANISOU 2121  CG  ASP A  39    16682  14002  14131  -1852   1304   -602       C
ATOM   2122  OD1 ASP A  39     -36.382   3.395  -8.248  1.00117.75           O
ANISOU 2122  OD1 ASP A  39    16677  13945  14118  -1775   1248   -554       O
ATOM   2123  OD2 ASP A  39     -38.229   3.240  -7.064  1.00119.65           O
ANISOU 2123  OD2 ASP A  39    16957  14209  14295  -2011   1429   -679       O
ATOM   2124  N   TYR A  40     -34.144   7.545  -7.464  1.00100.94           N
ANISOU 2124  N   TYR A  40    14163  11989  12200  -1348    889   -399       N
ATOM   2125  CA  TYR A  40     -33.920   8.982  -7.523  1.00 88.60           C
ANISOU 2125  CA  TYR A  40    12426  10519  10720  -1264    805   -385       C
ATOM   2126  C   TYR A  40     -35.026   9.587  -8.370  1.00 80.84           C
ANISOU 2126  C   TYR A  40    11252   9661   9801  -1330    824   -455       C
ATOM   2127  O   TYR A  40     -34.878   9.741  -9.586  1.00 70.52           O
ANISOU 2127  O   TYR A  40     9840   8408   8548  -1296    780   -454       O
ATOM   2128  CB  TYR A  40     -32.547   9.300  -8.096  1.00 85.93           C
ANISOU 2128  CB  TYR A  40    12057  10170  10423  -1119    695   -317       C
ATOM   2129  CG  TYR A  40     -31.406   8.938  -7.178  1.00 85.68           C
ANISOU 2129  CG  TYR A  40    12185  10036  10334  -1028    657   -258       C
ATOM   2130  CD1 TYR A  40     -31.029   9.780  -6.140  1.00 89.60           C
ANISOU 2130  CD1 TYR A  40    12676  10534  10834   -966    615   -236       C
ATOM   2131  CD2 TYR A  40     -30.708   7.749  -7.346  1.00 75.58           C
ANISOU 2131  CD2 TYR A  40    11064   8658   8994   -998    659   -228       C
ATOM   2132  CE1 TYR A  40     -29.982   9.450  -5.306  1.00 90.00           C
ANISOU 2132  CE1 TYR A  40    12868  10497  10829   -875    574   -190       C
ATOM   2133  CE2 TYR A  40     -29.663   7.410  -6.517  1.00 72.22           C
ANISOU 2133  CE2 TYR A  40    10786   8143   8511   -902    616   -182       C
ATOM   2134  CZ  TYR A  40     -29.300   8.259  -5.504  1.00 85.51           C
ANISOU 2134  CZ  TYR A  40    12456   9836  10199   -839    572   -165       C
ATOM   2135  OH  TYR A  40     -28.253   7.913  -4.682  1.00 90.08           O
ANISOU 2135  OH  TYR A  40    13180  10331  10717   -735    524   -126       O
ATOM   2136  N   ASP A  41     -36.144   9.914  -7.729  1.00 82.36           N
ANISOU 2136  N   ASP A  41    11404   9903   9984  -1424    888   -521       N
ATOM   2137  CA  ASP A  41     -37.383  10.159  -8.447  1.00 78.63           C
ANISOU 2137  CA  ASP A  41    10782   9544   9550  -1511    930   -610       C
ATOM   2138  C   ASP A  41     -37.367  11.515  -9.139  1.00 73.15           C
ANISOU 2138  C   ASP A  41     9889   8960   8944  -1422    838   -610       C
ATOM   2139  O   ASP A  41     -37.108  12.551  -8.514  1.00 67.86           O
ANISOU 2139  O   ASP A  41     9171   8312   8301  -1355    787   -585       O
ATOM   2140  CB  ASP A  41     -38.575  10.062  -7.501  1.00 79.15           C
ANISOU 2140  CB  ASP A  41    10868   9632   9574  -1641   1031   -691       C
ATOM   2141  CG  ASP A  41     -39.892  10.143  -8.237  1.00 84.88           C
ANISOU 2141  CG  ASP A  41    11444  10477  10328  -1738   1082   -802       C
ATOM   2142  OD1 ASP A  41     -40.260   9.161  -8.915  1.00 86.49           O
ANISOU 2142  OD1 ASP A  41    11682  10671  10508  -1819   1142   -842       O
ATOM   2143  OD2 ASP A  41     -40.555  11.197  -8.145  1.00 89.18           O
ANISOU 2143  OD2 ASP A  41    11837  11128  10918  -1730   1059   -853       O
ATOM   2144  N   ARG A  42     -37.673  11.502 -10.433  1.00 69.88           N
ANISOU 2144  N   ARG A  42     9367   8614   8572  -1423    821   -641       N
ATOM   2145  CA  ARG A  42     -37.682  12.706 -11.245  1.00 65.84           C
ANISOU 2145  CA  ARG A  42     8683   8200   8135  -1338    737   -642       C
ATOM   2146  C   ARG A  42     -39.086  13.150 -11.636  1.00 65.70           C
ANISOU 2146  C   ARG A  42     8517   8306   8139  -1403    768   -749       C
ATOM   2147  O   ARG A  42     -39.224  14.154 -12.341  1.00 70.07           O
ANISOU 2147  O   ARG A  42     8933   8944   8747  -1331    700   -760       O
ATOM   2148  CB  ARG A  42     -36.817  12.491 -12.492  1.00 60.83           C
ANISOU 2148  CB  ARG A  42     8035   7548   7530  -1262    677   -590       C
ATOM   2149  CG  ARG A  42     -35.324  12.522 -12.178  1.00 60.78           C
ANISOU 2149  CG  ARG A  42     8121   7451   7521  -1160    614   -490       C
ATOM   2150  CD  ARG A  42     -34.468  12.170 -13.380  1.00 63.27           C
ANISOU 2150  CD  ARG A  42     8433   7747   7859  -1098    566   -446       C
ATOM   2151  NE  ARG A  42     -33.047  12.137 -13.038  1.00 68.72           N
ANISOU 2151  NE  ARG A  42     9209   8359   8544  -1004    510   -366       N
ATOM   2152  CZ  ARG A  42     -32.130  12.948 -13.564  1.00 75.41           C
ANISOU 2152  CZ  ARG A  42     9988   9224   9441   -903    428   -321       C
ATOM   2153  NH1 ARG A  42     -32.485  13.863 -14.458  1.00 78.18           N
ANISOU 2153  NH1 ARG A  42    10200   9659   9847   -879    393   -340       N
ATOM   2154  NH2 ARG A  42     -30.857  12.845 -13.199  1.00 71.57           N
ANISOU 2154  NH2 ARG A  42     9576   8672   8945   -824    383   -262       N
ATOM   2155  N   SER A  43     -40.128  12.465 -11.151  1.00 60.98           N
ANISOU 2155  N   SER A  43     7949   7723   7498  -1534    869   -834       N
ATOM   2156  CA  SER A  43     -41.485  12.736 -11.611  1.00 63.76           C
ANISOU 2156  CA  SER A  43     8154   8203   7867  -1602    902   -954       C
ATOM   2157  C   SER A  43     -41.883  14.191 -11.403  1.00 65.71           C
ANISOU 2157  C   SER A  43     8260   8547   8161  -1531    840   -980       C
ATOM   2158  O   SER A  43     -42.669  14.739 -12.183  1.00 68.07           O
ANISOU 2158  O   SER A  43     8409   8960   8493  -1517    814  -1056       O
ATOM   2159  CB  SER A  43     -42.467  11.833 -10.882  1.00 68.19           C
ANISOU 2159  CB  SER A  43     8781   8760   8370  -1763   1030  -1044       C
ATOM   2160  OG  SER A  43     -42.638  12.309  -9.561  1.00 68.95           O
ANISOU 2160  OG  SER A  43     8911   8842   8445  -1782   1054  -1047       O
ATOM   2161  N   GLN A  44     -41.372  14.827 -10.356  1.00 59.64           N
ANISOU 2161  N   GLN A  44     7536   7734   7391  -1484    814   -924       N
ATOM   2162  CA  GLN A  44     -41.668  16.236 -10.153  1.00 59.39           C
ANISOU 2162  CA  GLN A  44     7381   7785   7402  -1409    751   -941       C
ATOM   2163  C   GLN A  44     -41.410  17.033 -11.414  1.00 62.67           C
ANISOU 2163  C   GLN A  44     7683   8258   7872  -1298    655   -922       C
ATOM   2164  O   GLN A  44     -42.193  17.918 -11.773  1.00 67.49           O
ANISOU 2164  O   GLN A  44     8159   8975   8510  -1265    622   -989       O
ATOM   2165  CB  GLN A  44     -40.816  16.777  -9.024  1.00 68.65           C
ANISOU 2165  CB  GLN A  44     8632   8883   8570  -1352    720   -858       C
ATOM   2166  CG  GLN A  44     -41.290  18.082  -8.496  1.00 70.92           C
ANISOU 2166  CG  GLN A  44     8815   9245   8886  -1307    682   -889       C
ATOM   2167  CD  GLN A  44     -41.061  18.151  -7.029  1.00 68.67           C
ANISOU 2167  CD  GLN A  44     8624   8900   8569  -1331    713   -861       C
ATOM   2168  OE1 GLN A  44     -40.302  18.990  -6.540  1.00 70.84           O
ANISOU 2168  OE1 GLN A  44     8908   9144   8864  -1242    651   -793       O
ATOM   2169  NE2 GLN A  44     -41.684  17.233  -6.307  1.00 65.95           N
ANISOU 2169  NE2 GLN A  44     8358   8530   8169  -1456    815   -914       N
ATOM   2170  N   TRP A  45     -40.314  16.720 -12.104  1.00 63.88           N
ANISOU 2170  N   TRP A  45     7895   8340   8035  -1236    612   -834       N
ATOM   2171  CA  TRP A  45     -39.924  17.411 -13.325  1.00 58.89           C
ANISOU 2171  CA  TRP A  45     7180   7745   7449  -1133    527   -805       C
ATOM   2172  C   TRP A  45     -40.574  16.766 -14.545  1.00 56.33           C
ANISOU 2172  C   TRP A  45     6797   7479   7125  -1173    546   -870       C
ATOM   2173  O   TRP A  45     -41.306  17.435 -15.278  1.00 65.64           O
ANISOU 2173  O   TRP A  45     7854   8759   8329  -1137    510   -933       O
ATOM   2174  CB  TRP A  45     -38.392  17.435 -13.427  1.00 56.92           C
ANISOU 2174  CB  TRP A  45     7016   7397   7212  -1050    473   -686       C
ATOM   2175  CG  TRP A  45     -37.828  17.654 -14.805  1.00 55.46           C
ANISOU 2175  CG  TRP A  45     6789   7222   7060   -973    410   -650       C
ATOM   2176  CD1 TRP A  45     -37.055  16.783 -15.509  1.00 59.60           C
ANISOU 2176  CD1 TRP A  45     7378   7687   7579   -969    409   -603       C
ATOM   2177  CD2 TRP A  45     -37.968  18.825 -15.632  1.00 57.14           C
ANISOU 2177  CD2 TRP A  45     6895   7504   7313   -887    340   -658       C
ATOM   2178  NE1 TRP A  45     -36.713  17.327 -16.723  1.00 62.90           N
ANISOU 2178  NE1 TRP A  45     7732   8135   8032   -893    347   -583       N
ATOM   2179  CE2 TRP A  45     -37.263  18.579 -16.825  1.00 61.59           C
ANISOU 2179  CE2 TRP A  45     7466   8044   7891   -842    304   -614       C
ATOM   2180  CE3 TRP A  45     -38.628  20.048 -15.485  1.00 55.63           C
ANISOU 2180  CE3 TRP A  45     6611   7388   7140   -842    303   -699       C
ATOM   2181  CZ2 TRP A  45     -37.201  19.516 -17.870  1.00 56.04           C
ANISOU 2181  CZ2 TRP A  45     6689   7386   7218   -756    238   -608       C
ATOM   2182  CZ3 TRP A  45     -38.564  20.981 -16.527  1.00 53.78           C
ANISOU 2182  CZ3 TRP A  45     6306   7196   6933   -750    234   -693       C
ATOM   2183  CH2 TRP A  45     -37.850  20.707 -17.697  1.00 49.54           C
ANISOU 2183  CH2 TRP A  45     5787   6628   6406   -710    204   -646       C
ATOM   2184  N   LEU A  46     -40.358  15.458 -14.743  1.00 55.19           N
ANISOU 2184  N   LEU A  46     6745   7274   6950  -1245    603   -861       N
ATOM   2185  CA  LEU A  46     -40.901  14.742 -15.898  1.00 52.88           C
ANISOU 2185  CA  LEU A  46     6408   7029   6656  -1289    626   -920       C
ATOM   2186  C   LEU A  46     -42.411  14.910 -16.052  1.00 54.33           C
ANISOU 2186  C   LEU A  46     6466   7340   6837  -1354    663  -1058       C
ATOM   2187  O   LEU A  46     -42.950  14.615 -17.119  1.00 66.79           O
ANISOU 2187  O   LEU A  46     7971   8985   8423  -1366    663  -1120       O
ATOM   2188  CB  LEU A  46     -40.567  13.250 -15.798  1.00 52.29           C
ANISOU 2188  CB  LEU A  46     6470   6862   6538  -1378    701   -900       C
ATOM   2189  CG  LEU A  46     -39.096  12.908 -15.537  1.00 53.66           C
ANISOU 2189  CG  LEU A  46     6778   6907   6702  -1318    671   -778       C
ATOM   2190  CD1 LEU A  46     -38.903  11.420 -15.380  1.00 52.96           C
ANISOU 2190  CD1 LEU A  46     6834   6730   6561  -1405    747   -770       C
ATOM   2191  CD2 LEU A  46     -38.219  13.410 -16.647  1.00 49.57           C
ANISOU 2191  CD2 LEU A  46     6215   6391   6228  -1204    581   -713       C
ATOM   2192  N   SER A  47     -43.103  15.364 -15.013  1.00 55.19           N
ANISOU 2192  N   SER A  47     6545   7489   6936  -1394    695  -1113       N
ATOM   2193  CA  SER A  47     -44.505  15.755 -15.140  1.00 56.25           C
ANISOU 2193  CA  SER A  47     6537   7761   7073  -1433    714  -1252       C
ATOM   2194  C   SER A  47     -44.682  16.855 -16.180  1.00 66.31           C
ANISOU 2194  C   SER A  47     7680   9127   8389  -1307    612  -1269       C
ATOM   2195  O   SER A  47     -45.451  16.706 -17.133  1.00 82.61           O
ANISOU 2195  O   SER A  47     9648  11285  10456  -1314    608  -1359       O
ATOM   2196  CB  SER A  47     -45.023  16.234 -13.785  1.00 59.34           C
ANISOU 2196  CB  SER A  47     6924   8172   7450  -1476    751  -1292       C
ATOM   2197  OG  SER A  47     -45.508  15.162 -13.027  1.00 75.62           O
ANISOU 2197  OG  SER A  47     9064  10204   9466  -1627    868  -1347       O
ATOM   2198  N   GLU A  48     -43.996  17.988 -15.997  1.00 61.33           N
ANISOU 2198  N   GLU A  48     7048   8470   7784  -1189    530  -1188       N
ATOM   2199  CA  GLU A  48     -44.167  19.145 -16.866  1.00 56.65           C
ANISOU 2199  CA  GLU A  48     6352   7952   7221  -1065    435  -1200       C
ATOM   2200  C   GLU A  48     -43.168  19.208 -18.012  1.00 57.18           C
ANISOU 2200  C   GLU A  48     6453   7966   7308   -976    371  -1108       C
ATOM   2201  O   GLU A  48     -43.308  20.090 -18.863  1.00 60.75           O
ANISOU 2201  O   GLU A  48     6834   8472   7775   -875    296  -1118       O
ATOM   2202  CB  GLU A  48     -44.041  20.439 -16.068  1.00 57.11           C
ANISOU 2202  CB  GLU A  48     6391   8015   7294   -987    385  -1172       C
ATOM   2203  CG  GLU A  48     -44.291  20.274 -14.606  1.00 64.02           C
ANISOU 2203  CG  GLU A  48     7306   8869   8150  -1071    451  -1190       C
ATOM   2204  CD  GLU A  48     -44.374  21.595 -13.871  1.00 67.71           C
ANISOU 2204  CD  GLU A  48     7732   9362   8632   -996    401  -1184       C
ATOM   2205  OE1 GLU A  48     -45.387  21.812 -13.174  1.00 78.03           O
ANISOU 2205  OE1 GLU A  48     8974  10746   9927  -1044    436  -1282       O
ATOM   2206  OE2 GLU A  48     -43.430  22.403 -13.966  1.00 64.70           O
ANISOU 2206  OE2 GLU A  48     7387   8924   8273   -894    332  -1086       O
ATOM   2207  N   LYS A  49     -42.174  18.311 -18.048  1.00 53.15           N
ANISOU 2207  N   LYS A  49     6055   7349   6792  -1009    398  -1021       N
ATOM   2208  CA  LYS A  49     -41.035  18.453 -18.958  1.00 54.52           C
ANISOU 2208  CA  LYS A  49     6270   7459   6985   -924    338   -922       C
ATOM   2209  C   LYS A  49     -41.461  18.852 -20.368  1.00 52.42           C
ANISOU 2209  C   LYS A  49     5915   7271   6730   -856    282   -964       C
ATOM   2210  O   LYS A  49     -40.854  19.733 -20.985  1.00 53.33           O
ANISOU 2210  O   LYS A  49     6027   7372   6866   -750    210   -906       O
ATOM   2211  CB  LYS A  49     -40.234  17.152 -19.008  1.00 56.27           C
ANISOU 2211  CB  LYS A  49     6604   7585   7191   -985    385   -864       C
ATOM   2212  CG  LYS A  49     -39.011  17.242 -19.891  1.00 54.75           C
ANISOU 2212  CG  LYS A  49     6455   7330   7019   -903    328   -768       C
ATOM   2213  CD  LYS A  49     -38.003  16.141 -19.609  1.00 51.23           C
ANISOU 2213  CD  LYS A  49     6134   6775   6557   -943    364   -696       C
ATOM   2214  CE  LYS A  49     -37.158  15.882 -20.846  1.00 54.09           C
ANISOU 2214  CE  LYS A  49     6512   7106   6934   -890    324   -643       C
ATOM   2215  NZ  LYS A  49     -35.819  15.311 -20.551  1.00 57.20           N
ANISOU 2215  NZ  LYS A  49     7017   7392   7322   -876    323   -553       N
ATOM   2216  N   PHE A  50     -42.522  18.241 -20.882  1.00 46.34           N
ANISOU 2216  N   PHE A  50     5075   6585   5945   -915    317  -1071       N
ATOM   2217  CA  PHE A  50     -42.983  18.533 -22.226  1.00 44.81           C
ANISOU 2217  CA  PHE A  50     4799   6470   5757   -849    265  -1121       C
ATOM   2218  C   PHE A  50     -44.231  19.406 -22.250  1.00 47.93           C
ANISOU 2218  C   PHE A  50     5070   6994   6148   -807    232  -1237       C
ATOM   2219  O   PHE A  50     -44.938  19.427 -23.258  1.00 60.37           O
ANISOU 2219  O   PHE A  50     6563   8659   7717   -774    204  -1317       O
ATOM   2220  CB  PHE A  50     -43.221  17.229 -22.973  1.00 47.97           C
ANISOU 2220  CB  PHE A  50     5204   6878   6143   -931    316  -1162       C
ATOM   2221  CG  PHE A  50     -41.994  16.408 -23.109  1.00 51.75           C
ANISOU 2221  CG  PHE A  50     5802   7236   6625   -953    336  -1053       C
ATOM   2222  CD1 PHE A  50     -41.070  16.693 -24.113  1.00 47.42           C
ANISOU 2222  CD1 PHE A  50     5280   6644   6093   -863    273   -971       C
ATOM   2223  CD2 PHE A  50     -41.732  15.379 -22.211  1.00 47.76           C
ANISOU 2223  CD2 PHE A  50     5390   6656   6100  -1058    416  -1032       C
ATOM   2224  CE1 PHE A  50     -39.912  15.955 -24.237  1.00 51.88           C
ANISOU 2224  CE1 PHE A  50     5948   7105   6660   -877    287   -877       C
ATOM   2225  CE2 PHE A  50     -40.582  14.636 -22.326  1.00 51.47           C
ANISOU 2225  CE2 PHE A  50     5973   7016   6567  -1064    426   -936       C
ATOM   2226  CZ  PHE A  50     -39.668  14.919 -23.352  1.00 56.15           C
ANISOU 2226  CZ  PHE A  50     6577   7576   7182   -973    360   -861       C
ATOM   2227  N   LYS A  51     -44.500  20.150 -21.178  1.00 42.00           N
ANISOU 2227  N   LYS A  51     4302   6258   5398   -799    231  -1251       N
ATOM   2228  CA  LYS A  51     -45.681  21.003 -21.101  1.00 50.40           C
ANISOU 2228  CA  LYS A  51     5248   7447   6456   -754    198  -1366       C
ATOM   2229  C   LYS A  51     -45.332  22.464 -20.829  1.00 57.41           C
ANISOU 2229  C   LYS A  51     6139   8319   7355   -630    119  -1311       C
ATOM   2230  O   LYS A  51     -46.188  23.238 -20.382  1.00 63.95           O
ANISOU 2230  O   LYS A  51     6890   9232   8177   -596     98  -1393       O
ATOM   2231  CB  LYS A  51     -46.635  20.481 -20.034  1.00 50.47           C
ANISOU 2231  CB  LYS A  51     5214   7513   6449   -877    283  -1471       C
ATOM   2232  CG  LYS A  51     -47.108  19.072 -20.301  1.00 59.45           C
ANISOU 2232  CG  LYS A  51     6347   8672   7570  -1009    369  -1543       C
ATOM   2233  CD  LYS A  51     -47.896  18.590 -19.092  1.00 59.46           C
ANISOU 2233  CD  LYS A  51     6333   8706   7552  -1143    465  -1632       C
ATOM   2234  CE  LYS A  51     -48.511  17.230 -19.308  1.00 48.21           C
ANISOU 2234  CE  LYS A  51     4902   7312   6105  -1287    562  -1724       C
ATOM   2235  NZ  LYS A  51     -49.273  16.944 -18.053  1.00 60.11           N
ANISOU 2235  NZ  LYS A  51     6400   8850   7590  -1414    656  -1811       N
ATOM   2236  N   LEU A  52     -44.091  22.858 -21.089  1.00 52.50           N
ANISOU 2236  N   LEU A  52     5607   7593   6748   -564     79  -1180       N
ATOM   2237  CA  LEU A  52     -43.652  24.221 -20.865  1.00 51.11           C
ANISOU 2237  CA  LEU A  52     5450   7389   6581   -455     11  -1122       C
ATOM   2238  C   LEU A  52     -43.376  24.961 -22.159  1.00 50.50           C
ANISOU 2238  C   LEU A  52     5376   7313   6500   -332    -69  -1093       C
ATOM   2239  O   LEU A  52     -43.015  26.140 -22.113  1.00 55.10           O
ANISOU 2239  O   LEU A  52     5985   7867   7084   -237   -125  -1046       O
ATOM   2240  CB  LEU A  52     -42.401  24.229 -19.976  1.00 45.45           C
ANISOU 2240  CB  LEU A  52     4838   6550   5881   -480     33  -1000       C
ATOM   2241  CG  LEU A  52     -42.694  23.711 -18.586  1.00 47.70           C
ANISOU 2241  CG  LEU A  52     5133   6829   6162   -583    104  -1026       C
ATOM   2242  CD1 LEU A  52     -41.418  23.555 -17.790  1.00 63.35           C
ANISOU 2242  CD1 LEU A  52     7224   8691   8156   -604    123   -910       C
ATOM   2243  CD2 LEU A  52     -43.599  24.698 -17.925  1.00 42.16           C
ANISOU 2243  CD2 LEU A  52     4357   6207   5456   -547     82  -1100       C
ATOM   2244  N   GLY A  53     -43.536  24.303 -23.307  1.00 51.75           N
ANISOU 2244  N   GLY A  53     5516   7498   6650   -334    -72  -1120       N
ATOM   2245  CA  GLY A  53     -43.290  24.945 -24.578  1.00 48.48           C
ANISOU 2245  CA  GLY A  53     5114   7081   6225   -220   -145  -1093       C
ATOM   2246  C   GLY A  53     -41.830  25.174 -24.908  1.00 57.13           C
ANISOU 2246  C   GLY A  53     6319   8053   7336   -188   -160   -955       C
ATOM   2247  O   GLY A  53     -41.518  26.055 -25.712  1.00 69.17           O
ANISOU 2247  O   GLY A  53     7874   9558   8848    -85   -220   -920       O
ATOM   2248  N   LEU A  54     -40.929  24.397 -24.313  1.00 58.80           N
ANISOU 2248  N   LEU A  54     6592   8181   7567   -274   -105   -882       N
ATOM   2249  CA  LEU A  54     -39.496  24.508 -24.551  1.00 51.51           C
ANISOU 2249  CA  LEU A  54     5764   7148   6660   -255   -112   -763       C
ATOM   2250  C   LEU A  54     -39.122  23.667 -25.761  1.00 51.00           C
ANISOU 2250  C   LEU A  54     5718   7066   6592   -266   -108   -744       C
ATOM   2251  O   LEU A  54     -39.599  22.536 -25.913  1.00 53.11           O
ANISOU 2251  O   LEU A  54     5956   7368   6856   -341    -65   -794       O
ATOM   2252  CB  LEU A  54     -38.710  24.031 -23.321  1.00 52.61           C
ANISOU 2252  CB  LEU A  54     5958   7213   6818   -331    -62   -702       C
ATOM   2253  CG  LEU A  54     -39.005  24.717 -21.983  1.00 41.26           C
ANISOU 2253  CG  LEU A  54     4509   5785   5384   -335    -56   -716       C
ATOM   2254  CD1 LEU A  54     -38.351  23.984 -20.817  1.00 40.24           C
ANISOU 2254  CD1 LEU A  54     4436   5589   5264   -418     -1   -669       C
ATOM   2255  CD2 LEU A  54     -38.501  26.135 -22.053  1.00 39.72           C
ANISOU 2255  CD2 LEU A  54     4339   5560   5194   -237   -113   -666       C
ATOM   2256  N   ASP A  55     -38.264  24.221 -26.624  1.00 41.15           N
ANISOU 2256  N   ASP A  55     4524   5764   5345   -197   -147   -675       N
ATOM   2257  CA  ASP A  55     -37.910  23.499 -27.843  1.00 50.26           C
ANISOU 2257  CA  ASP A  55     5697   6905   6496   -201   -146   -659       C
ATOM   2258  C   ASP A  55     -37.148  22.218 -27.518  1.00 57.76           C
ANISOU 2258  C   ASP A  55     6688   7796   7464   -296    -88   -616       C
ATOM   2259  O   ASP A  55     -37.446  21.150 -28.061  1.00 64.46           O
ANISOU 2259  O   ASP A  55     7519   8667   8306   -346    -61   -649       O
ATOM   2260  CB  ASP A  55     -37.093  24.393 -28.779  1.00 54.72           C
ANISOU 2260  CB  ASP A  55     6321   7417   7054   -114   -193   -594       C
ATOM   2261  CG  ASP A  55     -37.910  25.509 -29.384  1.00 56.00           C
ANISOU 2261  CG  ASP A  55     6458   7634   7185    -10   -254   -642       C
ATOM   2262  OD1 ASP A  55     -39.064  25.243 -29.808  1.00 56.56           O
ANISOU 2262  OD1 ASP A  55     6458   7798   7236      5   -269   -734       O
ATOM   2263  OD2 ASP A  55     -37.392  26.652 -29.425  1.00 49.81           O
ANISOU 2263  OD2 ASP A  55     5731   6802   6393     58   -286   -593       O
ATOM   2264  N   PHE A  56     -36.153  22.305 -26.634  1.00 54.12           N
ANISOU 2264  N   PHE A  56     6284   7258   7021   -316    -71   -544       N
ATOM   2265  CA  PHE A  56     -35.392  21.144 -26.179  1.00 50.59           C
ANISOU 2265  CA  PHE A  56     5888   6751   6584   -392    -22   -504       C
ATOM   2266  C   PHE A  56     -35.486  21.094 -24.661  1.00 52.31           C
ANISOU 2266  C   PHE A  56     6116   6954   6805   -439     10   -506       C
ATOM   2267  O   PHE A  56     -34.580  21.587 -23.964  1.00 47.13           O
ANISOU 2267  O   PHE A  56     5506   6240   6163   -420      2   -446       O
ATOM   2268  CB  PHE A  56     -33.932  21.218 -26.616  1.00 43.18           C
ANISOU 2268  CB  PHE A  56     5014   5731   5660   -364    -35   -417       C
ATOM   2269  CG  PHE A  56     -33.735  21.367 -28.075  1.00 41.10           C
ANISOU 2269  CG  PHE A  56     4752   5473   5392   -318    -64   -408       C
ATOM   2270  CD1 PHE A  56     -33.570  22.619 -28.642  1.00 40.93           C
ANISOU 2270  CD1 PHE A  56     4737   5449   5366   -239   -109   -390       C
ATOM   2271  CD2 PHE A  56     -33.668  20.238 -28.897  1.00 45.15           C
ANISOU 2271  CD2 PHE A  56     5269   5986   5900   -354    -45   -416       C
ATOM   2272  CE1 PHE A  56     -33.371  22.743 -30.016  1.00 42.29           C
ANISOU 2272  CE1 PHE A  56     4923   5620   5526   -196   -133   -380       C
ATOM   2273  CE2 PHE A  56     -33.471  20.360 -30.251  1.00 36.73           C
ANISOU 2273  CE2 PHE A  56     4206   4923   4827   -311    -71   -407       C
ATOM   2274  CZ  PHE A  56     -33.320  21.617 -30.805  1.00 40.40           C
ANISOU 2274  CZ  PHE A  56     4680   5384   5284   -232   -115   -388       C
ATOM   2275  N   PRO A  57     -36.541  20.483 -24.109  1.00 56.98           N
ANISOU 2275  N   PRO A  57     6670   7596   7382   -505     50   -578       N
ATOM   2276  CA  PRO A  57     -36.794  20.585 -22.665  1.00 52.20           C
ANISOU 2276  CA  PRO A  57     6073   6985   6774   -547     80   -590       C
ATOM   2277  C   PRO A  57     -35.588  20.137 -21.863  1.00 53.34           C
ANISOU 2277  C   PRO A  57     6307   7034   6924   -570    101   -512       C
ATOM   2278  O   PRO A  57     -34.892  19.188 -22.232  1.00 62.94           O
ANISOU 2278  O   PRO A  57     7578   8200   8138   -595    119   -476       O
ATOM   2279  CB  PRO A  57     -37.991  19.653 -22.455  1.00 46.69           C
ANISOU 2279  CB  PRO A  57     5335   6349   6056   -635    136   -682       C
ATOM   2280  CG  PRO A  57     -38.652  19.608 -23.786  1.00 41.88           C
ANISOU 2280  CG  PRO A  57     4661   5811   5442   -608    112   -738       C
ATOM   2281  CD  PRO A  57     -37.533  19.623 -24.769  1.00 50.00           C
ANISOU 2281  CD  PRO A  57     5737   6777   6482   -554     77   -658       C
ATOM   2282  N   ASN A  58     -35.327  20.847 -20.774  1.00 49.75           N
ANISOU 2282  N   ASN A  58     5868   6558   6476   -553     94   -488       N
ATOM   2283  CA  ASN A  58     -34.092  20.639 -20.035  1.00 47.53           C
ANISOU 2283  CA  ASN A  58     5666   6193   6201   -552     99   -415       C
ATOM   2284  C   ASN A  58     -34.116  21.506 -18.791  1.00 52.35           C
ANISOU 2284  C   ASN A  58     6276   6799   6815   -538     92   -409       C
ATOM   2285  O   ASN A  58     -34.920  22.434 -18.668  1.00 60.51           O
ANISOU 2285  O   ASN A  58     7248   7890   7852   -513     73   -449       O
ATOM   2286  CB  ASN A  58     -32.862  20.973 -20.889  1.00 52.64           C
ANISOU 2286  CB  ASN A  58     6338   6796   6868   -491     58   -351       C
ATOM   2287  CG  ASN A  58     -31.741  19.986 -20.687  1.00 52.78           C
ANISOU 2287  CG  ASN A  58     6432   6740   6881   -510     75   -302       C
ATOM   2288  OD1 ASN A  58     -31.793  19.171 -19.777  1.00 64.17           O
ANISOU 2288  OD1 ASN A  58     7924   8153   8304   -559    113   -306       O
ATOM   2289  ND2 ASN A  58     -30.709  20.072 -21.510  1.00 56.68           N
ANISOU 2289  ND2 ASN A  58     6943   7203   7391   -469     49   -259       N
ATOM   2290  N   LEU A  59     -33.202  21.204 -17.874  1.00 49.85           N
ANISOU 2290  N   LEU A  59     6029   6415   6496   -546    103   -361       N
ATOM   2291  CA  LEU A  59     -32.937  22.053 -16.735  1.00 45.64           C
ANISOU 2291  CA  LEU A  59     5504   5868   5969   -522     90   -342       C
ATOM   2292  C   LEU A  59     -31.463  22.436 -16.742  1.00 45.74           C
ANISOU 2292  C   LEU A  59     5557   5821   6000   -467     55   -275       C
ATOM   2293  O   LEU A  59     -30.603  21.559 -16.902  1.00 46.38           O
ANISOU 2293  O   LEU A  59     5693   5853   6076   -474     63   -243       O
ATOM   2294  CB  LEU A  59     -33.307  21.350 -15.422  1.00 51.76           C
ANISOU 2294  CB  LEU A  59     6327   6624   6717   -587    139   -361       C
ATOM   2295  CG  LEU A  59     -34.794  21.008 -15.304  1.00 48.63           C
ANISOU 2295  CG  LEU A  59     5885   6292   6300   -655    184   -441       C
ATOM   2296  CD1 LEU A  59     -35.004  19.904 -14.294  1.00 44.85           C
ANISOU 2296  CD1 LEU A  59     5484   5775   5783   -738    249   -455       C
ATOM   2297  CD2 LEU A  59     -35.595  22.242 -14.938  1.00 37.28           C
ANISOU 2297  CD2 LEU A  59     4370   4920   4874   -627    161   -482       C
ATOM   2298  N   PRO A  60     -31.122  23.716 -16.563  1.00 42.29           N
ANISOU 2298  N   PRO A  60     5095   5389   5585   -414     20   -257       N
ATOM   2299  CA  PRO A  60     -32.068  24.787 -16.224  1.00 41.80           C
ANISOU 2299  CA  PRO A  60     4978   5378   5526   -397      7   -293       C
ATOM   2300  C   PRO A  60     -32.846  25.319 -17.431  1.00 48.13           C
ANISOU 2300  C   PRO A  60     5722   6235   6330   -366    -16   -326       C
ATOM   2301  O   PRO A  60     -32.404  25.161 -18.570  1.00 45.41           O
ANISOU 2301  O   PRO A  60     5384   5880   5991   -345    -30   -307       O
ATOM   2302  CB  PRO A  60     -31.162  25.879 -15.650  1.00 41.26           C
ANISOU 2302  CB  PRO A  60     4923   5277   5476   -349    -22   -253       C
ATOM   2303  CG  PRO A  60     -29.851  25.698 -16.371  1.00 43.96           C
ANISOU 2303  CG  PRO A  60     5298   5573   5833   -324    -37   -207       C
ATOM   2304  CD  PRO A  60     -29.752  24.219 -16.778  1.00 33.64           C
ANISOU 2304  CD  PRO A  60     4023   4250   4510   -365    -11   -207       C
ATOM   2305  N   TYR A  61     -33.997  25.936 -17.197  1.00 47.47           N
ANISOU 2305  N   TYR A  61     5584   6213   6240   -359    -22   -380       N
ATOM   2306  CA  TYR A  61     -34.654  26.693 -18.248  1.00 52.49           C
ANISOU 2306  CA  TYR A  61     6171   6899   6872   -304    -58   -412       C
ATOM   2307  C   TYR A  61     -34.949  28.086 -17.730  1.00 52.26           C
ANISOU 2307  C   TYR A  61     6122   6888   6846   -248    -90   -421       C
ATOM   2308  O   TYR A  61     -35.005  28.312 -16.518  1.00 43.04           O
ANISOU 2308  O   TYR A  61     4957   5716   5682   -268    -77   -423       O
ATOM   2309  CB  TYR A  61     -35.949  26.032 -18.743  1.00 50.37           C
ANISOU 2309  CB  TYR A  61     5846   6707   6586   -336    -42   -490       C
ATOM   2310  CG  TYR A  61     -37.057  25.948 -17.699  1.00 48.76           C
ANISOU 2310  CG  TYR A  61     5597   6560   6371   -381    -13   -560       C
ATOM   2311  CD1 TYR A  61     -37.853  27.048 -17.394  1.00 41.34           C
ANISOU 2311  CD1 TYR A  61     4604   5677   5428   -333    -43   -606       C
ATOM   2312  CD2 TYR A  61     -37.312  24.755 -17.038  1.00 40.68           C
ANISOU 2312  CD2 TYR A  61     4590   5531   5335   -474     48   -583       C
ATOM   2313  CE1 TYR A  61     -38.863  26.953 -16.461  1.00 37.33           C
ANISOU 2313  CE1 TYR A  61     4049   5226   4908   -379    -13   -677       C
ATOM   2314  CE2 TYR A  61     -38.294  24.659 -16.101  1.00 47.22           C
ANISOU 2314  CE2 TYR A  61     5383   6409   6149   -526     83   -649       C
ATOM   2315  CZ  TYR A  61     -39.068  25.750 -15.817  1.00 47.63           C
ANISOU 2315  CZ  TYR A  61     5370   6524   6202   -480     53   -699       C
ATOM   2316  OH  TYR A  61     -40.055  25.617 -14.884  1.00 53.91           O
ANISOU 2316  OH  TYR A  61     6125   7374   6984   -538     92   -773       O
ATOM   2317  N   LEU A  62     -35.139  29.013 -18.674  1.00 52.38           N
ANISOU 2317  N   LEU A  62     6126   6921   6856   -176   -133   -426       N
ATOM   2318  CA  LEU A  62     -35.462  30.405 -18.381  1.00 48.01           C
ANISOU 2318  CA  LEU A  62     5563   6380   6297   -110   -170   -437       C
ATOM   2319  C   LEU A  62     -36.705  30.814 -19.153  1.00 54.61           C
ANISOU 2319  C   LEU A  62     6346   7294   7109    -54   -204   -508       C
ATOM   2320  O   LEU A  62     -36.811  30.536 -20.350  1.00 53.37           O
ANISOU 2320  O   LEU A  62     6189   7149   6940    -31   -219   -516       O
ATOM   2321  CB  LEU A  62     -34.324  31.353 -18.744  1.00 37.58           C
ANISOU 2321  CB  LEU A  62     4304   4989   4984    -61   -193   -370       C
ATOM   2322  CG  LEU A  62     -34.554  32.765 -18.191  1.00 42.00           C
ANISOU 2322  CG  LEU A  62     4870   5549   5538     -3   -221   -376       C
ATOM   2323  CD1 LEU A  62     -34.491  32.712 -16.685  1.00 39.37           C
ANISOU 2323  CD1 LEU A  62     4524   5213   5220    -46   -198   -376       C
ATOM   2324  CD2 LEU A  62     -33.513  33.726 -18.704  1.00 46.41           C
ANISOU 2324  CD2 LEU A  62     5498   6038   6099     40   -237   -319       C
ATOM   2325  N   ILE A  63     -37.635  31.481 -18.469  1.00 57.68           N
ANISOU 2325  N   ILE A  63     6691   7738   7489    -29   -219   -564       N
ATOM   2326  CA  ILE A  63     -38.821  32.049 -19.095  1.00 50.60           C
ANISOU 2326  CA  ILE A  63     5741   6920   6563     43   -263   -642       C
ATOM   2327  C   ILE A  63     -38.794  33.552 -18.880  1.00 54.43           C
ANISOU 2327  C   ILE A  63     6257   7387   7038    133   -309   -629       C
ATOM   2328  O   ILE A  63     -38.528  34.018 -17.768  1.00 43.54           O
ANISOU 2328  O   ILE A  63     4888   5982   5671    117   -297   -608       O
ATOM   2329  CB  ILE A  63     -40.110  31.450 -18.524  1.00 45.35           C
ANISOU 2329  CB  ILE A  63     4985   6355   5893     -4   -240   -742       C
ATOM   2330  CG1 ILE A  63     -40.215  29.969 -18.882  1.00 43.55           C
ANISOU 2330  CG1 ILE A  63     4736   6143   5669    -92   -192   -762       C
ATOM   2331  CG2 ILE A  63     -41.282  32.175 -19.078  1.00 49.26           C
ANISOU 2331  CG2 ILE A  63     5420   6938   6358     85   -294   -831       C
ATOM   2332  CD1 ILE A  63     -41.168  29.257 -17.978  1.00 43.68           C
ANISOU 2332  CD1 ILE A  63     4687   6228   5683   -176   -143   -844       C
ATOM   2333  N   ASP A  64     -39.062  34.309 -19.944  1.00 47.11           N
ANISOU 2333  N   ASP A  64     5351   6468   6080    229   -361   -642       N
ATOM   2334  CA  ASP A  64     -38.957  35.765 -19.884  1.00 50.94           C
ANISOU 2334  CA  ASP A  64     5891   6920   6546    320   -404   -623       C
ATOM   2335  C   ASP A  64     -39.714  36.342 -21.071  1.00 56.76           C
ANISOU 2335  C   ASP A  64     6634   7696   7236    431   -465   -672       C
ATOM   2336  O   ASP A  64     -39.244  36.242 -22.212  1.00 57.50           O
ANISOU 2336  O   ASP A  64     6783   7750   7314    456   -475   -636       O
ATOM   2337  CB  ASP A  64     -37.505  36.198 -19.906  1.00 52.63           C
ANISOU 2337  CB  ASP A  64     6201   7020   6774    306   -386   -522       C
ATOM   2338  CG  ASP A  64     -37.360  37.676 -19.775  1.00 62.05           C
ANISOU 2338  CG  ASP A  64     7460   8171   7946    386   -420   -503       C
ATOM   2339  OD1 ASP A  64     -38.280  38.279 -19.192  1.00 64.27           O
ANISOU 2339  OD1 ASP A  64     7702   8504   8212    434   -448   -560       O
ATOM   2340  OD2 ASP A  64     -36.340  38.234 -20.238  1.00 68.23           O
ANISOU 2340  OD2 ASP A  64     8333   8866   8724    398   -415   -437       O
ATOM   2341  N   GLY A  65     -40.864  36.951 -20.803  1.00 47.83           N
ANISOU 2341  N   GLY A  65     5450   6643   6079    501   -507   -755       N
ATOM   2342  CA  GLY A  65     -41.726  37.359 -21.892  1.00 52.29           C
ANISOU 2342  CA  GLY A  65     6010   7265   6595    614   -570   -820       C
ATOM   2343  C   GLY A  65     -42.070  36.161 -22.746  1.00 55.68           C
ANISOU 2343  C   GLY A  65     6382   7750   7025    575   -558   -860       C
ATOM   2344  O   GLY A  65     -42.505  35.121 -22.240  1.00 67.15           O
ANISOU 2344  O   GLY A  65     7744   9266   8505    483   -516   -909       O
ATOM   2345  N   ALA A  66     -41.854  36.301 -24.057  1.00 53.98           N
ANISOU 2345  N   ALA A  66     6228   7506   6777    642   -591   -839       N
ATOM   2346  CA  ALA A  66     -42.092  35.216 -25.001  1.00 55.33           C
ANISOU 2346  CA  ALA A  66     6355   7721   6947    613   -583   -871       C
ATOM   2347  C   ALA A  66     -40.916  34.256 -25.114  1.00 67.38           C
ANISOU 2347  C   ALA A  66     7918   9170   8513    501   -519   -782       C
ATOM   2348  O   ALA A  66     -41.098  33.126 -25.583  1.00 75.28           O
ANISOU 2348  O   ALA A  66     8869  10210   9525    444   -495   -808       O
ATOM   2349  CB  ALA A  66     -42.403  35.787 -26.383  1.00 56.97           C
ANISOU 2349  CB  ALA A  66     6617   7935   7096    741   -651   -891       C
ATOM   2350  N   HIS A  67     -39.726  34.680 -24.692  1.00 66.69           N
ANISOU 2350  N   HIS A  67     7915   8977   8446    471   -493   -683       N
ATOM   2351  CA  HIS A  67     -38.505  33.888 -24.807  1.00 59.90           C
ANISOU 2351  CA  HIS A  67     7097   8042   7622    380   -439   -601       C
ATOM   2352  C   HIS A  67     -38.450  32.788 -23.757  1.00 56.75           C
ANISOU 2352  C   HIS A  67     6633   7664   7266    263   -382   -607       C
ATOM   2353  O   HIS A  67     -38.442  33.075 -22.560  1.00 53.71           O
ANISOU 2353  O   HIS A  67     6233   7275   6899    235   -366   -605       O
ATOM   2354  CB  HIS A  67     -37.302  34.801 -24.649  1.00 49.98           C
ANISOU 2354  CB  HIS A  67     5945   6676   6369    391   -432   -511       C
ATOM   2355  CG  HIS A  67     -37.293  35.915 -25.632  1.00 49.08           C
ANISOU 2355  CG  HIS A  67     5920   6524   6205    498   -478   -499       C
ATOM   2356  ND1 HIS A  67     -37.312  37.238 -25.255  1.00 50.60           N
ANISOU 2356  ND1 HIS A  67     6173   6681   6373    567   -505   -489       N
ATOM   2357  CD2 HIS A  67     -37.304  35.903 -26.985  1.00 49.13           C
ANISOU 2357  CD2 HIS A  67     5974   6519   6174    552   -503   -497       C
ATOM   2358  CE1 HIS A  67     -37.313  37.998 -26.334  1.00 51.58           C
ANISOU 2358  CE1 HIS A  67     6388   6766   6443    658   -543   -479       C
ATOM   2359  NE2 HIS A  67     -37.306  37.211 -27.397  1.00 53.31           N
ANISOU 2359  NE2 HIS A  67     6600   7000   6654    652   -543   -483       N
ATOM   2360  N   ARG A  68     -38.365  31.537 -24.206  1.00 54.93           N
ANISOU 2360  N   ARG A  68     6375   7448   7049    196   -350   -612       N
ATOM   2361  CA  ARG A  68     -38.273  30.384 -23.314  1.00 50.46           C
ANISOU 2361  CA  ARG A  68     5769   6890   6514     85   -292   -616       C
ATOM   2362  C   ARG A  68     -37.053  29.558 -23.720  1.00 50.76           C
ANISOU 2362  C   ARG A  68     5861   6851   6572     27   -257   -539       C
ATOM   2363  O   ARG A  68     -37.099  28.832 -24.717  1.00 51.91           O
ANISOU 2363  O   ARG A  68     6002   7010   6711     19   -255   -548       O
ATOM   2364  CB  ARG A  68     -39.556  29.570 -23.368  1.00 47.38           C
ANISOU 2364  CB  ARG A  68     5284   6603   6113     52   -281   -718       C
ATOM   2365  CG  ARG A  68     -40.788  30.412 -23.157  1.00 57.74           C
ANISOU 2365  CG  ARG A  68     6533   8004   7401    123   -324   -809       C
ATOM   2366  CD  ARG A  68     -42.056  29.656 -23.502  1.00 68.68           C
ANISOU 2366  CD  ARG A  68     7819   9505   8772    101   -319   -925       C
ATOM   2367  NE  ARG A  68     -42.567  28.897 -22.363  1.00 72.70           N
ANISOU 2367  NE  ARG A  68     8268  10056   9298     -5   -259   -977       N
ATOM   2368  CZ  ARG A  68     -43.263  29.423 -21.363  1.00 76.09           C
ANISOU 2368  CZ  ARG A  68     8650  10537   9726     -3   -259  -1034       C
ATOM   2369  NH1 ARG A  68     -43.537  30.723 -21.350  1.00 78.64           N
ANISOU 2369  NH1 ARG A  68     8974  10876  10032    106   -321  -1047       N
ATOM   2370  NH2 ARG A  68     -43.680  28.645 -20.376  1.00 74.80           N
ANISOU 2370  NH2 ARG A  68     8444  10404   9573   -111   -195  -1079       N
ATOM   2371  N   LEU A  69     -35.983  29.650 -22.927  1.00 47.37           N
ANISOU 2371  N   LEU A  69     5480   6349   6168     -9   -232   -470       N
ATOM   2372  CA  LEU A  69     -34.679  29.077 -23.235  1.00 40.97           C
ANISOU 2372  CA  LEU A  69     4725   5464   5376    -48   -206   -399       C
ATOM   2373  C   LEU A  69     -34.349  27.907 -22.310  1.00 42.14           C
ANISOU 2373  C   LEU A  69     4868   5598   5546   -137   -158   -389       C
ATOM   2374  O   LEU A  69     -34.710  27.922 -21.138  1.00 48.44           O
ANISOU 2374  O   LEU A  69     5645   6411   6348   -167   -141   -408       O
ATOM   2375  CB  LEU A  69     -33.584  30.130 -23.090  1.00 44.27           C
ANISOU 2375  CB  LEU A  69     5209   5809   5803    -15   -217   -334       C
ATOM   2376  CG  LEU A  69     -33.740  31.499 -23.756  1.00 50.85           C
ANISOU 2376  CG  LEU A  69     6080   6632   6610     74   -259   -332       C
ATOM   2377  CD1 LEU A  69     -34.459  32.439 -22.831  1.00 47.41           C
ANISOU 2377  CD1 LEU A  69     5623   6225   6166    110   -280   -365       C
ATOM   2378  CD2 LEU A  69     -32.375  32.071 -24.071  1.00 55.27           C
ANISOU 2378  CD2 LEU A  69     6717   7106   7177     77   -249   -264       C
ATOM   2379  N   THR A  70     -33.677  26.881 -22.853  1.00 44.06           N
ANISOU 2379  N   THR A  70     5136   5810   5796   -177   -135   -360       N
ATOM   2380  CA  THR A  70     -32.879  25.906 -22.117  1.00 41.06           C
ANISOU 2380  CA  THR A  70     4786   5383   5431   -242    -96   -326       C
ATOM   2381  C   THR A  70     -31.418  26.083 -22.502  1.00 42.15           C
ANISOU 2381  C   THR A  70     4978   5453   5585   -225   -102   -260       C
ATOM   2382  O   THR A  70     -31.089  26.877 -23.386  1.00 42.61           O
ANISOU 2382  O   THR A  70     5052   5497   5641   -177   -127   -242       O
ATOM   2383  CB  THR A  70     -33.306  24.466 -22.402  1.00 44.69           C
ANISOU 2383  CB  THR A  70     5233   5864   5882   -304    -63   -355       C
ATOM   2384  OG1 THR A  70     -33.114  24.179 -23.797  1.00 45.46           O
ANISOU 2384  OG1 THR A  70     5334   5962   5976   -284    -76   -349       O
ATOM   2385  CG2 THR A  70     -34.752  24.235 -21.999  1.00 46.66           C
ANISOU 2385  CG2 THR A  70     5424   6188   6116   -335    -47   -434       C
ATOM   2386  N   GLN A  71     -30.548  25.317 -21.830  1.00 45.70           N
ANISOU 2386  N   GLN A  71     5460   5859   6046   -266    -78   -229       N
ATOM   2387  CA  GLN A  71     -29.093  25.388 -21.992  1.00 42.34           C
ANISOU 2387  CA  GLN A  71     5075   5376   5637   -255    -80   -179       C
ATOM   2388  C   GLN A  71     -28.495  26.542 -21.188  1.00 43.68           C
ANISOU 2388  C   GLN A  71     5257   5521   5820   -229    -93   -159       C
ATOM   2389  O   GLN A  71     -28.716  27.723 -21.509  1.00 42.79           O
ANISOU 2389  O   GLN A  71     5139   5414   5703   -189   -113   -160       O
ATOM   2390  CB  GLN A  71     -28.710  25.507 -23.473  1.00 34.13           C
ANISOU 2390  CB  GLN A  71     4044   4328   4595   -231    -92   -166       C
ATOM   2391  CG  GLN A  71     -29.138  24.323 -24.293  1.00 37.93           C
ANISOU 2391  CG  GLN A  71     4516   4829   5066   -258    -80   -184       C
ATOM   2392  CD  GLN A  71     -28.238  23.154 -24.032  1.00 45.91           C
ANISOU 2392  CD  GLN A  71     5559   5802   6085   -294    -58   -162       C
ATOM   2393  OE1 GLN A  71     -27.165  23.323 -23.442  1.00 43.32           O
ANISOU 2393  OE1 GLN A  71     5256   5435   5769   -288    -59   -134       O
ATOM   2394  NE2 GLN A  71     -28.659  21.958 -24.449  1.00 44.07           N
ANISOU 2394  NE2 GLN A  71     5325   5580   5839   -329    -39   -180       N
ATOM   2395  N   SER A  72     -27.703  26.202 -20.161  1.00 41.09           N
ANISOU 2395  N   SER A  72     4950   5163   5501   -247    -82   -141       N
ATOM   2396  CA  SER A  72     -27.223  27.218 -19.225  1.00 38.44           C
ANISOU 2396  CA  SER A  72     4619   4811   5177   -228    -91   -130       C
ATOM   2397  C   SER A  72     -26.424  28.310 -19.930  1.00 41.36           C
ANISOU 2397  C   SER A  72     5000   5157   5558   -197   -103   -111       C
ATOM   2398  O   SER A  72     -26.624  29.501 -19.659  1.00 48.29           O
ANISOU 2398  O   SER A  72     5878   6035   6437   -172   -114   -113       O
ATOM   2399  CB  SER A  72     -26.402  26.579 -18.106  1.00 40.37           C
ANISOU 2399  CB  SER A  72     4887   5027   5426   -245    -81   -118       C
ATOM   2400  OG  SER A  72     -25.485  25.625 -18.608  1.00 44.34           O
ANISOU 2400  OG  SER A  72     5413   5505   5931   -253    -76   -104       O
ATOM   2401  N   ASN A  73     -25.534  27.939 -20.855  1.00 41.36           N
ANISOU 2401  N   ASN A  73     5016   5135   5564   -200    -98    -96       N
ATOM   2402  CA  ASN A  73     -24.767  28.966 -21.555  1.00 38.99           C
ANISOU 2402  CA  ASN A  73     4735   4809   5270   -182    -99    -83       C
ATOM   2403  C   ASN A  73     -25.681  29.883 -22.362  1.00 41.15           C
ANISOU 2403  C   ASN A  73     5018   5095   5524   -151   -112    -89       C
ATOM   2404  O   ASN A  73     -25.463  31.098 -22.429  1.00 39.09           O
ANISOU 2404  O   ASN A  73     4783   4812   5259   -129   -115    -83       O
ATOM   2405  CB  ASN A  73     -23.733  28.322 -22.467  1.00 39.95           C
ANISOU 2405  CB  ASN A  73     4868   4911   5398   -197    -88    -74       C
ATOM   2406  CG  ASN A  73     -22.593  27.728 -21.716  1.00 45.91           C
ANISOU 2406  CG  ASN A  73     5621   5653   6171   -211    -82    -75       C
ATOM   2407  OD1 ASN A  73     -22.237  28.186 -20.630  1.00 50.90           O
ANISOU 2407  OD1 ASN A  73     6248   6281   6812   -208    -85    -79       O
ATOM   2408  ND2 ASN A  73     -22.012  26.687 -22.277  1.00 47.43           N
ANISOU 2408  ND2 ASN A  73     5817   5842   6365   -222    -77    -74       N
ATOM   2409  N   ALA A  74     -26.712  29.324 -22.988  1.00 42.61           N
ANISOU 2409  N   ALA A  74     5186   5312   5691   -144   -121   -105       N
ATOM   2410  CA  ALA A  74     -27.602  30.178 -23.761  1.00 41.64           C
ANISOU 2410  CA  ALA A  74     5073   5205   5543    -99   -142   -117       C
ATOM   2411  C   ALA A  74     -28.429  31.067 -22.842  1.00 46.32           C
ANISOU 2411  C   ALA A  74     5652   5819   6129    -71   -158   -137       C
ATOM   2412  O   ALA A  74     -28.698  32.221 -23.183  1.00 53.19           O
ANISOU 2412  O   ALA A  74     6552   6679   6980    -25   -176   -138       O
ATOM   2413  CB  ALA A  74     -28.484  29.332 -24.675  1.00 29.05           C
ANISOU 2413  CB  ALA A  74     3455   3650   3932    -95   -150   -140       C
ATOM   2414  N   ILE A  75     -28.785  30.570 -21.654  1.00 51.15           N
ANISOU 2414  N   ILE A  75     6228   6455   6753    -99   -152   -151       N
ATOM   2415  CA  ILE A  75     -29.468  31.401 -20.662  1.00 43.85           C
ANISOU 2415  CA  ILE A  75     5287   5550   5825    -78   -164   -170       C
ATOM   2416  C   ILE A  75     -28.568  32.545 -20.198  1.00 47.03           C
ANISOU 2416  C   ILE A  75     5726   5905   6237    -64   -163   -144       C
ATOM   2417  O   ILE A  75     -28.998  33.701 -20.137  1.00 44.15           O
ANISOU 2417  O   ILE A  75     5378   5539   5858    -22   -181   -151       O
ATOM   2418  CB  ILE A  75     -29.931  30.542 -19.475  1.00 36.35           C
ANISOU 2418  CB  ILE A  75     4300   4630   4883   -121   -148   -191       C
ATOM   2419  CG1 ILE A  75     -31.018  29.551 -19.914  1.00 32.70           C
ANISOU 2419  CG1 ILE A  75     3799   4219   4406   -140   -143   -231       C
ATOM   2420  CG2 ILE A  75     -30.416  31.432 -18.352  1.00 31.50           C
ANISOU 2420  CG2 ILE A  75     3671   4028   4268   -104   -157   -206       C
ATOM   2421  CD1 ILE A  75     -31.562  28.685 -18.777  1.00 36.57           C
ANISOU 2421  CD1 ILE A  75     4265   4734   4896   -193   -117   -257       C
ATOM   2422  N   LEU A  76     -27.306  32.241 -19.860  1.00 44.44           N
ANISOU 2422  N   LEU A  76     5413   5541   5931    -98   -143   -119       N
ATOM   2423  CA  LEU A  76     -26.364  33.295 -19.479  1.00 41.61           C
ANISOU 2423  CA  LEU A  76     5085   5141   5583    -94   -136   -103       C
ATOM   2424  C   LEU A  76     -26.102  34.272 -20.623  1.00 43.14           C
ANISOU 2424  C   LEU A  76     5330   5301   5759    -68   -136    -92       C
ATOM   2425  O   LEU A  76     -26.007  35.485 -20.403  1.00 45.25           O
ANISOU 2425  O   LEU A  76     5633   5543   6018    -48   -137    -89       O
ATOM   2426  CB  LEU A  76     -25.045  32.686 -19.017  1.00 47.55           C
ANISOU 2426  CB  LEU A  76     5834   5873   6361   -131   -117    -91       C
ATOM   2427  CG  LEU A  76     -25.044  31.825 -17.768  1.00 49.72           C
ANISOU 2427  CG  LEU A  76     6080   6164   6646   -152   -116    -97       C
ATOM   2428  CD1 LEU A  76     -23.782  31.039 -17.787  1.00 50.22           C
ANISOU 2428  CD1 LEU A  76     6148   6210   6725   -173   -106    -91       C
ATOM   2429  CD2 LEU A  76     -25.119  32.687 -16.519  1.00 52.35           C
ANISOU 2429  CD2 LEU A  76     6409   6497   6986   -143   -122   -104       C
ATOM   2430  N   ARG A  77     -25.926  33.770 -21.847  1.00 43.48           N
ANISOU 2430  N   ARG A  77     5390   5338   5793    -71   -131    -84       N
ATOM   2431  CA  ARG A  77     -25.718  34.701 -22.950  1.00 46.48           C
ANISOU 2431  CA  ARG A  77     5835   5680   6147    -46   -127    -74       C
ATOM   2432  C   ARG A  77     -26.945  35.593 -23.135  1.00 48.36           C
ANISOU 2432  C   ARG A  77     6096   5929   6348     18   -159    -88       C
ATOM   2433  O   ARG A  77     -26.806  36.776 -23.463  1.00 46.99           O
ANISOU 2433  O   ARG A  77     5991   5713   6150     46   -157    -79       O
ATOM   2434  CB  ARG A  77     -25.386  33.944 -24.235  1.00 43.69           C
ANISOU 2434  CB  ARG A  77     5494   5320   5787    -58   -117    -66       C
ATOM   2435  CG  ARG A  77     -24.014  33.300 -24.288  1.00 51.37           C
ANISOU 2435  CG  ARG A  77     6458   6273   6787   -112    -86    -57       C
ATOM   2436  CD  ARG A  77     -23.717  32.699 -25.693  1.00 62.37           C
ANISOU 2436  CD  ARG A  77     7871   7657   8169   -120    -76    -50       C
ATOM   2437  NE  ARG A  77     -23.127  31.352 -25.638  1.00 69.65           N
ANISOU 2437  NE  ARG A  77     8749   8598   9117   -155    -67    -52       N
ATOM   2438  CZ  ARG A  77     -22.982  30.531 -26.687  1.00 74.23           C
ANISOU 2438  CZ  ARG A  77     9330   9181   9691   -164    -62    -49       C
ATOM   2439  NH1 ARG A  77     -23.379  30.894 -27.907  1.00 66.97           N
ANISOU 2439  NH1 ARG A  77     8454   8251   8742   -141    -65    -43       N
ATOM   2440  NH2 ARG A  77     -22.436  29.331 -26.521  1.00 75.77           N
ANISOU 2440  NH2 ARG A  77     9491   9390   9908   -191    -56    -52       N
ATOM   2441  N   TYR A  78     -28.142  35.055 -22.882  1.00 45.20           N
ANISOU 2441  N   TYR A  78     5643   5588   5944     40   -186   -114       N
ATOM   2442  CA  TYR A  78     -29.366  35.843 -22.986  1.00 46.78           C
ANISOU 2442  CA  TYR A  78     5851   5814   6109    108   -222   -141       C
ATOM   2443  C   TYR A  78     -29.385  36.984 -21.980  1.00 49.23           C
ANISOU 2443  C   TYR A  78     6180   6105   6419    127   -227   -142       C
ATOM   2444  O   TYR A  78     -29.597  38.148 -22.343  1.00 58.09           O
ANISOU 2444  O   TYR A  78     7367   7196   7507    182   -243   -141       O
ATOM   2445  CB  TYR A  78     -30.583  34.950 -22.769  1.00 47.92           C
ANISOU 2445  CB  TYR A  78     5918   6037   6254    113   -242   -183       C
ATOM   2446  CG  TYR A  78     -31.869  35.734 -22.724  1.00 45.32           C
ANISOU 2446  CG  TYR A  78     5578   5750   5892    186   -283   -226       C
ATOM   2447  CD1 TYR A  78     -32.409  36.306 -23.879  1.00 49.14           C
ANISOU 2447  CD1 TYR A  78     6107   6233   6330    262   -317   -241       C
ATOM   2448  CD2 TYR A  78     -32.536  35.917 -21.531  1.00 44.02           C
ANISOU 2448  CD2 TYR A  78     5363   5625   5736    186   -291   -257       C
ATOM   2449  CE1 TYR A  78     -33.602  37.025 -23.828  1.00 55.19           C
ANISOU 2449  CE1 TYR A  78     6864   7046   7062    342   -363   -289       C
ATOM   2450  CE2 TYR A  78     -33.708  36.630 -21.463  1.00 47.51           C
ANISOU 2450  CE2 TYR A  78     5790   6114   6149    257   -331   -305       C
ATOM   2451  CZ  TYR A  78     -34.241  37.180 -22.601  1.00 55.84           C
ANISOU 2451  CZ  TYR A  78     6884   7173   7159    338   -369   -323       C
ATOM   2452  OH  TYR A  78     -35.412  37.886 -22.484  1.00 58.01           O
ANISOU 2452  OH  TYR A  78     7140   7500   7400    419   -415   -380       O
ATOM   2453  N   ILE A  79     -29.195  36.660 -20.702  1.00 50.71           N
ANISOU 2453  N   ILE A  79     6318   6309   6640     86   -214   -144       N
ATOM   2454  CA  ILE A  79     -29.215  37.673 -19.652  1.00 42.70           C
ANISOU 2454  CA  ILE A  79     5313   5282   5628    100   -218   -147       C
ATOM   2455  C   ILE A  79     -28.116  38.699 -19.896  1.00 46.64           C
ANISOU 2455  C   ILE A  79     5890   5707   6123     94   -196   -118       C
ATOM   2456  O   ILE A  79     -28.309  39.904 -19.686  1.00 52.40           O
ANISOU 2456  O   ILE A  79     6668   6409   6830    132   -205   -120       O
ATOM   2457  CB  ILE A  79     -29.084  36.998 -18.272  1.00 41.13           C
ANISOU 2457  CB  ILE A  79     5053   5110   5465     51   -204   -152       C
ATOM   2458  CG1 ILE A  79     -30.156  35.917 -18.073  1.00 38.63           C
ANISOU 2458  CG1 ILE A  79     4669   4860   5148     42   -213   -185       C
ATOM   2459  CG2 ILE A  79     -29.151  38.012 -17.136  1.00 39.46           C
ANISOU 2459  CG2 ILE A  79     4846   4890   5257     65   -209   -158       C
ATOM   2460  CD1 ILE A  79     -29.875  35.034 -16.852  1.00 34.11           C
ANISOU 2460  CD1 ILE A  79     4057   4300   4602    -15   -191   -185       C
ATOM   2461  N   ALA A  80     -26.951  38.244 -20.355  1.00 40.35           N
ANISOU 2461  N   ALA A  80     5110   4879   5344     44   -163    -96       N
ATOM   2462  CA  ALA A  80     -25.844  39.169 -20.568  1.00 47.34           C
ANISOU 2462  CA  ALA A  80     6063   5699   6226     23   -131    -79       C
ATOM   2463  C   ALA A  80     -26.145  40.126 -21.709  1.00 48.28           C
ANISOU 2463  C   ALA A  80     6278   5773   6295     70   -136    -72       C
ATOM   2464  O   ALA A  80     -25.877  41.330 -21.612  1.00 50.77           O
ANISOU 2464  O   ALA A  80     6666   6036   6589     81   -123    -67       O
ATOM   2465  CB  ALA A  80     -24.556  38.402 -20.854  1.00 51.17           C
ANISOU 2465  CB  ALA A  80     6533   6170   6740    -41    -96    -70       C
ATOM   2466  N   ARG A  81     -26.686  39.607 -22.801  1.00 43.67           N
ANISOU 2466  N   ARG A  81     5702   5204   5686    100   -154    -73       N
ATOM   2467  CA  ARG A  81     -27.095  40.473 -23.902  1.00 53.18           C
ANISOU 2467  CA  ARG A  81     7006   6367   6833    160   -167    -68       C
ATOM   2468  C   ARG A  81     -28.043  41.564 -23.421  1.00 57.65           C
ANISOU 2468  C   ARG A  81     7607   6932   7365    234   -203    -84       C
ATOM   2469  O   ARG A  81     -27.969  42.714 -23.870  1.00 53.81           O
ANISOU 2469  O   ARG A  81     7232   6382   6833    272   -199    -74       O
ATOM   2470  CB  ARG A  81     -27.765  39.635 -24.981  1.00 43.62           C
ANISOU 2470  CB  ARG A  81     5779   5193   5603    193   -193    -76       C
ATOM   2471  CG  ARG A  81     -27.107  39.661 -26.306  1.00 48.59           C
ANISOU 2471  CG  ARG A  81     6487   5770   6204    182   -167    -55       C
ATOM   2472  CD  ARG A  81     -27.907  38.786 -27.266  1.00 52.17           C
ANISOU 2472  CD  ARG A  81     6912   6271   6640    220   -201    -68       C
ATOM   2473  NE  ARG A  81     -27.546  37.391 -27.087  1.00 47.35           N
ANISOU 2473  NE  ARG A  81     6207   5705   6080    156   -185    -69       N
ATOM   2474  CZ  ARG A  81     -28.421  36.417 -26.962  1.00 43.26           C
ANISOU 2474  CZ  ARG A  81     5604   5259   5575    167   -213    -94       C
ATOM   2475  NH1 ARG A  81     -29.704  36.691 -26.994  1.00 44.37           N
ANISOU 2475  NH1 ARG A  81     5729   5443   5684    238   -259   -128       N
ATOM   2476  NH2 ARG A  81     -28.004  35.174 -26.805  1.00 54.61           N
ANISOU 2476  NH2 ARG A  81     6975   6722   7051    107   -194    -92       N
ATOM   2477  N   LYS A  82     -28.925  41.214 -22.482  1.00 59.62           N
ANISOU 2477  N   LYS A  82     7767   7250   7635    253   -235   -110       N
ATOM   2478  CA  LYS A  82     -29.999  42.100 -22.059  1.00 50.39           C
ANISOU 2478  CA  LYS A  82     6612   6099   6434    332   -278   -136       C
ATOM   2479  C   LYS A  82     -29.463  43.283 -21.262  1.00 52.77           C
ANISOU 2479  C   LYS A  82     6972   6344   6735    324   -258   -123       C
ATOM   2480  O   LYS A  82     -29.986  44.394 -21.369  1.00 61.82           O
ANISOU 2480  O   LYS A  82     8194   7460   7834    396   -282   -131       O
ATOM   2481  CB  LYS A  82     -31.005  41.277 -21.256  1.00 47.23           C
ANISOU 2481  CB  LYS A  82     6092   5793   6061    336   -306   -175       C
ATOM   2482  CG  LYS A  82     -32.090  42.040 -20.571  1.00 48.25           C
ANISOU 2482  CG  LYS A  82     6206   5958   6169    405   -347   -213       C
ATOM   2483  CD  LYS A  82     -33.268  41.128 -20.356  1.00 51.64           C
ANISOU 2483  CD  LYS A  82     6527   6488   6607    418   -376   -265       C
ATOM   2484  CE  LYS A  82     -34.078  41.534 -19.141  1.00 52.70           C
ANISOU 2484  CE  LYS A  82     6604   6671   6747    440   -396   -305       C
ATOM   2485  NZ  LYS A  82     -35.398  40.827 -19.105  1.00 58.18           N
ANISOU 2485  NZ  LYS A  82     7201   7468   7436    463   -425   -374       N
ATOM   2486  N   HIS A  83     -28.408  43.069 -20.482  1.00 54.86           N
ANISOU 2486  N   HIS A  83     7205   6591   7047    242   -215   -107       N
ATOM   2487  CA  HIS A  83     -27.825  44.084 -19.613  1.00 52.08           C
ANISOU 2487  CA  HIS A  83     6891   6194   6702    221   -191   -100       C
ATOM   2488  C   HIS A  83     -26.462  44.522 -20.106  1.00 54.83           C
ANISOU 2488  C   HIS A  83     7317   6465   7049    160   -134    -78       C
ATOM   2489  O   HIS A  83     -25.675  45.075 -19.336  1.00 60.96           O
ANISOU 2489  O   HIS A  83     8103   7213   7846    114   -101    -78       O
ATOM   2490  CB  HIS A  83     -27.729  43.563 -18.180  1.00 42.60           C
ANISOU 2490  CB  HIS A  83     5589   5044   5555    178   -189   -112       C
ATOM   2491  CG  HIS A  83     -29.038  43.078 -17.652  1.00 58.50           C
ANISOU 2491  CG  HIS A  83     7524   7135   7570    222   -233   -140       C
ATOM   2492  ND1 HIS A  83     -29.994  43.931 -17.148  1.00 58.44           N
ANISOU 2492  ND1 HIS A  83     7524   7142   7537    286   -267   -164       N
ATOM   2493  CD2 HIS A  83     -29.584  41.841 -17.620  1.00 62.83           C
ANISOU 2493  CD2 HIS A  83     7986   7749   8136    208   -246   -156       C
ATOM   2494  CE1 HIS A  83     -31.061  43.236 -16.803  1.00 62.77           C
ANISOU 2494  CE1 HIS A  83     7987   7770   8092    307   -298   -198       C
ATOM   2495  NE2 HIS A  83     -30.838  41.965 -17.075  1.00 63.69           N
ANISOU 2495  NE2 HIS A  83     8050   7916   8234    257   -282   -193       N
ATOM   2496  N   ASN A  84     -26.166  44.247 -21.370  1.00 56.22           N
ANISOU 2496  N   ASN A  84     7546   6614   7202    155   -119    -65       N
ATOM   2497  CA  ASN A  84     -24.967  44.746 -22.032  1.00 53.17           C
ANISOU 2497  CA  ASN A  84     7248   6151   6802     98    -60    -51       C
ATOM   2498  C   ASN A  84     -23.703  44.250 -21.329  1.00 58.46           C
ANISOU 2498  C   ASN A  84     7846   6833   7532      3    -15    -58       C
ATOM   2499  O   ASN A  84     -22.725  44.977 -21.170  1.00 62.76           O
ANISOU 2499  O   ASN A  84     8440   7328   8078    -52     36    -63       O
ATOM   2500  CB  ASN A  84     -25.020  46.263 -22.118  1.00 57.91           C
ANISOU 2500  CB  ASN A  84     7980   6672   7349    130    -47    -47       C
ATOM   2501  CG  ASN A  84     -24.000  46.814 -23.025  1.00 68.55           C
ANISOU 2501  CG  ASN A  84     9443   7936   8667     76     17    -36       C
ATOM   2502  OD1 ASN A  84     -23.469  46.101 -23.872  1.00 75.40           O
ANISOU 2502  OD1 ASN A  84    10304   8805   9541     37     41    -31       O
ATOM   2503  ND2 ASN A  84     -23.682  48.092 -22.847  1.00 72.18           N
ANISOU 2503  ND2 ASN A  84    10014   8320   9092     68     52    -37       N
ATOM   2504  N   LEU A  85     -23.730  42.984 -20.910  1.00 62.12           N
ANISOU 2504  N   LEU A  85     8196   7366   8041    -15    -33    -63       N
ATOM   2505  CA  LEU A  85     -22.631  42.344 -20.200  1.00 53.94           C
ANISOU 2505  CA  LEU A  85     7084   6353   7058    -87     -5    -75       C
ATOM   2506  C   LEU A  85     -21.849  41.391 -21.082  1.00 57.33           C
ANISOU 2506  C   LEU A  85     7495   6788   7500   -130     19    -74       C
ATOM   2507  O   LEU A  85     -21.360  40.363 -20.596  1.00 60.21           O
ANISOU 2507  O   LEU A  85     7775   7195   7905   -160     17    -84       O
ATOM   2508  CB  LEU A  85     -23.157  41.586 -18.991  1.00 49.25           C
ANISOU 2508  CB  LEU A  85     6389   5825   6499    -74    -41    -83       C
ATOM   2509  CG  LEU A  85     -23.724  42.446 -17.879  1.00 57.58           C
ANISOU 2509  CG  LEU A  85     7443   6882   7551    -45    -59    -90       C
ATOM   2510  CD1 LEU A  85     -23.931  41.578 -16.641  1.00 51.22           C
ANISOU 2510  CD1 LEU A  85     6541   6137   6783    -53    -81   -100       C
ATOM   2511  CD2 LEU A  85     -22.757  43.588 -17.622  1.00 61.30           C
ANISOU 2511  CD2 LEU A  85     7973   7298   8022    -83    -16    -98       C
ATOM   2512  N   CYS A  86     -21.748  41.696 -22.370  1.00 57.76           N
ANISOU 2512  N   CYS A  86     7632   6797   7518   -128     40    -63       N
ATOM   2513  CA  CYS A  86     -21.012  40.892 -23.333  1.00 59.75           C
ANISOU 2513  CA  CYS A  86     7876   7050   7777   -169     66    -63       C
ATOM   2514  C   CYS A  86     -19.699  41.586 -23.686  1.00 58.14           C
ANISOU 2514  C   CYS A  86     7728   6792   7569   -241    134    -81       C
ATOM   2515  O   CYS A  86     -19.486  42.767 -23.396  1.00 66.94           O
ANISOU 2515  O   CYS A  86     8911   7859   8665   -255    163    -88       O
ATOM   2516  CB  CYS A  86     -21.856  40.666 -24.594  1.00 73.64           C
ANISOU 2516  CB  CYS A  86     9686   8800   9493   -119     43    -44       C
ATOM   2517  SG  CYS A  86     -23.017  39.258 -24.550  1.00 88.82           S
ANISOU 2517  SG  CYS A  86    11512  10803  11432    -70    -19    -40       S
ATOM   2518  N   GLY A  87     -18.811  40.843 -24.331  1.00 44.23           N
ANISOU 2518  N   GLY A  87     5940   5040   5824   -291    164    -93       N
ATOM   2519  CA  GLY A  87     -17.623  41.466 -24.885  1.00 57.65           C
ANISOU 2519  CA  GLY A  87     7698   6693   7514   -364    235   -118       C
ATOM   2520  C   GLY A  87     -17.964  42.475 -25.969  1.00 65.80           C
ANISOU 2520  C   GLY A  87     8877   7644   8479   -352    263    -97       C
ATOM   2521  O   GLY A  87     -18.983  42.367 -26.657  1.00 64.63           O
ANISOU 2521  O   GLY A  87     8776   7487   8294   -284    224    -65       O
ATOM   2522  N   GLU A  88     -17.099  43.483 -26.115  1.00 68.12           N
ANISOU 2522  N   GLU A  88     9250   7879   8753   -419    333   -120       N
ATOM   2523  CA  GLU A  88     -17.310  44.551 -27.086  1.00 74.56           C
ANISOU 2523  CA  GLU A  88    10231   8603   9497   -414    371   -102       C
ATOM   2524  C   GLU A  88     -16.304  44.493 -28.228  1.00 69.17           C
ANISOU 2524  C   GLU A  88     9606   7882   8795   -494    445   -122       C
ATOM   2525  O   GLU A  88     -16.693  44.259 -29.374  1.00 83.05           O
ANISOU 2525  O   GLU A  88    11432   9613  10510   -464    439    -95       O
ATOM   2526  CB  GLU A  88     -17.268  45.918 -26.396  1.00 87.77           C
ANISOU 2526  CB  GLU A  88    11984  10219  11147   -426    400   -111       C
ATOM   2527  CG  GLU A  88     -17.866  45.915 -25.001  1.00101.27           C
ANISOU 2527  CG  GLU A  88    13604  11980  12894   -378    342   -110       C
ATOM   2528  CD  GLU A  88     -18.453  47.256 -24.614  1.00106.64           C
ANISOU 2528  CD  GLU A  88    14393  12596  13528   -339    341    -98       C
ATOM   2529  OE1 GLU A  88     -19.695  47.354 -24.501  1.00108.51           O
ANISOU 2529  OE1 GLU A  88    14647  12840  13740   -241    273    -69       O
ATOM   2530  OE2 GLU A  88     -17.673  48.211 -24.424  1.00107.32           O
ANISOU 2530  OE2 GLU A  88    14548  12626  13601   -408    409   -123       O
ATOM   2531  N   THR A  89     -15.017  44.688 -27.952  1.00 51.63           N
ANISOU 2531  N   THR A  89     7354   5662   6602   -596    516   -173       N
ATOM   2532  CA  THR A  89     -14.002  44.478 -28.972  1.00 51.93           C
ANISOU 2532  CA  THR A  89     7419   5681   6629   -680    588   -204       C
ATOM   2533  C   THR A  89     -13.949  43.019 -29.444  1.00 55.81           C
ANISOU 2533  C   THR A  89     7805   6244   7157   -662    549   -200       C
ATOM   2534  O   THR A  89     -14.524  42.100 -28.854  1.00 57.82           O
ANISOU 2534  O   THR A  89     7950   6566   7451   -599    474   -182       O
ATOM   2535  CB  THR A  89     -12.624  44.849 -28.447  1.00 52.50           C
ANISOU 2535  CB  THR A  89     7447   5766   6735   -793    666   -277       C
ATOM   2536  OG1 THR A  89     -12.199  43.828 -27.534  1.00 54.56           O
ANISOU 2536  OG1 THR A  89     7530   6128   7071   -790    624   -310       O
ATOM   2537  CG2 THR A  89     -12.664  46.204 -27.757  1.00 37.88           C
ANISOU 2537  CG2 THR A  89     5679   3855   4858   -813    701   -286       C
ATOM   2538  N   GLU A  90     -13.203  42.817 -30.524  1.00 54.32           N
ANISOU 2538  N   GLU A  90     7653   6035   6951   -725    608   -221       N
ATOM   2539  CA  GLU A  90     -13.032  41.478 -31.076  1.00 49.10           C
ANISOU 2539  CA  GLU A  90     6901   5434   6319   -716    581   -223       C
ATOM   2540  C   GLU A  90     -12.254  40.581 -30.121  1.00 51.00           C
ANISOU 2540  C   GLU A  90     6974   5767   6636   -741    564   -272       C
ATOM   2541  O   GLU A  90     -12.539  39.381 -30.030  1.00 56.30           O
ANISOU 2541  O   GLU A  90     7551   6500   7340   -693    504   -258       O
ATOM   2542  CB  GLU A  90     -12.340  41.580 -32.449  1.00 43.44           C
ANISOU 2542  CB  GLU A  90     6272   4671   5564   -786    657   -240       C
ATOM   2543  CG  GLU A  90     -12.080  40.283 -33.193  1.00 54.23           C
ANISOU 2543  CG  GLU A  90     7561   6090   6953   -784    640   -245       C
ATOM   2544  CD  GLU A  90     -13.311  39.397 -33.338  1.00 67.23           C
ANISOU 2544  CD  GLU A  90     9175   7767   8601   -677    546   -185       C
ATOM   2545  OE1 GLU A  90     -14.457  39.901 -33.312  1.00 69.00           O
ANISOU 2545  OE1 GLU A  90     9473   7957   8787   -602    503   -137       O
ATOM   2546  OE2 GLU A  90     -13.124  38.174 -33.478  1.00 70.25           O
ANISOU 2546  OE2 GLU A  90     9456   8213   9022   -668    516   -193       O
ATOM   2547  N   GLU A  91     -11.270  41.141 -29.399  1.00 55.95           N
ANISOU 2547  N   GLU A  91     7567   6405   7287   -813    614   -333       N
ATOM   2548  CA  GLU A  91     -10.442  40.335 -28.496  1.00 55.26           C
ANISOU 2548  CA  GLU A  91     7324   6408   7265   -829    595   -391       C
ATOM   2549  C   GLU A  91     -11.235  39.890 -27.280  1.00 47.54           C
ANISOU 2549  C   GLU A  91     6270   5474   6319   -745    509   -358       C
ATOM   2550  O   GLU A  91     -11.163  38.725 -26.876  1.00 57.30           O
ANISOU 2550  O   GLU A  91     7401   6778   7594   -708    457   -364       O
ATOM   2551  CB  GLU A  91      -9.193  41.096 -28.050  1.00 50.99           C
ANISOU 2551  CB  GLU A  91     6763   5873   6739   -927    672   -476       C
ATOM   2552  CG  GLU A  91      -8.204  41.400 -29.169  1.00 75.50           C
ANISOU 2552  CG  GLU A  91     9919   8948   9818  -1029    769   -529       C
ATOM   2553  CD  GLU A  91      -8.676  42.522 -30.105  1.00 88.26           C
ANISOU 2553  CD  GLU A  91    11722  10452  11361  -1057    829   -487       C
ATOM   2554  OE1 GLU A  91      -9.498  43.356 -29.661  1.00 95.18           O
ANISOU 2554  OE1 GLU A  91    12680  11274  12210  -1015    810   -440       O
ATOM   2555  OE2 GLU A  91      -8.229  42.568 -31.279  1.00 82.62           O
ANISOU 2555  OE2 GLU A  91    11078   9701  10613  -1118    894   -502       O
ATOM   2556  N   GLU A  92     -11.994  40.805 -26.681  1.00 46.35           N
ANISOU 2556  N   GLU A  92     6179   5283   6148   -713    495   -326       N
ATOM   2557  CA  GLU A  92     -12.884  40.420 -25.592  1.00 47.57           C
ANISOU 2557  CA  GLU A  92     6272   5475   6326   -634    416   -292       C
ATOM   2558  C   GLU A  92     -13.817  39.308 -26.025  1.00 45.45           C
ANISOU 2558  C   GLU A  92     5980   5232   6056   -563    352   -242       C
ATOM   2559  O   GLU A  92     -14.054  38.365 -25.264  1.00 53.70           O
ANISOU 2559  O   GLU A  92     6934   6334   7135   -522    297   -238       O
ATOM   2560  CB  GLU A  92     -13.713  41.607 -25.113  1.00 51.64           C
ANISOU 2560  CB  GLU A  92     6871   5938   6811   -605    410   -260       C
ATOM   2561  CG  GLU A  92     -12.960  42.717 -24.433  1.00 57.65           C
ANISOU 2561  CG  GLU A  92     7652   6677   7576   -667    465   -307       C
ATOM   2562  CD  GLU A  92     -13.839  43.945 -24.299  1.00 75.54           C
ANISOU 2562  CD  GLU A  92    10033   8871   9796   -635    465   -269       C
ATOM   2563  OE1 GLU A  92     -13.653  44.894 -25.077  1.00 80.31           O
ANISOU 2563  OE1 GLU A  92    10764   9399  10352   -677    527   -270       O
ATOM   2564  OE2 GLU A  92     -14.749  43.947 -23.439  1.00 85.31           O
ANISOU 2564  OE2 GLU A  92    11243  10128  11043   -566    403   -239       O
ATOM   2565  N   LYS A  93     -14.346  39.393 -27.256  1.00 45.49           N
ANISOU 2565  N   LYS A  93     6073   5193   6019   -549    360   -206       N
ATOM   2566  CA  LYS A  93     -15.287  38.383 -27.734  1.00 42.86           C
ANISOU 2566  CA  LYS A  93     5719   4885   5681   -484    302   -164       C
ATOM   2567  C   LYS A  93     -14.617  37.028 -27.884  1.00 44.48           C
ANISOU 2567  C   LYS A  93     5828   5148   5924   -501    293   -188       C
ATOM   2568  O   LYS A  93     -15.237  35.993 -27.605  1.00 48.45           O
ANISOU 2568  O   LYS A  93     6271   5693   6444   -452    237   -167       O
ATOM   2569  CB  LYS A  93     -15.931  38.820 -29.048  1.00 41.93           C
ANISOU 2569  CB  LYS A  93     5718   4708   5504   -462    313   -128       C
ATOM   2570  CG  LYS A  93     -16.862  40.027 -28.878  1.00 49.16           C
ANISOU 2570  CG  LYS A  93     6733   5571   6374   -415    301   -100       C
ATOM   2571  CD  LYS A  93     -17.469  40.517 -30.197  1.00 60.49           C
ANISOU 2571  CD  LYS A  93     8300   6943   7740   -381    308    -69       C
ATOM   2572  CE  LYS A  93     -18.792  41.246 -29.942  1.00 66.53           C
ANISOU 2572  CE  LYS A  93     9128   7686   8465   -291    256    -38       C
ATOM   2573  NZ  LYS A  93     -18.907  42.488 -30.748  1.00 70.94           N
ANISOU 2573  NZ  LYS A  93     9857   8151   8947   -281    291    -25       N
ATOM   2574  N   ILE A  94     -13.346  37.012 -28.298  1.00 47.93           N
ANISOU 2574  N   ILE A  94     6251   5588   6372   -571    349   -237       N
ATOM   2575  CA  ILE A  94     -12.630  35.746 -28.425  1.00 43.08           C
ANISOU 2575  CA  ILE A  94     5545   5031   5792   -581    338   -267       C
ATOM   2576  C   ILE A  94     -12.377  35.140 -27.057  1.00 38.27           C
ANISOU 2576  C   ILE A  94     4834   4481   5226   -555    295   -292       C
ATOM   2577  O   ILE A  94     -12.484  33.922 -26.879  1.00 43.74           O
ANISOU 2577  O   ILE A  94     5465   5216   5938   -518    250   -286       O
ATOM   2578  CB  ILE A  94     -11.315  35.942 -29.197  1.00 47.01           C
ANISOU 2578  CB  ILE A  94     6049   5525   6290   -663    411   -326       C
ATOM   2579  CG1 ILE A  94     -11.584  36.462 -30.610  1.00 41.31           C
ANISOU 2579  CG1 ILE A  94     5443   4737   5517   -687    455   -298       C
ATOM   2580  CG2 ILE A  94     -10.503  34.636 -29.210  1.00 41.05           C
ANISOU 2580  CG2 ILE A  94     5190   4837   5571   -665    393   -368       C
ATOM   2581  CD1 ILE A  94     -10.333  36.891 -31.312  1.00 38.14           C
ANISOU 2581  CD1 ILE A  94     5065   4320   5107   -783    542   -359       C
ATOM   2582  N   ARG A  95     -12.042  35.984 -26.072  1.00 42.04           N
ANISOU 2582  N   ARG A  95     5301   4958   5715   -574    309   -320       N
ATOM   2583  CA  ARG A  95     -11.778  35.524 -24.712  1.00 33.34           C
ANISOU 2583  CA  ARG A  95     4111   3908   4648   -546    268   -346       C
ATOM   2584  C   ARG A  95     -13.031  34.977 -24.056  1.00 34.04           C
ANISOU 2584  C   ARG A  95     4193   4005   4736   -474    202   -289       C
ATOM   2585  O   ARG A  95     -12.987  33.931 -23.400  1.00 46.07           O
ANISOU 2585  O   ARG A  95     5655   5572   6280   -438    158   -294       O
ATOM   2586  CB  ARG A  95     -11.218  36.654 -23.874  1.00 37.35           C
ANISOU 2586  CB  ARG A  95     4616   4410   5164   -584    300   -388       C
ATOM   2587  CG  ARG A  95      -9.866  37.155 -24.296  1.00 39.15           C
ANISOU 2587  CG  ARG A  95     4833   4644   5398   -667    371   -465       C
ATOM   2588  CD  ARG A  95      -9.301  38.027 -23.171  1.00 49.26           C
ANISOU 2588  CD  ARG A  95     6083   5939   6695   -695    390   -517       C
ATOM   2589  NE  ARG A  95      -7.900  37.707 -23.003  1.00 63.13           N
ANISOU 2589  NE  ARG A  95     7750   7757   8479   -738    415   -614       N
ATOM   2590  CZ  ARG A  95      -7.390  37.053 -21.974  1.00 55.48           C
ANISOU 2590  CZ  ARG A  95     6683   6856   7541   -699    368   -660       C
ATOM   2591  NH1 ARG A  95      -8.165  36.663 -20.971  1.00 52.34           N
ANISOU 2591  NH1 ARG A  95     6271   6468   7150   -624    299   -613       N
ATOM   2592  NH2 ARG A  95      -6.093  36.796 -21.962  1.00 51.43           N
ANISOU 2592  NH2 ARG A  95     6089   6404   7049   -735    391   -758       N
ATOM   2593  N   VAL A  96     -14.160  35.670 -24.213  1.00 34.01           N
ANISOU 2593  N   VAL A  96     4257   3960   4705   -450    194   -239       N
ATOM   2594  CA  VAL A  96     -15.428  35.151 -23.692  1.00 30.45           C
ANISOU 2594  CA  VAL A  96     3796   3522   4250   -388    137   -194       C
ATOM   2595  C   VAL A  96     -15.731  33.790 -24.306  1.00 38.62           C
ANISOU 2595  C   VAL A  96     4806   4581   5286   -365    110   -176       C
ATOM   2596  O   VAL A  96     -16.055  32.825 -23.598  1.00 45.51           O
ANISOU 2596  O   VAL A  96     5632   5487   6173   -334     71   -170       O
ATOM   2597  CB  VAL A  96     -16.567  36.149 -23.959  1.00 34.05           C
ANISOU 2597  CB  VAL A  96     4329   3936   4672   -362    134   -155       C
ATOM   2598  CG1 VAL A  96     -17.943  35.494 -23.752  1.00 33.08           C
ANISOU 2598  CG1 VAL A  96     4192   3835   4541   -303     80   -118       C
ATOM   2599  CG2 VAL A  96     -16.405  37.371 -23.098  1.00 39.60           C
ANISOU 2599  CG2 VAL A  96     5054   4618   5375   -375    151   -169       C
ATOM   2600  N   ASP A  97     -15.604  33.686 -25.635  1.00 35.99           N
ANISOU 2600  N   ASP A  97     4511   4229   4936   -383    134   -170       N
ATOM   2601  CA  ASP A  97     -15.944  32.445 -26.326  1.00 40.40           C
ANISOU 2601  CA  ASP A  97     5051   4807   5492   -363    111   -152       C
ATOM   2602  C   ASP A  97     -15.046  31.297 -25.876  1.00 40.42           C
ANISOU 2602  C   ASP A  97     4984   4851   5524   -368     99   -185       C
ATOM   2603  O   ASP A  97     -15.521  30.195 -25.575  1.00 39.28           O
ANISOU 2603  O   ASP A  97     4811   4730   5384   -336     62   -170       O
ATOM   2604  CB  ASP A  97     -15.831  32.641 -27.835  1.00 47.87           C
ANISOU 2604  CB  ASP A  97     6054   5722   6411   -385    144   -144       C
ATOM   2605  CG  ASP A  97     -16.984  33.435 -28.423  1.00 52.17           C
ANISOU 2605  CG  ASP A  97     6677   6230   6917   -354    137   -106       C
ATOM   2606  OD1 ASP A  97     -17.996  33.692 -27.737  1.00 55.26           O
ANISOU 2606  OD1 ASP A  97     7068   6627   7301   -312    102    -87       O
ATOM   2607  OD2 ASP A  97     -16.855  33.820 -29.591  1.00 49.62           O
ANISOU 2607  OD2 ASP A  97     6419   5872   6564   -370    167   -100       O
ATOM   2608  N   VAL A  98     -13.736  31.540 -25.833  1.00 36.41           N
ANISOU 2608  N   VAL A  98     4449   4353   5033   -406    131   -235       N
ATOM   2609  CA  VAL A  98     -12.799  30.483 -25.470  1.00 34.21           C
ANISOU 2609  CA  VAL A  98     4104   4118   4777   -400    115   -277       C
ATOM   2610  C   VAL A  98     -13.030  30.065 -24.031  1.00 45.91           C
ANISOU 2610  C   VAL A  98     5550   5623   6270   -357     70   -277       C
ATOM   2611  O   VAL A  98     -13.101  28.876 -23.718  1.00 49.12           O
ANISOU 2611  O   VAL A  98     5934   6050   6679   -321     34   -273       O
ATOM   2612  CB  VAL A  98     -11.353  30.958 -25.700  1.00 37.47           C
ANISOU 2612  CB  VAL A  98     4487   4545   5203   -451    160   -346       C
ATOM   2613  CG1 VAL A  98     -10.332  30.024 -25.007  1.00 31.12           C
ANISOU 2613  CG1 VAL A  98     3605   3796   4422   -428    133   -405       C
ATOM   2614  CG2 VAL A  98     -11.084  31.067 -27.207  1.00 25.67           C
ANISOU 2614  CG2 VAL A  98     3032   3029   3694   -495    206   -348       C
ATOM   2615  N   LEU A  99     -13.183  31.051 -23.142  1.00 42.53           N
ANISOU 2615  N   LEU A  99     5127   5187   5846   -360     73   -279       N
ATOM   2616  CA  LEU A  99     -13.414  30.778 -21.736  1.00 33.76           C
ANISOU 2616  CA  LEU A  99     3989   4095   4742   -321     34   -279       C
ATOM   2617  C   LEU A  99     -14.733  30.040 -21.524  1.00 39.30           C
ANISOU 2617  C   LEU A  99     4713   4789   5429   -284     -1   -225       C
ATOM   2618  O   LEU A  99     -14.792  29.060 -20.769  1.00 50.98           O
ANISOU 2618  O   LEU A  99     6176   6285   6907   -251    -34   -226       O
ATOM   2619  CB  LEU A  99     -13.391  32.092 -20.944  1.00 34.15           C
ANISOU 2619  CB  LEU A  99     4044   4134   4797   -337     49   -291       C
ATOM   2620  CG  LEU A  99     -12.764  32.061 -19.543  1.00 34.80           C
ANISOU 2620  CG  LEU A  99     4080   4249   4895   -317     26   -332       C
ATOM   2621  CD1 LEU A  99     -13.475  32.981 -18.575  1.00 33.01           C
ANISOU 2621  CD1 LEU A  99     3871   4007   4666   -308     20   -311       C
ATOM   2622  CD2 LEU A  99     -12.646  30.637 -18.982  1.00 37.61           C
ANISOU 2622  CD2 LEU A  99     4409   4632   5250   -266    -20   -336       C
ATOM   2623  N   GLU A 100     -15.809  30.513 -22.158  1.00 35.52           N
ANISOU 2623  N   GLU A 100     4276   4286   4934   -288      7   -184       N
ATOM   2624  CA  GLU A 100     -17.116  29.911 -21.917  1.00 38.36           C
ANISOU 2624  CA  GLU A 100     4647   4647   5279   -259    -22   -147       C
ATOM   2625  C   GLU A 100     -17.070  28.405 -22.161  1.00 40.38           C
ANISOU 2625  C   GLU A 100     4892   4917   5532   -247    -39   -144       C
ATOM   2626  O   GLU A 100     -17.460  27.609 -21.298  1.00 41.28           O
ANISOU 2626  O   GLU A 100     5001   5040   5641   -226    -62   -138       O
ATOM   2627  CB  GLU A 100     -18.167  30.580 -22.800  1.00 40.73           C
ANISOU 2627  CB  GLU A 100     4988   4928   5559   -258    -13   -117       C
ATOM   2628  CG  GLU A 100     -19.604  30.148 -22.524  1.00 43.61           C
ANISOU 2628  CG  GLU A 100     5355   5306   5910   -232    -40    -92       C
ATOM   2629  CD  GLU A 100     -20.461  30.185 -23.770  1.00 56.72           C
ANISOU 2629  CD  GLU A 100     7043   6961   7548   -224    -39    -75       C
ATOM   2630  OE1 GLU A 100     -20.892  31.286 -24.173  1.00 61.73           O
ANISOU 2630  OE1 GLU A 100     7712   7577   8165   -213    -35    -67       O
ATOM   2631  OE2 GLU A 100     -20.692  29.107 -24.354  1.00 65.01           O
ANISOU 2631  OE2 GLU A 100     8084   8023   8594   -225    -45    -70       O
ATOM   2632  N   ASN A 101     -16.537  27.999 -23.318  1.00 40.33           N
ANISOU 2632  N   ASN A 101     4887   4910   5526   -262    -24   -151       N
ATOM   2633  CA  ASN A 101     -16.433  26.580 -23.652  1.00 41.11           C
ANISOU 2633  CA  ASN A 101     4980   5018   5621   -250    -38   -151       C
ATOM   2634  C   ASN A 101     -15.417  25.871 -22.773  1.00 40.38           C
ANISOU 2634  C   ASN A 101     4863   4943   5537   -229    -57   -184       C
ATOM   2635  O   ASN A 101     -15.636  24.722 -22.375  1.00 47.84           O
ANISOU 2635  O   ASN A 101     5819   5889   6470   -205    -79   -177       O
ATOM   2636  CB  ASN A 101     -16.058  26.421 -25.122  1.00 38.83           C
ANISOU 2636  CB  ASN A 101     4699   4725   5331   -271    -16   -153       C
ATOM   2637  CG  ASN A 101     -17.175  26.831 -26.043  1.00 41.49           C
ANISOU 2637  CG  ASN A 101     5069   5047   5649   -276     -8   -120       C
ATOM   2638  OD1 ASN A 101     -18.011  26.013 -26.418  1.00 48.37           O
ANISOU 2638  OD1 ASN A 101     5947   5923   6507   -266    -21   -100       O
ATOM   2639  ND2 ASN A 101     -17.210  28.115 -26.400  1.00 38.34           N
ANISOU 2639  ND2 ASN A 101     4695   4629   5244   -290     13   -117       N
ATOM   2640  N   GLN A 102     -14.285  26.527 -22.496  1.00 40.68           N
ANISOU 2640  N   GLN A 102     4871   4994   5592   -237    -47   -227       N
ATOM   2641  CA  GLN A 102     -13.295  25.978 -21.576  1.00 42.64           C
ANISOU 2641  CA  GLN A 102     5090   5265   5845   -205    -72   -270       C
ATOM   2642  C   GLN A 102     -13.913  25.707 -20.213  1.00 45.97           C
ANISOU 2642  C   GLN A 102     5530   5683   6255   -171   -102   -252       C
ATOM   2643  O   GLN A 102     -13.759  24.612 -19.663  1.00 43.61           O
ANISOU 2643  O   GLN A 102     5245   5385   5939   -132   -131   -257       O
ATOM   2644  CB  GLN A 102     -12.113  26.936 -21.440  1.00 53.23           C
ANISOU 2644  CB  GLN A 102     6389   6629   7206   -226    -52   -328       C
ATOM   2645  CG  GLN A 102     -11.006  26.414 -20.554  1.00 46.66           C
ANISOU 2645  CG  GLN A 102     5517   5833   6378   -185    -83   -387       C
ATOM   2646  CD  GLN A 102     -10.469  25.097 -21.059  1.00 49.63           C
ANISOU 2646  CD  GLN A 102     5888   6223   6745   -153   -104   -407       C
ATOM   2647  OE1 GLN A 102     -10.365  24.875 -22.262  1.00 48.47           O
ANISOU 2647  OE1 GLN A 102     5741   6073   6601   -181    -81   -404       O
ATOM   2648  NE2 GLN A 102     -10.140  24.212 -20.148  1.00 56.65           N
ANISOU 2648  NE2 GLN A 102     6780   7124   7618    -92   -149   -427       N
ATOM   2649  N   ALA A 103     -14.652  26.689 -19.671  1.00 44.03           N
ANISOU 2649  N   ALA A 103     5292   5426   6011   -184    -94   -230       N
ATOM   2650  CA  ALA A 103     -15.285  26.514 -18.364  1.00 49.71           C
ANISOU 2650  CA  ALA A 103     6030   6141   6718   -158   -117   -215       C
ATOM   2651  C   ALA A 103     -16.206  25.302 -18.344  1.00 39.29           C
ANISOU 2651  C   ALA A 103     4750   4806   5373   -147   -129   -181       C
ATOM   2652  O   ALA A 103     -16.282  24.601 -17.334  1.00 42.57           O
ANISOU 2652  O   ALA A 103     5191   5216   5770   -119   -150   -181       O
ATOM   2653  CB  ALA A 103     -16.059  27.765 -17.960  1.00 23.85           C
ANISOU 2653  CB  ALA A 103     2756   2858   3448   -177   -105   -196       C
ATOM   2654  N   MET A 104     -16.906  25.028 -19.446  1.00 36.69           N
ANISOU 2654  N   MET A 104     4431   4468   5039   -170   -113   -156       N
ATOM   2655  CA  MET A 104     -17.795  23.865 -19.459  1.00 36.02           C
ANISOU 2655  CA  MET A 104     4383   4373   4931   -169   -117   -132       C
ATOM   2656  C   MET A 104     -16.994  22.560 -19.510  1.00 37.77           C
ANISOU 2656  C   MET A 104     4626   4588   5139   -143   -133   -147       C
ATOM   2657  O   MET A 104     -17.322  21.599 -18.806  1.00 49.26           O
ANISOU 2657  O   MET A 104     6126   6025   6566   -127   -143   -140       O
ATOM   2658  CB  MET A 104     -18.810  23.961 -20.615  1.00 28.29           C
ANISOU 2658  CB  MET A 104     3405   3394   3950   -198    -98   -109       C
ATOM   2659  CG  MET A 104     -19.885  22.823 -20.627  1.00 37.28           C
ANISOU 2659  CG  MET A 104     4575   4526   5064   -210    -94    -94       C
ATOM   2660  SD  MET A 104     -21.242  22.873 -19.396  1.00 47.12           S
ANISOU 2660  SD  MET A 104     5838   5774   6291   -223    -90    -86       S
ATOM   2661  CE  MET A 104     -20.469  21.830 -18.268  1.00 44.08           C
ANISOU 2661  CE  MET A 104     5501   5364   5885   -198   -103    -93       C
ATOM   2662  N   ASP A 105     -15.914  22.510 -20.292  1.00 39.81           N
ANISOU 2662  N   ASP A 105     4856   4858   5410   -137   -133   -173       N
ATOM   2663  CA  ASP A 105     -15.062  21.319 -20.280  1.00 35.43           C
ANISOU 2663  CA  ASP A 105     4319   4302   4841   -100   -155   -196       C
ATOM   2664  C   ASP A 105     -14.459  21.079 -18.898  1.00 36.69           C
ANISOU 2664  C   ASP A 105     4494   4461   4984    -49   -187   -221       C
ATOM   2665  O   ASP A 105     -14.492  19.961 -18.381  1.00 40.02           O
ANISOU 2665  O   ASP A 105     4971   4861   5372    -14   -207   -217       O
ATOM   2666  CB  ASP A 105     -13.945  21.449 -21.312  1.00 43.48           C
ANISOU 2666  CB  ASP A 105     5295   5344   5882   -103   -149   -231       C
ATOM   2667  CG  ASP A 105     -14.448  21.465 -22.729  1.00 49.71           C
ANISOU 2667  CG  ASP A 105     6082   6128   6677   -143   -122   -207       C
ATOM   2668  OD1 ASP A 105     -15.651  21.194 -22.966  1.00 54.52           O
ANISOU 2668  OD1 ASP A 105     6722   6720   7274   -162   -112   -168       O
ATOM   2669  OD2 ASP A 105     -13.617  21.772 -23.608  1.00 56.59           O
ANISOU 2669  OD2 ASP A 105     6920   7015   7565   -157   -108   -234       O
ATOM   2670  N   THR A 106     -13.883  22.117 -18.289  1.00 40.36           N
ANISOU 2670  N   THR A 106     4917   4949   5469    -43   -192   -249       N
ATOM   2671  CA  THR A 106     -13.311  21.964 -16.954  1.00 38.78           C
ANISOU 2671  CA  THR A 106     4729   4754   5252     10   -226   -277       C
ATOM   2672  C   THR A 106     -14.358  21.502 -15.944  1.00 48.17           C
ANISOU 2672  C   THR A 106     5986   5908   6408     17   -231   -238       C
ATOM   2673  O   THR A 106     -14.090  20.629 -15.107  1.00 45.07           O
ANISOU 2673  O   THR A 106     5648   5497   5978     69   -260   -247       O
ATOM   2674  CB  THR A 106     -12.671  23.277 -16.505  1.00 37.97           C
ANISOU 2674  CB  THR A 106     4566   4683   5179      3   -224   -314       C
ATOM   2675  OG1 THR A 106     -11.693  23.675 -17.480  1.00 43.22           O
ANISOU 2675  OG1 THR A 106     5172   5379   5872    -16   -209   -357       O
ATOM   2676  CG2 THR A 106     -11.980  23.103 -15.132  1.00 25.19           C
ANISOU 2676  CG2 THR A 106     2953   3077   3542     66   -265   -353       C
ATOM   2677  N   ARG A 107     -15.567  22.050 -16.022  1.00 53.09           N
ANISOU 2677  N   ARG A 107     6613   6521   7039    -32   -202   -199       N
ATOM   2678  CA  ARG A 107     -16.628  21.572 -15.141  1.00 46.34           C
ANISOU 2678  CA  ARG A 107     5820   5637   6151    -38   -198   -169       C
ATOM   2679  C   ARG A 107     -16.923  20.091 -15.375  1.00 51.68           C
ANISOU 2679  C   ARG A 107     6567   6280   6788    -31   -196   -155       C
ATOM   2680  O   ARG A 107     -17.137  19.340 -14.420  1.00 54.37           O
ANISOU 2680  O   ARG A 107     6981   6589   7087     -9   -204   -149       O
ATOM   2681  CB  ARG A 107     -17.887  22.419 -15.330  1.00 33.14           C
ANISOU 2681  CB  ARG A 107     4127   3970   4495    -91   -168   -141       C
ATOM   2682  CG  ARG A 107     -19.075  21.839 -14.635  1.00 39.91           C
ANISOU 2682  CG  ARG A 107     5039   4804   5319   -111   -153   -119       C
ATOM   2683  CD  ARG A 107     -20.381  22.435 -15.091  1.00 37.35           C
ANISOU 2683  CD  ARG A 107     4689   4495   5008   -161   -125   -103       C
ATOM   2684  NE  ARG A 107     -20.364  23.885 -15.148  1.00 43.04           N
ANISOU 2684  NE  ARG A 107     5354   5240   5761   -164   -127   -106       N
ATOM   2685  CZ  ARG A 107     -20.556  24.673 -14.101  1.00 47.19           C
ANISOU 2685  CZ  ARG A 107     5872   5771   6289   -158   -131   -110       C
ATOM   2686  NH1 ARG A 107     -20.786  24.152 -12.902  1.00 48.72           N
ANISOU 2686  NH1 ARG A 107     6110   5948   6454   -150   -134   -109       N
ATOM   2687  NH2 ARG A 107     -20.535  25.985 -14.264  1.00 49.45           N
ANISOU 2687  NH2 ARG A 107     6114   6073   6602   -161   -131   -113       N
ATOM   2688  N   LEU A 108     -16.931  19.649 -16.640  1.00 58.24           N
ANISOU 2688  N   LEU A 108     7386   7113   7629    -52   -183   -149       N
ATOM   2689  CA  LEU A 108     -17.289  18.267 -16.947  1.00 48.99           C
ANISOU 2689  CA  LEU A 108     6283   5908   6421    -54   -176   -136       C
ATOM   2690  C   LEU A 108     -16.156  17.312 -16.625  1.00 55.57           C
ANISOU 2690  C   LEU A 108     7163   6725   7225     14   -211   -161       C
ATOM   2691  O   LEU A 108     -16.403  16.139 -16.326  1.00 63.20           O
ANISOU 2691  O   LEU A 108     8219   7649   8145     28   -211   -150       O
ATOM   2692  CB  LEU A 108     -17.673  18.117 -18.420  1.00 47.06           C
ANISOU 2692  CB  LEU A 108     6008   5675   6196    -95   -153   -125       C
ATOM   2693  CG  LEU A 108     -18.907  18.853 -18.948  1.00 45.54           C
ANISOU 2693  CG  LEU A 108     5780   5500   6024   -153   -122   -105       C
ATOM   2694  CD1 LEU A 108     -19.052  18.606 -20.447  1.00 50.02           C
ANISOU 2694  CD1 LEU A 108     6323   6078   6605   -177   -108   -100       C
ATOM   2695  CD2 LEU A 108     -20.178  18.445 -18.204  1.00 35.09           C
ANISOU 2695  CD2 LEU A 108     4503   4158   4670   -186    -99    -91       C
ATOM   2696  N   ASP A 109     -14.913  17.793 -16.697  1.00 57.02           N
ANISOU 2696  N   ASP A 109     7291   6943   7432     57   -241   -199       N
ATOM   2697  CA  ASP A 109     -13.790  17.015 -16.199  1.00 52.96           C
ANISOU 2697  CA  ASP A 109     6813   6424   6888    138   -285   -236       C
ATOM   2698  C   ASP A 109     -13.987  16.663 -14.737  1.00 56.82           C
ANISOU 2698  C   ASP A 109     7384   6878   7328    180   -305   -231       C
ATOM   2699  O   ASP A 109     -13.655  15.554 -14.306  1.00 62.06           O
ANISOU 2699  O   ASP A 109     8137   7505   7939    239   -331   -238       O
ATOM   2700  CB  ASP A 109     -12.493  17.793 -16.387  1.00 57.18           C
ANISOU 2700  CB  ASP A 109     7255   7014   7458    170   -310   -292       C
ATOM   2701  CG  ASP A 109     -11.853  17.524 -17.729  1.00 67.58           C
ANISOU 2701  CG  ASP A 109     8526   8355   8798    162   -305   -315       C
ATOM   2702  OD1 ASP A 109     -12.408  16.706 -18.500  1.00 64.50           O
ANISOU 2702  OD1 ASP A 109     8177   7936   8394    139   -287   -284       O
ATOM   2703  OD2 ASP A 109     -10.797  18.129 -18.006  1.00 75.66           O
ANISOU 2703  OD2 ASP A 109     9471   9427   9851    175   -315   -369       O
ATOM   2704  N   PHE A 110     -14.543  17.597 -13.961  1.00 57.05           N
ANISOU 2704  N   PHE A 110     7393   6914   7370    152   -292   -218       N
ATOM   2705  CA  PHE A 110     -14.797  17.340 -12.554  1.00 56.92           C
ANISOU 2705  CA  PHE A 110     7457   6864   7307    185   -306   -211       C
ATOM   2706  C   PHE A 110     -16.086  16.559 -12.358  1.00 55.67           C
ANISOU 2706  C   PHE A 110     7394   6650   7107    136   -266   -167       C
ATOM   2707  O   PHE A 110     -16.146  15.665 -11.504  1.00 56.47           O
ANISOU 2707  O   PHE A 110     7608   6701   7146    171   -274   -162       O
ATOM   2708  CB  PHE A 110     -14.851  18.654 -11.773  1.00 61.36           C
ANISOU 2708  CB  PHE A 110     7958   7457   7899    175   -307   -219       C
ATOM   2709  CG  PHE A 110     -14.979  18.467 -10.293  1.00 63.28           C
ANISOU 2709  CG  PHE A 110     8279   7670   8094    215   -325   -218       C
ATOM   2710  CD1 PHE A 110     -14.028  17.756  -9.593  1.00 67.80           C
ANISOU 2710  CD1 PHE A 110     8913   8229   8620    308   -375   -250       C
ATOM   2711  CD2 PHE A 110     -16.053  18.984  -9.604  1.00 68.46           C
ANISOU 2711  CD2 PHE A 110     8951   8313   8748    165   -294   -188       C
ATOM   2712  CE1 PHE A 110     -14.134  17.570  -8.223  1.00 72.57           C
ANISOU 2712  CE1 PHE A 110     9600   8800   9172    351   -393   -248       C
ATOM   2713  CE2 PHE A 110     -16.170  18.803  -8.235  1.00 75.03           C
ANISOU 2713  CE2 PHE A 110     9860   9115   9533    199   -307   -187       C
ATOM   2714  CZ  PHE A 110     -15.204  18.103  -7.544  1.00 75.12           C
ANISOU 2714  CZ  PHE A 110     9940   9108   9495    293   -356   -215       C
ATOM   2715  N   ALA A 111     -17.128  16.875 -13.133  1.00 47.25           N
ANISOU 2715  N   ALA A 111     6289   5594   6071     54   -220   -141       N
ATOM   2716  CA  ALA A 111     -18.413  16.240 -12.874  1.00 46.96           C
ANISOU 2716  CA  ALA A 111     6329   5517   5998     -4   -176   -112       C
ATOM   2717  C   ALA A 111     -18.348  14.758 -13.157  1.00 52.76           C
ANISOU 2717  C   ALA A 111     7167   6200   6681      8   -170   -107       C
ATOM   2718  O   ALA A 111     -19.001  13.971 -12.468  1.00 61.32           O
ANISOU 2718  O   ALA A 111     8360   7231   7710    -12   -144    -94       O
ATOM   2719  CB  ALA A 111     -19.518  16.883 -13.702  1.00 45.55           C
ANISOU 2719  CB  ALA A 111     6077   5369   5860    -85   -135    -98       C
ATOM   2720  N   ARG A 112     -17.548  14.362 -14.146  1.00 53.65           N
ANISOU 2720  N   ARG A 112     7253   6324   6808     40   -192   -120       N
ATOM   2721  CA  ARG A 112     -17.518  12.966 -14.562  1.00 52.49           C
ANISOU 2721  CA  ARG A 112     7201   6128   6615     49   -185   -114       C
ATOM   2722  C   ARG A 112     -16.921  12.087 -13.476  1.00 59.57           C
ANISOU 2722  C   ARG A 112     8226   6968   7440    127   -216   -123       C
ATOM   2723  O   ARG A 112     -17.438  10.999 -13.199  1.00 65.72           O
ANISOU 2723  O   ARG A 112     9133   7680   8156    112   -189   -107       O
ATOM   2724  CB  ARG A 112     -16.719  12.828 -15.858  1.00 56.43           C
ANISOU 2724  CB  ARG A 112     7635   6659   7148     70   -205   -130       C
ATOM   2725  CG  ARG A 112     -17.557  12.748 -17.127  1.00 53.12           C
ANISOU 2725  CG  ARG A 112     7172   6253   6758     -8   -162   -113       C
ATOM   2726  CD  ARG A 112     -16.704  12.281 -18.293  1.00 57.16           C
ANISOU 2726  CD  ARG A 112     7655   6779   7285     21   -182   -129       C
ATOM   2727  NE  ARG A 112     -15.467  13.047 -18.355  1.00 66.17           N
ANISOU 2727  NE  ARG A 112     8714   7967   8462     78   -224   -161       N
ATOM   2728  CZ  ARG A 112     -15.333  14.197 -19.012  1.00 61.45           C
ANISOU 2728  CZ  ARG A 112     8005   7422   7921     48   -218   -168       C
ATOM   2729  NH1 ARG A 112     -16.366  14.710 -19.678  1.00 56.06           N
ANISOU 2729  NH1 ARG A 112     7283   6752   7266    -25   -179   -142       N
ATOM   2730  NH2 ARG A 112     -14.169  14.834 -18.995  1.00 51.99           N
ANISOU 2730  NH2 ARG A 112     6740   6265   6750     93   -249   -207       N
ATOM   2731  N   VAL A 113     -15.822  12.543 -12.872  1.00 52.02           N
ANISOU 2731  N   VAL A 113     7242   6036   6486    213   -272   -152       N
ATOM   2732  CA  VAL A 113     -15.216  11.841 -11.742  1.00 60.00           C
ANISOU 2732  CA  VAL A 113     8374   6999   7425    304   -312   -166       C
ATOM   2733  C   VAL A 113     -16.184  11.773 -10.562  1.00 60.94           C
ANISOU 2733  C   VAL A 113     8592   7066   7496    267   -277   -138       C
ATOM   2734  O   VAL A 113     -16.407  10.701  -9.985  1.00 66.71           O
ANISOU 2734  O   VAL A 113     9479   7720   8147    286   -267   -126       O
ATOM   2735  CB  VAL A 113     -13.892  12.521 -11.343  1.00 63.52           C
ANISOU 2735  CB  VAL A 113     8743   7499   7892    399   -380   -215       C
ATOM   2736  CG1 VAL A 113     -13.337  11.909 -10.069  1.00 51.47           C
ANISOU 2736  CG1 VAL A 113     7341   5929   6287    502   -427   -232       C
ATOM   2737  CG2 VAL A 113     -12.883  12.444 -12.496  1.00 60.40           C
ANISOU 2737  CG2 VAL A 113     8261   7154   7536    434   -410   -252       C
ATOM   2738  N   CYS A 114     -16.763  12.915 -10.171  1.00 52.01           N
ANISOU 2738  N   CYS A 114     7379   5973   6408    214   -257   -131       N
ATOM   2739  CA  CYS A 114     -17.582  12.912  -8.964  1.00 50.63           C
ANISOU 2739  CA  CYS A 114     7294   5756   6188    184   -227   -113       C
ATOM   2740  C   CYS A 114     -18.825  12.049  -9.112  1.00 61.48           C
ANISOU 2740  C   CYS A 114     8764   7074   7522     93   -155    -86       C
ATOM   2741  O   CYS A 114     -19.246  11.411  -8.143  1.00 58.22           O
ANISOU 2741  O   CYS A 114     8490   6594   7035     87   -131    -76       O
ATOM   2742  CB  CYS A 114     -17.966  14.324  -8.578  1.00 44.85           C
ANISOU 2742  CB  CYS A 114     6449   5081   5513    146   -219   -113       C
ATOM   2743  SG  CYS A 114     -16.578  15.151  -7.921  1.00 63.81           S
ANISOU 2743  SG  CYS A 114     8785   7527   7933    251   -294   -151       S
ATOM   2744  N   TYR A 115     -19.426  12.009 -10.303  1.00 63.39           N
ANISOU 2744  N   TYR A 115     8938   7342   7806     19   -118    -79       N
ATOM   2745  CA  TYR A 115     -20.573  11.135 -10.512  1.00 62.70           C
ANISOU 2745  CA  TYR A 115     8935   7208   7680    -72    -48    -66       C
ATOM   2746  C   TYR A 115     -20.170   9.683 -10.727  1.00 66.96           C
ANISOU 2746  C   TYR A 115     9617   7674   8152    -37    -49    -63       C
ATOM   2747  O   TYR A 115     -21.026   8.801 -10.623  1.00 73.62           O
ANISOU 2747  O   TYR A 115    10570   8460   8943   -106     13    -55       O
ATOM   2748  CB  TYR A 115     -21.397  11.615 -11.710  1.00 57.02           C
ANISOU 2748  CB  TYR A 115     8091   6548   7026   -158    -11    -67       C
ATOM   2749  CG  TYR A 115     -22.379  12.724 -11.393  1.00 47.74           C
ANISOU 2749  CG  TYR A 115     6826   5423   5891   -224     18    -70       C
ATOM   2750  CD1 TYR A 115     -23.642  12.445 -10.903  1.00 47.16           C
ANISOU 2750  CD1 TYR A 115     6804   5330   5786   -312     83    -75       C
ATOM   2751  CD2 TYR A 115     -22.037  14.053 -11.593  1.00 59.17           C
ANISOU 2751  CD2 TYR A 115     8139   6937   7405   -199    -18    -74       C
ATOM   2752  CE1 TYR A 115     -24.542  13.467 -10.617  1.00 56.10           C
ANISOU 2752  CE1 TYR A 115     7848   6515   6954   -365    106    -86       C
ATOM   2753  CE2 TYR A 115     -22.925  15.081 -11.310  1.00 60.00           C
ANISOU 2753  CE2 TYR A 115     8168   7086   7543   -249      4    -78       C
ATOM   2754  CZ  TYR A 115     -24.167  14.781 -10.826  1.00 58.39           C
ANISOU 2754  CZ  TYR A 115     8009   6868   7308   -328     63    -85       C
ATOM   2755  OH  TYR A 115     -25.029  15.801 -10.552  1.00 60.45           O
ANISOU 2755  OH  TYR A 115     8189   7178   7600   -370     80    -97       O
ATOM   2756  N   ASN A 116     -18.895   9.418 -11.010  1.00 71.95           N
ANISOU 2756  N   ASN A 116    10249   8307   8781     67   -114    -74       N
ATOM   2757  CA  ASN A 116     -18.443   8.066 -11.353  1.00 69.92           C
ANISOU 2757  CA  ASN A 116    10118   7985   8462    110   -122    -75       C
ATOM   2758  C   ASN A 116     -18.550   7.127 -10.155  1.00 79.04           C
ANISOU 2758  C   ASN A 116    11479   9040   9511    141   -110    -66       C
ATOM   2759  O   ASN A 116     -18.034   7.445  -9.075  1.00 75.74           O
ANISOU 2759  O   ASN A 116    11101   8612   9063    216   -152    -73       O
ATOM   2760  CB  ASN A 116     -16.999   8.104 -11.837  1.00 61.45           C
ANISOU 2760  CB  ASN A 116     8987   6948   7412    225   -202   -100       C
ATOM   2761  CG  ASN A 116     -16.615   6.868 -12.608  1.00 70.98           C
ANISOU 2761  CG  ASN A 116    10278   8111   8580    256   -208   -103       C
ATOM   2762  OD1 ASN A 116     -16.685   5.759 -12.096  1.00 74.64           O
ANISOU 2762  OD1 ASN A 116    10917   8486   8957    283   -198    -95       O
ATOM   2763  ND2 ASN A 116     -16.203   7.052 -13.851  1.00 82.12           N
ANISOU 2763  ND2 ASN A 116    11570   9578  10053    253   -223   -115       N
ATOM   2764  N   PRO A 117     -19.170   5.937 -10.314  1.00 88.53           N
ANISOU 2764  N   PRO A 117    12826  10163  10650     88    -54    -53       N
ATOM   2765  CA  PRO A 117     -19.250   4.977  -9.201  1.00 87.73           C
ANISOU 2765  CA  PRO A 117    12948   9951  10434    116    -36    -44       C
ATOM   2766  C   PRO A 117     -17.893   4.660  -8.593  1.00 84.63           C
ANISOU 2766  C   PRO A 117    12640   9528   9987    281   -127    -57       C
ATOM   2767  O   PRO A 117     -17.798   4.139  -7.478  1.00 83.84           O
ANISOU 2767  O   PRO A 117    12715   9346   9793    332   -132    -52       O
ATOM   2768  CB  PRO A 117     -19.857   3.731  -9.860  1.00 83.94           C
ANISOU 2768  CB  PRO A 117    12586   9400   9905     44     29    -36       C
ATOM   2769  CG  PRO A 117     -20.635   4.249 -11.016  1.00 80.54           C
ANISOU 2769  CG  PRO A 117    11985   9051   9567    -68     73    -40       C
ATOM   2770  CD  PRO A 117     -19.861   5.440 -11.520  1.00 87.38           C
ANISOU 2770  CD  PRO A 117    12649  10022  10528     -6      1    -50       C
ATOM   2771  N   ASP A 118     -16.840   4.989  -9.338  1.00 81.26           N
ANISOU 2771  N   ASP A 118    12086   9170   9617    365   -200    -80       N
ATOM   2772  CA  ASP A 118     -15.464   4.655  -9.010  1.00 84.85           C
ANISOU 2772  CA  ASP A 118    12592   9618  10030    527   -293   -110       C
ATOM   2773  C   ASP A 118     -14.686   5.821  -8.413  1.00 83.51           C
ANISOU 2773  C   ASP A 118    12294   9529   9906    603   -361   -139       C
ATOM   2774  O   ASP A 118     -13.492   5.668  -8.127  1.00 83.91           O
ANISOU 2774  O   ASP A 118    12360   9592   9929    743   -445   -178       O
ATOM   2775  CB  ASP A 118     -14.750   4.138 -10.255  1.00 87.74           C
ANISOU 2775  CB  ASP A 118    12906  10009  10422    570   -327   -129       C
ATOM   2776  CG  ASP A 118     -13.894   2.936  -9.957  1.00 97.59           C
ANISOU 2776  CG  ASP A 118    14331  11181  11569    704   -382   -146       C
ATOM   2777  OD1 ASP A 118     -12.910   2.701 -10.676  1.00101.88           O
ANISOU 2777  OD1 ASP A 118    14816  11763  12130    791   -442   -181       O
ATOM   2778  OD2 ASP A 118     -14.181   2.224  -8.977  1.00 98.93           O
ANISOU 2778  OD2 ASP A 118    14703  11249  11636    729   -366   -129       O
ATOM   2779  N   PHE A 119     -15.347   6.963  -8.197  1.00 76.91           N
ANISOU 2779  N   PHE A 119    11338   8748   9137    516   -326   -128       N
ATOM   2780  CA  PHE A 119     -14.760   8.200  -7.691  1.00 76.99           C
ANISOU 2780  CA  PHE A 119    11214   8839   9201    562   -376   -154       C
ATOM   2781  C   PHE A 119     -13.592   7.966  -6.743  1.00 81.76           C
ANISOU 2781  C   PHE A 119    11894   9429   9741    720   -462   -192       C
ATOM   2782  O   PHE A 119     -12.536   8.589  -6.894  1.00 89.65           O
ANISOU 2782  O   PHE A 119    12767  10509  10787    798   -528   -239       O
ATOM   2783  CB  PHE A 119     -15.842   9.030  -6.989  1.00 72.65           C
ANISOU 2783  CB  PHE A 119    10638   8294   8672    463   -319   -127       C
ATOM   2784  CG  PHE A 119     -15.305  10.142  -6.140  1.00 72.14           C
ANISOU 2784  CG  PHE A 119    10487   8286   8636    518   -367   -151       C
ATOM   2785  CD1 PHE A 119     -15.005  11.370  -6.700  1.00 72.91           C
ANISOU 2785  CD1 PHE A 119    10387   8482   8833    496   -382   -170       C
ATOM   2786  CD2 PHE A 119     -15.110   9.967  -4.778  1.00 75.92           C
ANISOU 2786  CD2 PHE A 119    11090   8716   9038    589   -394   -155       C
ATOM   2787  CE1 PHE A 119     -14.514  12.411  -5.919  1.00 74.44           C
ANISOU 2787  CE1 PHE A 119    10504   8728   9054    540   -421   -196       C
ATOM   2788  CE2 PHE A 119     -14.615  10.994  -3.990  1.00 76.04           C
ANISOU 2788  CE2 PHE A 119    11024   8787   9082    639   -438   -181       C
ATOM   2789  CZ  PHE A 119     -14.319  12.220  -4.563  1.00 76.18           C
ANISOU 2789  CZ  PHE A 119    10838   8906   9203    612   -450   -202       C
ATOM   2790  N   GLU A 120     -13.761   7.048  -5.786  1.00 76.75           N
ANISOU 2790  N   GLU A 120    11470   8695   8997    767   -460   -177       N
ATOM   2791  CA  GLU A 120     -12.769   6.898  -4.728  1.00 75.01           C
ANISOU 2791  CA  GLU A 120    11333   8459   8707    922   -544   -213       C
ATOM   2792  C   GLU A 120     -11.462   6.303  -5.234  1.00 76.93           C
ANISOU 2792  C   GLU A 120    11574   8725   8931   1063   -630   -265       C
ATOM   2793  O   GLU A 120     -10.400   6.624  -4.689  1.00 82.70           O
ANISOU 2793  O   GLU A 120    12266   9505   9651   1192   -715   -321       O
ATOM   2794  CB  GLU A 120     -13.331   6.062  -3.579  1.00 73.66           C
ANISOU 2794  CB  GLU A 120    11409   8166   8414    936   -516   -181       C
ATOM   2795  CG  GLU A 120     -12.869   6.569  -2.210  1.00 77.10           C
ANISOU 2795  CG  GLU A 120    11882   8606   8807   1031   -571   -203       C
ATOM   2796  CD  GLU A 120     -13.577   7.850  -1.780  1.00 80.02           C
ANISOU 2796  CD  GLU A 120    12120   9032   9251    928   -528   -188       C
ATOM   2797  OE1 GLU A 120     -14.826   7.901  -1.857  1.00 79.14           O
ANISOU 2797  OE1 GLU A 120    12029   8889   9152    783   -435   -143       O
ATOM   2798  OE2 GLU A 120     -12.885   8.807  -1.370  1.00 81.35           O
ANISOU 2798  OE2 GLU A 120    12163   9282   9464    990   -587   -226       O
ATOM   2799  N   LYS A 121     -11.502   5.445  -6.261  1.00 78.11           N
ANISOU 2799  N   LYS A 121    11758   8845   9074   1043   -611   -255       N
ATOM   2800  CA  LYS A 121     -10.252   4.994  -6.872  1.00 82.56           C
ANISOU 2800  CA  LYS A 121    12286   9448   9634   1170   -691   -312       C
ATOM   2801  C   LYS A 121      -9.602   6.118  -7.658  1.00 89.14           C
ANISOU 2801  C   LYS A 121    12864  10417  10587   1154   -717   -358       C
ATOM   2802  O   LYS A 121      -8.395   6.355  -7.538  1.00 87.37           O
ANISOU 2802  O   LYS A 121    12564  10262  10370   1275   -800   -430       O
ATOM   2803  CB  LYS A 121     -10.470   3.795  -7.799  1.00 86.48           C
ANISOU 2803  CB  LYS A 121    12884   9879  10095   1150   -662   -290       C
ATOM   2804  CG  LYS A 121      -9.397   3.716  -8.928  1.00 95.63           C
ANISOU 2804  CG  LYS A 121    13911  11118  11306   1218   -720   -346       C
ATOM   2805  CD  LYS A 121      -9.354   2.360  -9.675  1.00 96.97           C
ANISOU 2805  CD  LYS A 121    14211  11215  11418   1244   -715   -336       C
ATOM   2806  CE  LYS A 121     -10.037   2.384 -11.049  1.00 93.89           C
ANISOU 2806  CE  LYS A 121    13721  10847  11106   1100   -640   -303       C
ATOM   2807  NZ  LYS A 121      -9.869   1.052 -11.722  1.00 91.11           N
ANISOU 2807  NZ  LYS A 121    13498  10426  10694   1141   -644   -302       N
ATOM   2808  N   LEU A 122     -10.391   6.813  -8.482  1.00 90.51           N
ANISOU 2808  N   LEU A 122    12907  10630  10853   1006   -645   -323       N
ATOM   2809  CA  LEU A 122      -9.872   7.844  -9.373  1.00 86.73           C
ANISOU 2809  CA  LEU A 122    12204  10267  10483    973   -655   -360       C
ATOM   2810  C   LEU A 122      -9.611   9.169  -8.673  1.00 88.00           C
ANISOU 2810  C   LEU A 122    12241  10500  10694    974   -674   -387       C
ATOM   2811  O   LEU A 122      -9.035  10.070  -9.298  1.00 86.72           O
ANISOU 2811  O   LEU A 122    11902  10432  10614    957   -685   -428       O
ATOM   2812  CB  LEU A 122     -10.840   8.093 -10.534  1.00 79.78           C
ANISOU 2812  CB  LEU A 122    11245   9396   9673    822   -574   -312       C
ATOM   2813  CG  LEU A 122     -11.575   6.894 -11.131  1.00 75.19           C
ANISOU 2813  CG  LEU A 122    10792   8730   9046    772   -525   -268       C
ATOM   2814  CD1 LEU A 122     -12.835   7.344 -11.821  1.00 70.24           C
ANISOU 2814  CD1 LEU A 122    10099   8110   8478    614   -439   -219       C
ATOM   2815  CD2 LEU A 122     -10.676   6.176 -12.111  1.00 78.44           C
ANISOU 2815  CD2 LEU A 122    11187   9159   9456    840   -566   -304       C
ATOM   2816  N   LYS A 123     -10.028   9.314  -7.406  1.00 82.51           N
ANISOU 2816  N   LYS A 123    11639   9761   9949    988   -673   -367       N
ATOM   2817  CA  LYS A 123      -9.901  10.580  -6.696  1.00 73.71           C
ANISOU 2817  CA  LYS A 123    10415   8709   8881    980   -684   -387       C
ATOM   2818  C   LYS A 123      -8.457  11.081  -6.695  1.00 80.44           C
ANISOU 2818  C   LYS A 123    11143   9658   9763   1087   -764   -478       C
ATOM   2819  O   LYS A 123      -8.206  12.181  -7.203  1.00 85.38           O
ANISOU 2819  O   LYS A 123    11593  10369  10478   1031   -752   -504       O
ATOM   2820  CB  LYS A 123     -10.441  10.460  -5.268  1.00 65.35           C
ANISOU 2820  CB  LYS A 123     9500   7583   7748   1001   -681   -359       C
ATOM   2821  CG  LYS A 123     -10.110  11.655  -4.377  1.00 59.44           C
ANISOU 2821  CG  LYS A 123     8654   6897   7032   1023   -709   -391       C
ATOM   2822  CD  LYS A 123     -10.913  11.623  -3.088  1.00 70.29           C
ANISOU 2822  CD  LYS A 123    10163   8201   8343   1009   -685   -349       C
ATOM   2823  CE  LYS A 123     -10.372  10.573  -2.120  1.00 80.59           C
ANISOU 2823  CE  LYS A 123    11660   9433   9526   1152   -745   -368       C
ATOM   2824  NZ  LYS A 123      -9.603  11.158  -0.979  1.00 85.28           N
ANISOU 2824  NZ  LYS A 123    12235  10068  10098   1261   -816   -420       N
ATOM   2825  N   PRO A 124      -7.477  10.321  -6.181  1.00 76.63           N
ANISOU 2825  N   PRO A 124    10743   9167   9207   1240   -845   -534       N
ATOM   2826  CA  PRO A 124      -6.121  10.886  -6.065  1.00 71.93           C
ANISOU 2826  CA  PRO A 124    10014   8677   8640   1341   -921   -635       C
ATOM   2827  C   PRO A 124      -5.475  11.176  -7.407  1.00 73.59           C
ANISOU 2827  C   PRO A 124    10059   8971   8930   1307   -917   -683       C
ATOM   2828  O   PRO A 124      -4.649  12.096  -7.504  1.00 71.16           O
ANISOU 2828  O   PRO A 124     9589   8765   8682   1318   -941   -758       O
ATOM   2829  CB  PRO A 124      -5.349   9.805  -5.295  1.00 70.48           C
ANISOU 2829  CB  PRO A 124     9981   8454   8345   1520  -1009   -682       C
ATOM   2830  CG  PRO A 124      -6.384   8.836  -4.801  1.00 71.07           C
ANISOU 2830  CG  PRO A 124    10282   8391   8329   1501   -971   -594       C
ATOM   2831  CD  PRO A 124      -7.490   8.907  -5.780  1.00 74.58           C
ANISOU 2831  CD  PRO A 124    10696   8807   8832   1333   -873   -517       C
ATOM   2832  N   GLY A 125      -5.821  10.418  -8.446  1.00 67.60           N
ANISOU 2832  N   GLY A 125     9339   8174   8173   1262   -883   -645       N
ATOM   2833  CA  GLY A 125      -5.312  10.732  -9.767  1.00 62.85           C
ANISOU 2833  CA  GLY A 125     8584   7647   7648   1215   -869   -683       C
ATOM   2834  C   GLY A 125      -5.855  12.044 -10.291  1.00 67.58           C
ANISOU 2834  C   GLY A 125     9038   8294   8346   1069   -799   -655       C
ATOM   2835  O   GLY A 125      -5.124  12.826 -10.907  1.00 75.69           O
ANISOU 2835  O   GLY A 125     9907   9410   9440   1048   -800   -717       O
ATOM   2836  N   PHE A 126      -7.149  12.304 -10.054  1.00 63.04           N
ANISOU 2836  N   PHE A 126     8519   7659   7776    968   -735   -567       N
ATOM   2837  CA  PHE A 126      -7.738  13.588 -10.440  1.00 53.52           C
ANISOU 2837  CA  PHE A 126     7190   6492   6653    842   -674   -540       C
ATOM   2838  C   PHE A 126      -7.121  14.737  -9.662  1.00 49.12           C
ANISOU 2838  C   PHE A 126     6533   6003   6127    866   -701   -596       C
ATOM   2839  O   PHE A 126      -6.987  15.847 -10.185  1.00 57.26           O
ANISOU 2839  O   PHE A 126     7428   7095   7232    792   -670   -614       O
ATOM   2840  CB  PHE A 126      -9.258  13.576 -10.229  1.00 49.13           C
ANISOU 2840  CB  PHE A 126     6718   5863   6088    743   -609   -446       C
ATOM   2841  CG  PHE A 126      -9.942  14.793 -10.751  1.00 56.20           C
ANISOU 2841  CG  PHE A 126     7499   6793   7062    621   -550   -416       C
ATOM   2842  CD1 PHE A 126     -10.041  15.015 -12.114  1.00 59.92           C
ANISOU 2842  CD1 PHE A 126     7886   7292   7589    550   -513   -408       C
ATOM   2843  CD2 PHE A 126     -10.453  15.741  -9.883  1.00 62.91           C
ANISOU 2843  CD2 PHE A 126     8327   7648   7926    586   -534   -399       C
ATOM   2844  CE1 PHE A 126     -10.663  16.161 -12.611  1.00 64.33           C
ANISOU 2844  CE1 PHE A 126     8352   7878   8212    448   -463   -382       C
ATOM   2845  CE2 PHE A 126     -11.066  16.889 -10.368  1.00 68.47           C
ANISOU 2845  CE2 PHE A 126     8934   8382   8698    485   -484   -375       C
ATOM   2846  CZ  PHE A 126     -11.180  17.098 -11.737  1.00 63.28           C
ANISOU 2846  CZ  PHE A 126     8204   7749   8092    418   -449   -366       C
ATOM   2847  N   LEU A 127      -6.734  14.497  -8.414  1.00 54.96           N
ANISOU 2847  N   LEU A 127     7344   6732   6808    968   -757   -625       N
ATOM   2848  CA  LEU A 127      -6.140  15.574  -7.638  1.00 60.24           C
ANISOU 2848  CA  LEU A 127     7917   7469   7504    993   -783   -684       C
ATOM   2849  C   LEU A 127      -4.810  16.007  -8.244  1.00 60.67           C
ANISOU 2849  C   LEU A 127     7821   7626   7605   1028   -816   -789       C
ATOM   2850  O   LEU A 127      -4.522  17.204  -8.333  1.00 67.97           O
ANISOU 2850  O   LEU A 127     8613   8617   8594    970   -793   -827       O
ATOM   2851  CB  LEU A 127      -5.999  15.139  -6.182  1.00 61.97           C
ANISOU 2851  CB  LEU A 127     8255   7652   7641   1105   -841   -696       C
ATOM   2852  CG  LEU A 127      -7.351  15.092  -5.452  1.00 65.70           C
ANISOU 2852  CG  LEU A 127     8848   8035   8080   1042   -793   -600       C
ATOM   2853  CD1 LEU A 127      -7.331  14.088  -4.304  1.00 63.02           C
ANISOU 2853  CD1 LEU A 127     8692   7623   7632   1156   -842   -594       C
ATOM   2854  CD2 LEU A 127      -7.761  16.476  -4.951  1.00 60.95           C
ANISOU 2854  CD2 LEU A 127     8154   7470   7536    965   -760   -590       C
ATOM   2855  N   LYS A 128      -4.009  15.055  -8.720  1.00 61.58           N
ANISOU 2855  N   LYS A 128     7952   7756   7689   1115   -862   -842       N
ATOM   2856  CA  LYS A 128      -2.746  15.417  -9.355  1.00 69.35           C
ANISOU 2856  CA  LYS A 128     8788   8846   8718   1142   -888   -952       C
ATOM   2857  C   LYS A 128      -2.956  16.257 -10.613  1.00 70.19           C
ANISOU 2857  C   LYS A 128     8771   8985   8911   1000   -810   -937       C
ATOM   2858  O   LYS A 128      -2.054  17.009 -10.997  1.00 70.04           O
ANISOU 2858  O   LYS A 128     8612   9057   8942    981   -808  -1025       O
ATOM   2859  CB  LYS A 128      -1.932  14.153  -9.681  1.00 71.42           C
ANISOU 2859  CB  LYS A 128     9099   9113   8925   1265   -952  -1009       C
ATOM   2860  CG  LYS A 128      -1.379  13.404  -8.450  1.00 64.37           C
ANISOU 2860  CG  LYS A 128     8312   8207   7940   1436  -1046  -1058       C
ATOM   2861  N   GLU A 129      -4.139  16.176 -11.236  1.00 72.69           N
ANISOU 2861  N   GLU A 129     9142   9232   9243    897   -746   -831       N
ATOM   2862  CA  GLU A 129      -4.443  16.928 -12.454  1.00 61.32           C
ANISOU 2862  CA  GLU A 129     7609   7813   7876    769   -674   -807       C
ATOM   2863  C   GLU A 129      -4.875  18.372 -12.192  1.00 61.76           C
ANISOU 2863  C   GLU A 129     7594   7888   7985    676   -626   -789       C
ATOM   2864  O   GLU A 129      -4.860  19.184 -13.122  1.00 69.53           O
ANISOU 2864  O   GLU A 129     8489   8902   9027    582   -573   -793       O
ATOM   2865  CB  GLU A 129      -5.539  16.213 -13.252  1.00 48.21           C
ANISOU 2865  CB  GLU A 129     6036   6076   6205    708   -631   -710       C
ATOM   2866  CG  GLU A 129      -5.104  14.878 -13.842  1.00 59.38           C
ANISOU 2866  CG  GLU A 129     7507   7474   7579    778   -664   -727       C
ATOM   2867  CD  GLU A 129      -6.276  13.954 -14.163  1.00 65.65           C
ANISOU 2867  CD  GLU A 129     8429   8175   8339    741   -632   -630       C
ATOM   2868  OE1 GLU A 129      -6.309  12.830 -13.612  1.00 71.55           O
ANISOU 2868  OE1 GLU A 129     9305   8867   9015    824   -671   -619       O
ATOM   2869  OE2 GLU A 129      -7.156  14.340 -14.965  1.00 60.69           O
ANISOU 2869  OE2 GLU A 129     7779   7530   7752    630   -569   -569       O
ATOM   2870  N   ILE A 130      -5.256  18.717 -10.966  1.00 56.23           N
ANISOU 2870  N   ILE A 130     6936   7167   7262    699   -642   -770       N
ATOM   2871  CA  ILE A 130      -5.817  20.037 -10.675  1.00 49.67           C
ANISOU 2871  CA  ILE A 130     6053   6342   6475    611   -595   -742       C
ATOM   2872  C   ILE A 130      -4.793  21.161 -10.854  1.00 54.24           C
ANISOU 2872  C   ILE A 130     6493   7008   7108    585   -587   -834       C
ATOM   2873  O   ILE A 130      -5.151  22.231 -11.381  1.00 48.70           O
ANISOU 2873  O   ILE A 130     5734   6313   6458    482   -527   -813       O
ATOM   2874  CB  ILE A 130      -6.443  20.050  -9.270  1.00 40.34           C
ANISOU 2874  CB  ILE A 130     4957   5118   5253    648   -616   -703       C
ATOM   2875  CG1 ILE A 130      -7.626  19.081  -9.239  1.00 48.86           C
ANISOU 2875  CG1 ILE A 130     6172   6106   6285    636   -600   -608       C
ATOM   2876  CG2 ILE A 130      -6.936  21.440  -8.877  1.00 33.88           C
ANISOU 2876  CG2 ILE A 130     4081   4311   4478    569   -575   -684       C
ATOM   2877  CD1 ILE A 130      -8.525  19.255  -8.027  1.00 48.63           C
ANISOU 2877  CD1 ILE A 130     6224   6028   6224    633   -595   -555       C
ATOM   2878  N   PRO A 131      -3.522  20.999 -10.459  1.00 53.73           N
ANISOU 2878  N   PRO A 131     6370   7013   7030    673   -642   -944       N
ATOM   2879  CA  PRO A 131      -2.599  22.145 -10.588  1.00 53.64           C
ANISOU 2879  CA  PRO A 131     6222   7088   7071    631   -622  -1040       C
ATOM   2880  C   PRO A 131      -2.331  22.570 -12.028  1.00 49.29           C
ANISOU 2880  C   PRO A 131     5592   6564   6572    533   -560  -1058       C
ATOM   2881  O   PRO A 131      -2.182  23.770 -12.276  1.00 56.06           O
ANISOU 2881  O   PRO A 131     6373   7450   7476    444   -507  -1084       O
ATOM   2882  CB  PRO A 131      -1.324  21.654  -9.886  1.00 53.72           C
ANISOU 2882  CB  PRO A 131     6192   7171   7048    760   -702  -1162       C
ATOM   2883  CG  PRO A 131      -1.778  20.557  -8.990  1.00 52.20           C
ANISOU 2883  CG  PRO A 131     6137   6915   6782    869   -764  -1110       C
ATOM   2884  CD  PRO A 131      -2.865  19.872  -9.772  1.00 54.05           C
ANISOU 2884  CD  PRO A 131     6469   7061   7007    815   -724   -994       C
ATOM   2885  N   GLU A 132      -2.274  21.647 -12.992  1.00 48.05           N
ANISOU 2885  N   GLU A 132     5459   6393   6405    544   -561  -1045       N
ATOM   2886  CA  GLU A 132      -2.126  22.097 -14.375  1.00 62.59           C
ANISOU 2886  CA  GLU A 132     7237   8252   8293    443   -496  -1053       C
ATOM   2887  C   GLU A 132      -3.357  22.876 -14.857  1.00 59.93           C
ANISOU 2887  C   GLU A 132     6937   7849   7983    330   -426   -945       C
ATOM   2888  O   GLU A 132      -3.209  23.920 -15.504  1.00 52.32           O
ANISOU 2888  O   GLU A 132     5912   6905   7060    236   -365   -964       O
ATOM   2889  CB  GLU A 132      -1.808  20.924 -15.310  1.00 68.75           C
ANISOU 2889  CB  GLU A 132     8035   9032   9056    481   -514  -1063       C
ATOM   2890  CG  GLU A 132      -2.510  19.616 -15.018  1.00 83.02           C
ANISOU 2890  CG  GLU A 132     9968  10768  10808    557   -558   -986       C
ATOM   2891  CD  GLU A 132      -1.722  18.406 -15.515  1.00 96.12           C
ANISOU 2891  CD  GLU A 132    11632  12451  12437    642   -605  -1043       C
ATOM   2892  OE1 GLU A 132      -1.732  17.350 -14.843  1.00 99.71           O
ANISOU 2892  OE1 GLU A 132    12177  12875  12833    752   -669  -1035       O
ATOM   2893  OE2 GLU A 132      -1.077  18.516 -16.580  1.00101.23           O
ANISOU 2893  OE2 GLU A 132    12199  13147  13117    601   -578  -1098       O
ATOM   2894  N   LYS A 133      -4.576  22.413 -14.537  1.00 51.70           N
ANISOU 2894  N   LYS A 133     5999   6732   6915    337   -431   -839       N
ATOM   2895  CA  LYS A 133      -5.768  23.159 -14.955  1.00 45.44           C
ANISOU 2895  CA  LYS A 133     5234   5886   6144    241   -371   -747       C
ATOM   2896  C   LYS A 133      -5.731  24.589 -14.431  1.00 52.90           C
ANISOU 2896  C   LYS A 133     6130   6851   7120    189   -341   -767       C
ATOM   2897  O   LYS A 133      -6.005  25.540 -15.176  1.00 64.30           O
ANISOU 2897  O   LYS A 133     7549   8287   8596    100   -282   -748       O
ATOM   2898  CB  LYS A 133      -7.058  22.469 -14.487  1.00 42.14           C
ANISOU 2898  CB  LYS A 133     4926   5396   5691    259   -383   -648       C
ATOM   2899  CG  LYS A 133      -7.247  21.045 -14.995  1.00 45.21           C
ANISOU 2899  CG  LYS A 133     5381   5751   6044    301   -404   -619       C
ATOM   2900  CD  LYS A 133      -8.441  20.382 -14.349  1.00 51.83           C
ANISOU 2900  CD  LYS A 133     6329   6521   6842    314   -411   -538       C
ATOM   2901  CE  LYS A 133      -9.121  19.420 -15.312  1.00 57.69           C
ANISOU 2901  CE  LYS A 133     7130   7220   7570    290   -392   -483       C
ATOM   2902  NZ  LYS A 133      -8.500  18.076 -15.293  1.00 64.39           N
ANISOU 2902  NZ  LYS A 133     8032   8060   8375    375   -437   -511       N
ATOM   2903  N   MET A 134      -5.378  24.761 -13.147  1.00 44.34           N
ANISOU 2903  N   MET A 134     5036   5790   6021    247   -382   -807       N
ATOM   2904  CA  MET A 134      -5.373  26.092 -12.543  1.00 46.93           C
ANISOU 2904  CA  MET A 134     5322   6135   6376    201   -356   -826       C
ATOM   2905  C   MET A 134      -4.248  26.956 -13.091  1.00 49.31           C
ANISOU 2905  C   MET A 134     5519   6501   6714    148   -320   -924       C
ATOM   2906  O   MET A 134      -4.414  28.176 -13.208  1.00 50.21           O
ANISOU 2906  O   MET A 134     5610   6610   6857     68   -267   -922       O
ATOM   2907  CB  MET A 134      -5.253  25.992 -11.018  1.00 48.91           C
ANISOU 2907  CB  MET A 134     5589   6396   6597    281   -411   -848       C
ATOM   2908  CG  MET A 134      -6.296  25.119 -10.375  1.00 45.75           C
ANISOU 2908  CG  MET A 134     5299   5930   6152    330   -442   -760       C
ATOM   2909  SD  MET A 134      -7.900  25.917 -10.448  1.00 58.31           S
ANISOU 2909  SD  MET A 134     6939   7456   7760    239   -385   -649       S
ATOM   2910  CE  MET A 134      -8.785  24.749 -11.473  1.00 50.73           C
ANISOU 2910  CE  MET A 134     6055   6441   6779    225   -372   -571       C
ATOM   2911  N   LYS A 135      -3.096  26.352 -13.407  1.00 48.55           N
ANISOU 2911  N   LYS A 135     5365   6466   6616    192   -346  -1018       N
ATOM   2912  CA  LYS A 135      -2.031  27.103 -14.062  1.00 51.39           C
ANISOU 2912  CA  LYS A 135     5624   6891   7010    128   -301  -1120       C
ATOM   2913  C   LYS A 135      -2.525  27.710 -15.371  1.00 53.09           C
ANISOU 2913  C   LYS A 135     5856   7064   7251     14   -220  -1066       C
ATOM   2914  O   LYS A 135      -2.207  28.864 -15.693  1.00 48.27           O
ANISOU 2914  O   LYS A 135     5204   6469   6669    -75   -157  -1105       O
ATOM   2915  CB  LYS A 135      -0.820  26.202 -14.303  1.00 44.09           C
ANISOU 2915  CB  LYS A 135     4637   6040   6075    197   -344  -1228       C
ATOM   2916  CG  LYS A 135       0.453  26.951 -14.695  1.00 52.57           C
ANISOU 2916  CG  LYS A 135     5590   7202   7182    141   -304  -1366       C
ATOM   2917  CD  LYS A 135       1.665  26.025 -14.659  1.00 59.19           C
ANISOU 2917  CD  LYS A 135     6357   8128   8005    235   -364  -1489       C
ATOM   2918  CE  LYS A 135       2.814  26.523 -15.508  1.00 64.42           C
ANISOU 2918  CE  LYS A 135     6904   8873   8699    160   -309  -1618       C
ATOM   2919  NZ  LYS A 135       3.472  25.374 -16.222  1.00 66.49           N
ANISOU 2919  NZ  LYS A 135     7138   9177   8947    222   -345  -1674       N
ATOM   2920  N   LEU A 136      -3.328  26.951 -16.124  1.00 50.06           N
ANISOU 2920  N   LEU A 136     5541   6625   6854     16   -220   -977       N
ATOM   2921  CA  LEU A 136      -3.906  27.473 -17.356  1.00 48.07           C
ANISOU 2921  CA  LEU A 136     5317   6329   6618    -79   -151   -919       C
ATOM   2922  C   LEU A 136      -4.787  28.683 -17.073  1.00 45.97           C
ANISOU 2922  C   LEU A 136     5089   6015   6362   -141   -110   -857       C
ATOM   2923  O   LEU A 136      -4.663  29.715 -17.735  1.00 41.04           O
ANISOU 2923  O   LEU A 136     4454   5382   5756   -227    -45   -870       O
ATOM   2924  CB  LEU A 136      -4.698  26.378 -18.079  1.00 44.65           C
ANISOU 2924  CB  LEU A 136     4952   5847   6165    -56   -167   -836       C
ATOM   2925  CG  LEU A 136      -3.895  25.115 -18.387  1.00 52.39           C
ANISOU 2925  CG  LEU A 136     5908   6866   7131     11   -209   -890       C
ATOM   2926  CD1 LEU A 136      -4.835  23.953 -18.614  1.00 60.39           C
ANISOU 2926  CD1 LEU A 136     7006   7824   8115     53   -238   -800       C
ATOM   2927  CD2 LEU A 136      -2.952  25.296 -19.569  1.00 44.40           C
ANISOU 2927  CD2 LEU A 136     4832   5899   6141    -45   -165   -964       C
ATOM   2928  N   PHE A 137      -5.686  28.579 -16.087  1.00 46.60           N
ANISOU 2928  N   PHE A 137     5219   6061   6426    -96   -147   -792       N
ATOM   2929  CA  PHE A 137      -6.546  29.717 -15.780  1.00 42.78           C
ANISOU 2929  CA  PHE A 137     4770   5536   5950   -146   -113   -737       C
ATOM   2930  C   PHE A 137      -5.725  30.910 -15.304  1.00 48.93           C
ANISOU 2930  C   PHE A 137     5490   6352   6751   -188    -83   -817       C
ATOM   2931  O   PHE A 137      -5.952  32.045 -15.738  1.00 52.78           O
ANISOU 2931  O   PHE A 137     5991   6812   7250   -265    -24   -804       O
ATOM   2932  CB  PHE A 137      -7.606  29.322 -14.745  1.00 43.86           C
ANISOU 2932  CB  PHE A 137     4963   5637   6064    -91   -157   -665       C
ATOM   2933  CG  PHE A 137      -8.718  28.488 -15.313  1.00 42.25           C
ANISOU 2933  CG  PHE A 137     4828   5385   5842    -82   -164   -577       C
ATOM   2934  CD1 PHE A 137      -9.771  29.073 -15.970  1.00 49.94           C
ANISOU 2934  CD1 PHE A 137     5842   6314   6819   -135   -126   -508       C
ATOM   2935  CD2 PHE A 137      -8.690  27.117 -15.210  1.00 48.61           C
ANISOU 2935  CD2 PHE A 137     5658   6189   6622    -19   -207   -569       C
ATOM   2936  CE1 PHE A 137     -10.793  28.299 -16.512  1.00 53.23           C
ANISOU 2936  CE1 PHE A 137     6311   6694   7219   -129   -131   -439       C
ATOM   2937  CE2 PHE A 137      -9.701  26.340 -15.741  1.00 52.50           C
ANISOU 2937  CE2 PHE A 137     6212   6639   7098    -20   -207   -495       C
ATOM   2938  CZ  PHE A 137     -10.752  26.929 -16.396  1.00 49.98           C
ANISOU 2938  CZ  PHE A 137     5920   6284   6786    -77   -169   -433       C
ATOM   2939  N   SER A 138      -4.747  30.668 -14.429  1.00 59.87           N
ANISOU 2939  N   SER A 138     6811   7799   8136   -136   -122   -906       N
ATOM   2940  CA  SER A 138      -3.947  31.766 -13.900  1.00 52.17           C
ANISOU 2940  CA  SER A 138     5773   6868   7181   -176    -95   -993       C
ATOM   2941  C   SER A 138      -3.174  32.469 -15.005  1.00 50.94           C
ANISOU 2941  C   SER A 138     5575   6732   7046   -273    -19  -1058       C
ATOM   2942  O   SER A 138      -3.106  33.705 -15.035  1.00 42.85           O
ANISOU 2942  O   SER A 138     4550   5695   6036   -352     41  -1077       O
ATOM   2943  CB  SER A 138      -2.978  31.258 -12.838  1.00 47.59           C
ANISOU 2943  CB  SER A 138     5127   6363   6594    -92   -157  -1088       C
ATOM   2944  OG  SER A 138      -2.161  32.325 -12.405  1.00 51.50           O
ANISOU 2944  OG  SER A 138     5549   6907   7110   -138   -125  -1184       O
ATOM   2945  N   GLU A 139      -2.589  31.699 -15.932  1.00 47.52           N
ANISOU 2945  N   GLU A 139     5115   6327   6614   -271    -16  -1095       N
ATOM   2946  CA  GLU A 139      -1.839  32.324 -17.016  1.00 42.88           C
ANISOU 2946  CA  GLU A 139     4492   5757   6043   -370     62  -1162       C
ATOM   2947  C   GLU A 139      -2.764  33.088 -17.960  1.00 47.92           C
ANISOU 2947  C   GLU A 139     5220   6310   6678   -453    129  -1068       C
ATOM   2948  O   GLU A 139      -2.425  34.189 -18.406  1.00 54.97           O
ANISOU 2948  O   GLU A 139     6116   7192   7579   -549    206  -1105       O
ATOM   2949  CB  GLU A 139      -1.020  31.275 -17.757  1.00 38.75           C
ANISOU 2949  CB  GLU A 139     3918   5286   5519   -343     46  -1225       C
ATOM   2950  CG  GLU A 139       0.358  31.042 -17.122  1.00 50.15           C
ANISOU 2950  CG  GLU A 139     5247   6836   6971   -302     14  -1375       C
ATOM   2951  CD  GLU A 139       0.893  29.649 -17.403  1.00 70.45           C
ANISOU 2951  CD  GLU A 139     7784   9454   9528   -215    -47  -1414       C
ATOM   2952  OE1 GLU A 139       1.955  29.286 -16.846  1.00 76.44           O
ANISOU 2952  OE1 GLU A 139     8453  10303  10287   -154    -90  -1536       O
ATOM   2953  OE2 GLU A 139       0.248  28.917 -18.185  1.00 71.73           O
ANISOU 2953  OE2 GLU A 139     8010   9564   9678   -203    -53  -1327       O
ATOM   2954  N   PHE A 140      -3.954  32.540 -18.233  1.00 45.35           N
ANISOU 2954  N   PHE A 140     4973   5924   6336   -416    101   -951       N
ATOM   2955  CA  PHE A 140      -4.931  33.212 -19.085  1.00 44.18           C
ANISOU 2955  CA  PHE A 140     4911   5697   6178   -474    151   -862       C
ATOM   2956  C   PHE A 140      -5.357  34.547 -18.491  1.00 47.82           C
ANISOU 2956  C   PHE A 140     5407   6122   6640   -515    183   -844       C
ATOM   2957  O   PHE A 140      -5.358  35.573 -19.179  1.00 62.38           O
ANISOU 2957  O   PHE A 140     7295   7928   8480   -596    253   -843       O
ATOM   2958  CB  PHE A 140      -6.142  32.296 -19.282  1.00 53.23           C
ANISOU 2958  CB  PHE A 140     6119   6799   7306   -414    103   -754       C
ATOM   2959  CG  PHE A 140      -7.214  32.858 -20.180  1.00 47.85           C
ANISOU 2959  CG  PHE A 140     5524   6047   6611   -456    141   -667       C
ATOM   2960  CD1 PHE A 140      -6.924  33.240 -21.488  1.00 50.16           C
ANISOU 2960  CD1 PHE A 140     5842   6318   6899   -524    203   -677       C
ATOM   2961  CD2 PHE A 140      -8.527  32.958 -19.731  1.00 41.34           C
ANISOU 2961  CD2 PHE A 140     4755   5178   5773   -421    113   -579       C
ATOM   2962  CE1 PHE A 140      -7.921  33.744 -22.325  1.00 46.83           C
ANISOU 2962  CE1 PHE A 140     5509   5829   6456   -549    231   -599       C
ATOM   2963  CE2 PHE A 140      -9.540  33.459 -20.560  1.00 44.49           C
ANISOU 2963  CE2 PHE A 140     5231   5519   6155   -446    139   -508       C
ATOM   2964  CZ  PHE A 140      -9.236  33.851 -21.861  1.00 45.37           C
ANISOU 2964  CZ  PHE A 140     5374   5606   6258   -505    195   -516       C
ATOM   2965  N   LEU A 141      -5.726  34.554 -17.212  1.00 44.54           N
ANISOU 2965  N   LEU A 141     4982   5715   6225   -458    133   -828       N
ATOM   2966  CA  LEU A 141      -6.149  35.799 -16.565  1.00 47.69           C
ANISOU 2966  CA  LEU A 141     5412   6082   6625   -490    158   -811       C
ATOM   2967  C   LEU A 141      -5.043  36.854 -16.580  1.00 48.64           C
ANISOU 2967  C   LEU A 141     5491   6230   6760   -572    224   -913       C
ATOM   2968  O   LEU A 141      -5.314  38.042 -16.800  1.00 54.30           O
ANISOU 2968  O   LEU A 141     6264   6897   7471   -638    282   -897       O
ATOM   2969  CB  LEU A 141      -6.585  35.522 -15.131  1.00 36.19           C
ANISOU 2969  CB  LEU A 141     3941   4640   5167   -413     91   -791       C
ATOM   2970  CG  LEU A 141      -6.891  36.735 -14.256  1.00 42.01           C
ANISOU 2970  CG  LEU A 141     4696   5359   5909   -436    108   -788       C
ATOM   2971  CD1 LEU A 141      -8.104  37.472 -14.765  1.00 36.97           C
ANISOU 2971  CD1 LEU A 141     4149   4642   5255   -464    137   -696       C
ATOM   2972  CD2 LEU A 141      -7.124  36.273 -12.812  1.00 47.72           C
ANISOU 2972  CD2 LEU A 141     5394   6108   6629   -355     39   -782       C
ATOM   2973  N   GLY A 142      -3.796  36.442 -16.341  1.00 39.44           N
ANISOU 2973  N   GLY A 142     4231   5145   5611   -567    216  -1023       N
ATOM   2974  CA  GLY A 142      -2.694  37.390 -16.315  1.00 29.63           C
ANISOU 2974  CA  GLY A 142     2935   3941   4383   -651    282  -1137       C
ATOM   2975  C   GLY A 142      -2.913  38.426 -15.242  1.00 44.61           C
ANISOU 2975  C   GLY A 142     4840   5825   6284   -663    288  -1141       C
ATOM   2976  O   GLY A 142      -3.486  38.144 -14.184  1.00 41.89           O
ANISOU 2976  O   GLY A 142     4496   5483   5937   -584    221  -1097       O
ATOM   2977  N   LYS A 143      -2.490  39.659 -15.516  1.00 40.39           N
ANISOU 2977  N   LYS A 143     4323   5272   5752   -767    375  -1191       N
ATOM   2978  CA  LYS A 143      -2.734  40.739 -14.570  1.00 33.88           C
ANISOU 2978  CA  LYS A 143     3517   4426   4928   -786    388  -1192       C
ATOM   2979  C   LYS A 143      -4.085  41.432 -14.788  1.00 40.53           C
ANISOU 2979  C   LYS A 143     4486   5165   5748   -791    402  -1066       C
ATOM   2980  O   LYS A 143      -4.321  42.495 -14.214  1.00 47.51           O
ANISOU 2980  O   LYS A 143     5405   6016   6629   -822    429  -1063       O
ATOM   2981  CB  LYS A 143      -1.587  41.745 -14.630  1.00 36.48           C
ANISOU 2981  CB  LYS A 143     3803   4789   5269   -897    476  -1319       C
ATOM   2982  CG  LYS A 143      -0.238  41.148 -14.247  1.00 54.60           C
ANISOU 2982  CG  LYS A 143     5956   7203   7587   -884    456  -1464       C
ATOM   2983  CD  LYS A 143      -0.109  40.933 -12.734  1.00 70.82           C
ANISOU 2983  CD  LYS A 143     7937   9320   9653   -795    376  -1500       C
ATOM   2984  CE  LYS A 143      -0.329  39.455 -12.353  1.00 80.86           C
ANISOU 2984  CE  LYS A 143     9175  10629  10919   -660    266  -1463       C
ATOM   2985  NZ  LYS A 143      -0.751  39.232 -10.933  1.00 84.29           N
ANISOU 2985  NZ  LYS A 143     9598  11078  11350   -560    183  -1435       N
ATOM   2986  N   ARG A 144      -4.977  40.849 -15.589  1.00 47.07           N
ANISOU 2986  N   ARG A 144     5381   5944   6560   -757    381   -967       N
ATOM   2987  CA  ARG A 144      -6.254  41.480 -15.890  1.00 47.81           C
ANISOU 2987  CA  ARG A 144     5590   5947   6628   -754    390   -859       C
ATOM   2988  C   ARG A 144      -7.141  41.555 -14.645  1.00 43.67           C
ANISOU 2988  C   ARG A 144     5069   5418   6105   -680    326   -805       C
ATOM   2989  O   ARG A 144      -7.057  40.727 -13.738  1.00 46.16           O
ANISOU 2989  O   ARG A 144     5317   5788   6435   -611    260   -816       O
ATOM   2990  CB  ARG A 144      -6.967  40.718 -17.017  1.00 50.68           C
ANISOU 2990  CB  ARG A 144     6007   6274   6973   -726    375   -780       C
ATOM   2991  CG  ARG A 144      -6.205  40.705 -18.349  1.00 41.62           C
ANISOU 2991  CG  ARG A 144     4873   5120   5819   -802    443   -823       C
ATOM   2992  CD  ARG A 144      -6.839  39.755 -19.377  1.00 36.15           C
ANISOU 2992  CD  ARG A 144     4217   4406   5111   -763    416   -751       C
ATOM   2993  NE  ARG A 144      -6.040  39.736 -20.598  1.00 34.95           N
ANISOU 2993  NE  ARG A 144     4074   4253   4953   -837    482   -799       N
ATOM   2994  CZ  ARG A 144      -4.893  39.065 -20.727  1.00 43.77           C
ANISOU 2994  CZ  ARG A 144     5097   5443   6092   -856    489   -890       C
ATOM   2995  NH1 ARG A 144      -4.429  38.304 -19.735  1.00 40.98           N
ANISOU 2995  NH1 ARG A 144     4639   5167   5765   -795    426   -938       N
ATOM   2996  NH2 ARG A 144      -4.220  39.112 -21.867  1.00 46.83           N
ANISOU 2996  NH2 ARG A 144     5497   5826   6471   -930    555   -934       N
ATOM   2997  N   THR A 145      -7.978  42.590 -14.598  1.00 41.93           N
ANISOU 2997  N   THR A 145     4936   5129   5866   -695    349   -749       N
ATOM   2998  CA  THR A 145      -8.954  42.715 -13.521  1.00 41.01           C
ANISOU 2998  CA  THR A 145     4831   5002   5748   -629    294   -692       C
ATOM   2999  C   THR A 145     -10.046  41.662 -13.636  1.00 48.40           C
ANISOU 2999  C   THR A 145     5781   5933   6675   -549    228   -607       C
ATOM   3000  O   THR A 145     -10.489  41.106 -12.627  1.00 61.77           O
ANISOU 3000  O   THR A 145     7441   7655   8375   -485    168   -586       O
ATOM   3001  CB  THR A 145      -9.572  44.104 -13.547  1.00 47.49           C
ANISOU 3001  CB  THR A 145     5746   5750   6547   -663    336   -659       C
ATOM   3002  OG1 THR A 145      -8.535  45.078 -13.379  1.00 52.96           O
ANISOU 3002  OG1 THR A 145     6428   6447   7247   -746    404   -745       O
ATOM   3003  CG2 THR A 145     -10.635  44.244 -12.447  1.00 38.61           C
ANISOU 3003  CG2 THR A 145     4630   4619   5421   -593    278   -603       C
ATOM   3004  N   TRP A 146     -10.505  41.382 -14.852  1.00 45.35           N
ANISOU 3004  N   TRP A 146     5450   5510   6270   -556    242   -559       N
ATOM   3005  CA  TRP A 146     -11.449  40.304 -15.094  1.00 43.07           C
ANISOU 3005  CA  TRP A 146     5168   5222   5973   -491    187   -491       C
ATOM   3006  C   TRP A 146     -10.967  39.532 -16.298  1.00 42.83           C
ANISOU 3006  C   TRP A 146     5132   5200   5942   -511    204   -501       C
ATOM   3007  O   TRP A 146      -9.998  39.922 -16.953  1.00 45.32           O
ANISOU 3007  O   TRP A 146     5445   5515   6260   -576    260   -556       O
ATOM   3008  CB  TRP A 146     -12.867  40.814 -15.327  1.00 45.64           C
ANISOU 3008  CB  TRP A 146     5575   5493   6273   -463    177   -412       C
ATOM   3009  CG  TRP A 146     -13.359  41.743 -14.289  1.00 47.96           C
ANISOU 3009  CG  TRP A 146     5885   5772   6564   -450    168   -404       C
ATOM   3010  CD1 TRP A 146     -13.442  43.106 -14.380  1.00 43.22           C
ANISOU 3010  CD1 TRP A 146     5352   5122   5949   -485    212   -407       C
ATOM   3011  CD2 TRP A 146     -13.858  41.393 -12.997  1.00 52.83           C
ANISOU 3011  CD2 TRP A 146     6460   6420   7192   -397    115   -392       C
ATOM   3012  NE1 TRP A 146     -13.970  43.624 -13.221  1.00 44.11           N
ANISOU 3012  NE1 TRP A 146     5459   5237   6064   -455    185   -397       N
ATOM   3013  CE2 TRP A 146     -14.239  42.593 -12.357  1.00 49.27           C
ANISOU 3013  CE2 TRP A 146     6044   5941   6734   -402    127   -388       C
ATOM   3014  CE3 TRP A 146     -14.024  40.182 -12.316  1.00 56.10           C
ANISOU 3014  CE3 TRP A 146     6820   6879   7616   -348     62   -384       C
ATOM   3015  CZ2 TRP A 146     -14.774  42.615 -11.057  1.00 47.52           C
ANISOU 3015  CZ2 TRP A 146     5796   5741   6520   -361     87   -379       C
ATOM   3016  CZ3 TRP A 146     -14.559  40.207 -11.024  1.00 51.60           C
ANISOU 3016  CZ3 TRP A 146     6233   6325   7048   -309     25   -373       C
ATOM   3017  CH2 TRP A 146     -14.924  41.418 -10.412  1.00 43.98           C
ANISOU 3017  CH2 TRP A 146     5295   5337   6080   -316     38   -371       C
ATOM   3018  N   PHE A 147     -11.671  38.442 -16.607  1.00 41.76           N
ANISOU 3018  N   PHE A 147     4996   5070   5799   -460    160   -449       N
ATOM   3019  CA  PHE A 147     -11.080  37.463 -17.513  1.00 45.23           C
ANISOU 3019  CA  PHE A 147     5410   5532   6243   -468    163   -468       C
ATOM   3020  C   PHE A 147     -11.102  37.909 -18.970  1.00 55.87           C
ANISOU 3020  C   PHE A 147     6822   6834   7571   -517    217   -453       C
ATOM   3021  O   PHE A 147     -10.238  37.487 -19.747  1.00 61.99           O
ANISOU 3021  O   PHE A 147     7574   7628   8352   -552    244   -494       O
ATOM   3022  CB  PHE A 147     -11.778  36.128 -17.360  1.00 36.58           C
ANISOU 3022  CB  PHE A 147     4300   4454   5145   -402    103   -422       C
ATOM   3023  CG  PHE A 147     -11.127  35.210 -16.364  1.00 36.73           C
ANISOU 3023  CG  PHE A 147     4250   4527   5178   -361     59   -464       C
ATOM   3024  CD1 PHE A 147     -10.048  34.424 -16.719  1.00 37.29           C
ANISOU 3024  CD1 PHE A 147     4271   4639   5260   -361     57   -520       C
ATOM   3025  CD2 PHE A 147     -11.639  35.086 -15.091  1.00 38.12           C
ANISOU 3025  CD2 PHE A 147     4418   4712   5353   -314     17   -447       C
ATOM   3026  CE1 PHE A 147      -9.467  33.543 -15.784  1.00 47.27           C
ANISOU 3026  CE1 PHE A 147     5482   5951   6528   -307      8   -560       C
ATOM   3027  CE2 PHE A 147     -11.066  34.197 -14.154  1.00 41.84           C
ANISOU 3027  CE2 PHE A 147     4843   5227   5828   -265    -28   -483       C
ATOM   3028  CZ  PHE A 147      -9.994  33.432 -14.494  1.00 32.42           C
ANISOU 3028  CZ  PHE A 147     3605   4073   4641   -257    -35   -539       C
ATOM   3029  N   ALA A 148     -12.064  38.743 -19.365  1.00 54.56           N
ANISOU 3029  N   ALA A 148     6742   6610   7379   -518    231   -399       N
ATOM   3030  CA  ALA A 148     -12.069  39.323 -20.699  1.00 49.60           C
ANISOU 3030  CA  ALA A 148     6194   5928   6722   -562    284   -386       C
ATOM   3031  C   ALA A 148     -11.449  40.709 -20.716  1.00 58.39           C
ANISOU 3031  C   ALA A 148     7359   7003   7825   -631    353   -427       C
ATOM   3032  O   ALA A 148     -11.515  41.404 -21.736  1.00 62.81           O
ANISOU 3032  O   ALA A 148     8011   7502   8350   -670    405   -413       O
ATOM   3033  CB  ALA A 148     -13.494  39.370 -21.257  1.00 44.71           C
ANISOU 3033  CB  ALA A 148     5649   5267   6070   -511    256   -308       C
ATOM   3034  N   GLY A 149     -10.846  41.124 -19.610  1.00 60.89           N
ANISOU 3034  N   GLY A 149     7622   7349   8165   -649    358   -478       N
ATOM   3035  CA  GLY A 149     -10.145  42.388 -19.567  1.00 60.72           C
ANISOU 3035  CA  GLY A 149     7640   7296   8136   -726    430   -529       C
ATOM   3036  C   GLY A 149     -10.631  43.277 -18.447  1.00 55.80           C
ANISOU 3036  C   GLY A 149     7034   6656   7512   -706    416   -517       C
ATOM   3037  O   GLY A 149     -10.794  42.819 -17.312  1.00 58.53           O
ANISOU 3037  O   GLY A 149     7304   7050   7883   -656    360   -519       O
ATOM   3038  N   ASP A 150     -10.901  44.542 -18.771  1.00 55.03           N
ANISOU 3038  N   ASP A 150     7045   6483   7379   -742    467   -503       N
ATOM   3039  CA  ASP A 150     -11.144  45.562 -17.760  1.00 56.18           C
ANISOU 3039  CA  ASP A 150     7213   6608   7523   -741    469   -507       C
ATOM   3040  C   ASP A 150     -12.568  45.562 -17.222  1.00 58.25           C
ANISOU 3040  C   ASP A 150     7501   6857   7774   -648    399   -431       C
ATOM   3041  O   ASP A 150     -12.796  46.136 -16.155  1.00 60.22           O
ANISOU 3041  O   ASP A 150     7738   7109   8031   -632    383   -436       O
ATOM   3042  CB  ASP A 150     -10.820  46.955 -18.320  1.00 51.82           C
ANISOU 3042  CB  ASP A 150     6781   5975   6933   -819    558   -528       C
ATOM   3043  CG  ASP A 150      -9.352  47.320 -18.176  1.00 40.53           C
ANISOU 3043  CG  ASP A 150     5303   4572   5523   -924    634   -631       C
ATOM   3044  N   LYS A 151     -13.532  44.953 -17.909  1.00 62.35           N
ANISOU 3044  N   LYS A 151     8051   7365   8274   -589    357   -368       N
ATOM   3045  CA  LYS A 151     -14.931  45.097 -17.521  1.00 70.66           C
ANISOU 3045  CA  LYS A 151     9136   8404   9310   -509    300   -307       C
ATOM   3046  C   LYS A 151     -15.552  43.742 -17.204  1.00 62.92           C
ANISOU 3046  C   LYS A 151     8070   7484   8351   -446    229   -279       C
ATOM   3047  O   LYS A 151     -15.216  42.732 -17.827  1.00 64.28           O
ANISOU 3047  O   LYS A 151     8205   7684   8534   -452    225   -281       O
ATOM   3048  CB  LYS A 151     -15.731  45.836 -18.614  1.00 83.71           C
ANISOU 3048  CB  LYS A 151    10922   9979  10906   -488    315   -262       C
ATOM   3049  CG  LYS A 151     -16.249  44.970 -19.752  1.00 98.78           C
ANISOU 3049  CG  LYS A 151    12844  11890  12796   -454    291   -225       C
ATOM   3050  CD  LYS A 151     -17.615  45.456 -20.233  1.00104.41           C
ANISOU 3050  CD  LYS A 151    13650  12560  13460   -378    256   -173       C
ATOM   3051  CE  LYS A 151     -18.376  44.361 -20.972  1.00102.46           C
ANISOU 3051  CE  LYS A 151    13376  12345  13208   -325    208   -141       C
ATOM   3052  NZ  LYS A 151     -19.558  44.909 -21.714  1.00103.15           N
ANISOU 3052  NZ  LYS A 151    13564  12389  13238   -254    181   -104       N
ATOM   3053  N   LEU A 152     -16.445  43.724 -16.216  1.00 55.25           N
ANISOU 3053  N   LEU A 152     7074   6534   7386   -390    179   -255       N
ATOM   3054  CA  LEU A 152     -17.019  42.470 -15.748  1.00 51.46           C
ANISOU 3054  CA  LEU A 152     6520   6109   6924   -342    121   -235       C
ATOM   3055  C   LEU A 152     -17.895  41.854 -16.822  1.00 61.45           C
ANISOU 3055  C   LEU A 152     7815   7367   8167   -307    100   -194       C
ATOM   3056  O   LEU A 152     -18.676  42.536 -17.487  1.00 65.61           O
ANISOU 3056  O   LEU A 152     8419   7852   8657   -282    101   -167       O
ATOM   3057  CB  LEU A 152     -17.850  42.674 -14.482  1.00 56.58           C
ANISOU 3057  CB  LEU A 152     7143   6777   7578   -297     80   -222       C
ATOM   3058  CG  LEU A 152     -18.595  41.437 -13.952  1.00 48.81           C
ANISOU 3058  CG  LEU A 152     6099   5841   6604   -253     27   -202       C
ATOM   3059  CD1 LEU A 152     -17.645  40.405 -13.359  1.00 44.64           C
ANISOU 3059  CD1 LEU A 152     5499   5358   6106   -267     19   -231       C
ATOM   3060  CD2 LEU A 152     -19.610  41.867 -12.928  1.00 45.31           C
ANISOU 3060  CD2 LEU A 152     5654   5407   6156   -213     -3   -188       C
ATOM   3061  N   ASN A 153     -17.772  40.551 -16.977  1.00 56.09           N
ANISOU 3061  N   ASN A 153     7079   6730   7505   -300     78   -192       N
ATOM   3062  CA  ASN A 153     -18.461  39.842 -18.030  1.00 48.62           C
ANISOU 3062  CA  ASN A 153     6150   5782   6540   -276     62   -161       C
ATOM   3063  C   ASN A 153     -19.132  38.603 -17.473  1.00 50.60           C
ANISOU 3063  C   ASN A 153     6340   6082   6804   -240     16   -147       C
ATOM   3064  O   ASN A 153     -18.718  38.069 -16.439  1.00 55.79           O
ANISOU 3064  O   ASN A 153     6942   6771   7485   -243      2   -164       O
ATOM   3065  CB  ASN A 153     -17.507  39.428 -19.101  1.00 54.26           C
ANISOU 3065  CB  ASN A 153     6871   6488   7256   -317     97   -176       C
ATOM   3066  CG  ASN A 153     -18.099  39.543 -20.422  1.00 69.53           C
ANISOU 3066  CG  ASN A 153     8873   8389   9156   -304    103   -147       C
ATOM   3067  OD1 ASN A 153     -18.236  40.654 -20.946  1.00 85.18           O
ANISOU 3067  OD1 ASN A 153    10941  10319  11106   -308    130   -140       O
ATOM   3068  ND2 ASN A 153     -18.507  38.417 -20.986  1.00 72.72           N
ANISOU 3068  ND2 ASN A 153     9251   8820   9561   -283     78   -130       N
ATOM   3069  N   TYR A 154     -20.162  38.135 -18.177  1.00 36.37           N
ANISOU 3069  N   TYR A 154     4553   4284   4982   -209     -6   -120       N
ATOM   3070  CA  TYR A 154     -20.801  36.900 -17.740  1.00 41.99           C
ANISOU 3070  CA  TYR A 154     5213   5038   5701   -188    -39   -112       C
ATOM   3071  C   TYR A 154     -19.808  35.740 -17.656  1.00 46.07           C
ANISOU 3071  C   TYR A 154     5687   5576   6241   -211    -36   -126       C
ATOM   3072  O   TYR A 154     -19.985  34.850 -16.817  1.00 44.81           O
ANISOU 3072  O   TYR A 154     5492   5445   6090   -201    -58   -128       O
ATOM   3073  CB  TYR A 154     -21.987  36.566 -18.649  1.00 41.48           C
ANISOU 3073  CB  TYR A 154     5168   4981   5612   -157    -58    -92       C
ATOM   3074  CG  TYR A 154     -21.676  35.853 -19.946  1.00 45.23           C
ANISOU 3074  CG  TYR A 154     5654   5450   6080   -169    -47    -85       C
ATOM   3075  CD1 TYR A 154     -21.583  34.466 -19.996  1.00 43.32           C
ANISOU 3075  CD1 TYR A 154     5371   5238   5852   -179    -56    -85       C
ATOM   3076  CD2 TYR A 154     -21.519  36.562 -21.130  1.00 38.39           C
ANISOU 3076  CD2 TYR A 154     4850   4547   5191   -170    -27    -78       C
ATOM   3077  CE1 TYR A 154     -21.307  33.817 -21.172  1.00 36.67           C
ANISOU 3077  CE1 TYR A 154     4537   4391   5003   -189    -47    -80       C
ATOM   3078  CE2 TYR A 154     -21.241  35.907 -22.331  1.00 34.97           C
ANISOU 3078  CE2 TYR A 154     4429   4109   4750   -182    -16    -72       C
ATOM   3079  CZ  TYR A 154     -21.143  34.543 -22.347  1.00 41.15           C
ANISOU 3079  CZ  TYR A 154     5159   4925   5550   -191    -27    -74       C
ATOM   3080  OH  TYR A 154     -20.888  33.873 -23.534  1.00 34.68           O
ANISOU 3080  OH  TYR A 154     4350   4103   4724   -202    -17    -69       O
ATOM   3081  N   VAL A 155     -18.737  35.743 -18.468  1.00 51.45           N
ANISOU 3081  N   VAL A 155     6377   6244   6929   -243     -7   -142       N
ATOM   3082  CA  VAL A 155     -17.781  34.637 -18.369  1.00 53.63           C
ANISOU 3082  CA  VAL A 155     6608   6545   7223   -255     -9   -163       C
ATOM   3083  C   VAL A 155     -17.086  34.636 -17.037  1.00 50.33           C
ANISOU 3083  C   VAL A 155     6151   6148   6825   -253    -19   -193       C
ATOM   3084  O   VAL A 155     -16.595  33.587 -16.609  1.00 52.91           O
ANISOU 3084  O   VAL A 155     6444   6500   7159   -241    -38   -208       O
ATOM   3085  CB  VAL A 155     -16.680  34.622 -19.443  1.00 50.24           C
ANISOU 3085  CB  VAL A 155     6184   6105   6798   -292     25   -186       C
ATOM   3086  CG1 VAL A 155     -17.195  34.007 -20.709  1.00 50.10           C
ANISOU 3086  CG1 VAL A 155     6191   6079   6764   -287     25   -160       C
ATOM   3087  CG2 VAL A 155     -16.100  36.003 -19.637  1.00 50.30           C
ANISOU 3087  CG2 VAL A 155     6225   6082   6803   -328     67   -207       C
ATOM   3088  N   ASP A 156     -17.012  35.790 -16.371  1.00 46.43           N
ANISOU 3088  N   ASP A 156     5665   5643   6334   -261     -9   -205       N
ATOM   3089  CA  ASP A 156     -16.422  35.801 -15.037  1.00 41.57           C
ANISOU 3089  CA  ASP A 156     5010   5051   5735   -253    -23   -236       C
ATOM   3090  C   ASP A 156     -17.294  35.044 -14.059  1.00 44.21           C
ANISOU 3090  C   ASP A 156     5334   5402   6062   -215    -61   -212       C
ATOM   3091  O   ASP A 156     -16.780  34.464 -13.097  1.00 49.44           O
ANISOU 3091  O   ASP A 156     5969   6087   6730   -197    -82   -234       O
ATOM   3092  CB  ASP A 156     -16.198  37.226 -14.567  1.00 31.57           C
ANISOU 3092  CB  ASP A 156     3756   3767   4472   -274      1   -254       C
ATOM   3093  CG  ASP A 156     -15.254  37.978 -15.473  1.00 40.42           C
ANISOU 3093  CG  ASP A 156     4896   4867   5596   -324     50   -285       C
ATOM   3094  OD1 ASP A 156     -15.722  38.872 -16.222  1.00 45.64           O
ANISOU 3094  OD1 ASP A 156     5618   5485   6237   -339     77   -263       O
ATOM   3095  OD2 ASP A 156     -14.042  37.657 -15.447  1.00 45.08           O
ANISOU 3095  OD2 ASP A 156     5441   5483   6203   -347     63   -336       O
ATOM   3096  N   PHE A 157     -18.607  35.012 -14.310  1.00 39.15           N
ANISOU 3096  N   PHE A 157     4719   4752   5404   -201    -70   -175       N
ATOM   3097  CA  PHE A 157     -19.502  34.228 -13.462  1.00 44.73           C
ANISOU 3097  CA  PHE A 157     5419   5476   6101   -177    -97   -159       C
ATOM   3098  C   PHE A 157     -19.282  32.725 -13.663  1.00 40.82           C
ANISOU 3098  C   PHE A 157     4918   4992   5600   -172   -108   -156       C
ATOM   3099  O   PHE A 157     -19.321  31.961 -12.698  1.00 44.78           O
ANISOU 3099  O   PHE A 157     5418   5502   6093   -156   -125   -159       O
ATOM   3100  CB  PHE A 157     -20.958  34.636 -13.726  1.00 41.06           C
ANISOU 3100  CB  PHE A 157     4973   5009   5620   -167   -100   -134       C
ATOM   3101  CG  PHE A 157     -21.267  36.071 -13.332  1.00 35.31           C
ANISOU 3101  CG  PHE A 157     4258   4268   4891   -161    -96   -137       C
ATOM   3102  CD1 PHE A 157     -20.669  37.131 -13.988  1.00 38.51           C
ANISOU 3102  CD1 PHE A 157     4689   4644   5298   -175    -73   -143       C
ATOM   3103  CD2 PHE A 157     -22.137  36.350 -12.284  1.00 40.71           C
ANISOU 3103  CD2 PHE A 157     4934   4965   5569   -144   -111   -135       C
ATOM   3104  CE1 PHE A 157     -20.946  38.455 -13.616  1.00 46.47           C
ANISOU 3104  CE1 PHE A 157     5723   5633   6301   -169    -67   -145       C
ATOM   3105  CE2 PHE A 157     -22.419  37.647 -11.911  1.00 45.31           C
ANISOU 3105  CE2 PHE A 157     5531   5535   6149   -134   -109   -139       C
ATOM   3106  CZ  PHE A 157     -21.824  38.708 -12.575  1.00 47.76           C
ANISOU 3106  CZ  PHE A 157     5875   5813   6461   -145    -88   -143       C
ATOM   3107  N   LEU A 158     -19.011  32.287 -14.899  1.00 43.58           N
ANISOU 3107  N   LEU A 158     5273   5336   5949   -183    -97   -152       N
ATOM   3108  CA  LEU A 158     -18.630  30.894 -15.135  1.00 40.51           C
ANISOU 3108  CA  LEU A 158     4881   4954   5555   -177   -107   -155       C
ATOM   3109  C   LEU A 158     -17.257  30.574 -14.535  1.00 48.76           C
ANISOU 3109  C   LEU A 158     5905   6011   6610   -164   -117   -192       C
ATOM   3110  O   LEU A 158     -17.097  29.576 -13.817  1.00 44.01           O
ANISOU 3110  O   LEU A 158     5311   5415   5995   -138   -140   -196       O
ATOM   3111  CB  LEU A 158     -18.628  30.587 -16.627  1.00 31.02           C
ANISOU 3111  CB  LEU A 158     3688   3746   4352   -192    -92   -145       C
ATOM   3112  CG  LEU A 158     -19.978  30.602 -17.340  1.00 37.56           C
ANISOU 3112  CG  LEU A 158     4535   4572   5165   -194    -90   -116       C
ATOM   3113  CD1 LEU A 158     -19.730  30.558 -18.851  1.00 33.54           C
ANISOU 3113  CD1 LEU A 158     4037   4053   4655   -207    -74   -111       C
ATOM   3114  CD2 LEU A 158     -20.866  29.445 -16.892  1.00 31.01           C
ANISOU 3114  CD2 LEU A 158     3710   3753   4319   -189   -102   -105       C
ATOM   3115  N   ALA A 159     -16.245  31.388 -14.844  1.00 41.44           N
ANISOU 3115  N   ALA A 159     4955   5089   5702   -180   -101   -224       N
ATOM   3116  CA  ALA A 159     -14.938  31.196 -14.223  1.00 40.54           C
ANISOU 3116  CA  ALA A 159     4808   4999   5598   -165   -113   -275       C
ATOM   3117  C   ALA A 159     -15.050  31.140 -12.698  1.00 42.90           C
ANISOU 3117  C   ALA A 159     5106   5305   5888   -131   -141   -281       C
ATOM   3118  O   ALA A 159     -14.466  30.259 -12.058  1.00 41.80           O
ANISOU 3118  O   ALA A 159     4964   5181   5738    -93   -171   -304       O
ATOM   3119  CB  ALA A 159     -13.977  32.308 -14.658  1.00 40.36           C
ANISOU 3119  CB  ALA A 159     4757   4982   5596   -202    -80   -317       C
ATOM   3120  N   TYR A 160     -15.829  32.047 -12.098  1.00 41.89           N
ANISOU 3120  N   TYR A 160     4988   5168   5761   -140   -135   -262       N
ATOM   3121  CA  TYR A 160     -15.969  32.042 -10.646  1.00 32.35           C
ANISOU 3121  CA  TYR A 160     3782   3966   4544   -111   -159   -267       C
ATOM   3122  C   TYR A 160     -16.576  30.732 -10.148  1.00 45.83           C
ANISOU 3122  C   TYR A 160     5527   5666   6222    -82   -182   -242       C
ATOM   3123  O   TYR A 160     -16.086  30.140  -9.179  1.00 46.24           O
ANISOU 3123  O   TYR A 160     5589   5724   6257    -44   -209   -261       O
ATOM   3124  CB  TYR A 160     -16.817  33.222 -10.160  1.00 40.39           C
ANISOU 3124  CB  TYR A 160     4807   4974   5566   -127   -148   -249       C
ATOM   3125  CG  TYR A 160     -17.071  33.121  -8.664  1.00 53.55           C
ANISOU 3125  CG  TYR A 160     6480   6647   7220    -98   -171   -251       C
ATOM   3126  CD1 TYR A 160     -16.099  33.514  -7.750  1.00 43.82           C
ANISOU 3126  CD1 TYR A 160     5222   5433   5996    -80   -185   -294       C
ATOM   3127  CD2 TYR A 160     -18.253  32.572  -8.166  1.00 58.28           C
ANISOU 3127  CD2 TYR A 160     7112   7236   7796    -91   -178   -217       C
ATOM   3128  CE1 TYR A 160     -16.304  33.404  -6.398  1.00 42.41           C
ANISOU 3128  CE1 TYR A 160     5055   5258   5801    -51   -208   -297       C
ATOM   3129  CE2 TYR A 160     -18.456  32.443  -6.802  1.00 58.17           C
ANISOU 3129  CE2 TYR A 160     7113   7224   7766    -69   -195   -220       C
ATOM   3130  CZ  TYR A 160     -17.479  32.865  -5.925  1.00 54.82           C
ANISOU 3130  CZ  TYR A 160     6667   6813   7347    -46   -212   -257       C
ATOM   3131  OH  TYR A 160     -17.675  32.750  -4.563  1.00 57.07           O
ANISOU 3131  OH  TYR A 160     6973   7099   7612    -20   -230   -260       O
ATOM   3132  N   ASP A 161     -17.663  30.271 -10.777  1.00 39.18           N
ANISOU 3132  N   ASP A 161     4711   4808   5367   -100   -171   -203       N
ATOM   3133  CA  ASP A 161     -18.344  29.092 -10.251  1.00 34.92           C
ANISOU 3133  CA  ASP A 161     4216   4257   4796    -87   -181   -182       C
ATOM   3134  C   ASP A 161     -17.497  27.827 -10.408  1.00 38.97           C
ANISOU 3134  C   ASP A 161     4750   4765   5292    -57   -199   -196       C
ATOM   3135  O   ASP A 161     -17.407  27.017  -9.485  1.00 47.37           O
ANISOU 3135  O   ASP A 161     5856   5818   6326    -25   -218   -199       O
ATOM   3136  CB  ASP A 161     -19.697  28.937 -10.933  1.00 33.71           C
ANISOU 3136  CB  ASP A 161     4075   4096   4635   -118   -160   -150       C
ATOM   3137  CG  ASP A 161     -20.249  27.545 -10.821  1.00 43.32           C
ANISOU 3137  CG  ASP A 161     5340   5300   5821   -120   -158   -136       C
ATOM   3138  OD1 ASP A 161     -20.487  27.084  -9.687  1.00 52.69           O
ANISOU 3138  OD1 ASP A 161     6564   6476   6982   -109   -164   -135       O
ATOM   3139  OD2 ASP A 161     -20.451  26.906 -11.870  1.00 50.70           O
ANISOU 3139  OD2 ASP A 161     6279   6231   6753   -135   -148   -126       O
ATOM   3140  N   VAL A 162     -16.868  27.649 -11.567  1.00 36.83           N
ANISOU 3140  N   VAL A 162     4456   4501   5036    -64   -193   -207       N
ATOM   3141  CA  VAL A 162     -16.005  26.496 -11.825  1.00 40.46           C
ANISOU 3141  CA  VAL A 162     4931   4961   5482    -32   -213   -226       C
ATOM   3142  C   VAL A 162     -14.809  26.474 -10.874  1.00 44.85           C
ANISOU 3142  C   VAL A 162     5474   5535   6032     20   -246   -274       C
ATOM   3143  O   VAL A 162     -14.440  25.415 -10.349  1.00 47.12           O
ANISOU 3143  O   VAL A 162     5804   5813   6286     70   -276   -284       O
ATOM   3144  CB  VAL A 162     -15.564  26.518 -13.309  1.00 40.74           C
ANISOU 3144  CB  VAL A 162     4935   5005   5539    -56   -196   -233       C
ATOM   3145  CG1 VAL A 162     -14.374  25.607 -13.590  1.00 36.53           C
ANISOU 3145  CG1 VAL A 162     4397   4485   5000    -18   -218   -270       C
ATOM   3146  CG2 VAL A 162     -16.710  26.150 -14.177  1.00 34.65           C
ANISOU 3146  CG2 VAL A 162     4188   4216   4761    -89   -174   -190       C
ATOM   3147  N   LEU A 163     -14.156  27.627 -10.667  1.00 44.47           N
ANISOU 3147  N   LEU A 163     5370   5514   6013     13   -243   -309       N
ATOM   3148  CA  LEU A 163     -12.989  27.668  -9.789  1.00 42.72           C
ANISOU 3148  CA  LEU A 163     5123   5321   5788     63   -276   -368       C
ATOM   3149  C   LEU A 163     -13.392  27.445  -8.340  1.00 48.62           C
ANISOU 3149  C   LEU A 163     5916   6054   6503    103   -302   -357       C
ATOM   3150  O   LEU A 163     -12.691  26.760  -7.575  1.00 43.88           O
ANISOU 3150  O   LEU A 163     5337   5461   5873    168   -343   -390       O
ATOM   3151  CB  LEU A 163     -12.270  29.013  -9.911  1.00 42.54           C
ANISOU 3151  CB  LEU A 163     5029   5331   5803     32   -257   -414       C
ATOM   3152  CG  LEU A 163     -11.631  29.459 -11.224  1.00 42.79           C
ANISOU 3152  CG  LEU A 163     5014   5379   5865    -14   -224   -441       C
ATOM   3153  CD1 LEU A 163     -11.058  30.855 -11.049  1.00 40.78           C
ANISOU 3153  CD1 LEU A 163     4708   5146   5639    -51   -198   -486       C
ATOM   3154  CD2 LEU A 163     -10.574  28.486 -11.667  1.00 51.94           C
ANISOU 3154  CD2 LEU A 163     6152   6565   7018     23   -247   -490       C
ATOM   3155  N   ASP A 164     -14.509  28.041  -7.941  1.00 40.74           N
ANISOU 3155  N   ASP A 164     4936   5037   5507     68   -281   -315       N
ATOM   3156  CA  ASP A 164     -15.043  27.783  -6.616  1.00 45.68           C
ANISOU 3156  CA  ASP A 164     5614   5644   6098     95   -297   -300       C
ATOM   3157  C   ASP A 164     -15.225  26.286  -6.387  1.00 49.02           C
ANISOU 3157  C   ASP A 164     6119   6035   6470    132   -314   -282       C
ATOM   3158  O   ASP A 164     -14.773  25.737  -5.373  1.00 56.87           O
ANISOU 3158  O   ASP A 164     7160   7021   7426    191   -349   -301       O
ATOM   3159  CB  ASP A 164     -16.354  28.547  -6.445  1.00 41.50           C
ANISOU 3159  CB  ASP A 164     5089   5101   5578     44   -266   -258       C
ATOM   3160  CG  ASP A 164     -16.853  28.506  -5.049  1.00 48.93           C
ANISOU 3160  CG  ASP A 164     6073   6029   6489     64   -277   -250       C
ATOM   3161  OD1 ASP A 164     -16.049  28.753  -4.113  1.00 49.12           O
ANISOU 3161  OD1 ASP A 164     6089   6068   6507    108   -306   -285       O
ATOM   3162  OD2 ASP A 164     -18.050  28.209  -4.894  1.00 50.26           O
ANISOU 3162  OD2 ASP A 164     6283   6176   6639     34   -255   -213       O
ATOM   3163  N   VAL A 165     -15.845  25.600  -7.347  1.00 40.41           N
ANISOU 3163  N   VAL A 165     5055   4924   5376     99   -291   -249       N
ATOM   3164  CA  VAL A 165     -16.119  24.178  -7.186  1.00 43.56           C
ANISOU 3164  CA  VAL A 165     5543   5284   5723    122   -298   -230       C
ATOM   3165  C   VAL A 165     -14.830  23.394  -6.963  1.00 46.82           C
ANISOU 3165  C   VAL A 165     5978   5700   6109    202   -344   -271       C
ATOM   3166  O   VAL A 165     -14.765  22.516  -6.095  1.00 51.96           O
ANISOU 3166  O   VAL A 165     6718   6320   6705    253   -368   -271       O
ATOM   3167  CB  VAL A 165     -16.904  23.658  -8.397  1.00 49.68           C
ANISOU 3167  CB  VAL A 165     6327   6045   6505     69   -264   -197       C
ATOM   3168  CG1 VAL A 165     -16.745  22.157  -8.499  1.00 46.86           C
ANISOU 3168  CG1 VAL A 165     6053   5651   6099    100   -274   -192       C
ATOM   3169  CG2 VAL A 165     -18.379  24.069  -8.271  1.00 47.13           C
ANISOU 3169  CG2 VAL A 165     6011   5713   6185      7   -225   -163       C
ATOM   3170  N   TYR A 166     -13.786  23.692  -7.737  1.00 52.01           N
ANISOU 3170  N   TYR A 166     6563   6398   6802    216   -358   -313       N
ATOM   3171  CA  TYR A 166     -12.496  23.032  -7.537  1.00 42.85           C
ANISOU 3171  CA  TYR A 166     5406   5256   5619    299   -407   -367       C
ATOM   3172  C   TYR A 166     -11.924  23.366  -6.163  1.00 45.71           C
ANISOU 3172  C   TYR A 166     5773   5634   5959    363   -448   -407       C
ATOM   3173  O   TYR A 166     -11.448  22.485  -5.440  1.00 54.94           O
ANISOU 3173  O   TYR A 166     7012   6787   7074    446   -492   -427       O
ATOM   3174  CB  TYR A 166     -11.522  23.460  -8.635  1.00 34.30           C
ANISOU 3174  CB  TYR A 166     4227   4223   4583    287   -405   -415       C
ATOM   3175  CG  TYR A 166     -11.573  22.616  -9.886  1.00 46.10           C
ANISOU 3175  CG  TYR A 166     5736   5704   6077    271   -392   -398       C
ATOM   3176  CD1 TYR A 166     -12.525  22.853 -10.862  1.00 39.86           C
ANISOU 3176  CD1 TYR A 166     4938   4896   5312    192   -344   -347       C
ATOM   3177  CD2 TYR A 166     -10.650  21.588 -10.097  1.00 50.88           C
ANISOU 3177  CD2 TYR A 166     6360   6316   6655    340   -430   -438       C
ATOM   3178  CE1 TYR A 166     -12.567  22.100 -11.983  1.00 47.18           C
ANISOU 3178  CE1 TYR A 166     5877   5812   6238    178   -332   -334       C
ATOM   3179  CE2 TYR A 166     -10.682  20.823 -11.237  1.00 41.65           C
ANISOU 3179  CE2 TYR A 166     5203   5135   5486    325   -418   -424       C
ATOM   3180  CZ  TYR A 166     -11.639  21.092 -12.184  1.00 49.12           C
ANISOU 3180  CZ  TYR A 166     6141   6064   6460    240   -367   -371       C
ATOM   3181  OH  TYR A 166     -11.697  20.340 -13.333  1.00 51.59           O
ANISOU 3181  OH  TYR A 166     6465   6366   6773    224   -354   -357       O
ATOM   3182  N   ARG A 167     -11.980  24.638  -5.785  1.00 38.98           N
ANISOU 3182  N   ARG A 167     4855   4811   5145    329   -434   -418       N
ATOM   3183  CA  ARG A 167     -11.452  25.073  -4.501  1.00 40.06           C
ANISOU 3183  CA  ARG A 167     4986   4969   5267    383   -470   -459       C
ATOM   3184  C   ARG A 167     -12.195  24.434  -3.331  1.00 51.61           C
ANISOU 3184  C   ARG A 167     6561   6379   6669    416   -482   -419       C
ATOM   3185  O   ARG A 167     -11.607  24.236  -2.260  1.00 50.69           O
ANISOU 3185  O   ARG A 167     6478   6269   6514    494   -528   -455       O
ATOM   3186  CB  ARG A 167     -11.478  26.611  -4.460  1.00 42.03           C
ANISOU 3186  CB  ARG A 167     5144   5254   5572    325   -442   -473       C
ATOM   3187  CG  ARG A 167     -11.856  27.302  -3.191  1.00 50.29           C
ANISOU 3187  CG  ARG A 167     6202   6296   6609    331   -447   -468       C
ATOM   3188  CD  ARG A 167     -12.991  28.340  -3.452  1.00 46.80           C
ANISOU 3188  CD  ARG A 167     5739   5840   6204    243   -394   -418       C
ATOM   3189  NE  ARG A 167     -12.501  29.722  -3.345  1.00 41.39           N
ANISOU 3189  NE  ARG A 167     4970   5193   5562    216   -383   -458       N
ATOM   3190  CZ  ARG A 167     -13.264  30.799  -3.128  1.00 43.78           C
ANISOU 3190  CZ  ARG A 167     5257   5488   5888    165   -352   -431       C
ATOM   3191  NH1 ARG A 167     -14.588  30.697  -2.955  1.00 31.45           N
ANISOU 3191  NH1 ARG A 167     3748   3890   4312    136   -332   -369       N
ATOM   3192  NH2 ARG A 167     -12.689  31.997  -3.058  1.00 48.27           N
ANISOU 3192  NH2 ARG A 167     5758   6088   6492    142   -341   -473       N
ATOM   3193  N   ILE A 168     -13.471  24.078  -3.505  1.00 52.22           N
ANISOU 3193  N   ILE A 168     6703   6407   6732    358   -440   -352       N
ATOM   3194  CA  ILE A 168     -14.148  23.324  -2.450  1.00 44.41           C
ANISOU 3194  CA  ILE A 168     5834   5363   5676    381   -442   -320       C
ATOM   3195  C   ILE A 168     -13.588  21.907  -2.372  1.00 41.98           C
ANISOU 3195  C   ILE A 168     5626   5019   5303    459   -479   -330       C
ATOM   3196  O   ILE A 168     -13.211  21.433  -1.298  1.00 51.30           O
ANISOU 3196  O   ILE A 168     6889   6179   6425    538   -518   -348       O
ATOM   3197  CB  ILE A 168     -15.668  23.329  -2.667  1.00 43.64           C
ANISOU 3197  CB  ILE A 168     5770   5231   5581    290   -382   -259       C
ATOM   3198  CG1 ILE A 168     -16.231  24.724  -2.474  1.00 43.19           C
ANISOU 3198  CG1 ILE A 168     5633   5204   5574    233   -357   -252       C
ATOM   3199  CG2 ILE A 168     -16.398  22.399  -1.705  1.00 33.74           C
ANISOU 3199  CG2 ILE A 168     4652   3914   4253    297   -371   -229       C
ATOM   3200  CD1 ILE A 168     -17.501  24.907  -3.322  1.00 44.92           C
ANISOU 3200  CD1 ILE A 168     5833   5415   5818    144   -303   -211       C
ATOM   3201  N   PHE A 169     -13.483  21.228  -3.516  1.00 51.24           N
ANISOU 3201  N   PHE A 169     6798   6186   6484    446   -469   -323       N
ATOM   3202  CA  PHE A 169     -12.901  19.890  -3.539  1.00 50.07           C
ANISOU 3202  CA  PHE A 169     6746   6005   6275    525   -506   -337       C
ATOM   3203  C   PHE A 169     -11.488  19.888  -2.969  1.00 60.04           C
ANISOU 3203  C   PHE A 169     7986   7308   7519    641   -579   -410       C
ATOM   3204  O   PHE A 169     -11.124  19.003  -2.180  1.00 59.92           O
ANISOU 3204  O   PHE A 169     8083   7256   7429    734   -623   -423       O
ATOM   3205  CB  PHE A 169     -12.880  19.367  -4.960  1.00 46.63           C
ANISOU 3205  CB  PHE A 169     6282   5570   5863    491   -486   -327       C
ATOM   3206  CG  PHE A 169     -12.698  17.882  -5.064  1.00 48.68           C
ANISOU 3206  CG  PHE A 169     6667   5776   6056    548   -505   -321       C
ATOM   3207  CD1 PHE A 169     -13.681  17.019  -4.616  1.00 51.29           C
ANISOU 3207  CD1 PHE A 169     7137   6028   6323    522   -472   -271       C
ATOM   3208  CD2 PHE A 169     -11.569  17.351  -5.657  1.00 48.15           C
ANISOU 3208  CD2 PHE A 169     6576   5734   5984    622   -551   -369       C
ATOM   3209  CE1 PHE A 169     -13.532  15.652  -4.737  1.00 54.59           C
ANISOU 3209  CE1 PHE A 169     7682   6386   6673    571   -485   -264       C
ATOM   3210  CE2 PHE A 169     -11.417  15.991  -5.786  1.00 54.05           C
ANISOU 3210  CE2 PHE A 169     7442   6427   6666    678   -569   -363       C
ATOM   3211  CZ  PHE A 169     -12.404  15.139  -5.326  1.00 56.32           C
ANISOU 3211  CZ  PHE A 169     7881   6628   6888    652   -536   -308       C
ATOM   3212  N   GLU A 170     -10.675  20.875  -3.354  1.00 57.25           N
ANISOU 3212  N   GLU A 170     7492   7030   7229    637   -592   -464       N
ATOM   3213  CA  GLU A 170      -9.287  20.970  -2.909  1.00 49.98           C
ANISOU 3213  CA  GLU A 170     6523   6168   6301    740   -659   -552       C
ATOM   3214  C   GLU A 170      -9.034  22.406  -2.449  1.00 45.56           C
ANISOU 3214  C   GLU A 170     5849   5666   5794    709   -653   -588       C
ATOM   3215  O   GLU A 170      -8.802  23.312  -3.260  1.00 44.61           O
ANISOU 3215  O   GLU A 170     5612   5595   5743    641   -622   -610       O
ATOM   3216  CB  GLU A 170      -8.332  20.511  -4.014  1.00 54.87           C
ANISOU 3216  CB  GLU A 170     7082   6827   6938    770   -680   -604       C
ATOM   3217  CG  GLU A 170      -6.926  21.074  -3.934  1.00 67.54           C
ANISOU 3217  CG  GLU A 170     8568   8523   8570    830   -727   -711       C
ATOM   3218  CD  GLU A 170      -6.124  20.444  -2.822  1.00 80.51           C
ANISOU 3218  CD  GLU A 170    10273  10175  10142    973   -808   -771       C
ATOM   3219  OE1 GLU A 170      -4.963  20.048  -3.072  1.00 88.32           O
ANISOU 3219  OE1 GLU A 170    11216  11220  11122   1059   -862   -859       O
ATOM   3220  OE2 GLU A 170      -6.648  20.352  -1.693  1.00 84.91           O
ANISOU 3220  OE2 GLU A 170    10926  10685  10650   1004   -820   -737       O
ATOM   3221  N   PRO A 171      -9.095  22.661  -1.141  1.00 42.12           N
ANISOU 3221  N   PRO A 171     5455   5224   5325    753   -679   -596       N
ATOM   3222  CA  PRO A 171      -9.006  24.057  -0.685  1.00 46.80           C
ANISOU 3222  CA  PRO A 171     5949   5865   5968    713   -665   -622       C
ATOM   3223  C   PRO A 171      -7.668  24.714  -0.965  1.00 46.93           C
ANISOU 3223  C   PRO A 171     5832   5972   6029    740   -693   -723       C
ATOM   3224  O   PRO A 171      -7.592  25.948  -0.928  1.00 46.40           O
ANISOU 3224  O   PRO A 171     5671   5945   6016    681   -666   -746       O
ATOM   3225  CB  PRO A 171      -9.294  23.944   0.819  1.00 43.48           C
ANISOU 3225  CB  PRO A 171     5619   5413   5489    771   -695   -611       C
ATOM   3226  CG  PRO A 171     -10.160  22.705   0.913  1.00 40.20           C
ANISOU 3226  CG  PRO A 171     5359   4910   5006    778   -683   -540       C
ATOM   3227  CD  PRO A 171      -9.532  21.766  -0.063  1.00 42.22           C
ANISOU 3227  CD  PRO A 171     5621   5168   5251    818   -703   -562       C
ATOM   3228  N   LYS A 172      -6.620  23.949  -1.250  1.00 44.12           N
ANISOU 3228  N   LYS A 172     5466   5649   5649    826   -744   -791       N
ATOM   3229  CA  LYS A 172      -5.312  24.532  -1.502  1.00 63.25           C
ANISOU 3229  CA  LYS A 172     7754   8167   8110    850   -768   -903       C
ATOM   3230  C   LYS A 172      -5.023  24.766  -2.987  1.00 66.58           C
ANISOU 3230  C   LYS A 172     8085   8620   8592    770   -723   -919       C
ATOM   3231  O   LYS A 172      -3.928  25.237  -3.316  1.00 64.02           O
ANISOU 3231  O   LYS A 172     7646   8376   8301    775   -731  -1019       O
ATOM   3232  CB  LYS A 172      -4.219  23.633  -0.896  1.00 73.63           C
ANISOU 3232  CB  LYS A 172     9095   9517   9363   1001   -858   -990       C
ATOM   3233  CG  LYS A 172      -4.191  23.597   0.629  1.00 78.82           C
ANISOU 3233  CG  LYS A 172     9821  10165   9962   1094   -912  -1004       C
ATOM   3234  CD  LYS A 172      -3.014  22.769   1.165  1.00 87.19           C
ANISOU 3234  CD  LYS A 172    10901  11269  10958   1258  -1008  -1104       C
ATOM   3235  CE  LYS A 172      -3.319  21.265   1.195  1.00 89.25           C
ANISOU 3235  CE  LYS A 172    11330  11448  11134   1344  -1043  -1051       C
ATOM   3236  NZ  LYS A 172      -2.555  20.482   0.174  1.00 90.48           N
ANISOU 3236  NZ  LYS A 172    11455  11635  11288   1390  -1069  -1103       N
ATOM   3237  N   CYS A 173      -5.974  24.486  -3.890  1.00 66.00           N
ANISOU 3237  N   CYS A 173     8058   8487   8531    693   -671   -829       N
ATOM   3238  CA  CYS A 173      -5.652  24.455  -5.319  1.00 67.81           C
ANISOU 3238  CA  CYS A 173     8223   8739   8802    637   -637   -844       C
ATOM   3239  C   CYS A 173      -5.328  25.828  -5.902  1.00 62.22           C
ANISOU 3239  C   CYS A 173     7394   8082   8165    540   -584   -883       C
ATOM   3240  O   CYS A 173      -4.661  25.895  -6.940  1.00 69.29           O
ANISOU 3240  O   CYS A 173     8218   9017   9091    508   -563   -932       O
ATOM   3241  CB  CYS A 173      -6.783  23.803  -6.127  1.00 69.23           C
ANISOU 3241  CB  CYS A 173     8484   8844   8974    582   -597   -741       C
ATOM   3242  SG  CYS A 173      -8.359  24.629  -6.126  1.00 74.54           S
ANISOU 3242  SG  CYS A 173     9189   9460   9673    471   -529   -636       S
ATOM   3243  N   LEU A 174      -5.747  26.916  -5.262  1.00 46.14           N
ANISOU 3243  N   LEU A 174     5339   6043   6151    493   -558   -867       N
ATOM   3244  CA  LEU A 174      -5.462  28.256  -5.755  1.00 45.20           C
ANISOU 3244  CA  LEU A 174     5124   5961   6090    400   -504   -903       C
ATOM   3245  C   LEU A 174      -4.226  28.877  -5.114  1.00 51.90           C
ANISOU 3245  C   LEU A 174     5876   6892   6951    432   -528  -1025       C
ATOM   3246  O   LEU A 174      -3.910  30.039  -5.398  1.00 55.86           O
ANISOU 3246  O   LEU A 174     6302   7425   7498    352   -479  -1067       O
ATOM   3247  CB  LEU A 174      -6.679  29.174  -5.534  1.00 33.73           C
ANISOU 3247  CB  LEU A 174     3706   4456   4655    323   -456   -818       C
ATOM   3248  CG  LEU A 174      -7.930  28.795  -6.338  1.00 42.84           C
ANISOU 3248  CG  LEU A 174     4930   5540   5806    273   -420   -711       C
ATOM   3249  CD1 LEU A 174      -9.016  29.846  -6.224  1.00 36.82           C
ANISOU 3249  CD1 LEU A 174     4183   4742   5066    199   -374   -647       C
ATOM   3250  CD2 LEU A 174      -7.591  28.544  -7.824  1.00 46.51           C
ANISOU 3250  CD2 LEU A 174     5364   6013   6294    230   -389   -720       C
ATOM   3251  N   ASP A 175      -3.511  28.137  -4.273  1.00 56.44           N
ANISOU 3251  N   ASP A 175     6456   7503   7484    549   -603  -1089       N
ATOM   3252  CA  ASP A 175      -2.508  28.779  -3.423  1.00 60.93           C
ANISOU 3252  CA  ASP A 175     6940   8152   8060    587   -632  -1203       C
ATOM   3253  C   ASP A 175      -1.319  29.295  -4.220  1.00 58.02           C
ANISOU 3253  C   ASP A 175     6440   7869   7734    542   -605  -1323       C
ATOM   3254  O   ASP A 175      -0.759  30.345  -3.879  1.00 59.86           O
ANISOU 3254  O   ASP A 175     6588   8158   7999    500   -582  -1402       O
ATOM   3255  CB  ASP A 175      -2.036  27.811  -2.344  1.00 58.96           C
ANISOU 3255  CB  ASP A 175     6736   7921   7746    737   -726  -1247       C
ATOM   3256  CG  ASP A 175      -2.986  27.741  -1.200  1.00 67.71           C
ANISOU 3256  CG  ASP A 175     7948   8963   8814    770   -745  -1164       C
ATOM   3257  OD1 ASP A 175      -3.811  28.668  -1.083  1.00 68.44           O
ANISOU 3257  OD1 ASP A 175     8045   9021   8938    679   -691  -1101       O
ATOM   3258  OD2 ASP A 175      -2.907  26.775  -0.419  1.00 78.92           O
ANISOU 3258  OD2 ASP A 175     9453  10366  10169    887   -813  -1164       O
ATOM   3259  N   GLU A 176      -0.926  28.589  -5.275  1.00 54.36           N
ANISOU 3259  N   GLU A 176     5963   7419   7274    543   -602  -1342       N
ATOM   3260  CA  GLU A 176       0.198  29.030  -6.093  1.00 61.76           C
ANISOU 3260  CA  GLU A 176     6778   8439   8251    492   -568  -1461       C
ATOM   3261  C   GLU A 176      -0.165  30.152  -7.057  1.00 65.96           C
ANISOU 3261  C   GLU A 176     7283   8945   8835    337   -467  -1426       C
ATOM   3262  O   GLU A 176       0.682  30.538  -7.868  1.00 78.16           O
ANISOU 3262  O   GLU A 176     8740  10546  10411    274   -423  -1516       O
ATOM   3263  CB  GLU A 176       0.781  27.847  -6.882  1.00 54.61           C
ANISOU 3263  CB  GLU A 176     5865   7559   7325    553   -603  -1499       C
ATOM   3264  N   PHE A 177      -1.377  30.697  -6.985  1.00 56.03           N
ANISOU 3264  N   PHE A 177     6100   7603   7584    276   -427  -1306       N
ATOM   3265  CA  PHE A 177      -1.891  31.593  -8.018  1.00 47.81           C
ANISOU 3265  CA  PHE A 177     5066   6520   6581    146   -338  -1254       C
ATOM   3266  C   PHE A 177      -2.587  32.785  -7.380  1.00 49.29           C
ANISOU 3266  C   PHE A 177     5277   6670   6782     90   -303  -1207       C
ATOM   3267  O   PHE A 177      -3.817  32.862  -7.350  1.00 49.68           O
ANISOU 3267  O   PHE A 177     5409   6642   6823     73   -291  -1091       O
ATOM   3268  CB  PHE A 177      -2.835  30.838  -8.958  1.00 42.83           C
ANISOU 3268  CB  PHE A 177     4519   5816   5938    134   -326  -1140       C
ATOM   3269  CG  PHE A 177      -2.295  29.500  -9.408  1.00 51.43           C
ANISOU 3269  CG  PHE A 177     5607   6931   7005    209   -373  -1171       C
ATOM   3270  CD1 PHE A 177      -1.285  29.429 -10.364  1.00 49.99           C
ANISOU 3270  CD1 PHE A 177     5347   6806   6843    179   -349  -1261       C
ATOM   3271  CD2 PHE A 177      -2.797  28.316  -8.883  1.00 45.98           C
ANISOU 3271  CD2 PHE A 177     4997   6205   6270    307   -438  -1113       C
ATOM   3272  CE1 PHE A 177      -0.786  28.210 -10.784  1.00 41.16           C
ANISOU 3272  CE1 PHE A 177     4225   5712   5702    252   -395  -1292       C
ATOM   3273  CE2 PHE A 177      -2.305  27.092  -9.299  1.00 42.36           C
ANISOU 3273  CE2 PHE A 177     4547   5763   5785    379   -481  -1141       C
ATOM   3274  CZ  PHE A 177      -1.293  27.038 -10.246  1.00 47.79           C
ANISOU 3274  CZ  PHE A 177     5150   6512   6495    356   -463  -1231       C
ATOM   3275  N   PRO A 178      -1.823  33.758  -6.873  1.00 54.88           N
ANISOU 3275  N   PRO A 178     5908   7433   7510     57   -283  -1304       N
ATOM   3276  CA  PRO A 178      -2.470  34.944  -6.279  1.00 53.84           C
ANISOU 3276  CA  PRO A 178     5801   7263   7392      1   -247  -1262       C
ATOM   3277  C   PRO A 178      -3.467  35.590  -7.228  1.00 54.07           C
ANISOU 3277  C   PRO A 178     5898   7211   7436    -94   -176  -1160       C
ATOM   3278  O   PRO A 178      -4.550  36.012  -6.793  1.00 56.19           O
ANISOU 3278  O   PRO A 178     6232   7419   7698   -101   -172  -1070       O
ATOM   3279  CB  PRO A 178      -1.286  35.860  -5.950  1.00 43.21           C
ANISOU 3279  CB  PRO A 178     4351   5996   6070    -41   -220  -1402       C
ATOM   3280  CG  PRO A 178      -0.124  34.947  -5.897  1.00 43.14           C
ANISOU 3280  CG  PRO A 178     4264   6077   6051     37   -274  -1516       C
ATOM   3281  CD  PRO A 178      -0.362  33.899  -6.924  1.00 46.15           C
ANISOU 3281  CD  PRO A 178     4686   6428   6420     56   -282  -1460       C
ATOM   3282  N   ASN A 179      -3.099  35.688  -8.512  1.00 51.02           N
ANISOU 3282  N   ASN A 179     5496   6824   7065   -165   -121  -1181       N
ATOM   3283  CA  ASN A 179      -3.991  35.816  -9.665  1.00 42.61           C
ANISOU 3283  CA  ASN A 179     4504   5684   6001   -226    -72  -1083       C
ATOM   3284  C   ASN A 179      -5.449  35.497  -9.366  1.00 43.76           C
ANISOU 3284  C   ASN A 179     4742   5759   6128   -187   -101   -952       C
ATOM   3285  O   ASN A 179      -6.287  36.395  -9.203  1.00 42.20           O
ANISOU 3285  O   ASN A 179     4590   5511   5932   -226    -72   -893       O
ATOM   3286  CB  ASN A 179      -3.510  34.866 -10.785  1.00 34.54           C
ANISOU 3286  CB  ASN A 179     3466   4682   4978   -222    -71  -1103       C
ATOM   3287  CG  ASN A 179      -3.322  35.591 -12.066  1.00 56.13           C
ANISOU 3287  CG  ASN A 179     6205   7393   7727   -330     14  -1113       C
ATOM   3288  OD1 ASN A 179      -3.066  36.791 -12.050  1.00 77.80           O
ANISOU 3288  OD1 ASN A 179     8941  10133  10486   -409     74  -1151       O
ATOM   3289  ND2 ASN A 179      -3.467  34.908 -13.178  1.00 54.59           N
ANISOU 3289  ND2 ASN A 179     6037   7179   7528   -338     23  -1078       N
ATOM   3290  N   LEU A 180      -5.735  34.189  -9.302  1.00 46.30           N
ANISOU 3290  N   LEU A 180     5089   6078   6427   -110   -158   -914       N
ATOM   3291  CA  LEU A 180      -7.092  33.686  -9.136  1.00 49.02           C
ANISOU 3291  CA  LEU A 180     5516   6360   6749    -80   -180   -800       C
ATOM   3292  C   LEU A 180      -7.655  33.976  -7.746  1.00 56.27           C
ANISOU 3292  C   LEU A 180     6458   7268   7655    -40   -212   -775       C
ATOM   3293  O   LEU A 180      -8.863  34.213  -7.621  1.00 55.44           O
ANISOU 3293  O   LEU A 180     6412   7111   7542    -53   -203   -690       O
ATOM   3294  CB  LEU A 180      -7.106  32.187  -9.442  1.00 46.45           C
ANISOU 3294  CB  LEU A 180     5214   6034   6399    -16   -225   -780       C
ATOM   3295  CG  LEU A 180      -6.421  31.899 -10.788  1.00 51.21           C
ANISOU 3295  CG  LEU A 180     5785   6656   7016    -52   -195   -817       C
ATOM   3296  CD1 LEU A 180      -6.241  30.409 -11.090  1.00 43.80           C
ANISOU 3296  CD1 LEU A 180     4863   5726   6054     16   -241   -813       C
ATOM   3297  CD2 LEU A 180      -7.201  32.581 -11.902  1.00 47.30           C
ANISOU 3297  CD2 LEU A 180     5330   6109   6534   -136   -132   -752       C
ATOM   3298  N   LYS A 181      -6.808  33.977  -6.698  1.00 50.79           N
ANISOU 3298  N   LYS A 181     5715   6626   6956     10   -250   -852       N
ATOM   3299  CA  LYS A 181      -7.293  34.308  -5.357  1.00 49.46           C
ANISOU 3299  CA  LYS A 181     5570   6449   6774     46   -278   -833       C
ATOM   3300  C   LYS A 181      -7.796  35.743  -5.284  1.00 49.17           C
ANISOU 3300  C   LYS A 181     5535   6386   6761    -29   -227   -811       C
ATOM   3301  O   LYS A 181      -8.846  36.010  -4.688  1.00 55.14           O
ANISOU 3301  O   LYS A 181     6342   7101   7507    -24   -231   -743       O
ATOM   3302  CB  LYS A 181      -6.196  34.091  -4.319  1.00 61.21           C
ANISOU 3302  CB  LYS A 181     7001   8003   8251    116   -330   -930       C
ATOM   3303  CG  LYS A 181      -5.843  32.640  -4.094  1.00 69.95           C
ANISOU 3303  CG  LYS A 181     8131   9127   9320    216   -396   -944       C
ATOM   3304  CD  LYS A 181      -4.451  32.508  -3.520  1.00 74.20           C
ANISOU 3304  CD  LYS A 181     8590   9749   9854    280   -441  -1071       C
ATOM   3305  CE  LYS A 181      -4.480  32.454  -2.018  1.00 75.57           C
ANISOU 3305  CE  LYS A 181     8785   9932   9995    360   -497  -1084       C
ATOM   3306  NZ  LYS A 181      -3.751  31.236  -1.590  1.00 84.08           N
ANISOU 3306  NZ  LYS A 181     9874  11046  11028    482   -575  -1139       N
ATOM   3307  N   ASP A 182      -7.040  36.687  -5.855  1.00 44.18           N
ANISOU 3307  N   ASP A 182     4852   5776   6157   -100   -175   -875       N
ATOM   3308  CA  ASP A 182      -7.539  38.050  -5.970  1.00 48.38           C
ANISOU 3308  CA  ASP A 182     5406   6270   6706   -174   -119   -850       C
ATOM   3309  C   ASP A 182      -8.849  38.090  -6.744  1.00 57.46           C
ANISOU 3309  C   ASP A 182     6636   7350   7848   -199    -97   -742       C
ATOM   3310  O   ASP A 182      -9.763  38.838  -6.374  1.00 55.74           O
ANISOU 3310  O   ASP A 182     6460   7092   7627   -213    -85   -689       O
ATOM   3311  CB  ASP A 182      -6.510  38.938  -6.662  1.00 63.28           C
ANISOU 3311  CB  ASP A 182     7243   8182   8617   -257    -56   -935       C
ATOM   3312  CG  ASP A 182      -5.343  39.273  -5.783  1.00 65.37           C
ANISOU 3312  CG  ASP A 182     7424   8520   8894   -248    -67  -1052       C
ATOM   3313  OD1 ASP A 182      -4.513  40.112  -6.204  1.00 68.30           O
ANISOU 3313  OD1 ASP A 182     7752   8915   9285   -326     -7  -1133       O
ATOM   3314  OD2 ASP A 182      -5.255  38.697  -4.683  1.00 65.05           O
ANISOU 3314  OD2 ASP A 182     7364   8513   8840   -164   -133  -1067       O
ATOM   3315  N   PHE A 183      -8.951  37.295  -7.829  1.00 53.17           N
ANISOU 3315  N   PHE A 183     6109   6793   7299   -201    -92   -714       N
ATOM   3316  CA  PHE A 183     -10.143  37.327  -8.674  1.00 45.05           C
ANISOU 3316  CA  PHE A 183     5149   5706   6262   -224    -72   -623       C
ATOM   3317  C   PHE A 183     -11.385  36.886  -7.894  1.00 45.15           C
ANISOU 3317  C   PHE A 183     5207   5693   6255   -174   -112   -549       C
ATOM   3318  O   PHE A 183     -12.431  37.548  -7.949  1.00 46.46           O
ANISOU 3318  O   PHE A 183     5416   5821   6417   -192    -95   -494       O
ATOM   3319  CB  PHE A 183      -9.952  36.463  -9.938  1.00 42.90           C
ANISOU 3319  CB  PHE A 183     4882   5432   5987   -231    -64   -613       C
ATOM   3320  CG  PHE A 183     -11.260  36.104 -10.628  1.00 40.33           C
ANISOU 3320  CG  PHE A 183     4622   5057   5647   -228    -63   -521       C
ATOM   3321  CD1 PHE A 183     -11.826  36.963 -11.563  1.00 40.73           C
ANISOU 3321  CD1 PHE A 183     4715   5064   5696   -279    -18   -485       C
ATOM   3322  CD2 PHE A 183     -11.957  34.943 -10.283  1.00 41.16           C
ANISOU 3322  CD2 PHE A 183     4749   5158   5732   -174   -108   -475       C
ATOM   3323  CE1 PHE A 183     -13.035  36.670 -12.161  1.00 38.34           C
ANISOU 3323  CE1 PHE A 183     4464   4725   5377   -269    -23   -412       C
ATOM   3324  CE2 PHE A 183     -13.185  34.640 -10.876  1.00 45.91           C
ANISOU 3324  CE2 PHE A 183     5401   5723   6320   -176   -105   -402       C
ATOM   3325  CZ  PHE A 183     -13.723  35.509 -11.815  1.00 45.12           C
ANISOU 3325  CZ  PHE A 183     5331   5590   6223   -220    -66   -373       C
ATOM   3326  N   MET A 184     -11.299  35.756  -7.184  1.00 42.75           N
ANISOU 3326  N   MET A 184     4899   5411   5934   -110   -163   -551       N
ATOM   3327  CA  MET A 184     -12.429  35.314  -6.361  1.00 51.37           C
ANISOU 3327  CA  MET A 184     6038   6479   7002    -71   -192   -490       C
ATOM   3328  C   MET A 184     -12.838  36.400  -5.375  1.00 55.59           C
ANISOU 3328  C   MET A 184     6573   7007   7541    -80   -187   -487       C
ATOM   3329  O   MET A 184     -14.025  36.718  -5.231  1.00 56.74           O
ANISOU 3329  O   MET A 184     6757   7121   7679    -88   -180   -431       O
ATOM   3330  CB  MET A 184     -12.078  34.029  -5.605  1.00 34.42           C
ANISOU 3330  CB  MET A 184     3899   4351   4828     -1   -244   -505       C
ATOM   3331  CG  MET A 184     -11.551  32.909  -6.486  1.00 34.82           C
ANISOU 3331  CG  MET A 184     3948   4410   4870     17   -255   -516       C
ATOM   3332  SD  MET A 184     -12.771  32.247  -7.661  1.00 48.70           S
ANISOU 3332  SD  MET A 184     5762   6123   6620    -12   -233   -433       S
ATOM   3333  CE  MET A 184     -13.662  31.065  -6.652  1.00 50.03           C
ANISOU 3333  CE  MET A 184     6001   6266   6744     40   -269   -386       C
ATOM   3334  N   SER A 185     -11.854  36.998  -4.702  1.00 50.41           N
ANISOU 3334  N   SER A 185     5870   6385   6898    -78   -190   -556       N
ATOM   3335  CA  SER A 185     -12.142  38.035  -3.719  1.00 49.33           C
ANISOU 3335  CA  SER A 185     5731   6245   6766    -85   -186   -560       C
ATOM   3336  C   SER A 185     -12.764  39.259  -4.386  1.00 50.06           C
ANISOU 3336  C   SER A 185     5849   6300   6873   -146   -136   -529       C
ATOM   3337  O   SER A 185     -13.765  39.802  -3.902  1.00 50.56           O
ANISOU 3337  O   SER A 185     5944   6337   6929   -144   -136   -486       O
ATOM   3338  CB  SER A 185     -10.851  38.394  -2.989  1.00 49.55           C
ANISOU 3338  CB  SER A 185     5698   6324   6806    -74   -197   -651       C
ATOM   3339  OG  SER A 185     -11.140  38.790  -1.669  1.00 79.36           O
ANISOU 3339  OG  SER A 185     9477  10104  10573    -45   -220   -652       O
ATOM   3340  N   ARG A 186     -12.200  39.677  -5.524  1.00 50.20           N
ANISOU 3340  N   ARG A 186     5857   6310   6905   -197    -94   -553       N
ATOM   3341  CA  ARG A 186     -12.765  40.768  -6.312  1.00 52.21           C
ANISOU 3341  CA  ARG A 186     6156   6519   7162   -249    -47   -522       C
ATOM   3342  C   ARG A 186     -14.185  40.447  -6.758  1.00 57.68           C
ANISOU 3342  C   ARG A 186     6904   7175   7838   -230    -58   -439       C
ATOM   3343  O   ARG A 186     -15.066  41.318  -6.734  1.00 66.52           O
ANISOU 3343  O   ARG A 186     8064   8262   8950   -237    -45   -405       O
ATOM   3344  CB  ARG A 186     -11.867  41.037  -7.520  1.00 53.73           C
ANISOU 3344  CB  ARG A 186     6341   6709   7366   -306      2   -562       C
ATOM   3345  CG  ARG A 186     -12.220  42.261  -8.366  1.00 53.77           C
ANISOU 3345  CG  ARG A 186     6407   6658   7366   -364     59   -542       C
ATOM   3346  CD  ARG A 186     -10.984  42.763  -9.087  1.00 51.58           C
ANISOU 3346  CD  ARG A 186     6111   6387   7099   -434    117   -613       C
ATOM   3347  NE  ARG A 186     -10.293  41.656  -9.734  1.00 53.03           N
ANISOU 3347  NE  ARG A 186     6252   6607   7289   -429    108   -640       N
ATOM   3348  CZ  ARG A 186      -9.059  41.259  -9.445  1.00 57.57           C
ANISOU 3348  CZ  ARG A 186     6750   7243   7881   -434    104   -725       C
ATOM   3349  NH1 ARG A 186      -8.351  41.886  -8.521  1.00 71.86           N
ANISOU 3349  NH1 ARG A 186     8512   9087   9703   -448    110   -796       N
ATOM   3350  NH2 ARG A 186      -8.528  40.234 -10.089  1.00 56.55           N
ANISOU 3350  NH2 ARG A 186     6589   7145   7754   -421     92   -746       N
ATOM   3351  N   PHE A 187     -14.431  39.197  -7.155  1.00 41.95           N
ANISOU 3351  N   PHE A 187     4913   5190   5835   -202    -82   -413       N
ATOM   3352  CA  PHE A 187     -15.781  38.821  -7.547  1.00 47.79           C
ANISOU 3352  CA  PHE A 187     5696   5905   6558   -187    -92   -346       C
ATOM   3353  C   PHE A 187     -16.724  38.791  -6.349  1.00 52.45           C
ANISOU 3353  C   PHE A 187     6294   6498   7135   -154   -120   -321       C
ATOM   3354  O   PHE A 187     -17.869  39.261  -6.438  1.00 46.35           O
ANISOU 3354  O   PHE A 187     5551   5706   6354   -153   -116   -284       O
ATOM   3355  CB  PHE A 187     -15.784  37.464  -8.249  1.00 42.10           C
ANISOU 3355  CB  PHE A 187     4976   5192   5829   -172   -106   -330       C
ATOM   3356  CG  PHE A 187     -17.135  37.076  -8.756  1.00 41.25           C
ANISOU 3356  CG  PHE A 187     4905   5066   5704   -164   -111   -273       C
ATOM   3357  CD1 PHE A 187     -18.006  36.323  -7.961  1.00 34.65           C
ANISOU 3357  CD1 PHE A 187     4078   4236   4850   -136   -137   -248       C
ATOM   3358  CD2 PHE A 187     -17.561  37.514 -10.016  1.00 33.32           C
ANISOU 3358  CD2 PHE A 187     3928   4037   4697   -187    -86   -251       C
ATOM   3359  CE1 PHE A 187     -19.263  35.962  -8.429  1.00 31.82           C
ANISOU 3359  CE1 PHE A 187     3744   3869   4477   -135   -137   -209       C
ATOM   3360  CE2 PHE A 187     -18.802  37.172 -10.497  1.00 33.85           C
ANISOU 3360  CE2 PHE A 187     4019   4094   4747   -174    -94   -210       C
ATOM   3361  CZ  PHE A 187     -19.670  36.389  -9.696  1.00 44.65           C
ANISOU 3361  CZ  PHE A 187     5384   5478   6102   -151   -119   -192       C
ATOM   3362  N   GLU A 188     -16.276  38.196  -5.232  1.00 53.75           N
ANISOU 3362  N   GLU A 188     6438   6689   7297   -123   -149   -345       N
ATOM   3363  CA  GLU A 188     -17.117  38.115  -4.036  1.00 52.94           C
ANISOU 3363  CA  GLU A 188     6349   6587   7178    -96   -172   -324       C
ATOM   3364  C   GLU A 188     -17.352  39.489  -3.428  1.00 53.26           C
ANISOU 3364  C   GLU A 188     6386   6621   7228   -109   -159   -332       C
ATOM   3365  O   GLU A 188     -18.378  39.710  -2.773  1.00 48.95           O
ANISOU 3365  O   GLU A 188     5858   6070   6672    -98   -167   -306       O
ATOM   3366  CB  GLU A 188     -16.492  37.172  -3.009  1.00 42.97           C
ANISOU 3366  CB  GLU A 188     5078   5348   5901    -55   -206   -348       C
ATOM   3367  CG  GLU A 188     -16.611  35.711  -3.423  1.00 51.62           C
ANISOU 3367  CG  GLU A 188     6199   6439   6974    -35   -221   -328       C
ATOM   3368  CD  GLU A 188     -15.541  34.827  -2.813  1.00 54.39           C
ANISOU 3368  CD  GLU A 188     6544   6811   7310     12   -255   -367       C
ATOM   3369  OE1 GLU A 188     -14.660  35.367  -2.110  1.00 52.67           O
ANISOU 3369  OE1 GLU A 188     6292   6619   7102     29   -269   -417       O
ATOM   3370  OE2 GLU A 188     -15.589  33.593  -3.029  1.00 54.67           O
ANISOU 3370  OE2 GLU A 188     6612   6838   7322     36   -270   -352       O
ATOM   3371  N   GLY A 189     -16.430  40.428  -3.662  1.00 53.19           N
ANISOU 3371  N   GLY A 189     6358   6612   7239   -137   -136   -372       N
ATOM   3372  CA  GLY A 189     -16.576  41.779  -3.163  1.00 51.02           C
ANISOU 3372  CA  GLY A 189     6088   6325   6972   -154   -119   -383       C
ATOM   3373  C   GLY A 189     -17.477  42.687  -3.973  1.00 47.50           C
ANISOU 3373  C   GLY A 189     5688   5840   6521   -173    -93   -348       C
ATOM   3374  O   GLY A 189     -17.734  43.814  -3.546  1.00 56.76           O
ANISOU 3374  O   GLY A 189     6876   6995   7694   -180    -82   -352       O
ATOM   3375  N   LEU A 190     -17.961  42.242  -5.124  1.00 48.70           N
ANISOU 3375  N   LEU A 190     5864   5976   6664   -176    -87   -315       N
ATOM   3376  CA  LEU A 190     -18.892  43.057  -5.888  1.00 54.65           C
ANISOU 3376  CA  LEU A 190     6667   6694   7404   -178    -72   -284       C
ATOM   3377  C   LEU A 190     -20.124  43.325  -5.047  1.00 50.69           C
ANISOU 3377  C   LEU A 190     6172   6197   6890   -145    -96   -262       C
ATOM   3378  O   LEU A 190     -20.672  42.406  -4.443  1.00 57.61           O
ANISOU 3378  O   LEU A 190     7027   7100   7761   -124   -121   -250       O
ATOM   3379  CB  LEU A 190     -19.286  42.356  -7.193  1.00 58.71           C
ANISOU 3379  CB  LEU A 190     7202   7199   7907   -177    -69   -255       C
ATOM   3380  CG  LEU A 190     -18.221  42.215  -8.273  1.00 56.17           C
ANISOU 3380  CG  LEU A 190     6884   6865   7593   -213    -40   -274       C
ATOM   3381  CD1 LEU A 190     -18.597  41.107  -9.270  1.00 59.57           C
ANISOU 3381  CD1 LEU A 190     7318   7301   8015   -203    -49   -246       C
ATOM   3382  CD2 LEU A 190     -18.036  43.532  -8.983  1.00 52.44           C
ANISOU 3382  CD2 LEU A 190     6466   6347   7112   -243      1   -280       C
ATOM   3383  N   LYS A 191     -20.549  44.590  -5.013  1.00 60.31           N
ANISOU 3383  N   LYS A 191     7426   7388   8101   -143    -84   -260       N
ATOM   3384  CA  LYS A 191     -21.643  45.040  -4.157  1.00 60.57           C
ANISOU 3384  CA  LYS A 191     7461   7429   8124   -112   -105   -250       C
ATOM   3385  C   LYS A 191     -22.835  44.084  -4.166  1.00 65.46           C
ANISOU 3385  C   LYS A 191     8066   8078   8730    -84   -132   -227       C
ATOM   3386  O   LYS A 191     -23.156  43.468  -3.144  1.00 72.30           O
ANISOU 3386  O   LYS A 191     8901   8973   9595    -75   -149   -230       O
ATOM   3387  CB  LYS A 191     -22.063  46.454  -4.581  1.00 61.34           C
ANISOU 3387  CB  LYS A 191     7617   7485   8206   -104    -91   -246       C
ATOM   3388  CG  LYS A 191     -23.361  46.936  -3.970  1.00 72.40           C
ANISOU 3388  CG  LYS A 191     9023   8896   9590    -61   -117   -238       C
ATOM   3389  N   LYS A 192     -23.485  43.913  -5.320  1.00 70.64           N
ANISOU 3389  N   LYS A 192     8744   8725   9370    -73   -133   -208       N
ATOM   3390  CA  LYS A 192     -24.680  43.075  -5.356  1.00 64.98           C
ANISOU 3390  CA  LYS A 192     8009   8042   8640    -52   -153   -198       C
ATOM   3391  C   LYS A 192     -24.365  41.604  -5.090  1.00 72.97           C
ANISOU 3391  C   LYS A 192     8989   9077   9657    -70   -156   -195       C
ATOM   3392  O   LYS A 192     -25.186  40.901  -4.492  1.00 73.86           O
ANISOU 3392  O   LYS A 192     9084   9220   9760    -66   -166   -195       O
ATOM   3393  CB  LYS A 192     -25.394  43.245  -6.689  1.00 60.31           C
ANISOU 3393  CB  LYS A 192     7447   7440   8029    -31   -156   -187       C
ATOM   3394  CG  LYS A 192     -26.322  44.450  -6.740  1.00 66.92           C
ANISOU 3394  CG  LYS A 192     8315   8268   8845     11   -169   -193       C
ATOM   3395  CD  LYS A 192     -26.241  45.140  -8.083  1.00 78.56           C
ANISOU 3395  CD  LYS A 192     9853   9698  10298     28   -162   -182       C
ATOM   3396  CE  LYS A 192     -24.783  45.453  -8.467  1.00 79.73           C
ANISOU 3396  CE  LYS A 192    10035   9800  10460    -17   -126   -178       C
ATOM   3397  NZ  LYS A 192     -24.705  46.217  -9.754  1.00 78.36           N
ANISOU 3397  NZ  LYS A 192     9942   9573  10257     -6   -110   -168       N
ATOM   3398  N   ILE A 193     -23.186  41.126  -5.500  1.00 76.57           N
ANISOU 3398  N   ILE A 193     9444   9522  10126    -91   -145   -196       N
ATOM   3399  CA  ILE A 193     -22.834  39.721  -5.280  1.00 74.56           C
ANISOU 3399  CA  ILE A 193     9173   9286   9872    -98   -151   -195       C
ATOM   3400  C   ILE A 193     -22.723  39.420  -3.787  1.00 79.81           C
ANISOU 3400  C   ILE A 193     9824   9966  10534    -91   -164   -206       C
ATOM   3401  O   ILE A 193     -23.167  38.362  -3.315  1.00 79.39           O
ANISOU 3401  O   ILE A 193     9773   9927  10465    -90   -170   -200       O
ATOM   3402  CB  ILE A 193     -21.525  39.363  -6.016  1.00 67.21           C
ANISOU 3402  CB  ILE A 193     8239   8342   8954   -115   -141   -203       C
ATOM   3403  CG1 ILE A 193     -21.690  39.465  -7.533  1.00 68.26           C
ANISOU 3403  CG1 ILE A 193     8393   8459   9084   -123   -127   -188       C
ATOM   3404  CG2 ILE A 193     -21.050  37.959  -5.616  1.00 54.56           C
ANISOU 3404  CG2 ILE A 193     6627   6757   7348   -110   -154   -206       C
ATOM   3405  CD1 ILE A 193     -22.663  38.453  -8.109  1.00 69.36           C
ANISOU 3405  CD1 ILE A 193     8533   8612   9207   -116   -136   -168       C
ATOM   3406  N   SER A 194     -22.110  40.330  -3.022  1.00 76.01           N
ANISOU 3406  N   SER A 194     9335   9480  10065    -89   -164   -225       N
ATOM   3407  CA  SER A 194     -21.890  40.057  -1.605  1.00 71.69           C
ANISOU 3407  CA  SER A 194     8779   8947   9512    -78   -178   -238       C
ATOM   3408  C   SER A 194     -23.194  40.118  -0.822  1.00 61.66           C
ANISOU 3408  C   SER A 194     7513   7689   8224    -71   -183   -229       C
ATOM   3409  O   SER A 194     -23.443  39.274   0.047  1.00 60.07           O
ANISOU 3409  O   SER A 194     7320   7498   8004    -67   -189   -228       O
ATOM   3410  CB  SER A 194     -20.882  41.034  -1.024  1.00 78.50           C
ANISOU 3410  CB  SER A 194     9627   9807  10393    -79   -177   -268       C
ATOM   3411  OG  SER A 194     -20.675  40.735   0.343  1.00 87.40           O
ANISOU 3411  OG  SER A 194    10747  10951  11512    -60   -195   -283       O
ATOM   3412  N   ALA A 195     -24.031  41.114  -1.115  1.00 54.44           N
ANISOU 3412  N   ALA A 195     6599   6773   7312    -67   -178   -227       N
ATOM   3413  CA  ALA A 195     -25.384  41.148  -0.576  1.00 56.02           C
ANISOU 3413  CA  ALA A 195     6795   6994   7496    -61   -182   -227       C
ATOM   3414  C   ALA A 195     -26.068  39.789  -0.697  1.00 62.32           C
ANISOU 3414  C   ALA A 195     7595   7810   8274    -75   -177   -220       C
ATOM   3415  O   ALA A 195     -26.591  39.250   0.283  1.00 68.40           O
ANISOU 3415  O   ALA A 195     8367   8594   9026    -83   -173   -227       O
ATOM   3416  CB  ALA A 195     -26.187  42.232  -1.302  1.00 56.29           C
ANISOU 3416  CB  ALA A 195     6831   7026   7529    -44   -183   -228       C
ATOM   3417  N   TYR A 196     -26.044  39.211  -1.900  1.00 65.55           N
ANISOU 3417  N   TYR A 196     8008   8215   8684    -81   -172   -209       N
ATOM   3418  CA  TYR A 196     -26.673  37.918  -2.152  1.00 57.49           C
ANISOU 3418  CA  TYR A 196     6992   7208   7644   -100   -163   -205       C
ATOM   3419  C   TYR A 196     -25.915  36.774  -1.492  1.00 57.85           C
ANISOU 3419  C   TYR A 196     7063   7240   7677   -110   -161   -199       C
ATOM   3420  O   TYR A 196     -26.533  35.839  -0.962  1.00 51.66           O
ANISOU 3420  O   TYR A 196     6299   6463   6868   -129   -148   -201       O
ATOM   3421  CB  TYR A 196     -26.763  37.689  -3.658  1.00 55.16           C
ANISOU 3421  CB  TYR A 196     6695   6911   7353   -102   -161   -196       C
ATOM   3422  CG  TYR A 196     -27.242  36.319  -4.078  1.00 54.39           C
ANISOU 3422  CG  TYR A 196     6604   6824   7239   -125   -149   -193       C
ATOM   3423  CD1 TYR A 196     -28.526  35.883  -3.773  1.00 49.60           C
ANISOU 3423  CD1 TYR A 196     5985   6249   6612   -144   -136   -213       C
ATOM   3424  CD2 TYR A 196     -26.419  35.471  -4.806  1.00 52.94           C
ANISOU 3424  CD2 TYR A 196     6436   6622   7058   -132   -146   -178       C
ATOM   3425  CE1 TYR A 196     -28.973  34.635  -4.178  1.00 50.76           C
ANISOU 3425  CE1 TYR A 196     6142   6405   6742   -175   -118   -216       C
ATOM   3426  CE2 TYR A 196     -26.863  34.229  -5.220  1.00 54.37           C
ANISOU 3426  CE2 TYR A 196     6628   6808   7221   -155   -133   -176       C
ATOM   3427  CZ  TYR A 196     -28.135  33.817  -4.898  1.00 54.19           C
ANISOU 3427  CZ  TYR A 196     6598   6813   7177   -179   -117   -195       C
ATOM   3428  OH  TYR A 196     -28.563  32.581  -5.296  1.00 59.33           O
ANISOU 3428  OH  TYR A 196     7265   7468   7809   -210    -97   -198       O
ATOM   3429  N   MET A 197     -24.576  36.806  -1.545  1.00 60.39           N
ANISOU 3429  N   MET A 197     7390   7542   8012    -96   -172   -197       N
ATOM   3430  CA  MET A 197     -23.783  35.681  -1.054  1.00 68.65           C
ANISOU 3430  CA  MET A 197     8465   8577   9041    -89   -179   -196       C
ATOM   3431  C   MET A 197     -23.865  35.511   0.460  1.00 66.20           C
ANISOU 3431  C   MET A 197     8179   8266   8708    -80   -184   -204       C
ATOM   3432  O   MET A 197     -23.390  34.494   0.982  1.00 69.43           O
ANISOU 3432  O   MET A 197     8630   8660   9090    -68   -191   -203       O
ATOM   3433  CB  MET A 197     -22.320  35.837  -1.481  1.00 74.42           C
ANISOU 3433  CB  MET A 197     9184   9300   9793    -72   -192   -206       C
ATOM   3434  CG  MET A 197     -22.034  35.500  -2.944  1.00 77.28           C
ANISOU 3434  CG  MET A 197     9539   9656  10168    -82   -185   -197       C
ATOM   3435  SD  MET A 197     -20.283  35.245  -3.351  1.00 74.49           S
ANISOU 3435  SD  MET A 197     9172   9301   9830    -66   -198   -221       S
ATOM   3436  CE  MET A 197     -19.613  34.535  -1.845  1.00 77.33           C
ANISOU 3436  CE  MET A 197     9554   9664  10164    -27   -226   -241       C
ATOM   3437  N   LYS A 198     -24.440  36.479   1.177  1.00 54.10           N
ANISOU 3437  N   LYS A 198     6629   6746   7181    -81   -182   -212       N
ATOM   3438  CA  LYS A 198     -24.691  36.331   2.604  1.00 53.93           C
ANISOU 3438  CA  LYS A 198     6634   6724   7133    -77   -183   -220       C
ATOM   3439  C   LYS A 198     -26.139  35.987   2.907  1.00 55.78           C
ANISOU 3439  C   LYS A 198     6880   6972   7344   -110   -157   -221       C
ATOM   3440  O   LYS A 198     -26.453  35.610   4.043  1.00 56.06           O
ANISOU 3440  O   LYS A 198     6950   7002   7348   -118   -148   -227       O
ATOM   3441  CB  LYS A 198     -24.311  37.612   3.346  1.00 49.72           C
ANISOU 3441  CB  LYS A 198     6073   6198   6620    -58   -197   -235       C
ATOM   3442  CG  LYS A 198     -22.960  38.152   2.972  1.00 46.09           C
ANISOU 3442  CG  LYS A 198     5590   5734   6188    -38   -214   -247       C
ATOM   3443  CD  LYS A 198     -22.753  39.509   3.610  1.00 53.85           C
ANISOU 3443  CD  LYS A 198     6545   6723   7191    -30   -219   -265       C
ATOM   3444  CE  LYS A 198     -21.386  40.048   3.255  1.00 64.81           C
ANISOU 3444  CE  LYS A 198     7909   8111   8606    -21   -227   -288       C
ATOM   3445  NZ  LYS A 198     -20.498  38.925   2.834  1.00 66.91           N
ANISOU 3445  NZ  LYS A 198     8183   8375   8863     -8   -238   -293       N
ATOM   3446  N   SER A 199     -27.022  36.108   1.921  1.00 53.08           N
ANISOU 3446  N   SER A 199     6508   6648   7012   -131   -143   -223       N
ATOM   3447  CA  SER A 199     -28.416  35.772   2.127  1.00 56.73           C
ANISOU 3447  CA  SER A 199     6967   7135   7452   -166   -116   -239       C
ATOM   3448  C   SER A 199     -28.563  34.294   2.487  1.00 54.76           C
ANISOU 3448  C   SER A 199     6778   6867   7163   -199    -91   -235       C
ATOM   3449  O   SER A 199     -27.674  33.472   2.272  1.00 50.06           O
ANISOU 3449  O   SER A 199     6224   6239   6556   -187    -98   -217       O
ATOM   3450  CB  SER A 199     -29.231  36.120   0.882  1.00 62.84           C
ANISOU 3450  CB  SER A 199     7696   7937   8243   -172   -114   -249       C
ATOM   3451  OG  SER A 199     -29.228  35.058  -0.048  1.00 73.36           O
ANISOU 3451  OG  SER A 199     9044   9263   9567   -191   -102   -240       O
ATOM   3452  N   SER A 200     -29.688  33.977   3.112  1.00 68.93           N
ANISOU 3452  N   SER A 200     8583   8679   8930   -240    -58   -258       N
ATOM   3453  CA  SER A 200     -30.011  32.585   3.367  1.00 69.81           C
ANISOU 3453  CA  SER A 200     8760   8769   8996   -284    -21   -259       C
ATOM   3454  C   SER A 200     -30.364  31.869   2.079  1.00 61.00           C
ANISOU 3454  C   SER A 200     7632   7661   7884   -310     -6   -261       C
ATOM   3455  O   SER A 200     -30.311  30.639   2.038  1.00 55.39           O
ANISOU 3455  O   SER A 200     6986   6921   7139   -339     20   -254       O
ATOM   3456  CB  SER A 200     -31.173  32.496   4.359  1.00 75.43           C
ANISOU 3456  CB  SER A 200     9484   9501   9677   -334     21   -292       C
ATOM   3457  OG  SER A 200     -32.153  33.489   4.078  1.00 76.07           O
ANISOU 3457  OG  SER A 200     9479   9640   9785   -339     20   -326       O
ATOM   3458  N   ARG A 201     -30.738  32.629   1.042  1.00 64.31           N
ANISOU 3458  N   ARG A 201     7978   8119   8340   -296    -22   -271       N
ATOM   3459  CA  ARG A 201     -31.054  32.051  -0.260  1.00 73.97           C
ANISOU 3459  CA  ARG A 201     9183   9355   9569   -313    -13   -275       C
ATOM   3460  C   ARG A 201     -29.837  31.378  -0.882  1.00 71.87           C
ANISOU 3460  C   ARG A 201     8958   9044   9306   -291    -30   -237       C
ATOM   3461  O   ARG A 201     -29.954  30.293  -1.457  1.00 73.77           O
ANISOU 3461  O   ARG A 201     9228   9273   9528   -320     -9   -235       O
ATOM   3462  CB  ARG A 201     -31.598  33.128  -1.207  1.00 72.39           C
ANISOU 3462  CB  ARG A 201     8906   9199   9401   -287    -36   -292       C
ATOM   3463  CG  ARG A 201     -32.181  34.348  -0.507  1.00 76.02           C
ANISOU 3463  CG  ARG A 201     9324   9691   9870   -268    -47   -317       C
ATOM   3464  CD  ARG A 201     -33.015  35.202  -1.452  1.00 81.24           C
ANISOU 3464  CD  ARG A 201     9921  10399  10548   -241    -66   -345       C
ATOM   3465  NE  ARG A 201     -32.213  35.931  -2.436  1.00 78.80           N
ANISOU 3465  NE  ARG A 201     9609  10068  10265   -191   -100   -314       N
ATOM   3466  CZ  ARG A 201     -31.680  37.128  -2.208  1.00 71.91           C
ANISOU 3466  CZ  ARG A 201     8735   9178   9410   -149   -126   -300       C
ATOM   3467  NH1 ARG A 201     -31.856  37.703  -1.025  1.00 73.08           N
ANISOU 3467  NH1 ARG A 201     8879   9332   9555   -147   -126   -312       N
ATOM   3468  NH2 ARG A 201     -30.961  37.742  -3.143  1.00 61.43           N
ANISOU 3468  NH2 ARG A 201     7416   7824   8100   -115   -147   -276       N
ATOM   3469  N   PHE A 202     -28.661  32.002  -0.769  1.00 64.45           N
ANISOU 3469  N   PHE A 202     8018   8083   8389   -242    -65   -214       N
ATOM   3470  CA  PHE A 202     -27.450  31.520  -1.423  1.00 63.65           C
ANISOU 3470  CA  PHE A 202     7938   7951   8295   -215    -85   -189       C
ATOM   3471  C   PHE A 202     -27.208  30.028  -1.230  1.00 72.11           C
ANISOU 3471  C   PHE A 202     9085   8988   9327   -232    -68   -180       C
ATOM   3472  O   PHE A 202     -26.922  29.566  -0.121  1.00 70.72           O
ANISOU 3472  O   PHE A 202     8971   8784   9117   -226    -65   -178       O
ATOM   3473  CB  PHE A 202     -26.225  32.283  -0.936  1.00 66.13           C
ANISOU 3473  CB  PHE A 202     8247   8252   8629   -169   -118   -181       C
ATOM   3474  CG  PHE A 202     -25.039  32.104  -1.815  1.00 71.72           C
ANISOU 3474  CG  PHE A 202     8951   8945   9356   -143   -139   -170       C
ATOM   3475  CD1 PHE A 202     -25.087  32.517  -3.139  1.00 73.97           C
ANISOU 3475  CD1 PHE A 202     9194   9241   9668   -146   -140   -166       C
ATOM   3476  CD2 PHE A 202     -23.889  31.495  -1.348  1.00 71.18           C
ANISOU 3476  CD2 PHE A 202     8920   8853   9273   -112   -158   -169       C
ATOM   3477  CE1 PHE A 202     -23.998  32.349  -3.975  1.00 66.61           C
ANISOU 3477  CE1 PHE A 202     8258   8298   8753   -129   -153   -160       C
ATOM   3478  CE2 PHE A 202     -22.795  31.324  -2.179  1.00 67.10           C
ANISOU 3478  CE2 PHE A 202     8391   8331   8775    -89   -176   -169       C
ATOM   3479  CZ  PHE A 202     -22.856  31.753  -3.492  1.00 65.87           C
ANISOU 3479  CZ  PHE A 202     8192   8186   8648   -103   -170   -164       C
ATOM   3480  N   LEU A 203     -27.306  29.276  -2.330  1.00 82.71           N
ANISOU 3480  N   LEU A 203    10431  10328  10669   -250    -57   -175       N
ATOM   3481  CA  LEU A 203     -27.172  27.818  -2.329  1.00 79.70           C
ANISOU 3481  CA  LEU A 203    10127   9910  10247   -269    -37   -167       C
ATOM   3482  C   LEU A 203     -25.728  27.457  -2.679  1.00 80.33           C
ANISOU 3482  C   LEU A 203    10230   9960  10332   -217    -72   -148       C
ATOM   3483  O   LEU A 203     -25.384  27.170  -3.825  1.00 85.89           O
ANISOU 3483  O   LEU A 203    10915  10666  11054   -213    -79   -141       O
ATOM   3484  CB  LEU A 203     -28.164  27.201  -3.311  1.00 70.39           C
ANISOU 3484  CB  LEU A 203     8932   8749   9063   -321     -4   -180       C
ATOM   3485  CG  LEU A 203     -28.617  25.753  -3.116  1.00 63.91           C
ANISOU 3485  CG  LEU A 203     8194   7896   8191   -371     40   -185       C
ATOM   3486  CD1 LEU A 203     -29.175  25.539  -1.720  1.00 65.67           C
ANISOU 3486  CD1 LEU A 203     8476   8103   8371   -404     73   -199       C
ATOM   3487  CD2 LEU A 203     -29.651  25.374  -4.163  1.00 56.06           C
ANISOU 3487  CD2 LEU A 203     7160   6936   7202   -424     72   -209       C
ATOM   3488  N   ARG A 204     -24.864  27.480  -1.659  1.00 79.92           N
ANISOU 3488  N   ARG A 204    10218   9886  10263   -174    -97   -146       N
ATOM   3489  CA  ARG A 204     -23.468  27.105  -1.876  1.00 75.39           C
ANISOU 3489  CA  ARG A 204     9662   9292   9689   -118   -134   -142       C
ATOM   3490  C   ARG A 204     -23.321  25.601  -2.101  1.00 67.04           C
ANISOU 3490  C   ARG A 204     8692   8194   8587   -119   -124   -132       C
ATOM   3491  O   ARG A 204     -22.349  25.155  -2.724  1.00 60.38           O
ANISOU 3491  O   ARG A 204     7852   7342   7748    -80   -150   -132       O
ATOM   3492  CB  ARG A 204     -22.618  27.568  -0.693  1.00 77.72           C
ANISOU 3492  CB  ARG A 204     9971   9582   9976    -65   -167   -152       C
ATOM   3493  CG  ARG A 204     -21.287  28.223  -1.082  1.00 76.51           C
ANISOU 3493  CG  ARG A 204     9758   9450   9861    -16   -208   -168       C
ATOM   3494  CD  ARG A 204     -20.511  28.669   0.160  1.00 77.50           C
ANISOU 3494  CD  ARG A 204     9892   9578   9976     36   -241   -189       C
ATOM   3495  NE  ARG A 204     -21.411  29.047   1.242  1.00 75.81           N
ANISOU 3495  NE  ARG A 204     9700   9359   9743     13   -222   -183       N
ATOM   3496  CZ  ARG A 204     -21.715  30.305   1.556  1.00 87.37           C
ANISOU 3496  CZ  ARG A 204    11104  10852  11241     -1   -220   -191       C
ATOM   3497  NH1 ARG A 204     -21.178  31.318   0.881  1.00 85.30           N
ANISOU 3497  NH1 ARG A 204    10762  10617  11030      3   -231   -203       N
ATOM   3498  NH2 ARG A 204     -22.553  30.557   2.553  1.00 94.57           N
ANISOU 3498  NH2 ARG A 204    12039  11761  12132    -21   -202   -188       N
ATOM   3499  N   SER A 205     -24.284  24.820  -1.625  1.00 67.63           N
ANISOU 3499  N   SER A 205     8838   8243   8616   -165    -82   -129       N
ATOM   3500  CA  SER A 205     -24.329  23.380  -1.811  1.00 65.62           C
ANISOU 3500  CA  SER A 205     8681   7941   8309   -178    -61   -121       C
ATOM   3501  C   SER A 205     -25.796  22.967  -1.809  1.00 63.99           C
ANISOU 3501  C   SER A 205     8497   7735   8081   -266      3   -129       C
ATOM   3502  O   SER A 205     -26.671  23.770  -1.455  1.00 62.25           O
ANISOU 3502  O   SER A 205     8222   7551   7878   -304     23   -144       O
ATOM   3503  CB  SER A 205     -23.544  22.664  -0.702  1.00 59.82           C
ANISOU 3503  CB  SER A 205     8061   7153   7514   -121    -83   -117       C
ATOM   3504  OG  SER A 205     -24.121  22.916   0.575  1.00 60.23           O
ANISOU 3504  OG  SER A 205     8158   7193   7533   -140    -63   -121       O
ATOM   3505  N   PRO A 206     -26.112  21.725  -2.217  1.00 56.59           N
ANISOU 3505  N   PRO A 206     7636   6762   7104   -303     38   -127       N
ATOM   3506  CA  PRO A 206     -25.316  20.616  -2.767  1.00 62.77           C
ANISOU 3506  CA  PRO A 206     8490   7499   7859   -270     24   -112       C
ATOM   3507  C   PRO A 206     -24.771  20.929  -4.152  1.00 61.42           C
ANISOU 3507  C   PRO A 206     8226   7366   7747   -246     -8   -108       C
ATOM   3508  O   PRO A 206     -25.480  21.515  -4.963  1.00 66.69           O
ANISOU 3508  O   PRO A 206     8802   8081   8458   -288      8   -117       O
ATOM   3509  CB  PRO A 206     -26.316  19.443  -2.834  1.00 56.55           C
ANISOU 3509  CB  PRO A 206     7792   6674   7018   -351     92   -119       C
ATOM   3510  CG  PRO A 206     -27.457  19.836  -1.999  1.00 52.73           C
ANISOU 3510  CG  PRO A 206     7306   6208   6522   -418    140   -140       C
ATOM   3511  CD  PRO A 206     -27.514  21.337  -2.010  1.00 50.50           C
ANISOU 3511  CD  PRO A 206     6889   5993   6305   -396    106   -147       C
ATOM   3512  N   LEU A 207     -23.528  20.523  -4.414  1.00 57.41           N
ANISOU 3512  N   LEU A 207     7743   6836   7234   -177    -52   -101       N
ATOM   3513  CA  LEU A 207     -22.911  20.800  -5.707  1.00 58.02           C
ANISOU 3513  CA  LEU A 207     7736   6946   7362   -155    -78   -100       C
ATOM   3514  C   LEU A 207     -23.560  19.981  -6.818  1.00 62.61           C
ANISOU 3514  C   LEU A 207     8326   7522   7940   -209    -42    -96       C
ATOM   3515  O   LEU A 207     -23.886  20.509  -7.891  1.00 58.09           O
ANISOU 3515  O   LEU A 207     7664   6992   7415   -235    -38    -99       O
ATOM   3516  CB  LEU A 207     -21.415  20.512  -5.639  1.00 57.81           C
ANISOU 3516  CB  LEU A 207     7733   6905   7328    -68   -133   -105       C
ATOM   3517  CG  LEU A 207     -20.517  21.727  -5.430  1.00 59.40           C
ANISOU 3517  CG  LEU A 207     7846   7148   7575    -19   -176   -121       C
ATOM   3518  CD1 LEU A 207     -21.002  22.550  -4.252  1.00 60.85           C
ANISOU 3518  CD1 LEU A 207     8025   7340   7757    -29   -170   -123       C
ATOM   3519  CD2 LEU A 207     -19.116  21.241  -5.175  1.00 69.44           C
ANISOU 3519  CD2 LEU A 207     9152   8408   8826     68   -228   -140       C
ATOM   3520  N   PHE A 208     -23.769  18.697  -6.572  1.00 57.31           N
ANISOU 3520  N   PHE A 208     7769   6796   7209   -227    -15    -92       N
ATOM   3521  CA  PHE A 208     -24.238  17.773  -7.582  1.00 57.50           C
ANISOU 3521  CA  PHE A 208     7815   6809   7224   -274     19    -92       C
ATOM   3522  C   PHE A 208     -25.582  17.175  -7.180  1.00 60.83           C
ANISOU 3522  C   PHE A 208     8298   7211   7603   -364     88   -104       C
ATOM   3523  O   PHE A 208     -26.119  17.437  -6.095  1.00 53.92           O
ANISOU 3523  O   PHE A 208     7455   6329   6704   -389    112   -111       O
ATOM   3524  CB  PHE A 208     -23.193  16.683  -7.807  1.00 68.46           C
ANISOU 3524  CB  PHE A 208     9291   8146   8575   -216     -8    -82       C
ATOM   3525  CG  PHE A 208     -21.892  17.207  -8.337  1.00 69.34           C
ANISOU 3525  CG  PHE A 208     9329   8287   8729   -137    -71    -84       C
ATOM   3526  CD1 PHE A 208     -21.857  17.950  -9.502  1.00 60.65           C
ANISOU 3526  CD1 PHE A 208     8110   7242   7694   -151    -78    -87       C
ATOM   3527  CD2 PHE A 208     -20.707  16.965  -7.671  1.00 72.50           C
ANISOU 3527  CD2 PHE A 208     9783   8663   9102    -48   -120    -90       C
ATOM   3528  CE1 PHE A 208     -20.664  18.436  -9.988  1.00 62.35           C
ANISOU 3528  CE1 PHE A 208     8262   7483   7946    -91   -125    -95       C
ATOM   3529  CE2 PHE A 208     -19.509  17.445  -8.161  1.00 70.61           C
ANISOU 3529  CE2 PHE A 208     9467   8459   8902     17   -172   -106       C
ATOM   3530  CZ  PHE A 208     -19.489  18.179  -9.322  1.00 62.77           C
ANISOU 3530  CZ  PHE A 208     8356   7518   7974    -11   -170   -108       C
ATOM   3531  N   LEU A 209     -26.135  16.373  -8.089  1.00 63.32           N
ANISOU 3531  N   LEU A 209     8626   7522   7911   -419    126   -111       N
ATOM   3532  CA  LEU A 209     -27.372  15.675  -7.797  1.00 66.61           C
ANISOU 3532  CA  LEU A 209     9102   7921   8284   -515    201   -133       C
ATOM   3533  C   LEU A 209     -27.119  14.603  -6.743  1.00 69.65           C
ANISOU 3533  C   LEU A 209     9662   8217   8586   -512    225   -123       C
ATOM   3534  O   LEU A 209     -25.976  14.253  -6.443  1.00 61.19           O
ANISOU 3534  O   LEU A 209     8663   7098   7488   -427    178    -99       O
ATOM   3535  CB  LEU A 209     -27.969  15.059  -9.063  1.00 68.70           C
ANISOU 3535  CB  LEU A 209     9337   8206   8561   -572    234   -150       C
ATOM   3536  CG  LEU A 209     -28.823  15.970  -9.945  1.00 65.73           C
ANISOU 3536  CG  LEU A 209     8811   7918   8245   -608    237   -177       C
ATOM   3537  CD1 LEU A 209     -29.819  16.736  -9.078  1.00 55.77           C
ANISOU 3537  CD1 LEU A 209     7508   6697   6987   -653    265   -207       C
ATOM   3538  CD2 LEU A 209     -27.985  16.911 -10.790  1.00 76.38           C
ANISOU 3538  CD2 LEU A 209    10058   9307   9657   -533    170   -156       C
ATOM   3539  N   LYS A 210     -28.218  14.063  -6.199  1.00 76.14           N
ANISOU 3539  N   LYS A 210    10554   9016   9360   -606    302   -147       N
ATOM   3540  CA  LYS A 210     -28.136  13.232  -5.000  1.00 66.95           C
ANISOU 3540  CA  LYS A 210     9567   7764   8109   -612    334   -139       C
ATOM   3541  C   LYS A 210     -27.284  11.989  -5.211  1.00 62.45           C
ANISOU 3541  C   LYS A 210     9140   7109   7481   -564    321   -115       C
ATOM   3542  O   LYS A 210     -26.672  11.497  -4.258  1.00 65.20           O
ANISOU 3542  O   LYS A 210     9631   7381   7761   -508    307    -97       O
ATOM   3543  CB  LYS A 210     -29.537  12.839  -4.538  1.00 68.79           C
ANISOU 3543  CB  LYS A 210     9846   7989   8300   -741    433   -178       C
ATOM   3544  CG  LYS A 210     -30.147  13.784  -3.515  1.00 57.41           C
ANISOU 3544  CG  LYS A 210     8359   6587   6869   -768    448   -197       C
ATOM   3545  CD  LYS A 210     -31.580  13.378  -3.212  1.00 59.97           C
ANISOU 3545  CD  LYS A 210     8710   6918   7157   -906    551   -250       C
ATOM   3546  CE  LYS A 210     -32.306  14.506  -2.502  1.00 72.04           C
ANISOU 3546  CE  LYS A 210    10141   8515   8716   -935    559   -280       C
ATOM   3547  NZ  LYS A 210     -33.756  14.225  -2.321  1.00 79.17           N
ANISOU 3547  NZ  LYS A 210    11037   9449   9596  -1073    659   -348       N
ATOM   3548  N   MET A 211     -27.207  11.479  -6.441  1.00 68.65           N
ANISOU 3548  N   MET A 211     9892   7904   8288   -574    322   -116       N
ATOM   3549  CA  MET A 211     -26.488  10.237  -6.726  1.00 74.41           C
ANISOU 3549  CA  MET A 211    10758   8554   8962   -533    314    -98       C
ATOM   3550  C   MET A 211     -25.012  10.445  -7.055  1.00 72.91           C
ANISOU 3550  C   MET A 211    10537   8368   8796   -399    218    -74       C
ATOM   3551  O   MET A 211     -24.355   9.501  -7.503  1.00 72.10           O
ANISOU 3551  O   MET A 211    10520   8216   8660   -354    200    -64       O
ATOM   3552  CB  MET A 211     -27.157   9.483  -7.882  1.00 74.02           C
ANISOU 3552  CB  MET A 211    10697   8511   8918   -617    367   -116       C
ATOM   3553  CG  MET A 211     -26.848  10.053  -9.257  1.00 75.19           C
ANISOU 3553  CG  MET A 211    10679   8738   9152   -588    319   -115       C
ATOM   3554  SD  MET A 211     -27.883  11.481  -9.625  1.00 80.59           S
ANISOU 3554  SD  MET A 211    11159   9540   9921   -647    329   -145       S
ATOM   3555  CE  MET A 211     -29.352  10.674 -10.268  1.00 78.10           C
ANISOU 3555  CE  MET A 211    10850   9239   9587   -788    426   -193       C
ATOM   3556  N   ALA A 212     -24.477  11.647  -6.867  1.00 69.86           N
ANISOU 3556  N   ALA A 212    10031   8044   8470   -337    158    -71       N
ATOM   3557  CA  ALA A 212     -23.040  11.814  -6.991  1.00 68.71           C
ANISOU 3557  CA  ALA A 212     9866   7903   8339   -214     72    -61       C
ATOM   3558  C   ALA A 212     -22.337  11.159  -5.803  1.00 79.18           C
ANISOU 3558  C   ALA A 212    11358   9149   9579   -133     46    -53       C
ATOM   3559  O   ALA A 212     -22.920  10.985  -4.727  1.00 87.23           O
ANISOU 3559  O   ALA A 212    12482  10122  10541   -168     86    -51       O
ATOM   3560  CB  ALA A 212     -22.678  13.297  -7.089  1.00 56.26           C
ANISOU 3560  CB  ALA A 212     8121   6411   6845   -181     24    -66       C
ATOM   3561  N   MET A 213     -21.074  10.771  -6.018  1.00 74.76           N
ANISOU 3561  N   MET A 213    10828   8573   9005    -22    -23    -54       N
ATOM   3562  CA  MET A 213     -20.232  10.184  -4.979  1.00 69.74           C
ANISOU 3562  CA  MET A 213    10342   7870   8286     84    -67    -54       C
ATOM   3563  C   MET A 213     -19.592  11.228  -4.087  1.00 72.36           C
ANISOU 3563  C   MET A 213    10608   8244   8640    159   -126    -66       C
ATOM   3564  O   MET A 213     -19.069  10.880  -3.026  1.00 78.41           O
ANISOU 3564  O   MET A 213    11499   8960   9334    241   -159    -69       O
ATOM   3565  CB  MET A 213     -19.130   9.332  -5.606  1.00 68.40           C
ANISOU 3565  CB  MET A 213    10222   7676   8092    182   -123    -61       C
ATOM   3566  CG  MET A 213     -19.659   8.296  -6.560  1.00 72.36           C
ANISOU 3566  CG  MET A 213    10784   8135   8574    115    -70    -51       C
ATOM   3567  SD  MET A 213     -20.196   6.845  -5.652  1.00 77.90           S
ANISOU 3567  SD  MET A 213    11764   8697   9138     93    -11    -35       S
ATOM   3568  CE  MET A 213     -21.981   6.991  -5.795  1.00 79.06           C
ANISOU 3568  CE  MET A 213    11881   8851   9305   -100    110    -32       C
ATOM   3569  N   TRP A 214     -19.599  12.483  -4.515  1.00 73.64           N
ANISOU 3569  N   TRP A 214    10585   8498   8897    135   -140    -75       N
ATOM   3570  CA  TRP A 214     -19.099  13.613  -3.756  1.00 68.54           C
ANISOU 3570  CA  TRP A 214     9857   7902   8284    187   -186    -89       C
ATOM   3571  C   TRP A 214     -19.812  14.824  -4.327  1.00 69.99           C
ANISOU 3571  C   TRP A 214     9872   8162   8558    101   -156    -87       C
ATOM   3572  O   TRP A 214     -19.989  14.911  -5.544  1.00 75.85           O
ANISOU 3572  O   TRP A 214    10526   8940   9353     58   -142    -86       O
ATOM   3573  CB  TRP A 214     -17.569  13.747  -3.872  1.00 66.02           C
ANISOU 3573  CB  TRP A 214     9492   7615   7977    314   -274   -119       C
ATOM   3574  CG  TRP A 214     -17.013  14.940  -3.129  1.00 67.68           C
ANISOU 3574  CG  TRP A 214     9609   7882   8223    363   -319   -143       C
ATOM   3575  CD1 TRP A 214     -16.468  14.951  -1.872  1.00 57.40           C
ANISOU 3575  CD1 TRP A 214     8383   6560   6868    448   -362   -159       C
ATOM   3576  CD2 TRP A 214     -16.974  16.301  -3.594  1.00 71.27           C
ANISOU 3576  CD2 TRP A 214     9885   8422   8772    326   -322   -154       C
ATOM   3577  NE1 TRP A 214     -16.095  16.236  -1.527  1.00 57.52           N
ANISOU 3577  NE1 TRP A 214     8267   6645   6942    463   -391   -182       N
ATOM   3578  CE2 TRP A 214     -16.395  17.078  -2.570  1.00 62.52           C
ANISOU 3578  CE2 TRP A 214     8749   7341   7666    386   -364   -179       C
ATOM   3579  CE3 TRP A 214     -17.384  16.939  -4.773  1.00 77.09           C
ANISOU 3579  CE3 TRP A 214    10493   9210   9588    250   -292   -147       C
ATOM   3580  CZ2 TRP A 214     -16.216  18.453  -2.696  1.00 60.35           C
ANISOU 3580  CZ2 TRP A 214     8323   7139   7469    366   -373   -196       C
ATOM   3581  CZ3 TRP A 214     -17.195  18.309  -4.891  1.00 70.67           C
ANISOU 3581  CZ3 TRP A 214     9540   8465   8847    236   -303   -162       C
ATOM   3582  CH2 TRP A 214     -16.620  19.045  -3.863  1.00 62.59           C
ANISOU 3582  CH2 TRP A 214     8493   7464   7823    290   -340   -186       C
ATOM   3583  N   GLY A 215     -20.252  15.731  -3.455  1.00 69.88           N
ANISOU 3583  N   GLY A 215     9823   8171   8558     78   -146    -88       N
ATOM   3584  CA  GLY A 215     -20.948  16.930  -3.880  1.00 66.75           C
ANISOU 3584  CA  GLY A 215     9279   7843   8239      8   -123    -89       C
ATOM   3585  C   GLY A 215     -22.454  16.891  -3.724  1.00 70.22           C
ANISOU 3585  C   GLY A 215     9737   8274   8668   -102    -47    -81       C
ATOM   3586  O   GLY A 215     -23.105  17.921  -3.930  1.00 74.89           O
ANISOU 3586  O   GLY A 215    10215   8923   9317   -152    -31    -87       O
ATOM   3587  N   ASN A 216     -23.031  15.736  -3.388  1.00 73.36           N
ANISOU 3587  N   ASN A 216    10275   8603   8993   -143      1    -75       N
ATOM   3588  CA  ASN A 216     -24.392  15.687  -2.866  1.00 79.58           C
ANISOU 3588  CA  ASN A 216    11099   9381   9756   -246     76    -80       C
ATOM   3589  C   ASN A 216     -24.397  16.219  -1.439  1.00 95.69           C
ANISOU 3589  C   ASN A 216    13181  11409  11768   -223     69    -81       C
ATOM   3590  O   ASN A 216     -23.547  17.039  -1.076  1.00108.14           O
ANISOU 3590  O   ASN A 216    14697  13017  13375   -144      7    -82       O
ATOM   3591  CB  ASN A 216     -24.924  14.261  -2.906  1.00 78.96           C
ANISOU 3591  CB  ASN A 216    11173   9227   9603   -303    138    -78       C
ATOM   3592  CG  ASN A 216     -23.989  13.277  -2.224  1.00 75.03           C
ANISOU 3592  CG  ASN A 216    10848   8640   9019   -216    107    -63       C
ATOM   3593  OD1 ASN A 216     -22.773  13.461  -2.225  1.00 71.41           O
ANISOU 3593  OD1 ASN A 216    10372   8190   8572   -105     30    -60       O
ATOM   3594  ND2 ASN A 216     -24.554  12.228  -1.634  1.00 69.68           N
ANISOU 3594  ND2 ASN A 216    10344   7879   8253   -267    170    -61       N
ATOM   3595  N   LYS A 217     -25.316  15.761  -0.605  1.00 93.10           N
ANISOU 3595  N   LYS A 217    12957  11037  11379   -294    134    -86       N
ATOM   3596  CA  LYS A 217     -25.240  16.162   0.805  1.00 86.71           C
ANISOU 3596  CA  LYS A 217    12207  10206  10532   -265    126    -86       C
ATOM   3597  C   LYS A 217     -25.629  15.036   1.778  1.00 93.45           C
ANISOU 3597  C   LYS A 217    13269  10961  11275   -297    183    -82       C
ATOM   3598  O   LYS A 217     -25.914  15.297   2.950  1.00 96.83           O
ANISOU 3598  O   LYS A 217    13758  11369  11665   -305    200    -85       O
ATOM   3599  CB  LYS A 217     -26.110  17.401   1.048  1.00 75.94           C
ANISOU 3599  CB  LYS A 217    10711   8916   9227   -325    148   -103       C
ATOM   3600  CG  LYS A 217     -25.413  18.720   0.738  1.00 71.37           C
ANISOU 3600  CG  LYS A 217     9973   8411   8732   -258     78   -103       C
ATOM   3601  CD  LYS A 217     -24.141  18.869   1.544  1.00 82.84           C
ANISOU 3601  CD  LYS A 217    11473   9841  10162   -145      8    -95       C
ATOM   3602  CE  LYS A 217     -23.045  19.574   0.766  1.00 93.10           C
ANISOU 3602  CE  LYS A 217    12649  11194  11531    -70    -63    -99       C
ATOM   3603  NZ  LYS A 217     -22.020  20.233   1.638  1.00 96.97           N
ANISOU 3603  NZ  LYS A 217    13125  11696  12022     23   -126   -109       N
ATOM   3604  OXT LYS A 217     -25.661  13.843   1.448  1.00 91.82           O
ANISOU 3604  OXT LYS A 217    13187  10689  11012   -316    214    -75       O
TER
HETATM 3605  CB1 GSH A 701     -26.913  20.494 -19.719  1.00 62.28           C
ANISOU 3605  CB1 GSH A 701     7773   7762   8126   -380      3   -137       C
HETATM 3606  CB2 GSH A 701     -29.315  18.509 -14.588  1.00 80.65           C
ANISOU 3606  CB2 GSH A 701    10290  10029  10324   -547    137   -201       C
HETATM 3607  CG1 GSH A 701     -28.243  20.295 -19.025  1.00 65.95           C
ANISOU 3607  CG1 GSH A 701     8233   8254   8571   -425     32   -171       C
HETATM 3608  SG2 GSH A 701     -27.714  19.052 -14.044  1.00 87.62           S
ANISOU 3608  SG2 GSH A 701    11199  10870  11223   -464     84   -154       S
HETATM 3609  CD1 GSH A 701     -28.389  19.153 -18.044  1.00 69.81           C
ANISOU 3609  CD1 GSH A 701     8791   8708   9026   -469     67   -176       C
HETATM 3610  OE1 GSH A 701     -27.619  18.209 -18.076  1.00 66.16           O
ANISOU 3610  OE1 GSH A 701     8390   8200   8549   -466     71   -157       O
HETATM 3611  C1  GSH A 701     -26.685  23.040 -20.243  1.00 51.78           C
ANISOU 3611  C1  GSH A 701     6368   6467   6838   -314    -42   -126       C
HETATM 3612  C2  GSH A 701     -30.782  17.361 -16.179  1.00 75.76           C
ANISOU 3612  C2  GSH A 701     9633   9459   9693   -637    192   -260       C
HETATM 3613  C3  GSH A 701     -33.752  16.856 -18.485  1.00 79.34           C
ANISOU 3613  C3  GSH A 701     9916  10082  10150   -753    252   -411       C
HETATM 3614  CA1 GSH A 701     -26.722  21.600 -20.750  1.00 58.87           C
ANISOU 3614  CA1 GSH A 701     7292   7354   7720   -344    -23   -130       C
HETATM 3615  CA2 GSH A 701     -29.518  18.132 -16.010  1.00 74.50           C
ANISOU 3615  CA2 GSH A 701     9475   9275   9559   -557    138   -211       C
HETATM 3616  CA3 GSH A 701     -32.964  16.937 -17.214  1.00 71.31           C
ANISOU 3616  CA3 GSH A 701     8975   8999   9121   -738    251   -364       C
HETATM 3617  N1  GSH A 701     -25.618  21.314 -21.668  1.00 57.19           N
ANISOU 3617  N1  GSH A 701     7092   7118   7519   -325    -33   -110       N
HETATM 3618  N2  GSH A 701     -29.356  19.224 -16.982  1.00 77.11           N
ANISOU 3618  N2  GSH A 701     9719   9647   9931   -509     96   -205       N
HETATM 3619  N3  GSH A 701     -31.721  17.654 -17.251  1.00 76.56           N
ANISOU 3619  N3  GSH A 701     9646   9632   9813   -654    194   -302       N
HETATM 3620  O11 GSH A 701     -25.446  23.469 -19.800  1.00 49.17           O
ANISOU 3620  O11 GSH A 701     6053   6106   6523   -288    -56   -105       O
HETATM 3621  O12 GSH A 701     -27.764  23.512 -19.507  1.00 44.35           O
ANISOU 3621  O12 GSH A 701     5405   5557   5890   -324    -37   -150       O
HETATM 3622  O2  GSH A 701     -31.135  16.613 -15.300  1.00 78.49           O
ANISOU 3622  O2  GSH A 701    10050   9774  10000   -689    238   -274       O
HETATM 3623  O31 GSH A 701     -33.002  16.487 -19.579  1.00 84.62           O
ANISOU 3623  O31 GSH A 701    10595  10727  10829   -720    228   -376       O
HETATM 3624  O32 GSH A 701     -34.945  16.152 -18.339  1.00 86.33           O
ANISOU 3624  O32 GSH A 701    10790  11004  11007   -842    313   -483       O
TER
ATOM   3625  N   PRO B   1      -9.068 -19.212 -40.853  1.00 80.46           N
ANISOU 3625  N   PRO B   1    12449   8737   9387    663   -237   -430       N
ATOM   3626  CA  PRO B   1      -9.712 -17.998 -41.365  1.00 83.87           C
ANISOU 3626  CA  PRO B   1    12672   9273   9922    534   -193   -410       C
ATOM   3627  C   PRO B   1      -9.306 -17.656 -42.805  1.00 83.54           C
ANISOU 3627  C   PRO B   1    12444   9337   9960    514   -204   -435       C
ATOM   3628  O   PRO B   1      -8.145 -17.858 -43.174  1.00 76.93           O
ANISOU 3628  O   PRO B   1    11570   8538   9123    631   -272   -481       O
ATOM   3629  CB  PRO B   1      -9.223 -16.918 -40.397  1.00 78.75           C
ANISOU 3629  CB  PRO B   1    11942   8680   9298    595   -242   -416       C
ATOM   3630  CG  PRO B   1      -7.872 -17.396 -39.967  1.00 80.40           C
ANISOU 3630  CG  PRO B   1    12217   8878   9454    779   -337   -466       C
ATOM   3631  CD  PRO B   1      -7.928 -18.907 -39.969  1.00 79.71           C
ANISOU 3631  CD  PRO B   1    12357   8663   9267    825   -330   -465       C
ATOM   3632  N   MET B   2     -10.249 -17.146 -43.599  1.00 80.55           N
ANISOU 3632  N   MET B   2    11953   9007   9644    372   -138   -410       N
ATOM   3633  CA  MET B   2      -9.923 -16.665 -44.936  1.00 75.27           C
ANISOU 3633  CA  MET B   2    11106   8441   9051    346   -145   -430       C
ATOM   3634  C   MET B   2      -9.100 -15.385 -44.849  1.00 75.80           C
ANISOU 3634  C   MET B   2    11000   8618   9185    395   -194   -452       C
ATOM   3635  O   MET B   2      -9.259 -14.576 -43.931  1.00 79.27           O
ANISOU 3635  O   MET B   2    11414   9070   9635    390   -198   -437       O
ATOM   3636  CB  MET B   2     -11.192 -16.398 -45.744  1.00 66.03           C
ANISOU 3636  CB  MET B   2     9868   7295   7925    189    -66   -400       C
ATOM   3637  CG  MET B   2     -12.079 -17.605 -45.984  1.00 70.18           C
ANISOU 3637  CG  MET B   2    10542   7727   8396    117     -4   -387       C
ATOM   3638  SD  MET B   2     -13.600 -17.143 -46.854  1.00 80.65           S
ANISOU 3638  SD  MET B   2    11763   9103   9777    -63     82   -367       S
ATOM   3639  CE  MET B   2     -14.802 -18.249 -46.113  1.00 77.23           C
ANISOU 3639  CE  MET B   2    11539   8543   9262   -153    163   -354       C
ATOM   3640  N   ILE B   3      -8.212 -15.196 -45.814  1.00 68.45           N
ANISOU 3640  N   ILE B   3     9948   7764   8294    437   -228   -492       N
ATOM   3641  CA  ILE B   3      -7.388 -13.998 -45.864  1.00 63.36           C
ANISOU 3641  CA  ILE B   3     9136   7225   7712    470   -265   -523       C
ATOM   3642  C   ILE B   3      -7.798 -13.203 -47.091  1.00 63.17           C
ANISOU 3642  C   ILE B   3     8958   7281   7762    363   -221   -511       C
ATOM   3643  O   ILE B   3      -7.609 -13.651 -48.230  1.00 60.76           O
ANISOU 3643  O   ILE B   3     8622   6995   7468    350   -213   -528       O
ATOM   3644  CB  ILE B   3      -5.891 -14.319 -45.897  1.00 60.77           C
ANISOU 3644  CB  ILE B   3     8788   6934   7369    613   -342   -595       C
ATOM   3645  CG1 ILE B   3      -5.482 -15.111 -44.658  1.00 59.99           C
ANISOU 3645  CG1 ILE B   3     8854   6753   7186    736   -393   -609       C
ATOM   3646  CG2 ILE B   3      -5.081 -13.021 -45.972  1.00 52.33           C
ANISOU 3646  CG2 ILE B   3     7537   5981   6367    626   -367   -635       C
ATOM   3647  CD1 ILE B   3      -4.065 -15.600 -44.732  1.00 62.28           C
ANISOU 3647  CD1 ILE B   3     9137   7075   7449    888   -474   -689       C
ATOM   3648  N   LEU B   4      -8.359 -12.023 -46.855  1.00 58.54           N
ANISOU 3648  N   LEU B   4     8282   6737   7222    289   -194   -482       N
ATOM   3649  CA  LEU B   4      -8.592 -11.032 -47.895  1.00 58.85           C
ANISOU 3649  CA  LEU B   4     8174   6859   7330    207   -163   -476       C
ATOM   3650  C   LEU B   4      -7.508  -9.956 -47.804  1.00 62.41           C
ANISOU 3650  C   LEU B   4     8497   7393   7823    254   -198   -516       C
ATOM   3651  O   LEU B   4      -7.350  -9.307 -46.763  1.00 59.76           O
ANISOU 3651  O   LEU B   4     8153   7065   7490    281   -217   -516       O
ATOM   3652  CB  LEU B   4      -9.987 -10.431 -47.750  1.00 49.52           C
ANISOU 3652  CB  LEU B   4     6983   5668   6166     96   -108   -422       C
ATOM   3653  CG  LEU B   4     -10.192  -9.056 -48.371  1.00 52.78           C
ANISOU 3653  CG  LEU B   4     7250   6163   6642     32    -88   -412       C
ATOM   3654  CD1 LEU B   4      -9.998  -9.107 -49.890  1.00 55.04           C
ANISOU 3654  CD1 LEU B   4     7464   6495   6955      2    -74   -428       C
ATOM   3655  CD2 LEU B   4     -11.578  -8.577 -48.009  1.00 51.45           C
ANISOU 3655  CD2 LEU B   4     7090   5979   6478    -57    -45   -367       C
ATOM   3656  N   GLY B   5      -6.755  -9.779 -48.883  1.00 60.10           N
ANISOU 3656  N   GLY B   5     8108   7165   7562    260   -204   -556       N
ATOM   3657  CA  GLY B   5      -5.641  -8.843 -48.915  1.00 58.58           C
ANISOU 3657  CA  GLY B   5     7794   7055   7407    296   -229   -609       C
ATOM   3658  C   GLY B   5      -5.931  -7.676 -49.853  1.00 59.47           C
ANISOU 3658  C   GLY B   5     7790   7231   7576    199   -182   -593       C
ATOM   3659  O   GLY B   5      -6.432  -7.874 -50.957  1.00 71.16           O
ANISOU 3659  O   GLY B   5     9260   8713   9066    139   -148   -573       O
ATOM   3660  N   TYR B   6      -5.596  -6.474 -49.405  1.00 59.40           N
ANISOU 3660  N   TYR B   6     7700   7270   7599    188   -182   -605       N
ATOM   3661  CA  TYR B   6      -5.898  -5.275 -50.173  1.00 55.77           C
ANISOU 3661  CA  TYR B   6     7149   6859   7184     99   -137   -587       C
ATOM   3662  C   TYR B   6      -5.213  -4.104 -49.487  1.00 67.55           C
ANISOU 3662  C   TYR B   6     8564   8400   8702    111   -146   -619       C
ATOM   3663  O   TYR B   6      -4.771  -4.215 -48.339  1.00 69.65           O
ANISOU 3663  O   TYR B   6     8854   8658   8953    179   -185   -642       O
ATOM   3664  CB  TYR B   6      -7.417  -5.046 -50.286  1.00 49.42           C
ANISOU 3664  CB  TYR B   6     6383   6015   6380     17    -98   -511       C
ATOM   3665  CG  TYR B   6      -7.810  -4.048 -51.351  1.00 56.93           C
ANISOU 3665  CG  TYR B   6     7260   7006   7363    -64    -55   -492       C
ATOM   3666  CD1 TYR B   6      -7.394  -4.219 -52.672  1.00 60.08           C
ANISOU 3666  CD1 TYR B   6     7621   7436   7771    -82    -39   -516       C
ATOM   3667  CD2 TYR B   6      -8.583  -2.925 -51.043  1.00 52.12           C
ANISOU 3667  CD2 TYR B   6     6629   6404   6772   -117    -32   -452       C
ATOM   3668  CE1 TYR B   6      -7.739  -3.309 -53.667  1.00 52.77           C
ANISOU 3668  CE1 TYR B   6     6644   6541   6866   -151      0   -498       C
ATOM   3669  CE2 TYR B   6      -8.926  -2.000 -52.034  1.00 56.87           C
ANISOU 3669  CE2 TYR B   6     7179   7036   7394   -180      3   -435       C
ATOM   3670  CZ  TYR B   6      -8.491  -2.206 -53.347  1.00 50.87           C
ANISOU 3670  CZ  TYR B   6     6390   6301   6638   -195     20   -458       C
ATOM   3671  OH  TYR B   6      -8.809  -1.323 -54.342  1.00 52.17           O
ANISOU 3671  OH  TYR B   6     6520   6490   6814   -252     54   -442       O
ATOM   3672  N   TRP B   7      -5.108  -2.988 -50.212  1.00 67.13           N
ANISOU 3672  N   TRP B   7     8426   8395   8685     44   -107   -623       N
ATOM   3673  CA  TRP B   7      -4.724  -1.729 -49.593  1.00 61.87           C
ANISOU 3673  CA  TRP B   7     7697   7768   8045     29   -101   -640       C
ATOM   3674  C   TRP B   7      -5.748  -1.349 -48.534  1.00 66.70           C
ANISOU 3674  C   TRP B   7     8358   8335   8649     15   -102   -578       C
ATOM   3675  O   TRP B   7      -6.868  -1.854 -48.519  1.00 68.57           O
ANISOU 3675  O   TRP B   7     8665   8521   8868     -8    -93   -520       O
ATOM   3676  CB  TRP B   7      -4.618  -0.627 -50.645  1.00 64.14           C
ANISOU 3676  CB  TRP B   7     7912   8098   8362    -52    -49   -644       C
ATOM   3677  CG  TRP B   7      -3.797  -1.033 -51.839  1.00 61.22           C
ANISOU 3677  CG  TRP B   7     7501   7766   7996    -55    -36   -698       C
ATOM   3678  CD1 TRP B   7      -4.260  -1.512 -53.024  1.00 59.80           C
ANISOU 3678  CD1 TRP B   7     7342   7572   7808    -90    -13   -672       C
ATOM   3679  CD2 TRP B   7      -2.365  -1.016 -51.944  1.00 62.08           C
ANISOU 3679  CD2 TRP B   7     7536   7938   8115    -19    -47   -795       C
ATOM   3680  NE1 TRP B   7      -3.211  -1.788 -53.866  1.00 64.63           N
ANISOU 3680  NE1 TRP B   7     7902   8229   8425    -82     -7   -741       N
ATOM   3681  CE2 TRP B   7      -2.036  -1.489 -53.224  1.00 65.70           C
ANISOU 3681  CE2 TRP B   7     7976   8415   8571    -39    -26   -820       C
ATOM   3682  CE3 TRP B   7      -1.330  -0.645 -51.077  1.00 61.34           C
ANISOU 3682  CE3 TRP B   7     7385   7892   8030     28    -72   -870       C
ATOM   3683  CZ2 TRP B   7      -0.714  -1.596 -53.662  1.00 63.72           C
ANISOU 3683  CZ2 TRP B   7     7650   8231   8329    -17    -27   -919       C
ATOM   3684  CZ3 TRP B   7      -0.018  -0.753 -51.516  1.00 54.20           C
ANISOU 3684  CZ3 TRP B   7     6402   7058   7135     51    -74   -973       C
ATOM   3685  CH2 TRP B   7       0.275  -1.217 -52.791  1.00 55.78           C
ANISOU 3685  CH2 TRP B   7     6583   7276   7333     27    -51   -998       C
ATOM   3686  N   ASP B   8      -5.362  -0.457 -47.624  1.00 78.64           N
ANISOU 3686  N   ASP B   8     9832   9871  10176     27   -111   -596       N
ATOM   3687  CA  ASP B   8      -6.336  -0.001 -46.625  1.00 76.04           C
ANISOU 3687  CA  ASP B   8     9545   9504   9842      9   -109   -539       C
ATOM   3688  C   ASP B   8      -7.140   1.184 -47.140  1.00 69.94           C
ANISOU 3688  C   ASP B   8     8741   8740   9094    -78    -63   -493       C
ATOM   3689  O   ASP B   8      -7.244   2.229 -46.503  1.00 83.28           O
ANISOU 3689  O   ASP B   8    10404  10440  10799    -96    -55   -484       O
ATOM   3690  CB  ASP B   8      -5.659   0.324 -45.297  1.00 75.53           C
ANISOU 3690  CB  ASP B   8     9469   9453   9777     69   -146   -575       C
ATOM   3691  CG  ASP B   8      -4.486   1.236 -45.454  1.00 81.79           C
ANISOU 3691  CG  ASP B   8    10161  10317  10600     68   -140   -645       C
ATOM   3692  OD1 ASP B   8      -3.877   1.227 -46.542  1.00 87.24           O
ANISOU 3692  OD1 ASP B   8    10801  11046  11303     46   -119   -685       O
ATOM   3693  OD2 ASP B   8      -4.156   1.945 -44.484  1.00 86.79           O
ANISOU 3693  OD2 ASP B   8    10766  10969  11241     86   -153   -666       O
ATOM   3694  N   ILE B   9      -7.698   1.023 -48.333  1.00 57.53           N
ANISOU 3694  N   ILE B   9     7174   7163   7522   -126    -34   -468       N
ATOM   3695  CA  ILE B   9      -8.765   1.896 -48.794  1.00 60.20           C
ANISOU 3695  CA  ILE B   9     7510   7496   7869   -194      1   -415       C
ATOM   3696  C   ILE B   9     -10.024   1.047 -48.901  1.00 52.66           C
ANISOU 3696  C   ILE B   9     6618   6498   6891   -208      2   -369       C
ATOM   3697  O   ILE B   9     -10.007  -0.152 -48.599  1.00 53.56           O
ANISOU 3697  O   ILE B   9     6784   6582   6984   -172    -19   -375       O
ATOM   3698  CB  ILE B   9      -8.419   2.580 -50.131  1.00 54.16           C
ANISOU 3698  CB  ILE B   9     6699   6764   7117   -241     38   -429       C
ATOM   3699  CG1 ILE B   9      -8.291   1.535 -51.248  1.00 55.58           C
ANISOU 3699  CG1 ILE B   9     6891   6943   7285   -238     41   -441       C
ATOM   3700  CG2 ILE B   9      -7.156   3.405 -49.981  1.00 34.59           C
ANISOU 3700  CG2 ILE B   9     4158   4327   4658   -239     47   -486       C
ATOM   3701  CD1 ILE B   9      -8.301   2.106 -52.641  1.00 45.31           C
ANISOU 3701  CD1 ILE B   9     5566   5662   5988   -290     80   -439       C
ATOM   3702  N   ARG B  10     -11.131   1.668 -49.291  1.00 49.03           N
ANISOU 3702  N   ARG B  10     6160   6037   6434   -259     26   -327       N
ATOM   3703  CA  ARG B  10     -12.345   0.913 -49.604  1.00 51.88           C
ANISOU 3703  CA  ARG B  10     6566   6372   6775   -283     33   -297       C
ATOM   3704  C   ARG B  10     -12.187   0.218 -50.960  1.00 61.65           C
ANISOU 3704  C   ARG B  10     7801   7618   8007   -293     44   -310       C
ATOM   3705  O   ARG B  10     -12.060  -1.013 -51.034  1.00 59.04           O
ANISOU 3705  O   ARG B  10     7510   7264   7660   -273     34   -322       O
ATOM   3706  CB  ARG B  10     -13.541   1.870 -49.560  1.00 49.58           C
ANISOU 3706  CB  ARG B  10     6265   6087   6487   -324     49   -262       C
ATOM   3707  CG  ARG B  10     -14.867   1.338 -50.005  1.00 51.78           C
ANISOU 3707  CG  ARG B  10     6568   6357   6748   -357     61   -243       C
ATOM   3708  CD  ARG B  10     -15.879   2.470 -49.930  1.00 48.61           C
ANISOU 3708  CD  ARG B  10     6146   5975   6350   -383     69   -220       C
ATOM   3709  NE  ARG B  10     -16.992   2.318 -50.858  1.00 54.89           N
ANISOU 3709  NE  ARG B  10     6938   6785   7131   -412     80   -216       N
ATOM   3710  CZ  ARG B  10     -18.192   2.851 -50.653  1.00 62.28           C
ANISOU 3710  CZ  ARG B  10     7865   7737   8061   -430     82   -207       C
ATOM   3711  NH1 ARG B  10     -18.413   3.567 -49.554  1.00 62.22           N
ANISOU 3711  NH1 ARG B  10     7854   7726   8060   -426     76   -196       N
ATOM   3712  NH2 ARG B  10     -19.168   2.671 -51.536  1.00 58.06           N
ANISOU 3712  NH2 ARG B  10     7322   7226   7512   -450     87   -214       N
ATOM   3713  N   GLY B  11     -12.166   1.003 -52.041  1.00 55.65           N
ANISOU 3713  N   GLY B  11     7003   6886   7256   -324     65   -308       N
ATOM   3714  CA  GLY B  11     -11.759   0.514 -53.355  1.00 56.61           C
ANISOU 3714  CA  GLY B  11     7115   7021   7372   -331     77   -326       C
ATOM   3715  C   GLY B  11     -12.580  -0.655 -53.875  1.00 53.23           C
ANISOU 3715  C   GLY B  11     6726   6574   6926   -341     77   -316       C
ATOM   3716  O   GLY B  11     -13.810  -0.692 -53.762  1.00 52.41           O
ANISOU 3716  O   GLY B  11     6641   6460   6811   -367     82   -290       O
ATOM   3717  N   LEU B  12     -11.876  -1.628 -54.456  1.00 50.17           N
ANISOU 3717  N   LEU B  12     6346   6184   6532   -322     72   -343       N
ATOM   3718  CA  LEU B  12     -12.458  -2.824 -55.058  1.00 53.01           C
ANISOU 3718  CA  LEU B  12     6744   6524   6872   -331     75   -341       C
ATOM   3719  C   LEU B  12     -12.762  -3.936 -54.059  1.00 49.04           C
ANISOU 3719  C   LEU B  12     6307   5975   6350   -311     62   -339       C
ATOM   3720  O   LEU B  12     -13.243  -4.994 -54.477  1.00 58.35           O
ANISOU 3720  O   LEU B  12     7529   7132   7510   -324     69   -341       O
ATOM   3721  CB  LEU B  12     -11.527  -3.396 -56.141  1.00 52.63           C
ANISOU 3721  CB  LEU B  12     6681   6491   6824   -317     77   -373       C
ATOM   3722  CG  LEU B  12     -11.371  -2.681 -57.483  1.00 58.51           C
ANISOU 3722  CG  LEU B  12     7384   7272   7575   -348    101   -376       C
ATOM   3723  CD1 LEU B  12     -10.080  -3.143 -58.129  1.00 65.11           C
ANISOU 3723  CD1 LEU B  12     8197   8125   8415   -325    100   -421       C
ATOM   3724  CD2 LEU B  12     -12.560  -2.910 -58.420  1.00 47.06           C
ANISOU 3724  CD2 LEU B  12     5949   5822   6110   -384    115   -354       C
ATOM   3725  N   ALA B  13     -12.490  -3.749 -52.769  1.00 47.60           N
ANISOU 3725  N   ALA B  13     6143   5774   6168   -281     44   -338       N
ATOM   3726  CA  ALA B  13     -12.810  -4.773 -51.783  1.00 43.46           C
ANISOU 3726  CA  ALA B  13     5699   5196   5615   -263     35   -334       C
ATOM   3727  C   ALA B  13     -14.111  -4.512 -51.030  1.00 44.20           C
ANISOU 3727  C   ALA B  13     5820   5273   5702   -307     53   -304       C
ATOM   3728  O   ALA B  13     -14.543  -5.379 -50.255  1.00 48.80           O
ANISOU 3728  O   ALA B  13     6481   5806   6256   -308     57   -300       O
ATOM   3729  CB  ALA B  13     -11.654  -4.938 -50.787  1.00 41.24           C
ANISOU 3729  CB  ALA B  13     5438   4902   5330   -191      1   -358       C
ATOM   3730  N   HIS B  14     -14.750  -3.356 -51.236  1.00 40.06           N
ANISOU 3730  N   HIS B  14     5237   4785   5197   -343     65   -287       N
ATOM   3731  CA  HIS B  14     -16.001  -3.062 -50.535  1.00 46.88           C
ANISOU 3731  CA  HIS B  14     6115   5643   6055   -383     80   -268       C
ATOM   3732  C   HIS B  14     -17.033  -4.161 -50.764  1.00 45.69           C
ANISOU 3732  C   HIS B  14     6015   5468   5878   -427    105   -273       C
ATOM   3733  O   HIS B  14     -17.549  -4.748 -49.809  1.00 62.57           O
ANISOU 3733  O   HIS B  14     8216   7564   7993   -443    118   -272       O
ATOM   3734  CB  HIS B  14     -16.558  -1.699 -50.966  1.00 44.53           C
ANISOU 3734  CB  HIS B  14     5749   5393   5778   -408     86   -255       C
ATOM   3735  CG  HIS B  14     -17.573  -1.129 -50.022  1.00 50.90           C
ANISOU 3735  CG  HIS B  14     6556   6201   6583   -432     92   -241       C
ATOM   3736  ND1 HIS B  14     -17.305  -0.892 -48.689  1.00 51.59           N
ANISOU 3736  ND1 HIS B  14     6666   6265   6672   -412     82   -233       N
ATOM   3737  CD2 HIS B  14     -18.854  -0.733 -50.221  1.00 51.21           C
ANISOU 3737  CD2 HIS B  14     6572   6266   6619   -471    106   -240       C
ATOM   3738  CE1 HIS B  14     -18.377  -0.380 -48.109  1.00 49.60           C
ANISOU 3738  CE1 HIS B  14     6406   6022   6418   -443     93   -225       C
ATOM   3739  NE2 HIS B  14     -19.332  -0.277 -49.016  1.00 51.11           N
ANISOU 3739  NE2 HIS B  14     6567   6246   6606   -478    107   -232       N
ATOM   3740  N   ALA B  15     -17.329  -4.478 -52.031  1.00 44.29           N
ANISOU 3740  N   ALA B  15     5815   5313   5700   -451    117   -284       N
ATOM   3741  CA  ALA B  15     -18.319  -5.526 -52.301  1.00 49.12           C
ANISOU 3741  CA  ALA B  15     6469   5906   6287   -500    145   -298       C
ATOM   3742  C   ALA B  15     -17.891  -6.875 -51.729  1.00 48.51           C
ANISOU 3742  C   ALA B  15     6491   5762   6180   -486    150   -306       C
ATOM   3743  O   ALA B  15     -18.750  -7.681 -51.351  1.00 50.17           O
ANISOU 3743  O   ALA B  15     6762   5937   6362   -533    181   -315       O
ATOM   3744  CB  ALA B  15     -18.589  -5.654 -53.808  1.00 42.03           C
ANISOU 3744  CB  ALA B  15     5530   5047   5394   -520    153   -311       C
ATOM   3745  N   ILE B  16     -16.577  -7.137 -51.647  1.00 42.49           N
ANISOU 3745  N   ILE B  16     5748   4979   5418   -421    121   -307       N
ATOM   3746  CA  ILE B  16     -16.105  -8.401 -51.083  1.00 49.29           C
ANISOU 3746  CA  ILE B  16     6714   5771   6241   -389    117   -316       C
ATOM   3747  C   ILE B  16     -16.318  -8.440 -49.576  1.00 50.97           C
ANISOU 3747  C   ILE B  16     6998   5936   6431   -381    118   -305       C
ATOM   3748  O   ILE B  16     -16.758  -9.462 -49.039  1.00 55.03           O
ANISOU 3748  O   ILE B  16     7618   6386   6903   -401    142   -308       O
ATOM   3749  CB  ILE B  16     -14.629  -8.650 -51.435  1.00 55.38           C
ANISOU 3749  CB  ILE B  16     7480   6545   7018   -311     80   -333       C
ATOM   3750  CG1 ILE B  16     -14.476  -9.038 -52.912  1.00 45.54           C
ANISOU 3750  CG1 ILE B  16     6198   5326   5780   -324     87   -348       C
ATOM   3751  CG2 ILE B  16     -14.062  -9.733 -50.522  1.00 50.86           C
ANISOU 3751  CG2 ILE B  16     7024   5899   6402   -253     62   -342       C
ATOM   3752  CD1 ILE B  16     -13.057  -8.971 -53.423  1.00 35.89           C
ANISOU 3752  CD1 ILE B  16     4935   4129   4572   -258     54   -371       C
ATOM   3753  N   ARG B  17     -15.993  -7.340 -48.869  1.00 46.81           N
ANISOU 3753  N   ARG B  17     6422   5436   5928   -354     96   -292       N
ATOM   3754  CA  ARG B  17     -16.230  -7.270 -47.424  1.00 44.04           C
ANISOU 3754  CA  ARG B  17     6133   5044   5556   -347     97   -280       C
ATOM   3755  C   ARG B  17     -17.705  -7.420 -47.106  1.00 47.09           C
ANISOU 3755  C   ARG B  17     6547   5417   5927   -433    145   -276       C
ATOM   3756  O   ARG B  17     -18.085  -8.211 -46.235  1.00 60.46           O
ANISOU 3756  O   ARG B  17     8348   7046   7578   -450    168   -276       O
ATOM   3757  CB  ARG B  17     -15.721  -5.950 -46.837  1.00 43.25           C
ANISOU 3757  CB  ARG B  17     5959   4984   5489   -313     69   -271       C
ATOM   3758  CG  ARG B  17     -14.206  -5.820 -46.756  1.00 46.71           C
ANISOU 3758  CG  ARG B  17     6378   5433   5937   -226     23   -288       C
ATOM   3759  CD  ARG B  17     -13.767  -4.390 -47.063  1.00 52.48           C
ANISOU 3759  CD  ARG B  17     6993   6232   6714   -222     11   -288       C
ATOM   3760  NE  ARG B  17     -12.338  -4.194 -46.848  1.00 47.98           N
ANISOU 3760  NE  ARG B  17     6396   5679   6154   -148    -28   -317       N
ATOM   3761  CZ  ARG B  17     -11.628  -3.206 -47.372  1.00 53.37           C
ANISOU 3761  CZ  ARG B  17     6986   6420   6873   -142    -35   -333       C
ATOM   3762  NH1 ARG B  17     -12.207  -2.304 -48.150  1.00 59.67           N
ANISOU 3762  NH1 ARG B  17     7720   7254   7696   -200     -8   -315       N
ATOM   3763  NH2 ARG B  17     -10.332  -3.124 -47.118  1.00 61.19           N
ANISOU 3763  NH2 ARG B  17     7950   7431   7869    -78    -67   -373       N
ATOM   3764  N   LEU B  18     -18.555  -6.653 -47.794  1.00 44.84           N
ANISOU 3764  N   LEU B  18     6172   5195   5672   -487    162   -277       N
ATOM   3765  CA  LEU B  18     -19.997  -6.774 -47.584  1.00 42.47           C
ANISOU 3765  CA  LEU B  18     5881   4899   5359   -570    207   -288       C
ATOM   3766  C   LEU B  18     -20.475  -8.203 -47.829  1.00 44.49           C
ANISOU 3766  C   LEU B  18     6227   5104   5575   -618    247   -310       C
ATOM   3767  O   LEU B  18     -21.303  -8.728 -47.075  1.00 44.01           O
ANISOU 3767  O   LEU B  18     6237   5004   5482   -676    290   -321       O
ATOM   3768  CB  LEU B  18     -20.741  -5.797 -48.493  1.00 40.89           C
ANISOU 3768  CB  LEU B  18     5565   4779   5192   -603    209   -296       C
ATOM   3769  CG  LEU B  18     -20.372  -4.334 -48.320  1.00 45.42           C
ANISOU 3769  CG  LEU B  18     6058   5398   5800   -563    176   -275       C
ATOM   3770  CD1 LEU B  18     -20.826  -3.505 -49.537  1.00 39.09           C
ANISOU 3770  CD1 LEU B  18     5163   4667   5022   -575    170   -282       C
ATOM   3771  CD2 LEU B  18     -21.003  -3.857 -47.031  1.00 48.30           C
ANISOU 3771  CD2 LEU B  18     6437   5755   6161   -584    187   -270       C
ATOM   3772  N   LEU B  19     -19.963  -8.851 -48.876  1.00 47.06           N
ANISOU 3772  N   LEU B  19     6555   5427   5899   -599    239   -318       N
ATOM   3773  CA  LEU B  19     -20.373 -10.225 -49.138  1.00 57.58           C
ANISOU 3773  CA  LEU B  19     7980   6708   7191   -645    279   -339       C
ATOM   3774  C   LEU B  19     -19.819 -11.162 -48.070  1.00 52.73           C
ANISOU 3774  C   LEU B  19     7513   5996   6527   -611    282   -331       C
ATOM   3775  O   LEU B  19     -20.546 -12.009 -47.535  1.00 57.11           O
ANISOU 3775  O   LEU B  19     8171   6491   7037   -671    332   -344       O
ATOM   3776  CB  LEU B  19     -19.945 -10.657 -50.550  1.00 57.27           C
ANISOU 3776  CB  LEU B  19     7906   6692   7163   -630    268   -351       C
ATOM   3777  CG  LEU B  19     -20.449 -12.035 -51.014  1.00 49.53           C
ANISOU 3777  CG  LEU B  19     7009   5666   6145   -685    312   -377       C
ATOM   3778  CD1 LEU B  19     -21.959 -12.085 -51.185  1.00 48.86           C
ANISOU 3778  CD1 LEU B  19     6896   5614   6056   -790    367   -410       C
ATOM   3779  CD2 LEU B  19     -19.788 -12.426 -52.286  1.00 47.44           C
ANISOU 3779  CD2 LEU B  19     6715   5419   5891   -651    291   -384       C
ATOM   3780  N   LEU B  20     -18.541 -11.007 -47.725  1.00 46.01           N
ANISOU 3780  N   LEU B  20     6677   5127   5678   -513    229   -314       N
ATOM   3781  CA  LEU B  20     -17.978 -11.823 -46.656  1.00 52.46           C
ANISOU 3781  CA  LEU B  20     7638   5852   6441   -462    220   -308       C
ATOM   3782  C   LEU B  20     -18.814 -11.695 -45.393  1.00 66.88           C
ANISOU 3782  C   LEU B  20     9530   7641   8240   -512    257   -300       C
ATOM   3783  O   LEU B  20     -19.109 -12.695 -44.724  1.00 67.86           O
ANISOU 3783  O   LEU B  20     9802   7678   8304   -535    292   -304       O
ATOM   3784  CB  LEU B  20     -16.534 -11.408 -46.379  1.00 51.74           C
ANISOU 3784  CB  LEU B  20     7525   5772   6363   -345    152   -301       C
ATOM   3785  CG  LEU B  20     -15.461 -11.982 -47.299  1.00 60.82           C
ANISOU 3785  CG  LEU B  20     8670   6927   7514   -276    116   -318       C
ATOM   3786  CD1 LEU B  20     -14.099 -11.410 -46.930  1.00 67.24           C
ANISOU 3786  CD1 LEU B  20     9438   7766   8343   -169     51   -326       C
ATOM   3787  CD2 LEU B  20     -15.447 -13.500 -47.258  1.00 59.94           C
ANISOU 3787  CD2 LEU B  20     8714   6724   7338   -267    133   -329       C
ATOM   3788  N   GLU B  21     -19.234 -10.465 -45.072  1.00 66.86           N
ANISOU 3788  N   GLU B  21     9424   7702   8279   -533    252   -290       N
ATOM   3789  CA  GLU B  21     -19.990 -10.228 -43.851  1.00 53.40           C
ANISOU 3789  CA  GLU B  21     7767   5969   6553   -578    283   -285       C
ATOM   3790  C   GLU B  21     -21.428 -10.711 -43.982  1.00 53.52           C
ANISOU 3790  C   GLU B  21     7806   5980   6549   -699    358   -312       C
ATOM   3791  O   GLU B  21     -21.961 -11.315 -43.050  1.00 58.85           O
ANISOU 3791  O   GLU B  21     8599   6587   7174   -747    405   -319       O
ATOM   3792  CB  GLU B  21     -19.924  -8.749 -43.477  1.00 50.72           C
ANISOU 3792  CB  GLU B  21     7309   5699   6263   -555    251   -270       C
ATOM   3793  CG  GLU B  21     -18.548  -8.318 -42.943  1.00 58.74           C
ANISOU 3793  CG  GLU B  21     8324   6708   7286   -444    187   -252       C
ATOM   3794  CD  GLU B  21     -18.413  -8.465 -41.410  1.00 63.60           C
ANISOU 3794  CD  GLU B  21     9049   7258   7859   -414    184   -240       C
ATOM   3795  OE1 GLU B  21     -19.448  -8.553 -40.706  1.00 64.02           O
ANISOU 3795  OE1 GLU B  21     9153   7284   7889   -487    233   -240       O
ATOM   3796  OE2 GLU B  21     -17.271  -8.483 -40.905  1.00 57.81           O
ANISOU 3796  OE2 GLU B  21     8350   6502   7114   -316    132   -236       O
ATOM   3797  N   TYR B  22     -22.066 -10.492 -45.135  1.00 61.82           N
ANISOU 3797  N   TYR B  22     8751   7103   7634   -752    374   -335       N
ATOM   3798  CA  TYR B  22     -23.427 -10.990 -45.328  1.00 56.13           C
ANISOU 3798  CA  TYR B  22     8041   6390   6895   -868    445   -376       C
ATOM   3799  C   TYR B  22     -23.506 -12.502 -45.146  1.00 59.41           C
ANISOU 3799  C   TYR B  22     8620   6707   7247   -909    496   -391       C
ATOM   3800  O   TYR B  22     -24.494 -13.024 -44.614  1.00 61.40           O
ANISOU 3800  O   TYR B  22     8942   6926   7462  -1005    566   -421       O
ATOM   3801  CB  TYR B  22     -23.945 -10.617 -46.712  1.00 52.37           C
ANISOU 3801  CB  TYR B  22     7431   6006   6461   -899    442   -402       C
ATOM   3802  CG  TYR B  22     -25.332 -11.162 -46.943  1.00 57.54           C
ANISOU 3802  CG  TYR B  22     8085   6679   7096  -1016    513   -458       C
ATOM   3803  CD1 TYR B  22     -25.551 -12.271 -47.765  1.00 50.02           C
ANISOU 3803  CD1 TYR B  22     7179   5705   6121  -1063    549   -488       C
ATOM   3804  CD2 TYR B  22     -26.427 -10.596 -46.304  1.00 56.42           C
ANISOU 3804  CD2 TYR B  22     7898   6579   6958  -1084    547   -488       C
ATOM   3805  CE1 TYR B  22     -26.822 -12.772 -47.953  1.00 52.30           C
ANISOU 3805  CE1 TYR B  22     7463   6016   6392  -1178    619   -551       C
ATOM   3806  CE2 TYR B  22     -27.699 -11.092 -46.495  1.00 52.67           C
ANISOU 3806  CE2 TYR B  22     7414   6131   6466  -1196    616   -554       C
ATOM   3807  CZ  TYR B  22     -27.893 -12.182 -47.309  1.00 53.88           C
ANISOU 3807  CZ  TYR B  22     7610   6264   6597  -1245    653   -587       C
ATOM   3808  OH  TYR B  22     -29.171 -12.657 -47.480  1.00 54.74           O
ANISOU 3808  OH  TYR B  22     7703   6408   6689  -1363    725   -663       O
ATOM   3809  N   THR B  23     -22.486 -13.222 -45.593  1.00 59.97           N
ANISOU 3809  N   THR B  23     8756   6729   7301   -838    464   -375       N
ATOM   3810  CA  THR B  23     -22.484 -14.674 -45.519  1.00 59.59           C
ANISOU 3810  CA  THR B  23     8873   6581   7187   -866    508   -388       C
ATOM   3811  C   THR B  23     -21.897 -15.204 -44.217  1.00 62.82           C
ANISOU 3811  C   THR B  23     9455   6880   7533   -813    504   -363       C
ATOM   3812  O   THR B  23     -21.774 -16.420 -44.063  1.00 75.02           O
ANISOU 3812  O   THR B  23    11165   8327   9013   -820    535   -369       O
ATOM   3813  CB  THR B  23     -21.720 -15.266 -46.719  1.00 53.46           C
ANISOU 3813  CB  THR B  23     8087   5807   6418   -814    476   -389       C
ATOM   3814  OG1 THR B  23     -20.332 -14.898 -46.657  1.00 54.07           O
ANISOU 3814  OG1 THR B  23     8147   5885   6511   -683    396   -358       O
ATOM   3815  CG2 THR B  23     -22.326 -14.768 -48.034  1.00 37.67           C
ANISOU 3815  CG2 THR B  23     5926   3912   4473   -864    481   -414       C
ATOM   3816  N   GLY B  24     -21.545 -14.335 -43.274  1.00 62.85           N
ANISOU 3816  N   GLY B  24     9436   6895   7550   -758    466   -337       N
ATOM   3817  CA  GLY B  24     -20.971 -14.804 -42.021  1.00 53.68           C
ANISOU 3817  CA  GLY B  24     8440   5632   6324   -697    456   -316       C
ATOM   3818  C   GLY B  24     -19.681 -15.570 -42.194  1.00 55.06           C
ANISOU 3818  C   GLY B  24     8711   5745   6465   -578    400   -304       C
ATOM   3819  O   GLY B  24     -19.400 -16.480 -41.412  1.00 55.78           O
ANISOU 3819  O   GLY B  24     8991   5725   6477   -544    410   -299       O
ATOM   3820  N   SER B  25     -18.887 -15.233 -43.208  1.00 56.71           N
ANISOU 3820  N   SER B  25     8799   6023   6725   -510    341   -305       N
ATOM   3821  CA  SER B  25     -17.620 -15.918 -43.416  1.00 59.65           C
ANISOU 3821  CA  SER B  25     9244   6351   7068   -390    283   -304       C
ATOM   3822  C   SER B  25     -16.601 -15.539 -42.342  1.00 56.91           C
ANISOU 3822  C   SER B  25     8937   5983   6703   -267    216   -290       C
ATOM   3823  O   SER B  25     -16.576 -14.417 -41.830  1.00 56.23           O
ANISOU 3823  O   SER B  25     8751   5955   6659   -258    193   -279       O
ATOM   3824  CB  SER B  25     -17.057 -15.608 -44.805  1.00 64.14           C
ANISOU 3824  CB  SER B  25     9664   7007   7699   -360    244   -315       C
ATOM   3825  OG  SER B  25     -17.991 -15.932 -45.826  1.00 66.61           O
ANISOU 3825  OG  SER B  25     9935   7345   8028   -466    301   -331       O
ATOM   3826  N   ASP B  26     -15.758 -16.504 -42.003  1.00 53.79           N
ANISOU 3826  N   ASP B  26     8695   5503   6241   -169    182   -295       N
ATOM   3827  CA  ASP B  26     -14.685 -16.310 -41.043  1.00 55.67           C
ANISOU 3827  CA  ASP B  26     8982   5720   6451    -33    109   -293       C
ATOM   3828  C   ASP B  26     -13.463 -15.843 -41.824  1.00 59.50           C
ANISOU 3828  C   ASP B  26     9323   6292   6991     69     31   -315       C
ATOM   3829  O   ASP B  26     -12.869 -16.612 -42.589  1.00 65.16           O
ANISOU 3829  O   ASP B  26    10069   6997   7693    120      8   -336       O
ATOM   3830  CB  ASP B  26     -14.441 -17.607 -40.269  1.00 72.82           C
ANISOU 3830  CB  ASP B  26    11402   7752   8513     29    111   -293       C
ATOM   3831  CG  ASP B  26     -13.256 -17.528 -39.326  1.00 83.07           C
ANISOU 3831  CG  ASP B  26    12762   9028   9772    191     24   -301       C
ATOM   3832  OD1 ASP B  26     -13.209 -16.594 -38.500  1.00 86.20           O
ANISOU 3832  OD1 ASP B  26    13099   9462  10192    207      4   -291       O
ATOM   3833  OD2 ASP B  26     -12.378 -18.417 -39.402  1.00 86.55           O
ANISOU 3833  OD2 ASP B  26    13314   9414  10156    307    -25   -321       O
ATOM   3834  N   TYR B  27     -13.116 -14.569 -41.669  1.00 56.27           N
ANISOU 3834  N   TYR B  27     8758   5977   6647     90     -5   -314       N
ATOM   3835  CA  TYR B  27     -12.064 -13.977 -42.476  1.00 55.15           C
ANISOU 3835  CA  TYR B  27     8462   5930   6565    158    -63   -341       C
ATOM   3836  C   TYR B  27     -11.304 -12.944 -41.656  1.00 55.75           C
ANISOU 3836  C   TYR B  27     8459   6058   6666    234   -119   -350       C
ATOM   3837  O   TYR B  27     -11.750 -12.486 -40.602  1.00 57.38           O
ANISOU 3837  O   TYR B  27     8699   6243   6861    216   -107   -329       O
ATOM   3838  CB  TYR B  27     -12.634 -13.341 -43.763  1.00 60.00           C
ANISOU 3838  CB  TYR B  27     8914   6629   7253     57    -26   -336       C
ATOM   3839  CG  TYR B  27     -13.395 -12.056 -43.522  1.00 51.73           C
ANISOU 3839  CG  TYR B  27     7751   5643   6260    -23      1   -314       C
ATOM   3840  CD1 TYR B  27     -14.737 -12.078 -43.171  1.00 52.53           C
ANISOU 3840  CD1 TYR B  27     7895   5714   6350   -131     65   -291       C
ATOM   3841  CD2 TYR B  27     -12.763 -10.823 -43.614  1.00 46.54           C
ANISOU 3841  CD2 TYR B  27     6946   5073   5663      9    -37   -321       C
ATOM   3842  CE1 TYR B  27     -15.437 -10.898 -42.929  1.00 50.76           C
ANISOU 3842  CE1 TYR B  27     7566   5549   6173   -195     85   -276       C
ATOM   3843  CE2 TYR B  27     -13.449  -9.641 -43.372  1.00 44.64           C
ANISOU 3843  CE2 TYR B  27     6611   4883   5467    -57    -14   -300       C
ATOM   3844  CZ  TYR B  27     -14.784  -9.684 -43.028  1.00 47.73           C
ANISOU 3844  CZ  TYR B  27     7044   5245   5845   -153     43   -277       C
ATOM   3845  OH  TYR B  27     -15.473  -8.512 -42.794  1.00 53.40           O
ANISOU 3845  OH  TYR B  27     7668   6016   6605   -211     60   -261       O
ATOM   3846  N   GLU B  28     -10.142 -12.577 -42.179  1.00 61.66           N
ANISOU 3846  N   GLU B  28     9097   6879   7450    316   -176   -388       N
ATOM   3847  CA  GLU B  28      -9.286 -11.537 -41.637  1.00 57.75           C
ANISOU 3847  CA  GLU B  28     8498   6455   6991    383   -228   -412       C
ATOM   3848  C   GLU B  28      -8.700 -10.785 -42.829  1.00 62.40           C
ANISOU 3848  C   GLU B  28     8906   7150   7654    368   -237   -441       C
ATOM   3849  O   GLU B  28      -8.615 -11.330 -43.937  1.00 57.50           O
ANISOU 3849  O   GLU B  28     8270   6538   7041    352   -225   -452       O
ATOM   3850  CB  GLU B  28      -8.198 -12.154 -40.725  1.00 53.38           C
ANISOU 3850  CB  GLU B  28     8048   5861   6373    536   -300   -451       C
ATOM   3851  CG  GLU B  28      -6.950 -11.306 -40.453  1.00 76.74           C
ANISOU 3851  CG  GLU B  28    10881   8909   9366    631   -367   -506       C
ATOM   3852  CD  GLU B  28      -7.193 -10.050 -39.589  1.00 96.28           C
ANISOU 3852  CD  GLU B  28    13280  11423  11877    598   -362   -488       C
ATOM   3853  OE1 GLU B  28      -8.239  -9.364 -39.742  1.00 94.95           O
ANISOU 3853  OE1 GLU B  28    13061  11266  11750    477   -303   -440       O
ATOM   3854  OE2 GLU B  28      -6.315  -9.760 -38.738  1.00102.42           O
ANISOU 3854  OE2 GLU B  28    14049  12225  12641    701   -421   -529       O
ATOM   3855  N   GLU B  29      -8.311  -9.533 -42.609  1.00 58.75           N
ANISOU 3855  N   GLU B  29     8313   6764   7243    369   -252   -453       N
ATOM   3856  CA  GLU B  29      -7.734  -8.711 -43.662  1.00 50.88           C
ANISOU 3856  CA  GLU B  29     7154   5865   6313    347   -253   -481       C
ATOM   3857  C   GLU B  29      -6.227  -8.581 -43.489  1.00 53.15           C
ANISOU 3857  C   GLU B  29     7384   6208   6604    460   -317   -554       C
ATOM   3858  O   GLU B  29      -5.739  -8.330 -42.384  1.00 65.71           O
ANISOU 3858  O   GLU B  29     8993   7799   8176    533   -358   -575       O
ATOM   3859  CB  GLU B  29      -8.395  -7.333 -43.678  1.00 52.63           C
ANISOU 3859  CB  GLU B  29     7270   6136   6591    254   -215   -449       C
ATOM   3860  CG  GLU B  29      -9.918  -7.428 -43.631  1.00 64.74           C
ANISOU 3860  CG  GLU B  29     8860   7622   8117    153   -159   -389       C
ATOM   3861  CD  GLU B  29     -10.611  -6.173 -44.107  1.00 71.67           C
ANISOU 3861  CD  GLU B  29     9624   8557   9051     61   -121   -364       C
ATOM   3862  OE1 GLU B  29     -11.319  -5.551 -43.281  1.00 80.07           O
ANISOU 3862  OE1 GLU B  29    10694   9612  10119     25   -106   -335       O
ATOM   3863  OE2 GLU B  29     -10.457  -5.817 -45.304  1.00 71.01           O
ANISOU 3863  OE2 GLU B  29     9452   8526   9004     28   -108   -373       O
ATOM   3864  N   LYS B  30      -5.499  -8.765 -44.582  1.00 52.75           N
ANISOU 3864  N   LYS B  30     7260   6208   6574    476   -326   -598       N
ATOM   3865  CA  LYS B  30      -4.083  -8.416 -44.674  1.00 56.62           C
ANISOU 3865  CA  LYS B  30     7650   6779   7083    558   -374   -681       C
ATOM   3866  C   LYS B  30      -4.000  -7.041 -45.340  1.00 61.05           C
ANISOU 3866  C   LYS B  30     8054   7426   7717    471   -336   -687       C
ATOM   3867  O   LYS B  30      -4.076  -6.934 -46.567  1.00 73.63           O
ANISOU 3867  O   LYS B  30     9586   9050   9340    408   -301   -686       O
ATOM   3868  CB  LYS B  30      -3.322  -9.484 -45.457  1.00 57.92           C
ANISOU 3868  CB  LYS B  30     7836   6947   7224    628   -404   -733       C
ATOM   3869  CG  LYS B  30      -1.859  -9.166 -45.737  1.00 64.95           C
ANISOU 3869  CG  LYS B  30     8607   7935   8137    703   -448   -833       C
ATOM   3870  CD  LYS B  30      -1.054  -8.989 -44.452  1.00 64.57           C
ANISOU 3870  CD  LYS B  30     8565   7906   8064    817   -512   -888       C
ATOM   3871  CE  LYS B  30       0.442  -8.834 -44.737  1.00 67.42           C
ANISOU 3871  CE  LYS B  30     8806   8369   8440    901   -559  -1007       C
ATOM   3872  NZ  LYS B  30       1.233  -8.401 -43.531  1.00 69.68           N
ANISOU 3872  NZ  LYS B  30     9064   8698   8714    999   -618  -1072       N
ATOM   3873  N   ILE B  31      -3.863  -5.984 -44.532  1.00 54.36           N
ANISOU 3873  N   ILE B  31     7150   6613   6893    466   -341   -692       N
ATOM   3874  CA  ILE B  31      -3.840  -4.619 -45.051  1.00 56.38           C
ANISOU 3874  CA  ILE B  31     7276   6937   7209    381   -300   -693       C
ATOM   3875  C   ILE B  31      -2.451  -4.284 -45.578  1.00 62.18           C
ANISOU 3875  C   ILE B  31     7895   7761   7969    417   -318   -788       C
ATOM   3876  O   ILE B  31      -1.442  -4.502 -44.901  1.00 66.35           O
ANISOU 3876  O   ILE B  31     8411   8321   8481    517   -372   -861       O
ATOM   3877  CB  ILE B  31      -4.279  -3.616 -43.975  1.00 48.70           C
ANISOU 3877  CB  ILE B  31     6294   5962   6250    356   -294   -662       C
ATOM   3878  CG1 ILE B  31      -5.502  -4.155 -43.227  1.00 51.01           C
ANISOU 3878  CG1 ILE B  31     6712   6165   6504    341   -285   -587       C
ATOM   3879  N   TYR B  32      -2.395  -3.742 -46.790  1.00 60.60           N
ANISOU 3879  N   TYR B  32     7612   7605   7807    337   -272   -793       N
ATOM   3880  CA  TYR B  32      -1.166  -3.204 -47.348  1.00 63.40           C
ANISOU 3880  CA  TYR B  32     7848   8050   8192    342   -269   -884       C
ATOM   3881  C   TYR B  32      -1.248  -1.685 -47.325  1.00 72.23           C
ANISOU 3881  C   TYR B  32     8883   9207   9352    255   -223   -877       C
ATOM   3882  O   TYR B  32      -2.297  -1.111 -47.632  1.00 73.77           O
ANISOU 3882  O   TYR B  32     9099   9369   9560    170   -177   -798       O
ATOM   3883  CB  TYR B  32      -0.929  -3.734 -48.757  1.00 61.07           C
ANISOU 3883  CB  TYR B  32     7529   7773   7902    315   -246   -904       C
ATOM   3884  CG  TYR B  32      -0.696  -5.226 -48.764  1.00 68.51           C
ANISOU 3884  CG  TYR B  32     8551   8680   8801    409   -295   -924       C
ATOM   3885  CD1 TYR B  32       0.593  -5.749 -48.727  1.00 66.75           C
ANISOU 3885  CD1 TYR B  32     8287   8511   8565    507   -345  -1028       C
ATOM   3886  CD2 TYR B  32      -1.770  -6.119 -48.786  1.00 70.23           C
ANISOU 3886  CD2 TYR B  32     8889   8810   8987    401   -292   -844       C
ATOM   3887  CE1 TYR B  32       0.812  -7.120 -48.723  1.00 65.04           C
ANISOU 3887  CE1 TYR B  32     8155   8257   8302    603   -394  -1046       C
ATOM   3888  CE2 TYR B  32      -1.565  -7.492 -48.778  1.00 64.44           C
ANISOU 3888  CE2 TYR B  32     8244   8033   8206    485   -333   -861       C
ATOM   3889  CZ  TYR B  32      -0.270  -7.988 -48.737  1.00 68.83           C
ANISOU 3889  CZ  TYR B  32     8766   8638   8747    591   -386   -959       C
ATOM   3890  OH  TYR B  32      -0.065  -9.354 -48.730  1.00 70.45           O
ANISOU 3890  OH  TYR B  32     9071   8796   8900    684   -430   -976       O
ATOM   3891  N   SER B  33      -0.161  -1.042 -46.911  1.00 77.05           N
ANISOU 3891  N   SER B  33     9405   9890   9981    282   -235   -964       N
ATOM   3892  CA  SER B  33      -0.122   0.398 -46.725  1.00 72.77           C
ANISOU 3892  CA  SER B  33     8793   9383   9473    208   -193   -967       C
ATOM   3893  C   SER B  33       0.756   1.026 -47.792  1.00 78.27           C
ANISOU 3893  C   SER B  33     9387  10152  10199    146   -146  -1041       C
ATOM   3894  O   SER B  33       1.763   0.452 -48.213  1.00 91.34           O
ANISOU 3894  O   SER B  33    10993  11862  11852    192   -165  -1130       O
ATOM   3895  CB  SER B  33       0.403   0.766 -45.335  1.00 73.83           C
ANISOU 3895  CB  SER B  33     8905   9541   9604    273   -236  -1013       C
ATOM   3896  OG  SER B  33      -0.194  -0.037 -44.330  1.00 70.94           O
ANISOU 3896  OG  SER B  33     8644   9109   9201    349   -287   -962       O
ATOM   3897  N   MET B  34       0.360   2.211 -48.227  1.00 78.12           N
ANISOU 3897  N   MET B  34     9342  10134  10205     42    -81  -1006       N
ATOM   3898  CA  MET B  34       1.053   2.938 -49.275  1.00 80.41           C
ANISOU 3898  CA  MET B  34     9556  10480  10517    -38    -20  -1064       C
ATOM   3899  C   MET B  34       1.654   4.197 -48.668  1.00 91.73           C
ANISOU 3899  C   MET B  34    10919  11961  11973    -77      7  -1120       C
ATOM   3900  O   MET B  34       0.974   4.920 -47.929  1.00 94.68           O
ANISOU 3900  O   MET B  34    11324  12300  12351    -98     12  -1060       O
ATOM   3901  CB  MET B  34       0.086   3.278 -50.409  1.00 81.08           C
ANISOU 3901  CB  MET B  34     9687  10517  10601   -129     37   -978       C
ATOM   3902  CG  MET B  34       0.722   3.861 -51.654  1.00 86.19           C
ANISOU 3902  CG  MET B  34    10281  11207  11261   -212    105  -1029       C
ATOM   3903  SD  MET B  34      -0.454   3.973 -53.026  1.00 83.59           S
ANISOU 3903  SD  MET B  34    10026  10817  10919   -290    155   -926       S
ATOM   3904  CE  MET B  34      -0.545   2.255 -53.511  1.00 80.42           C
ANISOU 3904  CE  MET B  34     9656  10402  10499   -217    105   -922       C
ATOM   3905  N   GLY B  35       2.932   4.442 -48.956  1.00 95.34           N
ANISOU 3905  N   GLY B  35    11279  12502  12444    -87     26  -1241       N
ATOM   3906  CA  GLY B  35       3.578   5.639 -48.460  1.00 97.05           C
ANISOU 3906  CA  GLY B  35    11424  12770  12682   -136     62  -1309       C
ATOM   3907  C   GLY B  35       3.063   6.891 -49.141  1.00 96.78           C
ANISOU 3907  C   GLY B  35    11410  12703  12657   -264    150  -1255       C
ATOM   3908  O   GLY B  35       2.540   6.862 -50.256  1.00 97.72           O
ANISOU 3908  O   GLY B  35    11575  12786  12769   -321    191  -1199       O
ATOM   3909  N   ASP B  36       3.202   8.019 -48.444  1.00 91.08           N
ANISOU 3909  N   ASP B  36    10662  11995  11949   -306    177  -1273       N
ATOM   3910  CA  ASP B  36       2.797   9.297 -49.020  1.00 89.83           C
ANISOU 3910  CA  ASP B  36    10534  11803  11794   -425    262  -1230       C
ATOM   3911  C   ASP B  36       3.785   9.713 -50.097  1.00 95.96           C
ANISOU 3911  C   ASP B  36    11252  12633  12575   -512    339  -1326       C
ATOM   3912  O   ASP B  36       3.788   9.148 -51.196  1.00 92.17           O
ANISOU 3912  O   ASP B  36    10788  12149  12085   -528    357  -1320       O
ATOM   3913  CB  ASP B  36       2.703  10.381 -47.947  1.00 85.78           C
ANISOU 3913  CB  ASP B  36    10013  11286  11292   -445    271  -1227       C
ATOM   3914  CG  ASP B  36       2.176   9.855 -46.636  1.00 84.92           C
ANISOU 3914  CG  ASP B  36     9929  11155  11181   -344    187  -1181       C
ATOM   3915  OD1 ASP B  36       2.903   9.953 -45.617  1.00 81.74           O
ANISOU 3915  OD1 ASP B  36     9463  10805  10788   -297    154  -1259       O
ATOM   3916  OD2 ASP B  36       1.032   9.347 -46.627  1.00 89.79           O
ANISOU 3916  OD2 ASP B  36    10629  11703  11783   -313    156  -1072       O
ATOM   3917  N   ALA B  37       4.624  10.708 -49.783  1.00108.61           N
ANISOU 3917  N   ALA B  37    12789  14287  14191   -574    390  -1418       N
ATOM   3918  CA  ALA B  37       5.734  11.155 -50.620  1.00106.84           C
ANISOU 3918  CA  ALA B  37    12496  14127  13971   -665    471  -1536       C
ATOM   3919  C   ALA B  37       5.250  11.554 -52.009  1.00 99.32           C
ANISOU 3919  C   ALA B  37    11622  13116  12997   -763    551  -1473       C
ATOM   3920  O   ALA B  37       4.036  11.607 -52.263  1.00 95.02           O
ANISOU 3920  O   ALA B  37    11182  12485  12436   -759    541  -1340       O
ATOM   3921  CB  ALA B  37       6.802  10.055 -50.724  1.00103.55           C
ANISOU 3921  CB  ALA B  37    11980  13802  13562   -594    426  -1658       C
ATOM   3922  N   PRO B  38       6.161  11.906 -52.907  1.00 94.32           N
ANISOU 3922  N   PRO B  38    10946  12529  12361   -855    633  -1571       N
ATOM   3923  CA  PRO B  38       5.848  11.822 -54.338  1.00 97.32           C
ANISOU 3923  CA  PRO B  38    11395  12867  12717   -918    689  -1525       C
ATOM   3924  C   PRO B  38       5.915  10.386 -54.830  1.00 93.42           C
ANISOU 3924  C   PRO B  38    10876  12396  12224   -834    626  -1529       C
ATOM   3925  O   PRO B  38       5.230  10.012 -55.787  1.00 92.03           O
ANISOU 3925  O   PRO B  38    10775  12166  12027   -843    634  -1447       O
ATOM   3926  CB  PRO B  38       6.928  12.694 -54.990  1.00102.53           C
ANISOU 3926  CB  PRO B  38    12009  13574  13372  -1048    802  -1646       C
ATOM   3927  CG  PRO B  38       7.419  13.581 -53.887  1.00 96.66           C
ANISOU 3927  CG  PRO B  38    11211  12868  12647  -1074    819  -1713       C
ATOM   3928  CD  PRO B  38       7.328  12.764 -52.648  1.00 92.63           C
ANISOU 3928  CD  PRO B  38    10643  12391  12161   -934    700  -1711       C
ATOM   3929  N   ASP B  39       6.760   9.578 -54.188  1.00 94.32           N
ANISOU 3929  N   ASP B  39    10886  12592  12357   -750    564  -1630       N
ATOM   3930  CA  ASP B  39       6.817   8.138 -54.437  1.00 89.53           C
ANISOU 3930  CA  ASP B  39    10263  12005  11748   -650    489  -1635       C
ATOM   3931  C   ASP B  39       5.815   7.486 -53.502  1.00 95.23           C
ANISOU 3931  C   ASP B  39    11047  12669  12468   -538    393  -1526       C
ATOM   3932  O   ASP B  39       6.069   7.332 -52.304  1.00110.53           O
ANISOU 3932  O   ASP B  39    12945  14636  14416   -461    332  -1561       O
ATOM   3933  CB  ASP B  39       8.219   7.578 -54.213  1.00 84.42           C
ANISOU 3933  CB  ASP B  39     9484  11475  11116   -603    465  -1803       C
ATOM   3934  CG  ASP B  39       9.313   8.528 -54.661  1.00 88.51           C
ANISOU 3934  CG  ASP B  39     9919  12067  11643   -723    566  -1938       C
ATOM   3935  OD1 ASP B  39      10.296   8.692 -53.909  1.00 89.88           O
ANISOU 3935  OD1 ASP B  39     9982  12333  11834   -702    553  -2072       O
ATOM   3936  OD2 ASP B  39       9.193   9.107 -55.764  1.00 90.36           O
ANISOU 3936  OD2 ASP B  39    10201  12268  11863   -840    660  -1916       O
ATOM   3937  N   TYR B  40       4.660   7.126 -54.037  1.00 87.84           N
ANISOU 3937  N   TYR B  40    10210  11649  11514   -534    383  -1397       N
ATOM   3938  CA  TYR B  40       3.676   6.423 -53.233  1.00 77.26           C
ANISOU 3938  CA  TYR B  40     8932  10253  10169   -439    300  -1299       C
ATOM   3939  C   TYR B  40       4.159   4.996 -53.023  1.00 79.85           C
ANISOU 3939  C   TYR B  40     9229  10617  10493   -327    223  -1350       C
ATOM   3940  O   TYR B  40       3.833   4.095 -53.804  1.00 85.93           O
ANISOU 3940  O   TYR B  40    10036  11362  11250   -305    209  -1315       O
ATOM   3941  CB  TYR B  40       2.313   6.468 -53.914  1.00 70.40           C
ANISOU 3941  CB  TYR B  40     8170   9295   9281   -472    316  -1163       C
ATOM   3942  CG  TYR B  40       1.745   7.866 -54.068  1.00 66.07           C
ANISOU 3942  CG  TYR B  40     7671   8704   8729   -565    382  -1107       C
ATOM   3943  CD1 TYR B  40       0.809   8.348 -53.171  1.00 68.36           C
ANISOU 3943  CD1 TYR B  40     8011   8945   9018   -547    357  -1024       C
ATOM   3944  CD2 TYR B  40       2.139   8.698 -55.116  1.00 64.57           C
ANISOU 3944  CD2 TYR B  40     7485   8520   8529   -668    471  -1137       C
ATOM   3945  CE1 TYR B  40       0.276   9.614 -53.302  1.00 68.99           C
ANISOU 3945  CE1 TYR B  40     8141   8982   9089   -621    412   -974       C
ATOM   3946  CE2 TYR B  40       1.609   9.977 -55.257  1.00 62.42           C
ANISOU 3946  CE2 TYR B  40     7275   8198   8242   -746    530  -1084       C
ATOM   3947  CZ  TYR B  40       0.673  10.424 -54.343  1.00 66.04           C
ANISOU 3947  CZ  TYR B  40     7781   8609   8702   -717    497  -1002       C
ATOM   3948  OH  TYR B  40       0.111  11.680 -54.444  1.00 66.59           O
ANISOU 3948  OH  TYR B  40     7920   8628   8755   -782    548   -949       O
ATOM   3949  N   ASP B  41       4.959   4.799 -51.977  1.00 82.72           N
ANISOU 3949  N   ASP B  41     9526  11039  10866   -251    172  -1438       N
ATOM   3950  CA  ASP B  41       5.686   3.558 -51.730  1.00 82.37           C
ANISOU 3950  CA  ASP B  41     9441  11042  10812   -136     98  -1517       C
ATOM   3951  C   ASP B  41       4.774   2.333 -51.725  1.00 83.94           C
ANISOU 3951  C   ASP B  41     9739  11167  10987    -56     36  -1419       C
ATOM   3952  O   ASP B  41       3.941   2.166 -50.825  1.00 80.79           O
ANISOU 3952  O   ASP B  41     9412  10707  10578     -9     -7  -1335       O
ATOM   3953  CB  ASP B  41       6.436   3.674 -50.402  1.00 83.42           C
ANISOU 3953  CB  ASP B  41     9510  11235  10952    -57     44  -1607       C
ATOM   3954  CG  ASP B  41       7.326   2.485 -50.129  1.00 82.04           C
ANISOU 3954  CG  ASP B  41     9290  11120  10762     73    -36  -1708       C
ATOM   3955  OD1 ASP B  41       7.880   1.925 -51.104  1.00 78.80           O
ANISOU 3955  OD1 ASP B  41     8842  10748  10349     70    -24  -1769       O
ATOM   3956  OD2 ASP B  41       7.478   2.127 -48.938  1.00 77.76           O
ANISOU 3956  OD2 ASP B  41     8754  10585  10207    182   -113  -1730       O
ATOM   3957  N   ARG B  42       4.921   1.477 -52.739  1.00 81.31           N
ANISOU 3957  N   ARG B  42     9413  10838  10644    -47     37  -1431       N
ATOM   3958  CA  ARG B  42       4.181   0.228 -52.848  1.00 74.49           C
ANISOU 3958  CA  ARG B  42     8640   9909   9756     24    -16  -1354       C
ATOM   3959  C   ARG B  42       5.013  -0.976 -52.415  1.00 77.21           C
ANISOU 3959  C   ARG B  42     8965  10292  10080    157    -96  -1441       C
ATOM   3960  O   ARG B  42       4.715  -2.105 -52.815  1.00 84.07           O
ANISOU 3960  O   ARG B  42     9896  11122  10926    209   -129  -1409       O
ATOM   3961  CB  ARG B  42       3.687   0.038 -54.282  1.00 77.61           C
ANISOU 3961  CB  ARG B  42     9067  10273  10147    -49     36  -1302       C
ATOM   3962  CG  ARG B  42       2.529   0.935 -54.661  1.00 77.82           C
ANISOU 3962  CG  ARG B  42     9154  10237  10178   -148     93  -1190       C
ATOM   3963  CD  ARG B  42       2.436   1.128 -56.163  1.00 80.10           C
ANISOU 3963  CD  ARG B  42     9445  10523  10464   -235    158  -1178       C
ATOM   3964  NE  ARG B  42       1.068   1.406 -56.587  1.00 79.69           N
ANISOU 3964  NE  ARG B  42     9481  10396  10402   -285    182  -1054       N
ATOM   3965  CZ  ARG B  42       0.226   0.477 -57.028  1.00 78.03           C
ANISOU 3965  CZ  ARG B  42     9336  10136  10175   -260    157   -986       C
ATOM   3966  NH1 ARG B  42       0.613  -0.795 -57.113  1.00 75.53           N
ANISOU 3966  NH1 ARG B  42     9019   9830   9849   -186    111  -1022       N
ATOM   3967  NH2 ARG B  42      -1.004   0.820 -57.394  1.00 74.85           N
ANISOU 3967  NH2 ARG B  42     9001   9677   9763   -305    178   -887       N
ATOM   3968  N   SER B  43       6.053  -0.753 -51.608  1.00 78.95           N
ANISOU 3968  N   SER B  43     9103  10589  10307    215   -129  -1554       N
ATOM   3969  CA  SER B  43       6.957  -1.823 -51.199  1.00 73.06           C
ANISOU 3969  CA  SER B  43     8332   9891   9537    354   -211  -1654       C
ATOM   3970  C   SER B  43       6.318  -2.797 -50.218  1.00 70.37           C
ANISOU 3970  C   SER B  43     8110   9470   9157    472   -292  -1583       C
ATOM   3971  O   SER B  43       6.753  -3.950 -50.138  1.00 72.24           O
ANISOU 3971  O   SER B  43     8376   9711   9362    588   -359  -1630       O
ATOM   3972  CB  SER B  43       8.211  -1.224 -50.572  1.00 63.24           C
ANISOU 3972  CB  SER B  43     6963   8758   8309    384   -224  -1803       C
ATOM   3973  OG  SER B  43       7.857  -0.409 -49.461  1.00 53.04           O
ANISOU 3973  OG  SER B  43     5683   7447   7025    375   -228  -1767       O
ATOM   3974  N   GLN B  44       5.309  -2.361 -49.463  1.00 66.65           N
ANISOU 3974  N   GLN B  44     7714   8925   8684    446   -287  -1476       N
ATOM   3975  CA  GLN B  44       4.644  -3.272 -48.536  1.00 68.38           C
ANISOU 3975  CA  GLN B  44     8058   9062   8862    544   -354  -1406       C
ATOM   3976  C   GLN B  44       4.027  -4.455 -49.271  1.00 73.99           C
ANISOU 3976  C   GLN B  44     8867   9702   9544    560   -361  -1342       C
ATOM   3977  O   GLN B  44       4.024  -5.581 -48.766  1.00 78.79           O
ANISOU 3977  O   GLN B  44     9564  10266  10107    671   -426  -1340       O
ATOM   3978  CB  GLN B  44       3.580  -2.519 -47.747  1.00 63.08           C
ANISOU 3978  CB  GLN B  44     7444   8326   8197    489   -332  -1301       C
ATOM   3979  CG  GLN B  44       3.486  -2.920 -46.306  1.00 70.93           C
ANISOU 3979  CG  GLN B  44     8510   9285   9157    597   -402  -1292       C
ATOM   3980  CD  GLN B  44       2.837  -1.848 -45.472  1.00 76.05           C
ANISOU 3980  CD  GLN B  44     9163   9910   9823    539   -377  -1232       C
ATOM   3981  OE1 GLN B  44       3.325  -0.719 -45.414  1.00 76.19           O
ANISOU 3981  OE1 GLN B  44     9079   9992   9876    483   -344  -1282       O
ATOM   3982  NE2 GLN B  44       1.721  -2.187 -44.829  1.00 75.42           N
ANISOU 3982  NE2 GLN B  44     9202   9737   9718    545   -387  -1127       N
ATOM   3983  N   TRP B  45       3.490  -4.215 -50.459  1.00 71.25           N
ANISOU 3983  N   TRP B  45     8512   9340   9219    450   -294  -1289       N
ATOM   3984  CA  TRP B  45       2.915  -5.268 -51.275  1.00 66.14           C
ANISOU 3984  CA  TRP B  45     7945   8634   8549    452   -293  -1234       C
ATOM   3985  C   TRP B  45       3.942  -5.853 -52.233  1.00 66.52           C
ANISOU 3985  C   TRP B  45     7930   8748   8598    485   -301  -1333       C
ATOM   3986  O   TRP B  45       4.054  -7.080 -52.358  1.00 64.52           O
ANISOU 3986  O   TRP B  45     7739   8466   8309    570   -347  -1344       O
ATOM   3987  CB  TRP B  45       1.714  -4.708 -52.039  1.00 64.55           C
ANISOU 3987  CB  TRP B  45     7774   8383   8368    324   -222  -1125       C
ATOM   3988  CG  TRP B  45       1.332  -5.464 -53.279  1.00 67.30           C
ANISOU 3988  CG  TRP B  45     8158   8705   8709    292   -199  -1094       C
ATOM   3989  CD1 TRP B  45       1.386  -5.006 -54.556  1.00 68.80           C
ANISOU 3989  CD1 TRP B  45     8292   8926   8921    202   -139  -1099       C
ATOM   3990  CD2 TRP B  45       0.807  -6.795 -53.351  1.00 65.99           C
ANISOU 3990  CD2 TRP B  45     8098   8471   8505    346   -231  -1053       C
ATOM   3991  NE1 TRP B  45       0.937  -5.966 -55.421  1.00 73.75           N
ANISOU 3991  NE1 TRP B  45     8975   9515   9531    201   -137  -1064       N
ATOM   3992  CE2 TRP B  45       0.573  -7.075 -54.705  1.00 73.21           C
ANISOU 3992  CE2 TRP B  45     9005   9385   9426    286   -191  -1036       C
ATOM   3993  CE3 TRP B  45       0.511  -7.774 -52.400  1.00 68.20           C
ANISOU 3993  CE3 TRP B  45     8487   8685   8742    437   -286  -1029       C
ATOM   3994  CZ2 TRP B  45       0.064  -8.297 -55.138  1.00 73.57           C
ANISOU 3994  CZ2 TRP B  45     9139   9372   9441    312   -205  -1000       C
ATOM   3995  CZ3 TRP B  45       0.007  -8.984 -52.828  1.00 70.70           C
ANISOU 3995  CZ3 TRP B  45     8902   8938   9025    460   -296   -992       C
ATOM   3996  CH2 TRP B  45      -0.213  -9.235 -54.186  1.00 70.22           C
ANISOU 3996  CH2 TRP B  45     8822   8883   8976    396   -256   -979       C
ATOM   3997  N   LEU B  46       4.717  -4.985 -52.883  1.00 65.40           N
ANISOU 3997  N   LEU B  46     7664   8692   8491    417   -253  -1409       N
ATOM   3998  CA  LEU B  46       5.721  -5.431 -53.841  1.00 70.04           C
ANISOU 3998  CA  LEU B  46     8177   9353   9083    433   -251  -1512       C
ATOM   3999  C   LEU B  46       6.693  -6.434 -53.227  1.00 75.73           C
ANISOU 3999  C   LEU B  46     8889  10113   9771    590   -340  -1617       C
ATOM   4000  O   LEU B  46       7.247  -7.281 -53.941  1.00 76.42           O
ANISOU 4000  O   LEU B  46     8963  10228   9845    638   -360  -1677       O
ATOM   4001  CB  LEU B  46       6.468  -4.216 -54.385  1.00 70.79           C
ANISOU 4001  CB  LEU B  46     8142   9538   9218    333   -182  -1592       C
ATOM   4002  CG  LEU B  46       5.921  -3.699 -55.708  1.00 73.17           C
ANISOU 4002  CG  LEU B  46     8446   9819   9538    197    -94  -1532       C
ATOM   4003  CD1 LEU B  46       6.825  -2.619 -56.283  1.00 72.04           C
ANISOU 4003  CD1 LEU B  46     8185   9765   9424    102    -22  -1628       C
ATOM   4004  CD2 LEU B  46       5.762  -4.875 -56.676  1.00 69.36           C
ANISOU 4004  CD2 LEU B  46     8010   9309   9035    225   -107  -1515       C
ATOM   4005  N   SER B  47       6.906  -6.359 -51.911  1.00 77.48           N
ANISOU 4005  N   SER B  47     9124  10337   9976    678   -398  -1641       N
ATOM   4006  CA  SER B  47       7.785  -7.304 -51.230  1.00 80.02           C
ANISOU 4006  CA  SER B  47     9455  10691  10258    845   -493  -1739       C
ATOM   4007  C   SER B  47       7.190  -8.710 -51.211  1.00 86.08           C
ANISOU 4007  C   SER B  47    10376  11358  10973    932   -543  -1669       C
ATOM   4008  O   SER B  47       7.878  -9.690 -51.519  1.00 91.75           O
ANISOU 4008  O   SER B  47    11099  12100  11660   1034   -594  -1745       O
ATOM   4009  CB  SER B  47       8.054  -6.803 -49.813  1.00 80.97           C
ANISOU 4009  CB  SER B  47     9564  10831  10371    913   -540  -1772       C
ATOM   4010  OG  SER B  47       8.203  -7.871 -48.897  1.00 88.94           O
ANISOU 4010  OG  SER B  47    10673  11799  11320   1077   -636  -1787       O
ATOM   4011  N   GLU B  48       5.909  -8.826 -50.852  1.00 84.72           N
ANISOU 4011  N   GLU B  48    10331  11073  10786    892   -526  -1530       N
ATOM   4012  CA  GLU B  48       5.199 -10.095 -50.719  1.00 77.31           C
ANISOU 4012  CA  GLU B  48     9554  10025   9793    955   -560  -1455       C
ATOM   4013  C   GLU B  48       4.584 -10.595 -52.025  1.00 85.12           C
ANISOU 4013  C   GLU B  48    10576  10975  10790    874   -509  -1395       C
ATOM   4014  O   GLU B  48       4.126 -11.741 -52.062  1.00 90.38           O
ANISOU 4014  O   GLU B  48    11371  11560  11411    925   -534  -1350       O
ATOM   4015  CB  GLU B  48       4.077  -9.947 -49.680  1.00 67.69           C
ANISOU 4015  CB  GLU B  48     8454   8709   8555    937   -557  -1342       C
ATOM   4016  CG  GLU B  48       4.130 -10.864 -48.474  1.00 75.17           C
ANISOU 4016  CG  GLU B  48     9535   9591   9433   1082   -637  -1344       C
ATOM   4017  CD  GLU B  48       2.951 -10.626 -47.517  1.00 80.23           C
ANISOU 4017  CD  GLU B  48    10288  10137  10059   1039   -618  -1231       C
ATOM   4018  OE1 GLU B  48       2.566 -11.543 -46.735  1.00 74.82           O
ANISOU 4018  OE1 GLU B  48     9761   9358   9309   1121   -659  -1193       O
ATOM   4019  OE2 GLU B  48       2.404  -9.507 -47.556  1.00 79.37           O
ANISOU 4019  OE2 GLU B  48    10112  10045  10000    922   -560  -1182       O
ATOM   4020  N   LYS B  49       4.589  -9.781 -53.094  1.00 83.76           N
ANISOU 4020  N   LYS B  49    10298  10857  10669    750   -437  -1397       N
ATOM   4021  CA  LYS B  49       3.647  -9.961 -54.207  1.00 74.60           C
ANISOU 4021  CA  LYS B  49     9179   9645   9520    645   -377  -1308       C
ATOM   4022  C   LYS B  49       3.817 -11.303 -54.911  1.00 72.36           C
ANISOU 4022  C   LYS B  49     8956   9336   9203    707   -404  -1327       C
ATOM   4023  O   LYS B  49       2.830 -11.943 -55.293  1.00 68.28           O
ANISOU 4023  O   LYS B  49     8541   8735   8667    671   -384  -1239       O
ATOM   4024  CB  LYS B  49       3.803  -8.809 -55.204  1.00 79.21           C
ANISOU 4024  CB  LYS B  49     9642  10298  10156    517   -301  -1323       C
ATOM   4025  CG  LYS B  49       3.357  -9.107 -56.641  1.00 73.08           C
ANISOU 4025  CG  LYS B  49     8873   9505   9388    437   -249  -1284       C
ATOM   4026  CD  LYS B  49       2.784  -7.863 -57.326  1.00 63.33           C
ANISOU 4026  CD  LYS B  49     7590   8281   8191    294   -168  -1230       C
ATOM   4027  CE  LYS B  49       3.173  -7.785 -58.803  1.00 64.54           C
ANISOU 4027  CE  LYS B  49     7681   8480   8360    226   -117  -1267       C
ATOM   4028  NZ  LYS B  49       2.521  -6.642 -59.515  1.00 58.52           N
ANISOU 4028  NZ  LYS B  49     6900   7712   7622     95    -39  -1206       N
ATOM   4029  N   PHE B  50       5.053 -11.751 -55.102  1.00 75.28           N
ANISOU 4029  N   PHE B  50     9262   9777   9562    800   -449  -1447       N
ATOM   4030  CA  PHE B  50       5.284 -13.008 -55.794  1.00 75.63           C
ANISOU 4030  CA  PHE B  50     9361   9802   9575    864   -477  -1472       C
ATOM   4031  C   PHE B  50       5.556 -14.160 -54.835  1.00 74.71           C
ANISOU 4031  C   PHE B  50     9362   9631   9391   1028   -566  -1498       C
ATOM   4032  O   PHE B  50       6.105 -15.187 -55.248  1.00 74.11           O
ANISOU 4032  O   PHE B  50     9318   9559   9283   1118   -608  -1555       O
ATOM   4033  CB  PHE B  50       6.422 -12.849 -56.801  1.00 72.99           C
ANISOU 4033  CB  PHE B  50     8886   9580   9268    858   -465  -1590       C
ATOM   4034  CG  PHE B  50       6.097 -11.909 -57.924  1.00 70.34           C
ANISOU 4034  CG  PHE B  50     8466   9277   8982    698   -372  -1558       C
ATOM   4035  CD1 PHE B  50       5.443 -12.363 -59.055  1.00 68.60           C
ANISOU 4035  CD1 PHE B  50     8290   9013   8763    629   -330  -1494       C
ATOM   4036  CD2 PHE B  50       6.419 -10.564 -57.835  1.00 78.58           C
ANISOU 4036  CD2 PHE B  50     9399  10390  10069    616   -326  -1589       C
ATOM   4037  CE1 PHE B  50       5.123 -11.497 -60.091  1.00 67.51           C
ANISOU 4037  CE1 PHE B  50     8088   8899   8662    490   -248  -1463       C
ATOM   4038  CE2 PHE B  50       6.113  -9.690 -58.869  1.00 82.26           C
ANISOU 4038  CE2 PHE B  50     9808  10875  10571    473   -239  -1557       C
ATOM   4039  CZ  PHE B  50       5.463 -10.159 -60.001  1.00 73.62           C
ANISOU 4039  CZ  PHE B  50     8762   9736   9473    414   -202  -1493       C
ATOM   4040  N   LYS B  51       5.141 -14.026 -53.573  1.00 75.31           N
ANISOU 4040  N   LYS B  51     9519   9653   9444   1069   -595  -1453       N
ATOM   4041  CA  LYS B  51       5.389 -15.033 -52.547  1.00 80.35           C
ANISOU 4041  CA  LYS B  51    10287  10233  10010   1228   -680  -1475       C
ATOM   4042  C   LYS B  51       4.101 -15.554 -51.916  1.00 81.96           C
ANISOU 4042  C   LYS B  51    10674  10295  10171   1206   -667  -1348       C
ATOM   4043  O   LYS B  51       4.135 -16.082 -50.796  1.00 85.24           O
ANISOU 4043  O   LYS B  51    11209  10651  10527   1317   -725  -1346       O
ATOM   4044  CB  LYS B  51       6.309 -14.466 -51.461  1.00 77.32           C
ANISOU 4044  CB  LYS B  51     9834   9922   9623   1325   -739  -1566       C
ATOM   4045  CG  LYS B  51       7.778 -14.458 -51.835  1.00 71.85           C
ANISOU 4045  CG  LYS B  51     8999   9360   8941   1411   -784  -1726       C
ATOM   4046  CD  LYS B  51       8.482 -13.227 -51.302  1.00 68.20           C
ANISOU 4046  CD  LYS B  51     8384   9008   8522   1395   -782  -1807       C
ATOM   4047  CE  LYS B  51       9.944 -13.235 -51.717  1.00 73.90           C
ANISOU 4047  CE  LYS B  51     8954   9870   9255   1470   -820  -1981       C
ATOM   4048  NZ  LYS B  51      10.482 -11.869 -51.943  1.00 81.43           N
ANISOU 4048  NZ  LYS B  51     9721  10941  10276   1363   -762  -2051       N
ATOM   4049  N   LEU B  52       2.964 -15.426 -52.606  1.00 73.06           N
ANISOU 4049  N   LEU B  52     9573   9116   9069   1066   -591  -1246       N
ATOM   4050  CA  LEU B  52       1.678 -15.805 -52.037  1.00 63.07           C
ANISOU 4050  CA  LEU B  52     8464   7730   7771   1023   -565  -1134       C
ATOM   4051  C   LEU B  52       1.012 -16.970 -52.758  1.00 66.88           C
ANISOU 4051  C   LEU B  52     9066   8126   8217   1001   -543  -1085       C
ATOM   4052  O   LEU B  52      -0.135 -17.306 -52.438  1.00 67.41           O
ANISOU 4052  O   LEU B  52     9257   8096   8260    942   -507   -997       O
ATOM   4053  CB  LEU B  52       0.750 -14.596 -52.010  1.00 52.88           C
ANISOU 4053  CB  LEU B  52     7110   6447   6534    878   -496  -1058       C
ATOM   4054  CG  LEU B  52       1.306 -13.600 -50.990  1.00 59.21           C
ANISOU 4054  CG  LEU B  52     7837   7307   7355    915   -525  -1097       C
ATOM   4055  CD1 LEU B  52       0.587 -12.255 -51.006  1.00 61.23           C
ANISOU 4055  CD1 LEU B  52     8009   7587   7668    780   -461  -1038       C
ATOM   4056  CD2 LEU B  52       1.282 -14.222 -49.605  1.00 52.30           C
ANISOU 4056  CD2 LEU B  52     7103   6356   6412   1029   -584  -1090       C
ATOM   4057  N   GLY B  53       1.698 -17.609 -53.700  1.00 66.35           N
ANISOU 4057  N   GLY B  53     8969   8094   8147   1044   -560  -1146       N
ATOM   4058  CA  GLY B  53       1.077 -18.676 -54.458  1.00 74.16           C
ANISOU 4058  CA  GLY B  53    10064   9007   9106   1015   -535  -1103       C
ATOM   4059  C   GLY B  53       0.019 -18.230 -55.440  1.00 73.04           C
ANISOU 4059  C   GLY B  53     9876   8863   9013    850   -449  -1028       C
ATOM   4060  O   GLY B  53      -0.690 -19.079 -55.989  1.00 77.63           O
ANISOU 4060  O   GLY B  53    10551   9374   9570    810   -420   -984       O
ATOM   4061  N   LEU B  54      -0.099 -16.925 -55.682  1.00 63.98           N
ANISOU 4061  N   LEU B  54     8590   7790   7930    756   -409  -1016       N
ATOM   4062  CA  LEU B  54      -1.108 -16.381 -56.576  1.00 59.69           C
ANISOU 4062  CA  LEU B  54     8002   7249   7429    609   -334   -948       C
ATOM   4063  C   LEU B  54      -0.683 -16.551 -58.027  1.00 58.85           C
ANISOU 4063  C   LEU B  54     7815   7199   7348    578   -314   -986       C
ATOM   4064  O   LEU B  54       0.498 -16.462 -58.366  1.00 64.33           O
ANISOU 4064  O   LEU B  54     8420   7969   8054    637   -343  -1073       O
ATOM   4065  CB  LEU B  54      -1.353 -14.900 -56.269  1.00 61.21           C
ANISOU 4065  CB  LEU B  54     8091   7494   7672    531   -303   -924       C
ATOM   4066  CG  LEU B  54      -1.588 -14.498 -54.810  1.00 53.56           C
ANISOU 4066  CG  LEU B  54     7170   6491   6688    562   -325   -899       C
ATOM   4067  CD1 LEU B  54      -1.564 -12.971 -54.612  1.00 48.91           C
ANISOU 4067  CD1 LEU B  54     6460   5971   6154    496   -299   -895       C
ATOM   4068  CD2 LEU B  54      -2.875 -15.102 -54.286  1.00 50.13           C
ANISOU 4068  CD2 LEU B  54     6881   5951   6217    525   -302   -816       C
ATOM   4069  N   ASP B  55      -1.672 -16.798 -58.891  1.00 68.23           N
ANISOU 4069  N   ASP B  55     9033   8351   8542    483   -262   -926       N
ATOM   4070  CA  ASP B  55      -1.397 -17.100 -60.295  1.00 62.71           C
ANISOU 4070  CA  ASP B  55     8278   7690   7858    452   -241   -954       C
ATOM   4071  C   ASP B  55      -1.054 -15.845 -61.097  1.00 69.27           C
ANISOU 4071  C   ASP B  55     8957   8617   8746    376   -203   -974       C
ATOM   4072  O   ASP B  55      -0.148 -15.862 -61.940  1.00 68.20           O
ANISOU 4072  O   ASP B  55     8741   8547   8624    392   -205  -1041       O
ATOM   4073  CB  ASP B  55      -2.602 -17.807 -60.910  1.00 67.63           C
ANISOU 4073  CB  ASP B  55     8989   8243   8464    379   -200   -886       C
ATOM   4074  CG  ASP B  55      -2.694 -19.266 -60.506  1.00 72.86           C
ANISOU 4074  CG  ASP B  55     9805   8815   9064    454   -230   -887       C
ATOM   4075  OD1 ASP B  55      -1.654 -19.960 -60.586  1.00 69.86           O
ANISOU 4075  OD1 ASP B  55     9438   8448   8660    559   -279   -955       O
ATOM   4076  OD2 ASP B  55      -3.810 -19.722 -60.138  1.00 71.06           O
ANISOU 4076  OD2 ASP B  55     9688   8504   8809    406   -202   -825       O
ATOM   4077  N   PHE B  56      -1.795 -14.762 -60.878  1.00 78.92           N
ANISOU 4077  N   PHE B  56    10145   9844   9996    291   -165   -918       N
ATOM   4078  CA  PHE B  56      -1.495 -13.448 -61.447  1.00 75.22           C
ANISOU 4078  CA  PHE B  56     9554   9454   9574    221   -127   -932       C
ATOM   4079  C   PHE B  56      -1.537 -12.487 -60.271  1.00 65.59           C
ANISOU 4079  C   PHE B  56     8313   8240   8367    222   -135   -919       C
ATOM   4080  O   PHE B  56      -2.577 -11.869 -60.012  1.00 64.81           O
ANISOU 4080  O   PHE B  56     8235   8111   8277    154   -105   -847       O
ATOM   4081  CB  PHE B  56      -2.491 -13.049 -62.542  1.00 76.17           C
ANISOU 4081  CB  PHE B  56     9663   9569   9711    110    -69   -871       C
ATOM   4082  CG  PHE B  56      -2.678 -14.091 -63.617  1.00 65.73           C
ANISOU 4082  CG  PHE B  56     8377   8227   8371    104    -61   -873       C
ATOM   4083  CD1 PHE B  56      -3.727 -15.002 -63.546  1.00 63.17           C
ANISOU 4083  CD1 PHE B  56     8156   7828   8018     93    -58   -819       C
ATOM   4084  CD2 PHE B  56      -1.805 -14.164 -64.691  1.00 54.54           C
ANISOU 4084  CD2 PHE B  56     6890   6867   6963    106    -52   -933       C
ATOM   4085  CE1 PHE B  56      -3.893 -15.975 -64.527  1.00 60.24           C
ANISOU 4085  CE1 PHE B  56     7820   7438   7630     86    -50   -824       C
ATOM   4086  CE2 PHE B  56      -1.965 -15.131 -65.674  1.00 45.60           C
ANISOU 4086  CE2 PHE B  56     5793   5718   5816    102    -45   -935       C
ATOM   4087  CZ  PHE B  56      -3.005 -16.036 -65.596  1.00 45.68           C
ANISOU 4087  CZ  PHE B  56     5906   5652   5798     94    -46   -880       C
ATOM   4088  N   PRO B  57      -0.435 -12.374 -59.519  1.00 67.16           N
ANISOU 4088  N   PRO B  57     8473   8481   8565    305   -178   -992       N
ATOM   4089  CA  PRO B  57      -0.446 -11.611 -58.259  1.00 65.53           C
ANISOU 4089  CA  PRO B  57     8259   8274   8365    322   -194   -983       C
ATOM   4090  C   PRO B  57      -1.018 -10.217 -58.422  1.00 62.19           C
ANISOU 4090  C   PRO B  57     7776   7874   7980    215   -139   -936       C
ATOM   4091  O   PRO B  57      -0.629  -9.458 -59.315  1.00 68.42           O
ANISOU 4091  O   PRO B  57     8477   8722   8797    153    -99   -963       O
ATOM   4092  CB  PRO B  57       1.035 -11.568 -57.866  1.00 61.09           C
ANISOU 4092  CB  PRO B  57     7622   7784   7804    414   -240  -1094       C
ATOM   4093  CG  PRO B  57       1.571 -12.850 -58.391  1.00 63.54           C
ANISOU 4093  CG  PRO B  57     7969   8088   8084    492   -275  -1144       C
ATOM   4094  CD  PRO B  57       0.842 -13.088 -59.705  1.00 66.14           C
ANISOU 4094  CD  PRO B  57     8312   8396   8422    401   -222  -1091       C
ATOM   4095  N   ASN B  58      -1.951  -9.881 -57.544  1.00 56.64           N
ANISOU 4095  N   ASN B  58     7127   7121   7272    193   -137   -867       N
ATOM   4096  CA  ASN B  58      -2.726  -8.660 -57.701  1.00 62.75           C
ANISOU 4096  CA  ASN B  58     7865   7902   8074     96    -88   -811       C
ATOM   4097  C   ASN B  58      -3.530  -8.461 -56.423  1.00 62.33           C
ANISOU 4097  C   ASN B  58     7874   7797   8010    103   -102   -756       C
ATOM   4098  O   ASN B  58      -3.673  -9.380 -55.610  1.00 64.54           O
ANISOU 4098  O   ASN B  58     8240   8024   8257    167   -139   -749       O
ATOM   4099  CB  ASN B  58      -3.631  -8.754 -58.936  1.00 62.65           C
ANISOU 4099  CB  ASN B  58     7868   7873   8064     16    -44   -760       C
ATOM   4100  CG  ASN B  58      -3.982  -7.412 -59.509  1.00 67.11           C
ANISOU 4100  CG  ASN B  58     8373   8470   8656    -72      6   -733       C
ATOM   4101  OD1 ASN B  58      -3.791  -6.383 -58.873  1.00 73.69           O
ANISOU 4101  OD1 ASN B  58     9168   9324   9506    -85     12   -736       O
ATOM   4102  ND2 ASN B  58      -4.515  -7.414 -60.720  1.00 67.93           N
ANISOU 4102  ND2 ASN B  58     8477   8573   8759   -130     40   -707       N
ATOM   4103  N   LEU B  59      -4.060  -7.252 -56.257  1.00 56.40           N
ANISOU 4103  N   LEU B  59     7086   7059   7284     36    -70   -718       N
ATOM   4104  CA  LEU B  59      -4.893  -6.917 -55.120  1.00 57.60           C
ANISOU 4104  CA  LEU B  59     7286   7170   7431     30    -76   -665       C
ATOM   4105  C   LEU B  59      -6.246  -6.406 -55.608  1.00 59.71           C
ANISOU 4105  C   LEU B  59     7568   7416   7705    -59    -33   -592       C
ATOM   4106  O   LEU B  59      -6.292  -5.534 -56.491  1.00 61.34           O
ANISOU 4106  O   LEU B  59     7715   7658   7932   -118      2   -588       O
ATOM   4107  CB  LEU B  59      -4.218  -5.850 -54.233  1.00 58.15           C
ANISOU 4107  CB  LEU B  59     7294   7279   7520     47    -86   -696       C
ATOM   4108  CG  LEU B  59      -2.922  -6.231 -53.519  1.00 55.12           C
ANISOU 4108  CG  LEU B  59     6890   6925   7128    145   -137   -776       C
ATOM   4109  CD1 LEU B  59      -2.061  -4.987 -53.302  1.00 42.37           C
ANISOU 4109  CD1 LEU B  59     5171   5381   5545    130   -125   -830       C
ATOM   4110  CD2 LEU B  59      -3.222  -6.943 -52.203  1.00 54.05           C
ANISOU 4110  CD2 LEU B  59     6850   6729   6956    218   -182   -756       C
ATOM   4111  N   PRO B  60      -7.367  -6.882 -55.032  1.00 46.00           N
ANISOU 4111  N   PRO B  60     5908   5621   5947    -71    -33   -541       N
ATOM   4112  CA  PRO B  60      -7.382  -7.793 -53.879  1.00 51.68           C
ANISOU 4112  CA  PRO B  60     6715   6286   6634     -9    -67   -541       C
ATOM   4113  C   PRO B  60      -7.070  -9.239 -54.217  1.00 61.34           C
ANISOU 4113  C   PRO B  60     8007   7474   7824     40    -86   -564       C
ATOM   4114  O   PRO B  60      -7.083  -9.620 -55.392  1.00 65.20           O
ANISOU 4114  O   PRO B  60     8479   7976   8316     14    -69   -572       O
ATOM   4115  CB  PRO B  60      -8.816  -7.696 -53.384  1.00 54.29           C
ANISOU 4115  CB  PRO B  60     7100   6572   6955    -66    -43   -479       C
ATOM   4116  CG  PRO B  60      -9.597  -7.465 -54.634  1.00 49.70           C
ANISOU 4116  CG  PRO B  60     6484   6011   6387   -141     -5   -456       C
ATOM   4117  CD  PRO B  60      -8.728  -6.542 -55.469  1.00 37.62           C
ANISOU 4117  CD  PRO B  60     4859   4545   4889   -148      2   -484       C
ATOM   4118  N   TYR B  61      -6.795 -10.029 -53.179  1.00 60.90           N
ANISOU 4118  N   TYR B  61     8037   7369   7731    115   -123   -576       N
ATOM   4119  CA  TYR B  61      -6.710 -11.477 -53.295  1.00 60.46           C
ANISOU 4119  CA  TYR B  61     8084   7258   7632    163   -140   -588       C
ATOM   4120  C   TYR B  61      -7.447 -12.101 -52.122  1.00 60.64           C
ANISOU 4120  C   TYR B  61     8237   7194   7608    176   -143   -552       C
ATOM   4121  O   TYR B  61      -7.713 -11.442 -51.111  1.00 64.65           O
ANISOU 4121  O   TYR B  61     8748   7696   8119    172   -146   -532       O
ATOM   4122  CB  TYR B  61      -5.256 -11.972 -53.342  1.00 65.22           C
ANISOU 4122  CB  TYR B  61     8670   7889   8222    270   -192   -662       C
ATOM   4123  CG  TYR B  61      -4.487 -11.774 -52.057  1.00 70.03           C
ANISOU 4123  CG  TYR B  61     9292   8501   8816    363   -242   -696       C
ATOM   4124  CD1 TYR B  61      -4.566 -12.700 -51.022  1.00 69.84           C
ANISOU 4124  CD1 TYR B  61     9404   8398   8733    438   -276   -690       C
ATOM   4125  CD2 TYR B  61      -3.670 -10.666 -51.884  1.00 68.39           C
ANISOU 4125  CD2 TYR B  61     8965   8373   8646    375   -254   -739       C
ATOM   4126  CE1 TYR B  61      -3.858 -12.517 -49.854  1.00 77.00           C
ANISOU 4126  CE1 TYR B  61    10325   9309   9620    531   -327   -724       C
ATOM   4127  CE2 TYR B  61      -2.955 -10.484 -50.727  1.00 69.55           C
ANISOU 4127  CE2 TYR B  61     9116   8531   8780    461   -303   -778       C
ATOM   4128  CZ  TYR B  61      -3.053 -11.410 -49.710  1.00 73.50           C
ANISOU 4128  CZ  TYR B  61     9751   8955   9221    544   -343   -770       C
ATOM   4129  OH  TYR B  61      -2.341 -11.224 -48.547  1.00 71.08           O
ANISOU 4129  OH  TYR B  61     9452   8659   8895    639   -396   -812       O
ATOM   4130  N   LEU B  62      -7.775 -13.384 -52.264  1.00 56.57           N
ANISOU 4130  N   LEU B  62     7838   6610   7047    188   -139   -547       N
ATOM   4131  CA  LEU B  62      -8.444 -14.120 -51.198  1.00 51.26           C
ANISOU 4131  CA  LEU B  62     7312   5844   6319    195   -133   -517       C
ATOM   4132  C   LEU B  62      -7.809 -15.493 -51.050  1.00 56.37           C
ANISOU 4132  C   LEU B  62     8087   6425   6905    290   -168   -548       C
ATOM   4133  O   LEU B  62      -7.643 -16.221 -52.031  1.00 55.90           O
ANISOU 4133  O   LEU B  62     8036   6363   6839    291   -163   -565       O
ATOM   4134  CB  LEU B  62      -9.949 -14.261 -51.453  1.00 43.40           C
ANISOU 4134  CB  LEU B  62     6355   4813   5322     77    -68   -469       C
ATOM   4135  CG  LEU B  62     -10.777 -14.717 -50.239  1.00 45.65           C
ANISOU 4135  CG  LEU B  62     6777   5011   5558     57    -47   -439       C
ATOM   4136  CD1 LEU B  62     -11.277 -13.535 -49.409  1.00 43.23           C
ANISOU 4136  CD1 LEU B  62     6412   4733   5280     18    -37   -413       C
ATOM   4137  CD2 LEU B  62     -11.948 -15.569 -50.696  1.00 45.01           C
ANISOU 4137  CD2 LEU B  62     6775   4876   5450    -35     13   -421       C
ATOM   4138  N   ILE B  63      -7.455 -15.842 -49.824  1.00 60.04           N
ANISOU 4138  N   ILE B  63     8656   6835   7320    375   -205   -555       N
ATOM   4139  CA  ILE B  63      -6.873 -17.139 -49.512  1.00 58.59           C
ANISOU 4139  CA  ILE B  63     8620   6577   7065    480   -245   -582       C
ATOM   4140  C   ILE B  63      -7.891 -17.879 -48.654  1.00 59.09           C
ANISOU 4140  C   ILE B  63     8866   6522   7063    443   -207   -537       C
ATOM   4141  O   ILE B  63      -8.225 -17.441 -47.544  1.00 63.16           O
ANISOU 4141  O   ILE B  63     9421   7011   7564    439   -205   -513       O
ATOM   4142  CB  ILE B  63      -5.509 -16.994 -48.820  1.00 56.23           C
ANISOU 4142  CB  ILE B  63     8303   6310   6750    627   -326   -641       C
ATOM   4143  CG1 ILE B  63      -4.563 -16.197 -49.719  1.00 58.75           C
ANISOU 4143  CG1 ILE B  63     8432   6753   7137    640   -348   -694       C
ATOM   4144  CG2 ILE B  63      -4.894 -18.358 -48.507  1.00 46.01           C
ANISOU 4144  CG2 ILE B  63     7172   4936   5372    754   -375   -674       C
ATOM   4145  CD1 ILE B  63      -3.318 -15.707 -49.031  1.00 59.65           C
ANISOU 4145  CD1 ILE B  63     8482   6928   7254    758   -417   -760       C
ATOM   4146  N   ASP B  64      -8.432 -18.971 -49.192  1.00 63.65           N
ANISOU 4146  N   ASP B  64     9553   7030   7602    403   -170   -526       N
ATOM   4147  CA  ASP B  64      -9.432 -19.806 -48.516  1.00 64.71           C
ANISOU 4147  CA  ASP B  64     9873   7045   7668    350   -119   -490       C
ATOM   4148  C   ASP B  64      -8.939 -21.238 -48.657  1.00 66.13           C
ANISOU 4148  C   ASP B  64    10219   7136   7771    435   -141   -514       C
ATOM   4149  O   ASP B  64      -9.307 -21.944 -49.596  1.00 75.50           O
ANISOU 4149  O   ASP B  64    11430   8302   8952    380   -104   -515       O
ATOM   4150  CB  ASP B  64     -10.839 -19.604 -49.110  1.00 57.45           C
ANISOU 4150  CB  ASP B  64     8911   6135   6782    184    -33   -456       C
ATOM   4151  CG  ASP B  64     -11.937 -20.297 -48.300  1.00 64.94           C
ANISOU 4151  CG  ASP B  64    10036   6973   7667    109     31   -428       C
ATOM   4152  OD1 ASP B  64     -11.729 -20.588 -47.105  1.00 67.70           O
ANISOU 4152  OD1 ASP B  64    10522   7245   7954    173     12   -421       O
ATOM   4153  OD2 ASP B  64     -13.021 -20.556 -48.866  1.00 67.66           O
ANISOU 4153  OD2 ASP B  64    10381   7307   8018    -16    102   -417       O
ATOM   4154  N   GLY B  65      -8.069 -21.644 -47.736  1.00 68.58           N
ANISOU 4154  N   GLY B  65    10641   7397   8019    576   -206   -537       N
ATOM   4155  CA  GLY B  65      -7.482 -22.970 -47.748  1.00 60.37           C
ANISOU 4155  CA  GLY B  65     9773   6269   6895    684   -241   -564       C
ATOM   4156  C   GLY B  65      -6.540 -23.194 -48.907  1.00 66.42           C
ANISOU 4156  C   GLY B  65    10436   7108   7693    750   -286   -615       C
ATOM   4157  O   GLY B  65      -5.540 -22.487 -49.058  1.00 78.98           O
ANISOU 4157  O   GLY B  65    11876   8801   9330    829   -347   -659       O
ATOM   4158  N   ALA B  66      -6.858 -24.184 -49.730  1.00 65.42           N
ANISOU 4158  N   ALA B  66    10390   6928   7540    713   -252   -613       N
ATOM   4159  CA  ALA B  66      -6.113 -24.485 -50.946  1.00 70.77           C
ANISOU 4159  CA  ALA B  66    10976   7668   8246    757   -282   -658       C
ATOM   4160  C   ALA B  66      -6.502 -23.591 -52.131  1.00 70.60           C
ANISOU 4160  C   ALA B  66    10739   7761   8326    632   -239   -649       C
ATOM   4161  O   ALA B  66      -6.018 -23.821 -53.244  1.00 78.44           O
ANISOU 4161  O   ALA B  66    11653   8805   9345    646   -251   -682       O
ATOM   4162  CB  ALA B  66      -6.313 -25.959 -51.318  1.00 67.51           C
ANISOU 4162  CB  ALA B  66    10752   7143   7757    770   -262   -660       C
ATOM   4163  N   HIS B  67      -7.349 -22.585 -51.929  1.00 64.97           N
ANISOU 4163  N   HIS B  67     9934   7086   7664    518   -191   -609       N
ATOM   4164  CA  HIS B  67      -7.781 -21.682 -52.990  1.00 62.52           C
ANISOU 4164  CA  HIS B  67     9436   6878   7441    406   -152   -598       C
ATOM   4165  C   HIS B  67      -7.118 -20.325 -52.799  1.00 59.11           C
ANISOU 4165  C   HIS B  67     8832   6554   7072    436   -190   -614       C
ATOM   4166  O   HIS B  67      -7.338 -19.658 -51.786  1.00 67.64           O
ANISOU 4166  O   HIS B  67     9914   7631   8155    433   -192   -593       O
ATOM   4167  CB  HIS B  67      -9.305 -21.542 -52.997  1.00 63.73           C
ANISOU 4167  CB  HIS B  67     9610   7000   7603    253    -69   -547       C
ATOM   4168  CG  HIS B  67     -10.028 -22.834 -53.234  1.00 67.08           C
ANISOU 4168  CG  HIS B  67    10196   7324   7968    202    -19   -538       C
ATOM   4169  ND1 HIS B  67     -11.127 -23.218 -52.498  1.00 67.31           N
ANISOU 4169  ND1 HIS B  67    10357   7266   7953    119     43   -508       N
ATOM   4170  CD2 HIS B  67      -9.810 -23.828 -54.128  1.00 66.45           C
ANISOU 4170  CD2 HIS B  67    10168   7216   7865    217    -16   -560       C
ATOM   4171  CE1 HIS B  67     -11.553 -24.393 -52.926  1.00 64.94           C
ANISOU 4171  CE1 HIS B  67    10184   6887   7603     80     84   -513       C
ATOM   4172  NE2 HIS B  67     -10.774 -24.784 -53.916  1.00 64.90           N
ANISOU 4172  NE2 HIS B  67    10134   6914   7610    141     48   -542       N
ATOM   4173  N   ARG B  68      -6.315 -19.918 -53.772  1.00 63.95           N
ANISOU 4173  N   ARG B  68     9302   7262   7736    459   -214   -654       N
ATOM   4174  CA  ARG B  68      -5.696 -18.597 -53.798  1.00 67.97           C
ANISOU 4174  CA  ARG B  68     9639   7878   8308    466   -235   -675       C
ATOM   4175  C   ARG B  68      -6.181 -17.881 -55.049  1.00 68.67           C
ANISOU 4175  C   ARG B  68     9590   8039   8462    352   -186   -659       C
ATOM   4176  O   ARG B  68      -5.859 -18.291 -56.171  1.00 74.71           O
ANISOU 4176  O   ARG B  68    10318   8832   9238    350   -183   -685       O
ATOM   4177  CB  ARG B  68      -4.178 -18.703 -53.780  1.00 69.35           C
ANISOU 4177  CB  ARG B  68     9767   8104   8477    602   -308   -752       C
ATOM   4178  CG  ARG B  68      -3.678 -19.749 -52.817  1.00 74.42           C
ANISOU 4178  CG  ARG B  68    10573   8664   9038    734   -364   -777       C
ATOM   4179  CD  ARG B  68      -2.413 -19.287 -52.150  1.00 81.91           C
ANISOU 4179  CD  ARG B  68    11456   9677   9989    860   -438   -845       C
ATOM   4180  NE  ARG B  68      -2.355 -19.706 -50.758  1.00 92.04           N
ANISOU 4180  NE  ARG B  68    12888  10881  11203    955   -479   -840       N
ATOM   4181  CZ  ARG B  68      -1.714 -19.037 -49.811  1.00 96.42           C
ANISOU 4181  CZ  ARG B  68    13397  11477  11760   1031   -528   -874       C
ATOM   4182  NH1 ARG B  68      -1.080 -17.913 -50.113  1.00 97.40           N
ANISOU 4182  NH1 ARG B  68    13330  11722  11955   1015   -536   -917       N
ATOM   4183  NH2 ARG B  68      -1.716 -19.490 -48.566  1.00 99.79           N
ANISOU 4183  NH2 ARG B  68    13976  11823  12116   1119   -565   -866       N
ATOM   4184  N   LEU B  69      -6.959 -16.824 -54.853  1.00 60.82           N
ANISOU 4184  N   LEU B  69     8528   7074   7507    264   -150   -618       N
ATOM   4185  CA  LEU B  69      -7.633 -16.127 -55.935  1.00 59.24           C
ANISOU 4185  CA  LEU B  69     8222   6930   7358    155   -102   -594       C
ATOM   4186  C   LEU B  69      -7.204 -14.675 -55.948  1.00 57.54           C
ANISOU 4186  C   LEU B  69     7866   6802   7197    142   -107   -602       C
ATOM   4187  O   LEU B  69      -7.023 -14.066 -54.893  1.00 65.27           O
ANISOU 4187  O   LEU B  69     8840   7783   8179    171   -126   -599       O
ATOM   4188  CB  LEU B  69      -9.165 -16.182 -55.787  1.00 51.96           C
ANISOU 4188  CB  LEU B  69     7354   5962   6427     51    -46   -540       C
ATOM   4189  CG  LEU B  69      -9.882 -17.525 -55.773  1.00 49.20           C
ANISOU 4189  CG  LEU B  69     7148   5521   6023     27    -19   -529       C
ATOM   4190  CD1 LEU B  69      -9.828 -18.142 -54.410  1.00 51.04           C
ANISOU 4190  CD1 LEU B  69     7527   5667   6198     84    -36   -523       C
ATOM   4191  CD2 LEU B  69     -11.318 -17.302 -56.178  1.00 55.82           C
ANISOU 4191  CD2 LEU B  69     7968   6363   6877    -98     43   -495       C
ATOM   4192  N   THR B  70      -7.038 -14.137 -57.142  1.00 54.14           N
ANISOU 4192  N   THR B  70     7328   6438   6806     98    -87   -613       N
ATOM   4193  CA  THR B  70      -7.104 -12.706 -57.385  1.00 56.60           C
ANISOU 4193  CA  THR B  70     7523   6816   7164     43    -67   -602       C
ATOM   4194  C   THR B  70      -8.246 -12.451 -58.370  1.00 56.08           C
ANISOU 4194  C   THR B  70     7434   6758   7114    -57    -19   -562       C
ATOM   4195  O   THR B  70      -8.935 -13.381 -58.808  1.00 53.24           O
ANISOU 4195  O   THR B  70     7139   6358   6731    -84     -1   -548       O
ATOM   4196  CB  THR B  70      -5.769 -12.154 -57.908  1.00 58.29           C
ANISOU 4196  CB  THR B  70     7634   7108   7408     82    -85   -662       C
ATOM   4197  OG1 THR B  70      -5.522 -12.628 -59.239  1.00 56.07           O
ANISOU 4197  OG1 THR B  70     7325   6849   7129     66    -71   -684       O
ATOM   4198  CG2 THR B  70      -4.638 -12.586 -57.018  1.00 57.28           C
ANISOU 4198  CG2 THR B  70     7527   6978   7258    192   -140   -717       C
ATOM   4199  N   GLN B  71      -8.436 -11.170 -58.699  1.00 55.22           N
ANISOU 4199  N   GLN B  71     7238   6704   7041   -107      2   -547       N
ATOM   4200  CA  GLN B  71      -9.518 -10.654 -59.539  1.00 46.80           C
ANISOU 4200  CA  GLN B  71     6141   5654   5987   -190     41   -511       C
ATOM   4201  C   GLN B  71     -10.825 -10.581 -58.756  1.00 46.93           C
ANISOU 4201  C   GLN B  71     6206   5633   5993   -233     56   -468       C
ATOM   4202  O   GLN B  71     -11.465 -11.608 -58.507  1.00 52.32           O
ANISOU 4202  O   GLN B  71     6969   6264   6646   -244     64   -461       O
ATOM   4203  CB  GLN B  71      -9.682 -11.476 -60.825  1.00 35.44           C
ANISOU 4203  CB  GLN B  71     4711   4216   4538   -212     56   -521       C
ATOM   4204  CG  GLN B  71      -8.535 -11.298 -61.786  1.00 41.85           C
ANISOU 4204  CG  GLN B  71     5458   5078   5365   -189     52   -563       C
ATOM   4205  CD  GLN B  71      -8.489  -9.903 -62.370  1.00 50.97           C
ANISOU 4205  CD  GLN B  71     6531   6288   6548   -234     75   -555       C
ATOM   4206  OE1 GLN B  71      -9.502  -9.197 -62.413  1.00 45.22           O
ANISOU 4206  OE1 GLN B  71     5797   5562   5824   -284     95   -515       O
ATOM   4207  NE2 GLN B  71      -7.320  -9.501 -62.834  1.00 56.59           N
ANISOU 4207  NE2 GLN B  71     7183   7044   7274   -215     75   -598       N
ATOM   4208  N   SER B  72     -11.230  -9.350 -58.403  1.00 42.80           N
ANISOU 4208  N   SER B  72     5634   5138   5491   -263     65   -445       N
ATOM   4209  CA  SER B  72     -12.349  -9.125 -57.483  1.00 44.26           C
ANISOU 4209  CA  SER B  72     5853   5297   5669   -297     76   -412       C
ATOM   4210  C   SER B  72     -13.642  -9.819 -57.916  1.00 45.42           C
ANISOU 4210  C   SER B  72     6038   5423   5796   -355    105   -401       C
ATOM   4211  O   SER B  72     -14.423 -10.257 -57.057  1.00 51.13           O
ANISOU 4211  O   SER B  72     6823   6105   6499   -377    117   -390       O
ATOM   4212  CB  SER B  72     -12.589  -7.622 -57.315  1.00 39.71           C
ANISOU 4212  CB  SER B  72     5207   4762   5118   -320     81   -393       C
ATOM   4213  OG  SER B  72     -12.691  -6.969 -58.563  1.00 37.34           O
ANISOU 4213  OG  SER B  72     4849   4508   4833   -350     97   -392       O
ATOM   4214  N   ASN B  73     -13.903  -9.918 -59.232  1.00 40.59           N
ANISOU 4214  N   ASN B  73     5393   4842   5188   -385    119   -408       N
ATOM   4215  CA  ASN B  73     -15.119 -10.605 -59.684  1.00 41.40           C
ANISOU 4215  CA  ASN B  73     5524   4933   5272   -441    147   -409       C
ATOM   4216  C   ASN B  73     -15.002 -12.104 -59.470  1.00 43.77           C
ANISOU 4216  C   ASN B  73     5917   5173   5541   -432    152   -424       C
ATOM   4217  O   ASN B  73     -15.982 -12.762 -59.109  1.00 50.41           O
ANISOU 4217  O   ASN B  73     6815   5979   6359   -479    179   -426       O
ATOM   4218  CB  ASN B  73     -15.420 -10.330 -61.156  1.00 44.87           C
ANISOU 4218  CB  ASN B  73     5906   5423   5720   -469    157   -416       C
ATOM   4219  CG  ASN B  73     -15.794  -8.887 -61.440  1.00 46.45           C
ANISOU 4219  CG  ASN B  73     6036   5675   5938   -482    156   -399       C
ATOM   4220  OD1 ASN B  73     -16.516  -8.234 -60.686  1.00 49.28           O
ANISOU 4220  OD1 ASN B  73     6386   6039   6300   -499    158   -384       O
ATOM   4221  ND2 ASN B  73     -15.309  -8.389 -62.556  1.00 54.43           N
ANISOU 4221  ND2 ASN B  73     7002   6721   6956   -474    154   -403       N
ATOM   4222  N   ALA B  74     -13.807 -12.659 -59.677  1.00 45.87           N
ANISOU 4222  N   ALA B  74     6203   5424   5803   -373    129   -442       N
ATOM   4223  CA  ALA B  74     -13.583 -14.069 -59.381  1.00 49.67           C
ANISOU 4223  CA  ALA B  74     6788   5837   6247   -349    128   -457       C
ATOM   4224  C   ALA B  74     -13.790 -14.361 -57.898  1.00 54.24           C
ANISOU 4224  C   ALA B  74     7456   6354   6799   -335    127   -445       C
ATOM   4225  O   ALA B  74     -14.395 -15.377 -57.535  1.00 56.52           O
ANISOU 4225  O   ALA B  74     7847   6579   7050   -362    152   -446       O
ATOM   4226  CB  ALA B  74     -12.177 -14.477 -59.822  1.00 48.52           C
ANISOU 4226  CB  ALA B  74     6638   5697   6101   -273     95   -485       C
ATOM   4227  N   ILE B  75     -13.306 -13.467 -57.030  1.00 54.84           N
ANISOU 4227  N   ILE B  75     7501   6445   6891   -296    102   -434       N
ATOM   4228  CA  ILE B  75     -13.456 -13.632 -55.581  1.00 52.91           C
ANISOU 4228  CA  ILE B  75     7340   6144   6621   -278     98   -422       C
ATOM   4229  C   ILE B  75     -14.931 -13.582 -55.173  1.00 47.32           C
ANISOU 4229  C   ILE B  75     6659   5418   5902   -366    143   -403       C
ATOM   4230  O   ILE B  75     -15.410 -14.429 -54.408  1.00 38.45           O
ANISOU 4230  O   ILE B  75     5648   4223   4737   -385    166   -402       O
ATOM   4231  CB  ILE B  75     -12.630 -12.566 -54.840  1.00 50.73           C
ANISOU 4231  CB  ILE B  75     7006   5901   6369   -222     61   -419       C
ATOM   4232  CG1 ILE B  75     -11.141 -12.739 -55.136  1.00 58.38           C
ANISOU 4232  CG1 ILE B  75     7950   6888   7342   -133     18   -454       C
ATOM   4233  CG2 ILE B  75     -12.850 -12.667 -53.378  1.00 51.45           C
ANISOU 4233  CG2 ILE B  75     7179   5936   6432   -204     57   -405       C
ATOM   4234  CD1 ILE B  75     -10.273 -11.697 -54.471  1.00 60.37           C
ANISOU 4234  CD1 ILE B  75     8136   7182   7620    -83    -14   -464       C
ATOM   4235  N   LEU B  76     -15.675 -12.582 -55.662  1.00 43.90           N
ANISOU 4235  N   LEU B  76     6127   5049   5503   -421    159   -394       N
ATOM   4236  CA  LEU B  76     -17.113 -12.552 -55.395  1.00 44.90           C
ANISOU 4236  CA  LEU B  76     6264   5174   5621   -505    201   -391       C
ATOM   4237  C   LEU B  76     -17.775 -13.844 -55.845  1.00 48.49           C
ANISOU 4237  C   LEU B  76     6794   5589   6043   -559    241   -413       C
ATOM   4238  O   LEU B  76     -18.552 -14.443 -55.096  1.00 54.82           O
ANISOU 4238  O   LEU B  76     7678   6339   6811   -609    278   -419       O
ATOM   4239  CB  LEU B  76     -17.773 -11.355 -56.077  1.00 37.00           C
ANISOU 4239  CB  LEU B  76     5145   4256   4657   -542    204   -387       C
ATOM   4240  CG  LEU B  76     -17.213 -10.022 -55.626  1.00 43.64           C
ANISOU 4240  CG  LEU B  76     5919   5132   5528   -501    174   -366       C
ATOM   4241  CD1 LEU B  76     -17.521  -8.932 -56.621  1.00 33.07           C
ANISOU 4241  CD1 LEU B  76     4479   3866   4218   -517    170   -363       C
ATOM   4242  CD2 LEU B  76     -17.739  -9.660 -54.218  1.00 51.52           C
ANISOU 4242  CD2 LEU B  76     6949   6106   6519   -515    181   -353       C
ATOM   4243  N   ARG B  77     -17.475 -14.287 -57.074  1.00 55.15           N
ANISOU 4243  N   ARG B  77     7612   6453   6891   -553    237   -428       N
ATOM   4244  CA  ARG B  77     -18.106 -15.488 -57.617  1.00 49.26           C
ANISOU 4244  CA  ARG B  77     6929   5673   6115   -608    276   -453       C
ATOM   4245  C   ARG B  77     -17.813 -16.705 -56.749  1.00 53.03           C
ANISOU 4245  C   ARG B  77     7560   6048   6540   -591    289   -455       C
ATOM   4246  O   ARG B  77     -18.709 -17.521 -56.488  1.00 48.76           O
ANISOU 4246  O   ARG B  77     7102   5460   5964   -662    340   -472       O
ATOM   4247  CB  ARG B  77     -17.638 -15.723 -59.056  1.00 48.44           C
ANISOU 4247  CB  ARG B  77     6774   5606   6025   -591    263   -467       C
ATOM   4248  CG  ARG B  77     -18.129 -14.685 -60.055  1.00 53.61           C
ANISOU 4248  CG  ARG B  77     7301   6352   6716   -618    260   -469       C
ATOM   4249  CD  ARG B  77     -17.873 -15.104 -61.505  1.00 62.77           C
ANISOU 4249  CD  ARG B  77     8428   7541   7880   -615    257   -486       C
ATOM   4250  NE  ARG B  77     -19.125 -15.081 -62.260  1.00 80.28           N
ANISOU 4250  NE  ARG B  77    10600   9805  10098   -687    286   -510       N
ATOM   4251  CZ  ARG B  77     -19.755 -16.160 -62.721  1.00 89.48           C
ANISOU 4251  CZ  ARG B  77    11809  10951  11240   -740    321   -541       C
ATOM   4252  NH1 ARG B  77     -19.251 -17.376 -62.523  1.00 92.11           N
ANISOU 4252  NH1 ARG B  77    12245  11210  11544   -729    332   -547       N
ATOM   4253  NH2 ARG B  77     -20.898 -16.021 -63.378  1.00 92.03           N
ANISOU 4253  NH2 ARG B  77    12074  11329  11564   -800    343   -572       N
ATOM   4254  N   TYR B  78     -16.562 -16.825 -56.280  1.00 55.55           N
ANISOU 4254  N   TYR B  78     7923   6334   6851   -495    244   -444       N
ATOM   4255  CA  TYR B  78     -16.153 -17.919 -55.406  1.00 51.75           C
ANISOU 4255  CA  TYR B  78     7599   5751   6312   -454    244   -446       C
ATOM   4256  C   TYR B  78     -16.942 -17.918 -54.106  1.00 59.67           C
ANISOU 4256  C   TYR B  78     8685   6702   7285   -500    278   -434       C
ATOM   4257  O   TYR B  78     -17.366 -18.977 -53.621  1.00 58.77           O
ANISOU 4257  O   TYR B  78     8715   6500   7115   -534    318   -441       O
ATOM   4258  CB  TYR B  78     -14.655 -17.800 -55.110  1.00 54.55           C
ANISOU 4258  CB  TYR B  78     7957   6102   6668   -330    178   -445       C
ATOM   4259  CG  TYR B  78     -14.133 -18.694 -53.993  1.00 61.14           C
ANISOU 4259  CG  TYR B  78     8954   6836   7439   -261    161   -445       C
ATOM   4260  CD1 TYR B  78     -13.736 -20.006 -54.254  1.00 60.36           C
ANISOU 4260  CD1 TYR B  78     8978   6665   7290   -222    159   -463       C
ATOM   4261  CD2 TYR B  78     -14.013 -18.222 -52.689  1.00 59.79           C
ANISOU 4261  CD2 TYR B  78     8821   6640   7256   -226    144   -428       C
ATOM   4262  CE1 TYR B  78     -13.256 -20.826 -53.252  1.00 57.34           C
ANISOU 4262  CE1 TYR B  78     8760   6185   6840   -148    140   -464       C
ATOM   4263  CE2 TYR B  78     -13.530 -19.039 -51.673  1.00 63.17           C
ANISOU 4263  CE2 TYR B  78     9409   6973   7618   -153    126   -430       C
ATOM   4264  CZ  TYR B  78     -13.155 -20.340 -51.966  1.00 67.76           C
ANISOU 4264  CZ  TYR B  78    10119   7481   8145   -112    123   -447       C
ATOM   4265  OH  TYR B  78     -12.677 -21.162 -50.975  1.00 68.71           O
ANISOU 4265  OH  TYR B  78    10415   7501   8192    -30    101   -449       O
ATOM   4266  N   ILE B  79     -17.127 -16.738 -53.516  1.00 65.61           N
ANISOU 4266  N   ILE B  79     9356   7502   8070   -503    266   -416       N
ATOM   4267  CA  ILE B  79     -17.856 -16.641 -52.257  1.00 56.15           C
ANISOU 4267  CA  ILE B  79     8228   6261   6847   -546    297   -406       C
ATOM   4268  C   ILE B  79     -19.342 -16.887 -52.482  1.00 58.07           C
ANISOU 4268  C   ILE B  79     8469   6512   7082   -673    369   -427       C
ATOM   4269  O   ILE B  79     -20.006 -17.523 -51.655  1.00 64.49           O
ANISOU 4269  O   ILE B  79     9399   7256   7849   -730    419   -435       O
ATOM   4270  CB  ILE B  79     -17.583 -15.281 -51.592  1.00 48.44           C
ANISOU 4270  CB  ILE B  79     7158   5337   5909   -509    261   -384       C
ATOM   4271  CG1 ILE B  79     -16.114 -15.184 -51.200  1.00 51.04           C
ANISOU 4271  CG1 ILE B  79     7505   5652   6237   -386    196   -376       C
ATOM   4272  CG2 ILE B  79     -18.456 -15.086 -50.365  1.00 48.91           C
ANISOU 4272  CG2 ILE B  79     7274   5364   5948   -563    297   -376       C
ATOM   4273  CD1 ILE B  79     -15.583 -13.750 -51.175  1.00 53.74           C
ANISOU 4273  CD1 ILE B  79     7708   6076   6635   -347    155   -365       C
ATOM   4274  N   ALA B  80     -19.885 -16.424 -53.616  1.00 50.48           N
ANISOU 4274  N   ALA B  80     7382   5637   6163   -719    376   -444       N
ATOM   4275  CA  ALA B  80     -21.314 -16.615 -53.864  1.00 52.97           C
ANISOU 4275  CA  ALA B  80     7678   5976   6473   -836    440   -478       C
ATOM   4276  C   ALA B  80     -21.638 -18.085 -54.076  1.00 55.03           C
ANISOU 4276  C   ALA B  80     8066   6162   6683   -891    493   -507       C
ATOM   4277  O   ALA B  80     -22.666 -18.578 -53.601  1.00 56.37           O
ANISOU 4277  O   ALA B  80     8298   6300   6819   -988    560   -536       O
ATOM   4278  CB  ALA B  80     -21.771 -15.781 -55.062  1.00 58.24           C
ANISOU 4278  CB  ALA B  80     8186   6754   7190   -856    426   -493       C
ATOM   4279  N   ARG B  81     -20.764 -18.798 -54.783  1.00 59.94           N
ANISOU 4279  N   ARG B  81     8728   6754   7294   -834    468   -503       N
ATOM   4280  CA  ARG B  81     -20.927 -20.236 -54.955  1.00 58.44           C
ANISOU 4280  CA  ARG B  81     8676   6479   7048   -874    514   -526       C
ATOM   4281  C   ARG B  81     -21.004 -20.951 -53.609  1.00 60.36           C
ANISOU 4281  C   ARG B  81     9101   6607   7226   -887    551   -519       C
ATOM   4282  O   ARG B  81     -21.855 -21.831 -53.403  1.00 57.84           O
ANISOU 4282  O   ARG B  81     8886   6228   6860   -985    626   -549       O
ATOM   4283  CB  ARG B  81     -19.764 -20.779 -55.783  1.00 54.30           C
ANISOU 4283  CB  ARG B  81     8170   5939   6523   -785    467   -519       C
ATOM   4284  CG  ARG B  81     -20.107 -21.202 -57.176  1.00 49.14           C
ANISOU 4284  CG  ARG B  81     7456   5329   5884   -830    486   -549       C
ATOM   4285  CD  ARG B  81     -18.850 -21.631 -57.886  1.00 48.82           C
ANISOU 4285  CD  ARG B  81     7428   5275   5844   -732    433   -540       C
ATOM   4286  NE  ARG B  81     -18.335 -20.538 -58.698  1.00 47.82           N
ANISOU 4286  NE  ARG B  81     7139   5251   5780   -683    381   -530       N
ATOM   4287  CZ  ARG B  81     -17.061 -20.180 -58.772  1.00 50.09           C
ANISOU 4287  CZ  ARG B  81     7395   5552   6084   -578    320   -513       C
ATOM   4288  NH1 ARG B  81     -16.136 -20.832 -58.084  1.00 42.52           N
ANISOU 4288  NH1 ARG B  81     6550   4517   5087   -497    292   -507       N
ATOM   4289  NH2 ARG B  81     -16.720 -19.161 -59.550  1.00 66.34           N
ANISOU 4289  NH2 ARG B  81     9310   7702   8194   -555    287   -507       N
ATOM   4290  N   LYS B  82     -20.111 -20.590 -52.679  1.00 56.28           N
ANISOU 4290  N   LYS B  82     8628   6055   6701   -790    500   -483       N
ATOM   4291  CA  LYS B  82     -20.063 -21.249 -51.378  1.00 63.27           C
ANISOU 4291  CA  LYS B  82     9700   6825   7517   -783    525   -472       C
ATOM   4292  C   LYS B  82     -21.332 -21.046 -50.565  1.00 60.12           C
ANISOU 4292  C   LYS B  82     9324   6418   7103   -901    598   -487       C
ATOM   4293  O   LYS B  82     -21.499 -21.710 -49.541  1.00 70.80           O
ANISOU 4293  O   LYS B  82    10848   7666   8388   -923    639   -484       O
ATOM   4294  CB  LYS B  82     -18.860 -20.744 -50.560  1.00 65.51           C
ANISOU 4294  CB  LYS B  82    10000   7090   7798   -647    447   -437       C
ATOM   4295  CG  LYS B  82     -17.527 -21.296 -51.026  1.00 73.09           C
ANISOU 4295  CG  LYS B  82    11001   8025   8745   -522    382   -434       C
ATOM   4296  CD  LYS B  82     -16.377 -20.838 -50.146  1.00 75.79           C
ANISOU 4296  CD  LYS B  82    11361   8356   9081   -389    307   -413       C
ATOM   4297  CE  LYS B  82     -16.703 -21.003 -48.673  1.00 81.69           C
ANISOU 4297  CE  LYS B  82    12254   9015   9769   -395    331   -398       C
ATOM   4298  NZ  LYS B  82     -15.482 -20.889 -47.812  1.00 82.56           N
ANISOU 4298  NZ  LYS B  82    12423   9094   9853   -248    254   -387       N
ATOM   4299  N   HIS B  83     -22.217 -20.147 -50.981  1.00 58.72           N
ANISOU 4299  N   HIS B  83     8984   6347   6982   -975    615   -506       N
ATOM   4300  CA  HIS B  83     -23.365 -19.780 -50.162  1.00 63.77           C
ANISOU 4300  CA  HIS B  83     9619   6997   7614  -1076    675   -527       C
ATOM   4301  C   HIS B  83     -24.621 -19.599 -51.011  1.00 71.48           C
ANISOU 4301  C   HIS B  83    10472   8065   8622  -1194    726   -582       C
ATOM   4302  O   HIS B  83     -25.563 -18.924 -50.568  1.00 67.34           O
ANISOU 4302  O   HIS B  83     9875   7596   8115  -1263    757   -606       O
ATOM   4303  CB  HIS B  83     -23.069 -18.489 -49.351  1.00 60.51           C
ANISOU 4303  CB  HIS B  83     9124   6630   7238  -1015    623   -491       C
ATOM   4304  CG  HIS B  83     -21.933 -18.632 -48.377  1.00 61.24           C
ANISOU 4304  CG  HIS B  83     9334   6638   7295   -904    575   -448       C
ATOM   4305  ND1 HIS B  83     -22.076 -19.235 -47.147  1.00 60.02           N
ANISOU 4305  ND1 HIS B  83     9357   6377   7072   -922    615   -442       N
ATOM   4306  CD2 HIS B  83     -20.634 -18.253 -48.457  1.00 61.84           C
ANISOU 4306  CD2 HIS B  83     9379   6724   7391   -771    491   -415       C
ATOM   4307  CE1 HIS B  83     -20.914 -19.231 -46.517  1.00 56.83           C
ANISOU 4307  CE1 HIS B  83     9026   5921   6646   -795    550   -406       C
ATOM   4308  NE2 HIS B  83     -20.023 -18.637 -47.288  1.00 54.31           N
ANISOU 4308  NE2 HIS B  83     8576   5676   6382   -704    475   -393       N
ATOM   4309  N   ASN B  84     -24.634 -20.158 -52.231  1.00 68.63           N
ANISOU 4309  N   ASN B  84    10079   7728   8270  -1209    731   -607       N
ATOM   4310  CA  ASN B  84     -25.812 -20.193 -53.100  1.00 69.48           C
ANISOU 4310  CA  ASN B  84    10085   7917   8397  -1318    780   -671       C
ATOM   4311  C   ASN B  84     -26.321 -18.795 -53.441  1.00 77.94           C
ANISOU 4311  C   ASN B  84    10958   9122   9533  -1312    743   -680       C
ATOM   4312  O   ASN B  84     -27.510 -18.493 -53.310  1.00 78.26           O
ANISOU 4312  O   ASN B  84    10932   9223   9580  -1405    790   -734       O
ATOM   4313  CB  ASN B  84     -26.921 -21.036 -52.479  1.00 77.92           C
ANISOU 4313  CB  ASN B  84    11263   8932   9412  -1458    886   -727       C
ATOM   4314  CG  ASN B  84     -26.686 -22.506 -52.670  1.00 90.62           C
ANISOU 4314  CG  ASN B  84    13044  10428  10958  -1488    934   -738       C
ATOM   4315  OD1 ASN B  84     -25.549 -22.938 -52.877  1.00 93.24           O
ANISOU 4315  OD1 ASN B  84    13453  10698  11276  -1386    884   -693       O
ATOM   4316  ND2 ASN B  84     -27.761 -23.287 -52.639  1.00 95.46           N
ANISOU 4316  ND2 ASN B  84    13717  11020  11534  -1630   1034   -806       N
ATOM   4317  N   LEU B  85     -25.413 -17.949 -53.919  1.00 79.28           N
ANISOU 4317  N   LEU B  85    11036   9338   9747  -1202    661   -634       N
ATOM   4318  CA  LEU B  85     -25.730 -16.575 -54.282  1.00 79.52           C
ANISOU 4318  CA  LEU B  85    10897   9483   9832  -1179    618   -633       C
ATOM   4319  C   LEU B  85     -25.415 -16.303 -55.751  1.00 81.14           C
ANISOU 4319  C   LEU B  85    10996   9760  10072  -1134    574   -635       C
ATOM   4320  O   LEU B  85     -24.990 -15.206 -56.134  1.00 78.02           O
ANISOU 4320  O   LEU B  85    10498   9428   9718  -1065    515   -606       O
ATOM   4321  CB  LEU B  85     -25.006 -15.596 -53.362  1.00 69.62           C
ANISOU 4321  CB  LEU B  85     9633   8221   8597  -1096    566   -577       C
ATOM   4322  CG  LEU B  85     -25.661 -15.551 -51.986  1.00 64.81           C
ANISOU 4322  CG  LEU B  85     9088   7574   7962  -1154    611   -586       C
ATOM   4323  CD1 LEU B  85     -24.634 -15.314 -50.892  1.00 67.43           C
ANISOU 4323  CD1 LEU B  85     9500   7836   8282  -1070    573   -528       C
ATOM   4324  CD2 LEU B  85     -26.747 -14.511 -51.949  1.00 59.56           C
ANISOU 4324  CD2 LEU B  85     8291   7010   7329  -1202    619   -620       C
ATOM   4325  N   CYS B  86     -25.624 -17.310 -56.588  1.00 74.81           N
ANISOU 4325  N   CYS B  86    10227   8946   9252  -1178    606   -670       N
ATOM   4326  CA  CYS B  86     -25.566 -17.174 -58.031  1.00 71.24           C
ANISOU 4326  CA  CYS B  86     9678   8565   8826  -1157    577   -685       C
ATOM   4327  C   CYS B  86     -26.968 -17.354 -58.594  1.00 66.35           C
ANISOU 4327  C   CYS B  86     8989   8017   8203  -1256    625   -763       C
ATOM   4328  O   CYS B  86     -27.835 -17.954 -57.959  1.00 67.68           O
ANISOU 4328  O   CYS B  86     9214   8161   8343  -1353    693   -810       O
ATOM   4329  CB  CYS B  86     -24.614 -18.206 -58.648  1.00 81.37           C
ANISOU 4329  CB  CYS B  86    11044   9783  10090  -1118    569   -668       C
ATOM   4330  SG  CYS B  86     -22.851 -17.935 -58.369  1.00 88.74           S
ANISOU 4330  SG  CYS B  86    12019  10664  11034   -983    498   -595       S
ATOM   4331  N   GLY B  87     -27.181 -16.839 -59.801  1.00 66.75           N
ANISOU 4331  N   GLY B  87     8921   8160   8281  -1234    591   -783       N
ATOM   4332  CA  GLY B  87     -28.468 -17.014 -60.447  1.00 65.63           C
ANISOU 4332  CA  GLY B  87     8703   8097   8134  -1315    628   -867       C
ATOM   4333  C   GLY B  87     -28.814 -18.478 -60.640  1.00 61.65           C
ANISOU 4333  C   GLY B  87     8291   7540   7595  -1405    698   -916       C
ATOM   4334  O   GLY B  87     -27.943 -19.344 -60.723  1.00 59.83           O
ANISOU 4334  O   GLY B  87     8167   7221   7345  -1382    702   -881       O
ATOM   4335  N   GLU B  88     -30.116 -18.755 -60.694  1.00 69.50           N
ANISOU 4335  N   GLU B  88     9241   8590   8576  -1509    755  -1006       N
ATOM   4336  CA  GLU B  88     -30.629 -20.103 -60.889  1.00 67.74           C
ANISOU 4336  CA  GLU B  88     9096   8326   8317  -1615    834  -1069       C
ATOM   4337  C   GLU B  88     -31.192 -20.297 -62.292  1.00 69.95           C
ANISOU 4337  C   GLU B  88     9274   8697   8606  -1636    830  -1136       C
ATOM   4338  O   GLU B  88     -30.751 -21.184 -63.022  1.00 72.07           O
ANISOU 4338  O   GLU B  88     9599   8924   8861  -1638    839  -1133       O
ATOM   4339  CB  GLU B  88     -31.695 -20.412 -59.832  1.00 67.88           C
ANISOU 4339  CB  GLU B  88     9152   8332   8306  -1737    919  -1135       C
ATOM   4340  CG  GLU B  88     -31.160 -20.420 -58.415  1.00 84.02           C
ANISOU 4340  CG  GLU B  88    11324  10271  10331  -1726    933  -1072       C
ATOM   4341  CD  GLU B  88     -32.222 -20.073 -57.377  1.00 97.47           C
ANISOU 4341  CD  GLU B  88    13007  12004  12024  -1816    989  -1128       C
ATOM   4342  OE1 GLU B  88     -33.338 -19.653 -57.763  1.00100.78           O
ANISOU 4342  OE1 GLU B  88    13291  12541  12459  -1872   1003  -1215       O
ATOM   4343  OE2 GLU B  88     -31.932 -20.218 -56.169  1.00 99.29           O
ANISOU 4343  OE2 GLU B  88    13355  12142  12228  -1826   1016  -1089       O
ATOM   4344  N   THR B  89     -32.155 -19.483 -62.701  1.00 63.77           N
ANISOU 4344  N   THR B  89     8345   8041   7843  -1646    811  -1199       N
ATOM   4345  CA  THR B  89     -32.682 -19.631 -64.043  1.00 59.71           C
ANISOU 4345  CA  THR B  89     7734   7619   7334  -1654    799  -1266       C
ATOM   4346  C   THR B  89     -31.763 -18.940 -65.052  1.00 67.70           C
ANISOU 4346  C   THR B  89     8695   8656   8371  -1525    709  -1196       C
ATOM   4347  O   THR B  89     -30.959 -18.071 -64.705  1.00 71.56           O
ANISOU 4347  O   THR B  89     9186   9123   8880  -1434    654  -1113       O
ATOM   4348  CB  THR B  89     -34.106 -19.069 -64.117  1.00 51.43           C
ANISOU 4348  CB  THR B  89     6549   6702   6289  -1707    811  -1375       C
ATOM   4349  OG1 THR B  89     -34.075 -17.641 -63.999  1.00 51.06           O
ANISOU 4349  OG1 THR B  89     6409   6722   6269  -1611    736  -1340       O
ATOM   4350  CG2 THR B  89     -34.932 -19.632 -62.990  1.00 53.81           C
ANISOU 4350  CG2 THR B  89     6902   6976   6566  -1837    904  -1441       C
ATOM   4351  N   GLU B  90     -31.893 -19.340 -66.321  1.00 64.01           N
ANISOU 4351  N   GLU B  90     8183   8236   7901  -1522    700  -1235       N
ATOM   4352  CA  GLU B  90     -31.070 -18.747 -67.372  1.00 63.34           C
ANISOU 4352  CA  GLU B  90     8056   8176   7835  -1411    623  -1177       C
ATOM   4353  C   GLU B  90     -31.215 -17.228 -67.423  1.00 74.97           C
ANISOU 4353  C   GLU B  90     9427   9728   9328  -1326    554  -1156       C
ATOM   4354  O   GLU B  90     -30.231 -16.519 -67.674  1.00 73.84           O
ANISOU 4354  O   GLU B  90     9289   9564   9201  -1231    498  -1075       O
ATOM   4355  CB  GLU B  90     -31.422 -19.360 -68.727  1.00 64.55           C
ANISOU 4355  CB  GLU B  90     8165   8383   7979  -1429    626  -1238       C
ATOM   4356  CG  GLU B  90     -30.759 -18.692 -69.931  1.00 58.77           C
ANISOU 4356  CG  GLU B  90     7379   7691   7259  -1321    551  -1193       C
ATOM   4357  CD  GLU B  90     -29.244 -18.936 -70.024  1.00 61.60           C
ANISOU 4357  CD  GLU B  90     7827   7951   7625  -1258    529  -1094       C
ATOM   4358  OE1 GLU B  90     -28.672 -19.703 -69.205  1.00 59.46           O
ANISOU 4358  OE1 GLU B  90     7666   7579   7348  -1288    567  -1061       O
ATOM   4359  OE2 GLU B  90     -28.622 -18.356 -70.940  1.00 58.01           O
ANISOU 4359  OE2 GLU B  90     7338   7524   7181  -1175    475  -1055       O
ATOM   4360  N   GLU B  91     -32.431 -16.704 -67.195  1.00 80.71           N
ANISOU 4360  N   GLU B  91    10064  10548  10053  -1360    560  -1234       N
ATOM   4361  CA  GLU B  91     -32.606 -15.251 -67.216  1.00 79.26           C
ANISOU 4361  CA  GLU B  91     9796  10437   9884  -1274    493  -1217       C
ATOM   4362  C   GLU B  91     -31.835 -14.589 -66.084  1.00 72.49           C
ANISOU 4362  C   GLU B  91     8993   9508   9042  -1234    479  -1126       C
ATOM   4363  O   GLU B  91     -31.226 -13.529 -66.275  1.00 71.02           O
ANISOU 4363  O   GLU B  91     8786   9329   8869  -1139    418  -1062       O
ATOM   4364  CB  GLU B  91     -34.078 -14.855 -67.134  1.00 81.30           C
ANISOU 4364  CB  GLU B  91     9946  10812  10134  -1313    500  -1328       C
ATOM   4365  CG  GLU B  91     -34.292 -13.393 -67.531  1.00 87.60           C
ANISOU 4365  CG  GLU B  91    10655  11694  10935  -1204    418  -1320       C
ATOM   4366  CD  GLU B  91     -35.505 -12.734 -66.871  1.00 91.35           C
ANISOU 4366  CD  GLU B  91    11042  12259  11406  -1224    418  -1402       C
ATOM   4367  OE1 GLU B  91     -36.326 -13.444 -66.250  1.00 92.32           O
ANISOU 4367  OE1 GLU B  91    11154  12399  11523  -1333    485  -1486       O
ATOM   4368  OE2 GLU B  91     -35.631 -11.491 -66.976  1.00 89.50           O
ANISOU 4368  OE2 GLU B  91    10754  12078  11172  -1131    352  -1387       O
ATOM   4369  N   GLU B  92     -31.835 -15.201 -64.901  1.00 66.15           N
ANISOU 4369  N   GLU B  92     8267   8632   8234  -1305    536  -1122       N
ATOM   4370  CA  GLU B  92     -31.064 -14.634 -63.799  1.00 68.32           C
ANISOU 4370  CA  GLU B  92     8599   8838   8522  -1265    521  -1038       C
ATOM   4371  C   GLU B  92     -29.574 -14.676 -64.099  1.00 67.28           C
ANISOU 4371  C   GLU B  92     8534   8629   8400  -1187    486   -943       C
ATOM   4372  O   GLU B  92     -28.851 -13.715 -63.811  1.00 70.72           O
ANISOU 4372  O   GLU B  92     8964   9053   8854  -1111    439   -875       O
ATOM   4373  CB  GLU B  92     -31.376 -15.370 -62.499  1.00 69.51           C
ANISOU 4373  CB  GLU B  92     8833   8922   8657  -1358    593  -1056       C
ATOM   4374  CG  GLU B  92     -32.762 -15.064 -61.969  1.00 67.39           C
ANISOU 4374  CG  GLU B  92     8490   8732   8382  -1429    626  -1147       C
ATOM   4375  CD  GLU B  92     -33.348 -16.226 -61.214  1.00 73.88           C
ANISOU 4375  CD  GLU B  92     9391   9504   9177  -1559    721  -1205       C
ATOM   4376  OE1 GLU B  92     -34.597 -16.337 -61.165  1.00 75.54           O
ANISOU 4376  OE1 GLU B  92     9531   9793   9377  -1644    764  -1312       O
ATOM   4377  OE2 GLU B  92     -32.554 -17.025 -60.673  1.00 75.25           O
ANISOU 4377  OE2 GLU B  92     9699   9559   9334  -1575    753  -1149       O
ATOM   4378  N   LYS B  93     -29.099 -15.772 -64.699  1.00 55.68           N
ANISOU 4378  N   LYS B  93     7125   7111   6919  -1207    508   -942       N
ATOM   4379  CA  LYS B  93     -27.689 -15.863 -65.055  1.00 50.08           C
ANISOU 4379  CA  LYS B  93     6471   6339   6219  -1133    474   -865       C
ATOM   4380  C   LYS B  93     -27.307 -14.811 -66.089  1.00 55.36           C
ANISOU 4380  C   LYS B  93     7059   7070   6904  -1047    410   -838       C
ATOM   4381  O   LYS B  93     -26.157 -14.360 -66.128  1.00 67.05           O
ANISOU 4381  O   LYS B  93     8562   8516   8399   -977    375   -771       O
ATOM   4382  CB  LYS B  93     -27.366 -17.260 -65.577  1.00 56.01           C
ANISOU 4382  CB  LYS B  93     7297   7033   6950  -1171    510   -881       C
ATOM   4383  CG  LYS B  93     -27.781 -18.389 -64.653  1.00 61.69           C
ANISOU 4383  CG  LYS B  93     8117   7680   7641  -1263    581   -912       C
ATOM   4384  CD  LYS B  93     -26.641 -19.376 -64.495  1.00 65.08           C
ANISOU 4384  CD  LYS B  93     8674   7998   8054  -1239    590   -865       C
ATOM   4385  CE  LYS B  93     -27.037 -20.557 -63.626  1.00 66.31           C
ANISOU 4385  CE  LYS B  93     8956   8068   8171  -1328    665   -895       C
ATOM   4386  NZ  LYS B  93     -27.665 -21.634 -64.430  1.00 60.07           N
ANISOU 4386  NZ  LYS B  93     8182   7283   7357  -1409    716   -963       N
ATOM   4387  N   ILE B  94     -28.246 -14.398 -66.929  1.00 44.96           N
ANISOU 4387  N   ILE B  94     5653   5848   5583  -1050    396   -894       N
ATOM   4388  CA  ILE B  94     -27.905 -13.405 -67.937  1.00 50.92           C
ANISOU 4388  CA  ILE B  94     6351   6654   6344   -966    337   -868       C
ATOM   4389  C   ILE B  94     -27.830 -12.031 -67.306  1.00 45.93           C
ANISOU 4389  C   ILE B  94     5689   6039   5724   -912    301   -828       C
ATOM   4390  O   ILE B  94     -26.835 -11.315 -67.469  1.00 43.92           O
ANISOU 4390  O   ILE B  94     5449   5760   5480   -845    267   -763       O
ATOM   4391  CB  ILE B  94     -28.914 -13.434 -69.100  1.00 46.80           C
ANISOU 4391  CB  ILE B  94     5752   6226   5805   -974    327   -944       C
ATOM   4392  CG1 ILE B  94     -28.770 -14.716 -69.906  1.00 48.69           C
ANISOU 4392  CG1 ILE B  94     6022   6444   6032  -1016    357   -972       C
ATOM   4393  CG2 ILE B  94     -28.718 -12.239 -69.994  1.00 41.52           C
ANISOU 4393  CG2 ILE B  94     5035   5609   5131   -883    266   -918       C
ATOM   4394  CD1 ILE B  94     -30.045 -15.072 -70.658  1.00 50.12           C
ANISOU 4394  CD1 ILE B  94     6131   6717   6196  -1060    369  -1074       C
ATOM   4395  N   ARG B  95     -28.891 -11.648 -66.591  1.00 46.80           N
ANISOU 4395  N   ARG B  95     5756   6194   5831   -943    310   -873       N
ATOM   4396  CA  ARG B  95     -28.862 -10.445 -65.764  1.00 48.36           C
ANISOU 4396  CA  ARG B  95     5937   6399   6041   -901    283   -838       C
ATOM   4397  C   ARG B  95     -27.577 -10.349 -64.939  1.00 44.81           C
ANISOU 4397  C   ARG B  95     5560   5858   5609   -877    283   -754       C
ATOM   4398  O   ARG B  95     -26.878  -9.332 -64.989  1.00 55.60           O
ANISOU 4398  O   ARG B  95     6921   7218   6985   -810    245   -699       O
ATOM   4399  CB  ARG B  95     -30.085 -10.418 -64.856  1.00 46.13           C
ANISOU 4399  CB  ARG B  95     5617   6158   5754   -960    310   -902       C
ATOM   4400  CG  ARG B  95     -31.371 -10.339 -65.623  1.00 45.51           C
ANISOU 4400  CG  ARG B  95     5449   6186   5657   -973    301   -997       C
ATOM   4401  CD  ARG B  95     -32.462  -9.801 -64.751  1.00 55.74           C
ANISOU 4401  CD  ARG B  95     6688   7541   6952  -1000    308  -1054       C
ATOM   4402  NE  ARG B  95     -33.045  -8.617 -65.362  1.00 62.33           N
ANISOU 4402  NE  ARG B  95     7442   8466   7775   -919    245  -1082       N
ATOM   4403  CZ  ARG B  95     -33.147  -7.444 -64.757  1.00 61.61           C
ANISOU 4403  CZ  ARG B  95     7331   8391   7688   -865    211  -1057       C
ATOM   4404  NH1 ARG B  95     -32.709  -7.307 -63.525  1.00 56.54           N
ANISOU 4404  NH1 ARG B  95     6734   7684   7064   -889    233  -1006       N
ATOM   4405  NH2 ARG B  95     -33.693  -6.414 -65.383  1.00 74.59           N
ANISOU 4405  NH2 ARG B  95     8913  10114   9313   -784    152  -1086       N
ATOM   4406  N   VAL B  96     -27.236 -11.406 -64.190  1.00 39.54           N
ANISOU 4406  N   VAL B  96     4965   5117   4941   -928    325   -746       N
ATOM   4407  CA  VAL B  96     -26.029 -11.358 -63.358  1.00 40.34           C
ANISOU 4407  CA  VAL B  96     5135   5137   5055   -895    320   -677       C
ATOM   4408  C   VAL B  96     -24.808 -11.010 -64.198  1.00 45.36           C
ANISOU 4408  C   VAL B  96     5773   5759   5701   -825    284   -627       C
ATOM   4409  O   VAL B  96     -24.121 -10.021 -63.937  1.00 47.06           O
ANISOU 4409  O   VAL B  96     5979   5969   5931   -771    254   -581       O
ATOM   4410  CB  VAL B  96     -25.810 -12.683 -62.617  1.00 42.71           C
ANISOU 4410  CB  VAL B  96     5531   5356   5342   -950    367   -681       C
ATOM   4411  CG1 VAL B  96     -24.417 -12.673 -61.969  1.00 37.49           C
ANISOU 4411  CG1 VAL B  96     4938   4618   4690   -894    349   -614       C
ATOM   4412  CG2 VAL B  96     -26.888 -12.898 -61.585  1.00 39.41           C
ANISOU 4412  CG2 VAL B  96     5123   4940   4912  -1024    411   -724       C
ATOM   4413  N   ASP B  97     -24.535 -11.818 -65.233  1.00 50.51           N
ANISOU 4413  N   ASP B  97     6439   6409   6345   -830    290   -642       N
ATOM   4414  CA  ASP B  97     -23.346 -11.623 -66.066  1.00 39.72           C
ANISOU 4414  CA  ASP B  97     5077   5028   4986   -772    264   -603       C
ATOM   4415  C   ASP B  97     -23.302 -10.230 -66.668  1.00 44.67           C
ANISOU 4415  C   ASP B  97     5647   5709   5618   -720    226   -584       C
ATOM   4416  O   ASP B  97     -22.244  -9.592 -66.692  1.00 54.43           O
ANISOU 4416  O   ASP B  97     6891   6924   6866   -673    208   -539       O
ATOM   4417  CB  ASP B  97     -23.307 -12.651 -67.192  1.00 50.79           C
ANISOU 4417  CB  ASP B  97     6490   6433   6375   -790    276   -632       C
ATOM   4418  CG  ASP B  97     -23.084 -14.062 -66.700  1.00 59.31           C
ANISOU 4418  CG  ASP B  97     7648   7442   7444   -832    313   -643       C
ATOM   4419  OD1 ASP B  97     -22.519 -14.227 -65.603  1.00 62.76           O
ANISOU 4419  OD1 ASP B  97     8143   7818   7884   -823    318   -615       O
ATOM   4420  OD2 ASP B  97     -23.479 -15.006 -67.419  1.00 60.34           O
ANISOU 4420  OD2 ASP B  97     7788   7578   7559   -870    335   -683       O
ATOM   4421  N   VAL B  98     -24.432  -9.753 -67.190  1.00 45.32           N
ANISOU 4421  N   VAL B  98     5674   5860   5687   -725    216   -622       N
ATOM   4422  CA  VAL B  98     -24.473  -8.424 -67.799  1.00 42.06           C
ANISOU 4422  CA  VAL B  98     5223   5491   5266   -668    179   -605       C
ATOM   4423  C   VAL B  98     -24.157  -7.356 -66.759  1.00 48.01           C
ANISOU 4423  C   VAL B  98     5980   6226   6034   -642    166   -564       C
ATOM   4424  O   VAL B  98     -23.231  -6.550 -66.930  1.00 49.61           O
ANISOU 4424  O   VAL B  98     6196   6410   6243   -599    151   -519       O
ATOM   4425  CB  VAL B  98     -25.845  -8.187 -68.458  1.00 41.22           C
ANISOU 4425  CB  VAL B  98     5059   5466   5136   -669    164   -665       C
ATOM   4426  CG1 VAL B  98     -26.047  -6.707 -68.814  1.00 34.02           C
ANISOU 4426  CG1 VAL B  98     4123   4594   4209   -602    122   -649       C
ATOM   4427  CG2 VAL B  98     -25.995  -9.080 -69.678  1.00 36.36           C
ANISOU 4427  CG2 VAL B  98     4438   4872   4505   -684    171   -703       C
ATOM   4428  N   LEU B  99     -24.903  -7.366 -65.646  1.00 46.56           N
ANISOU 4428  N   LEU B  99     5787   6046   5857   -673    178   -582       N
ATOM   4429  CA  LEU B  99     -24.740  -6.358 -64.601  1.00 49.50           C
ANISOU 4429  CA  LEU B  99     6160   6406   6243   -651    165   -548       C
ATOM   4430  C   LEU B  99     -23.343  -6.390 -64.007  1.00 50.77           C
ANISOU 4430  C   LEU B  99     6368   6498   6423   -635    170   -494       C
ATOM   4431  O   LEU B  99     -22.762  -5.335 -63.721  1.00 47.23           O
ANISOU 4431  O   LEU B  99     5919   6043   5985   -597    153   -457       O
ATOM   4432  CB  LEU B  99     -25.771  -6.575 -63.495  1.00 47.55           C
ANISOU 4432  CB  LEU B  99     5899   6171   5996   -698    185   -583       C
ATOM   4433  CG  LEU B  99     -26.320  -5.396 -62.669  1.00 48.29           C
ANISOU 4433  CG  LEU B  99     5962   6292   6094   -677    166   -578       C
ATOM   4434  CD1 LEU B  99     -26.464  -5.794 -61.224  1.00 39.65           C
ANISOU 4434  CD1 LEU B  99     4894   5160   5011   -723    195   -578       C
ATOM   4435  CD2 LEU B  99     -25.534  -4.102 -62.785  1.00 44.30           C
ANISOU 4435  CD2 LEU B  99     5462   5777   5594   -611    134   -523       C
ATOM   4436  N   GLU B 100     -22.799  -7.592 -63.785  1.00 49.61           N
ANISOU 4436  N   GLU B 100     6265   6303   6281   -661    193   -495       N
ATOM   4437  CA  GLU B 100     -21.460  -7.691 -63.219  1.00 51.25           C
ANISOU 4437  CA  GLU B 100     6515   6454   6505   -635    192   -456       C
ATOM   4438  C   GLU B 100     -20.451  -6.949 -64.081  1.00 54.19           C
ANISOU 4438  C   GLU B 100     6872   6835   6883   -590    173   -430       C
ATOM   4439  O   GLU B 100     -19.640  -6.167 -63.570  1.00 54.78           O
ANISOU 4439  O   GLU B 100     6947   6894   6972   -561    163   -401       O
ATOM   4440  CB  GLU B 100     -21.041  -9.149 -63.050  1.00 42.45           C
ANISOU 4440  CB  GLU B 100     5457   5287   5384   -658    213   -467       C
ATOM   4441  CG  GLU B 100     -19.623  -9.292 -62.525  1.00 47.52           C
ANISOU 4441  CG  GLU B 100     6138   5878   6038   -617    203   -438       C
ATOM   4442  CD  GLU B 100     -19.036 -10.676 -62.736  1.00 64.55           C
ANISOU 4442  CD  GLU B 100     8353   7989   8183   -618    214   -451       C
ATOM   4443  OE1 GLU B 100     -17.880 -10.767 -63.201  1.00 70.92           O
ANISOU 4443  OE1 GLU B 100     9162   8787   8997   -577    200   -444       O
ATOM   4444  OE2 GLU B 100     -19.722 -11.678 -62.435  1.00 72.06           O
ANISOU 4444  OE2 GLU B 100     9351   8912   9116   -661    240   -473       O
ATOM   4445  N   ASN B 101     -20.516  -7.148 -65.397  1.00 57.91           N
ANISOU 4445  N   ASN B 101     7329   7333   7341   -587    171   -446       N
ATOM   4446  CA  ASN B 101     -19.594  -6.462 -66.295  1.00 45.10           C
ANISOU 4446  CA  ASN B 101     5700   5718   5718   -553    162   -426       C
ATOM   4447  C   ASN B 101     -19.944  -4.993 -66.423  1.00 40.39           C
ANISOU 4447  C   ASN B 101     5083   5150   5112   -529    146   -409       C
ATOM   4448  O   ASN B 101     -19.052  -4.141 -66.393  1.00 46.55           O
ANISOU 4448  O   ASN B 101     5871   5918   5899   -507    145   -383       O
ATOM   4449  CB  ASN B 101     -19.595  -7.143 -67.660  1.00 47.60           C
ANISOU 4449  CB  ASN B 101     6016   6052   6019   -558    167   -447       C
ATOM   4450  CG  ASN B 101     -18.883  -8.453 -67.632  1.00 46.89           C
ANISOU 4450  CG  ASN B 101     5956   5924   5937   -570    181   -458       C
ATOM   4451  OD1 ASN B 101     -17.675  -8.498 -67.765  1.00 53.06           O
ANISOU 4451  OD1 ASN B 101     6748   6684   6728   -549    181   -447       O
ATOM   4452  ND2 ASN B 101     -19.623  -9.535 -67.431  1.00 55.83           N
ANISOU 4452  ND2 ASN B 101     7104   7047   7061   -605    194   -485       N
ATOM   4453  N   GLN B 102     -21.236  -4.679 -66.586  1.00 44.37           N
ANISOU 4453  N   GLN B 102     5564   5697   5599   -531    134   -430       N
ATOM   4454  CA  GLN B 102     -21.674  -3.285 -66.613  1.00 48.49           C
ANISOU 4454  CA  GLN B 102     6075   6243   6105   -498    114   -417       C
ATOM   4455  C   GLN B 102     -21.163  -2.510 -65.402  1.00 54.78           C
ANISOU 4455  C   GLN B 102     6880   7011   6923   -491    115   -384       C
ATOM   4456  O   GLN B 102     -20.737  -1.358 -65.533  1.00 55.55           O
ANISOU 4456  O   GLN B 102     6990   7103   7013   -463    108   -358       O
ATOM   4457  CB  GLN B 102     -23.202  -3.217 -66.673  1.00 50.62           C
ANISOU 4457  CB  GLN B 102     6312   6568   6356   -498     97   -457       C
ATOM   4458  CG  GLN B 102     -23.754  -1.849 -66.992  1.00 48.51           C
ANISOU 4458  CG  GLN B 102     6040   6332   6060   -448     67   -453       C
ATOM   4459  CD  GLN B 102     -23.021  -1.207 -68.159  1.00 52.73           C
ANISOU 4459  CD  GLN B 102     6612   6855   6570   -412     63   -427       C
ATOM   4460  OE1 GLN B 102     -23.015  -1.730 -69.276  1.00 54.64           O
ANISOU 4460  OE1 GLN B 102     6857   7110   6792   -410     63   -444       O
ATOM   4461  NE2 GLN B 102     -22.387  -0.084 -67.900  1.00 42.26           N
ANISOU 4461  NE2 GLN B 102     5318   5500   5241   -389     63   -388       N
ATOM   4462  N   ALA B 103     -21.189  -3.135 -64.213  1.00 54.83           N
ANISOU 4462  N   ALA B 103     6886   6993   6951   -517    125   -387       N
ATOM   4463  CA  ALA B 103     -20.747  -2.457 -62.996  1.00 51.80           C
ANISOU 4463  CA  ALA B 103     6509   6584   6587   -509    123   -359       C
ATOM   4464  C   ALA B 103     -19.280  -2.076 -63.070  1.00 51.08           C
ANISOU 4464  C   ALA B 103     6435   6463   6511   -491    130   -333       C
ATOM   4465  O   ALA B 103     -18.909  -0.962 -62.689  1.00 56.19           O
ANISOU 4465  O   ALA B 103     7083   7105   7162   -474    126   -312       O
ATOM   4466  CB  ALA B 103     -20.980  -3.326 -61.767  1.00 26.71           C
ANISOU 4466  CB  ALA B 103     3343   3382   3425   -539    135   -368       C
ATOM   4467  N   MET B 104     -18.421  -2.987 -63.534  1.00 54.20           N
ANISOU 4467  N   MET B 104     6842   6840   6912   -496    140   -341       N
ATOM   4468  CA  MET B 104     -17.013  -2.623 -63.661  1.00 51.33           C
ANISOU 4468  CA  MET B 104     6483   6459   6560   -482    148   -331       C
ATOM   4469  C   MET B 104     -16.846  -1.470 -64.639  1.00 48.78           C
ANISOU 4469  C   MET B 104     6162   6153   6219   -472    153   -320       C
ATOM   4470  O   MET B 104     -16.060  -0.549 -64.400  1.00 56.50           O
ANISOU 4470  O   MET B 104     7143   7121   7204   -467    163   -308       O
ATOM   4471  CB  MET B 104     -16.176  -3.821 -64.098  1.00 54.01           C
ANISOU 4471  CB  MET B 104     6833   6784   6906   -484    156   -350       C
ATOM   4472  CG  MET B 104     -14.671  -3.513 -64.194  1.00 58.49           C
ANISOU 4472  CG  MET B 104     7393   7344   7487   -469    165   -355       C
ATOM   4473  SD  MET B 104     -13.854  -3.208 -62.608  1.00 63.74           S
ANISOU 4473  SD  MET B 104     8053   7988   8178   -450    156   -353       S
ATOM   4474  CE  MET B 104     -14.026  -4.817 -61.849  1.00 54.22           C
ANISOU 4474  CE  MET B 104     6880   6749   6972   -440    143   -366       C
ATOM   4475  N   ASP B 105     -17.600  -1.496 -65.731  1.00 41.84           N
ANISOU 4475  N   ASP B 105     5287   5298   5313   -470    149   -328       N
ATOM   4476  CA  ASP B 105     -17.510  -0.430 -66.715  1.00 51.36           C
ANISOU 4476  CA  ASP B 105     6514   6512   6489   -456    153   -317       C
ATOM   4477  C   ASP B 105     -17.907   0.901 -66.103  1.00 50.85           C
ANISOU 4477  C   ASP B 105     6460   6445   6416   -439    145   -295       C
ATOM   4478  O   ASP B 105     -17.256   1.919 -66.351  1.00 56.59           O
ANISOU 4478  O   ASP B 105     7215   7156   7131   -435    161   -280       O
ATOM   4479  CB  ASP B 105     -18.406  -0.759 -67.912  1.00 52.59           C
ANISOU 4479  CB  ASP B 105     6674   6696   6611   -447    142   -333       C
ATOM   4480  CG  ASP B 105     -17.711  -1.593 -68.959  1.00 49.69           C
ANISOU 4480  CG  ASP B 105     6313   6327   6241   -459    158   -347       C
ATOM   4481  OD1 ASP B 105     -16.563  -2.027 -68.748  1.00 58.28           O
ANISOU 4481  OD1 ASP B 105     7396   7393   7353   -474    177   -349       O
ATOM   4482  OD2 ASP B 105     -18.335  -1.830 -70.002  1.00 63.49           O
ANISOU 4482  OD2 ASP B 105     8066   8097   7959   -450    150   -361       O
ATOM   4483  N   THR B 106     -18.972   0.908 -65.292  1.00 46.50           N
ANISOU 4483  N   THR B 106     5890   5910   5869   -432    123   -298       N
ATOM   4484  CA  THR B 106     -19.443   2.145 -64.671  1.00 52.33           C
ANISOU 4484  CA  THR B 106     6637   6649   6599   -411    110   -281       C
ATOM   4485  C   THR B 106     -18.498   2.607 -63.564  1.00 53.07           C
ANISOU 4485  C   THR B 106     6730   6712   6723   -423    125   -262       C
ATOM   4486  O   THR B 106     -18.288   3.811 -63.357  1.00 49.25           O
ANISOU 4486  O   THR B 106     6269   6215   6230   -411    129   -243       O
ATOM   4487  CB  THR B 106     -20.857   1.937 -64.118  1.00 52.59           C
ANISOU 4487  CB  THR B 106     6640   6715   6628   -404     85   -301       C
ATOM   4488  OG1 THR B 106     -21.730   1.489 -65.167  1.00 46.96           O
ANISOU 4488  OG1 THR B 106     5918   6040   5886   -393     70   -330       O
ATOM   4489  CG2 THR B 106     -21.402   3.244 -63.527  1.00 51.16           C
ANISOU 4489  CG2 THR B 106     6466   6539   6434   -375     67   -287       C
ATOM   4490  N   ARG B 107     -17.933   1.666 -62.823  1.00 50.46           N
ANISOU 4490  N   ARG B 107     6379   6368   6425   -442    132   -270       N
ATOM   4491  CA  ARG B 107     -16.940   2.045 -61.840  1.00 48.63           C
ANISOU 4491  CA  ARG B 107     6144   6113   6221   -447    142   -260       C
ATOM   4492  C   ARG B 107     -15.766   2.718 -62.527  1.00 49.56           C
ANISOU 4492  C   ARG B 107     6277   6220   6333   -453    168   -260       C
ATOM   4493  O   ARG B 107     -15.456   3.885 -62.250  1.00 46.05           O
ANISOU 4493  O   ARG B 107     5847   5765   5885   -453    179   -247       O
ATOM   4494  CB  ARG B 107     -16.503   0.818 -61.043  1.00 50.57           C
ANISOU 4494  CB  ARG B 107     6376   6345   6493   -455    140   -274       C
ATOM   4495  CG  ARG B 107     -15.331   1.058 -60.129  1.00 44.07           C
ANISOU 4495  CG  ARG B 107     5545   5504   5695   -449    146   -276       C
ATOM   4496  CD  ARG B 107     -14.756  -0.250 -59.669  1.00 42.36           C
ANISOU 4496  CD  ARG B 107     5330   5273   5494   -443    140   -295       C
ATOM   4497  NE  ARG B 107     -15.769  -1.181 -59.165  1.00 39.68           N
ANISOU 4497  NE  ARG B 107     5006   4923   5148   -450    130   -294       N
ATOM   4498  CZ  ARG B 107     -16.254  -1.155 -57.927  1.00 43.27           C
ANISOU 4498  CZ  ARG B 107     5469   5364   5609   -450    121   -285       C
ATOM   4499  NH1 ARG B 107     -15.842  -0.228 -57.056  1.00 45.84           N
ANISOU 4499  NH1 ARG B 107     5783   5685   5947   -437    117   -273       N
ATOM   4500  NH2 ARG B 107     -17.159  -2.049 -57.553  1.00 37.58           N
ANISOU 4500  NH2 ARG B 107     4768   4632   4878   -467    122   -291       N
ATOM   4501  N   LEU B 108     -15.147   2.012 -63.485  1.00 47.54           N
ANISOU 4501  N   LEU B 108     6022   5968   6074   -462    182   -277       N
ATOM   4502  CA  LEU B 108     -13.945   2.511 -64.146  1.00 41.78           C
ANISOU 4502  CA  LEU B 108     5302   5231   5340   -478    214   -288       C
ATOM   4503  C   LEU B 108     -14.197   3.835 -64.856  1.00 53.73           C
ANISOU 4503  C   LEU B 108     6862   6736   6816   -480    231   -269       C
ATOM   4504  O   LEU B 108     -13.311   4.697 -64.909  1.00 62.42           O
ANISOU 4504  O   LEU B 108     7980   7823   7914   -501    264   -273       O
ATOM   4505  CB  LEU B 108     -13.418   1.471 -65.130  1.00 41.45           C
ANISOU 4505  CB  LEU B 108     5254   5198   5297   -487    224   -312       C
ATOM   4506  CG  LEU B 108     -12.708   0.299 -64.448  1.00 47.85           C
ANISOU 4506  CG  LEU B 108     6032   6009   6141   -481    215   -338       C
ATOM   4507  CD1 LEU B 108     -11.953  -0.547 -65.438  1.00 43.81           C
ANISOU 4507  CD1 LEU B 108     5513   5506   5627   -487    228   -367       C
ATOM   4508  CD2 LEU B 108     -11.787   0.774 -63.369  1.00 37.08           C
ANISOU 4508  CD2 LEU B 108     4646   4640   4802   -479    220   -350       C
ATOM   4509  N   ASP B 109     -15.397   4.020 -65.405  1.00 51.82           N
ANISOU 4509  N   ASP B 109     6645   6502   6541   -457    209   -254       N
ATOM   4510  CA  ASP B 109     -15.735   5.306 -66.004  1.00 54.90           C
ANISOU 4510  CA  ASP B 109     7095   6878   6885   -444    217   -235       C
ATOM   4511  C   ASP B 109     -15.548   6.439 -65.013  1.00 60.25           C
ANISOU 4511  C   ASP B 109     7786   7535   7570   -445    225   -219       C
ATOM   4512  O   ASP B 109     -15.109   7.533 -65.383  1.00 63.93           O
ANISOU 4512  O   ASP B 109     8308   7975   8008   -456    255   -210       O
ATOM   4513  CB  ASP B 109     -17.175   5.285 -66.513  1.00 60.94           C
ANISOU 4513  CB  ASP B 109     7874   7664   7615   -403    179   -230       C
ATOM   4514  CG  ASP B 109     -17.311   4.554 -67.832  1.00 63.03           C
ANISOU 4514  CG  ASP B 109     8150   7944   7855   -399    178   -245       C
ATOM   4515  OD1 ASP B 109     -16.268   4.167 -68.408  1.00 65.96           O
ANISOU 4515  OD1 ASP B 109     8525   8305   8233   -429    211   -255       O
ATOM   4516  OD2 ASP B 109     -18.455   4.362 -68.285  1.00 63.43           O
ANISOU 4516  OD2 ASP B 109     8200   8022   7879   -366    145   -253       O
ATOM   4517  N   PHE B 110     -15.877   6.192 -63.743  1.00 62.54           N
ANISOU 4517  N   PHE B 110     8031   7834   7896   -439    202   -217       N
ATOM   4518  CA  PHE B 110     -15.678   7.183 -62.693  1.00 49.16           C
ANISOU 4518  CA  PHE B 110     6341   6124   6214   -441    207   -204       C
ATOM   4519  C   PHE B 110     -14.222   7.221 -62.231  1.00 42.93           C
ANISOU 4519  C   PHE B 110     5530   5324   5457   -477    242   -223       C
ATOM   4520  O   PHE B 110     -13.627   8.296 -62.116  1.00 49.27           O
ANISOU 4520  O   PHE B 110     6362   6106   6251   -496    273   -221       O
ATOM   4521  CB  PHE B 110     -16.619   6.888 -61.527  1.00 51.02           C
ANISOU 4521  CB  PHE B 110     6539   6375   6471   -421    170   -199       C
ATOM   4522  CG  PHE B 110     -16.558   7.897 -60.433  1.00 52.07           C
ANISOU 4522  CG  PHE B 110     6676   6493   6614   -418    170   -185       C
ATOM   4523  CD1 PHE B 110     -16.705   9.243 -60.706  1.00 52.91           C
ANISOU 4523  CD1 PHE B 110     6838   6579   6687   -407    180   -167       C
ATOM   4524  CD2 PHE B 110     -16.337   7.505 -59.129  1.00 55.26           C
ANISOU 4524  CD2 PHE B 110     7037   6899   7059   -425    162   -189       C
ATOM   4525  CE1 PHE B 110     -16.650  10.175 -59.690  1.00 47.96           C
ANISOU 4525  CE1 PHE B 110     6217   5938   6070   -406    182   -155       C
ATOM   4526  CE2 PHE B 110     -16.287   8.435 -58.104  1.00 47.43           C
ANISOU 4526  CE2 PHE B 110     6048   5896   6078   -422    162   -177       C
ATOM   4527  CZ  PHE B 110     -16.438   9.766 -58.391  1.00 49.93           C
ANISOU 4527  CZ  PHE B 110     6412   6194   6363   -415    172   -161       C
ATOM   4528  N   ALA B 111     -13.621   6.063 -61.981  1.00 40.38           N
ANISOU 4528  N   ALA B 111     5159   5016   5168   -485    239   -247       N
ATOM   4529  CA  ALA B 111     -12.239   6.054 -61.508  1.00 49.45           C
ANISOU 4529  CA  ALA B 111     6277   6166   6346   -509    264   -277       C
ATOM   4530  C   ALA B 111     -11.299   6.693 -62.523  1.00 58.52           C
ANISOU 4530  C   ALA B 111     7453   7307   7473   -546    315   -297       C
ATOM   4531  O   ALA B 111     -10.291   7.302 -62.144  1.00 53.50           O
ANISOU 4531  O   ALA B 111     6805   6671   6851   -575    347   -323       O
ATOM   4532  CB  ALA B 111     -11.799   4.624 -61.195  1.00 45.62           C
ANISOU 4532  CB  ALA B 111     5747   5697   5891   -498    245   -304       C
ATOM   4533  N   ARG B 112     -11.628   6.578 -63.813  1.00 58.01           N
ANISOU 4533  N   ARG B 112     7428   7239   7374   -548    325   -289       N
ATOM   4534  CA  ARG B 112     -10.805   7.174 -64.857  1.00 61.41           C
ANISOU 4534  CA  ARG B 112     7899   7658   7777   -588    379   -307       C
ATOM   4535  C   ARG B 112     -10.658   8.675 -64.649  1.00 63.62           C
ANISOU 4535  C   ARG B 112     8233   7906   8032   -612    414   -295       C
ATOM   4536  O   ARG B 112      -9.554   9.220 -64.766  1.00 68.81           O
ANISOU 4536  O   ARG B 112     8897   8559   8691   -662    469   -329       O
ATOM   4537  CB  ARG B 112     -11.403   6.884 -66.237  1.00 63.14           C
ANISOU 4537  CB  ARG B 112     8165   7872   7953   -578    377   -293       C
ATOM   4538  CG  ARG B 112     -10.719   5.749 -66.979  1.00 71.01           C
ANISOU 4538  CG  ARG B 112     9126   8891   8962   -592    388   -327       C
ATOM   4539  CD  ARG B 112     -11.156   5.678 -68.445  1.00 70.83           C
ANISOU 4539  CD  ARG B 112     9161   8861   8891   -590    397   -316       C
ATOM   4540  NE  ARG B 112     -12.492   5.106 -68.586  1.00 68.27           N
ANISOU 4540  NE  ARG B 112     8837   8548   8556   -542    344   -290       N
ATOM   4541  CZ  ARG B 112     -12.767   3.804 -68.512  1.00 71.82           C
ANISOU 4541  CZ  ARG B 112     9235   9022   9031   -527    313   -302       C
ATOM   4542  NH1 ARG B 112     -11.795   2.914 -68.301  1.00 63.75           N
ANISOU 4542  NH1 ARG B 112     8162   8013   8046   -544    323   -335       N
ATOM   4543  NH2 ARG B 112     -14.021   3.385 -68.652  1.00 77.63           N
ANISOU 4543  NH2 ARG B 112     9972   9771   9754   -493    272   -287       N
ATOM   4544  N   VAL B 113     -11.763   9.369 -64.357  1.00 53.95           N
ANISOU 4544  N   VAL B 113     7053   6662   6783   -578    386   -254       N
ATOM   4545  CA  VAL B 113     -11.645  10.820 -64.239  1.00 57.84           C
ANISOU 4545  CA  VAL B 113     7615   7117   7245   -597    421   -240       C
ATOM   4546  C   VAL B 113     -10.990  11.200 -62.916  1.00 60.10           C
ANISOU 4546  C   VAL B 113     7852   7409   7575   -618    431   -258       C
ATOM   4547  O   VAL B 113     -10.244  12.185 -62.853  1.00 58.56           O
ANISOU 4547  O   VAL B 113     7690   7191   7367   -664    484   -274       O
ATOM   4548  CB  VAL B 113     -13.009  11.515 -64.435  1.00 49.86           C
ANISOU 4548  CB  VAL B 113     6675   6084   6186   -544    386   -196       C
ATOM   4549  CG1 VAL B 113     -13.731  10.900 -65.619  1.00 44.19           C
ANISOU 4549  CG1 VAL B 113     5984   5376   5432   -511    361   -187       C
ATOM   4550  CG2 VAL B 113     -13.864  11.468 -63.170  1.00 53.55           C
ANISOU 4550  CG2 VAL B 113     7094   6568   6683   -504    333   -179       C
ATOM   4551  N   CYS B 114     -11.208  10.416 -61.852  1.00 65.60           N
ANISOU 4551  N   CYS B 114     8471   8135   8318   -590    385   -261       N
ATOM   4552  CA  CYS B 114     -10.642  10.783 -60.556  1.00 66.56           C
ANISOU 4552  CA  CYS B 114     8549   8263   8478   -602    388   -278       C
ATOM   4553  C   CYS B 114      -9.136  10.561 -60.530  1.00 63.28           C
ANISOU 4553  C   CYS B 114     8084   7870   8090   -647    430   -338       C
ATOM   4554  O   CYS B 114      -8.411  11.315 -59.879  1.00 70.59           O
ANISOU 4554  O   CYS B 114     8997   8795   9029   -678    460   -365       O
ATOM   4555  CB  CYS B 114     -11.335  10.008 -59.427  1.00 63.63           C
ANISOU 4555  CB  CYS B 114     8124   7912   8142   -557    329   -263       C
ATOM   4556  SG  CYS B 114     -13.097  10.434 -59.206  1.00 61.29           S
ANISOU 4556  SG  CYS B 114     7868   7601   7818   -509    283   -209       S
ATOM   4557  N   TYR B 115      -8.640   9.555 -61.236  1.00 60.26           N
ANISOU 4557  N   TYR B 115     7671   7511   7715   -652    433   -367       N
ATOM   4558  CA  TYR B 115      -7.200   9.388 -61.300  1.00 65.04           C
ANISOU 4558  CA  TYR B 115     8225   8145   8342   -692    473   -437       C
ATOM   4559  C   TYR B 115      -6.558  10.240 -62.384  1.00 64.17           C
ANISOU 4559  C   TYR B 115     8168   8017   8195   -759    549   -460       C
ATOM   4560  O   TYR B 115      -5.329  10.331 -62.433  1.00 69.14           O
ANISOU 4560  O   TYR B 115     8757   8674   8840   -807    595   -528       O
ATOM   4561  CB  TYR B 115      -6.859   7.927 -61.534  1.00 60.47           C
ANISOU 4561  CB  TYR B 115     7589   7600   7786   -665    444   -466       C
ATOM   4562  CG  TYR B 115      -7.031   7.056 -60.301  1.00 59.94           C
ANISOU 4562  CG  TYR B 115     7467   7550   7756   -611    383   -466       C
ATOM   4563  CD1 TYR B 115      -6.135   7.133 -59.230  1.00 50.88           C
ANISOU 4563  CD1 TYR B 115     6262   6429   6640   -606    379   -513       C
ATOM   4564  CD2 TYR B 115      -8.081   6.151 -60.215  1.00 55.10           C
ANISOU 4564  CD2 TYR B 115     6866   6928   7141   -566    333   -423       C
ATOM   4565  CE1 TYR B 115      -6.282   6.329 -58.122  1.00 52.55           C
ANISOU 4565  CE1 TYR B 115     6440   6649   6876   -551    324   -512       C
ATOM   4566  CE2 TYR B 115      -8.235   5.342 -59.117  1.00 58.29           C
ANISOU 4566  CE2 TYR B 115     7238   7338   7570   -522    286   -423       C
ATOM   4567  CZ  TYR B 115      -7.336   5.442 -58.068  1.00 57.50           C
ANISOU 4567  CZ  TYR B 115     7093   7257   7497   -511    280   -465       C
ATOM   4568  OH  TYR B 115      -7.486   4.638 -56.966  1.00 56.20           O
ANISOU 4568  OH  TYR B 115     6912   7092   7349   -462    233   -463       O
ATOM   4569  N   ASN B 116      -7.351  10.827 -63.247  1.00 62.91           N
ANISOU 4569  N   ASN B 116     8102   7816   7986   -761    562   -412       N
ATOM   4570  CA  ASN B 116      -6.831  11.669 -64.304  1.00 69.29           C
ANISOU 4570  CA  ASN B 116     8985   8594   8747   -824    637   -428       C
ATOM   4571  C   ASN B 116      -6.362  12.988 -63.707  1.00 75.16           C
ANISOU 4571  C   ASN B 116     9762   9313   9483   -873    688   -443       C
ATOM   4572  O   ASN B 116      -7.090  13.588 -62.909  1.00 73.78           O
ANISOU 4572  O   ASN B 116     9611   9116   9307   -841    658   -401       O
ATOM   4573  CB  ASN B 116      -7.926  11.906 -65.336  1.00 73.12           C
ANISOU 4573  CB  ASN B 116     9573   9038   9173   -795    625   -369       C
ATOM   4574  CG  ASN B 116      -7.424  12.591 -66.571  1.00 69.62           C
ANISOU 4574  CG  ASN B 116     9223   8558   8672   -854    701   -382       C
ATOM   4575  OD1 ASN B 116      -6.900  13.701 -66.507  1.00 70.26           O
ANISOU 4575  OD1 ASN B 116     9362   8605   8728   -910    765   -398       O
ATOM   4576  ND2 ASN B 116      -7.598  11.940 -67.715  1.00 63.46           N
ANISOU 4576  ND2 ASN B 116     8467   7780   7866   -844    699   -378       N
ATOM   4577  N   PRO B 117      -5.164  13.468 -64.050  1.00 79.15           N
ANISOU 4577  N   PRO B 117    10268   9823   9982   -954    768   -507       N
ATOM   4578  CA  PRO B 117      -4.705  14.750 -63.482  1.00 79.60           C
ANISOU 4578  CA  PRO B 117    10361   9854  10030  -1011    825   -527       C
ATOM   4579  C   PRO B 117      -5.564  15.931 -63.895  1.00 79.46           C
ANISOU 4579  C   PRO B 117    10489   9757   9944  -1011    846   -462       C
ATOM   4580  O   PRO B 117      -5.611  16.933 -63.170  1.00 84.05           O
ANISOU 4580  O   PRO B 117    11105  10310  10519  -1027    864   -454       O
ATOM   4581  CB  PRO B 117      -3.268  14.878 -64.009  1.00 75.29           C
ANISOU 4581  CB  PRO B 117     9787   9334   9484  -1107    915   -619       C
ATOM   4582  CG  PRO B 117      -2.861  13.477 -64.331  1.00 79.84           C
ANISOU 4582  CG  PRO B 117    10266   9973  10098  -1080    880   -657       C
ATOM   4583  CD  PRO B 117      -4.109  12.795 -64.822  1.00 75.32           C
ANISOU 4583  CD  PRO B 117     9734   9377   9506  -1001    810   -575       C
ATOM   4584  N   ASP B 118      -6.259  15.834 -65.025  1.00 77.08           N
ANISOU 4584  N   ASP B 118    10277   9421   9590   -985    839   -417       N
ATOM   4585  CA  ASP B 118      -7.200  16.846 -65.476  1.00 78.41           C
ANISOU 4585  CA  ASP B 118    10592   9515   9685   -960    842   -355       C
ATOM   4586  C   ASP B 118      -8.587  16.672 -64.865  1.00 75.70           C
ANISOU 4586  C   ASP B 118    10239   9174   9348   -858    745   -291       C
ATOM   4587  O   ASP B 118      -9.571  17.167 -65.437  1.00 68.36           O
ANISOU 4587  O   ASP B 118     9417   8199   8357   -808    723   -240       O
ATOM   4588  CB  ASP B 118      -7.300  16.820 -67.000  1.00 84.20           C
ANISOU 4588  CB  ASP B 118    11429  10213  10351   -971    876   -343       C
ATOM   4589  CG  ASP B 118      -6.045  17.310 -67.669  1.00 92.38           C
ANISOU 4589  CG  ASP B 118    12512  11229  11360  -1083    988   -402       C
ATOM   4590  OD1 ASP B 118      -5.645  18.469 -67.420  1.00 97.32           O
ANISOU 4590  OD1 ASP B 118    13215  11808  11956  -1143   1055   -415       O
ATOM   4591  OD2 ASP B 118      -5.453  16.525 -68.436  1.00 93.62           O
ANISOU 4591  OD2 ASP B 118    12627  11419  11526  -1114   1011   -441       O
ATOM   4592  N   PHE B 119      -8.678  15.984 -63.718  1.00 66.60           N
ANISOU 4592  N   PHE B 119     8965   8074   8265   -825    689   -298       N
ATOM   4593  CA  PHE B 119      -9.969  15.728 -63.092  1.00 59.77           C
ANISOU 4593  CA  PHE B 119     8081   7219   7412   -739    603   -248       C
ATOM   4594  C   PHE B 119     -10.804  16.997 -62.994  1.00 52.61           C
ANISOU 4594  C   PHE B 119     7285   6254   6449   -709    599   -203       C
ATOM   4595  O   PHE B 119     -12.001  16.987 -63.310  1.00 47.27           O
ANISOU 4595  O   PHE B 119     6653   5570   5739   -637    544   -162       O
ATOM   4596  CB  PHE B 119      -9.759  15.112 -61.709  1.00 60.22           C
ANISOU 4596  CB  PHE B 119     8013   7324   7542   -726    564   -267       C
ATOM   4597  CG  PHE B 119     -10.888  15.353 -60.747  1.00 54.75           C
ANISOU 4597  CG  PHE B 119     7315   6629   6858   -664    502   -224       C
ATOM   4598  CD1 PHE B 119     -12.044  14.563 -60.794  1.00 51.43           C
ANISOU 4598  CD1 PHE B 119     6872   6230   6440   -597    433   -193       C
ATOM   4599  CD2 PHE B 119     -10.791  16.357 -59.777  1.00 45.64           C
ANISOU 4599  CD2 PHE B 119     6175   5455   5710   -676    515   -221       C
ATOM   4600  CE1 PHE B 119     -13.103  14.770 -59.885  1.00 56.86           C
ANISOU 4600  CE1 PHE B 119     7548   6922   7135   -545    380   -163       C
ATOM   4601  CE2 PHE B 119     -11.846  16.569 -58.855  1.00 56.26           C
ANISOU 4601  CE2 PHE B 119     7511   6802   7064   -618    457   -185       C
ATOM   4602  CZ  PHE B 119     -13.008  15.776 -58.917  1.00 56.10           C
ANISOU 4602  CZ  PHE B 119     7466   6806   7045   -553    390   -157       C
ATOM   4603  N   GLU B 120     -10.188  18.105 -62.582  1.00 49.61           N
ANISOU 4603  N   GLU B 120     6954   5838   6057   -762    657   -217       N
ATOM   4604  CA  GLU B 120     -10.966  19.323 -62.389  1.00 58.46           C
ANISOU 4604  CA  GLU B 120     8186   6902   7125   -727    650   -175       C
ATOM   4605  C   GLU B 120     -11.665  19.740 -63.677  1.00 71.89           C
ANISOU 4605  C   GLU B 120    10028   8551   8738   -689    650   -140       C
ATOM   4606  O   GLU B 120     -12.855  20.078 -63.659  1.00 77.49           O
ANISOU 4606  O   GLU B 120    10789   9244   9409   -605    590    -99       O
ATOM   4607  CB  GLU B 120     -10.077  20.446 -61.858  1.00 50.51           C
ANISOU 4607  CB  GLU B 120     7221   5857   6113   -803    725   -201       C
ATOM   4608  CG  GLU B 120     -10.147  20.607 -60.353  1.00 65.09           C
ANISOU 4608  CG  GLU B 120     8982   7732   8018   -790    692   -204       C
ATOM   4609  CD  GLU B 120     -11.573  20.699 -59.829  1.00 71.12           C
ANISOU 4609  CD  GLU B 120     9755   8495   8774   -692    606   -150       C
ATOM   4610  OE1 GLU B 120     -11.853  20.050 -58.799  1.00 75.85           O
ANISOU 4610  OE1 GLU B 120    10241   9145   9433   -660    552   -151       O
ATOM   4611  OE2 GLU B 120     -12.407  21.428 -60.423  1.00 72.40           O
ANISOU 4611  OE2 GLU B 120    10039   8606   8865   -645    594   -112       O
ATOM   4612  N   LYS B 121     -10.952  19.688 -64.811  1.00 78.03           N
ANISOU 4612  N   LYS B 121    10865   9304   9478   -744    714   -161       N
ATOM   4613  CA  LYS B 121     -11.550  20.077 -66.086  1.00 83.18           C
ANISOU 4613  CA  LYS B 121    11663   9903  10039   -706    717   -129       C
ATOM   4614  C   LYS B 121     -12.625  19.085 -66.518  1.00 76.69           C
ANISOU 4614  C   LYS B 121    10792   9126   9219   -615    628   -107       C
ATOM   4615  O   LYS B 121     -13.668  19.482 -67.051  1.00 77.98           O
ANISOU 4615  O   LYS B 121    11051   9261   9316   -534    583    -73       O
ATOM   4616  CB  LYS B 121     -10.471  20.195 -67.168  1.00 92.15           C
ANISOU 4616  CB  LYS B 121    12871  11005  11137   -797    813   -162       C
ATOM   4617  CG  LYS B 121     -10.931  19.705 -68.553  1.00104.72           C
ANISOU 4617  CG  LYS B 121    14530  12587  12671   -756    796   -144       C
ATOM   4618  CD  LYS B 121      -9.844  19.766 -69.624  1.00109.87           C
ANISOU 4618  CD  LYS B 121    15250  13208  13286   -851    895   -180       C
ATOM   4619  CE  LYS B 121      -8.587  19.054 -69.169  1.00110.49           C
ANISOU 4619  CE  LYS B 121    15180  13350  13451   -943    941   -245       C
ATOM   4620  NZ  LYS B 121      -7.757  18.563 -70.303  1.00113.07           N
ANISOU 4620  NZ  LYS B 121    15520  13683  13760  -1010   1005   -284       N
ATOM   4621  N   LEU B 122     -12.393  17.792 -66.295  1.00 67.89           N
ANISOU 4621  N   LEU B 122     9533   8082   8178   -623    601   -131       N
ATOM   4622  CA  LEU B 122     -13.340  16.785 -66.758  1.00 63.43           C
ANISOU 4622  CA  LEU B 122     8922   7562   7616   -551    528   -117       C
ATOM   4623  C   LEU B 122     -14.601  16.722 -65.913  1.00 59.26           C
ANISOU 4623  C   LEU B 122     8348   7064   7106   -468    443    -94       C
ATOM   4624  O   LEU B 122     -15.620  16.206 -66.388  1.00 63.27           O
ANISOU 4624  O   LEU B 122     8849   7599   7594   -399    383    -84       O
ATOM   4625  CB  LEU B 122     -12.681  15.409 -66.780  1.00 60.77           C
ANISOU 4625  CB  LEU B 122     8458   7285   7348   -588    529   -152       C
ATOM   4626  CG  LEU B 122     -11.294  15.396 -67.392  1.00 54.95           C
ANISOU 4626  CG  LEU B 122     7734   6535   6610   -679    614   -191       C
ATOM   4627  CD1 LEU B 122     -10.562  14.117 -67.035  1.00 59.31           C
ANISOU 4627  CD1 LEU B 122     8144   7151   7240   -709    608   -232       C
ATOM   4628  CD2 LEU B 122     -11.431  15.587 -68.898  1.00 49.76           C
ANISOU 4628  CD2 LEU B 122     7195   5838   5873   -676    641   -180       C
ATOM   4629  N   LYS B 123     -14.556  17.220 -64.680  1.00 49.29           N
ANISOU 4629  N   LYS B 123     7049   5800   5878   -475    439    -91       N
ATOM   4630  CA  LYS B 123     -15.665  16.991 -63.764  1.00 50.80           C
ANISOU 4630  CA  LYS B 123     7173   6030   6098   -408    363    -78       C
ATOM   4631  C   LYS B 123     -16.981  17.598 -64.245  1.00 57.75           C
ANISOU 4631  C   LYS B 123     8140   6895   6907   -317    310    -54       C
ATOM   4632  O   LYS B 123     -18.016  16.915 -64.134  1.00 56.09           O
ANISOU 4632  O   LYS B 123     7863   6737   6709   -258    243    -58       O
ATOM   4633  CB  LYS B 123     -15.272  17.498 -62.372  1.00 54.21           C
ANISOU 4633  CB  LYS B 123     7561   6460   6577   -438    375    -80       C
ATOM   4634  CG  LYS B 123     -16.402  17.537 -61.368  1.00 60.07           C
ANISOU 4634  CG  LYS B 123     8254   7230   7338   -374    307    -66       C
ATOM   4635  CD  LYS B 123     -15.862  17.760 -59.960  1.00 59.43           C
ANISOU 4635  CD  LYS B 123     8108   7156   7315   -411    320    -74       C
ATOM   4636  CE  LYS B 123     -14.946  18.967 -59.902  1.00 54.68           C
ANISOU 4636  CE  LYS B 123     7588   6497   6690   -464    388    -75       C
ATOM   4637  NZ  LYS B 123     -14.399  19.170 -58.531  1.00 65.89           N
ANISOU 4637  NZ  LYS B 123     8938   7929   8167   -499    399    -89       N
ATOM   4638  N   PRO B 124     -17.031  18.823 -64.788  1.00 61.79           N
ANISOU 4638  N   PRO B 124     8798   7341   7340   -298    334    -36       N
ATOM   4639  CA  PRO B 124     -18.330  19.342 -65.257  1.00 59.43           C
ANISOU 4639  CA  PRO B 124     8579   7033   6967   -192    271    -20       C
ATOM   4640  C   PRO B 124     -18.982  18.473 -66.316  1.00 65.99           C
ANISOU 4640  C   PRO B 124     9396   7904   7773   -141    228    -31       C
ATOM   4641  O   PRO B 124     -20.192  18.223 -66.251  1.00 72.36           O
ANISOU 4641  O   PRO B 124    10164   8759   8570    -58    153    -40       O
ATOM   4642  CB  PRO B 124     -17.972  20.726 -65.807  1.00 51.72           C
ANISOU 4642  CB  PRO B 124     7785   5963   5903   -194    322      0       C
ATOM   4643  CG  PRO B 124     -16.753  21.094 -65.131  1.00 52.30           C
ANISOU 4643  CG  PRO B 124     7845   6006   6019   -297    399     -5       C
ATOM   4644  CD  PRO B 124     -15.977  19.839 -64.921  1.00 55.31           C
ANISOU 4644  CD  PRO B 124     8080   6447   6487   -367    418    -33       C
ATOM   4645  N   GLY B 125     -18.214  17.997 -67.294  1.00 61.50           N
ANISOU 4645  N   GLY B 125     8852   7320   7193   -191    275    -37       N
ATOM   4646  CA  GLY B 125     -18.792  17.133 -68.309  1.00 64.73           C
ANISOU 4646  CA  GLY B 125     9245   7769   7581   -147    236    -49       C
ATOM   4647  C   GLY B 125     -19.166  15.760 -67.779  1.00 68.49           C
ANISOU 4647  C   GLY B 125     9554   8330   8138   -152    194    -73       C
ATOM   4648  O   GLY B 125     -20.213  15.210 -68.138  1.00 70.76           O
ANISOU 4648  O   GLY B 125     9805   8667   8413    -86    132    -89       O
ATOM   4649  N   PHE B 126     -18.317  15.182 -66.924  1.00 64.98           N
ANISOU 4649  N   PHE B 126     9012   7903   7776   -228    227    -81       N
ATOM   4650  CA  PHE B 126     -18.646  13.876 -66.371  1.00 57.14           C
ANISOU 4650  CA  PHE B 126     7879   6978   6853   -234    191   -101       C
ATOM   4651  C   PHE B 126     -19.897  13.936 -65.502  1.00 58.15           C
ANISOU 4651  C   PHE B 126     7955   7146   6993   -174    127   -106       C
ATOM   4652  O   PHE B 126     -20.654  12.962 -65.435  1.00 66.58           O
ANISOU 4652  O   PHE B 126     8941   8272   8086   -154     85   -128       O
ATOM   4653  CB  PHE B 126     -17.479  13.308 -65.575  1.00 53.91           C
ANISOU 4653  CB  PHE B 126     7389   6574   6520   -315    235   -111       C
ATOM   4654  CG  PHE B 126     -17.796  11.994 -64.947  1.00 55.21           C
ANISOU 4654  CG  PHE B 126     7433   6796   6749   -319    201   -129       C
ATOM   4655  CD1 PHE B 126     -17.721  10.825 -65.691  1.00 48.10           C
ANISOU 4655  CD1 PHE B 126     6493   5923   5859   -329    198   -147       C
ATOM   4656  CD2 PHE B 126     -18.238  11.930 -63.632  1.00 48.69           C
ANISOU 4656  CD2 PHE B 126     6543   5992   5967   -311    173   -129       C
ATOM   4657  CE1 PHE B 126     -18.040   9.609 -65.130  1.00 48.60           C
ANISOU 4657  CE1 PHE B 126     6462   6031   5974   -335    171   -164       C
ATOM   4658  CE2 PHE B 126     -18.568  10.721 -63.060  1.00 50.28           C
ANISOU 4658  CE2 PHE B 126     6650   6236   6216   -317    148   -146       C
ATOM   4659  CZ  PHE B 126     -18.469   9.556 -63.809  1.00 56.43           C
ANISOU 4659  CZ  PHE B 126     7398   7038   7004   -330    148   -163       C
ATOM   4660  N   LEU B 127     -20.141  15.069 -64.843  1.00 56.24           N
ANISOU 4660  N   LEU B 127     7762   6876   6731   -148    120    -90       N
ATOM   4661  CA  LEU B 127     -21.370  15.219 -64.069  1.00 43.48           C
ANISOU 4661  CA  LEU B 127     6100   5301   5119    -86     59   -100       C
ATOM   4662  C   LEU B 127     -22.598  15.149 -64.965  1.00 50.17           C
ANISOU 4662  C   LEU B 127     6970   6185   5907      1     -0   -122       C
ATOM   4663  O   LEU B 127     -23.623  14.582 -64.582  1.00 54.09           O
ANISOU 4663  O   LEU B 127     7382   6748   6424     34    -50   -153       O
ATOM   4664  CB  LEU B 127     -21.335  16.533 -63.290  1.00 47.93           C
ANISOU 4664  CB  LEU B 127     6724   5822   5666    -71     65    -79       C
ATOM   4665  CG  LEU B 127     -20.392  16.545 -62.069  1.00 53.66           C
ANISOU 4665  CG  LEU B 127     7394   6533   6460   -146    107    -70       C
ATOM   4666  CD1 LEU B 127     -20.188  17.937 -61.562  1.00 47.38           C
ANISOU 4666  CD1 LEU B 127     6682   5684   5637   -140    126    -49       C
ATOM   4667  CD2 LEU B 127     -20.902  15.630 -60.950  1.00 56.58           C
ANISOU 4667  CD2 LEU B 127     7635   6965   6900   -153     74    -88       C
ATOM   4668  N   LYS B 128     -22.502  15.679 -66.183  1.00 58.12           N
ANISOU 4668  N   LYS B 128     8092   7152   6838     36      6   -112       N
ATOM   4669  CA  LYS B 128     -23.645  15.653 -67.088  1.00 58.88           C
ANISOU 4669  CA  LYS B 128     8216   7285   6870    130    -55   -138       C
ATOM   4670  C   LYS B 128     -23.927  14.252 -67.638  1.00 61.06           C
ANISOU 4670  C   LYS B 128     8398   7625   7176    115    -71   -171       C
ATOM   4671  O   LYS B 128     -25.045  13.998 -68.108  1.00 51.01           O
ANISOU 4671  O   LYS B 128     7102   6410   5871    188   -131   -209       O
ATOM   4672  CB  LYS B 128     -23.411  16.657 -68.219  1.00 61.69           C
ANISOU 4672  CB  LYS B 128     8742   7570   7128    176    -42   -115       C
ATOM   4673  CG  LYS B 128     -23.294  18.106 -67.752  1.00 59.53           C
ANISOU 4673  CG  LYS B 128     8582   7227   6809    202    -30    -86       C
ATOM   4674  N   GLU B 129     -22.949  13.336 -67.578  1.00 65.34           N
ANISOU 4674  N   GLU B 129     8885   8163   7779     25    -21   -163       N
ATOM   4675  CA  GLU B 129     -23.173  11.956 -67.994  1.00 63.23           C
ANISOU 4675  CA  GLU B 129     8528   7951   7544      4    -32   -194       C
ATOM   4676  C   GLU B 129     -23.856  11.115 -66.922  1.00 60.93           C
ANISOU 4676  C   GLU B 129     8109   7724   7319    -13    -58   -224       C
ATOM   4677  O   GLU B 129     -24.348  10.023 -67.233  1.00 59.65           O
ANISOU 4677  O   GLU B 129     7877   7615   7174    -20    -75   -259       O
ATOM   4678  CB  GLU B 129     -21.853  11.264 -68.355  1.00 67.78           C
ANISOU 4678  CB  GLU B 129     9098   8497   8156    -80     30   -179       C
ATOM   4679  CG  GLU B 129     -20.830  12.080 -69.122  1.00 74.59           C
ANISOU 4679  CG  GLU B 129    10079   9288   8973   -101     82   -150       C
ATOM   4680  CD  GLU B 129     -19.547  11.284 -69.382  1.00 79.74           C
ANISOU 4680  CD  GLU B 129    10700   9927   9669   -187    141   -150       C
ATOM   4681  OE1 GLU B 129     -18.441  11.829 -69.168  1.00 80.20           O
ANISOU 4681  OE1 GLU B 129    10797   9938   9736   -242    198   -134       O
ATOM   4682  OE2 GLU B 129     -19.649  10.104 -69.793  1.00 80.52           O
ANISOU 4682  OE2 GLU B 129    10734  10067   9794   -198    130   -171       O
ATOM   4683  N   ILE B 130     -23.868  11.577 -65.675  1.00 58.00           N
ANISOU 4683  N   ILE B 130     7711   7345   6980    -26    -57   -213       N
ATOM   4684  CA  ILE B 130     -24.321  10.771 -64.540  1.00 55.35           C
ANISOU 4684  CA  ILE B 130     7265   7056   6708    -58    -67   -236       C
ATOM   4685  C   ILE B 130     -25.821  10.493 -64.642  1.00 56.06           C
ANISOU 4685  C   ILE B 130     7301   7221   6777     -2   -123   -290       C
ATOM   4686  O   ILE B 130     -26.238   9.350 -64.406  1.00 62.34           O
ANISOU 4686  O   ILE B 130     8011   8064   7610    -38   -125   -325       O
ATOM   4687  CB  ILE B 130     -23.933  11.437 -63.197  1.00 52.98           C
ANISOU 4687  CB  ILE B 130     6961   6727   6444    -82    -51   -211       C
ATOM   4688  CG1 ILE B 130     -22.404  11.581 -63.092  1.00 48.83           C
ANISOU 4688  CG1 ILE B 130     6471   6140   5944   -144      7   -173       C
ATOM   4689  CG2 ILE B 130     -24.497  10.672 -61.950  1.00 34.68           C
ANISOU 4689  CG2 ILE B 130     4540   4453   4182   -112    -62   -235       C
ATOM   4690  CD1 ILE B 130     -21.881  11.930 -61.687  1.00 35.13           C
ANISOU 4690  CD1 ILE B 130     4708   4383   4256   -180     27   -156       C
ATOM   4691  N   PRO B 131     -26.677  11.467 -64.978  1.00 54.30           N
ANISOU 4691  N   PRO B 131     7123   7014   6493     85   -170   -305       N
ATOM   4692  CA  PRO B 131     -28.116  11.151 -65.028  1.00 50.51           C
ANISOU 4692  CA  PRO B 131     6574   6621   5997    137   -225   -373       C
ATOM   4693  C   PRO B 131     -28.483  10.034 -65.984  1.00 56.76           C
ANISOU 4693  C   PRO B 131     7320   7462   6782    130   -234   -416       C
ATOM   4694  O   PRO B 131     -29.361   9.226 -65.657  1.00 60.23           O
ANISOU 4694  O   PRO B 131     7663   7975   7247    114   -249   -475       O
ATOM   4695  CB  PRO B 131     -28.744  12.481 -65.443  1.00 45.28           C
ANISOU 4695  CB  PRO B 131     5993   5956   5257    246   -275   -379       C
ATOM   4696  CG  PRO B 131     -27.860  13.471 -64.852  1.00 49.96           C
ANISOU 4696  CG  PRO B 131     6663   6468   5853    229   -242   -317       C
ATOM   4697  CD  PRO B 131     -26.465  12.925 -65.026  1.00 54.04           C
ANISOU 4697  CD  PRO B 131     7198   6926   6409    137   -175   -271       C
ATOM   4698  N   GLU B 132     -27.848   9.944 -67.154  1.00 62.38           N
ANISOU 4698  N   GLU B 132     8100   8140   7463    136   -219   -393       N
ATOM   4699  CA  GLU B 132     -28.236   8.879 -68.074  1.00 60.26           C
ANISOU 4699  CA  GLU B 132     7787   7922   7188    131   -229   -437       C
ATOM   4700  C   GLU B 132     -27.719   7.525 -67.590  1.00 58.44           C
ANISOU 4700  C   GLU B 132     7480   7694   7032     28   -183   -437       C
ATOM   4701  O   GLU B 132     -28.412   6.511 -67.725  1.00 61.11           O
ANISOU 4701  O   GLU B 132     7741   8092   7385      9   -192   -492       O
ATOM   4702  CB  GLU B 132     -27.763   9.198 -69.493  1.00 68.37           C
ANISOU 4702  CB  GLU B 132     8913   8911   8152    172   -230   -415       C
ATOM   4703  CG  GLU B 132     -26.327   8.784 -69.784  1.00 89.74           C
ANISOU 4703  CG  GLU B 132    11659  11550  10890     93   -165   -362       C
ATOM   4704  CD  GLU B 132     -25.615   9.729 -70.731  1.00101.85           C
ANISOU 4704  CD  GLU B 132    13326  13014  12358    125   -149   -319       C
ATOM   4705  OE1 GLU B 132     -26.298  10.507 -71.436  1.00109.86           O
ANISOU 4705  OE1 GLU B 132    14413  14035  13295    218   -193   -332       O
ATOM   4706  OE2 GLU B 132     -24.363   9.705 -70.745  1.00103.30           O
ANISOU 4706  OE2 GLU B 132    13547  13138  12566     58    -90   -277       O
ATOM   4707  N   LYS B 133     -26.528   7.487 -66.979  1.00 58.67           N
ANISOU 4707  N   LYS B 133     7529   7658   7105    -36   -133   -382       N
ATOM   4708  CA  LYS B 133     -26.045   6.233 -66.399  1.00 53.60           C
ANISOU 4708  CA  LYS B 133     6824   7014   6528   -120    -96   -384       C
ATOM   4709  C   LYS B 133     -27.034   5.701 -65.371  1.00 56.72           C
ANISOU 4709  C   LYS B 133     7134   7463   6955   -142   -108   -429       C
ATOM   4710  O   LYS B 133     -27.495   4.559 -65.473  1.00 66.37           O
ANISOU 4710  O   LYS B 133     8299   8724   8194   -179   -102   -472       O
ATOM   4711  CB  LYS B 133     -24.666   6.421 -65.766  1.00 49.60           C
ANISOU 4711  CB  LYS B 133     6349   6437   6058   -171    -50   -328       C
ATOM   4712  CG  LYS B 133     -23.584   6.897 -66.723  1.00 57.11           C
ANISOU 4712  CG  LYS B 133     7381   7337   6983   -168    -24   -291       C
ATOM   4713  CD  LYS B 133     -22.323   7.283 -65.961  1.00 56.63           C
ANISOU 4713  CD  LYS B 133     7341   7219   6958   -214     18   -250       C
ATOM   4714  CE  LYS B 133     -21.184   6.340 -66.247  1.00 58.33           C
ANISOU 4714  CE  LYS B 133     7542   7413   7206   -270     58   -245       C
ATOM   4715  NZ  LYS B 133     -20.477   6.690 -67.497  1.00 60.05           N
ANISOU 4715  NZ  LYS B 133     7828   7603   7385   -267     81   -233       N
ATOM   4716  N   MET B 134     -27.390   6.532 -64.381  1.00 49.84           N
ANISOU 4716  N   MET B 134     6257   6592   6088   -123   -122   -424       N
ATOM   4717  CA  MET B 134     -28.345   6.118 -63.355  1.00 48.30           C
ANISOU 4717  CA  MET B 134     5985   6448   5919   -147   -128   -471       C
ATOM   4718  C   MET B 134     -29.664   5.662 -63.969  1.00 52.76           C
ANISOU 4718  C   MET B 134     6491   7099   6456   -120   -161   -552       C
ATOM   4719  O   MET B 134     -30.205   4.616 -63.584  1.00 54.27           O
ANISOU 4719  O   MET B 134     6615   7330   6674   -178   -144   -600       O
ATOM   4720  CB  MET B 134     -28.587   7.250 -62.365  1.00 46.22           C
ANISOU 4720  CB  MET B 134     5730   6177   5655   -116   -145   -456       C
ATOM   4721  CG  MET B 134     -27.342   7.678 -61.595  1.00 51.72           C
ANISOU 4721  CG  MET B 134     6471   6796   6383   -149   -110   -387       C
ATOM   4722  SD  MET B 134     -26.496   6.289 -60.810  1.00 56.38           S
ANISOU 4722  SD  MET B 134     7030   7355   7038   -245    -59   -372       S
ATOM   4723  CE  MET B 134     -25.068   6.125 -61.892  1.00 53.95           C
ANISOU 4723  CE  MET B 134     6781   6991   6725   -255    -33   -328       C
ATOM   4724  N   LYS B 135     -30.194   6.428 -64.934  1.00 45.43           N
ANISOU 4724  N   LYS B 135     5591   6201   5469    -33   -208   -573       N
ATOM   4725  CA  LYS B 135     -31.439   6.022 -65.584  1.00 54.62           C
ANISOU 4725  CA  LYS B 135     6693   7458   6603      2   -246   -661       C
ATOM   4726  C   LYS B 135     -31.350   4.598 -66.125  1.00 57.54           C
ANISOU 4726  C   LYS B 135     7024   7845   6995    -65   -215   -689       C
ATOM   4727  O   LYS B 135     -32.296   3.812 -65.992  1.00 54.06           O
ANISOU 4727  O   LYS B 135     6502   7476   6563    -97   -215   -768       O
ATOM   4728  CB  LYS B 135     -31.800   6.985 -66.711  1.00 53.68           C
ANISOU 4728  CB  LYS B 135     6631   7356   6408    116   -303   -672       C
ATOM   4729  CG  LYS B 135     -33.128   6.642 -67.377  1.00 51.03           C
ANISOU 4729  CG  LYS B 135     6225   7127   6036    167   -351   -775       C
ATOM   4730  CD  LYS B 135     -33.808   7.894 -67.914  1.00 61.70           C
ANISOU 4730  CD  LYS B 135     7622   8508   7312    301   -423   -801       C
ATOM   4731  CE  LYS B 135     -34.847   7.571 -68.978  1.00 72.52           C
ANISOU 4731  CE  LYS B 135     8947   9975   8631    370   -477   -896       C
ATOM   4732  NZ  LYS B 135     -34.222   7.282 -70.304  1.00 78.19           N
ANISOU 4732  NZ  LYS B 135     9737  10656   9316    386   -473   -864       N
ATOM   4733  N   LEU B 136     -30.207   4.244 -66.721  1.00 48.14           N
ANISOU 4733  N   LEU B 136     5890   6588   5812    -92   -185   -630       N
ATOM   4734  CA  LEU B 136     -30.021   2.890 -67.217  1.00 47.69           C
ANISOU 4734  CA  LEU B 136     5806   6539   5777   -155   -154   -651       C
ATOM   4735  C   LEU B 136     -30.122   1.865 -66.090  1.00 51.35           C
ANISOU 4735  C   LEU B 136     6215   7002   6294   -247   -111   -669       C
ATOM   4736  O   LEU B 136     -30.711   0.791 -66.265  1.00 49.78           O
ANISOU 4736  O   LEU B 136     5965   6846   6103   -295    -96   -729       O
ATOM   4737  CB  LEU B 136     -28.674   2.790 -67.942  1.00 54.16           C
ANISOU 4737  CB  LEU B 136     6698   7284   6596   -165   -128   -582       C
ATOM   4738  CG  LEU B 136     -28.649   3.336 -69.380  1.00 44.95           C
ANISOU 4738  CG  LEU B 136     5587   6122   5369    -92   -159   -580       C
ATOM   4739  CD1 LEU B 136     -27.420   2.864 -70.104  1.00 45.64           C
ANISOU 4739  CD1 LEU B 136     5725   6150   5464   -127   -122   -532       C
ATOM   4740  CD2 LEU B 136     -29.881   2.896 -70.135  1.00 49.80           C
ANISOU 4740  CD2 LEU B 136     6146   6825   5950    -56   -197   -664       C
ATOM   4741  N   PHE B 137     -29.581   2.191 -64.915  1.00 56.09           N
ANISOU 4741  N   PHE B 137     6832   7552   6927   -275    -90   -622       N
ATOM   4742  CA  PHE B 137     -29.652   1.255 -63.801  1.00 52.36           C
ANISOU 4742  CA  PHE B 137     6328   7070   6498   -358    -49   -635       C
ATOM   4743  C   PHE B 137     -31.071   1.165 -63.248  1.00 51.74           C
ANISOU 4743  C   PHE B 137     6174   7069   6414   -372    -58   -718       C
ATOM   4744  O   PHE B 137     -31.526   0.079 -62.862  1.00 47.94           O
ANISOU 4744  O   PHE B 137     5657   6607   5950   -446    -22   -766       O
ATOM   4745  CB  PHE B 137     -28.654   1.667 -62.721  1.00 52.58           C
ANISOU 4745  CB  PHE B 137     6396   7024   6557   -375    -28   -564       C
ATOM   4746  CG  PHE B 137     -27.252   1.200 -62.995  1.00 55.24           C
ANISOU 4746  CG  PHE B 137     6785   7290   6914   -398     -0   -506       C
ATOM   4747  CD1 PHE B 137     -26.884  -0.110 -62.748  1.00 62.74           C
ANISOU 4747  CD1 PHE B 137     7735   8213   7888   -461     36   -511       C
ATOM   4748  CD2 PHE B 137     -26.315   2.059 -63.528  1.00 46.60           C
ANISOU 4748  CD2 PHE B 137     5742   6157   5808   -356     -9   -454       C
ATOM   4749  CE1 PHE B 137     -25.606  -0.535 -63.021  1.00 59.84           C
ANISOU 4749  CE1 PHE B 137     7411   7790   7537   -472     56   -467       C
ATOM   4750  CE2 PHE B 137     -25.040   1.637 -63.800  1.00 41.90           C
ANISOU 4750  CE2 PHE B 137     5182   5508   5229   -378     18   -414       C
ATOM   4751  CZ  PHE B 137     -24.685   0.345 -63.548  1.00 50.82           C
ANISOU 4751  CZ  PHE B 137     6304   6618   6386   -431     46   -422       C
ATOM   4752  N   SER B 138     -31.796   2.286 -63.228  1.00 45.20           N
ANISOU 4752  N   SER B 138     5327   6290   5558   -301   -104   -743       N
ATOM   4753  CA  SER B 138     -33.171   2.259 -62.735  1.00 43.28           C
ANISOU 4753  CA  SER B 138     5003   6134   5308   -308   -116   -835       C
ATOM   4754  C   SER B 138     -34.054   1.403 -63.630  1.00 51.81           C
ANISOU 4754  C   SER B 138     6023   7294   6369   -323   -119   -927       C
ATOM   4755  O   SER B 138     -34.760   0.500 -63.159  1.00 47.00           O
ANISOU 4755  O   SER B 138     5355   6726   5775   -401    -84   -998       O
ATOM   4756  CB  SER B 138     -33.734   3.671 -62.657  1.00 43.06           C
ANISOU 4756  CB  SER B 138     4970   6144   5247   -212   -172   -846       C
ATOM   4757  OG  SER B 138     -35.057   3.622 -62.172  1.00 57.77           O
ANISOU 4757  OG  SER B 138     6745   8101   7106   -219   -184   -946       O
ATOM   4758  N   GLU B 139     -34.020   1.677 -64.935  1.00 59.86           N
ANISOU 4758  N   GLU B 139     7061   8334   7350   -251   -159   -931       N
ATOM   4759  CA  GLU B 139     -34.828   0.910 -65.875  1.00 61.02           C
ANISOU 4759  CA  GLU B 139     7150   8559   7475   -256   -168  -1021       C
ATOM   4760  C   GLU B 139     -34.515  -0.582 -65.794  1.00 56.61           C
ANISOU 4760  C   GLU B 139     6585   7973   6952   -369   -103  -1028       C
ATOM   4761  O   GLU B 139     -35.413  -1.417 -65.941  1.00 53.35           O
ANISOU 4761  O   GLU B 139     6104   7631   6537   -419    -86  -1123       O
ATOM   4762  CB  GLU B 139     -34.614   1.445 -67.287  1.00 56.39           C
ANISOU 4762  CB  GLU B 139     6608   7979   6840   -159   -219  -1005       C
ATOM   4763  CG  GLU B 139     -35.465   2.653 -67.623  1.00 64.59           C
ANISOU 4763  CG  GLU B 139     7633   9084   7824    -40   -293  -1051       C
ATOM   4764  CD  GLU B 139     -35.022   3.340 -68.902  1.00 83.38           C
ANISOU 4764  CD  GLU B 139    10095  11438  10149     61   -338  -1009       C
ATOM   4765  OE1 GLU B 139     -35.499   4.470 -69.151  1.00 87.59           O
ANISOU 4765  OE1 GLU B 139    10653  11998  10630    171   -400  -1025       O
ATOM   4766  OE2 GLU B 139     -34.203   2.756 -69.659  1.00 88.37           O
ANISOU 4766  OE2 GLU B 139    10774  12019  10785     32   -312   -964       O
ATOM   4767  N   PHE B 140     -33.254  -0.932 -65.521  1.00 55.27           N
ANISOU 4767  N   PHE B 140     6487   7702   6811   -409    -66   -934       N
ATOM   4768  CA  PHE B 140     -32.859  -2.337 -65.468  1.00 55.47           C
ANISOU 4768  CA  PHE B 140     6524   7689   6863   -504     -8   -934       C
ATOM   4769  C   PHE B 140     -33.409  -3.020 -64.223  1.00 54.59           C
ANISOU 4769  C   PHE B 140     6383   7582   6777   -597     42   -977       C
ATOM   4770  O   PHE B 140     -33.859  -4.172 -64.285  1.00 52.20           O
ANISOU 4770  O   PHE B 140     6058   7298   6478   -676     85  -1037       O
ATOM   4771  CB  PHE B 140     -31.332  -2.432 -65.525  1.00 54.90           C
ANISOU 4771  CB  PHE B 140     6537   7513   6811   -505     10   -829       C
ATOM   4772  CG  PHE B 140     -30.788  -3.841 -65.554  1.00 57.62           C
ANISOU 4772  CG  PHE B 140     6908   7809   7176   -584     61   -823       C
ATOM   4773  CD1 PHE B 140     -31.037  -4.681 -66.629  1.00 52.32           C
ANISOU 4773  CD1 PHE B 140     6221   7169   6490   -600     67   -868       C
ATOM   4774  CD2 PHE B 140     -29.982  -4.310 -64.514  1.00 55.62           C
ANISOU 4774  CD2 PHE B 140     6703   7475   6954   -635    101   -770       C
ATOM   4775  CE1 PHE B 140     -30.511  -5.979 -66.662  1.00 44.86           C
ANISOU 4775  CE1 PHE B 140     5310   6173   5561   -670    114   -860       C
ATOM   4776  CE2 PHE B 140     -29.448  -5.593 -64.546  1.00 57.52           C
ANISOU 4776  CE2 PHE B 140     6982   7666   7207   -696    143   -763       C
ATOM   4777  CZ  PHE B 140     -29.714  -6.433 -65.629  1.00 51.11           C
ANISOU 4777  CZ  PHE B 140     6157   6883   6380   -714    151   -808       C
ATOM   4778  N   LEU B 141     -33.363  -2.337 -63.077  1.00 53.17           N
ANISOU 4778  N   LEU B 141     6210   7379   6612   -594     43   -947       N
ATOM   4779  CA  LEU B 141     -33.965  -2.899 -61.875  1.00 55.41           C
ANISOU 4779  CA  LEU B 141     6470   7670   6914   -682     92   -992       C
ATOM   4780  C   LEU B 141     -35.471  -3.034 -62.039  1.00 60.68           C
ANISOU 4780  C   LEU B 141     7041   8454   7562   -702     89  -1120       C
ATOM   4781  O   LEU B 141     -36.054  -4.046 -61.633  1.00 52.48           O
ANISOU 4781  O   LEU B 141     5979   7432   6528   -802    146  -1188       O
ATOM   4782  CB  LEU B 141     -33.643  -2.033 -60.658  1.00 62.49           C
ANISOU 4782  CB  LEU B 141     7391   8525   7827   -665     87   -937       C
ATOM   4783  CG  LEU B 141     -34.261  -2.541 -59.353  1.00 66.67           C
ANISOU 4783  CG  LEU B 141     7904   9057   8370   -755    139   -981       C
ATOM   4784  CD1 LEU B 141     -33.660  -3.900 -58.965  1.00 59.14           C
ANISOU 4784  CD1 LEU B 141     7018   8023   7430   -846    205   -956       C
ATOM   4785  CD2 LEU B 141     -34.094  -1.523 -58.231  1.00 71.55           C
ANISOU 4785  CD2 LEU B 141     8533   9652   9001   -725    124   -936       C
ATOM   4786  N   GLY B 142     -36.112  -2.030 -62.644  1.00 59.79           N
ANISOU 4786  N   GLY B 142     6875   8421   7421   -609     24  -1161       N
ATOM   4787  CA  GLY B 142     -37.554  -2.082 -62.799  1.00 60.25           C
ANISOU 4787  CA  GLY B 142     6830   8605   7460   -616     13  -1296       C
ATOM   4788  C   GLY B 142     -38.225  -2.178 -61.445  1.00 57.89           C
ANISOU 4788  C   GLY B 142     6491   8326   7177   -693     56  -1346       C
ATOM   4789  O   GLY B 142     -37.870  -1.468 -60.504  1.00 56.20           O
ANISOU 4789  O   GLY B 142     6309   8066   6978   -676     52  -1285       O
ATOM   4790  N   LYS B 143     -39.188  -3.083 -61.316  1.00 56.91           N
ANISOU 4790  N   LYS B 143     6302   8271   7052   -786    105  -1461       N
ATOM   4791  CA  LYS B 143     -39.946  -3.193 -60.081  1.00 59.35           C
ANISOU 4791  CA  LYS B 143     6569   8611   7372   -868    153  -1526       C
ATOM   4792  C   LYS B 143     -39.533  -4.402 -59.257  1.00 59.98           C
ANISOU 4792  C   LYS B 143     6720   8600   7472  -1004    248  -1499       C
ATOM   4793  O   LYS B 143     -40.302  -4.846 -58.398  1.00 65.99           O
ANISOU 4793  O   LYS B 143     7448   9391   8234  -1103    309  -1579       O
ATOM   4794  CB  LYS B 143     -41.448  -3.234 -60.382  1.00 64.99           C
ANISOU 4794  CB  LYS B 143     7152   9477   8063   -881    145  -1695       C
ATOM   4795  CG  LYS B 143     -41.955  -2.023 -61.147  1.00 68.62           C
ANISOU 4795  CG  LYS B 143     7546  10032   8493   -733     44  -1734       C
ATOM   4796  CD  LYS B 143     -43.369  -2.231 -61.693  1.00 73.59           C
ANISOU 4796  CD  LYS B 143     8042  10823   9097   -736     30  -1912       C
ATOM   4797  CE  LYS B 143     -43.426  -3.418 -62.645  1.00 82.05           C
ANISOU 4797  CE  LYS B 143     9103  11909  10163   -800     65  -1962       C
ATOM   4798  NZ  LYS B 143     -44.266  -3.155 -63.860  1.00 84.99           N
ANISOU 4798  NZ  LYS B 143     9379  12415  10497   -708     -6  -2077       N
ATOM   4799  N   ARG B 144     -38.339  -4.946 -59.499  1.00 60.94           N
ANISOU 4799  N   ARG B 144     6941   8609   7604  -1010    263  -1394       N
ATOM   4800  CA  ARG B 144     -37.896  -6.140 -58.787  1.00 66.00           C
ANISOU 4800  CA  ARG B 144     7666   9155   8255  -1125    347  -1367       C
ATOM   4801  C   ARG B 144     -37.303  -5.779 -57.430  1.00 62.03           C
ANISOU 4801  C   ARG B 144     7233   8567   7768  -1135    365  -1285       C
ATOM   4802  O   ARG B 144     -36.858  -4.654 -57.203  1.00 59.65           O
ANISOU 4802  O   ARG B 144     6933   8255   7477  -1046    309  -1218       O
ATOM   4803  CB  ARG B 144     -36.862  -6.906 -59.611  1.00 62.04           C
ANISOU 4803  CB  ARG B 144     7243   8575   7756  -1119    352  -1296       C
ATOM   4804  CG  ARG B 144     -37.089  -6.829 -61.084  1.00 53.47           C
ANISOU 4804  CG  ARG B 144     6100   7561   6655  -1059    304  -1335       C
ATOM   4805  CD  ARG B 144     -35.813  -7.145 -61.849  1.00 58.67           C
ANISOU 4805  CD  ARG B 144     6839   8134   7320  -1017    288  -1235       C
ATOM   4806  NE  ARG B 144     -36.101  -7.792 -63.130  1.00 56.28           N
ANISOU 4806  NE  ARG B 144     6504   7879   7001  -1021    284  -1292       N
ATOM   4807  CZ  ARG B 144     -36.511  -7.157 -64.223  1.00 53.18           C
ANISOU 4807  CZ  ARG B 144     6045   7572   6590   -937    221  -1330       C
ATOM   4808  NH1 ARG B 144     -36.683  -5.843 -64.213  1.00 48.92           N
ANISOU 4808  NH1 ARG B 144     5471   7074   6042   -839    156  -1316       N
ATOM   4809  NH2 ARG B 144     -36.745  -7.842 -65.337  1.00 48.76           N
ANISOU 4809  NH2 ARG B 144     5460   7051   6015   -948    222  -1383       N
ATOM   4810  N   THR B 145     -37.304  -6.761 -56.519  1.00 64.62           N
ANISOU 4810  N   THR B 145     7627   8832   8096  -1247    446  -1293       N
ATOM   4811  CA  THR B 145     -36.717  -6.543 -55.196  1.00 67.02           C
ANISOU 4811  CA  THR B 145     8007   9047   8409  -1259    466  -1217       C
ATOM   4812  C   THR B 145     -35.208  -6.389 -55.290  1.00 70.44           C
ANISOU 4812  C   THR B 145     8532   9376   8857  -1185    431  -1084       C
ATOM   4813  O   THR B 145     -34.621  -5.528 -54.623  1.00 69.00           O
ANISOU 4813  O   THR B 145     8371   9156   8688  -1127    398  -1012       O
ATOM   4814  CB  THR B 145     -37.061  -7.693 -54.241  1.00 64.24           C
ANISOU 4814  CB  THR B 145     7723   8642   8042  -1395    564  -1258       C
ATOM   4815  OG1 THR B 145     -38.484  -7.878 -54.204  1.00 74.09           O
ANISOU 4815  OG1 THR B 145     8879   9996   9277  -1477    606  -1397       O
ATOM   4816  N   TRP B 146     -34.564  -7.227 -56.096  1.00 65.18           N
ANISOU 4816  N   TRP B 146     7916   8663   8187  -1189    439  -1057       N
ATOM   4817  CA  TRP B 146     -33.133  -7.170 -56.325  1.00 59.81           C
ANISOU 4817  CA  TRP B 146     7311   7895   7519  -1121    407   -947       C
ATOM   4818  C   TRP B 146     -32.901  -7.177 -57.825  1.00 66.93           C
ANISOU 4818  C   TRP B 146     8178   8833   8419  -1068    367   -948       C
ATOM   4819  O   TRP B 146     -33.847  -7.250 -58.617  1.00 69.70           O
ANISOU 4819  O   TRP B 146     8452   9273   8758  -1081    363  -1032       O
ATOM   4820  CB  TRP B 146     -32.413  -8.333 -55.642  1.00 56.40           C
ANISOU 4820  CB  TRP B 146     7001   7350   7079  -1180    462   -907       C
ATOM   4821  CG  TRP B 146     -32.754  -8.438 -54.191  1.00 52.92           C
ANISOU 4821  CG  TRP B 146     6605   6872   6630  -1242    509   -915       C
ATOM   4822  CD1 TRP B 146     -33.554  -9.376 -53.598  1.00 44.34           C
ANISOU 4822  CD1 TRP B 146     5555   5773   5519  -1356    588   -984       C
ATOM   4823  CD2 TRP B 146     -32.320  -7.561 -53.148  1.00 57.08           C
ANISOU 4823  CD2 TRP B 146     7149   7368   7170  -1197    485   -856       C
ATOM   4824  NE1 TRP B 146     -33.634  -9.138 -52.245  1.00 54.17           N
ANISOU 4824  NE1 TRP B 146     6844   6979   6759  -1384    614   -968       N
ATOM   4825  CE2 TRP B 146     -32.885  -8.030 -51.944  1.00 57.20           C
ANISOU 4825  CE2 TRP B 146     7213   7352   7167  -1284    548   -890       C
ATOM   4826  CE3 TRP B 146     -31.500  -6.431 -53.112  1.00 64.29           C
ANISOU 4826  CE3 TRP B 146     8046   8275   8106  -1097    420   -782       C
ATOM   4827  CZ2 TRP B 146     -32.658  -7.406 -50.721  1.00 62.75           C
ANISOU 4827  CZ2 TRP B 146     7945   8021   7875  -1267    543   -848       C
ATOM   4828  CZ3 TRP B 146     -31.283  -5.809 -51.898  1.00 68.34           C
ANISOU 4828  CZ3 TRP B 146     8583   8756   8626  -1083    416   -744       C
ATOM   4829  CH2 TRP B 146     -31.861  -6.301 -50.718  1.00 68.85           C
ANISOU 4829  CH2 TRP B 146     8693   8793   8674  -1165    475   -776       C
ATOM   4830  N   PHE B 147     -31.632  -7.109 -58.221  1.00 62.79           N
ANISOU 4830  N   PHE B 147     7709   8243   7905  -1007    338   -861       N
ATOM   4831  CA  PHE B 147     -31.322  -6.854 -59.621  1.00 61.67           C
ANISOU 4831  CA  PHE B 147     7536   8135   7761   -943    294   -852       C
ATOM   4832  C   PHE B 147     -31.513  -8.074 -60.519  1.00 59.16           C
ANISOU 4832  C   PHE B 147     7226   7822   7429   -994    325   -899       C
ATOM   4833  O   PHE B 147     -31.598  -7.908 -61.733  1.00 51.63           O
ANISOU 4833  O   PHE B 147     6230   6918   6468   -952    292   -916       O
ATOM   4834  CB  PHE B 147     -29.902  -6.308 -59.744  1.00 55.52           C
ANISOU 4834  CB  PHE B 147     6807   7292   6998   -868    258   -753       C
ATOM   4835  CG  PHE B 147     -29.839  -4.813 -59.686  1.00 52.20           C
ANISOU 4835  CG  PHE B 147     6349   6902   6583   -791    206   -722       C
ATOM   4836  CD1 PHE B 147     -30.207  -4.047 -60.800  1.00 48.33           C
ANISOU 4836  CD1 PHE B 147     5807   6479   6078   -729    161   -741       C
ATOM   4837  CD2 PHE B 147     -29.439  -4.162 -58.510  1.00 42.98           C
ANISOU 4837  CD2 PHE B 147     5205   5695   5430   -778    203   -675       C
ATOM   4838  CE1 PHE B 147     -30.156  -2.658 -60.762  1.00 46.19           C
ANISOU 4838  CE1 PHE B 147     5518   6228   5804   -655    115   -712       C
ATOM   4839  CE2 PHE B 147     -29.402  -2.775 -58.443  1.00 47.49           C
ANISOU 4839  CE2 PHE B 147     5748   6291   6004   -710    160   -648       C
ATOM   4840  CZ  PHE B 147     -29.754  -2.012 -59.577  1.00 54.25           C
ANISOU 4840  CZ  PHE B 147     6562   7207   6842   -648    116   -665       C
ATOM   4841  N   ALA B 148     -31.626  -9.276 -59.968  1.00 62.62           N
ANISOU 4841  N   ALA B 148     7723   8210   7860  -1083    388   -922       N
ATOM   4842  CA  ALA B 148     -31.909 -10.467 -60.758  1.00 66.40           C
ANISOU 4842  CA  ALA B 148     8213   8693   8323  -1142    425   -975       C
ATOM   4843  C   ALA B 148     -33.061 -11.243 -60.139  1.00 70.59           C
ANISOU 4843  C   ALA B 148     8738   9246   8837  -1258    496  -1068       C
ATOM   4844  O   ALA B 148     -32.975 -12.450 -59.906  1.00 84.68           O
ANISOU 4844  O   ALA B 148    10602  10966  10605  -1336    558  -1082       O
ATOM   4845  CB  ALA B 148     -30.667 -11.346 -60.888  1.00 67.92           C
ANISOU 4845  CB  ALA B 148     8508   8782   8515  -1136    438   -908       C
ATOM   4846  N   GLY B 149     -34.150 -10.552 -59.827  1.00 63.44           N
ANISOU 4846  N   GLY B 149     7744   8431   7931  -1271    492  -1137       N
ATOM   4847  CA  GLY B 149     -35.369 -11.195 -59.397  1.00 65.84           C
ANISOU 4847  CA  GLY B 149     8018   8781   8219  -1385    560  -1247       C
ATOM   4848  C   GLY B 149     -35.670 -11.007 -57.923  1.00 79.21           C
ANISOU 4848  C   GLY B 149     9741  10443   9910  -1438    601  -1248       C
ATOM   4849  O   GLY B 149     -35.242 -10.047 -57.276  1.00 81.75           O
ANISOU 4849  O   GLY B 149    10067  10748  10248  -1371    560  -1183       O
ATOM   4850  N   ASP B 150     -36.445 -11.951 -57.392  1.00 80.01           N
ANISOU 4850  N   ASP B 150     9870  10540   9991  -1565    687  -1330       N
ATOM   4851  CA  ASP B 150     -36.927 -11.920 -56.022  1.00 71.04           C
ANISOU 4851  CA  ASP B 150     8764   9382   8846  -1639    742  -1353       C
ATOM   4852  C   ASP B 150     -35.880 -12.367 -55.008  1.00 67.37           C
ANISOU 4852  C   ASP B 150     8455   8769   8372  -1645    770  -1251       C
ATOM   4853  O   ASP B 150     -36.162 -12.351 -53.804  1.00 69.14           O
ANISOU 4853  O   ASP B 150     8724   8960   8585  -1701    815  -1258       O
ATOM   4854  CB  ASP B 150     -38.174 -12.805 -55.893  1.00 78.97           C
ANISOU 4854  CB  ASP B 150     9743  10436   9825  -1785    836  -1490       C
ATOM   4855  CG  ASP B 150     -39.394 -12.203 -56.566  1.00 81.96           C
ANISOU 4855  CG  ASP B 150     9950  10980  10210  -1781    809  -1614       C
ATOM   4856  N   LYS B 151     -34.683 -12.750 -55.446  1.00 65.56           N
ANISOU 4856  N   LYS B 151     8308   8455   8145  -1584    741  -1161       N
ATOM   4857  CA  LYS B 151     -33.672 -13.325 -54.567  1.00 60.89           C
ANISOU 4857  CA  LYS B 151     7872   7726   7539  -1583    764  -1076       C
ATOM   4858  C   LYS B 151     -32.394 -12.491 -54.620  1.00 60.84           C
ANISOU 4858  C   LYS B 151     7872   7684   7559  -1449    679   -965       C
ATOM   4859  O   LYS B 151     -32.013 -11.992 -55.684  1.00 62.35           O
ANISOU 4859  O   LYS B 151     7994   7922   7772  -1371    618   -943       O
ATOM   4860  CB  LYS B 151     -33.392 -14.782 -54.963  1.00 57.91           C
ANISOU 4860  CB  LYS B 151     7604   7268   7130  -1644    820  -1085       C
ATOM   4861  CG  LYS B 151     -32.841 -15.672 -53.877  1.00 63.34           C
ANISOU 4861  CG  LYS B 151     8469   7817   7781  -1685    875  -1042       C
ATOM   4862  CD  LYS B 151     -32.499 -17.058 -54.426  1.00 75.82           C
ANISOU 4862  CD  LYS B 151    10160   9318   9328  -1728    919  -1048       C
ATOM   4863  CE  LYS B 151     -31.320 -17.696 -53.676  1.00 86.16           C
ANISOU 4863  CE  LYS B 151    11649  10480  10607  -1685    920   -961       C
ATOM   4864  NZ  LYS B 151     -30.354 -18.414 -54.581  1.00 85.49           N
ANISOU 4864  NZ  LYS B 151    11622  10344  10518  -1625    891   -921       N
ATOM   4865  N   LEU B 152     -31.750 -12.329 -53.461  1.00 58.38           N
ANISOU 4865  N   LEU B 152     7647   7291   7243  -1427    679   -900       N
ATOM   4866  CA  LEU B 152     -30.516 -11.560 -53.365  1.00 53.97           C
ANISOU 4866  CA  LEU B 152     7099   6700   6709  -1310    607   -804       C
ATOM   4867  C   LEU B 152     -29.360 -12.309 -54.018  1.00 60.60           C
ANISOU 4867  C   LEU B 152     8013   7469   7543  -1262    589   -753       C
ATOM   4868  O   LEU B 152     -29.321 -13.542 -54.042  1.00 64.30           O
ANISOU 4868  O   LEU B 152     8579   7872   7980  -1317    638   -771       O
ATOM   4869  CB  LEU B 152     -30.179 -11.256 -51.902  1.00 53.64           C
ANISOU 4869  CB  LEU B 152     7128   6593   6660  -1301    614   -759       C
ATOM   4870  CG  LEU B 152     -28.920 -10.435 -51.581  1.00 55.56           C
ANISOU 4870  CG  LEU B 152     7381   6802   6926  -1189    545   -669       C
ATOM   4871  CD1 LEU B 152     -29.032  -8.983 -52.068  1.00 52.51           C
ANISOU 4871  CD1 LEU B 152     6863   6508   6578  -1122    483   -660       C
ATOM   4872  CD2 LEU B 152     -28.599 -10.478 -50.094  1.00 49.73           C
ANISOU 4872  CD2 LEU B 152     6739   5985   6170  -1193    564   -635       C
ATOM   4873  N   ASN B 153     -28.396 -11.539 -54.520  1.00 58.50           N
ANISOU 4873  N   ASN B 153     7706   7214   7305  -1160    519   -693       N
ATOM   4874  CA  ASN B 153     -27.396 -12.020 -55.458  1.00 52.62           C
ANISOU 4874  CA  ASN B 153     6989   6439   6564  -1107    491   -660       C
ATOM   4875  C   ASN B 153     -26.107 -11.240 -55.262  1.00 52.71           C
ANISOU 4875  C   ASN B 153     7003   6426   6598  -1005    431   -585       C
ATOM   4876  O   ASN B 153     -26.133 -10.058 -54.898  1.00 56.51           O
ANISOU 4876  O   ASN B 153     7423   6947   7102   -968    399   -565       O
ATOM   4877  CB  ASN B 153     -27.909 -11.848 -56.888  1.00 67.12           C
ANISOU 4877  CB  ASN B 153     8727   8363   8412  -1108    475   -701       C
ATOM   4878  CG  ASN B 153     -27.412 -12.906 -57.802  1.00 63.46           C
ANISOU 4878  CG  ASN B 153     8311   7865   7937  -1111    485   -703       C
ATOM   4879  OD1 ASN B 153     -26.316 -12.802 -58.346  1.00 70.63           O
ANISOU 4879  OD1 ASN B 153     9229   8751   8857  -1038    444   -655       O
ATOM   4880  ND2 ASN B 153     -28.200 -13.949 -57.968  1.00 51.00           N
ANISOU 4880  ND2 ASN B 153     6765   6281   6333  -1199    544   -765       N
ATOM   4881  N   TYR B 154     -24.970 -11.895 -55.524  1.00 49.03           N
ANISOU 4881  N   TYR B 154     6605   5897   6125   -960    417   -550       N
ATOM   4882  CA  TYR B 154     -23.705 -11.189 -55.327  1.00 50.90           C
ANISOU 4882  CA  TYR B 154     6839   6118   6385   -868    363   -493       C
ATOM   4883  C   TYR B 154     -23.623  -9.953 -56.211  1.00 51.85           C
ANISOU 4883  C   TYR B 154     6845   6319   6538   -824    320   -482       C
ATOM   4884  O   TYR B 154     -23.001  -8.952 -55.828  1.00 52.36           O
ANISOU 4884  O   TYR B 154     6880   6391   6623   -769    286   -446       O
ATOM   4885  CB  TYR B 154     -22.513 -12.119 -55.564  1.00 50.63           C
ANISOU 4885  CB  TYR B 154     6886   6016   6336   -823    352   -472       C
ATOM   4886  CG  TYR B 154     -22.086 -12.297 -57.005  1.00 60.92           C
ANISOU 4886  CG  TYR B 154     8143   7352   7651   -798    333   -478       C
ATOM   4887  CD1 TYR B 154     -21.095 -11.493 -57.574  1.00 60.50           C
ANISOU 4887  CD1 TYR B 154     8031   7329   7626   -727    286   -449       C
ATOM   4888  CD2 TYR B 154     -22.645 -13.301 -57.787  1.00 60.09           C
ANISOU 4888  CD2 TYR B 154     8059   7245   7526   -852    367   -516       C
ATOM   4889  CE1 TYR B 154     -20.705 -11.671 -58.891  1.00 56.69           C
ANISOU 4889  CE1 TYR B 154     7514   6875   7150   -709    274   -456       C
ATOM   4890  CE2 TYR B 154     -22.258 -13.492 -59.092  1.00 62.14           C
ANISOU 4890  CE2 TYR B 154     8282   7534   7795   -830    350   -522       C
ATOM   4891  CZ  TYR B 154     -21.294 -12.680 -59.645  1.00 60.01           C
ANISOU 4891  CZ  TYR B 154     7956   7294   7552   -758    304   -491       C
ATOM   4892  OH  TYR B 154     -20.933 -12.899 -60.953  1.00 53.50           O
ANISOU 4892  OH  TYR B 154     7100   6497   6733   -741    292   -500       O
ATOM   4893  N   VAL B 155     -24.291  -9.985 -57.364  1.00 53.43           N
ANISOU 4893  N   VAL B 155     6984   6578   6739   -848    324   -518       N
ATOM   4894  CA  VAL B 155     -24.300  -8.838 -58.264  1.00 57.51           C
ANISOU 4894  CA  VAL B 155     7410   7166   7276   -804    285   -510       C
ATOM   4895  C   VAL B 155     -24.951  -7.630 -57.591  1.00 55.24           C
ANISOU 4895  C   VAL B 155     7069   6921   7000   -798    272   -509       C
ATOM   4896  O   VAL B 155     -24.602  -6.479 -57.888  1.00 52.72           O
ANISOU 4896  O   VAL B 155     6703   6633   6696   -744    235   -482       O
ATOM   4897  CB  VAL B 155     -24.978  -9.236 -59.604  1.00 53.10           C
ANISOU 4897  CB  VAL B 155     6807   6660   6708   -829    292   -555       C
ATOM   4898  CG1 VAL B 155     -26.503  -9.118 -59.550  1.00 47.97           C
ANISOU 4898  CG1 VAL B 155     6103   6075   6048   -886    313   -618       C
ATOM   4899  CG2 VAL B 155     -24.410  -8.430 -60.738  1.00 47.01           C
ANISOU 4899  CG2 VAL B 155     5986   5927   5948   -768    251   -533       C
ATOM   4900  N   ASP B 156     -25.850  -7.865 -56.630  1.00 55.21           N
ANISOU 4900  N   ASP B 156     7078   6914   6985   -854    304   -539       N
ATOM   4901  CA  ASP B 156     -26.407  -6.764 -55.851  1.00 58.48           C
ANISOU 4901  CA  ASP B 156     7447   7363   7408   -846    292   -538       C
ATOM   4902  C   ASP B 156     -25.379  -6.091 -54.945  1.00 53.59           C
ANISOU 4902  C   ASP B 156     6858   6698   6805   -794    267   -478       C
ATOM   4903  O   ASP B 156     -25.582  -4.933 -54.561  1.00 50.88           O
ANISOU 4903  O   ASP B 156     6470   6387   6474   -767    244   -465       O
ATOM   4904  CB  ASP B 156     -27.571  -7.252 -55.002  1.00 58.12           C
ANISOU 4904  CB  ASP B 156     7412   7325   7347   -926    339   -590       C
ATOM   4905  CG  ASP B 156     -28.765  -7.612 -55.830  1.00 54.70           C
ANISOU 4905  CG  ASP B 156     6920   6963   6901   -978    360   -667       C
ATOM   4906  OD1 ASP B 156     -29.432  -6.686 -56.345  1.00 49.67           O
ANISOU 4906  OD1 ASP B 156     6195   6409   6270   -951    329   -695       O
ATOM   4907  OD2 ASP B 156     -29.023  -8.826 -55.966  1.00 52.99           O
ANISOU 4907  OD2 ASP B 156     6750   6719   6665  -1044    406   -702       O
ATOM   4908  N   PHE B 157     -24.294  -6.784 -54.586  1.00 39.43           N
ANISOU 4908  N   PHE B 157     5140   4832   5008   -775    270   -445       N
ATOM   4909  CA  PHE B 157     -23.246  -6.136 -53.816  1.00 45.34           C
ANISOU 4909  CA  PHE B 157     5907   5548   5772   -719    242   -397       C
ATOM   4910  C   PHE B 157     -22.404  -5.209 -54.694  1.00 51.26           C
ANISOU 4910  C   PHE B 157     6605   6328   6544   -659    204   -371       C
ATOM   4911  O   PHE B 157     -21.963  -4.157 -54.221  1.00 53.46           O
ANISOU 4911  O   PHE B 157     6861   6613   6840   -622    181   -344       O
ATOM   4912  CB  PHE B 157     -22.375  -7.189 -53.117  1.00 49.15           C
ANISOU 4912  CB  PHE B 157     6489   5949   6239   -709    253   -382       C
ATOM   4913  CG  PHE B 157     -23.115  -7.998 -52.082  1.00 55.65           C
ANISOU 4913  CG  PHE B 157     7386   6726   7032   -768    296   -401       C
ATOM   4914  CD1 PHE B 157     -24.254  -8.732 -52.422  1.00 50.92           C
ANISOU 4914  CD1 PHE B 157     6793   6142   6414   -846    341   -448       C
ATOM   4915  CD2 PHE B 157     -22.686  -8.016 -50.763  1.00 61.63           C
ANISOU 4915  CD2 PHE B 157     8211   7428   7779   -749    295   -378       C
ATOM   4916  CE1 PHE B 157     -24.934  -9.466 -51.474  1.00 53.68           C
ANISOU 4916  CE1 PHE B 157     7218   6447   6733   -913    391   -472       C
ATOM   4917  CE2 PHE B 157     -23.369  -8.748 -49.802  1.00 58.71           C
ANISOU 4917  CE2 PHE B 157     7923   7009   7375   -808    340   -395       C
ATOM   4918  CZ  PHE B 157     -24.487  -9.475 -50.156  1.00 60.32           C
ANISOU 4918  CZ  PHE B 157     8137   7224   7559   -894    392   -442       C
ATOM   4919  N   LEU B 158     -22.211  -5.559 -55.976  1.00 50.20           N
ANISOU 4919  N   LEU B 158     6454   6212   6407   -653    200   -381       N
ATOM   4920  CA  LEU B 158     -21.509  -4.678 -56.908  1.00 44.52           C
ANISOU 4920  CA  LEU B 158     5692   5522   5703   -607    173   -362       C
ATOM   4921  C   LEU B 158     -22.379  -3.498 -57.321  1.00 50.99           C
ANISOU 4921  C   LEU B 158     6451   6401   6522   -601    159   -368       C
ATOM   4922  O   LEU B 158     -21.893  -2.366 -57.435  1.00 45.21           O
ANISOU 4922  O   LEU B 158     5698   5680   5799   -563    138   -343       O
ATOM   4923  CB  LEU B 158     -21.083  -5.453 -58.149  1.00 41.91           C
ANISOU 4923  CB  LEU B 158     5368   5192   5365   -605    176   -373       C
ATOM   4924  CG  LEU B 158     -20.073  -6.576 -57.983  1.00 45.64           C
ANISOU 4924  CG  LEU B 158     5900   5608   5833   -594    182   -370       C
ATOM   4925  CD1 LEU B 158     -20.271  -7.553 -59.127  1.00 50.61           C
ANISOU 4925  CD1 LEU B 158     6537   6244   6449   -615    195   -395       C
ATOM   4926  CD2 LEU B 158     -18.675  -5.989 -57.994  1.00 40.79           C
ANISOU 4926  CD2 LEU B 158     5277   4985   5237   -540    159   -346       C
ATOM   4927  N   ALA B 159     -23.659  -3.743 -57.585  1.00 49.23           N
ANISOU 4927  N   ALA B 159     6202   6218   6284   -637    169   -408       N
ATOM   4928  CA  ALA B 159     -24.546  -2.636 -57.908  1.00 48.52           C
ANISOU 4928  CA  ALA B 159     6057   6189   6188   -619    149   -423       C
ATOM   4929  C   ALA B 159     -24.575  -1.626 -56.768  1.00 51.05           C
ANISOU 4929  C   ALA B 159     6371   6505   6520   -602    138   -400       C
ATOM   4930  O   ALA B 159     -24.439  -0.418 -56.999  1.00 46.17           O
ANISOU 4930  O   ALA B 159     5734   5906   5904   -559    113   -380       O
ATOM   4931  CB  ALA B 159     -25.952  -3.160 -58.223  1.00 45.25           C
ANISOU 4931  CB  ALA B 159     5608   5828   5756   -661    162   -486       C
ATOM   4932  N   TYR B 160     -24.723  -2.114 -55.520  1.00 47.75           N
ANISOU 4932  N   TYR B 160     5980   6055   6107   -637    160   -403       N
ATOM   4933  CA  TYR B 160     -24.781  -1.222 -54.356  1.00 45.38           C
ANISOU 4933  CA  TYR B 160     5676   5750   5817   -624    151   -383       C
ATOM   4934  C   TYR B 160     -23.502  -0.405 -54.228  1.00 48.91           C
ANISOU 4934  C   TYR B 160     6135   6166   6281   -574    130   -333       C
ATOM   4935  O   TYR B 160     -23.546   0.817 -54.038  1.00 53.44           O
ANISOU 4935  O   TYR B 160     6686   6758   6860   -544    111   -317       O
ATOM   4936  CB  TYR B 160     -25.033  -2.018 -53.059  1.00 50.79           C
ANISOU 4936  CB  TYR B 160     6403   6396   6500   -671    182   -393       C
ATOM   4937  CG  TYR B 160     -24.854  -1.169 -51.799  1.00 55.23           C
ANISOU 4937  CG  TYR B 160     6970   6942   7073   -654    173   -366       C
ATOM   4938  CD1 TYR B 160     -25.880  -0.339 -51.334  1.00 50.03           C
ANISOU 4938  CD1 TYR B 160     6266   6329   6414   -661    168   -387       C
ATOM   4939  CD2 TYR B 160     -23.642  -1.164 -51.103  1.00 53.92           C
ANISOU 4939  CD2 TYR B 160     6848   6720   6919   -624    165   -325       C
ATOM   4940  CE1 TYR B 160     -25.699   0.467 -50.224  1.00 46.80           C
ANISOU 4940  CE1 TYR B 160     5861   5906   6017   -644    159   -362       C
ATOM   4941  CE2 TYR B 160     -23.460  -0.375 -49.986  1.00 51.71           C
ANISOU 4941  CE2 TYR B 160     6569   6428   6649   -606    155   -303       C
ATOM   4942  CZ  TYR B 160     -24.489   0.439 -49.550  1.00 53.97           C
ANISOU 4942  CZ  TYR B 160     6815   6755   6936   -618    154   -319       C
ATOM   4943  OH  TYR B 160     -24.295   1.222 -48.435  1.00 56.06           O
ANISOU 4943  OH  TYR B 160     7082   7007   7211   -601    144   -297       O
ATOM   4944  N   ASP B 161     -22.350  -1.067 -54.329  1.00 48.24           N
ANISOU 4944  N   ASP B 161     6088   6037   6203   -565    135   -314       N
ATOM   4945  CA  ASP B 161     -21.076  -0.373 -54.186  1.00 46.58           C
ANISOU 4945  CA  ASP B 161     5883   5805   6009   -524    119   -281       C
ATOM   4946  C   ASP B 161     -20.901   0.701 -55.259  1.00 47.29           C
ANISOU 4946  C   ASP B 161     5944   5927   6099   -497    105   -272       C
ATOM   4947  O   ASP B 161     -20.594   1.857 -54.943  1.00 52.22           O
ANISOU 4947  O   ASP B 161     6559   6554   6731   -474     95   -252       O
ATOM   4948  CB  ASP B 161     -19.925  -1.377 -54.225  1.00 42.47           C
ANISOU 4948  CB  ASP B 161     5402   5243   5493   -514    124   -278       C
ATOM   4949  CG  ASP B 161     -18.567  -0.699 -54.289  1.00 47.47           C
ANISOU 4949  CG  ASP B 161     6026   5868   6143   -475    111   -261       C
ATOM   4950  OD1 ASP B 161     -18.401   0.390 -53.687  1.00 44.77           O
ANISOU 4950  OD1 ASP B 161     5666   5532   5812   -461    103   -245       O
ATOM   4951  OD2 ASP B 161     -17.669  -1.250 -54.955  1.00 47.87           O
ANISOU 4951  OD2 ASP B 161     6085   5910   6195   -462    111   -268       O
ATOM   4952  N   VAL B 162     -21.092   0.341 -56.533  1.00 45.72           N
ANISOU 4952  N   VAL B 162     5737   5748   5885   -499    107   -286       N
ATOM   4953  CA  VAL B 162     -20.926   1.311 -57.624  1.00 45.92           C
ANISOU 4953  CA  VAL B 162     5752   5796   5900   -473     96   -277       C
ATOM   4954  C   VAL B 162     -21.923   2.464 -57.487  1.00 42.06           C
ANISOU 4954  C   VAL B 162     5244   5339   5397   -454     79   -278       C
ATOM   4955  O   VAL B 162     -21.546   3.638 -57.576  1.00 39.67           O
ANISOU 4955  O   VAL B 162     4951   5032   5091   -427     72   -256       O
ATOM   4956  CB  VAL B 162     -21.040   0.616 -58.997  1.00 37.79           C
ANISOU 4956  CB  VAL B 162     4722   4783   4853   -478    100   -296       C
ATOM   4957  CG1 VAL B 162     -20.968   1.644 -60.136  1.00 41.06           C
ANISOU 4957  CG1 VAL B 162     5139   5216   5246   -448     90   -286       C
ATOM   4958  CG2 VAL B 162     -19.921  -0.390 -59.145  1.00 33.91           C
ANISOU 4958  CG2 VAL B 162     4250   4258   4374   -487    114   -294       C
ATOM   4959  N   LEU B 163     -23.203   2.153 -57.251  1.00 44.57           N
ANISOU 4959  N   LEU B 163     5538   5691   5705   -469     74   -309       N
ATOM   4960  CA  LEU B 163     -24.182   3.217 -57.008  1.00 52.63           C
ANISOU 4960  CA  LEU B 163     6536   6749   6712   -445     53   -319       C
ATOM   4961  C   LEU B 163     -23.839   4.041 -55.769  1.00 57.35           C
ANISOU 4961  C   LEU B 163     7141   7322   7328   -437     52   -291       C
ATOM   4962  O   LEU B 163     -24.141   5.238 -55.715  1.00 52.74           O
ANISOU 4962  O   LEU B 163     6555   6751   6732   -403     33   -283       O
ATOM   4963  CB  LEU B 163     -25.592   2.638 -56.867  1.00 52.87           C
ANISOU 4963  CB  LEU B 163     6527   6828   6731   -470     53   -373       C
ATOM   4964  CG  LEU B 163     -26.244   2.022 -58.109  1.00 47.98           C
ANISOU 4964  CG  LEU B 163     5888   6252   6089   -472     48   -415       C
ATOM   4965  CD1 LEU B 163     -27.561   1.310 -57.767  1.00 43.31           C
ANISOU 4965  CD1 LEU B 163     5253   5710   5492   -514     59   -480       C
ATOM   4966  CD2 LEU B 163     -26.413   3.059 -59.223  1.00 36.32           C
ANISOU 4966  CD2 LEU B 163     4414   4805   4583   -409     15   -412       C
ATOM   4967  N   ASP B 164     -23.216   3.427 -54.760  1.00 55.61           N
ANISOU 4967  N   ASP B 164     6934   7063   7130   -464     69   -279       N
ATOM   4968  CA  ASP B 164     -22.822   4.203 -53.592  1.00 50.51           C
ANISOU 4968  CA  ASP B 164     6295   6396   6502   -454     66   -254       C
ATOM   4969  C   ASP B 164     -21.725   5.210 -53.933  1.00 49.40           C
ANISOU 4969  C   ASP B 164     6171   6234   6366   -425     63   -222       C
ATOM   4970  O   ASP B 164     -21.755   6.341 -53.442  1.00 46.38           O
ANISOU 4970  O   ASP B 164     5788   5850   5983   -406     54   -207       O
ATOM   4971  CB  ASP B 164     -22.373   3.271 -52.466  1.00 54.69           C
ANISOU 4971  CB  ASP B 164     6843   6887   7048   -481     83   -250       C
ATOM   4972  CG  ASP B 164     -22.273   3.979 -51.121  1.00 57.06           C
ANISOU 4972  CG  ASP B 164     7146   7173   7362   -474     79   -234       C
ATOM   4973  OD1 ASP B 164     -23.156   4.810 -50.800  1.00 52.11           O
ANISOU 4973  OD1 ASP B 164     6495   6574   6728   -468     68   -240       O
ATOM   4974  OD2 ASP B 164     -21.300   3.704 -50.385  1.00 58.82           O
ANISOU 4974  OD2 ASP B 164     7392   7358   7599   -470     82   -218       O
ATOM   4975  N   VAL B 165     -20.743   4.825 -54.764  1.00 46.94           N
ANISOU 4975  N   VAL B 165     5874   5906   6055   -425     73   -217       N
ATOM   4976  CA  VAL B 165     -19.664   5.751 -55.112  1.00 44.52           C
ANISOU 4976  CA  VAL B 165     5583   5581   5751   -411     80   -197       C
ATOM   4977  C   VAL B 165     -20.222   6.956 -55.848  1.00 47.33           C
ANISOU 4977  C   VAL B 165     5954   5951   6078   -386     71   -189       C
ATOM   4978  O   VAL B 165     -19.830   8.097 -55.576  1.00 41.66           O
ANISOU 4978  O   VAL B 165     5254   5217   5358   -375     75   -172       O
ATOM   4979  CB  VAL B 165     -18.563   5.054 -55.937  1.00 43.06           C
ANISOU 4979  CB  VAL B 165     5406   5383   5572   -420     96   -203       C
ATOM   4980  CG1 VAL B 165     -18.102   3.768 -55.234  1.00 30.67           C
ANISOU 4980  CG1 VAL B 165     3833   3798   4023   -432     99   -214       C
ATOM   4981  N   TYR B 166     -21.148   6.726 -56.786  1.00 49.83           N
ANISOU 4981  N   TYR B 166     6269   6297   6367   -374     58   -206       N
ATOM   4982  CA  TYR B 166     -21.759   7.835 -57.513  1.00 48.24           C
ANISOU 4982  CA  TYR B 166     6092   6109   6127   -335     41   -202       C
ATOM   4983  C   TYR B 166     -22.524   8.744 -56.570  1.00 54.52           C
ANISOU 4983  C   TYR B 166     6879   6915   6919   -313     22   -200       C
ATOM   4984  O   TYR B 166     -22.435   9.972 -56.660  1.00 54.91           O
ANISOU 4984  O   TYR B 166     6967   6949   6948   -284     17   -182       O
ATOM   4985  CB  TYR B 166     -22.686   7.303 -58.606  1.00 42.08           C
ANISOU 4985  CB  TYR B 166     5303   5368   5318   -319     24   -231       C
ATOM   4986  CG  TYR B 166     -21.934   7.026 -59.882  1.00 46.02           C
ANISOU 4986  CG  TYR B 166     5833   5852   5802   -322     39   -225       C
ATOM   4987  CD1 TYR B 166     -21.072   5.953 -59.962  1.00 42.84           C
ANISOU 4987  CD1 TYR B 166     5418   5434   5426   -360     63   -226       C
ATOM   4988  CD2 TYR B 166     -22.050   7.865 -60.984  1.00 48.93           C
ANISOU 4988  CD2 TYR B 166     6250   6217   6124   -285     31   -218       C
ATOM   4989  CE1 TYR B 166     -20.366   5.703 -61.100  1.00 51.66           C
ANISOU 4989  CE1 TYR B 166     6559   6540   6530   -365     79   -225       C
ATOM   4990  CE2 TYR B 166     -21.342   7.620 -62.141  1.00 50.35           C
ANISOU 4990  CE2 TYR B 166     6463   6382   6288   -293     50   -213       C
ATOM   4991  CZ  TYR B 166     -20.503   6.532 -62.192  1.00 48.89           C
ANISOU 4991  CZ  TYR B 166     6253   6188   6135   -335     75   -218       C
ATOM   4992  OH  TYR B 166     -19.784   6.247 -63.330  1.00 47.27           O
ANISOU 4992  OH  TYR B 166     6074   5970   5915   -346     95   -218       O
ATOM   4993  N   ARG B 167     -23.306   8.134 -55.679  1.00 62.51           N
ANISOU 4993  N   ARG B 167     7849   7953   7950   -328     13   -222       N
ATOM   4994  CA  ARG B 167     -24.022   8.830 -54.615  1.00 58.85           C
ANISOU 4994  CA  ARG B 167     7368   7503   7489   -315     -2   -226       C
ATOM   4995  C   ARG B 167     -23.092   9.715 -53.792  1.00 55.42           C
ANISOU 4995  C   ARG B 167     6959   7027   7073   -315     10   -190       C
ATOM   4996  O   ARG B 167     -23.400  10.881 -53.523  1.00 54.04           O
ANISOU 4996  O   ARG B 167     6800   6850   6882   -284     -4   -181       O
ATOM   4997  CB  ARG B 167     -24.691   7.768 -53.741  1.00 49.48           C
ANISOU 4997  CB  ARG B 167     6138   6338   6322   -353      4   -254       C
ATOM   4998  CG  ARG B 167     -25.669   8.225 -52.751  1.00 48.34           C
ANISOU 4998  CG  ARG B 167     5966   6222   6179   -348     -9   -274       C
ATOM   4999  CD  ARG B 167     -26.428   7.012 -52.254  1.00 49.87           C
ANISOU 4999  CD  ARG B 167     6125   6441   6382   -396      7   -314       C
ATOM   5000  NE  ARG B 167     -25.657   6.148 -51.361  1.00 48.74           N
ANISOU 5000  NE  ARG B 167     6002   6252   6266   -440     35   -295       N
ATOM   5001  CZ  ARG B 167     -26.226   5.342 -50.460  1.00 51.23           C
ANISOU 5001  CZ  ARG B 167     6308   6570   6587   -485     55   -320       C
ATOM   5002  NH1 ARG B 167     -27.544   5.307 -50.352  1.00 62.98           N
ANISOU 5002  NH1 ARG B 167     7756   8112   8062   -501     54   -370       N
ATOM   5003  NH2 ARG B 167     -25.497   4.582 -49.654  1.00 42.99           N
ANISOU 5003  NH2 ARG B 167     5299   5477   5559   -514     77   -300       N
ATOM   5004  N   ILE B 168     -21.946   9.170 -53.370  1.00 51.73           N
ANISOU 5004  N   ILE B 168     6493   6526   6635   -347     34   -176       N
ATOM   5005  CA  ILE B 168     -20.997   9.958 -52.594  1.00 44.38           C
ANISOU 5005  CA  ILE B 168     5577   5563   5722   -350     46   -152       C
ATOM   5006  C   ILE B 168     -20.460  11.113 -53.433  1.00 43.60           C
ANISOU 5006  C   ILE B 168     5522   5443   5599   -333     56   -136       C
ATOM   5007  O   ILE B 168     -20.371  12.256 -52.964  1.00 55.36           O
ANISOU 5007  O   ILE B 168     7034   6917   7083   -321     57   -122       O
ATOM   5008  CB  ILE B 168     -19.867   9.059 -52.067  1.00 46.11           C
ANISOU 5008  CB  ILE B 168     5785   5760   5974   -378     64   -153       C
ATOM   5009  CG1 ILE B 168     -20.399   8.109 -50.998  1.00 49.75           C
ANISOU 5009  CG1 ILE B 168     6225   6226   6451   -393     57   -164       C
ATOM   5010  CG2 ILE B 168     -18.712   9.902 -51.521  1.00 44.81           C
ANISOU 5010  CG2 ILE B 168     5631   5570   5826   -380     78   -140       C
ATOM   5011  CD1 ILE B 168     -19.640   6.800 -50.914  1.00 45.99           C
ANISOU 5011  CD1 ILE B 168     5752   5732   5989   -410     67   -172       C
ATOM   5012  N   PHE B 169     -20.116  10.844 -54.691  1.00 45.15           N
ANISOU 5012  N   PHE B 169     5741   5637   5777   -335     66   -139       N
ATOM   5013  CA  PHE B 169     -19.582  11.907 -55.539  1.00 45.72           C
ANISOU 5013  CA  PHE B 169     5871   5681   5817   -327     85   -125       C
ATOM   5014  C   PHE B 169     -20.644  12.944 -55.860  1.00 44.42           C
ANISOU 5014  C   PHE B 169     5747   5522   5608   -278     59   -119       C
ATOM   5015  O   PHE B 169     -20.365  14.145 -55.807  1.00 44.96           O
ANISOU 5015  O   PHE B 169     5869   5558   5655   -267     70   -102       O
ATOM   5016  CB  PHE B 169     -18.997  11.345 -56.827  1.00 39.20           C
ANISOU 5016  CB  PHE B 169     5064   4851   4978   -341    104   -131       C
ATOM   5017  CG  PHE B 169     -18.350  12.391 -57.691  1.00 49.97           C
ANISOU 5017  CG  PHE B 169     6499   6180   6306   -344    134   -119       C
ATOM   5018  CD1 PHE B 169     -17.107  12.907 -57.360  1.00 57.02           C
ANISOU 5018  CD1 PHE B 169     7404   7045   7217   -382    175   -119       C
ATOM   5019  CD2 PHE B 169     -18.991  12.882 -58.832  1.00 45.49           C
ANISOU 5019  CD2 PHE B 169     5993   5609   5684   -308    123   -114       C
ATOM   5020  CE1 PHE B 169     -16.504  13.883 -58.162  1.00 62.06           C
ANISOU 5020  CE1 PHE B 169     8116   7645   7817   -398    214   -113       C
ATOM   5021  CE2 PHE B 169     -18.390  13.843 -59.629  1.00 43.58           C
ANISOU 5021  CE2 PHE B 169     5835   5324   5400   -314    157   -102       C
ATOM   5022  CZ  PHE B 169     -17.148  14.348 -59.296  1.00 50.17           C
ANISOU 5022  CZ  PHE B 169     6685   6126   6252   -365    207   -101       C
ATOM   5023  N   GLU B 170     -21.860  12.501 -56.189  1.00 51.09           N
ANISOU 5023  N   GLU B 170     6570   6408   6435   -247     24   -138       N
ATOM   5024  CA  GLU B 170     -23.004  13.374 -56.468  1.00 49.18           C
ANISOU 5024  CA  GLU B 170     6356   6184   6147   -186    -12   -146       C
ATOM   5025  C   GLU B 170     -24.196  12.963 -55.605  1.00 56.33           C
ANISOU 5025  C   GLU B 170     7193   7142   7069   -174    -44   -176       C
ATOM   5026  O   GLU B 170     -24.957  12.055 -55.990  1.00 54.36           O
ANISOU 5026  O   GLU B 170     6900   6938   6816   -173    -60   -210       O
ATOM   5027  CB  GLU B 170     -23.381  13.340 -57.947  1.00 51.94           C
ANISOU 5027  CB  GLU B 170     6746   6544   6445   -149    -26   -157       C
ATOM   5028  CG  GLU B 170     -24.604  14.197 -58.282  1.00 68.47           C
ANISOU 5028  CG  GLU B 170     8870   8662   8483    -69    -74   -174       C
ATOM   5029  CD  GLU B 170     -24.628  15.507 -57.502  1.00 93.37           C
ANISOU 5029  CD  GLU B 170    12067  11785  11625    -42    -78   -154       C
ATOM   5030  OE1 GLU B 170     -23.741  16.352 -57.760  1.00105.57           O
ANISOU 5030  OE1 GLU B 170    13694  13269  13150    -51    -47   -121       O
ATOM   5031  OE2 GLU B 170     -25.515  15.687 -56.622  1.00 90.62           O
ANISOU 5031  OE2 GLU B 170    11672  11474  11286    -18   -109   -174       O
ATOM   5032  N   PRO B 171     -24.412  13.632 -54.455  1.00 59.96           N
ANISOU 5032  N   PRO B 171     7642   7598   7542   -168    -51   -170       N
ATOM   5033  CA  PRO B 171     -25.434  13.155 -53.493  1.00 46.12           C
ANISOU 5033  CA  PRO B 171     5821   5894   5810   -173    -70   -202       C
ATOM   5034  C   PRO B 171     -26.839  13.015 -54.062  1.00 44.73           C
ANISOU 5034  C   PRO B 171     5614   5781   5600   -130   -109   -251       C
ATOM   5035  O   PRO B 171     -27.541  12.058 -53.714  1.00 49.65           O
ANISOU 5035  O   PRO B 171     6173   6450   6241   -158   -110   -291       O
ATOM   5036  CB  PRO B 171     -25.380  14.215 -52.380  1.00 45.08           C
ANISOU 5036  CB  PRO B 171     5700   5741   5686   -161    -73   -183       C
ATOM   5037  CG  PRO B 171     -23.981  14.793 -52.482  1.00 42.79           C
ANISOU 5037  CG  PRO B 171     5467   5388   5403   -181    -40   -141       C
ATOM   5038  CD  PRO B 171     -23.648  14.788 -53.939  1.00 51.64           C
ANISOU 5038  CD  PRO B 171     6637   6494   6488   -168    -33   -136       C
ATOM   5039  N   LYS B 172     -27.274  13.928 -54.924  1.00 48.38           N
ANISOU 5039  N   LYS B 172     6124   6249   6010    -60   -139   -256       N
ATOM   5040  CA  LYS B 172     -28.621  13.886 -55.496  1.00 52.54           C
ANISOU 5040  CA  LYS B 172     6619   6845   6498     -3   -185   -314       C
ATOM   5041  C   LYS B 172     -28.771  12.933 -56.681  1.00 52.17           C
ANISOU 5041  C   LYS B 172     6558   6826   6437     -8   -187   -340       C
ATOM   5042  O   LYS B 172     -29.872  12.845 -57.224  1.00 55.29           O
ANISOU 5042  O   LYS B 172     6922   7287   6799     40   -225   -397       O
ATOM   5043  CB  LYS B 172     -29.051  15.291 -55.951  1.00 44.69           C
ANISOU 5043  CB  LYS B 172     5693   5844   5442     90   -226   -312       C
ATOM   5044  CG  LYS B 172     -29.233  16.279 -54.827  1.00 40.10           C
ANISOU 5044  CG  LYS B 172     5118   5251   4867    110   -235   -302       C
ATOM   5045  CD  LYS B 172     -28.977  17.696 -55.301  1.00 40.59           C
ANISOU 5045  CD  LYS B 172     5292   5259   4873    180   -251   -269       C
ATOM   5046  CE  LYS B 172     -29.079  18.699 -54.168  1.00 43.47           C
ANISOU 5046  CE  LYS B 172     5667   5604   5243    196   -257   -255       C
ATOM   5047  NZ  LYS B 172     -28.196  18.340 -52.979  1.00 50.28           N
ANISOU 5047  NZ  LYS B 172     6492   6437   6176    106   -208   -222       N
ATOM   5048  N   CYS B 173     -27.722  12.218 -57.096  1.00 50.17           N
ANISOU 5048  N   CYS B 173     6324   6532   6206    -61   -148   -307       N
ATOM   5049  CA  CYS B 173     -27.778  11.472 -58.357  1.00 48.81           C
ANISOU 5049  CA  CYS B 173     6154   6379   6013    -58   -151   -326       C
ATOM   5050  C   CYS B 173     -28.867  10.392 -58.388  1.00 52.14           C
ANISOU 5050  C   CYS B 173     6491   6877   6444    -75   -164   -394       C
ATOM   5051  O   CYS B 173     -29.282   9.993 -59.481  1.00 54.58           O
ANISOU 5051  O   CYS B 173     6795   7220   6723    -50   -182   -426       O
ATOM   5052  CB  CYS B 173     -26.407  10.843 -58.677  1.00 38.95           C
ANISOU 5052  CB  CYS B 173     4933   5074   4792   -117   -104   -284       C
ATOM   5053  SG  CYS B 173     -25.960   9.392 -57.729  1.00 62.93           S
ANISOU 5053  SG  CYS B 173     7906   8109   7895   -206    -67   -287       S
ATOM   5054  N   LEU B 174     -29.349   9.915 -57.237  1.00 52.57           N
ANISOU 5054  N   LEU B 174     6482   6959   6535   -120   -153   -420       N
ATOM   5055  CA  LEU B 174     -30.435   8.936 -57.200  1.00 53.65           C
ANISOU 5055  CA  LEU B 174     6540   7169   6676   -147   -156   -494       C
ATOM   5056  C   LEU B 174     -31.796   9.573 -56.929  1.00 54.22           C
ANISOU 5056  C   LEU B 174     6562   7317   6722    -94   -199   -560       C
ATOM   5057  O   LEU B 174     -32.784   8.851 -56.787  1.00 53.19           O
ANISOU 5057  O   LEU B 174     6356   7258   6595   -122   -198   -635       O
ATOM   5058  CB  LEU B 174     -30.159   7.848 -56.147  1.00 39.10           C
ANISOU 5058  CB  LEU B 174     4665   5307   4883   -240   -108   -491       C
ATOM   5059  CG  LEU B 174     -28.836   7.101 -56.302  1.00 45.63           C
ANISOU 5059  CG  LEU B 174     5535   6065   5737   -288    -70   -436       C
ATOM   5060  CD1 LEU B 174     -28.693   5.945 -55.297  1.00 32.20           C
ANISOU 5060  CD1 LEU B 174     3816   4346   4074   -368    -29   -442       C
ATOM   5061  CD2 LEU B 174     -28.708   6.612 -57.763  1.00 49.11           C
ANISOU 5061  CD2 LEU B 174     5988   6516   6154   -274    -76   -447       C
ATOM   5062  N   ASP B 175     -31.867  10.903 -56.875  1.00 53.61           N
ANISOU 5062  N   ASP B 175     6526   7228   6614    -18   -234   -541       N
ATOM   5063  CA  ASP B 175     -33.079  11.581 -56.420  1.00 53.94           C
ANISOU 5063  CA  ASP B 175     6521   7340   6634     37   -276   -603       C
ATOM   5064  C   ASP B 175     -34.272  11.254 -57.298  1.00 55.55           C
ANISOU 5064  C   ASP B 175     6666   7640   6800     84   -317   -696       C
ATOM   5065  O   ASP B 175     -35.407  11.162 -56.814  1.00 59.15           O
ANISOU 5065  O   ASP B 175     7039   8180   7254     88   -334   -780       O
ATOM   5066  CB  ASP B 175     -32.861  13.093 -56.413  1.00 54.83           C
ANISOU 5066  CB  ASP B 175     6710   7413   6711    123   -311   -561       C
ATOM   5067  CG  ASP B 175     -32.428  13.607 -55.079  1.00 65.35           C
ANISOU 5067  CG  ASP B 175     8050   8702   8079     90   -288   -519       C
ATOM   5068  OD1 ASP B 175     -32.243  12.780 -54.160  1.00 69.13           O
ANISOU 5068  OD1 ASP B 175     8481   9177   8608      4   -246   -517       O
ATOM   5069  OD2 ASP B 175     -32.293  14.844 -54.952  1.00 70.99           O
ANISOU 5069  OD2 ASP B 175     8825   9383   8765    153   -311   -488       O
ATOM   5070  N   GLU B 176     -34.037  11.099 -58.597  1.00 61.57           N
ANISOU 5070  N   GLU B 176     7469   8397   7530    121   -332   -690       N
ATOM   5071  CA  GLU B 176     -35.108  10.957 -59.566  1.00 55.29           C
ANISOU 5071  CA  GLU B 176     6629   7691   6688    186   -381   -778       C
ATOM   5072  C   GLU B 176     -35.582   9.518 -59.709  1.00 63.81           C
ANISOU 5072  C   GLU B 176     7619   8830   7794    104   -350   -845       C
ATOM   5073  O   GLU B 176     -36.609   9.279 -60.348  1.00 62.66           O
ANISOU 5073  O   GLU B 176     7411   8778   7618    144   -386   -939       O
ATOM   5074  CB  GLU B 176     -34.642  11.516 -60.912  1.00 41.98           C
ANISOU 5074  CB  GLU B 176     5039   5965   4945    269   -412   -740       C
ATOM   5075  N   PHE B 177     -34.887   8.559 -59.101  1.00 69.65           N
ANISOU 5075  N   PHE B 177     8353   9521   8589     -7   -285   -806       N
ATOM   5076  CA  PHE B 177     -35.162   7.139 -59.292  1.00 68.45           C
ANISOU 5076  CA  PHE B 177     8143   9405   8461    -93   -246   -858       C
ATOM   5077  C   PHE B 177     -35.452   6.543 -57.924  1.00 66.74           C
ANISOU 5077  C   PHE B 177     7875   9195   8288   -188   -198   -882       C
ATOM   5078  O   PHE B 177     -34.550   5.990 -57.278  1.00 73.74           O
ANISOU 5078  O   PHE B 177     8801  10005   9214   -263   -147   -817       O
ATOM   5079  CB  PHE B 177     -33.995   6.441 -59.989  1.00 63.92           C
ANISOU 5079  CB  PHE B 177     7630   8755   7900   -131   -213   -788       C
ATOM   5080  CG  PHE B 177     -33.430   7.232 -61.129  1.00 56.85           C
ANISOU 5080  CG  PHE B 177     6812   7825   6963    -45   -250   -740       C
ATOM   5081  CD1 PHE B 177     -34.016   7.176 -62.382  1.00 58.81           C
ANISOU 5081  CD1 PHE B 177     7050   8130   7164     17   -290   -792       C
ATOM   5082  CD2 PHE B 177     -32.335   8.067 -60.939  1.00 62.17           C
ANISOU 5082  CD2 PHE B 177     7572   8410   7639    -26   -243   -647       C
ATOM   5083  CE1 PHE B 177     -33.511   7.918 -63.433  1.00 58.50           C
ANISOU 5083  CE1 PHE B 177     7097   8052   7078     96   -320   -747       C
ATOM   5084  CE2 PHE B 177     -31.828   8.820 -61.980  1.00 60.15           C
ANISOU 5084  CE2 PHE B 177     7399   8117   7339     45   -267   -606       C
ATOM   5085  CZ  PHE B 177     -32.414   8.738 -63.235  1.00 59.26           C
ANISOU 5085  CZ  PHE B 177     7287   8054   7176    107   -306   -653       C
ATOM   5086  N   PRO B 178     -36.703   6.652 -57.451  1.00 65.64           N
ANISOU 5086  N   PRO B 178     7651   9149   8140   -186   -212   -979       N
ATOM   5087  CA  PRO B 178     -37.055   6.086 -56.136  1.00 56.07           C
ANISOU 5087  CA  PRO B 178     6395   7944   6964   -284   -159  -1009       C
ATOM   5088  C   PRO B 178     -36.754   4.605 -56.061  1.00 56.26           C
ANISOU 5088  C   PRO B 178     6423   7938   7016   -399    -91  -1012       C
ATOM   5089  O   PRO B 178     -36.356   4.080 -55.013  1.00 65.62           O
ANISOU 5089  O   PRO B 178     7633   9067   8232   -482    -37   -979       O
ATOM   5090  CB  PRO B 178     -38.564   6.360 -56.034  1.00 54.63           C
ANISOU 5090  CB  PRO B 178     6110   7890   6759   -257   -189  -1139       C
ATOM   5091  CG  PRO B 178     -38.885   7.308 -57.129  1.00 50.54           C
ANISOU 5091  CG  PRO B 178     5596   7418   6191   -122   -270  -1159       C
ATOM   5092  CD  PRO B 178     -37.891   7.078 -58.203  1.00 62.78           C
ANISOU 5092  CD  PRO B 178     7225   8897   7733   -102   -272  -1081       C
ATOM   5093  N   ASN B 179     -37.013   3.920 -57.163  1.00 52.44           N
ANISOU 5093  N   ASN B 179     5917   7493   6515   -402    -94  -1058       N
ATOM   5094  CA  ASN B 179     -36.408   2.667 -57.578  1.00 51.99           C
ANISOU 5094  CA  ASN B 179     5893   7388   6474   -478    -45  -1035       C
ATOM   5095  C   ASN B 179     -35.097   2.341 -56.890  1.00 53.36           C
ANISOU 5095  C   ASN B 179     6153   7442   6680   -525     -4   -927       C
ATOM   5096  O   ASN B 179     -34.984   1.339 -56.175  1.00 52.36           O
ANISOU 5096  O   ASN B 179     6042   7280   6574   -620     56   -930       O
ATOM   5097  CB  ASN B 179     -36.145   2.748 -59.083  1.00 56.36           C
ANISOU 5097  CB  ASN B 179     6463   7951   6999   -407    -87  -1025       C
ATOM   5098  CG  ASN B 179     -36.307   1.462 -59.729  1.00 52.78           C
ANISOU 5098  CG  ASN B 179     5990   7516   6547   -475    -51  -1072       C
ATOM   5099  OD1 ASN B 179     -36.815   0.533 -59.112  1.00 69.64           O
ANISOU 5099  OD1 ASN B 179     8091   9670   8698   -573      4  -1130       O
ATOM   5100  ND2 ASN B 179     -35.882   1.358 -60.964  1.00 50.97           N
ANISOU 5100  ND2 ASN B 179     5789   7278   6300   -429    -75  -1050       N
ATOM   5101  N   LEU B 180     -34.090   3.174 -57.160  1.00 54.64           N
ANISOU 5101  N   LEU B 180     6378   7542   6842   -455    -35   -835       N
ATOM   5102  CA  LEU B 180     -32.722   2.894 -56.752  1.00 52.30           C
ANISOU 5102  CA  LEU B 180     6158   7141   6572   -485     -5   -739       C
ATOM   5103  C   LEU B 180     -32.484   3.324 -55.319  1.00 52.02           C
ANISOU 5103  C   LEU B 180     6139   7065   6559   -505     11   -704       C
ATOM   5104  O   LEU B 180     -31.742   2.654 -54.592  1.00 51.97           O
ANISOU 5104  O   LEU B 180     6177   6991   6577   -561     52   -661       O
ATOM   5105  CB  LEU B 180     -31.734   3.587 -57.700  1.00 57.89           C
ANISOU 5105  CB  LEU B 180     6921   7805   7268   -412    -38   -669       C
ATOM   5106  CG  LEU B 180     -31.673   3.106 -59.165  1.00 55.46           C
ANISOU 5106  CG  LEU B 180     6617   7517   6939   -392    -49   -686       C
ATOM   5107  CD1 LEU B 180     -30.729   3.983 -59.984  1.00 59.90           C
ANISOU 5107  CD1 LEU B 180     7242   8033   7484   -321    -77   -617       C
ATOM   5108  CD2 LEU B 180     -31.262   1.631 -59.272  1.00 37.43           C
ANISOU 5108  CD2 LEU B 180     4345   5202   4676   -473     -1   -688       C
ATOM   5109  N   LYS B 181     -33.104   4.432 -54.894  1.00 48.50           N
ANISOU 5109  N   LYS B 181     5663   6662   6104   -455    -22   -723       N
ATOM   5110  CA  LYS B 181     -33.079   4.781 -53.475  1.00 48.84           C
ANISOU 5110  CA  LYS B 181     5710   6679   6167   -482     -5   -704       C
ATOM   5111  C   LYS B 181     -33.621   3.631 -52.639  1.00 55.20           C
ANISOU 5111  C   LYS B 181     6495   7493   6985   -584     52   -754       C
ATOM   5112  O   LYS B 181     -32.990   3.190 -51.669  1.00 54.20           O
ANISOU 5112  O   LYS B 181     6418   7298   6879   -634     90   -710       O
ATOM   5113  CB  LYS B 181     -33.888   6.051 -53.221  1.00 47.83           C
ANISOU 5113  CB  LYS B 181     5541   6610   6022   -414    -50   -736       C
ATOM   5114  CG  LYS B 181     -33.274   7.301 -53.799  1.00 54.07           C
ANISOU 5114  CG  LYS B 181     6378   7371   6795   -318    -99   -676       C
ATOM   5115  CD  LYS B 181     -34.321   8.361 -53.998  1.00 61.92           C
ANISOU 5115  CD  LYS B 181     7331   8441   7755   -236   -153   -732       C
ATOM   5116  CE  LYS B 181     -34.603   9.125 -52.728  1.00 74.94           C
ANISOU 5116  CE  LYS B 181     8966  10091   9416   -232   -156   -730       C
ATOM   5117  NZ  LYS B 181     -35.116  10.490 -53.060  1.00 82.67           N
ANISOU 5117  NZ  LYS B 181     9948  11107  10357   -122   -220   -746       N
ATOM   5118  N   ASP B 182     -34.776   3.097 -53.036  1.00 49.92           N
ANISOU 5118  N   ASP B 182     5761   6907   6301   -616     62   -852       N
ATOM   5119  CA  ASP B 182     -35.365   2.013 -52.265  1.00 59.96           C
ANISOU 5119  CA  ASP B 182     7019   8186   7579   -724    126   -910       C
ATOM   5120  C   ASP B 182     -34.473   0.775 -52.274  1.00 57.41           C
ANISOU 5120  C   ASP B 182     6772   7775   7265   -789    175   -862       C
ATOM   5121  O   ASP B 182     -34.397   0.061 -51.269  1.00 61.45           O
ANISOU 5121  O   ASP B 182     7326   8239   7783   -867    230   -859       O
ATOM   5122  CB  ASP B 182     -36.777   1.731 -52.784  1.00 60.31           C
ANISOU 5122  CB  ASP B 182     6968   8346   7602   -748    127  -1037       C
ATOM   5123  CG  ASP B 182     -37.714   2.954 -52.621  1.00 82.39           C
ANISOU 5123  CG  ASP B 182     9686  11233  10384   -677     75  -1095       C
ATOM   5124  OD1 ASP B 182     -37.231   4.055 -52.258  1.00 84.33           O
ANISOU 5124  OD1 ASP B 182     9961  11446  10635   -604     36  -1029       O
ATOM   5125  OD2 ASP B 182     -38.940   2.822 -52.837  1.00 91.12           O
ANISOU 5125  OD2 ASP B 182    10702  12445  11473   -693     74  -1214       O
ATOM   5126  N   PHE B 183     -33.746   0.537 -53.370  1.00 50.69           N
ANISOU 5126  N   PHE B 183     5949   6898   6412   -753    156   -823       N
ATOM   5127  CA  PHE B 183     -32.817  -0.590 -53.403  1.00 50.49           C
ANISOU 5127  CA  PHE B 183     5999   6789   6395   -801    195   -777       C
ATOM   5128  C   PHE B 183     -31.662  -0.372 -52.425  1.00 54.34           C
ANISOU 5128  C   PHE B 183     6562   7185   6901   -789    200   -687       C
ATOM   5129  O   PHE B 183     -31.310  -1.273 -51.648  1.00 47.40           O
ANISOU 5129  O   PHE B 183     5744   6241   6024   -849    245   -672       O
ATOM   5130  CB  PHE B 183     -32.295  -0.812 -54.832  1.00 45.07           C
ANISOU 5130  CB  PHE B 183     5319   6102   5701   -760    170   -758       C
ATOM   5131  CG  PHE B 183     -31.018  -1.605 -54.887  1.00 46.44           C
ANISOU 5131  CG  PHE B 183     5576   6183   5887   -775    192   -690       C
ATOM   5132  CD1 PHE B 183     -31.043  -2.987 -54.790  1.00 40.71           C
ANISOU 5132  CD1 PHE B 183     4889   5424   5156   -852    244   -714       C
ATOM   5133  CD2 PHE B 183     -29.784  -0.964 -54.993  1.00 45.34           C
ANISOU 5133  CD2 PHE B 183     5477   5991   5761   -712    162   -607       C
ATOM   5134  CE1 PHE B 183     -29.859  -3.721 -54.817  1.00 43.91           C
ANISOU 5134  CE1 PHE B 183     5373   5744   5567   -854    257   -655       C
ATOM   5135  CE2 PHE B 183     -28.601  -1.688 -55.022  1.00 47.03           C
ANISOU 5135  CE2 PHE B 183     5757   6128   5984   -719    178   -556       C
ATOM   5136  CZ  PHE B 183     -28.636  -3.072 -54.942  1.00 43.65           C
ANISOU 5136  CZ  PHE B 183     5369   5668   5549   -784    222   -579       C
ATOM   5137  N   MET B 184     -31.071   0.831 -52.446  1.00 50.87           N
ANISOU 5137  N   MET B 184     6121   6735   6470   -711    154   -631       N
ATOM   5138  CA  MET B 184     -29.977   1.155 -51.533  1.00 52.40           C
ANISOU 5138  CA  MET B 184     6373   6853   6683   -695    154   -555       C
ATOM   5139  C   MET B 184     -30.415   1.021 -50.086  1.00 48.28           C
ANISOU 5139  C   MET B 184     5862   6317   6164   -745    186   -570       C
ATOM   5140  O   MET B 184     -29.658   0.527 -49.242  1.00 50.08           O
ANISOU 5140  O   MET B 184     6156   6472   6398   -767    209   -528       O
ATOM   5141  CB  MET B 184     -29.451   2.565 -51.816  1.00 47.42           C
ANISOU 5141  CB  MET B 184     5733   6226   6058   -611    105   -508       C
ATOM   5142  CG  MET B 184     -29.009   2.765 -53.286  1.00 41.12           C
ANISOU 5142  CG  MET B 184     4936   5438   5250   -563     77   -494       C
ATOM   5143  SD  MET B 184     -27.536   1.811 -53.681  1.00 52.01           S
ANISOU 5143  SD  MET B 184     6378   6740   6642   -577     97   -441       S
ATOM   5144  CE  MET B 184     -26.257   2.806 -52.917  1.00 46.11           C
ANISOU 5144  CE  MET B 184     5668   5936   5916   -535     84   -370       C
ATOM   5145  N   SER B 185     -31.650   1.412 -49.787  1.00 55.67           N
ANISOU 5145  N   SER B 185     6736   7323   7091   -763    187   -635       N
ATOM   5146  CA  SER B 185     -32.137   1.296 -48.418  1.00 52.24           C
ANISOU 5146  CA  SER B 185     6311   6879   6657   -818    223   -655       C
ATOM   5147  C   SER B 185     -32.333  -0.163 -48.016  1.00 61.41           C
ANISOU 5147  C   SER B 185     7524   8002   7805   -914    290   -686       C
ATOM   5148  O   SER B 185     -31.997  -0.548 -46.887  1.00 68.99           O
ANISOU 5148  O   SER B 185     8552   8898   8763   -952    323   -659       O
ATOM   5149  CB  SER B 185     -33.435   2.078 -48.262  1.00 54.29           C
ANISOU 5149  CB  SER B 185     6484   7234   6910   -812    209   -728       C
ATOM   5150  OG  SER B 185     -33.911   1.955 -46.935  1.00 70.68           O
ANISOU 5150  OG  SER B 185     8569   9302   8986   -872    249   -751       O
ATOM   5151  N   ARG B 186     -32.876  -0.991 -48.923  1.00 58.46           N
ANISOU 5151  N   ARG B 186     7130   7665   7419   -956    311   -743       N
ATOM   5152  CA  ARG B 186     -33.072  -2.408 -48.615  1.00 53.59           C
ANISOU 5152  CA  ARG B 186     6573   7005   6784  -1053    381   -775       C
ATOM   5153  C   ARG B 186     -31.742  -3.134 -48.412  1.00 57.28           C
ANISOU 5153  C   ARG B 186     7152   7361   7250  -1043    390   -695       C
ATOM   5154  O   ARG B 186     -31.644  -4.039 -47.568  1.00 54.76           O
ANISOU 5154  O   ARG B 186     6921   6974   6913  -1105    442   -693       O
ATOM   5155  CB  ARG B 186     -33.882  -3.085 -49.719  1.00 49.01           C
ANISOU 5155  CB  ARG B 186     5942   6490   6191  -1095    399   -856       C
ATOM   5156  CG  ARG B 186     -35.389  -2.984 -49.550  1.00 53.13           C
ANISOU 5156  CG  ARG B 186     6374   7112   6701  -1155    426   -970       C
ATOM   5157  CD  ARG B 186     -36.134  -3.972 -50.478  1.00 54.12           C
ANISOU 5157  CD  ARG B 186     6464   7289   6809  -1221    463  -1059       C
ATOM   5158  NE  ARG B 186     -35.655  -3.866 -51.851  1.00 58.36           N
ANISOU 5158  NE  ARG B 186     6980   7843   7352  -1148    410  -1033       N
ATOM   5159  CZ  ARG B 186     -36.050  -2.928 -52.703  1.00 62.00           C
ANISOU 5159  CZ  ARG B 186     7352   8392   7815  -1067    346  -1060       C
ATOM   5160  NH1 ARG B 186     -36.943  -2.016 -52.319  1.00 66.04           N
ANISOU 5160  NH1 ARG B 186     7782   8985   8325  -1044    323  -1116       N
ATOM   5161  NH2 ARG B 186     -35.547  -2.899 -53.937  1.00 52.74           N
ANISOU 5161  NH2 ARG B 186     6176   7221   6641  -1004    305  -1031       N
ATOM   5162  N   PHE B 187     -30.710  -2.771 -49.185  1.00 53.86           N
ANISOU 5162  N   PHE B 187     6724   6909   6833   -963    340   -634       N
ATOM   5163  CA  PHE B 187     -29.407  -3.403 -49.000  1.00 49.96           C
ANISOU 5163  CA  PHE B 187     6323   6320   6338   -943    342   -568       C
ATOM   5164  C   PHE B 187     -28.849  -3.096 -47.618  1.00 44.94           C
ANISOU 5164  C   PHE B 187     5746   5625   5706   -928    342   -521       C
ATOM   5165  O   PHE B 187     -28.408  -3.995 -46.892  1.00 44.18           O
ANISOU 5165  O   PHE B 187     5746   5451   5590   -956    374   -504       O
ATOM   5166  CB  PHE B 187     -28.426  -2.951 -50.083  1.00 54.44           C
ANISOU 5166  CB  PHE B 187     6872   6890   6923   -863    291   -521       C
ATOM   5167  CG  PHE B 187     -27.126  -3.700 -50.053  1.00 50.92           C
ANISOU 5167  CG  PHE B 187     6510   6362   6477   -841    291   -471       C
ATOM   5168  CD1 PHE B 187     -26.999  -4.921 -50.708  1.00 51.03           C
ANISOU 5168  CD1 PHE B 187     6568   6348   6474   -873    316   -488       C
ATOM   5169  CD2 PHE B 187     -26.037  -3.206 -49.340  1.00 42.98           C
ANISOU 5169  CD2 PHE B 187     5538   5308   5483   -787    265   -414       C
ATOM   5170  CE1 PHE B 187     -25.802  -5.638 -50.666  1.00 52.28           C
ANISOU 5170  CE1 PHE B 187     6806   6432   6628   -844    312   -447       C
ATOM   5171  CE2 PHE B 187     -24.832  -3.912 -49.302  1.00 52.07           C
ANISOU 5171  CE2 PHE B 187     6761   6392   6630   -758    260   -379       C
ATOM   5172  CZ  PHE B 187     -24.716  -5.136 -49.969  1.00 52.96           C
ANISOU 5172  CZ  PHE B 187     6919   6477   6725   -783    282   -396       C
ATOM   5173  N   GLU B 188     -28.884  -1.828 -47.230  1.00 48.95           N
ANISOU 5173  N   GLU B 188     6200   6167   6232   -882    307   -503       N
ATOM   5174  CA  GLU B 188     -28.403  -1.417 -45.917  1.00 53.71           C
ANISOU 5174  CA  GLU B 188     6846   6722   6838   -866    304   -463       C
ATOM   5175  C   GLU B 188     -29.266  -1.960 -44.777  1.00 59.26           C
ANISOU 5175  C   GLU B 188     7589   7408   7517   -945    359   -502       C
ATOM   5176  O   GLU B 188     -28.763  -2.128 -43.656  1.00 62.03           O
ANISOU 5176  O   GLU B 188     8016   7694   7859   -945    370   -469       O
ATOM   5177  CB  GLU B 188     -28.304   0.112 -45.889  1.00 47.12           C
ANISOU 5177  CB  GLU B 188     5942   5932   6029   -801    254   -439       C
ATOM   5178  CG  GLU B 188     -27.235   0.629 -46.886  1.00 41.91           C
ANISOU 5178  CG  GLU B 188     5268   5269   5387   -728    209   -394       C
ATOM   5179  CD  GLU B 188     -27.224   2.137 -47.022  1.00 59.08           C
ANISOU 5179  CD  GLU B 188     7384   7484   7578   -671    168   -376       C
ATOM   5180  OE1 GLU B 188     -28.104   2.801 -46.439  1.00 60.74           O
ANISOU 5180  OE1 GLU B 188     7556   7734   7787   -679    166   -401       O
ATOM   5181  OE2 GLU B 188     -26.315   2.666 -47.698  1.00 67.84           O
ANISOU 5181  OE2 GLU B 188     8493   8586   8700   -619    139   -340       O
ATOM   5182  N   GLY B 189     -30.534  -2.282 -45.044  1.00 47.04           N
ANISOU 5182  N   GLY B 189     5997   5919   5958  -1016    396   -577       N
ATOM   5183  CA  GLY B 189     -31.376  -2.872 -44.028  1.00 36.89           C
ANISOU 5183  CA  GLY B 189     4752   4618   4646  -1107    461   -624       C
ATOM   5184  C   GLY B 189     -31.185  -4.358 -43.779  1.00 48.08           C
ANISOU 5184  C   GLY B 189     6290   5952   6028  -1175    522   -629       C
ATOM   5185  O   GLY B 189     -31.811  -4.902 -42.867  1.00 54.23           O
ANISOU 5185  O   GLY B 189     7126   6702   6777  -1258    585   -665       O
ATOM   5186  N   LEU B 190     -30.352  -5.042 -44.553  1.00 52.30           N
ANISOU 5186  N   LEU B 190     6872   6442   6559  -1145    509   -597       N
ATOM   5187  CA  LEU B 190     -30.116  -6.455 -44.279  1.00 50.35           C
ANISOU 5187  CA  LEU B 190     6756   6103   6270  -1200    563   -598       C
ATOM   5188  C   LEU B 190     -29.393  -6.607 -42.945  1.00 44.89           C
ANISOU 5188  C   LEU B 190     6182   5317   5556  -1178    568   -546       C
ATOM   5189  O   LEU B 190     -28.396  -5.927 -42.687  1.00 45.65           O
ANISOU 5189  O   LEU B 190     6276   5396   5673  -1086    510   -485       O
ATOM   5190  CB  LEU B 190     -29.312  -7.094 -45.413  1.00 52.32           C
ANISOU 5190  CB  LEU B 190     7028   6329   6523  -1159    540   -574       C
ATOM   5191  CG  LEU B 190     -29.904  -6.931 -46.811  1.00 51.22           C
ANISOU 5191  CG  LEU B 190     6777   6280   6404  -1168    527   -620       C
ATOM   5192  CD1 LEU B 190     -28.974  -7.493 -47.868  1.00 48.81           C
ANISOU 5192  CD1 LEU B 190     6498   5945   6102  -1120    500   -588       C
ATOM   5193  CD2 LEU B 190     -31.239  -7.615 -46.888  1.00 46.49           C
ANISOU 5193  CD2 LEU B 190     6164   5719   5782  -1282    598   -710       C
ATOM   5194  N   LYS B 191     -29.874  -7.541 -42.120  1.00 44.51           N
ANISOU 5194  N   LYS B 191     6246   5205   5461  -1263    641   -573       N
ATOM   5195  CA  LYS B 191     -29.471  -7.620 -40.716  1.00 50.91           C
ANISOU 5195  CA  LYS B 191     7170   5932   6241  -1254    654   -536       C
ATOM   5196  C   LYS B 191     -27.953  -7.599 -40.553  1.00 54.47           C
ANISOU 5196  C   LYS B 191     7687   6316   6693  -1137    589   -459       C
ATOM   5197  O   LYS B 191     -27.399  -6.710 -39.899  1.00 59.85           O
ANISOU 5197  O   LYS B 191     8344   7001   7394  -1068    542   -419       O
ATOM   5198  CB  LYS B 191     -30.068  -8.873 -40.077  1.00 51.73           C
ANISOU 5198  CB  LYS B 191     7417   5957   6281  -1362    747   -575       C
ATOM   5199  CG  LYS B 191     -29.945  -8.921 -38.565  1.00 61.59           C
ANISOU 5199  CG  LYS B 191     8786   7127   7490  -1371    773   -551       C
ATOM   5200  N   LYS B 192     -27.260  -8.563 -41.162  1.00 60.41           N
ANISOU 5200  N   LYS B 192     8516   7012   7425  -1113    585   -444       N
ATOM   5201  CA  LYS B 192     -25.815  -8.634 -40.991  1.00 54.65           C
ANISOU 5201  CA  LYS B 192     7848   6223   6692  -1001    524   -385       C
ATOM   5202  C   LYS B 192     -25.111  -7.474 -41.680  1.00 59.05           C
ANISOU 5202  C   LYS B 192     8269   6856   7311   -912    448   -357       C
ATOM   5203  O   LYS B 192     -24.060  -7.023 -41.201  1.00 56.75           O
ANISOU 5203  O   LYS B 192     7990   6544   7030   -824    395   -316       O
ATOM   5204  CB  LYS B 192     -25.290  -9.971 -41.501  1.00 52.29           C
ANISOU 5204  CB  LYS B 192     7666   5849   6354   -994    539   -384       C
ATOM   5205  CG  LYS B 192     -25.845 -11.163 -40.728  1.00 52.33           C
ANISOU 5205  CG  LYS B 192     7840   5757   6285  -1077    619   -407       C
ATOM   5206  CD  LYS B 192     -25.097 -12.455 -41.016  1.00 63.27           C
ANISOU 5206  CD  LYS B 192     9371   7046   7621  -1044    622   -395       C
ATOM   5207  CE  LYS B 192     -24.177 -12.865 -39.867  1.00 65.13           C
ANISOU 5207  CE  LYS B 192     9771   7174   7802   -964    599   -354       C
ATOM   5208  NZ  LYS B 192     -24.096 -14.355 -39.752  1.00 61.77           N
ANISOU 5208  NZ  LYS B 192     9544   6629   7295   -989    647   -363       N
ATOM   5209  N   ILE B 193     -25.685  -6.956 -42.774  1.00 49.84           N
ANISOU 5209  N   ILE B 193     6976   5779   6184   -935    442   -382       N
ATOM   5210  CA  ILE B 193     -25.089  -5.802 -43.451  1.00 50.80           C
ANISOU 5210  CA  ILE B 193     6979   5966   6356   -860    377   -357       C
ATOM   5211  C   ILE B 193     -25.147  -4.589 -42.534  1.00 55.78           C
ANISOU 5211  C   ILE B 193     7562   6625   7009   -834    354   -339       C
ATOM   5212  O   ILE B 193     -24.142  -3.900 -42.307  1.00 49.26           O
ANISOU 5212  O   ILE B 193     6718   5795   6204   -756    304   -300       O
ATOM   5213  CB  ILE B 193     -25.803  -5.521 -44.793  1.00 47.41           C
ANISOU 5213  CB  ILE B 193     6440   5622   5953   -889    378   -391       C
ATOM   5214  CG1 ILE B 193     -25.544  -6.627 -45.819  1.00 44.62           C
ANISOU 5214  CG1 ILE B 193     6125   5244   5584   -900    391   -403       C
ATOM   5215  CG2 ILE B 193     -25.378  -4.174 -45.371  1.00 39.12           C
ANISOU 5215  CG2 ILE B 193     5279   4636   4947   -821    319   -367       C
ATOM   5216  CD1 ILE B 193     -24.313  -6.391 -46.637  1.00 47.84           C
ANISOU 5216  CD1 ILE B 193     6506   5654   6016   -815    336   -367       C
ATOM   5217  N   SER B 194     -26.340  -4.326 -41.992  1.00 54.01           N
ANISOU 5217  N   SER B 194     7312   6431   6778   -903    392   -373       N
ATOM   5218  CA  SER B 194     -26.555  -3.223 -41.068  1.00 46.36           C
ANISOU 5218  CA  SER B 194     6301   5489   5826   -888    377   -362       C
ATOM   5219  C   SER B 194     -25.661  -3.353 -39.839  1.00 47.39           C
ANISOU 5219  C   SER B 194     6529   5541   5936   -843    364   -321       C
ATOM   5220  O   SER B 194     -24.885  -2.444 -39.516  1.00 56.20           O
ANISOU 5220  O   SER B 194     7610   6666   7077   -772    315   -286       O
ATOM   5221  CB  SER B 194     -28.027  -3.191 -40.676  1.00 49.81           C
ANISOU 5221  CB  SER B 194     6708   5966   6250   -980    430   -419       C
ATOM   5222  OG  SER B 194     -28.242  -2.277 -39.630  1.00 52.36           O
ANISOU 5222  OG  SER B 194     7009   6304   6583   -971    421   -410       O
ATOM   5223  N   ALA B 195     -25.754  -4.491 -39.145  1.00 46.74           N
ANISOU 5223  N   ALA B 195     6578   5379   5803   -884    409   -328       N
ATOM   5224  CA  ALA B 195     -24.874  -4.763 -38.010  1.00 50.43           C
ANISOU 5224  CA  ALA B 195     7159   5764   6239   -830    394   -292       C
ATOM   5225  C   ALA B 195     -23.411  -4.497 -38.352  1.00 60.30           C
ANISOU 5225  C   ALA B 195     8394   7007   7511   -719    324   -254       C
ATOM   5226  O   ALA B 195     -22.667  -3.932 -37.546  1.00 67.41           O
ANISOU 5226  O   ALA B 195     9303   7894   8416   -653    285   -228       O
ATOM   5227  CB  ALA B 195     -25.059  -6.208 -37.547  1.00 44.43           C
ANISOU 5227  CB  ALA B 195     6562   4908   5411   -880    451   -305       C
ATOM   5228  N   TYR B 196     -22.985  -4.886 -39.555  1.00 71.89           N
ANISOU 5228  N   TYR B 196     9834   8490   8992   -700    308   -257       N
ATOM   5229  CA  TYR B 196     -21.600  -4.681 -39.962  1.00 63.96           C
ANISOU 5229  CA  TYR B 196     8808   7486   8008   -602    247   -233       C
ATOM   5230  C   TYR B 196     -21.276  -3.202 -40.114  1.00 55.41           C
ANISOU 5230  C   TYR B 196     7598   6475   6979   -562    205   -219       C
ATOM   5231  O   TYR B 196     -20.161  -2.778 -39.791  1.00 51.42           O
ANISOU 5231  O   TYR B 196     7086   5965   6486   -486    160   -202       O
ATOM   5232  CB  TYR B 196     -21.345  -5.450 -41.258  1.00 59.64           C
ANISOU 5232  CB  TYR B 196     8258   6941   7461   -603    248   -245       C
ATOM   5233  CG  TYR B 196     -20.027  -5.199 -41.952  1.00 63.85           C
ANISOU 5233  CG  TYR B 196     8744   7494   8021   -517    192   -232       C
ATOM   5234  CD1 TYR B 196     -18.824  -5.307 -41.280  1.00 64.88           C
ANISOU 5234  CD1 TYR B 196     8927   7587   8139   -431    151   -221       C
ATOM   5235  CD2 TYR B 196     -19.992  -4.894 -43.309  1.00 64.73           C
ANISOU 5235  CD2 TYR B 196     8763   7664   8167   -522    184   -240       C
ATOM   5236  CE1 TYR B 196     -17.616  -5.098 -41.939  1.00 63.30           C
ANISOU 5236  CE1 TYR B 196     8675   7414   7964   -358    104   -223       C
ATOM   5237  CE2 TYR B 196     -18.803  -4.686 -43.968  1.00 59.07           C
ANISOU 5237  CE2 TYR B 196     8006   6966   7474   -455    142   -235       C
ATOM   5238  CZ  TYR B 196     -17.620  -4.790 -43.278  1.00 57.91           C
ANISOU 5238  CZ  TYR B 196     7900   6787   7316   -376    104   -230       C
ATOM   5239  OH  TYR B 196     -16.442  -4.572 -43.942  1.00 58.31           O
ANISOU 5239  OH  TYR B 196     7900   6866   7390   -315     66   -238       O
ATOM   5240  N   MET B 197     -22.231  -2.396 -40.579  1.00 49.95           N
ANISOU 5240  N   MET B 197     6811   5851   6317   -611    219   -231       N
ATOM   5241  CA  MET B 197     -21.935  -0.977 -40.737  1.00 55.67           C
ANISOU 5241  CA  MET B 197     7432   6634   7086   -573    182   -217       C
ATOM   5242  C   MET B 197     -21.919  -0.265 -39.391  1.00 55.86           C
ANISOU 5242  C   MET B 197     7467   6648   7110   -557    173   -203       C
ATOM   5243  O   MET B 197     -21.184   0.711 -39.218  1.00 44.66           O
ANISOU 5243  O   MET B 197     5998   5251   5719   -505    136   -186       O
ATOM   5244  CB  MET B 197     -22.933  -0.328 -41.701  1.00 58.12           C
ANISOU 5244  CB  MET B 197     7647   7017   7419   -614    192   -236       C
ATOM   5245  CG  MET B 197     -22.999  -1.031 -43.061  1.00 64.27           C
ANISOU 5245  CG  MET B 197     8414   7810   8196   -630    200   -252       C
ATOM   5246  SD  MET B 197     -23.984  -0.241 -44.354  1.00 67.06           S
ANISOU 5246  SD  MET B 197     8657   8250   8571   -654    198   -277       S
ATOM   5247  CE  MET B 197     -25.474   0.163 -43.474  1.00 57.25           C
ANISOU 5247  CE  MET B 197     7390   7043   7320   -712    227   -310       C
ATOM   5248  N   LYS B 198     -22.675  -0.768 -38.416  1.00 54.97           N
ANISOU 5248  N   LYS B 198     7423   6498   6963   -604    210   -212       N
ATOM   5249  CA  LYS B 198     -22.615  -0.265 -37.051  1.00 47.60           C
ANISOU 5249  CA  LYS B 198     6519   5544   6023   -589    204   -199       C
ATOM   5250  C   LYS B 198     -21.486  -0.914 -36.242  1.00 49.82           C
ANISOU 5250  C   LYS B 198     6905   5753   6272   -524    181   -181       C
ATOM   5251  O   LYS B 198     -21.614  -1.102 -35.028  1.00 54.74           O
ANISOU 5251  O   LYS B 198     7607   6330   6863   -526    193   -176       O
ATOM   5252  CB  LYS B 198     -23.978  -0.455 -36.382  1.00 37.31           C
ANISOU 5252  CB  LYS B 198     5242   4239   4695   -673    259   -223       C
ATOM   5253  CG  LYS B 198     -25.099   0.251 -37.128  1.00 34.64           C
ANISOU 5253  CG  LYS B 198     4792   3984   4387   -723    272   -253       C
ATOM   5254  CD  LYS B 198     -26.394   0.257 -36.367  1.00 41.34           C
ANISOU 5254  CD  LYS B 198     5645   4846   5217   -802    322   -288       C
ATOM   5255  CE  LYS B 198     -27.554  -0.121 -37.255  1.00 52.97           C
ANISOU 5255  CE  LYS B 198     7068   6370   6687   -876    360   -340       C
ATOM   5256  NZ  LYS B 198     -27.842   0.924 -38.273  1.00 62.63           N
ANISOU 5256  NZ  LYS B 198     8163   7681   7951   -847    323   -351       N
ATOM   5257  N   SER B 199     -20.368  -1.240 -36.887  1.00 50.64           N
ANISOU 5257  N   SER B 199     7009   5848   6381   -461    146   -176       N
ATOM   5258  CA  SER B 199     -19.242  -1.903 -36.253  1.00 42.11           C
ANISOU 5258  CA  SER B 199     6023   4709   5269   -385    114   -170       C
ATOM   5259  C   SER B 199     -17.947  -1.216 -36.655  1.00 47.17           C
ANISOU 5259  C   SER B 199     6585   5390   5947   -305     58   -171       C
ATOM   5260  O   SER B 199     -17.900  -0.388 -37.567  1.00 52.76           O
ANISOU 5260  O   SER B 199     7183   6161   6701   -315     51   -172       O
ATOM   5261  CB  SER B 199     -19.173  -3.381 -36.632  1.00 45.51           C
ANISOU 5261  CB  SER B 199     6563   5078   5652   -390    134   -180       C
ATOM   5262  OG  SER B 199     -18.221  -3.562 -37.664  1.00 53.58           O
ANISOU 5262  OG  SER B 199     7543   6121   6694   -338     99   -186       O
ATOM   5263  N   SER B 200     -16.885  -1.574 -35.947  1.00 51.58           N
ANISOU 5263  N   SER B 200     7205   5912   6480   -223     20   -175       N
ATOM   5264  CA  SER B 200     -15.580  -0.972 -36.163  1.00 53.84           C
ANISOU 5264  CA  SER B 200     7418   6240   6797   -146    -31   -190       C
ATOM   5265  C   SER B 200     -14.884  -1.529 -37.389  1.00 65.57           C
ANISOU 5265  C   SER B 200     8881   7742   8293   -122    -44   -208       C
ATOM   5266  O   SER B 200     -13.952  -0.896 -37.903  1.00 74.28           O
ANISOU 5266  O   SER B 200     9895   8896   9431    -84    -73   -227       O
ATOM   5267  CB  SER B 200     -14.698  -1.199 -34.938  1.00 54.17           C
ANISOU 5267  CB  SER B 200     7532   6245   6805    -59    -73   -200       C
ATOM   5268  OG  SER B 200     -14.779  -2.556 -34.520  1.00 55.56           O
ANISOU 5268  OG  SER B 200     7856   6340   6915    -37    -67   -200       O
ATOM   5269  N   ARG B 201     -15.302  -2.699 -37.862  1.00 61.03           N
ANISOU 5269  N   ARG B 201     8384   7122   7683   -147    -20   -208       N
ATOM   5270  CA  ARG B 201     -14.668  -3.266 -39.039  1.00 57.67           C
ANISOU 5270  CA  ARG B 201     7938   6710   7265   -124    -32   -226       C
ATOM   5271  C   ARG B 201     -15.011  -2.488 -40.301  1.00 56.48           C
ANISOU 5271  C   ARG B 201     7667   6627   7165   -179    -14   -223       C
ATOM   5272  O   ARG B 201     -14.233  -2.544 -41.257  1.00 61.95           O
ANISOU 5272  O   ARG B 201     8311   7349   7877   -152    -31   -242       O
ATOM   5273  CB  ARG B 201     -15.063  -4.732 -39.186  1.00 47.58           C
ANISOU 5273  CB  ARG B 201     6784   5360   5932   -138     -8   -226       C
ATOM   5274  CG  ARG B 201     -15.192  -5.440 -37.864  1.00 42.83           C
ANISOU 5274  CG  ARG B 201     6328   4678   5269   -112     -6   -219       C
ATOM   5275  CD  ARG B 201     -15.473  -6.948 -38.006  1.00 45.70           C
ANISOU 5275  CD  ARG B 201     6835   4958   5569   -123     21   -221       C
ATOM   5276  NE  ARG B 201     -16.853  -7.281 -38.362  1.00 47.14           N
ANISOU 5276  NE  ARG B 201     7039   5127   5745   -240     91   -213       N
ATOM   5277  CZ  ARG B 201     -17.903  -7.126 -37.560  1.00 50.06           C
ANISOU 5277  CZ  ARG B 201     7448   5473   6097   -312    137   -203       C
ATOM   5278  NH1 ARG B 201     -17.751  -6.619 -36.346  1.00 58.76           N
ANISOU 5278  NH1 ARG B 201     8578   6560   7187   -279    120   -192       N
ATOM   5279  NH2 ARG B 201     -19.117  -7.460 -37.976  1.00 51.64           N
ANISOU 5279  NH2 ARG B 201     7654   5673   6293   -419    201   -210       N
ATOM   5280  N   PHE B 202     -16.126  -1.743 -40.314  1.00 47.97           N
ANISOU 5280  N   PHE B 202     6543   5574   6108   -251     18   -205       N
ATOM   5281  CA  PHE B 202     -16.561  -1.054 -41.528  1.00 46.56           C
ANISOU 5281  CA  PHE B 202     6268   5454   5967   -296     34   -203       C
ATOM   5282  C   PHE B 202     -15.575   0.038 -41.919  1.00 50.71           C
ANISOU 5282  C   PHE B 202     6703   6031   6533   -259      6   -210       C
ATOM   5283  O   PHE B 202     -15.170   0.848 -41.083  1.00 59.79           O
ANISOU 5283  O   PHE B 202     7829   7191   7695   -232    -12   -209       O
ATOM   5284  CB  PHE B 202     -17.955  -0.452 -41.355  1.00 42.23           C
ANISOU 5284  CB  PHE B 202     5693   4926   5426   -366     66   -191       C
ATOM   5285  CG  PHE B 202     -18.670  -0.223 -42.663  1.00 50.42           C
ANISOU 5285  CG  PHE B 202     6668   6009   6482   -413     85   -196       C
ATOM   5286  CD1 PHE B 202     -18.940  -1.290 -43.518  1.00 47.69           C
ANISOU 5286  CD1 PHE B 202     6353   5649   6119   -439    104   -208       C
ATOM   5287  CD2 PHE B 202     -19.051   1.053 -43.056  1.00 49.15           C
ANISOU 5287  CD2 PHE B 202     6422   5901   6351   -426     82   -189       C
ATOM   5288  CE1 PHE B 202     -19.583  -1.088 -44.723  1.00 43.73           C
ANISOU 5288  CE1 PHE B 202     5794   5192   5631   -475    117   -216       C
ATOM   5289  CE2 PHE B 202     -19.697   1.267 -44.256  1.00 49.73           C
ANISOU 5289  CE2 PHE B 202     6447   6015   6434   -457     93   -196       C
ATOM   5290  CZ  PHE B 202     -19.960   0.197 -45.096  1.00 53.32           C
ANISOU 5290  CZ  PHE B 202     6926   6460   6871   -481    110   -211       C
ATOM   5291  N   LEU B 203     -15.193   0.058 -43.196  1.00 53.85           N
ANISOU 5291  N   LEU B 203     7052   6459   6948   -263      7   -221       N
ATOM   5292  CA  LEU B 203     -14.250   1.026 -43.761  1.00 50.05           C
ANISOU 5292  CA  LEU B 203     6491   6026   6501   -242     -7   -234       C
ATOM   5293  C   LEU B 203     -14.983   1.750 -44.886  1.00 58.26           C
ANISOU 5293  C   LEU B 203     7476   7102   7559   -294     17   -221       C
ATOM   5294  O   LEU B 203     -15.037   1.264 -46.017  1.00 62.91           O
ANISOU 5294  O   LEU B 203     8060   7699   8146   -309     28   -227       O
ATOM   5295  CB  LEU B 203     -12.967   0.336 -44.261  1.00 43.99           C
ANISOU 5295  CB  LEU B 203     5724   5260   5731   -191    -28   -268       C
ATOM   5296  CG  LEU B 203     -11.912   1.196 -44.975  1.00 52.52           C
ANISOU 5296  CG  LEU B 203     6722   6391   6842   -180    -32   -295       C
ATOM   5297  CD1 LEU B 203     -11.367   2.281 -44.056  1.00 61.86           C
ANISOU 5297  CD1 LEU B 203     7864   7595   8043   -161    -45   -306       C
ATOM   5298  CD2 LEU B 203     -10.771   0.354 -45.483  1.00 54.34           C
ANISOU 5298  CD2 LEU B 203     6954   6629   7066   -133    -52   -337       C
ATOM   5299  N   ARG B 204     -15.547   2.920 -44.576  1.00 59.57           N
ANISOU 5299  N   ARG B 204     7606   7288   7739   -315     24   -204       N
ATOM   5300  CA  ARG B 204     -16.409   3.600 -45.538  1.00 69.88           C
ANISOU 5300  CA  ARG B 204     8875   8623   9052   -354     41   -192       C
ATOM   5301  C   ARG B 204     -15.635   4.469 -46.518  1.00 72.06           C
ANISOU 5301  C   ARG B 204     9105   8929   9346   -349     44   -198       C
ATOM   5302  O   ARG B 204     -16.199   4.893 -47.534  1.00 72.47           O
ANISOU 5302  O   ARG B 204     9140   9001   9396   -372     56   -191       O
ATOM   5303  CB  ARG B 204     -17.444   4.456 -44.807  1.00 74.09           C
ANISOU 5303  CB  ARG B 204     9398   9165   9587   -374     46   -176       C
ATOM   5304  CG  ARG B 204     -16.868   5.338 -43.716  1.00 75.48           C
ANISOU 5304  CG  ARG B 204     9562   9339   9777   -351     33   -171       C
ATOM   5305  CD  ARG B 204     -17.973   5.829 -42.804  1.00 77.07           C
ANISOU 5305  CD  ARG B 204     9768   9541   9975   -370     37   -157       C
ATOM   5306  NE  ARG B 204     -19.071   6.421 -43.559  1.00 82.96           N
ANISOU 5306  NE  ARG B 204    10485  10318  10718   -397     47   -153       N
ATOM   5307  CZ  ARG B 204     -19.112   7.694 -43.955  1.00 87.80           C
ANISOU 5307  CZ  ARG B 204    11065  10954  11341   -391     44   -144       C
ATOM   5308  NH1 ARG B 204     -18.110   8.524 -43.667  1.00 78.76           N
ANISOU 5308  NH1 ARG B 204     9908   9806  10213   -371     38   -141       N
ATOM   5309  NH2 ARG B 204     -20.163   8.142 -44.638  1.00 92.01           N
ANISOU 5309  NH2 ARG B 204    11581  11514  11864   -403     46   -145       N
ATOM   5310  N   SER B 205     -14.374   4.749 -46.227  1.00 70.69           N
ANISOU 5310  N   SER B 205     8914   8759   9187   -321     35   -217       N
ATOM   5311  CA  SER B 205     -13.516   5.563 -47.073  1.00 68.87           C
ANISOU 5311  CA  SER B 205     8643   8554   8970   -327     47   -233       C
ATOM   5312  C   SER B 205     -12.100   5.471 -46.511  1.00 64.76           C
ANISOU 5312  C   SER B 205     8103   8041   8462   -292     34   -271       C
ATOM   5313  O   SER B 205     -11.926   5.084 -45.354  1.00 72.64           O
ANISOU 5313  O   SER B 205     9118   9024   9457   -259     11   -277       O
ATOM   5314  CB  SER B 205     -14.011   7.022 -47.133  1.00 69.95           C
ANISOU 5314  CB  SER B 205     8763   8703   9113   -350     61   -212       C
ATOM   5315  OG  SER B 205     -13.341   7.847 -46.200  1.00 80.13           O
ANISOU 5315  OG  SER B 205    10033   9995  10417   -339     58   -223       O
ATOM   5316  N   PRO B 206     -11.070   5.803 -47.306  1.00 52.19           N
ANISOU 5316  N   PRO B 206     6474   6474   6881   -297     48   -304       N
ATOM   5317  CA  PRO B 206     -10.989   6.407 -48.643  1.00 51.59           C
ANISOU 5317  CA  PRO B 206     6382   6414   6805   -336     79   -305       C
ATOM   5318  C   PRO B 206     -11.596   5.558 -49.740  1.00 55.56           C
ANISOU 5318  C   PRO B 206     6908   6910   7292   -346     84   -290       C
ATOM   5319  O   PRO B 206     -11.508   4.328 -49.680  1.00 53.89           O
ANISOU 5319  O   PRO B 206     6714   6689   7074   -323     66   -300       O
ATOM   5320  CB  PRO B 206      -9.470   6.565 -48.887  1.00 47.62           C
ANISOU 5320  CB  PRO B 206     5836   5940   6316   -331     90   -363       C
ATOM   5321  CG  PRO B 206      -8.796   6.206 -47.612  1.00 49.68           C
ANISOU 5321  CG  PRO B 206     6083   6207   6586   -284     58   -395       C
ATOM   5322  CD  PRO B 206      -9.750   5.348 -46.838  1.00 52.31           C
ANISOU 5322  CD  PRO B 206     6467   6505   6904   -256     28   -357       C
ATOM   5323  N   LEU B 207     -12.188   6.230 -50.735  1.00 56.98           N
ANISOU 5323  N   LEU B 207     7094   7093   7462   -378    106   -268       N
ATOM   5324  CA  LEU B 207     -12.741   5.526 -51.892  1.00 57.53           C
ANISOU 5324  CA  LEU B 207     7181   7162   7516   -389    111   -259       C
ATOM   5325  C   LEU B 207     -11.640   5.021 -52.822  1.00 56.03           C
ANISOU 5325  C   LEU B 207     6975   6985   7328   -390    124   -295       C
ATOM   5326  O   LEU B 207     -11.717   3.890 -53.311  1.00 55.05           O
ANISOU 5326  O   LEU B 207     6862   6859   7197   -381    116   -302       O
ATOM   5327  CB  LEU B 207     -13.713   6.434 -52.653  1.00 46.04           C
ANISOU 5327  CB  LEU B 207     5742   5708   6042   -410    125   -230       C
ATOM   5328  CG  LEU B 207     -15.177   6.360 -52.215  1.00 48.38           C
ANISOU 5328  CG  LEU B 207     6054   6002   6328   -406    107   -202       C
ATOM   5329  CD1 LEU B 207     -15.350   6.869 -50.805  1.00 57.65           C
ANISOU 5329  CD1 LEU B 207     7222   7168   7514   -397     95   -193       C
ATOM   5330  CD2 LEU B 207     -16.043   7.164 -53.159  1.00 56.96           C
ANISOU 5330  CD2 LEU B 207     7155   7097   7390   -413    113   -185       C
ATOM   5331  N   PHE B 208     -10.614   5.835 -53.076  1.00 53.51           N
ANISOU 5331  N   PHE B 208     6632   6683   7018   -406    149   -323       N
ATOM   5332  CA  PHE B 208      -9.530   5.493 -53.994  1.00 53.55           C
ANISOU 5332  CA  PHE B 208     6614   6708   7025   -416    168   -367       C
ATOM   5333  C   PHE B 208      -8.168   5.581 -53.297  1.00 61.31           C
ANISOU 5333  C   PHE B 208     7551   7716   8029   -402    167   -425       C
ATOM   5334  O   PHE B 208      -8.083   5.751 -52.080  1.00 64.55           O
ANISOU 5334  O   PHE B 208     7950   8125   8450   -377    145   -429       O
ATOM   5335  CB  PHE B 208      -9.583   6.402 -55.216  1.00 50.69           C
ANISOU 5335  CB  PHE B 208     6269   6345   6645   -460    210   -358       C
ATOM   5336  CG  PHE B 208     -10.895   6.375 -55.921  1.00 51.71           C
ANISOU 5336  CG  PHE B 208     6440   6457   6750   -463    205   -311       C
ATOM   5337  CD1 PHE B 208     -11.321   5.233 -56.565  1.00 47.58           C
ANISOU 5337  CD1 PHE B 208     5925   5936   6218   -451    190   -307       C
ATOM   5338  CD2 PHE B 208     -11.706   7.495 -55.950  1.00 53.19           C
ANISOU 5338  CD2 PHE B 208     6659   6630   6919   -473    213   -275       C
ATOM   5339  CE1 PHE B 208     -12.535   5.205 -57.227  1.00 49.23           C
ANISOU 5339  CE1 PHE B 208     6164   6138   6403   -453    184   -274       C
ATOM   5340  CE2 PHE B 208     -12.925   7.471 -56.616  1.00 51.38           C
ANISOU 5340  CE2 PHE B 208     6464   6395   6665   -466    201   -242       C
ATOM   5341  CZ  PHE B 208     -13.339   6.321 -57.249  1.00 50.20           C
ANISOU 5341  CZ  PHE B 208     6312   6253   6508   -457    187   -244       C
ATOM   5342  N   LEU B 209      -7.095   5.469 -54.089  1.00 64.85           N
ANISOU 5342  N   LEU B 209     7968   8192   8481   -417    192   -478       N
ATOM   5343  CA  LEU B 209      -5.721   5.569 -53.602  1.00 64.39           C
ANISOU 5343  CA  LEU B 209     7852   8173   8441   -406    194   -553       C
ATOM   5344  C   LEU B 209      -5.295   7.030 -53.399  1.00 65.51           C
ANISOU 5344  C   LEU B 209     7975   8325   8590   -455    236   -571       C
ATOM   5345  O   LEU B 209      -5.988   7.978 -53.783  1.00 63.20           O
ANISOU 5345  O   LEU B 209     7723   8005   8284   -497    267   -525       O
ATOM   5346  CB  LEU B 209      -4.730   4.905 -54.563  1.00 64.24           C
ANISOU 5346  CB  LEU B 209     7799   8186   8422   -409    208   -614       C
ATOM   5347  CG  LEU B 209      -4.493   3.391 -54.719  1.00 53.70           C
ANISOU 5347  CG  LEU B 209     6463   6858   7084   -353    168   -636       C
ATOM   5348  CD1 LEU B 209      -4.465   2.682 -53.349  1.00 49.36           C
ANISOU 5348  CD1 LEU B 209     5919   6300   6537   -279    110   -642       C
ATOM   5349  CD2 LEU B 209      -5.415   2.709 -55.722  1.00 56.00           C
ANISOU 5349  CD2 LEU B 209     6803   7119   7356   -363    170   -585       C
ATOM   5350  N   LYS B 210      -4.100   7.193 -52.816  1.00 66.13           N
ANISOU 5350  N   LYS B 210     7993   8445   8687   -448    239   -647       N
ATOM   5351  CA  LYS B 210      -3.620   8.507 -52.391  1.00 63.72           C
ANISOU 5351  CA  LYS B 210     7665   8153   8391   -493    277   -676       C
ATOM   5352  C   LYS B 210      -3.365   9.440 -53.568  1.00 64.20           C
ANISOU 5352  C   LYS B 210     7745   8211   8439   -576    351   -687       C
ATOM   5353  O   LYS B 210      -3.553  10.657 -53.440  1.00 65.50           O
ANISOU 5353  O   LYS B 210     7936   8354   8596   -623    390   -669       O
ATOM   5354  CB  LYS B 210      -2.336   8.364 -51.574  1.00 61.93           C
ANISOU 5354  CB  LYS B 210     7359   7984   8187   -465    262   -771       C
ATOM   5355  CG  LYS B 210      -2.515   8.143 -50.072  1.00 66.15           C
ANISOU 5355  CG  LYS B 210     7886   8516   8731   -398    204   -763       C
ATOM   5356  CD  LYS B 210      -1.259   7.452 -49.493  1.00 76.99           C
ANISOU 5356  CD  LYS B 210     9187   9950  10117   -337    167   -863       C
ATOM   5357  CE  LYS B 210      -1.345   7.223 -47.990  1.00 81.61           C
ANISOU 5357  CE  LYS B 210     9771  10532  10704   -263    107   -861       C
ATOM   5358  NZ  LYS B 210      -1.122   8.483 -47.219  1.00 92.67           N
ANISOU 5358  NZ  LYS B 210    11143  11948  12120   -298    131   -881       N
ATOM   5359  N   MET B 211      -2.930   8.904 -54.711  1.00 57.56           N
ANISOU 5359  N   MET B 211     6896   7385   7588   -595    374   -716       N
ATOM   5360  CA  MET B 211      -2.673   9.735 -55.882  1.00 59.64           C
ANISOU 5360  CA  MET B 211     7190   7639   7830   -676    450   -728       C
ATOM   5361  C   MET B 211      -3.940  10.041 -56.684  1.00 70.47           C
ANISOU 5361  C   MET B 211     8655   8951   9169   -688    458   -635       C
ATOM   5362  O   MET B 211      -3.839  10.522 -57.818  1.00 77.89           O
ANISOU 5362  O   MET B 211     9638   9875  10080   -743    513   -635       O
ATOM   5363  CB  MET B 211      -1.619   9.076 -56.777  1.00 59.95           C
ANISOU 5363  CB  MET B 211     7182   7725   7873   -695    475   -806       C
ATOM   5364  CG  MET B 211      -2.133   7.905 -57.618  1.00 56.90           C
ANISOU 5364  CG  MET B 211     6819   7325   7474   -658    444   -770       C
ATOM   5365  SD  MET B 211      -2.341   6.402 -56.653  1.00 60.25           S
ANISOU 5365  SD  MET B 211     7211   7763   7918   -552    350   -764       S
ATOM   5366  CE  MET B 211      -0.688   6.186 -56.007  1.00 63.60           C
ANISOU 5366  CE  MET B 211     7531   8265   8369   -531    344   -893       C
ATOM   5367  N   ALA B 212      -5.120   9.785 -56.122  1.00 68.82           N
ANISOU 5367  N   ALA B 212     8478   8712   8958   -638    405   -562       N
ATOM   5368  CA  ALA B 212      -6.366  10.162 -56.766  1.00 61.69           C
ANISOU 5368  CA  ALA B 212     7655   7763   8023   -641    406   -485       C
ATOM   5369  C   ALA B 212      -6.605  11.653 -56.610  1.00 64.68           C
ANISOU 5369  C   ALA B 212     8085   8109   8382   -679    444   -462       C
ATOM   5370  O   ALA B 212      -6.149  12.277 -55.650  1.00 74.43           O
ANISOU 5370  O   ALA B 212     9292   9353   9635   -690    452   -487       O
ATOM   5371  CB  ALA B 212      -7.544   9.397 -56.171  1.00 48.79           C
ANISOU 5371  CB  ALA B 212     6028   6116   6393   -580    341   -429       C
ATOM   5372  N   MET B 213      -7.326  12.223 -57.571  1.00 63.97           N
ANISOU 5372  N   MET B 213     8076   7981   8250   -696    467   -417       N
ATOM   5373  CA  MET B 213      -7.703  13.627 -57.508  1.00 63.83           C
ANISOU 5373  CA  MET B 213     8129   7920   8202   -721    498   -388       C
ATOM   5374  C   MET B 213      -8.961  13.850 -56.687  1.00 70.35           C
ANISOU 5374  C   MET B 213     8976   8728   9027   -668    444   -328       C
ATOM   5375  O   MET B 213      -9.320  15.008 -56.444  1.00 79.97           O
ANISOU 5375  O   MET B 213    10250   9912  10222   -677    461   -304       O
ATOM   5376  CB  MET B 213      -7.905  14.188 -58.923  1.00 54.34           C
ANISOU 5376  CB  MET B 213     7023   6680   6945   -754    545   -368       C
ATOM   5377  CG  MET B 213      -6.673  14.147 -59.801  1.00 61.45           C
ANISOU 5377  CG  MET B 213     7917   7594   7839   -821    613   -430       C
ATOM   5378  SD  MET B 213      -5.223  14.966 -59.108  1.00 67.08           S
ANISOU 5378  SD  MET B 213     8584   8328   8576   -898    681   -513       S
ATOM   5379  CE  MET B 213      -5.803  16.645 -59.034  1.00 69.75           C
ANISOU 5379  CE  MET B 213     9044   8593   8864   -926    722   -466       C
ATOM   5380  N   TRP B 214      -9.630  12.774 -56.271  1.00 66.01           N
ANISOU 5380  N   TRP B 214     8384   8197   8498   -615    384   -308       N
ATOM   5381  CA  TRP B 214     -10.845  12.821 -55.467  1.00 54.84           C
ANISOU 5381  CA  TRP B 214     6978   6775   7085   -568    334   -261       C
ATOM   5382  C   TRP B 214     -10.979  11.484 -54.754  1.00 53.78           C
ANISOU 5382  C   TRP B 214     6781   6668   6984   -532    286   -268       C
ATOM   5383  O   TRP B 214     -10.482  10.461 -55.234  1.00 56.77           O
ANISOU 5383  O   TRP B 214     7131   7065   7373   -531    283   -293       O
ATOM   5384  CB  TRP B 214     -12.083  13.108 -56.329  1.00 54.94           C
ANISOU 5384  CB  TRP B 214     7058   6764   7053   -544    320   -215       C
ATOM   5385  CG  TRP B 214     -13.362  13.201 -55.539  1.00 57.43           C
ANISOU 5385  CG  TRP B 214     7373   7079   7367   -499    271   -179       C
ATOM   5386  CD1 TRP B 214     -13.892  14.326 -54.971  1.00 60.70           C
ANISOU 5386  CD1 TRP B 214     7823   7473   7767   -487    267   -157       C
ATOM   5387  CD2 TRP B 214     -14.269  12.125 -55.219  1.00 48.44           C
ANISOU 5387  CD2 TRP B 214     6197   5964   6243   -464    223   -168       C
ATOM   5388  NE1 TRP B 214     -15.067  14.015 -54.322  1.00 59.83           N
ANISOU 5388  NE1 TRP B 214     7693   7378   7663   -445    218   -136       N
ATOM   5389  CE2 TRP B 214     -15.314  12.673 -54.455  1.00 45.08           C
ANISOU 5389  CE2 TRP B 214     5781   5536   5812   -435    194   -144       C
ATOM   5390  CE3 TRP B 214     -14.290  10.755 -55.502  1.00 50.78           C
ANISOU 5390  CE3 TRP B 214     6459   6281   6554   -458    206   -181       C
ATOM   5391  CZ2 TRP B 214     -16.366  11.908 -53.978  1.00 44.92           C
ANISOU 5391  CZ2 TRP B 214     5731   5537   5800   -408    154   -137       C
ATOM   5392  CZ3 TRP B 214     -15.336   9.992 -55.021  1.00 51.54           C
ANISOU 5392  CZ3 TRP B 214     6534   6392   6656   -432    167   -170       C
ATOM   5393  CH2 TRP B 214     -16.359  10.568 -54.268  1.00 50.96           C
ANISOU 5393  CH2 TRP B 214     6465   6319   6577   -411    144   -150       C
ATOM   5394  N   GLY B 215     -11.639  11.496 -53.597  1.00 52.18           N
ANISOU 5394  N   GLY B 215     6565   6465   6797   -503    250   -247       N
ATOM   5395  CA  GLY B 215     -11.830  10.268 -52.850  1.00 47.24           C
ANISOU 5395  CA  GLY B 215     5900   5855   6195   -471    209   -250       C
ATOM   5396  C   GLY B 215     -10.590   9.717 -52.178  1.00 49.55           C
ANISOU 5396  C   GLY B 215     6143   6168   6517   -466    207   -298       C
ATOM   5397  O   GLY B 215     -10.646   8.614 -51.619  1.00 48.20           O
ANISOU 5397  O   GLY B 215     5954   6002   6357   -434    174   -304       O
ATOM   5398  N   ASN B 216      -9.469  10.431 -52.228  1.00 59.59           N
ANISOU 5398  N   ASN B 216     7395   7450   7797   -496    242   -339       N
ATOM   5399  CA  ASN B 216      -8.246  10.027 -51.551  1.00 65.76           C
ANISOU 5399  CA  ASN B 216     8119   8262   8605   -486    237   -398       C
ATOM   5400  C   ASN B 216      -8.260  10.547 -50.126  1.00 78.05           C
ANISOU 5400  C   ASN B 216     9660   9819  10178   -468    218   -398       C
ATOM   5401  O   ASN B 216      -8.756  11.646 -49.863  1.00 91.94           O
ANISOU 5401  O   ASN B 216    11445  11559  11930   -488    233   -369       O
ATOM   5402  CB  ASN B 216      -7.025  10.572 -52.285  1.00 63.65           C
ANISOU 5402  CB  ASN B 216     7829   8017   8339   -534    290   -457       C
ATOM   5403  CG  ASN B 216      -7.048  12.091 -52.413  1.00 66.93           C
ANISOU 5403  CG  ASN B 216     8279   8411   8739   -586    339   -448       C
ATOM   5404  OD1 ASN B 216      -8.104  12.702 -52.600  1.00 60.92           O
ANISOU 5404  OD1 ASN B 216     7577   7613   7956   -587    338   -388       O
ATOM   5405  ND2 ASN B 216      -5.876  12.704 -52.331  1.00 75.79           N
ANISOU 5405  ND2 ASN B 216     9367   9557   9873   -629    382   -513       N
ATOM   5406  N   LYS B 217      -7.746   9.753 -49.197  1.00 87.64           N
ANISOU 5406  N   LYS B 217    10838  11053  11410   -425    181   -429       N
ATOM   5407  CA  LYS B 217      -7.597  10.269 -47.828  1.00106.53           C
ANISOU 5407  CA  LYS B 217    13212  13448  13817   -406    164   -438       C
ATOM   5408  C   LYS B 217      -6.301   9.766 -47.166  1.00116.95           C
ANISOU 5408  C   LYS B 217    14474  14808  15153   -371    144   -513       C
ATOM   5409  O   LYS B 217      -5.220   9.788 -47.767  1.00119.32           O
ANISOU 5409  O   LYS B 217    14732  15144  15461   -391    169   -578       O
ATOM   5410  CB  LYS B 217      -8.812   9.909 -46.947  1.00 99.79           C
ANISOU 5410  CB  LYS B 217    12393  12565  12956   -372    125   -379       C
ATOM   5411  CG  LYS B 217     -10.156   9.773 -47.669  1.00 86.11           C
ANISOU 5411  CG  LYS B 217    10708  10805  11204   -385    127   -319       C
ATOM   5412  CD  LYS B 217     -10.912  11.070 -47.724  1.00 78.50           C
ANISOU 5412  CD  LYS B 217     9770   9826  10232   -413    147   -283       C
ATOM   5413  CE  LYS B 217     -12.130  10.944 -48.620  1.00 72.92           C
ANISOU 5413  CE  LYS B 217     9102   9104   9501   -418    146   -240       C
ATOM   5414  NZ  LYS B 217     -13.117  12.029 -48.342  1.00 69.04           N
ANISOU 5414  NZ  LYS B 217     8637   8598   8997   -422    146   -203       N
ATOM   5415  OXT LYS B 217      -6.295   9.348 -46.004  1.00116.37           O
ANISOU 5415  OXT LYS B 217    14395  14735  15084   -320    102   -517       O
TER
HETATM 5416  CB1 GSH B 701      -8.075  -5.031 -60.537  1.00 71.12           C
ANISOU 5416  CB1 GSH B 701     8930   8925   9168   -293    106   -518       C
HETATM 5417  CB2 GSH B 701      -5.817  -2.191 -56.568  1.00 77.38           C
ANISOU 5417  CB2 GSH B 701     9611   9772  10017   -220     68   -592       C
HETATM 5418  CG1 GSH B 701      -6.602  -5.044 -60.232  1.00 71.89           C
ANISOU 5418  CG1 GSH B 701     8985   9053   9278   -251     93   -581       C
HETATM 5419  SG2 GSH B 701      -7.143  -1.070 -56.997  1.00 79.38           S
ANISOU 5419  SG2 GSH B 701     9882  10009  10270   -294    106   -519       S
HETATM 5420  CD1 GSH B 701      -6.019  -3.803 -59.642  1.00 79.58           C
ANISOU 5420  CD1 GSH B 701     9910  10055  10270   -261    103   -599       C
HETATM 5421  OE1 GSH B 701      -6.180  -2.734 -60.223  1.00 73.41           O
ANISOU 5421  OE1 GSH B 701     9108   9290   9495   -315    140   -584       O
HETATM 5422  C1  GSH B 701      -9.594  -7.013 -60.028  1.00 59.55           C
ANISOU 5422  C1  GSH B 701     7576   7382   7667   -277     82   -479       C
HETATM 5423  C2  GSH B 701      -3.451  -2.796 -57.307  1.00 77.30           C
ANISOU 5423  C2  GSH B 701     9509   9843  10017   -170     61   -734       C
HETATM 5424  C3  GSH B 701      -0.343  -4.625 -58.639  1.00 91.91           C
ANISOU 5424  C3  GSH B 701    11242  11815  11865    -61     27   -961       C
HETATM 5425  CA1 GSH B 701      -8.640  -6.351 -61.014  1.00 68.81           C
ANISOU 5425  CA1 GSH B 701     8686   8604   8856   -287     98   -510       C
HETATM 5426  CA2 GSH B 701      -4.916  -2.701 -57.641  1.00 76.71           C
ANISOU 5426  CA2 GSH B 701     9493   9720   9932   -216     78   -646       C
HETATM 5427  CA3 GSH B 701      -1.236  -3.972 -57.599  1.00 87.68           C
ANISOU 5427  CA3 GSH B 701    10747  11237  11332    -74     22   -891       C
HETATM 5428  N1  GSH B 701      -9.052  -6.319 -62.424  1.00 69.75           N
ANISOU 5428  N1  GSH B 701     8796   8738   8967   -329    124   -501       N
HETATM 5429  N2  GSH B 701      -5.435  -3.891 -58.324  1.00 82.81           N
ANISOU 5429  N2  GSH B 701    10313  10464  10686   -206     69   -626       N
HETATM 5430  N3  GSH B 701      -2.668  -3.923 -57.819  1.00 83.64           N
ANISOU 5430  N3  GSH B 701    10305  10665  10811   -121     39   -791       N
HETATM 5431  O11 GSH B 701     -10.791  -6.356 -59.866  1.00 58.95           O
ANISOU 5431  O11 GSH B 701     7505   7302   7592   -321     96   -436       O
HETATM 5432  O12 GSH B 701      -9.048  -7.475 -58.836  1.00 58.64           O
ANISOU 5432  O12 GSH B 701     7492   7243   7547   -223     52   -495       O
HETATM 5433  O2  GSH B 701      -2.857  -1.812 -56.914  1.00 70.30           O
ANISOU 5433  O2  GSH B 701     8572   8991   9148   -186     76   -767       O
HETATM 5434  O31 GSH B 701       0.763  -5.271 -58.120  1.00 93.75           O
ANISOU 5434  O31 GSH B 701    11440  12087  12093     27    -21  -1050       O
HETATM 5435  O32 GSH B 701      -1.007  -5.361 -59.624  1.00 91.17           O
ANISOU 5435  O32 GSH B 701    11198  11687  11757    -81     38   -917       O
TER
ATOM   5436  N   PRO D   1     -31.760 -17.045 -86.840  1.00 79.58           N
ANISOU 5436  N   PRO D   1     9549  11054   9633   -656     64  -1492       N
ATOM   5437  CA  PRO D   1     -30.371 -17.022 -86.378  1.00 79.70           C
ANISOU 5437  CA  PRO D   1     9651  10953   9679   -666     91  -1375       C
ATOM   5438  C   PRO D   1     -30.088 -15.919 -85.365  1.00 76.90           C
ANISOU 5438  C   PRO D   1     9319  10563   9337   -632     77  -1308       C
ATOM   5439  O   PRO D   1     -30.796 -14.917 -85.265  1.00 73.09           O
ANISOU 5439  O   PRO D   1     8801  10139   8829   -572     32  -1332       O
ATOM   5440  CB  PRO D   1     -29.583 -16.767 -87.666  1.00 72.01           C
ANISOU 5440  CB  PRO D   1     8723   9963   8675   -599     64  -1328       C
ATOM   5441  CG  PRO D   1     -30.518 -15.968 -88.506  1.00 70.31           C
ANISOU 5441  CG  PRO D   1     8464   9844   8406   -514      1  -1387       C
ATOM   5442  CD  PRO D   1     -31.880 -16.534 -88.219  1.00 72.31           C
ANISOU 5442  CD  PRO D   1     8624  10188   8661   -562      6  -1508       C
ATOM   5443  N   MET D   2     -29.015 -16.118 -84.620  1.00 68.65           N
ANISOU 5443  N   MET D   2     8334   9421   8327   -665    112  -1226       N
ATOM   5444  CA  MET D   2     -28.560 -15.102 -83.702  1.00 64.51           C
ANISOU 5444  CA  MET D   2     7837   8856   7817   -634    102  -1156       C
ATOM   5445  C   MET D   2     -28.011 -13.911 -84.466  1.00 64.88           C
ANISOU 5445  C   MET D   2     7921   8900   7832   -540     58  -1100       C
ATOM   5446  O   MET D   2     -27.581 -14.027 -85.617  1.00 61.87           O
ANISOU 5446  O   MET D   2     7566   8518   7426   -510     48  -1091       O
ATOM   5447  CB  MET D   2     -27.481 -15.669 -82.800  1.00 58.44           C
ANISOU 5447  CB  MET D   2     7125   7988   7091   -686    148  -1090       C
ATOM   5448  CG  MET D   2     -27.865 -16.949 -82.150  1.00 65.83           C
ANISOU 5448  CG  MET D   2     8056   8907   8051   -779    198  -1137       C
ATOM   5449  SD  MET D   2     -26.472 -17.480 -81.173  1.00 73.87           S
ANISOU 5449  SD  MET D   2     9157   9804   9106   -810    238  -1054       S
ATOM   5450  CE  MET D   2     -26.418 -19.207 -81.586  1.00 74.60           C
ANISOU 5450  CE  MET D   2     9278   9865   9200   -883    285  -1098       C
ATOM   5451  N   ILE D   3     -27.995 -12.758 -83.802  1.00 55.53           N
ANISOU 5451  N   ILE D   3     6748   7706   6644   -497     35  -1061       N
ATOM   5452  CA  ILE D   3     -27.399 -11.560 -84.377  1.00 60.56           C
ANISOU 5452  CA  ILE D   3     7438   8323   7247   -416      3  -1001       C
ATOM   5453  C   ILE D   3     -26.295 -11.079 -83.465  1.00 55.30           C
ANISOU 5453  C   ILE D   3     6822   7576   6615   -430     28   -916       C
ATOM   5454  O   ILE D   3     -26.532 -10.818 -82.283  1.00 61.57           O
ANISOU 5454  O   ILE D   3     7598   8360   7436   -449     34   -908       O
ATOM   5455  CB  ILE D   3     -28.414 -10.431 -84.598  1.00 61.57           C
ANISOU 5455  CB  ILE D   3     7546   8520   7327   -334    -54  -1036       C
ATOM   5456  CG1 ILE D   3     -29.661 -10.943 -85.322  1.00 62.14           C
ANISOU 5456  CG1 ILE D   3     7550   8691   7369   -321    -83  -1141       C
ATOM   5457  CG2 ILE D   3     -27.725  -9.269 -85.338  1.00 44.25           C
ANISOU 5457  CG2 ILE D   3     5435   6292   5088   -254    -80   -971       C
ATOM   5458  CD1 ILE D   3     -30.697  -9.871 -85.526  1.00 63.28           C
ANISOU 5458  CD1 ILE D   3     7671   8912   7462   -228   -148  -1188       C
ATOM   5459  N   LEU D   4     -25.111 -10.931 -84.027  1.00 49.34           N
ANISOU 5459  N   LEU D   4     6124   6766   5856   -418     43   -858       N
ATOM   5460  CA  LEU D   4     -23.966 -10.336 -83.369  1.00 46.71           C
ANISOU 5460  CA  LEU D   4     5837   6364   5547   -422     64   -785       C
ATOM   5461  C   LEU D   4     -23.723  -8.990 -84.041  1.00 63.64           C
ANISOU 5461  C   LEU D   4     8036   8503   7642   -354     40   -749       C
ATOM   5462  O   LEU D   4     -23.306  -8.939 -85.205  1.00 65.51           O
ANISOU 5462  O   LEU D   4     8312   8735   7843   -331     41   -743       O
ATOM   5463  CB  LEU D   4     -22.754 -11.242 -83.496  1.00 47.58           C
ANISOU 5463  CB  LEU D   4     5971   6420   5689   -467    104   -759       C
ATOM   5464  CG  LEU D   4     -21.457 -10.722 -82.908  1.00 49.49           C
ANISOU 5464  CG  LEU D   4     6250   6598   5955   -471    127   -697       C
ATOM   5465  CD1 LEU D   4     -21.500 -10.843 -81.389  1.00 44.66           C
ANISOU 5465  CD1 LEU D   4     5619   5962   5387   -502    137   -686       C
ATOM   5466  CD2 LEU D   4     -20.285 -11.484 -83.504  1.00 36.24           C
ANISOU 5466  CD2 LEU D   4     4594   4885   4290   -494    157   -686       C
ATOM   5467  N   GLY D   5     -24.008  -7.907 -83.322  1.00 60.28           N
ANISOU 5467  N   GLY D   5     7621   8075   7209   -322     22   -728       N
ATOM   5468  CA  GLY D   5     -23.702  -6.564 -83.786  1.00 60.82           C
ANISOU 5468  CA  GLY D   5     7759   8122   7228   -262      7   -688       C
ATOM   5469  C   GLY D   5     -22.365  -6.109 -83.226  1.00 57.27           C
ANISOU 5469  C   GLY D   5     7353   7599   6806   -292     47   -623       C
ATOM   5470  O   GLY D   5     -22.054  -6.360 -82.066  1.00 64.15           O
ANISOU 5470  O   GLY D   5     8194   8449   7731   -334     66   -609       O
ATOM   5471  N   TYR D   6     -21.577  -5.453 -84.073  1.00 56.07           N
ANISOU 5471  N   TYR D   6     7274   7413   6616   -273     63   -590       N
ATOM   5472  CA  TYR D   6     -20.269  -4.937 -83.689  1.00 48.65           C
ANISOU 5472  CA  TYR D   6     6376   6411   5696   -305    107   -541       C
ATOM   5473  C   TYR D   6     -19.772  -4.022 -84.795  1.00 54.49           C
ANISOU 5473  C   TYR D   6     7210   7122   6370   -276    120   -518       C
ATOM   5474  O   TYR D   6     -20.396  -3.901 -85.852  1.00 64.95           O
ANISOU 5474  O   TYR D   6     8570   8473   7637   -228     93   -536       O
ATOM   5475  CB  TYR D   6     -19.252  -6.056 -83.424  1.00 44.85           C
ANISOU 5475  CB  TYR D   6     5857   5909   5273   -369    146   -543       C
ATOM   5476  CG  TYR D   6     -18.029  -5.576 -82.664  1.00 54.06           C
ANISOU 5476  CG  TYR D   6     7039   7027   6472   -401    184   -507       C
ATOM   5477  CD1 TYR D   6     -18.165  -4.859 -81.470  1.00 52.77           C
ANISOU 5477  CD1 TYR D   6     6869   6850   6330   -397    177   -486       C
ATOM   5478  CD2 TYR D   6     -16.742  -5.812 -83.146  1.00 55.88           C
ANISOU 5478  CD2 TYR D   6     7288   7231   6712   -434    226   -503       C
ATOM   5479  CE1 TYR D   6     -17.054  -4.395 -80.775  1.00 56.45           C
ANISOU 5479  CE1 TYR D   6     7345   7278   6825   -426    211   -461       C
ATOM   5480  CE2 TYR D   6     -15.617  -5.354 -82.450  1.00 62.55           C
ANISOU 5480  CE2 TYR D   6     8137   8042   7586   -464    261   -484       C
ATOM   5481  CZ  TYR D   6     -15.782  -4.643 -81.267  1.00 60.33           C
ANISOU 5481  CZ  TYR D   6     7848   7748   7325   -459    253   -463       C
ATOM   5482  OH  TYR D   6     -14.676  -4.198 -80.576  1.00 57.47           O
ANISOU 5482  OH  TYR D   6     7486   7358   6992   -488    286   -452       O
ATOM   5483  N   TRP D   7     -18.633  -3.379 -84.533  1.00 55.03           N
ANISOU 5483  N   TRP D   7     7323   7139   6448   -307    165   -481       N
ATOM   5484  CA  TRP D   7     -17.942  -2.564 -85.519  1.00 58.16           C
ANISOU 5484  CA  TRP D   7     7817   7496   6784   -302    197   -460       C
ATOM   5485  C   TRP D   7     -17.312  -3.453 -86.592  1.00 61.52           C
ANISOU 5485  C   TRP D   7     8242   7927   7207   -332    224   -479       C
ATOM   5486  O   TRP D   7     -17.235  -4.678 -86.464  1.00 60.26           O
ANISOU 5486  O   TRP D   7     8007   7793   7097   -360    222   -504       O
ATOM   5487  CB  TRP D   7     -16.869  -1.693 -84.851  1.00 57.64           C
ANISOU 5487  CB  TRP D   7     7787   7378   6734   -343    246   -427       C
ATOM   5488  CG  TRP D   7     -17.395  -0.739 -83.787  1.00 68.01           C
ANISOU 5488  CG  TRP D   7     9109   8682   8051   -316    224   -406       C
ATOM   5489  CD1 TRP D   7     -17.224  -0.842 -82.431  1.00 64.71           C
ANISOU 5489  CD1 TRP D   7     8626   8264   7697   -343    225   -400       C
ATOM   5490  CD2 TRP D   7     -18.169   0.456 -83.999  1.00 78.54           C
ANISOU 5490  CD2 TRP D   7    10525  10002   9314   -252    195   -389       C
ATOM   5491  NE1 TRP D   7     -17.843   0.207 -81.792  1.00 65.53           N
ANISOU 5491  NE1 TRP D   7     8760   8358   7780   -306    202   -380       N
ATOM   5492  CE2 TRP D   7     -18.430   1.017 -82.727  1.00 71.14           C
ANISOU 5492  CE2 TRP D   7     9562   9061   8409   -247    182   -374       C
ATOM   5493  CE3 TRP D   7     -18.668   1.104 -85.139  1.00 82.64           C
ANISOU 5493  CE3 TRP D   7    11146  10512   9743   -191    177   -386       C
ATOM   5494  CZ2 TRP D   7     -19.168   2.188 -82.564  1.00 70.71           C
ANISOU 5494  CZ2 TRP D   7     9573   8993   8300   -185    150   -358       C
ATOM   5495  CZ3 TRP D   7     -19.402   2.271 -84.974  1.00 82.08           C
ANISOU 5495  CZ3 TRP D   7    11147  10425   9613   -123    143   -370       C
ATOM   5496  CH2 TRP D   7     -19.645   2.799 -83.695  1.00 78.36           C
ANISOU 5496  CH2 TRP D   7    10643   9951   9178   -121    130   -357       C
ATOM   5497  N   ASP D   8     -16.839  -2.817 -87.662  1.00 71.46           N
ANISOU 5497  N   ASP D   8     9595   9155   8402   -326    253   -467       N
ATOM   5498  CA  ASP D   8     -16.202  -3.561 -88.744  1.00 75.96           C
ANISOU 5498  CA  ASP D   8    10171   9727   8962   -355    283   -485       C
ATOM   5499  C   ASP D   8     -14.713  -3.753 -88.471  1.00 70.72           C
ANISOU 5499  C   ASP D   8     9490   9036   8345   -430    349   -485       C
ATOM   5500  O   ASP D   8     -13.901  -3.766 -89.398  1.00 79.81           O
ANISOU 5500  O   ASP D   8    10685  10170   9469   -461    394   -492       O
ATOM   5501  CB  ASP D   8     -16.428  -2.866 -90.095  1.00 81.24           C
ANISOU 5501  CB  ASP D   8    10955  10378   9533   -313    284   -478       C
ATOM   5502  CG  ASP D   8     -16.130  -1.366 -90.061  1.00 92.03           C
ANISOU 5502  CG  ASP D   8    12439  11686  10842   -304    313   -442       C
ATOM   5503  OD1 ASP D   8     -15.838  -0.817 -88.976  1.00 95.95           O
ANISOU 5503  OD1 ASP D   8    12920  12162  11375   -328    328   -423       O
ATOM   5504  OD2 ASP D   8     -16.193  -0.731 -91.137  1.00 93.88           O
ANISOU 5504  OD2 ASP D   8    12790  11892  10989   -273    323   -433       O
ATOM   5505  N   ILE D   9     -14.351  -3.905 -87.201  1.00 65.63           N
ANISOU 5505  N   ILE D   9     8778   8390   7768   -459    353   -482       N
ATOM   5506  CA  ILE D   9     -12.993  -4.266 -86.809  1.00 68.34           C
ANISOU 5506  CA  ILE D   9     9081   8723   8164   -520    403   -497       C
ATOM   5507  C   ILE D   9     -13.008  -5.627 -86.116  1.00 65.88           C
ANISOU 5507  C   ILE D   9     8669   8440   7922   -527    378   -520       C
ATOM   5508  O   ILE D   9     -14.070  -6.240 -85.945  1.00 63.05           O
ANISOU 5508  O   ILE D   9     8277   8107   7571   -496    331   -525       O
ATOM   5509  CB  ILE D   9     -12.366  -3.192 -85.901  1.00 67.72           C
ANISOU 5509  CB  ILE D   9     9022   8612   8096   -546    436   -478       C
ATOM   5510  CG1 ILE D   9     -13.233  -2.973 -84.664  1.00 70.37           C
ANISOU 5510  CG1 ILE D   9     9322   8954   8461   -513    389   -459       C
ATOM   5511  CG2 ILE D   9     -12.208  -1.891 -86.655  1.00 67.92           C
ANISOU 5511  CG2 ILE D   9     9163   8596   8045   -549    473   -458       C
ATOM   5512  CD1 ILE D   9     -12.441  -2.600 -83.439  1.00 71.29           C
ANISOU 5512  CD1 ILE D   9     9403   9055   8628   -547    413   -456       C
ATOM   5513  N   ARG D  10     -11.828  -6.114 -85.721  1.00 69.00           N
ANISOU 5513  N   ARG D  10     9020   8832   8365   -568    411   -542       N
ATOM   5514  CA  ARG D  10     -11.735  -7.392 -85.014  1.00 69.32           C
ANISOU 5514  CA  ARG D  10     8984   8890   8466   -569    388   -564       C
ATOM   5515  C   ARG D  10     -12.126  -7.242 -83.547  1.00 68.44           C
ANISOU 5515  C   ARG D  10     8839   8772   8393   -557    362   -547       C
ATOM   5516  O   ARG D  10     -13.095  -7.858 -83.086  1.00 71.75           O
ANISOU 5516  O   ARG D  10     9232   9203   8827   -538    323   -546       O
ATOM   5517  CB  ARG D  10     -10.321  -7.957 -85.134  1.00 63.14           C
ANISOU 5517  CB  ARG D  10     8169   8110   7713   -602    426   -600       C
ATOM   5518  CG  ARG D  10      -9.978  -9.004 -84.101  1.00 64.96           C
ANISOU 5518  CG  ARG D  10     8334   8345   8002   -596    405   -621       C
ATOM   5519  CD  ARG D  10      -8.487  -9.279 -84.142  1.00 65.01           C
ANISOU 5519  CD  ARG D  10     8309   8359   8032   -619    440   -664       C
ATOM   5520  NE  ARG D  10      -8.004 -10.070 -83.013  1.00 63.38           N
ANISOU 5520  NE  ARG D  10     8052   8154   7877   -602    418   -686       N
ATOM   5521  CZ  ARG D  10      -7.034 -10.972 -83.120  1.00 55.30           C
ANISOU 5521  CZ  ARG D  10     6993   7145   6875   -598    423   -733       C
ATOM   5522  NH1 ARG D  10      -6.472 -11.187 -84.303  1.00 54.19           N
ANISOU 5522  NH1 ARG D  10     6854   7021   6714   -617    453   -763       N
ATOM   5523  NH2 ARG D  10      -6.631 -11.658 -82.063  1.00 50.17           N
ANISOU 5523  NH2 ARG D  10     6309   6490   6261   -570    397   -753       N
ATOM   5524  N   GLY D  11     -11.376  -6.427 -82.805  1.00 58.79           N
ANISOU 5524  N   GLY D  11     7617   7532   7187   -575    386   -540       N
ATOM   5525  CA  GLY D  11     -11.701  -6.056 -81.439  1.00 55.06           C
ANISOU 5525  CA  GLY D  11     7123   7052   6745   -564    365   -521       C
ATOM   5526  C   GLY D  11     -12.237  -7.131 -80.513  1.00 56.07           C
ANISOU 5526  C   GLY D  11     7202   7186   6914   -549    327   -527       C
ATOM   5527  O   GLY D  11     -11.614  -8.178 -80.313  1.00 61.65           O
ANISOU 5527  O   GLY D  11     7876   7895   7652   -554    328   -553       O
ATOM   5528  N   LEU D  12     -13.408  -6.871 -79.941  1.00 58.51           N
ANISOU 5528  N   LEU D  12     7513   7498   7218   -529    295   -506       N
ATOM   5529  CA  LEU D  12     -13.954  -7.654 -78.842  1.00 54.26           C
ANISOU 5529  CA  LEU D  12     6941   6960   6717   -524    268   -509       C
ATOM   5530  C   LEU D  12     -14.942  -8.708 -79.303  1.00 58.36           C
ANISOU 5530  C   LEU D  12     7450   7498   7228   -521    247   -527       C
ATOM   5531  O   LEU D  12     -15.461  -9.465 -78.473  1.00 61.93           O
ANISOU 5531  O   LEU D  12     7882   7946   7703   -526    232   -535       O
ATOM   5532  CB  LEU D  12     -14.642  -6.725 -77.832  1.00 58.54           C
ANISOU 5532  CB  LEU D  12     7484   7497   7261   -512    251   -482       C
ATOM   5533  CG  LEU D  12     -13.839  -5.913 -76.813  1.00 55.97           C
ANISOU 5533  CG  LEU D  12     7156   7151   6960   -518    266   -467       C
ATOM   5534  CD1 LEU D  12     -14.757  -4.908 -76.142  1.00 58.58           C
ANISOU 5534  CD1 LEU D  12     7498   7481   7279   -502    247   -440       C
ATOM   5535  CD2 LEU D  12     -13.231  -6.832 -75.770  1.00 55.94           C
ANISOU 5535  CD2 LEU D  12     7119   7135   7001   -523    262   -482       C
ATOM   5536  N   ALA D  13     -15.249  -8.748 -80.594  1.00 59.42           N
ANISOU 5536  N   ALA D  13     7601   7652   7325   -515    248   -537       N
ATOM   5537  CA  ALA D  13     -16.097  -9.799 -81.130  1.00 58.21           C
ANISOU 5537  CA  ALA D  13     7433   7521   7163   -517    232   -564       C
ATOM   5538  C   ALA D  13     -15.289 -11.001 -81.597  1.00 56.39           C
ANISOU 5538  C   ALA D  13     7196   7281   6949   -533    248   -588       C
ATOM   5539  O   ALA D  13     -15.876 -12.031 -81.953  1.00 54.28           O
ANISOU 5539  O   ALA D  13     6918   7025   6679   -542    240   -614       O
ATOM   5540  CB  ALA D  13     -16.951  -9.253 -82.283  1.00 45.40           C
ANISOU 5540  CB  ALA D  13     5832   5929   5488   -492    216   -569       C
ATOM   5541  N   HIS D  14     -13.962 -10.892 -81.580  1.00 48.92           N
ANISOU 5541  N   HIS D  14     6252   6316   6018   -539    272   -587       N
ATOM   5542  CA  HIS D  14     -13.115 -11.946 -82.127  1.00 51.35           C
ANISOU 5542  CA  HIS D  14     6553   6621   6337   -547    286   -616       C
ATOM   5543  C   HIS D  14     -13.354 -13.263 -81.415  1.00 48.64           C
ANISOU 5543  C   HIS D  14     6199   6261   6020   -550    272   -633       C
ATOM   5544  O   HIS D  14     -13.625 -14.281 -82.056  1.00 50.67           O
ANISOU 5544  O   HIS D  14     6459   6523   6270   -556    271   -656       O
ATOM   5545  CB  HIS D  14     -11.647 -11.536 -82.025  1.00 53.51           C
ANISOU 5545  CB  HIS D  14     6820   6885   6625   -552    313   -623       C
ATOM   5546  CG  HIS D  14     -10.732 -12.372 -82.855  1.00 52.59           C
ANISOU 5546  CG  HIS D  14     6696   6776   6511   -557    329   -658       C
ATOM   5547  ND1 HIS D  14     -10.900 -12.528 -84.213  1.00 58.34           N
ANISOU 5547  ND1 HIS D  14     7440   7521   7207   -565    340   -668       N
ATOM   5548  CD2 HIS D  14      -9.637 -13.096 -82.522  1.00 52.74           C
ANISOU 5548  CD2 HIS D  14     6693   6790   6557   -550    334   -690       C
ATOM   5549  CE1 HIS D  14      -9.947 -13.314 -84.682  1.00 57.78           C
ANISOU 5549  CE1 HIS D  14     7354   7453   7145   -568    355   -703       C
ATOM   5550  NE2 HIS D  14      -9.166 -13.668 -83.677  1.00 55.33           N
ANISOU 5550  NE2 HIS D  14     7020   7132   6871   -556    350   -719       N
ATOM   5551  N   ALA D  15     -13.263 -13.258 -80.078  1.00 56.37           N
ANISOU 5551  N   ALA D  15     7175   7218   7027   -545    264   -622       N
ATOM   5552  CA  ALA D  15     -13.512 -14.468 -79.299  1.00 54.22           C
ANISOU 5552  CA  ALA D  15     6913   6918   6771   -547    254   -636       C
ATOM   5553  C   ALA D  15     -14.937 -14.966 -79.490  1.00 47.69           C
ANISOU 5553  C   ALA D  15     6090   6102   5927   -569    248   -644       C
ATOM   5554  O   ALA D  15     -15.159 -16.171 -79.662  1.00 58.44           O
ANISOU 5554  O   ALA D  15     7467   7449   7287   -583    252   -669       O
ATOM   5555  CB  ALA D  15     -13.229 -14.206 -77.819  1.00 61.30           C
ANISOU 5555  CB  ALA D  15     7812   7787   7692   -536    246   -620       C
ATOM   5556  N   ILE D  16     -15.915 -14.051 -79.476  1.00 42.59           N
ANISOU 5556  N   ILE D  16     5431   5483   5268   -573    239   -631       N
ATOM   5557  CA  ILE D  16     -17.312 -14.421 -79.700  1.00 48.28           C
ANISOU 5557  CA  ILE D  16     6142   6230   5972   -593    231   -653       C
ATOM   5558  C   ILE D  16     -17.472 -15.103 -81.053  1.00 52.14           C
ANISOU 5558  C   ILE D  16     6629   6742   6438   -599    235   -682       C
ATOM   5559  O   ILE D  16     -18.108 -16.162 -81.163  1.00 56.75           O
ANISOU 5559  O   ILE D  16     7214   7328   7020   -625    241   -715       O
ATOM   5560  CB  ILE D  16     -18.231 -13.187 -79.590  1.00 50.05           C
ANISOU 5560  CB  ILE D  16     6348   6490   6180   -580    214   -641       C
ATOM   5561  CG1 ILE D  16     -18.236 -12.608 -78.174  1.00 47.14           C
ANISOU 5561  CG1 ILE D  16     5979   6099   5834   -579    211   -616       C
ATOM   5562  CG2 ILE D  16     -19.634 -13.556 -79.943  1.00 45.87           C
ANISOU 5562  CG2 ILE D  16     5796   6002   5630   -596    204   -679       C
ATOM   5563  CD1 ILE D  16     -18.741 -11.179 -78.099  1.00 38.48           C
ANISOU 5563  CD1 ILE D  16     4872   5028   4721   -555    194   -595       C
ATOM   5564  N   ARG D  17     -16.910 -14.498 -82.107  1.00 49.20           N
ANISOU 5564  N   ARG D  17     6259   6388   6048   -578    236   -673       N
ATOM   5565  CA  ARG D  17     -16.999 -15.098 -83.437  1.00 47.45           C
ANISOU 5565  CA  ARG D  17     6038   6188   5802   -580    239   -700       C
ATOM   5566  C   ARG D  17     -16.371 -16.487 -83.456  1.00 46.57           C
ANISOU 5566  C   ARG D  17     5938   6047   5710   -597    254   -722       C
ATOM   5567  O   ARG D  17     -16.982 -17.447 -83.928  1.00 51.60           O
ANISOU 5567  O   ARG D  17     6575   6693   6337   -617    256   -754       O
ATOM   5568  CB  ARG D  17     -16.339 -14.197 -84.477  1.00 47.61           C
ANISOU 5568  CB  ARG D  17     6071   6221   5796   -558    244   -684       C
ATOM   5569  CG  ARG D  17     -17.061 -12.884 -84.734  1.00 46.64           C
ANISOU 5569  CG  ARG D  17     5957   6124   5639   -533    227   -667       C
ATOM   5570  CD  ARG D  17     -16.331 -12.139 -85.818  1.00 44.26           C
ANISOU 5570  CD  ARG D  17     5689   5822   5304   -518    242   -653       C
ATOM   5571  NE  ARG D  17     -16.579 -10.699 -85.866  1.00 46.93           N
ANISOU 5571  NE  ARG D  17     6060   6162   5608   -491    234   -625       N
ATOM   5572  CZ  ARG D  17     -15.640  -9.791 -85.619  1.00 59.34           C
ANISOU 5572  CZ  ARG D  17     7660   7706   7182   -496    259   -597       C
ATOM   5573  NH1 ARG D  17     -14.408 -10.187 -85.302  1.00 62.32           N
ANISOU 5573  NH1 ARG D  17     8023   8060   7594   -523    289   -600       N
ATOM   5574  NH2 ARG D  17     -15.921  -8.493 -85.697  1.00 62.26           N
ANISOU 5574  NH2 ARG D  17     8072   8071   7514   -472    255   -571       N
ATOM   5575  N   LEU D  18     -15.155 -16.620 -82.935  1.00 47.10           N
ANISOU 5575  N   LEU D  18     6016   6079   5799   -587    263   -710       N
ATOM   5576  CA  LEU D  18     -14.540 -17.940 -82.852  1.00 45.59           C
ANISOU 5576  CA  LEU D  18     5845   5856   5622   -590    271   -733       C
ATOM   5577  C   LEU D  18     -15.459 -18.933 -82.144  1.00 44.26           C
ANISOU 5577  C   LEU D  18     5698   5664   5457   -616    272   -749       C
ATOM   5578  O   LEU D  18     -15.711 -20.032 -82.650  1.00 45.19           O
ANISOU 5578  O   LEU D  18     5833   5774   5565   -634    281   -779       O
ATOM   5579  CB  LEU D  18     -13.185 -17.831 -82.147  1.00 52.22           C
ANISOU 5579  CB  LEU D  18     6689   6668   6485   -564    272   -725       C
ATOM   5580  CG  LEU D  18     -12.148 -17.002 -82.938  1.00 53.39           C
ANISOU 5580  CG  LEU D  18     6816   6841   6630   -551    283   -724       C
ATOM   5581  CD1 LEU D  18     -10.978 -16.567 -82.071  1.00 52.63           C
ANISOU 5581  CD1 LEU D  18     6709   6731   6558   -530    284   -722       C
ATOM   5582  CD2 LEU D  18     -11.658 -17.761 -84.162  1.00 50.74           C
ANISOU 5582  CD2 LEU D  18     6481   6517   6281   -551    294   -754       C
ATOM   5583  N   LEU D  19     -16.021 -18.538 -80.994  1.00 45.85           N
ANISOU 5583  N   LEU D  19     5901   5852   5667   -625    268   -733       N
ATOM   5584  CA  LEU D  19     -16.878 -19.455 -80.238  1.00 43.96           C
ANISOU 5584  CA  LEU D  19     5691   5586   5427   -661    279   -752       C
ATOM   5585  C   LEU D  19     -18.191 -19.753 -80.971  1.00 46.55           C
ANISOU 5585  C   LEU D  19     5997   5956   5735   -700    286   -788       C
ATOM   5586  O   LEU D  19     -18.632 -20.903 -81.000  1.00 46.30           O
ANISOU 5586  O   LEU D  19     5992   5903   5695   -736    305   -821       O
ATOM   5587  CB  LEU D  19     -17.145 -18.890 -78.840  1.00 46.42           C
ANISOU 5587  CB  LEU D  19     6009   5877   5753   -663    275   -728       C
ATOM   5588  CG  LEU D  19     -17.894 -19.804 -77.861  1.00 47.78           C
ANISOU 5588  CG  LEU D  19     6224   6008   5921   -704    294   -746       C
ATOM   5589  CD1 LEU D  19     -17.000 -20.942 -77.400  1.00 48.27           C
ANISOU 5589  CD1 LEU D  19     6357   6000   5983   -689    301   -748       C
ATOM   5590  CD2 LEU D  19     -18.405 -19.014 -76.677  1.00 44.04           C
ANISOU 5590  CD2 LEU D  19     5743   5533   5457   -711    290   -726       C
ATOM   5591  N   LEU D  20     -18.840 -18.739 -81.559  1.00 49.38           N
ANISOU 5591  N   LEU D  20     6309   6372   6080   -690    270   -787       N
ATOM   5592  CA  LEU D  20     -20.021 -19.006 -82.383  1.00 49.13           C
ANISOU 5592  CA  LEU D  20     6248   6393   6025   -715    270   -833       C
ATOM   5593  C   LEU D  20     -19.692 -19.979 -83.512  1.00 53.70           C
ANISOU 5593  C   LEU D  20     6839   6972   6593   -722    280   -859       C
ATOM   5594  O   LEU D  20     -20.492 -20.865 -83.844  1.00 59.45           O
ANISOU 5594  O   LEU D  20     7564   7715   7310   -762    294   -907       O
ATOM   5595  CB  LEU D  20     -20.575 -17.702 -82.965  1.00 43.66           C
ANISOU 5595  CB  LEU D  20     5515   5762   5313   -682    242   -827       C
ATOM   5596  CG  LEU D  20     -21.351 -16.722 -82.089  1.00 50.01           C
ANISOU 5596  CG  LEU D  20     6295   6589   6119   -676    227   -819       C
ATOM   5597  CD1 LEU D  20     -21.739 -15.481 -82.896  1.00 54.34           C
ANISOU 5597  CD1 LEU D  20     6821   7191   6636   -628    196   -814       C
ATOM   5598  CD2 LEU D  20     -22.582 -17.364 -81.473  1.00 46.79           C
ANISOU 5598  CD2 LEU D  20     5866   6199   5712   -727    241   -870       C
ATOM   5599  N   GLU D  21     -18.518 -19.826 -84.123  1.00 53.38           N
ANISOU 5599  N   GLU D  21     6811   6918   6555   -688    276   -835       N
ATOM   5600  CA  GLU D  21     -18.127 -20.738 -85.189  1.00 50.38           C
ANISOU 5600  CA  GLU D  21     6442   6537   6164   -691    285   -859       C
ATOM   5601  C   GLU D  21     -17.827 -22.124 -84.629  1.00 52.08           C
ANISOU 5601  C   GLU D  21     6703   6693   6390   -717    306   -876       C
ATOM   5602  O   GLU D  21     -18.301 -23.134 -85.156  1.00 53.69           O
ANISOU 5602  O   GLU D  21     6919   6899   6582   -749    320   -915       O
ATOM   5603  CB  GLU D  21     -16.925 -20.170 -85.941  1.00 44.09           C
ANISOU 5603  CB  GLU D  21     5644   5743   5364   -652    280   -834       C
ATOM   5604  CG  GLU D  21     -17.242 -18.924 -86.732  1.00 50.45           C
ANISOU 5604  CG  GLU D  21     6426   6598   6145   -629    265   -821       C
ATOM   5605  CD  GLU D  21     -18.025 -19.203 -88.013  1.00 62.03           C
ANISOU 5605  CD  GLU D  21     7879   8112   7579   -632    258   -857       C
ATOM   5606  OE1 GLU D  21     -17.922 -20.324 -88.565  1.00 64.04           O
ANISOU 5606  OE1 GLU D  21     8140   8360   7832   -651    270   -887       O
ATOM   5607  OE2 GLU D  21     -18.743 -18.286 -88.476  1.00 65.76           O
ANISOU 5607  OE2 GLU D  21     8337   8628   8022   -610    238   -857       O
ATOM   5608  N   TYR D  22     -17.056 -22.193 -83.545  1.00 49.83           N
ANISOU 5608  N   TYR D  22     6452   6356   6125   -701    307   -850       N
ATOM   5609  CA  TYR D  22     -16.720 -23.495 -82.988  1.00 50.58           C
ANISOU 5609  CA  TYR D  22     6610   6386   6221   -712    323   -865       C
ATOM   5610  C   TYR D  22     -17.965 -24.255 -82.530  1.00 54.40           C
ANISOU 5610  C   TYR D  22     7121   6856   6694   -774    348   -897       C
ATOM   5611  O   TYR D  22     -18.028 -25.483 -82.638  1.00 50.30           O
ANISOU 5611  O   TYR D  22     6654   6296   6162   -801    370   -925       O
ATOM   5612  CB  TYR D  22     -15.745 -23.329 -81.834  1.00 47.12           C
ANISOU 5612  CB  TYR D  22     6204   5898   5800   -674    313   -834       C
ATOM   5613  CG  TYR D  22     -15.475 -24.634 -81.156  1.00 50.90           C
ANISOU 5613  CG  TYR D  22     6765   6303   6270   -676    325   -849       C
ATOM   5614  CD1 TYR D  22     -16.154 -24.986 -79.996  1.00 46.73           C
ANISOU 5614  CD1 TYR D  22     6290   5729   5736   -708    341   -847       C
ATOM   5615  CD2 TYR D  22     -14.571 -25.545 -81.699  1.00 48.57           C
ANISOU 5615  CD2 TYR D  22     6505   5980   5968   -645    322   -867       C
ATOM   5616  CE1 TYR D  22     -15.919 -26.196 -79.371  1.00 53.49           C
ANISOU 5616  CE1 TYR D  22     7243   6506   6575   -709    355   -859       C
ATOM   5617  CE2 TYR D  22     -14.327 -26.761 -81.081  1.00 47.22           C
ANISOU 5617  CE2 TYR D  22     6426   5734   5781   -638    330   -880       C
ATOM   5618  CZ  TYR D  22     -15.007 -27.082 -79.921  1.00 56.70           C
ANISOU 5618  CZ  TYR D  22     7690   6882   6970   -670    348   -875       C
ATOM   5619  OH  TYR D  22     -14.774 -28.282 -79.296  1.00 69.11           O
ANISOU 5619  OH  TYR D  22     9373   8368   8517   -661    359   -886       O
ATOM   5620  N   THR D  23     -18.948 -23.552 -81.982  1.00 57.63           N
ANISOU 5620  N   THR D  23     7498   7295   7105   -800    349   -897       N
ATOM   5621  CA  THR D  23     -20.135 -24.221 -81.471  1.00 54.21           C
ANISOU 5621  CA  THR D  23     7085   6853   6661   -869    380   -937       C
ATOM   5622  C   THR D  23     -21.150 -24.516 -82.560  1.00 53.75           C
ANISOU 5622  C   THR D  23     6980   6857   6585   -909    389   -993       C
ATOM   5623  O   THR D  23     -22.188 -25.122 -82.274  1.00 52.14           O
ANISOU 5623  O   THR D  23     6784   6658   6371   -976    421  -1041       O
ATOM   5624  CB  THR D  23     -20.799 -23.376 -80.383  1.00 48.11           C
ANISOU 5624  CB  THR D  23     6290   6092   5896   -882    378   -924       C
ATOM   5625  OG1 THR D  23     -21.085 -22.073 -80.912  1.00 44.99           O
ANISOU 5625  OG1 THR D  23     5818   5772   5504   -850    346   -913       O
ATOM   5626  CG2 THR D  23     -19.882 -23.244 -79.201  1.00 42.05           C
ANISOU 5626  CG2 THR D  23     5577   5259   5143   -849    372   -877       C
ATOM   5627  N   GLY D  24     -20.887 -24.096 -83.788  1.00 53.89           N
ANISOU 5627  N   GLY D  24     6953   6927   6598   -872    365   -992       N
ATOM   5628  CA  GLY D  24     -21.821 -24.374 -84.857  1.00 60.46           C
ANISOU 5628  CA  GLY D  24     7741   7822   7410   -901    368  -1049       C
ATOM   5629  C   GLY D  24     -23.028 -23.484 -84.836  1.00 63.37           C
ANISOU 5629  C   GLY D  24     8040   8268   7770   -908    353  -1078       C
ATOM   5630  O   GLY D  24     -24.050 -23.815 -85.440  1.00 62.81           O
ANISOU 5630  O   GLY D  24     7929   8254   7681   -943    360  -1143       O
ATOM   5631  N   SER D  25     -22.930 -22.348 -84.165  1.00 68.92           N
ANISOU 5631  N   SER D  25     8726   8978   8483   -873    331  -1036       N
ATOM   5632  CA  SER D  25     -24.074 -21.474 -83.974  1.00 61.90           C
ANISOU 5632  CA  SER D  25     7776   8158   7585   -874    313  -1065       C
ATOM   5633  C   SER D  25     -24.481 -20.806 -85.281  1.00 64.38           C
ANISOU 5633  C   SER D  25     8038   8552   7872   -827    276  -1087       C
ATOM   5634  O   SER D  25     -23.633 -20.334 -86.045  1.00 56.61           O
ANISOU 5634  O   SER D  25     7068   7562   6880   -774    255  -1046       O
ATOM   5635  CB  SER D  25     -23.726 -20.427 -82.933  1.00 61.63           C
ANISOU 5635  CB  SER D  25     7748   8101   7568   -842    297  -1009       C
ATOM   5636  OG  SER D  25     -23.570 -21.020 -81.653  1.00 63.62           O
ANISOU 5636  OG  SER D  25     8047   8287   7838   -885    329   -997       O
ATOM   5637  N   ASP D  26     -25.789 -20.764 -85.533  1.00 66.91           N
ANISOU 5637  N   ASP D  26     8301   8949   8174   -847    269  -1160       N
ATOM   5638  CA  ASP D  26     -26.323 -20.141 -86.738  1.00 66.73           C
ANISOU 5638  CA  ASP D  26     8230   9008   8117   -794    227  -1192       C
ATOM   5639  C   ASP D  26     -26.569 -18.674 -86.421  1.00 65.17           C
ANISOU 5639  C   ASP D  26     8013   8843   7908   -730    185  -1163       C
ATOM   5640  O   ASP D  26     -27.427 -18.345 -85.593  1.00 63.92           O
ANISOU 5640  O   ASP D  26     7817   8716   7755   -747    183  -1195       O
ATOM   5641  CB  ASP D  26     -27.600 -20.834 -87.211  1.00 75.51           C
ANISOU 5641  CB  ASP D  26     9284  10197   9211   -838    235  -1297       C
ATOM   5642  CG  ASP D  26     -28.316 -20.055 -88.317  1.00 83.48           C
ANISOU 5642  CG  ASP D  26    10238  11301  10178   -768    181  -1340       C
ATOM   5643  OD1 ASP D  26     -29.550 -20.182 -88.416  1.00 86.23           O
ANISOU 5643  OD1 ASP D  26    10518  11733  10510   -787    173  -1433       O
ATOM   5644  OD2 ASP D  26     -27.652 -19.314 -89.081  1.00 87.39           O
ANISOU 5644  OD2 ASP D  26    10763  11790  10653   -694    147  -1287       O
ATOM   5645  N   TYR D  27     -25.815 -17.796 -87.077  1.00 58.62           N
ANISOU 5645  N   TYR D  27     7212   8002   7060   -661    156  -1107       N
ATOM   5646  CA  TYR D  27     -25.840 -16.381 -86.753  1.00 62.57           C
ANISOU 5646  CA  TYR D  27     7714   8511   7546   -600    122  -1067       C
ATOM   5647  C   TYR D  27     -25.473 -15.580 -87.984  1.00 65.43           C
ANISOU 5647  C   TYR D  27     8105   8890   7865   -526     90  -1042       C
ATOM   5648  O   TYR D  27     -24.747 -16.051 -88.865  1.00 73.13           O
ANISOU 5648  O   TYR D  27     9110   9843   8833   -526    102  -1028       O
ATOM   5649  CB  TYR D  27     -24.861 -16.025 -85.624  1.00 61.24           C
ANISOU 5649  CB  TYR D  27     7587   8266   7415   -610    143   -992       C
ATOM   5650  CG  TYR D  27     -23.421 -16.074 -86.077  1.00 53.02           C
ANISOU 5650  CG  TYR D  27     6600   7165   6381   -597    158   -932       C
ATOM   5651  CD1 TYR D  27     -22.823 -17.285 -86.382  1.00 43.05           C
ANISOU 5651  CD1 TYR D  27     5354   5868   5134   -635    187   -940       C
ATOM   5652  CD2 TYR D  27     -22.673 -14.916 -86.227  1.00 52.15           C
ANISOU 5652  CD2 TYR D  27     6524   7034   6258   -547    145   -874       C
ATOM   5653  CE1 TYR D  27     -21.524 -17.355 -86.802  1.00 41.78           C
ANISOU 5653  CE1 TYR D  27     5233   5661   4980   -622    200   -897       C
ATOM   5654  CE2 TYR D  27     -21.352 -14.968 -86.652  1.00 47.92           C
ANISOU 5654  CE2 TYR D  27     6029   6451   5729   -544    164   -832       C
ATOM   5655  CZ  TYR D  27     -20.782 -16.199 -86.941  1.00 54.39           C
ANISOU 5655  CZ  TYR D  27     6855   7245   6567   -579    190   -846       C
ATOM   5656  OH  TYR D  27     -19.470 -16.300 -87.375  1.00 56.03           O
ANISOU 5656  OH  TYR D  27     7094   7414   6781   -574    209   -816       O
ATOM   5657  N   GLU D  28     -25.989 -14.366 -88.032  1.00 68.24           N
ANISOU 5657  N   GLU D  28     8459   9282   8188   -461     49  -1039       N
ATOM   5658  CA  GLU D  28     -25.568 -13.352 -88.978  1.00 68.04           C
ANISOU 5658  CA  GLU D  28     8487   9253   8113   -386     21  -1001       C
ATOM   5659  C   GLU D  28     -24.932 -12.231 -88.180  1.00 61.77           C
ANISOU 5659  C   GLU D  28     7736   8406   7327   -365     23   -929       C
ATOM   5660  O   GLU D  28     -25.091 -12.154 -86.959  1.00 67.12           O
ANISOU 5660  O   GLU D  28     8389   9071   8042   -394     33   -921       O
ATOM   5661  CB  GLU D  28     -26.756 -12.839 -89.802  1.00 77.96           C
ANISOU 5661  CB  GLU D  28     9718  10593   9308   -315    -35  -1063       C
ATOM   5662  CG  GLU D  28     -28.002 -12.611 -88.953  1.00 94.85           C
ANISOU 5662  CG  GLU D  28    11790  12796  11454   -311    -60  -1122       C
ATOM   5663  CD  GLU D  28     -29.197 -12.115 -89.748  1.00104.83           C
ANISOU 5663  CD  GLU D  28    13021  14155  12655   -230   -122  -1198       C
ATOM   5664  OE1 GLU D  28     -30.277 -12.732 -89.622  1.00109.62           O
ANISOU 5664  OE1 GLU D  28    13543  14839  13268   -255   -131  -1291       O
ATOM   5665  OE2 GLU D  28     -29.068 -11.106 -90.479  1.00104.11           O
ANISOU 5665  OE2 GLU D  28    12992  14061  12505   -140   -162  -1169       O
ATOM   5666  N   GLU D  29     -24.205 -11.367 -88.878  1.00 55.94           N
ANISOU 5666  N   GLU D  29     7066   7637   6551   -319     18   -880       N
ATOM   5667  CA  GLU D  29     -23.517 -10.238 -88.278  1.00 52.07           C
ANISOU 5667  CA  GLU D  29     6627   7094   6061   -301     26   -814       C
ATOM   5668  C   GLU D  29     -24.174  -8.921 -88.684  1.00 58.09           C
ANISOU 5668  C   GLU D  29     7431   7882   6757   -216    -19   -813       C
ATOM   5669  O   GLU D  29     -24.615  -8.756 -89.823  1.00 59.81           O
ANISOU 5669  O   GLU D  29     7675   8135   6916   -161    -50   -840       O
ATOM   5670  CB  GLU D  29     -22.049 -10.242 -88.689  1.00 50.05           C
ANISOU 5670  CB  GLU D  29     6428   6775   5814   -325     69   -762       C
ATOM   5671  CG  GLU D  29     -21.267 -11.413 -88.139  1.00 54.72           C
ANISOU 5671  CG  GLU D  29     6988   7334   6469   -395    109   -759       C
ATOM   5672  CD  GLU D  29     -19.837 -11.057 -87.800  1.00 66.10           C
ANISOU 5672  CD  GLU D  29     8468   8714   7935   -417    147   -706       C
ATOM   5673  OE1 GLU D  29     -18.946 -11.528 -88.522  1.00 79.49           O
ANISOU 5673  OE1 GLU D  29    10183  10391   9631   -435    174   -703       O
ATOM   5674  OE2 GLU D  29     -19.591 -10.324 -86.817  1.00 76.63           O
ANISOU 5674  OE2 GLU D  29     9808  10021   9286   -418    152   -674       O
ATOM   5675  N   LYS D  30     -24.243  -7.981 -87.749  1.00 62.79           N
ANISOU 5675  N   LYS D  30     8040   8459   7359   -199    -27   -783       N
ATOM   5676  CA  LYS D  30     -24.697  -6.626 -88.043  1.00 58.74           C
ANISOU 5676  CA  LYS D  30     7586   7952   6779   -114    -67   -771       C
ATOM   5677  C   LYS D  30     -23.476  -5.716 -87.916  1.00 64.54           C
ANISOU 5677  C   LYS D  30     8409   8605   7507   -123    -30   -694       C
ATOM   5678  O   LYS D  30     -23.114  -5.302 -86.811  1.00 70.56           O
ANISOU 5678  O   LYS D  30     9166   9335   8309   -150    -12   -661       O
ATOM   5679  CB  LYS D  30     -25.833  -6.235 -87.107  1.00 62.93           C
ANISOU 5679  CB  LYS D  30     8061   8532   7317    -86   -107   -806       C
ATOM   5680  CG  LYS D  30     -26.280  -4.776 -87.182  1.00 73.74           C
ANISOU 5680  CG  LYS D  30     9495   9901   8620      7   -151   -791       C
ATOM   5681  CD  LYS D  30     -26.705  -4.374 -88.575  1.00 80.44           C
ANISOU 5681  CD  LYS D  30    10407  10777   9381     95   -194   -816       C
ATOM   5682  CE  LYS D  30     -26.896  -2.876 -88.685  1.00 82.43           C
ANISOU 5682  CE  LYS D  30    10758  11003   9559    189   -230   -787       C
ATOM   5683  NZ  LYS D  30     -26.287  -2.352 -89.942  1.00 87.73           N
ANISOU 5683  NZ  LYS D  30    11556  11625  10152    232   -222   -751       N
ATOM   5684  N   ILE D  31     -22.816  -5.438 -89.041  1.00 64.71           N
ANISOU 5684  N   ILE D  31     8512   8595   7480   -107    -13   -672       N
ATOM   5685  CA  ILE D  31     -21.573  -4.668 -89.015  1.00 69.30           C
ANISOU 5685  CA  ILE D  31     9177   9101   8054   -132     36   -610       C
ATOM   5686  C   ILE D  31     -21.898  -3.179 -88.996  1.00 77.74           C
ANISOU 5686  C   ILE D  31    10336  10145   9056    -63     13   -583       C
ATOM   5687  O   ILE D  31     -22.672  -2.685 -89.828  1.00 76.20           O
ANISOU 5687  O   ILE D  31    10196   9973   8784     18    -33   -602       O
ATOM   5688  CB  ILE D  31     -20.664  -5.023 -90.208  1.00 50.14           C
ANISOU 5688  CB  ILE D  31     6802   6647   5602   -156     75   -602       C
ATOM   5689  CG1 ILE D  31     -20.825  -6.501 -90.597  1.00 49.86           C
ANISOU 5689  CG1 ILE D  31     6686   6655   5604   -189     73   -646       C
ATOM   5690  N   TYR D  32     -21.314  -2.465 -88.034  1.00 70.82           N
ANISOU 5690  N   TYR D  32     9480   9221   8207    -92     41   -541       N
ATOM   5691  CA  TYR D  32     -21.391  -1.015 -87.942  1.00 62.98           C
ANISOU 5691  CA  TYR D  32     8588   8188   7155    -40     33   -507       C
ATOM   5692  C   TYR D  32     -20.059  -0.428 -88.381  1.00 70.75           C
ANISOU 5692  C   TYR D  32     9671   9095   8115    -86    102   -463       C
ATOM   5693  O   TYR D  32     -18.997  -0.936 -88.013  1.00 67.69           O
ANISOU 5693  O   TYR D  32     9243   8686   7789   -168    157   -452       O
ATOM   5694  CB  TYR D  32     -21.725  -0.566 -86.512  1.00 59.01           C
ANISOU 5694  CB  TYR D  32     8038   7688   6697    -43     20   -497       C
ATOM   5695  CG  TYR D  32     -23.084  -1.043 -86.059  1.00 61.08           C
ANISOU 5695  CG  TYR D  32     8205   8028   6977     -3    -43   -549       C
ATOM   5696  CD1 TYR D  32     -24.217  -0.267 -86.272  1.00 55.34           C
ANISOU 5696  CD1 TYR D  32     7508   7334   6183     95   -106   -574       C
ATOM   5697  CD2 TYR D  32     -23.240  -2.286 -85.445  1.00 56.29           C
ANISOU 5697  CD2 TYR D  32     7480   7460   6446    -62    -37   -580       C
ATOM   5698  CE1 TYR D  32     -25.456  -0.704 -85.885  1.00 53.33           C
ANISOU 5698  CE1 TYR D  32     7157   7161   5943    127   -159   -635       C
ATOM   5699  CE2 TYR D  32     -24.485  -2.732 -85.057  1.00 50.70           C
ANISOU 5699  CE2 TYR D  32     6688   6825   5752    -38    -83   -637       C
ATOM   5700  CZ  TYR D  32     -25.587  -1.938 -85.279  1.00 53.12           C
ANISOU 5700  CZ  TYR D  32     7013   7174   5996     54   -144   -668       C
ATOM   5701  OH  TYR D  32     -26.833  -2.378 -84.891  1.00 56.14           O
ANISOU 5701  OH  TYR D  32     7301   7640   6392     74   -187   -738       O
ATOM   5702  N   SER D  33     -20.115   0.626 -89.183  1.00 80.81           N
ANISOU 5702  N   SER D  33    11080  10329   9295    -32    101   -443       N
ATOM   5703  CA  SER D  33     -18.926   1.262 -89.723  1.00 84.02           C
ANISOU 5703  CA  SER D  33    11599  10661   9664    -79    173   -408       C
ATOM   5704  C   SER D  33     -18.723   2.608 -89.048  1.00 83.63           C
ANISOU 5704  C   SER D  33    11636  10552   9587    -72    193   -370       C
ATOM   5705  O   SER D  33     -19.682   3.246 -88.606  1.00 81.74           O
ANISOU 5705  O   SER D  33    11413  10325   9319      3    137   -368       O
ATOM   5706  CB  SER D  33     -19.043   1.451 -91.236  1.00 93.42           C
ANISOU 5706  CB  SER D  33    12904  11835  10756    -31    170   -412       C
ATOM   5707  OG  SER D  33     -17.788   1.781 -91.798  1.00103.24           O
ANISOU 5707  OG  SER D  33    14238  13013  11976   -101    254   -389       O
ATOM   5708  N   MET D  34     -17.469   3.040 -88.969  1.00 87.98           N
ANISOU 5708  N   MET D  34    12239  11042  10146   -153    274   -345       N
ATOM   5709  CA  MET D  34     -17.143   4.322 -88.366  1.00 91.18           C
ANISOU 5709  CA  MET D  34    12733  11386  10525   -162    306   -311       C
ATOM   5710  C   MET D  34     -16.584   5.250 -89.436  1.00108.86           C
ANISOU 5710  C   MET D  34    15154  13548  12662   -168    363   -290       C
ATOM   5711  O   MET D  34     -15.839   4.813 -90.318  1.00112.82           O
ANISOU 5711  O   MET D  34    15679  14038  13150   -220    414   -301       O
ATOM   5712  CB  MET D  34     -16.137   4.162 -87.234  1.00 76.79           C
ANISOU 5712  CB  MET D  34    10824   9557   8796   -257    360   -308       C
ATOM   5713  CG  MET D  34     -16.374   5.116 -86.084  1.00 81.96           C
ANISOU 5713  CG  MET D  34    11491  10188   9461   -243    350   -284       C
ATOM   5714  SD  MET D  34     -15.149   4.962 -84.757  1.00 93.22           S
ANISOU 5714  SD  MET D  34    12817  11609  10992   -349    411   -286       S
ATOM   5715  CE  MET D  34     -13.654   4.702 -85.720  1.00101.01           C
ANISOU 5715  CE  MET D  34    13841  12567  11970   -445    507   -305       C
ATOM   5716  N   GLY D  35     -16.915   6.542 -89.327  1.00120.96           N
ANISOU 5716  N   GLY D  35    16819  15023  14118   -119    358   -262       N
ATOM   5717  CA  GLY D  35     -16.621   7.487 -90.383  1.00131.66           C
ANISOU 5717  CA  GLY D  35    18375  16296  15355   -106    403   -241       C
ATOM   5718  C   GLY D  35     -15.203   8.033 -90.374  1.00137.26           C
ANISOU 5718  C   GLY D  35    19156  16933  16062   -227    520   -229       C
ATOM   5719  O   GLY D  35     -14.432   7.879 -89.428  1.00137.59           O
ANISOU 5719  O   GLY D  35    19099  16986  16193   -313    564   -236       O
ATOM   5720  N   ASP D  36     -14.878   8.719 -91.470  1.00138.57           N
ANISOU 5720  N   ASP D  36    19507  17025  16119   -230    572   -216       N
ATOM   5721  CA  ASP D  36     -13.539   9.238 -91.718  1.00139.56           C
ANISOU 5721  CA  ASP D  36    19722  17080  16224   -352    696   -216       C
ATOM   5722  C   ASP D  36     -13.303  10.542 -90.962  1.00140.18           C
ANISOU 5722  C   ASP D  36    19903  17085  16273   -377    739   -190       C
ATOM   5723  O   ASP D  36     -13.788  10.705 -89.837  1.00134.72           O
ANISOU 5723  O   ASP D  36    19129  16421  15637   -342    688   -181       O
ATOM   5724  CB  ASP D  36     -13.317   9.427 -93.221  1.00140.29           C
ANISOU 5724  CB  ASP D  36    19982  17117  16203   -351    740   -214       C
ATOM   5725  CG  ASP D  36     -13.949   8.322 -94.044  1.00139.98           C
ANISOU 5725  CG  ASP D  36    19873  17147  16167   -284    669   -233       C
ATOM   5726  OD1 ASP D  36     -14.850   8.621 -94.854  1.00141.42           O
ANISOU 5726  OD1 ASP D  36    20175  17311  16249   -173    610   -221       O
ATOM   5727  OD2 ASP D  36     -13.540   7.150 -93.876  1.00137.41           O
ANISOU 5727  OD2 ASP D  36    19375  16893  15942   -339    671   -264       O
ATOM   5728  N   ALA D  37     -12.520  11.450 -91.563  1.00141.64           N
ANISOU 5728  N   ALA D  37    20269  17176  16372   -445    841   -182       N
ATOM   5729  CA  ALA D  37     -12.325  12.838 -91.146  1.00136.97           C
ANISOU 5729  CA  ALA D  37    19834  16492  15718   -466    894   -156       C
ATOM   5730  C   ALA D  37     -11.484  12.941 -89.877  1.00133.80           C
ANISOU 5730  C   ALA D  37    19308  16109  15422   -573    949   -174       C
ATOM   5731  O   ALA D  37     -11.117  11.913 -89.287  1.00127.08           O
ANISOU 5731  O   ALA D  37    18249  15344  14691   -617    935   -205       O
ATOM   5732  CB  ALA D  37     -13.680  13.527 -90.948  1.00133.84           C
ANISOU 5732  CB  ALA D  37    19527  16074  15251   -313    791   -119       C
ATOM   5733  N   PRO D  38     -11.112  14.155 -89.453  1.00135.98           N
ANISOU 5733  N   PRO D  38    19712  16302  15652   -619   1015   -159       N
ATOM   5734  CA  PRO D  38     -10.576  14.314 -88.090  1.00138.22           C
ANISOU 5734  CA  PRO D  38    19870  16613  16036   -690   1041   -173       C
ATOM   5735  C   PRO D  38     -11.557  13.891 -87.012  1.00139.93           C
ANISOU 5735  C   PRO D  38    19931  16902  16332   -593    921   -158       C
ATOM   5736  O   PRO D  38     -11.134  13.625 -85.879  1.00139.67           O
ANISOU 5736  O   PRO D  38    19746  16918  16405   -645    926   -177       O
ATOM   5737  CB  PRO D  38     -10.263  15.813 -88.004  1.00137.95           C
ANISOU 5737  CB  PRO D  38    20041  16464  15910   -732   1122   -154       C
ATOM   5738  CG  PRO D  38      -9.995  16.220 -89.414  1.00137.21           C
ANISOU 5738  CG  PRO D  38    20159  16286  15688   -755   1193   -149       C
ATOM   5739  CD  PRO D  38     -10.895  15.364 -90.271  1.00137.08           C
ANISOU 5739  CD  PRO D  38    20120  16318  15648   -637   1094   -137       C
ATOM   5740  N   ASP D  39     -12.853  13.862 -87.316  1.00141.16           N
ANISOU 5740  N   ASP D  39    20128  17070  16438   -453    816   -131       N
ATOM   5741  CA  ASP D  39     -13.832  13.195 -86.475  1.00141.12           C
ANISOU 5741  CA  ASP D  39    19955  17152  16512   -366    703   -130       C
ATOM   5742  C   ASP D  39     -13.706  11.684 -86.658  1.00143.47           C
ANISOU 5742  C   ASP D  39    20071  17544  16899   -386    675   -163       C
ATOM   5743  O   ASP D  39     -12.936  11.198 -87.488  1.00152.34           O
ANISOU 5743  O   ASP D  39    21203  18664  18016   -453    735   -184       O
ATOM   5744  CB  ASP D  39     -15.241  13.655 -86.828  1.00140.05           C
ANISOU 5744  CB  ASP D  39    19920  17006  16288   -211    604   -106       C
ATOM   5745  CG  ASP D  39     -15.289  15.104 -87.232  1.00139.06           C
ANISOU 5745  CG  ASP D  39    20040  16765  16031   -181    641    -74       C
ATOM   5746  OD1 ASP D  39     -15.811  15.393 -88.332  1.00137.25           O
ANISOU 5746  OD1 ASP D  39    19966  16494  15686    -98    615    -63       O
ATOM   5747  OD2 ASP D  39     -14.812  15.946 -86.443  1.00138.42           O
ANISOU 5747  OD2 ASP D  39    20001  16634  15960   -238    695    -62       O
ATOM   5748  N   TYR D  40     -14.478  10.918 -85.875  1.00131.79           N
ANISOU 5748  N   TYR D  40    18429  16146  15500   -329    587   -170       N
ATOM   5749  CA  TYR D  40     -14.556   9.460 -86.015  1.00120.35           C
ANISOU 5749  CA  TYR D  40    16818  14783  14128   -334    550   -199       C
ATOM   5750  C   TYR D  40     -16.041   9.122 -85.904  1.00110.92           C
ANISOU 5750  C   TYR D  40    15573  13644  12927   -211    435   -198       C
ATOM   5751  O   TYR D  40     -16.505   8.587 -84.894  1.00111.80           O
ANISOU 5751  O   TYR D  40    15543  13815  13120   -197    384   -208       O
ATOM   5752  CB  TYR D  40     -13.704   8.739 -84.964  1.00123.06           C
ANISOU 5752  CB  TYR D  40    16992  15172  14594   -424    580   -223       C
ATOM   5753  CG  TYR D  40     -12.223   9.102 -85.005  1.00124.53           C
ANISOU 5753  CG  TYR D  40    17210  15316  14790   -546    692   -240       C
ATOM   5754  CD1 TYR D  40     -11.523   9.075 -86.186  1.00121.16           C
ANISOU 5754  CD1 TYR D  40    16868  14858  14309   -597    760   -254       C
ATOM   5755  CD2 TYR D  40     -11.518   9.404 -83.853  1.00126.81           C
ANISOU 5755  CD2 TYR D  40    17433  15605  15145   -611    730   -249       C
ATOM   5756  CE1 TYR D  40     -10.186   9.396 -86.259  1.00120.83           C
ANISOU 5756  CE1 TYR D  40    16851  14787  14274   -714    868   -282       C
ATOM   5757  CE2 TYR D  40     -10.163   9.713 -83.901  1.00125.59           C
ANISOU 5757  CE2 TYR D  40    17294  15424  14999   -724    833   -280       C
ATOM   5758  CZ  TYR D  40      -9.498   9.710 -85.112  1.00121.83           C
ANISOU 5758  CZ  TYR D  40    16904  14919  14466   -779    904   -299       C
ATOM   5759  OH  TYR D  40      -8.165  10.007 -85.158  1.00120.72           O
ANISOU 5759  OH  TYR D  40    16772  14760  14335   -898   1011   -341       O
ATOM   5760  N   ASP D  41     -16.782   9.465 -86.954  1.00103.67           N
ANISOU 5760  N   ASP D  41    14778  12706  11906   -122    397   -192       N
ATOM   5761  CA  ASP D  41     -18.238   9.508 -86.885  1.00104.42           C
ANISOU 5761  CA  ASP D  41    14860  12845  11969      8    289   -198       C
ATOM   5762  C   ASP D  41     -18.845   8.134 -86.632  1.00105.17           C
ANISOU 5762  C   ASP D  41    14767  13045  12150     22    227   -235       C
ATOM   5763  O   ASP D  41     -18.655   7.205 -87.423  1.00103.92           O
ANISOU 5763  O   ASP D  41    14568  12917  12001      1    234   -256       O
ATOM   5764  CB  ASP D  41     -18.806  10.088 -88.176  1.00107.93           C
ANISOU 5764  CB  ASP D  41    15479  13250  12279    104    261   -192       C
ATOM   5765  CG  ASP D  41     -20.257   9.726 -88.365  1.00109.83           C
ANISOU 5765  CG  ASP D  41    15667  13566  12496    235    146   -222       C
ATOM   5766  OD1 ASP D  41     -21.115  10.433 -87.800  1.00112.45           O
ANISOU 5766  OD1 ASP D  41    16023  13904  12800    322     85   -221       O
ATOM   5767  OD2 ASP D  41     -20.543   8.730 -89.057  1.00109.40           O
ANISOU 5767  OD2 ASP D  41    15542  13572  12454    250    116   -254       O
ATOM   5768  N   ARG D  42     -19.619   8.027 -85.548  1.00103.50           N
ANISOU 5768  N   ARG D  42    14448  12884  11994     58    169   -245       N
ATOM   5769  CA  ARG D  42     -20.277   6.787 -85.154  1.00 97.06           C
ANISOU 5769  CA  ARG D  42    13461  12162  11257     65    115   -284       C
ATOM   5770  C   ARG D  42     -21.783   6.824 -85.396  1.00 98.79           C
ANISOU 5770  C   ARG D  42    13668  12440  11426    187     17   -316       C
ATOM   5771  O   ARG D  42     -22.522   6.059 -84.765  1.00 99.21           O
ANISOU 5771  O   ARG D  42    13581  12570  11542    197    -30   -352       O
ATOM   5772  CB  ARG D  42     -20.004   6.487 -83.677  1.00 90.35           C
ANISOU 5772  CB  ARG D  42    12483  11333  10513      1    127   -281       C
ATOM   5773  CG  ARG D  42     -18.544   6.360 -83.289  1.00 80.74           C
ANISOU 5773  CG  ARG D  42    11249  10074   9353   -113    214   -263       C
ATOM   5774  CD  ARG D  42     -18.399   6.089 -81.791  1.00 76.35           C
ANISOU 5774  CD  ARG D  42    10573   9542   8894   -157    214   -263       C
ATOM   5775  NE  ARG D  42     -16.993   6.052 -81.390  1.00 76.86           N
ANISOU 5775  NE  ARG D  42    10622   9573   9009   -256    291   -255       N
ATOM   5776  CZ  ARG D  42     -16.463   5.156 -80.560  1.00 76.75           C
ANISOU 5776  CZ  ARG D  42    10485   9590   9086   -313    304   -270       C
ATOM   5777  NH1 ARG D  42     -17.226   4.210 -80.021  1.00 79.44           N
ANISOU 5777  NH1 ARG D  42    10718   9988   9478   -290    251   -288       N
ATOM   5778  NH2 ARG D  42     -15.167   5.213 -80.263  1.00 68.22           N
ANISOU 5778  NH2 ARG D  42     9394   8483   8042   -392    370   -272       N
ATOM   5779  N   SER D  43     -22.259   7.690 -86.300  1.00 98.68           N
ANISOU 5779  N   SER D  43    13802  12393  11297    282    -13   -311       N
ATOM   5780  CA  SER D  43     -23.690   7.983 -86.350  1.00 94.59           C
ANISOU 5780  CA  SER D  43    13280  11931  10727    413   -112   -348       C
ATOM   5781  C   SER D  43     -24.535   6.795 -86.801  1.00 90.39           C
ANISOU 5781  C   SER D  43    12623  11502  10219    446   -170   -411       C
ATOM   5782  O   SER D  43     -25.722   6.743 -86.465  1.00 87.54           O
ANISOU 5782  O   SER D  43    12191  11216   9856    525   -247   -459       O
ATOM   5783  CB  SER D  43     -23.959   9.181 -87.255  1.00 95.54           C
ANISOU 5783  CB  SER D  43    13604  11988  10708    518   -134   -331       C
ATOM   5784  OG  SER D  43     -23.183   9.099 -88.430  1.00103.36           O
ANISOU 5784  OG  SER D  43    14705  12923  11644    486    -81   -311       O
ATOM   5785  N   GLN D  44     -23.964   5.840 -87.542  1.00 85.58           N
ANISOU 5785  N   GLN D  44    11984  10901   9633    385   -133   -417       N
ATOM   5786  CA  GLN D  44     -24.747   4.681 -87.960  1.00 77.40           C
ANISOU 5786  CA  GLN D  44    10828   9959   8620    407   -183   -479       C
ATOM   5787  C   GLN D  44     -25.111   3.803 -86.768  1.00 76.72           C
ANISOU 5787  C   GLN D  44    10563   9941   8645    350   -191   -510       C
ATOM   5788  O   GLN D  44     -26.197   3.214 -86.731  1.00 73.53           O
ANISOU 5788  O   GLN D  44    10059   9627   8253    394   -251   -574       O
ATOM   5789  CB  GLN D  44     -23.979   3.878 -89.005  1.00 79.38           C
ANISOU 5789  CB  GLN D  44    11094  10195   8871    350   -136   -475       C
ATOM   5790  CG  GLN D  44     -24.245   2.385 -88.959  1.00 85.00           C
ANISOU 5790  CG  GLN D  44    11645  10987   9662    301   -145   -524       C
ATOM   5791  CD  GLN D  44     -23.356   1.605 -89.903  1.00 99.33           C
ANISOU 5791  CD  GLN D  44    13476  12782  11483    238    -93   -516       C
ATOM   5792  OE1 GLN D  44     -22.360   2.128 -90.406  1.00104.85           O
ANISOU 5792  OE1 GLN D  44    14288  13405  12146    205    -35   -472       O
ATOM   5793  NE2 GLN D  44     -23.703   0.340 -90.140  1.00104.03           N
ANISOU 5793  NE2 GLN D  44    13957  13445  12125    214   -109   -564       N
ATOM   5794  N   TRP D  45     -24.215   3.705 -85.785  1.00 78.53           N
ANISOU 5794  N   TRP D  45    10752  10131   8954    251   -131   -471       N
ATOM   5795  CA  TRP D  45     -24.503   2.939 -84.578  1.00 70.31           C
ANISOU 5795  CA  TRP D  45     9562   9140   8011    197   -134   -494       C
ATOM   5796  C   TRP D  45     -25.431   3.712 -83.652  1.00 69.34           C
ANISOU 5796  C   TRP D  45     9421   9045   7882    258   -185   -508       C
ATOM   5797  O   TRP D  45     -26.425   3.166 -83.162  1.00 69.83           O
ANISOU 5797  O   TRP D  45     9371   9185   7975    274   -228   -564       O
ATOM   5798  CB  TRP D  45     -23.200   2.574 -83.861  1.00 69.25           C
ANISOU 5798  CB  TRP D  45     9399   8955   7957     83    -58   -452       C
ATOM   5799  CG  TRP D  45     -23.357   2.244 -82.389  1.00 73.56           C
ANISOU 5799  CG  TRP D  45     9838   9524   8588     37    -57   -457       C
ATOM   5800  CD1 TRP D  45     -22.649   2.777 -81.356  1.00 70.48           C
ANISOU 5800  CD1 TRP D  45     9455   9086   8239     -9    -20   -416       C
ATOM   5801  CD2 TRP D  45     -24.267   1.294 -81.803  1.00 65.96           C
ANISOU 5801  CD2 TRP D  45     8749   8635   7676     29    -90   -508       C
ATOM   5802  NE1 TRP D  45     -23.062   2.229 -80.173  1.00 69.54           N
ANISOU 5802  NE1 TRP D  45     9229   9005   8190    -38    -32   -435       N
ATOM   5803  CE2 TRP D  45     -24.053   1.316 -80.420  1.00 64.28           C
ANISOU 5803  CE2 TRP D  45     8483   8410   7529    -20    -71   -491       C
ATOM   5804  CE3 TRP D  45     -25.242   0.437 -82.319  1.00 67.20           C
ANISOU 5804  CE3 TRP D  45     8838   8868   7826     54   -130   -571       C
ATOM   5805  CZ2 TRP D  45     -24.777   0.517 -79.541  1.00 63.53           C
ANISOU 5805  CZ2 TRP D  45     8279   8369   7490    -47    -87   -531       C
ATOM   5806  CZ3 TRP D  45     -25.956  -0.348 -81.452  1.00 71.05           C
ANISOU 5806  CZ3 TRP D  45     9213   9413   8371     21   -143   -616       C
ATOM   5807  CH2 TRP D  45     -25.719  -0.309 -80.074  1.00 68.20           C
ANISOU 5807  CH2 TRP D  45     8810   9031   8073    -30   -119   -594       C
ATOM   5808  N   LEU D  46     -25.142   4.995 -83.427  1.00 74.17           N
ANISOU 5808  N   LEU D  46    10143   9591   8447    291   -177   -463       N
ATOM   5809  CA  LEU D  46     -25.967   5.803 -82.536  1.00 63.81           C
ANISOU 5809  CA  LEU D  46     8821   8299   7125    353   -224   -474       C
ATOM   5810  C   LEU D  46     -27.404   5.938 -83.016  1.00 62.01           C
ANISOU 5810  C   LEU D  46     8577   8150   6834    474   -314   -541       C
ATOM   5811  O   LEU D  46     -28.254   6.381 -82.238  1.00 70.35           O
ANISOU 5811  O   LEU D  46     9590   9248   7892    525   -360   -570       O
ATOM   5812  CB  LEU D  46     -25.334   7.181 -82.355  1.00 61.00           C
ANISOU 5812  CB  LEU D  46     8607   7849   6721    368   -195   -413       C
ATOM   5813  CG  LEU D  46     -24.047   7.157 -81.516  1.00 68.50           C
ANISOU 5813  CG  LEU D  46     9543   8738   7746    249   -112   -361       C
ATOM   5814  CD1 LEU D  46     -22.957   8.001 -82.144  1.00 78.99           C
ANISOU 5814  CD1 LEU D  46    11027   9969   9019    224    -50   -309       C
ATOM   5815  CD2 LEU D  46     -24.309   7.624 -80.099  1.00 69.35           C
ANISOU 5815  CD2 LEU D  46     9597   8851   7901    242   -122   -354       C
ATOM   5816  N   SER D  47     -27.700   5.538 -84.255  1.00 70.15           N
ANISOU 5816  N   SER D  47     9634   9210   7809    522   -340   -574       N
ATOM   5817  CA  SER D  47     -29.059   5.628 -84.783  1.00 77.86           C
ANISOU 5817  CA  SER D  47    10589  10273   8721    645   -431   -651       C
ATOM   5818  C   SER D  47     -29.950   4.539 -84.203  1.00 76.01           C
ANISOU 5818  C   SER D  47    10170  10149   8560    613   -457   -731       C
ATOM   5819  O   SER D  47     -31.135   4.774 -83.944  1.00 69.47           O
ANISOU 5819  O   SER D  47     9284   9403   7709    694   -526   -801       O
ATOM   5820  CB  SER D  47     -29.031   5.509 -86.303  1.00 84.53           C
ANISOU 5820  CB  SER D  47    11523  11112   9482    703   -448   -662       C
ATOM   5821  OG  SER D  47     -27.893   6.157 -86.827  1.00 90.59           O
ANISOU 5821  OG  SER D  47    12448  11766  10205    678   -389   -583       O
ATOM   5822  N   GLU D  48     -29.403   3.330 -84.027  1.00 76.57           N
ANISOU 5822  N   GLU D  48    10151  10227   8715    496   -402   -728       N
ATOM   5823  CA  GLU D  48     -30.146   2.192 -83.501  1.00 69.94           C
ANISOU 5823  CA  GLU D  48     9151   9480   7944    446   -410   -801       C
ATOM   5824  C   GLU D  48     -29.878   1.920 -82.031  1.00 68.83           C
ANISOU 5824  C   GLU D  48     8932   9325   7896    350   -367   -780       C
ATOM   5825  O   GLU D  48     -30.637   1.156 -81.425  1.00 69.87           O
ANISOU 5825  O   GLU D  48     8941   9530   8076    314   -375   -844       O
ATOM   5826  CB  GLU D  48     -29.794   0.913 -84.258  1.00 71.69           C
ANISOU 5826  CB  GLU D  48     9328   9716   8193    379   -378   -819       C
ATOM   5827  CG  GLU D  48     -30.332   0.794 -85.639  1.00 76.22           C
ANISOU 5827  CG  GLU D  48     9932  10337   8690    462   -426   -869       C
ATOM   5828  CD  GLU D  48     -29.486  -0.146 -86.458  1.00 81.83           C
ANISOU 5828  CD  GLU D  48    10654  11016   9420    392   -377   -846       C
ATOM   5829  OE1 GLU D  48     -28.541  -0.729 -85.883  1.00 79.22           O
ANISOU 5829  OE1 GLU D  48    10301  10635   9165    283   -309   -799       O
ATOM   5830  OE2 GLU D  48     -29.747  -0.288 -87.671  1.00 90.39           O
ANISOU 5830  OE2 GLU D  48    11776  12128  10442    451   -407   -878       O
ATOM   5831  N   LYS D  49     -28.804   2.495 -81.471  1.00 62.99           N
ANISOU 5831  N   LYS D  49     8262   8492   7178    306   -318   -695       N
ATOM   5832  CA  LYS D  49     -28.346   2.195 -80.119  1.00 61.23           C
ANISOU 5832  CA  LYS D  49     7977   8245   7042    213   -272   -666       C
ATOM   5833  C   LYS D  49     -29.504   2.010 -79.146  1.00 62.94           C
ANISOU 5833  C   LYS D  49     8084   8540   7290    219   -306   -731       C
ATOM   5834  O   LYS D  49     -29.645   0.954 -78.516  1.00 58.62           O
ANISOU 5834  O   LYS D  49     7439   8024   6809    137   -279   -761       O
ATOM   5835  CB  LYS D  49     -27.413   3.308 -79.633  1.00 61.79           C
ANISOU 5835  CB  LYS D  49     8146   8225   7108    209   -241   -586       C
ATOM   5836  CG  LYS D  49     -26.797   3.061 -78.272  1.00 58.57           C
ANISOU 5836  CG  LYS D  49     7684   7786   6784    119   -194   -552       C
ATOM   5837  CD  LYS D  49     -25.915   4.217 -77.845  1.00 61.61           C
ANISOU 5837  CD  LYS D  49     8163   8088   7158    117   -165   -483       C
ATOM   5838  CE  LYS D  49     -24.895   3.794 -76.791  1.00 57.91           C
ANISOU 5838  CE  LYS D  49     7653   7577   6772     18   -106   -445       C
ATOM   5839  NZ  LYS D  49     -23.699   4.696 -76.756  1.00 54.86           N
ANISOU 5839  NZ  LYS D  49     7362   7107   6374     -5    -59   -383       N
ATOM   5840  N   PHE D  50     -30.377   3.007 -79.053  1.00 58.27           N
ANISOU 5840  N   PHE D  50     7511   7983   6645    316   -365   -760       N
ATOM   5841  CA  PHE D  50     -31.459   2.948 -78.087  1.00 59.02           C
ANISOU 5841  CA  PHE D  50     7503   8156   6768    322   -395   -827       C
ATOM   5842  C   PHE D  50     -32.746   2.385 -78.666  1.00 63.49           C
ANISOU 5842  C   PHE D  50     7979   8838   7306    369   -447   -939       C
ATOM   5843  O   PHE D  50     -33.750   2.315 -77.947  1.00 58.99           O
ANISOU 5843  O   PHE D  50     7314   8347   6753    374   -473  -1013       O
ATOM   5844  CB  PHE D  50     -31.687   4.337 -77.488  1.00 57.93           C
ANISOU 5844  CB  PHE D  50     7422   7996   6594    398   -428   -803       C
ATOM   5845  CG  PHE D  50     -30.515   4.830 -76.681  1.00 59.28           C
ANISOU 5845  CG  PHE D  50     7655   8064   6804    336   -372   -707       C
ATOM   5846  CD1 PHE D  50     -30.325   4.398 -75.383  1.00 56.59           C
ANISOU 5846  CD1 PHE D  50     7239   7718   6544    247   -333   -696       C
ATOM   5847  CD2 PHE D  50     -29.577   5.684 -77.240  1.00 58.52           C
ANISOU 5847  CD2 PHE D  50     7694   7877   6662    362   -353   -632       C
ATOM   5848  CE1 PHE D  50     -29.257   4.842 -74.648  1.00 61.04           C
ANISOU 5848  CE1 PHE D  50     7854   8197   7142    196   -285   -616       C
ATOM   5849  CE2 PHE D  50     -28.497   6.125 -76.510  1.00 62.01           C
ANISOU 5849  CE2 PHE D  50     8185   8235   7142    300   -299   -556       C
ATOM   5850  CZ  PHE D  50     -28.336   5.708 -75.217  1.00 64.23           C
ANISOU 5850  CZ  PHE D  50     8381   8518   7503    221   -268   -549       C
ATOM   5851  N   LYS D  51     -32.732   1.959 -79.932  1.00 68.47           N
ANISOU 5851  N   LYS D  51     8634   9485   7895    399   -461   -961       N
ATOM   5852  CA  LYS D  51     -33.896   1.371 -80.581  1.00 67.10           C
ANISOU 5852  CA  LYS D  51     8374   9427   7694    442   -510  -1074       C
ATOM   5853  C   LYS D  51     -33.785  -0.144 -80.717  1.00 68.25           C
ANISOU 5853  C   LYS D  51     8434   9599   7899    330   -460  -1108       C
ATOM   5854  O   LYS D  51     -34.494  -0.736 -81.537  1.00 71.66           O
ANISOU 5854  O   LYS D  51     8812  10112   8305    356   -490  -1192       O
ATOM   5855  CB  LYS D  51     -34.106   2.012 -81.949  1.00 67.78           C
ANISOU 5855  CB  LYS D  51     8551   9522   7679    571   -572  -1087       C
ATOM   5856  CG  LYS D  51     -33.957   3.529 -81.938  1.00 76.68           C
ANISOU 5856  CG  LYS D  51     9806  10590   8737    678   -609  -1032       C
ATOM   5857  CD  LYS D  51     -34.473   4.189 -83.221  1.00 74.71           C
ANISOU 5857  CD  LYS D  51     9646  10366   8374    829   -686  -1067       C
ATOM   5858  CE  LYS D  51     -34.963   5.592 -82.913  1.00 79.63           C
ANISOU 5858  CE  LYS D  51    10346  10980   8928    954   -747  -1066       C
ATOM   5859  NZ  LYS D  51     -35.423   6.357 -84.097  1.00 87.70           N
ANISOU 5859  NZ  LYS D  51    11482  12012   9826   1116   -826  -1093       N
ATOM   5860  N   LEU D  52     -32.925  -0.784 -79.920  1.00 62.85           N
ANISOU 5860  N   LEU D  52     7740   8849   7292    211   -387  -1048       N
ATOM   5861  CA  LEU D  52     -32.610  -2.200 -80.081  1.00 58.75           C
ANISOU 5861  CA  LEU D  52     7170   8330   6823    107   -335  -1063       C
ATOM   5862  C   LEU D  52     -32.988  -3.038 -78.866  1.00 60.65           C
ANISOU 5862  C   LEU D  52     7315   8595   7134      3   -293  -1102       C
ATOM   5863  O   LEU D  52     -32.624  -4.220 -78.809  1.00 64.01           O
ANISOU 5863  O   LEU D  52     7715   9002   7603    -91   -240  -1104       O
ATOM   5864  CB  LEU D  52     -31.118  -2.388 -80.387  1.00 55.84           C
ANISOU 5864  CB  LEU D  52     6889   7853   6474     59   -283   -961       C
ATOM   5865  CG  LEU D  52     -30.706  -2.211 -81.858  1.00 58.11           C
ANISOU 5865  CG  LEU D  52     7256   8123   6701    119   -301   -941       C
ATOM   5866  CD1 LEU D  52     -29.220  -1.964 -81.979  1.00 61.17           C
ANISOU 5866  CD1 LEU D  52     7741   8402   7100     84   -252   -838       C
ATOM   5867  CD2 LEU D  52     -31.133  -3.413 -82.711  1.00 43.78           C
ANISOU 5867  CD2 LEU D  52     5380   6369   4886     92   -300  -1012       C
ATOM   5868  N   GLY D  53     -33.677  -2.461 -77.885  1.00 56.95           N
ANISOU 5868  N   GLY D  53     6804   8162   6672     18   -311  -1132       N
ATOM   5869  CA  GLY D  53     -34.153  -3.241 -76.761  1.00 58.25           C
ANISOU 5869  CA  GLY D  53     6883   8355   6895    -81   -269  -1180       C
ATOM   5870  C   GLY D  53     -33.102  -3.714 -75.782  1.00 64.41           C
ANISOU 5870  C   GLY D  53     7697   9037   7738   -179   -200  -1095       C
ATOM   5871  O   GLY D  53     -33.387  -4.608 -74.978  1.00 63.47           O
ANISOU 5871  O   GLY D  53     7525   8927   7662   -273   -155  -1132       O
ATOM   5872  N   LEU D  54     -31.899  -3.137 -75.810  1.00 58.97           N
ANISOU 5872  N   LEU D  54     7100   8255   7052   -161   -190   -990       N
ATOM   5873  CA  LEU D  54     -30.816  -3.576 -74.935  1.00 60.32           C
ANISOU 5873  CA  LEU D  54     7303   8336   7279   -242   -132   -915       C
ATOM   5874  C   LEU D  54     -30.857  -2.845 -73.598  1.00 64.01           C
ANISOU 5874  C   LEU D  54     7769   8782   7771   -247   -129   -887       C
ATOM   5875  O   LEU D  54     -31.118  -1.640 -73.545  1.00 63.07           O
ANISOU 5875  O   LEU D  54     7671   8674   7620   -170   -170   -876       O
ATOM   5876  CB  LEU D  54     -29.460  -3.347 -75.602  1.00 54.54           C
ANISOU 5876  CB  LEU D  54     6660   7522   6540   -227   -118   -827       C
ATOM   5877  CG  LEU D  54     -29.366  -3.916 -77.008  1.00 52.02           C
ANISOU 5877  CG  LEU D  54     6353   7221   6191   -212   -124   -849       C
ATOM   5878  CD1 LEU D  54     -28.069  -3.463 -77.651  1.00 51.19           C
ANISOU 5878  CD1 LEU D  54     6339   7039   6072   -192   -110   -767       C
ATOM   5879  CD2 LEU D  54     -29.476  -5.436 -76.957  1.00 53.89           C
ANISOU 5879  CD2 LEU D  54     6539   7470   6465   -300    -84   -892       C
ATOM   5880  N   ASP D  55     -30.575  -3.585 -72.515  1.00 61.73           N
ANISOU 5880  N   ASP D  55     7463   8457   7534   -335    -79   -874       N
ATOM   5881  CA  ASP D  55     -30.621  -2.990 -71.180  1.00 53.88           C
ANISOU 5881  CA  ASP D  55     6466   7443   6565   -346    -73   -850       C
ATOM   5882  C   ASP D  55     -29.555  -1.921 -71.022  1.00 53.25           C
ANISOU 5882  C   ASP D  55     6460   7290   6483   -302    -80   -758       C
ATOM   5883  O   ASP D  55     -29.816  -0.854 -70.454  1.00 54.45           O
ANISOU 5883  O   ASP D  55     6617   7447   6624   -258   -105   -745       O
ATOM   5884  CB  ASP D  55     -30.454  -4.061 -70.097  1.00 48.17           C
ANISOU 5884  CB  ASP D  55     5727   6685   5890   -448    -16   -852       C
ATOM   5885  CG  ASP D  55     -31.656  -4.989 -70.001  1.00 57.22           C
ANISOU 5885  CG  ASP D  55     6800   7904   7036   -506      1   -954       C
ATOM   5886  OD1 ASP D  55     -32.738  -4.509 -69.624  1.00 61.36           O
ANISOU 5886  OD1 ASP D  55     7265   8501   7548   -489    -21  -1018       O
ATOM   5887  OD2 ASP D  55     -31.524  -6.198 -70.310  1.00 68.84           O
ANISOU 5887  OD2 ASP D  55     8274   9364   8519   -570     39   -975       O
ATOM   5888  N   PHE D  56     -28.350  -2.186 -71.518  1.00 49.09           N
ANISOU 5888  N   PHE D  56     5989   6698   5964   -316    -56   -698       N
ATOM   5889  CA  PHE D  56     -27.223  -1.264 -71.406  1.00 49.81           C
ANISOU 5889  CA  PHE D  56     6149   6720   6056   -290    -51   -618       C
ATOM   5890  C   PHE D  56     -26.571  -1.188 -72.776  1.00 54.27           C
ANISOU 5890  C   PHE D  56     6767   7267   6588   -259    -54   -596       C
ATOM   5891  O   PHE D  56     -25.520  -1.807 -73.008  1.00 49.00           O
ANISOU 5891  O   PHE D  56     6124   6551   5943   -300    -19   -564       O
ATOM   5892  CB  PHE D  56     -26.225  -1.718 -70.342  1.00 50.00           C
ANISOU 5892  CB  PHE D  56     6185   6680   6134   -353     -8   -572       C
ATOM   5893  CG  PHE D  56     -26.802  -1.800 -68.970  1.00 48.67           C
ANISOU 5893  CG  PHE D  56     5977   6520   5993   -385     -1   -589       C
ATOM   5894  CD1 PHE D  56     -27.235  -3.015 -68.460  1.00 49.15           C
ANISOU 5894  CD1 PHE D  56     6002   6594   6080   -451     27   -630       C
ATOM   5895  CD2 PHE D  56     -26.908  -0.663 -68.174  1.00 50.24           C
ANISOU 5895  CD2 PHE D  56     6184   6713   6192   -354    -17   -565       C
ATOM   5896  CE1 PHE D  56     -27.780  -3.097 -67.169  1.00 46.39           C
ANISOU 5896  CE1 PHE D  56     5624   6249   5751   -488     40   -647       C
ATOM   5897  CE2 PHE D  56     -27.454  -0.740 -66.890  1.00 47.09           C
ANISOU 5897  CE2 PHE D  56     5750   6324   5819   -386     -9   -582       C
ATOM   5898  CZ  PHE D  56     -27.882  -1.963 -66.391  1.00 34.68           C
ANISOU 5898  CZ  PHE D  56     4142   4764   4269   -454     21   -623       C
ATOM   5899  N   PRO D  57     -27.170  -0.406 -73.712  1.00 55.25           N
ANISOU 5899  N   PRO D  57     6914   7426   6652   -182    -96   -616       N
ATOM   5900  CA  PRO D  57     -26.789  -0.479 -75.134  1.00 51.63           C
ANISOU 5900  CA  PRO D  57     6504   6960   6153   -153   -101   -610       C
ATOM   5901  C   PRO D  57     -25.306  -0.309 -75.372  1.00 54.97           C
ANISOU 5901  C   PRO D  57     6996   7305   6587   -179    -60   -541       C
ATOM   5902  O   PRO D  57     -24.695   0.688 -74.973  1.00 58.10           O
ANISOU 5902  O   PRO D  57     7445   7653   6978   -167    -50   -493       O
ATOM   5903  CB  PRO D  57     -27.595   0.664 -75.763  1.00 58.07           C
ANISOU 5903  CB  PRO D  57     7356   7810   6897    -52   -156   -630       C
ATOM   5904  CG  PRO D  57     -28.833   0.739 -74.899  1.00 56.94           C
ANISOU 5904  CG  PRO D  57     7136   7735   6764    -38   -188   -689       C
ATOM   5905  CD  PRO D  57     -28.321   0.491 -73.496  1.00 50.76           C
ANISOU 5905  CD  PRO D  57     6326   6911   6048   -114   -146   -655       C
ATOM   5906  N   ASN D  58     -24.722  -1.304 -76.029  1.00 61.17           N
ANISOU 5906  N   ASN D  58     7777   8079   7385   -220    -33   -544       N
ATOM   5907  CA  ASN D  58     -23.283  -1.369 -76.221  1.00 54.59           C
ANISOU 5907  CA  ASN D  58     6990   7181   6570   -256     11   -495       C
ATOM   5908  C   ASN D  58     -23.010  -2.268 -77.423  1.00 52.44           C
ANISOU 5908  C   ASN D  58     6721   6918   6285   -268     21   -513       C
ATOM   5909  O   ASN D  58     -23.905  -2.949 -77.922  1.00 54.56           O
ANISOU 5909  O   ASN D  58     6951   7240   6541   -259     -1   -563       O
ATOM   5910  CB  ASN D  58     -22.612  -1.885 -74.949  1.00 57.00           C
ANISOU 5910  CB  ASN D  58     7262   7454   6941   -316     43   -475       C
ATOM   5911  CG  ASN D  58     -21.267  -1.250 -74.695  1.00 56.87           C
ANISOU 5911  CG  ASN D  58     7292   7378   6937   -332     76   -425       C
ATOM   5912  OD1 ASN D  58     -20.603  -0.787 -75.613  1.00 66.82           O
ANISOU 5912  OD1 ASN D  58     8607   8615   8166   -321     91   -407       O
ATOM   5913  ND2 ASN D  58     -20.844  -1.259 -73.443  1.00 50.96           N
ANISOU 5913  ND2 ASN D  58     6523   6606   6235   -361     90   -408       N
ATOM   5914  N   LEU D  59     -21.766  -2.245 -77.899  1.00 54.22           N
ANISOU 5914  N   LEU D  59     6993   7096   6513   -291     57   -479       N
ATOM   5915  CA  LEU D  59     -21.289  -3.200 -78.889  1.00 48.58           C
ANISOU 5915  CA  LEU D  59     6278   6383   5797   -314     76   -494       C
ATOM   5916  C   LEU D  59     -20.042  -3.884 -78.352  1.00 54.51           C
ANISOU 5916  C   LEU D  59     7015   7094   6603   -372    118   -476       C
ATOM   5917  O   LEU D  59     -19.142  -3.197 -77.853  1.00 54.26           O
ANISOU 5917  O   LEU D  59     7009   7022   6584   -384    142   -443       O
ATOM   5918  CB  LEU D  59     -20.957  -2.521 -80.239  1.00 51.57           C
ANISOU 5918  CB  LEU D  59     6733   6748   6113   -278     79   -480       C
ATOM   5919  CG  LEU D  59     -21.988  -1.620 -80.931  1.00 61.40           C
ANISOU 5919  CG  LEU D  59     8024   8021   7286   -200     33   -492       C
ATOM   5920  CD1 LEU D  59     -21.306  -0.634 -81.850  1.00 65.13           C
ANISOU 5920  CD1 LEU D  59     8603   8446   7697   -175     53   -458       C
ATOM   5921  CD2 LEU D  59     -23.019  -2.439 -81.707  1.00 57.26           C
ANISOU 5921  CD2 LEU D  59     7456   7561   6740   -174     -3   -549       C
ATOM   5922  N   PRO D  60     -19.923  -5.218 -78.459  1.00 53.04           N
ANISOU 5922  N   PRO D  60     6790   6916   6445   -406    129   -501       N
ATOM   5923  CA  PRO D  60     -20.827  -6.157 -79.138  1.00 53.93           C
ANISOU 5923  CA  PRO D  60     6873   7073   6545   -406    111   -546       C
ATOM   5924  C   PRO D  60     -22.140  -6.425 -78.409  1.00 58.65           C
ANISOU 5924  C   PRO D  60     7421   7713   7152   -407     86   -582       C
ATOM   5925  O   PRO D  60     -22.157  -6.484 -77.174  1.00 50.93           O
ANISOU 5925  O   PRO D  60     6422   6719   6210   -431     93   -573       O
ATOM   5926  CB  PRO D  60     -20.010  -7.442 -79.180  1.00 50.76           C
ANISOU 5926  CB  PRO D  60     6458   6650   6180   -451    140   -554       C
ATOM   5927  CG  PRO D  60     -19.161  -7.352 -77.962  1.00 47.10           C
ANISOU 5927  CG  PRO D  60     5992   6144   5759   -473    159   -526       C
ATOM   5928  CD  PRO D  60     -18.778  -5.917 -77.846  1.00 45.30           C
ANISOU 5928  CD  PRO D  60     5799   5900   5514   -449    160   -491       C
ATOM   5929  N   TYR D  61     -23.223  -6.600 -79.164  1.00 57.81           N
ANISOU 5929  N   TYR D  61     7291   7662   7011   -382     58   -629       N
ATOM   5930  CA  TYR D  61     -24.461  -7.129 -78.615  1.00 53.33           C
ANISOU 5930  CA  TYR D  61     6665   7146   6454   -399     43   -684       C
ATOM   5931  C   TYR D  61     -24.788  -8.447 -79.297  1.00 52.70           C
ANISOU 5931  C   TYR D  61     6554   7092   6375   -434     54   -734       C
ATOM   5932  O   TYR D  61     -24.191  -8.810 -80.311  1.00 59.65           O
ANISOU 5932  O   TYR D  61     7460   7961   7242   -430     62   -727       O
ATOM   5933  CB  TYR D  61     -25.620  -6.131 -78.751  1.00 53.25           C
ANISOU 5933  CB  TYR D  61     6639   7193   6402   -337     -4   -713       C
ATOM   5934  CG  TYR D  61     -26.041  -5.738 -80.151  1.00 48.38           C
ANISOU 5934  CG  TYR D  61     6044   6616   5722   -271    -39   -738       C
ATOM   5935  CD1 TYR D  61     -26.808  -6.588 -80.934  1.00 55.77           C
ANISOU 5935  CD1 TYR D  61     6936   7612   6642   -274    -52   -805       C
ATOM   5936  CD2 TYR D  61     -25.728  -4.485 -80.665  1.00 45.48           C
ANISOU 5936  CD2 TYR D  61     5747   6226   5307   -205    -59   -698       C
ATOM   5937  CE1 TYR D  61     -27.224  -6.213 -82.218  1.00 54.41           C
ANISOU 5937  CE1 TYR D  61     6786   7479   6408   -205    -90   -831       C
ATOM   5938  CE2 TYR D  61     -26.143  -4.105 -81.939  1.00 54.36           C
ANISOU 5938  CE2 TYR D  61     6907   7382   6365   -137    -94   -720       C
ATOM   5939  CZ  TYR D  61     -26.891  -4.976 -82.708  1.00 52.10           C
ANISOU 5939  CZ  TYR D  61     6572   7159   6065   -134   -113   -787       C
ATOM   5940  OH  TYR D  61     -27.296  -4.620 -83.967  1.00 59.49           O
ANISOU 5940  OH  TYR D  61     7544   8128   6931    -60   -151   -812       O
ATOM   5941  N   LEU D  62     -25.733  -9.178 -78.716  1.00 48.45           N
ANISOU 5941  N   LEU D  62     5964   6590   5854   -475     59   -789       N
ATOM   5942  CA  LEU D  62     -26.178 -10.444 -79.286  1.00 51.84           C
ANISOU 5942  CA  LEU D  62     6364   7048   6283   -517     74   -846       C
ATOM   5943  C   LEU D  62     -27.675 -10.602 -79.077  1.00 65.74           C
ANISOU 5943  C   LEU D  62     8058   8888   8033   -529     59   -930       C
ATOM   5944  O   LEU D  62     -28.156 -10.454 -77.946  1.00 71.30           O
ANISOU 5944  O   LEU D  62     8739   9596   8757   -556     67   -941       O
ATOM   5945  CB  LEU D  62     -25.438 -11.627 -78.662  1.00 44.04           C
ANISOU 5945  CB  LEU D  62     5398   5998   5337   -586    121   -830       C
ATOM   5946  CG  LEU D  62     -25.819 -12.984 -79.246  1.00 45.48           C
ANISOU 5946  CG  LEU D  62     5564   6197   5517   -636    143   -887       C
ATOM   5947  CD1 LEU D  62     -24.958 -13.255 -80.448  1.00 45.25           C
ANISOU 5947  CD1 LEU D  62     5566   6151   5476   -613    142   -865       C
ATOM   5948  CD2 LEU D  62     -25.662 -14.083 -78.202  1.00 49.29           C
ANISOU 5948  CD2 LEU D  62     6066   6628   6033   -709    188   -892       C
ATOM   5949  N   ILE D  63     -28.412 -10.910 -80.152  1.00 55.00           N
ANISOU 5949  N   ILE D  63     6664   7594   6639   -511     39   -994       N
ATOM   5950  CA  ILE D  63     -29.842 -11.202 -80.056  1.00 50.54           C
ANISOU 5950  CA  ILE D  63     6022   7118   6063   -530     28  -1094       C
ATOM   5951  C   ILE D  63     -30.073 -12.685 -80.296  1.00 50.72           C
ANISOU 5951  C   ILE D  63     6023   7147   6100   -612     71  -1151       C
ATOM   5952  O   ILE D  63     -29.545 -13.261 -81.251  1.00 62.54           O
ANISOU 5952  O   ILE D  63     7546   8628   7590   -612     77  -1142       O
ATOM   5953  CB  ILE D  63     -30.676 -10.356 -81.029  1.00 54.97           C
ANISOU 5953  CB  ILE D  63     6552   7764   6569   -439    -35  -1144       C
ATOM   5954  CG1 ILE D  63     -30.579  -8.895 -80.641  1.00 60.08           C
ANISOU 5954  CG1 ILE D  63     7230   8401   7198   -361    -74  -1094       C
ATOM   5955  CG2 ILE D  63     -32.135 -10.767 -80.974  1.00 53.19           C
ANISOU 5955  CG2 ILE D  63     6234   7643   6334   -461    -44  -1265       C
ATOM   5956  CD1 ILE D  63     -29.697  -8.149 -81.513  1.00 64.97           C
ANISOU 5956  CD1 ILE D  63     7927   8975   7784   -293    -95  -1024       C
ATOM   5957  N   ASP D  64     -30.867 -13.300 -79.437  1.00 54.62           N
ANISOU 5957  N   ASP D  64     6475   7665   6614   -687    104  -1213       N
ATOM   5958  CA  ASP D  64     -31.115 -14.725 -79.558  1.00 55.54           C
ANISOU 5958  CA  ASP D  64     6582   7779   6741   -777    155  -1270       C
ATOM   5959  C   ASP D  64     -32.490 -15.016 -78.956  1.00 57.12           C
ANISOU 5959  C   ASP D  64     6707   8055   6940   -838    175  -1377       C
ATOM   5960  O   ASP D  64     -32.617 -15.518 -77.840  1.00 67.94           O
ANISOU 5960  O   ASP D  64     8091   9387   8334   -919    226  -1384       O
ATOM   5961  CB  ASP D  64     -30.032 -15.553 -78.874  1.00 58.32           C
ANISOU 5961  CB  ASP D  64     7013   8020   7127   -836    207  -1201       C
ATOM   5962  CG  ASP D  64     -30.137 -17.014 -79.217  1.00 64.01           C
ANISOU 5962  CG  ASP D  64     7747   8725   7850   -916    256  -1250       C
ATOM   5963  OD1 ASP D  64     -30.599 -17.325 -80.329  1.00 70.27           O
ANISOU 5963  OD1 ASP D  64     8501   9579   8620   -908    242  -1309       O
ATOM   5964  OD2 ASP D  64     -29.768 -17.852 -78.377  1.00 67.75           O
ANISOU 5964  OD2 ASP D  64     8276   9124   8343   -985    307  -1232       O
ATOM   5965  N   GLY D  65     -33.531 -14.712 -79.723  1.00 53.69           N
ANISOU 5965  N   GLY D  65     6193   7731   6474   -800    136  -1469       N
ATOM   5966  CA  GLY D  65     -34.876 -14.940 -79.244  1.00 56.32           C
ANISOU 5966  CA  GLY D  65     6440   8155   6804   -856    153  -1589       C
ATOM   5967  C   GLY D  65     -35.262 -13.888 -78.233  1.00 66.50           C
ANISOU 5967  C   GLY D  65     7705   9465   8099   -825    130  -1581       C
ATOM   5968  O   GLY D  65     -35.176 -12.687 -78.509  1.00 76.85           O
ANISOU 5968  O   GLY D  65     9014  10797   9388   -716     65  -1544       O
ATOM   5969  N   ALA D  66     -35.680 -14.323 -77.049  1.00 68.47           N
ANISOU 5969  N   ALA D  66     7943   9701   8372   -919    187  -1614       N
ATOM   5970  CA  ALA D  66     -35.984 -13.367 -75.995  1.00 71.70           C
ANISOU 5970  CA  ALA D  66     8333  10121   8789   -896    170  -1602       C
ATOM   5971  C   ALA D  66     -34.733 -12.717 -75.422  1.00 73.53           C
ANISOU 5971  C   ALA D  66     8655  10242   9040   -851    160  -1459       C
ATOM   5972  O   ALA D  66     -34.844 -11.721 -74.702  1.00 75.87           O
ANISOU 5972  O   ALA D  66     8943  10544   9340   -808    133  -1433       O
ATOM   5973  CB  ALA D  66     -36.770 -14.056 -74.882  1.00 71.68           C
ANISOU 5973  CB  ALA D  66     8298  10132   8803  -1019    241  -1680       C
ATOM   5974  N   HIS D  67     -33.556 -13.240 -75.742  1.00 70.13           N
ANISOU 5974  N   HIS D  67     8307   9718   8623   -857    178  -1373       N
ATOM   5975  CA  HIS D  67     -32.318 -12.864 -75.081  1.00 63.58           C
ANISOU 5975  CA  HIS D  67     7560   8781   7816   -836    182  -1253       C
ATOM   5976  C   HIS D  67     -31.598 -11.808 -75.906  1.00 60.61           C
ANISOU 5976  C   HIS D  67     7208   8397   7422   -726    123  -1182       C
ATOM   5977  O   HIS D  67     -31.214 -12.061 -77.053  1.00 64.17           O
ANISOU 5977  O   HIS D  67     7675   8850   7857   -697    108  -1175       O
ATOM   5978  CB  HIS D  67     -31.443 -14.096 -74.864  1.00 67.23           C
ANISOU 5978  CB  HIS D  67     8097   9147   8299   -908    240  -1212       C
ATOM   5979  CG  HIS D  67     -32.093 -15.134 -74.004  1.00 68.40           C
ANISOU 5979  CG  HIS D  67     8248   9286   8457  -1021    307  -1275       C
ATOM   5980  ND1 HIS D  67     -32.079 -16.478 -74.314  1.00 68.31           N
ANISOU 5980  ND1 HIS D  67     8268   9244   8442  -1099    359  -1311       N
ATOM   5981  CD2 HIS D  67     -32.795 -15.019 -72.851  1.00 63.04           C
ANISOU 5981  CD2 HIS D  67     7549   8618   7784  -1074    336  -1311       C
ATOM   5982  CE1 HIS D  67     -32.733 -17.148 -73.381  1.00 66.17           C
ANISOU 5982  CE1 HIS D  67     8006   8963   8173  -1198    420  -1366       C
ATOM   5983  NE2 HIS D  67     -33.178 -16.285 -72.483  1.00 65.20           N
ANISOU 5983  NE2 HIS D  67     7850   8867   8057  -1186    408  -1368       N
ATOM   5984  N   ARG D  68     -31.436 -10.627 -75.318  1.00 49.82           N
ANISOU 5984  N   ARG D  68     5851   7022   6058   -670     92  -1133       N
ATOM   5985  CA  ARG D  68     -30.737  -9.501 -75.917  1.00 48.84           C
ANISOU 5985  CA  ARG D  68     5765   6877   5913   -573     44  -1063       C
ATOM   5986  C   ARG D  68     -29.645  -9.094 -74.942  1.00 51.90           C
ANISOU 5986  C   ARG D  68     6214   7173   6332   -579     62   -967       C
ATOM   5987  O   ARG D  68     -29.940  -8.532 -73.888  1.00 58.41           O
ANISOU 5987  O   ARG D  68     7026   7998   7169   -582     61   -961       O
ATOM   5988  CB  ARG D  68     -31.691  -8.339 -76.200  1.00 53.97           C
ANISOU 5988  CB  ARG D  68     6370   7611   6525   -489    -16  -1107       C
ATOM   5989  CG  ARG D  68     -32.994  -8.761 -76.871  1.00 62.61           C
ANISOU 5989  CG  ARG D  68     7382   8816   7591   -489    -35  -1228       C
ATOM   5990  CD  ARG D  68     -33.665  -7.610 -77.621  1.00 71.06           C
ANISOU 5990  CD  ARG D  68     8430   9962   8607   -371   -111  -1263       C
ATOM   5991  NE  ARG D  68     -34.370  -8.124 -78.795  1.00 76.61           N
ANISOU 5991  NE  ARG D  68     9085  10748   9276   -350   -135  -1352       N
ATOM   5992  CZ  ARG D  68     -34.255  -7.663 -80.046  1.00 70.80           C
ANISOU 5992  CZ  ARG D  68     8380  10031   8490   -258   -185  -1346       C
ATOM   5993  NH1 ARG D  68     -33.481  -6.617 -80.345  1.00 52.02           N
ANISOU 5993  NH1 ARG D  68     6088   7592   6086   -177   -215  -1255       N
ATOM   5994  NH2 ARG D  68     -34.950  -8.253 -81.012  1.00 73.93           N
ANISOU 5994  NH2 ARG D  68     8724  10507   8859   -248   -203  -1437       N
ATOM   5995  N   LEU D  69     -28.392  -9.343 -75.317  1.00 51.91           N
ANISOU 5995  N   LEU D  69     6275   7103   6343   -576     77   -899       N
ATOM   5996  CA  LEU D  69     -27.240  -9.256 -74.433  1.00 44.98           C
ANISOU 5996  CA  LEU D  69     5452   6141   5499   -592    101   -821       C
ATOM   5997  C   LEU D  69     -26.269  -8.163 -74.874  1.00 47.76           C
ANISOU 5997  C   LEU D  69     5846   6459   5839   -526     77   -752       C
ATOM   5998  O   LEU D  69     -26.135  -7.878 -76.063  1.00 57.25           O
ANISOU 5998  O   LEU D  69     7062   7680   7010   -482     57   -751       O
ATOM   5999  CB  LEU D  69     -26.495 -10.604 -74.400  1.00 40.18           C
ANISOU 5999  CB  LEU D  69     4878   5474   4914   -651    144   -811       C
ATOM   6000  CG  LEU D  69     -27.058 -11.633 -73.420  1.00 53.43           C
ANISOU 6000  CG  LEU D  69     6552   7140   6610   -731    185   -852       C
ATOM   6001  CD1 LEU D  69     -28.347 -12.207 -73.963  1.00 56.99           C
ANISOU 6001  CD1 LEU D  69     6947   7667   7041   -767    191   -945       C
ATOM   6002  CD2 LEU D  69     -26.034 -12.736 -73.144  1.00 53.02           C
ANISOU 6002  CD2 LEU D  69     6563   7005   6577   -769    222   -819       C
ATOM   6003  N   THR D  70     -25.583  -7.553 -73.908  1.00 51.28           N
ANISOU 6003  N   THR D  70     6320   6856   6308   -522     84   -696       N
ATOM   6004  CA  THR D  70     -24.351  -6.806 -74.165  1.00 55.16           C
ANISOU 6004  CA  THR D  70     6861   7299   6799   -487     83   -630       C
ATOM   6005  C   THR D  70     -23.271  -7.309 -73.214  1.00 50.14           C
ANISOU 6005  C   THR D  70     6251   6597   6205   -524    114   -591       C
ATOM   6006  O   THR D  70     -23.500  -8.225 -72.415  1.00 56.04           O
ANISOU 6006  O   THR D  70     6989   7329   6974   -571    135   -610       O
ATOM   6007  CB  THR D  70     -24.513  -5.293 -73.983  1.00 56.62           C
ANISOU 6007  CB  THR D  70     7058   7491   6963   -431     54   -604       C
ATOM   6008  OG1 THR D  70     -25.130  -5.034 -72.716  1.00 61.22           O
ANISOU 6008  OG1 THR D  70     7613   8083   7565   -445     51   -612       O
ATOM   6009  CG2 THR D  70     -25.333  -4.686 -75.112  1.00 50.41           C
ANISOU 6009  CG2 THR D  70     6270   6761   6124   -372     16   -635       C
ATOM   6010  N   GLN D  71     -22.098  -6.669 -73.292  1.00 44.69           N
ANISOU 6010  N   GLN D  71     5594   5866   5520   -502    119   -542       N
ATOM   6011  CA  GLN D  71     -20.908  -7.041 -72.531  1.00 47.45           C
ANISOU 6011  CA  GLN D  71     5965   6160   5904   -523    142   -511       C
ATOM   6012  C   GLN D  71     -20.334  -8.346 -73.067  1.00 47.15           C
ANISOU 6012  C   GLN D  71     5938   6103   5874   -547    161   -527       C
ATOM   6013  O   GLN D  71     -20.967  -9.406 -72.965  1.00 47.89           O
ANISOU 6013  O   GLN D  71     6023   6203   5970   -579    170   -561       O
ATOM   6014  CB  GLN D  71     -21.206  -7.141 -71.023  1.00 47.04           C
ANISOU 6014  CB  GLN D  71     5906   6090   5879   -544    147   -508       C
ATOM   6015  CG  GLN D  71     -21.688  -5.835 -70.415  1.00 47.39           C
ANISOU 6015  CG  GLN D  71     5939   6150   5917   -519    128   -491       C
ATOM   6016  CD  GLN D  71     -20.571  -4.810 -70.276  1.00 55.23           C
ANISOU 6016  CD  GLN D  71     6957   7111   6916   -493    130   -446       C
ATOM   6017  OE1 GLN D  71     -19.388  -5.129 -70.451  1.00 51.15           O
ANISOU 6017  OE1 GLN D  71     6458   6562   6413   -499    148   -432       O
ATOM   6018  NE2 GLN D  71     -20.942  -3.569 -69.962  1.00 55.64           N
ANISOU 6018  NE2 GLN D  71     7010   7173   6955   -466    115   -429       N
ATOM   6019  N   SER D  72     -19.124  -8.267 -73.635  1.00 46.26           N
ANISOU 6019  N   SER D  72     5845   5967   5763   -534    171   -508       N
ATOM   6020  CA  SER D  72     -18.587  -9.381 -74.411  1.00 37.23           C
ANISOU 6020  CA  SER D  72     4710   4815   4621   -547    185   -526       C
ATOM   6021  C   SER D  72     -18.401 -10.624 -73.556  1.00 47.28           C
ANISOU 6021  C   SER D  72     5995   6051   5916   -573    197   -539       C
ATOM   6022  O   SER D  72     -18.587 -11.748 -74.040  1.00 57.18           O
ANISOU 6022  O   SER D  72     7258   7304   7166   -593    206   -566       O
ATOM   6023  CB  SER D  72     -17.270  -8.978 -75.060  1.00 37.71           C
ANISOU 6023  CB  SER D  72     4786   4861   4681   -531    196   -509       C
ATOM   6024  OG  SER D  72     -16.318  -8.616 -74.092  1.00 43.33           O
ANISOU 6024  OG  SER D  72     5501   5543   5419   -527    203   -490       O
ATOM   6025  N   ASN D  73     -18.037 -10.448 -72.278  1.00 43.04           N
ANISOU 6025  N   ASN D  73     5468   5483   5401   -571    197   -520       N
ATOM   6026  CA  ASN D  73     -17.915 -11.599 -71.392  1.00 36.29           C
ANISOU 6026  CA  ASN D  73     4643   4586   4559   -589    208   -530       C
ATOM   6027  C   ASN D  73     -19.275 -12.221 -71.107  1.00 40.02           C
ANISOU 6027  C   ASN D  73     5118   5068   5020   -631    217   -558       C
ATOM   6028  O   ASN D  73     -19.422 -13.444 -71.138  1.00 48.27           O
ANISOU 6028  O   ASN D  73     6193   6088   6058   -658    235   -582       O
ATOM   6029  CB  ASN D  73     -17.223 -11.187 -70.103  1.00 49.50           C
ANISOU 6029  CB  ASN D  73     6330   6226   6252   -570    203   -505       C
ATOM   6030  CG  ASN D  73     -15.765 -10.886 -70.311  1.00 56.11           C
ANISOU 6030  CG  ASN D  73     7165   7054   7102   -537    199   -496       C
ATOM   6031  OD1 ASN D  73     -15.166 -11.317 -71.292  1.00 57.12           O
ANISOU 6031  OD1 ASN D  73     7291   7188   7224   -530    204   -511       O
ATOM   6032  ND2 ASN D  73     -15.189 -10.119 -69.406  1.00 59.47           N
ANISOU 6032  ND2 ASN D  73     7585   7469   7544   -518    192   -477       N
ATOM   6033  N   ALA D  74     -20.288 -11.401 -70.841  1.00 42.94           N
ANISOU 6033  N   ALA D  74     5456   5475   5385   -638    209   -561       N
ATOM   6034  CA  ALA D  74     -21.620 -11.958 -70.627  1.00 51.69           C
ANISOU 6034  CA  ALA D  74     6553   6605   6481   -683    222   -603       C
ATOM   6035  C   ALA D  74     -22.131 -12.651 -71.878  1.00 58.56           C
ANISOU 6035  C   ALA D  74     7407   7510   7332   -701    228   -644       C
ATOM   6036  O   ALA D  74     -22.822 -13.675 -71.785  1.00 57.61           O
ANISOU 6036  O   ALA D  74     7297   7387   7204   -752    253   -686       O
ATOM   6037  CB  ALA D  74     -22.592 -10.864 -70.196  1.00 50.30           C
ANISOU 6037  CB  ALA D  74     6335   6475   6302   -678    207   -608       C
ATOM   6038  N   ILE D  75     -21.785 -12.119 -73.054  1.00 61.23           N
ANISOU 6038  N   ILE D  75     7727   7878   7660   -664    209   -636       N
ATOM   6039  CA  ILE D  75     -22.156 -12.758 -74.318  1.00 55.60           C
ANISOU 6039  CA  ILE D  75     7001   7198   6927   -674    211   -673       C
ATOM   6040  C   ILE D  75     -21.463 -14.112 -74.458  1.00 56.61           C
ANISOU 6040  C   ILE D  75     7170   7277   7061   -699    235   -680       C
ATOM   6041  O   ILE D  75     -22.093 -15.108 -74.828  1.00 51.38           O
ANISOU 6041  O   ILE D  75     6510   6623   6388   -739    254   -724       O
ATOM   6042  CB  ILE D  75     -21.842 -11.819 -75.497  1.00 47.70           C
ANISOU 6042  CB  ILE D  75     5986   6231   5908   -625    187   -657       C
ATOM   6043  CG1 ILE D  75     -22.843 -10.656 -75.514  1.00 48.74           C
ANISOU 6043  CG1 ILE D  75     6083   6416   6019   -597    159   -667       C
ATOM   6044  CG2 ILE D  75     -21.892 -12.541 -76.802  1.00 42.55           C
ANISOU 6044  CG2 ILE D  75     5330   5599   5236   -629    189   -687       C
ATOM   6045  CD1 ILE D  75     -22.472  -9.522 -76.462  1.00 34.49           C
ANISOU 6045  CD1 ILE D  75     4289   4628   4188   -541    136   -640       C
ATOM   6046  N   LEU D  76     -20.161 -14.182 -74.125  1.00 57.31           N
ANISOU 6046  N   LEU D  76     7294   7315   7166   -674    236   -643       N
ATOM   6047  CA  LEU D  76     -19.441 -15.455 -74.210  1.00 38.21           C
ANISOU 6047  CA  LEU D  76     4921   4848   4749   -684    253   -651       C
ATOM   6048  C   LEU D  76     -20.021 -16.487 -73.248  1.00 40.48           C
ANISOU 6048  C   LEU D  76     5253   5093   5034   -730    278   -673       C
ATOM   6049  O   LEU D  76     -20.162 -17.666 -73.595  1.00 47.66           O
ANISOU 6049  O   LEU D  76     6197   5981   5931   -760    299   -702       O
ATOM   6050  CB  LEU D  76     -17.950 -15.248 -73.934  1.00 37.71           C
ANISOU 6050  CB  LEU D  76     4878   4748   4703   -640    243   -618       C
ATOM   6051  CG  LEU D  76     -17.112 -14.505 -74.985  1.00 46.29           C
ANISOU 6051  CG  LEU D  76     5936   5864   5789   -605    232   -606       C
ATOM   6052  CD1 LEU D  76     -15.873 -13.904 -74.370  1.00 42.52           C
ANISOU 6052  CD1 LEU D  76     5461   5365   5331   -571    226   -580       C
ATOM   6053  CD2 LEU D  76     -16.726 -15.399 -76.185  1.00 47.35           C
ANISOU 6053  CD2 LEU D  76     6077   6000   5911   -607    240   -630       C
ATOM   6054  N   ARG D  77     -20.365 -16.070 -72.034  1.00 52.13           N
ANISOU 6054  N   ARG D  77     6736   6554   6517   -740    281   -659       N
ATOM   6055  CA  ARG D  77     -20.848 -17.037 -71.053  1.00 56.60           C
ANISOU 6055  CA  ARG D  77     7361   7069   7073   -788    312   -678       C
ATOM   6056  C   ARG D  77     -22.166 -17.642 -71.495  1.00 58.51           C
ANISOU 6056  C   ARG D  77     7587   7346   7298   -855    341   -735       C
ATOM   6057  O   ARG D  77     -22.401 -18.843 -71.307  1.00 60.41           O
ANISOU 6057  O   ARG D  77     7888   7543   7523   -903    377   -763       O
ATOM   6058  CB  ARG D  77     -20.992 -16.385 -69.684  1.00 44.42           C
ANISOU 6058  CB  ARG D  77     5828   5509   5541   -786    310   -654       C
ATOM   6059  CG  ARG D  77     -19.684 -15.993 -69.085  1.00 53.98           C
ANISOU 6059  CG  ARG D  77     7063   6680   6767   -726    286   -609       C
ATOM   6060  CD  ARG D  77     -19.868 -15.262 -67.786  1.00 62.05           C
ANISOU 6060  CD  ARG D  77     8088   7691   7799   -723    282   -586       C
ATOM   6061  NE  ARG D  77     -18.914 -15.779 -66.819  1.00 79.57           N
ANISOU 6061  NE  ARG D  77    10379   9838  10015   -692    279   -566       N
ATOM   6062  CZ  ARG D  77     -19.201 -16.727 -65.937  1.00 88.25           C
ANISOU 6062  CZ  ARG D  77    11562  10875  11093   -721    304   -576       C
ATOM   6063  NH1 ARG D  77     -20.425 -17.240 -65.895  1.00 95.57           N
ANISOU 6063  NH1 ARG D  77    12503  11806  12004   -795    342   -609       N
ATOM   6064  NH2 ARG D  77     -18.265 -17.166 -65.107  1.00 89.49           N
ANISOU 6064  NH2 ARG D  77    11792  10967  11242   -677    293   -559       N
ATOM   6065  N   TYR D  78     -23.025 -16.831 -72.110  1.00 48.08           N
ANISOU 6065  N   TYR D  78     6187   6104   5976   -857    326   -758       N
ATOM   6066  CA  TYR D  78     -24.334 -17.313 -72.528  1.00 41.80           C
ANISOU 6066  CA  TYR D  78     5359   5359   5164   -918    350   -826       C
ATOM   6067  C   TYR D  78     -24.201 -18.402 -73.587  1.00 49.58           C
ANISOU 6067  C   TYR D  78     6364   6338   6136   -938    366   -856       C
ATOM   6068  O   TYR D  78     -24.849 -19.454 -73.497  1.00 60.05           O
ANISOU 6068  O   TYR D  78     7719   7650   7448  -1007    408   -906       O
ATOM   6069  CB  TYR D  78     -25.148 -16.130 -73.031  1.00 40.00           C
ANISOU 6069  CB  TYR D  78     5043   5222   4933   -892    317   -845       C
ATOM   6070  CG  TYR D  78     -26.353 -16.474 -73.849  1.00 47.95           C
ANISOU 6070  CG  TYR D  78     5995   6304   5922   -930    325   -924       C
ATOM   6071  CD1 TYR D  78     -27.553 -16.711 -73.231  1.00 55.04           C
ANISOU 6071  CD1 TYR D  78     6865   7234   6813   -995    354   -988       C
ATOM   6072  CD2 TYR D  78     -26.304 -16.526 -75.239  1.00 49.28           C
ANISOU 6072  CD2 TYR D  78     6134   6515   6076   -901    304   -941       C
ATOM   6073  CE1 TYR D  78     -28.671 -17.014 -73.941  1.00 59.14           C
ANISOU 6073  CE1 TYR D  78     7323   7833   7315  -1031    362  -1073       C
ATOM   6074  CE2 TYR D  78     -27.439 -16.832 -75.974  1.00 54.43           C
ANISOU 6074  CE2 TYR D  78     6730   7243   6710   -931    308  -1022       C
ATOM   6075  CZ  TYR D  78     -28.629 -17.072 -75.298  1.00 61.54           C
ANISOU 6075  CZ  TYR D  78     7596   8180   7605   -997    337  -1091       C
ATOM   6076  OH  TYR D  78     -29.811 -17.379 -75.932  1.00 65.42           O
ANISOU 6076  OH  TYR D  78     8020   8758   8078  -1033    343  -1187       O
ATOM   6077  N   ILE D  79     -23.350 -18.172 -74.596  1.00 46.93           N
ANISOU 6077  N   ILE D  79     6016   6011   5803   -882    337   -829       N
ATOM   6078  CA  ILE D  79     -23.045 -19.208 -75.585  1.00 42.19           C
ANISOU 6078  CA  ILE D  79     5439   5398   5191   -894    349   -851       C
ATOM   6079  C   ILE D  79     -22.392 -20.421 -74.925  1.00 41.33           C
ANISOU 6079  C   ILE D  79     5426   5198   5080   -916    380   -842       C
ATOM   6080  O   ILE D  79     -22.721 -21.567 -75.253  1.00 50.21           O
ANISOU 6080  O   ILE D  79     6588   6301   6187   -964    413   -882       O
ATOM   6081  CB  ILE D  79     -22.157 -18.635 -76.707  1.00 44.54           C
ANISOU 6081  CB  ILE D  79     5712   5720   5492   -829    315   -821       C
ATOM   6082  CG1 ILE D  79     -22.848 -17.466 -77.408  1.00 44.13           C
ANISOU 6082  CG1 ILE D  79     5586   5750   5430   -801    284   -831       C
ATOM   6083  CG2 ILE D  79     -21.774 -19.731 -77.723  1.00 41.91           C
ANISOU 6083  CG2 ILE D  79     5403   5372   5147   -838    328   -843       C
ATOM   6084  CD1 ILE D  79     -21.875 -16.468 -77.989  1.00 46.85           C
ANISOU 6084  CD1 ILE D  79     5923   6100   5777   -735    254   -782       C
ATOM   6085  N   ALA D  80     -21.453 -20.195 -73.994  1.00 38.76           N
ANISOU 6085  N   ALA D  80     5146   4815   4766   -876    369   -792       N
ATOM   6086  CA  ALA D  80     -20.789 -21.318 -73.322  1.00 42.99           C
ANISOU 6086  CA  ALA D  80     5784   5260   5291   -879    389   -784       C
ATOM   6087  C   ALA D  80     -21.785 -22.174 -72.554  1.00 49.20           C
ANISOU 6087  C   ALA D  80     6630   6008   6056   -960    439   -822       C
ATOM   6088  O   ALA D  80     -21.652 -23.402 -72.508  1.00 50.98           O
ANISOU 6088  O   ALA D  80     6944   6168   6258   -988    470   -840       O
ATOM   6089  CB  ALA D  80     -19.698 -20.824 -72.366  1.00 37.60           C
ANISOU 6089  CB  ALA D  80     5132   4532   4622   -817    363   -733       C
ATOM   6090  N   ARG D  81     -22.773 -21.534 -71.918  1.00 49.61           N
ANISOU 6090  N   ARG D  81     6642   6096   6111  -1001    451   -836       N
ATOM   6091  CA  ARG D  81     -23.817 -22.268 -71.214  1.00 53.06           C
ANISOU 6091  CA  ARG D  81     7127   6508   6527  -1092    508   -883       C
ATOM   6092  C   ARG D  81     -24.663 -23.086 -72.177  1.00 60.07           C
ANISOU 6092  C   ARG D  81     7996   7430   7398  -1160    543   -952       C
ATOM   6093  O   ARG D  81     -25.180 -24.148 -71.804  1.00 60.33           O
ANISOU 6093  O   ARG D  81     8105   7414   7405  -1239    601   -993       O
ATOM   6094  CB  ARG D  81     -24.703 -21.300 -70.424  1.00 52.57           C
ANISOU 6094  CB  ARG D  81     7006   6492   6474  -1117    510   -892       C
ATOM   6095  CG  ARG D  81     -24.666 -21.512 -68.921  1.00 55.09           C
ANISOU 6095  CG  ARG D  81     7414   6736   6784  -1141    538   -873       C
ATOM   6096  CD  ARG D  81     -24.771 -20.210 -68.162  1.00 52.68           C
ANISOU 6096  CD  ARG D  81     7051   6467   6500  -1108    508   -842       C
ATOM   6097  NE  ARG D  81     -25.716 -19.286 -68.781  1.00 56.15           N
ANISOU 6097  NE  ARG D  81     7366   7014   6952  -1116    490   -878       N
ATOM   6098  CZ  ARG D  81     -25.593 -17.966 -68.711  1.00 55.81           C
ANISOU 6098  CZ  ARG D  81     7253   7021   6931  -1057    444   -846       C
ATOM   6099  NH1 ARG D  81     -24.565 -17.452 -68.058  1.00 53.78           N
ANISOU 6099  NH1 ARG D  81     7028   6717   6688   -996    416   -780       N
ATOM   6100  NH2 ARG D  81     -26.484 -17.172 -69.289  1.00 63.87           N
ANISOU 6100  NH2 ARG D  81     8175   8138   7956  -1056    424   -883       N
ATOM   6101  N   LYS D  82     -24.809 -22.613 -73.419  1.00 49.88           N
ANISOU 6101  N   LYS D  82     6611   6222   6118  -1133    511   -969       N
ATOM   6102  CA  LYS D  82     -25.595 -23.348 -74.406  1.00 56.51           C
ANISOU 6102  CA  LYS D  82     7423   7105   6942  -1191    539  -1039       C
ATOM   6103  C   LYS D  82     -24.946 -24.670 -74.777  1.00 58.52           C
ANISOU 6103  C   LYS D  82     7774   7283   7180  -1204    565  -1040       C
ATOM   6104  O   LYS D  82     -25.640 -25.603 -75.194  1.00 62.51           O
ANISOU 6104  O   LYS D  82     8295   7791   7665  -1279    611  -1103       O
ATOM   6105  CB  LYS D  82     -25.779 -22.505 -75.670  1.00 55.41           C
ANISOU 6105  CB  LYS D  82     7173   7067   6813  -1142    491  -1051       C
ATOM   6106  CG  LYS D  82     -27.135 -21.882 -75.848  1.00 52.57           C
ANISOU 6106  CG  LYS D  82     6715   6809   6450  -1174    489  -1117       C
ATOM   6107  CD  LYS D  82     -27.453 -21.767 -77.320  1.00 58.55           C
ANISOU 6107  CD  LYS D  82     7399   7649   7199  -1150    462  -1156       C
ATOM   6108  CE  LYS D  82     -28.309 -20.558 -77.636  1.00 64.39           C
ANISOU 6108  CE  LYS D  82     8034   8495   7936  -1113    419  -1187       C
ATOM   6109  NZ  LYS D  82     -28.664 -20.546 -79.089  1.00 68.51           N
ANISOU 6109  NZ  LYS D  82     8495   9094   8441  -1086    392  -1233       N
ATOM   6110  N   HIS D  83     -23.620 -24.769 -74.650  1.00 55.52           N
ANISOU 6110  N   HIS D  83     7453   6837   6804  -1131    537   -977       N
ATOM   6111  CA  HIS D  83     -22.886 -25.864 -75.274  1.00 57.10           C
ANISOU 6111  CA  HIS D  83     7724   6982   6989  -1118    545   -977       C
ATOM   6112  C   HIS D  83     -21.990 -26.587 -74.281  1.00 48.25           C
ANISOU 6112  C   HIS D  83     6736   5746   5851  -1091    554   -940       C
ATOM   6113  O   HIS D  83     -21.113 -27.356 -74.687  1.00 49.92           O
ANISOU 6113  O   HIS D  83     7011   5907   6051  -1052    546   -930       O
ATOM   6114  CB  HIS D  83     -22.085 -25.350 -76.479  1.00 51.95           C
ANISOU 6114  CB  HIS D  83     7003   6381   6355  -1042    494   -953       C
ATOM   6115  CG  HIS D  83     -22.956 -24.812 -77.572  1.00 51.43           C
ANISOU 6115  CG  HIS D  83     6828   6418   6293  -1060    483   -994       C
ATOM   6116  ND1 HIS D  83     -23.114 -23.463 -77.804  1.00 58.48           N
ANISOU 6116  ND1 HIS D  83     7630   7386   7203  -1017    443   -975       N
ATOM   6117  CD2 HIS D  83     -23.751 -25.442 -78.468  1.00 50.48           C
ANISOU 6117  CD2 HIS D  83     6681   6339   6158  -1114    508  -1057       C
ATOM   6118  CE1 HIS D  83     -23.952 -23.285 -78.810  1.00 56.47           C
ANISOU 6118  CE1 HIS D  83     7302   7214   6942  -1035    438  -1024       C
ATOM   6119  NE2 HIS D  83     -24.359 -24.471 -79.224  1.00 54.77           N
ANISOU 6119  NE2 HIS D  83     7117   6984   6709  -1095    476  -1077       N
ATOM   6120  N   ASN D  84     -22.218 -26.366 -72.989  1.00 47.42           N
ANISOU 6120  N   ASN D  84     6678   5600   5740  -1109    570   -924       N
ATOM   6121  CA  ASN D  84     -21.425 -26.987 -71.936  1.00 47.25           C
ANISOU 6121  CA  ASN D  84     6791   5467   5695  -1076    575   -891       C
ATOM   6122  C   ASN D  84     -19.939 -26.701 -72.131  1.00 52.50           C
ANISOU 6122  C   ASN D  84     7453   6119   6375   -960    513   -842       C
ATOM   6123  O   ASN D  84     -19.094 -27.588 -72.025  1.00 58.99           O
ANISOU 6123  O   ASN D  84     8377   6865   7173   -916    507   -834       O
ATOM   6124  CB  ASN D  84     -21.695 -28.489 -71.862  1.00 49.27           C
ANISOU 6124  CB  ASN D  84     7182   5635   5905  -1138    633   -927       C
ATOM   6125  CG  ASN D  84     -21.148 -29.106 -70.607  1.00 55.49           C
ANISOU 6125  CG  ASN D  84     8126   6301   6654  -1114    645   -899       C
ATOM   6126  OD1 ASN D  84     -20.739 -28.397 -69.685  1.00 62.82           O
ANISOU 6126  OD1 ASN D  84     9057   7219   7594  -1063    616   -858       O
ATOM   6127  ND2 ASN D  84     -21.098 -30.434 -70.571  1.00 49.52           N
ANISOU 6127  ND2 ASN D  84     7513   5451   5851  -1143    687   -920       N
ATOM   6128  N   LEU D  85     -19.619 -25.446 -72.447  1.00 47.63           N
ANISOU 6128  N   LEU D  85     6721   5579   5796   -910    467   -816       N
ATOM   6129  CA  LEU D  85     -18.240 -24.999 -72.574  1.00 48.64           C
ANISOU 6129  CA  LEU D  85     6831   5709   5942   -811    414   -778       C
ATOM   6130  C   LEU D  85     -17.872 -24.131 -71.377  1.00 61.12           C
ANISOU 6130  C   LEU D  85     8410   7277   7536   -770    391   -740       C
ATOM   6131  O   LEU D  85     -17.183 -23.115 -71.501  1.00 53.40           O
ANISOU 6131  O   LEU D  85     7356   6345   6586   -714    351   -715       O
ATOM   6132  CB  LEU D  85     -18.021 -24.271 -73.894  1.00 47.63           C
ANISOU 6132  CB  LEU D  85     6588   5670   5841   -787    387   -780       C
ATOM   6133  CG  LEU D  85     -18.130 -25.168 -75.133  1.00 51.72           C
ANISOU 6133  CG  LEU D  85     7109   6196   6345   -810    402   -815       C
ATOM   6134  CD1 LEU D  85     -18.050 -24.340 -76.392  1.00 61.91           C
ANISOU 6134  CD1 LEU D  85     8290   7575   7657   -792    378   -816       C
ATOM   6135  CD2 LEU D  85     -17.061 -26.265 -75.138  1.00 45.62           C
ANISOU 6135  CD2 LEU D  85     6431   5350   5554   -761    395   -816       C
ATOM   6136  N   CYS D  86     -18.377 -24.544 -70.210  1.00 77.55           N
ANISOU 6136  N   CYS D  86    10578   9294   9593   -806    420   -740       N
ATOM   6137  CA  CYS D  86     -18.163 -23.939 -68.902  1.00 70.83           C
ANISOU 6137  CA  CYS D  86     9751   8416   8744   -778    406   -708       C
ATOM   6138  C   CYS D  86     -17.455 -24.942 -67.995  1.00 76.11           C
ANISOU 6138  C   CYS D  86    10569   8976   9373   -734    406   -701       C
ATOM   6139  O   CYS D  86     -17.639 -26.155 -68.134  1.00 93.82           O
ANISOU 6139  O   CYS D  86    12916  11154  11578   -764    439   -724       O
ATOM   6140  CB  CYS D  86     -19.502 -23.537 -68.273  1.00 65.91           C
ANISOU 6140  CB  CYS D  86     9110   7812   8121   -863    446   -720       C
ATOM   6141  SG  CYS D  86     -20.310 -22.044 -68.941  1.00 74.34           S
ANISOU 6141  SG  CYS D  86    10009   9007   9231   -886    430   -725       S
ATOM   6142  N   GLY D  87     -16.647 -24.438 -67.063  1.00 68.43           N
ANISOU 6142  N   GLY D  87     9612   7982   8405   -661    369   -671       N
ATOM   6143  CA  GLY D  87     -15.978 -25.318 -66.114  1.00 67.99           C
ANISOU 6143  CA  GLY D  87     9705   7824   8305   -604    360   -665       C
ATOM   6144  C   GLY D  87     -16.960 -26.120 -65.278  1.00 69.79           C
ANISOU 6144  C   GLY D  87    10064   7968   8485   -683    421   -674       C
ATOM   6145  O   GLY D  87     -18.076 -25.678 -64.995  1.00 74.94           O
ANISOU 6145  O   GLY D  87    10678   8648   9146   -771    461   -679       O
ATOM   6146  N   GLU D  88     -16.536 -27.328 -64.882  1.00 66.71           N
ANISOU 6146  N   GLU D  88     9836   7472   8039   -650    429   -681       N
ATOM   6147  CA  GLU D  88     -17.390 -28.252 -64.134  1.00 71.99           C
ANISOU 6147  CA  GLU D  88    10661   8043   8650   -730    496   -693       C
ATOM   6148  C   GLU D  88     -17.038 -28.305 -62.649  1.00 69.85           C
ANISOU 6148  C   GLU D  88    10517   7685   8337   -678    485   -667       C
ATOM   6149  O   GLU D  88     -17.910 -28.125 -61.796  1.00 60.29           O
ANISOU 6149  O   GLU D  88     9346   6450   7111   -754    532   -664       O
ATOM   6150  CB  GLU D  88     -17.321 -29.666 -64.727  1.00 85.56           C
ANISOU 6150  CB  GLU D  88    12503   9686  10320   -743    525   -721       C
ATOM   6151  CG  GLU D  88     -18.469 -30.571 -64.246  1.00101.08           C
ANISOU 6151  CG  GLU D  88    14610  11567  12230   -865    617   -746       C
ATOM   6152  CD  GLU D  88     -18.057 -32.014 -63.901  1.00106.76           C
ANISOU 6152  CD  GLU D  88    15555  12143  12868   -836    638   -753       C
ATOM   6153  OE1 GLU D  88     -16.858 -32.373 -63.994  1.00104.76           O
ANISOU 6153  OE1 GLU D  88    15353  11853  12596   -708    575   -740       O
ATOM   6154  OE2 GLU D  88     -18.957 -32.794 -63.522  1.00106.32           O
ANISOU 6154  OE2 GLU D  88    15628  12008  12761   -943    721   -777       O
ATOM   6155  N   THR D  89     -15.772 -28.566 -62.326  1.00 71.97           N
ANISOU 6155  N   THR D  89    10852   7910   8584   -548    423   -654       N
ATOM   6156  CA  THR D  89     -15.323 -28.650 -60.947  1.00 70.59           C
ANISOU 6156  CA  THR D  89    10804   7653   8364   -478    401   -632       C
ATOM   6157  C   THR D  89     -15.173 -27.256 -60.334  1.00 75.20           C
ANISOU 6157  C   THR D  89    11261   8313   8999   -451    364   -607       C
ATOM   6158  O   THR D  89     -15.181 -26.234 -61.025  1.00 75.73           O
ANISOU 6158  O   THR D  89    11148   8493   9134   -464    344   -604       O
ATOM   6159  CB  THR D  89     -13.996 -29.400 -60.860  1.00 65.17           C
ANISOU 6159  CB  THR D  89    10223   6905   7635   -335    339   -639       C
ATOM   6160  OG1 THR D  89     -12.914 -28.480 -61.034  1.00 71.66           O
ANISOU 6160  OG1 THR D  89    10903   7817   8509   -229    260   -636       O
ATOM   6161  CG2 THR D  89     -13.917 -30.462 -61.924  1.00 54.78           C
ANISOU 6161  CG2 THR D  89     8956   5561   6296   -345    355   -666       C
ATOM   6162  N   GLU D  90     -15.043 -27.217 -59.006  1.00 76.35           N
ANISOU 6162  N   GLU D  90    11512   8392   9106   -414    356   -588       N
ATOM   6163  CA  GLU D  90     -14.817 -25.934 -58.352  1.00 74.28           C
ANISOU 6163  CA  GLU D  90    11139   8195   8888   -380    318   -565       C
ATOM   6164  C   GLU D  90     -13.455 -25.372 -58.736  1.00 72.88           C
ANISOU 6164  C   GLU D  90    10855   8086   8749   -254    235   -569       C
ATOM   6165  O   GLU D  90     -13.339 -24.184 -59.061  1.00 67.62           O
ANISOU 6165  O   GLU D  90    10022   7522   8148   -259    213   -561       O
ATOM   6166  CB  GLU D  90     -14.963 -26.079 -56.834  1.00 77.02           C
ANISOU 6166  CB  GLU D  90    11632   8452   9181   -365    329   -546       C
ATOM   6167  CG  GLU D  90     -14.552 -24.854 -55.992  1.00 81.14           C
ANISOU 6167  CG  GLU D  90    12065   9026   9739   -309    281   -523       C
ATOM   6168  CD  GLU D  90     -15.396 -23.609 -56.257  1.00 84.01           C
ANISOU 6168  CD  GLU D  90    12252   9494  10173   -402    306   -513       C
ATOM   6169  OE1 GLU D  90     -16.642 -23.714 -56.324  1.00 85.58           O
ANISOU 6169  OE1 GLU D  90    12458   9691  10369   -525    375   -519       O
ATOM   6170  OE2 GLU D  90     -14.808 -22.515 -56.395  1.00 79.38           O
ANISOU 6170  OE2 GLU D  90    11523   8995   9641   -350    256   -504       O
ATOM   6171  N   GLU D  91     -12.419 -26.216 -58.740  1.00 72.51           N
ANISOU 6171  N   GLU D  91    10906   7986   8660   -144    190   -587       N
ATOM   6172  CA  GLU D  91     -11.100 -25.758 -59.168  1.00 74.05           C
ANISOU 6172  CA  GLU D  91    10993   8253   8890    -29    114   -606       C
ATOM   6173  C   GLU D  91     -11.143 -25.182 -60.580  1.00 73.71           C
ANISOU 6173  C   GLU D  91    10774   8318   8914    -79    121   -617       C
ATOM   6174  O   GLU D  91     -10.418 -24.229 -60.879  1.00 77.97           O
ANISOU 6174  O   GLU D  91    11171   8947   9505    -35     80   -625       O
ATOM   6175  CB  GLU D  91     -10.086 -26.906 -59.078  1.00 75.79           C
ANISOU 6175  CB  GLU D  91    11349   8400   9048     95     68   -635       C
ATOM   6176  CG  GLU D  91      -9.562 -27.209 -57.647  1.00 86.27           C
ANISOU 6176  CG  GLU D  91    12827   9643  10311    201     28   -633       C
ATOM   6177  CD  GLU D  91     -10.495 -28.108 -56.793  1.00 92.69           C
ANISOU 6177  CD  GLU D  91    13855  10318  11043    143     87   -609       C
ATOM   6178  OE1 GLU D  91     -10.592 -27.872 -55.562  1.00 88.94           O
ANISOU 6178  OE1 GLU D  91    13460   9795  10536    166     82   -589       O
ATOM   6179  OE2 GLU D  91     -11.116 -29.055 -57.336  1.00 90.67           O
ANISOU 6179  OE2 GLU D  91    13695  10001  10755     72    142   -613       O
ATOM   6180  N   GLU D  92     -12.010 -25.719 -61.448  1.00 72.85           N
ANISOU 6180  N   GLU D  92    10674   8202   8804   -175    175   -620       N
ATOM   6181  CA  GLU D  92     -12.114 -25.233 -62.824  1.00 69.37           C
ANISOU 6181  CA  GLU D  92    10080   7857   8419   -221    182   -631       C
ATOM   6182  C   GLU D  92     -12.839 -23.893 -62.906  1.00 60.92           C
ANISOU 6182  C   GLU D  92     8869   6874   7406   -296    201   -609       C
ATOM   6183  O   GLU D  92     -12.434 -23.016 -63.675  1.00 65.87           O
ANISOU 6183  O   GLU D  92     9355   7591   8082   -286    179   -612       O
ATOM   6184  CB  GLU D  92     -12.842 -26.255 -63.696  1.00 72.17           C
ANISOU 6184  CB  GLU D  92    10493   8178   8750   -296    233   -646       C
ATOM   6185  CG  GLU D  92     -12.130 -27.581 -63.864  1.00 74.91           C
ANISOU 6185  CG  GLU D  92    10974   8446   9044   -224    215   -670       C
ATOM   6186  CD  GLU D  92     -12.943 -28.568 -64.682  1.00 75.64           C
ANISOU 6186  CD  GLU D  92    11127   8502   9112   -312    273   -686       C
ATOM   6187  OE1 GLU D  92     -14.186 -28.606 -64.545  1.00 73.21           O
ANISOU 6187  OE1 GLU D  92    10839   8180   8799   -428    337   -681       O
ATOM   6188  OE2 GLU D  92     -12.337 -29.312 -65.466  1.00 84.68           O
ANISOU 6188  OE2 GLU D  92    12296   9635  10243   -265    255   -710       O
ATOM   6189  N   LYS D  93     -13.924 -23.733 -62.144  1.00 54.57           N
ANISOU 6189  N   LYS D  93     8105   6041   6590   -374    244   -591       N
ATOM   6190  CA  LYS D  93     -14.660 -22.475 -62.128  1.00 52.02           C
ANISOU 6190  CA  LYS D  93     7656   5794   6314   -437    258   -573       C
ATOM   6191  C   LYS D  93     -13.809 -21.313 -61.629  1.00 58.41           C
ANISOU 6191  C   LYS D  93     8380   6654   7158   -365    207   -557       C
ATOM   6192  O   LYS D  93     -14.012 -20.169 -62.048  1.00 60.04           O
ANISOU 6192  O   LYS D  93     8458   6943   7412   -391    204   -547       O
ATOM   6193  CB  LYS D  93     -15.901 -22.622 -61.260  1.00 57.86           C
ANISOU 6193  CB  LYS D  93     8467   6489   7028   -526    312   -566       C
ATOM   6194  CG  LYS D  93     -16.869 -23.667 -61.751  1.00 56.74           C
ANISOU 6194  CG  LYS D  93     8396   6308   6855   -618    374   -592       C
ATOM   6195  CD  LYS D  93     -18.290 -23.301 -61.349  1.00 64.37           C
ANISOU 6195  CD  LYS D  93     9340   7293   7825   -732    431   -599       C
ATOM   6196  CE  LYS D  93     -19.119 -24.552 -61.220  1.00 71.55           C
ANISOU 6196  CE  LYS D  93    10383   8123   8680   -820    502   -629       C
ATOM   6197  NZ  LYS D  93     -18.397 -25.491 -60.326  1.00 78.32           N
ANISOU 6197  NZ  LYS D  93    11423   8858   9476   -758    496   -615       N
ATOM   6198  N   ILE D  94     -12.865 -21.578 -60.730  1.00 61.60           N
ANISOU 6198  N   ILE D  94     8860   7010   7537   -272    167   -558       N
ATOM   6199  CA  ILE D  94     -11.965 -20.527 -60.265  1.00 58.15           C
ANISOU 6199  CA  ILE D  94     8339   6624   7132   -201    119   -554       C
ATOM   6200  C   ILE D  94     -11.008 -20.121 -61.380  1.00 63.45           C
ANISOU 6200  C   ILE D  94     8893   7374   7841   -159     88   -577       C
ATOM   6201  O   ILE D  94     -10.824 -18.928 -61.661  1.00 58.00           O
ANISOU 6201  O   ILE D  94     8079   6761   7197   -170     80   -572       O
ATOM   6202  CB  ILE D  94     -11.205 -20.998 -59.015  1.00 55.22           C
ANISOU 6202  CB  ILE D  94     8082   6183   6717   -104     80   -558       C
ATOM   6203  CG1 ILE D  94     -12.122 -21.002 -57.797  1.00 57.23           C
ANISOU 6203  CG1 ILE D  94     8430   6374   6942   -151    112   -530       C
ATOM   6204  CG2 ILE D  94      -9.959 -20.164 -58.806  1.00 54.79           C
ANISOU 6204  CG2 ILE D  94     7935   6191   6693    -12     22   -576       C
ATOM   6205  CD1 ILE D  94     -11.771 -22.081 -56.790  1.00 54.80           C
ANISOU 6205  CD1 ILE D  94     8306   5955   6560    -82     98   -534       C
ATOM   6206  N   ARG D  95     -10.388 -21.113 -62.036  1.00 68.55           N
ANISOU 6206  N   ARG D  95     9583   7997   8464   -114     74   -607       N
ATOM   6207  CA  ARG D  95      -9.466 -20.830 -63.139  1.00 62.22           C
ANISOU 6207  CA  ARG D  95     8676   7269   7695    -79     51   -637       C
ATOM   6208  C   ARG D  95     -10.141 -20.035 -64.252  1.00 55.68           C
ANISOU 6208  C   ARG D  95     7733   6513   6909   -167     85   -623       C
ATOM   6209  O   ARG D  95      -9.546 -19.103 -64.802  1.00 64.21           O
ANISOU 6209  O   ARG D  95     8702   7667   8027   -158     73   -633       O
ATOM   6210  CB  ARG D  95      -8.898 -22.131 -63.697  1.00 51.13           C
ANISOU 6210  CB  ARG D  95     7348   5824   6255    -26     36   -671       C
ATOM   6211  CG  ARG D  95      -8.128 -22.921 -62.703  1.00 43.51           C
ANISOU 6211  CG  ARG D  95     6502   4790   5241     80     -7   -691       C
ATOM   6212  CD  ARG D  95      -7.492 -24.114 -63.355  1.00 42.62           C
ANISOU 6212  CD  ARG D  95     6454   4646   5094    142    -26   -729       C
ATOM   6213  NE  ARG D  95      -6.044 -23.968 -63.340  1.00 52.62           N
ANISOU 6213  NE  ARG D  95     7664   5960   6367    258    -88   -781       N
ATOM   6214  CZ  ARG D  95      -5.350 -23.548 -64.381  1.00 66.68           C
ANISOU 6214  CZ  ARG D  95     9316   7829   8189    264    -97   -816       C
ATOM   6215  NH1 ARG D  95      -5.988 -23.268 -65.498  1.00 69.10           N
ANISOU 6215  NH1 ARG D  95     9551   8175   8527    167    -52   -798       N
ATOM   6216  NH2 ARG D  95      -4.035 -23.416 -64.320  1.00 69.61           N
ANISOU 6216  NH2 ARG D  95     9631   8252   8566    365   -150   -875       N
ATOM   6217  N   VAL D  96     -11.373 -20.405 -64.610  1.00 43.62           N
ANISOU 6217  N   VAL D  96     6237   4964   5371   -253    129   -607       N
ATOM   6218  CA  VAL D  96     -12.146 -19.634 -65.584  1.00 50.22           C
ANISOU 6218  CA  VAL D  96     6973   5869   6240   -330    157   -596       C
ATOM   6219  C   VAL D  96     -12.289 -18.178 -65.136  1.00 55.06           C
ANISOU 6219  C   VAL D  96     7500   6532   6886   -342    152   -572       C
ATOM   6220  O   VAL D  96     -11.823 -17.251 -65.811  1.00 57.91           O
ANISOU 6220  O   VAL D  96     7765   6959   7278   -336    142   -574       O
ATOM   6221  CB  VAL D  96     -13.521 -20.285 -65.804  1.00 49.22           C
ANISOU 6221  CB  VAL D  96     6896   5712   6092   -416    204   -593       C
ATOM   6222  CG1 VAL D  96     -14.423 -19.355 -66.601  1.00 58.11           C
ANISOU 6222  CG1 VAL D  96     7919   6913   7248   -484    224   -585       C
ATOM   6223  CG2 VAL D  96     -13.369 -21.620 -66.508  1.00 43.79           C
ANISOU 6223  CG2 VAL D  96     6280   4983   5375   -413    214   -619       C
ATOM   6224  N   ASP D  97     -12.937 -17.960 -63.984  1.00 49.18           N
ANISOU 6224  N   ASP D  97     6797   5755   6133   -362    160   -550       N
ATOM   6225  CA  ASP D  97     -13.237 -16.603 -63.527  1.00 50.23           C
ANISOU 6225  CA  ASP D  97     6855   5933   6295   -380    158   -526       C
ATOM   6226  C   ASP D  97     -11.982 -15.740 -63.432  1.00 49.99           C
ANISOU 6226  C   ASP D  97     6758   5943   6291   -316    123   -532       C
ATOM   6227  O   ASP D  97     -11.995 -14.568 -63.831  1.00 51.21           O
ANISOU 6227  O   ASP D  97     6825   6156   6475   -336    126   -522       O
ATOM   6228  CB  ASP D  97     -13.938 -16.658 -62.176  1.00 53.42           C
ANISOU 6228  CB  ASP D  97     7328   6288   6682   -400    170   -508       C
ATOM   6229  CG  ASP D  97     -15.298 -17.298 -62.257  1.00 62.56           C
ANISOU 6229  CG  ASP D  97     8534   7420   7818   -483    215   -511       C
ATOM   6230  OD1 ASP D  97     -15.875 -17.297 -63.371  1.00 64.86           O
ANISOU 6230  OD1 ASP D  97     8772   7753   8117   -530    234   -523       O
ATOM   6231  OD2 ASP D  97     -15.791 -17.787 -61.207  1.00 61.55           O
ANISOU 6231  OD2 ASP D  97     8495   7230   7660   -503    235   -506       O
ATOM   6232  N   VAL D  98     -10.893 -16.303 -62.901  1.00 47.04           N
ANISOU 6232  N   VAL D  98     6429   5539   5903   -239     92   -554       N
ATOM   6233  CA  VAL D  98      -9.626 -15.581 -62.826  1.00 44.67           C
ANISOU 6233  CA  VAL D  98     6060   5286   5627   -179     60   -577       C
ATOM   6234  C   VAL D  98      -9.110 -15.235 -64.225  1.00 53.32           C
ANISOU 6234  C   VAL D  98     7069   6444   6745   -192     68   -599       C
ATOM   6235  O   VAL D  98      -8.730 -14.086 -64.494  1.00 54.99           O
ANISOU 6235  O   VAL D  98     7196   6711   6986   -204     72   -601       O
ATOM   6236  CB  VAL D  98      -8.596 -16.401 -62.025  1.00 48.82           C
ANISOU 6236  CB  VAL D  98     6654   5771   6126    -83     19   -609       C
ATOM   6237  CG1 VAL D  98      -7.196 -15.736 -62.098  1.00 38.83           C
ANISOU 6237  CG1 VAL D  98     5299   4568   4885    -21    -13   -654       C
ATOM   6238  CG2 VAL D  98      -9.079 -16.591 -60.554  1.00 37.77           C
ANISOU 6238  CG2 VAL D  98     5345   4306   4699    -69     12   -584       C
ATOM   6239  N   LEU D  99      -9.090 -16.222 -65.140  1.00 51.94           N
ANISOU 6239  N   LEU D  99     6923   6257   6554   -194     75   -617       N
ATOM   6240  CA  LEU D  99      -8.550 -15.984 -66.481  1.00 55.96           C
ANISOU 6240  CA  LEU D  99     7359   6823   7081   -204     83   -642       C
ATOM   6241  C   LEU D  99      -9.391 -14.974 -67.250  1.00 57.58           C
ANISOU 6241  C   LEU D  99     7503   7070   7304   -278    115   -611       C
ATOM   6242  O   LEU D  99      -8.843 -14.061 -67.886  1.00 49.56           O
ANISOU 6242  O   LEU D  99     6415   6107   6308   -287    123   -621       O
ATOM   6243  CB  LEU D  99      -8.460 -17.294 -67.269  1.00 56.38           C
ANISOU 6243  CB  LEU D  99     7461   6850   7110   -192     84   -665       C
ATOM   6244  CG  LEU D  99      -7.258 -17.445 -68.220  1.00 52.06           C
ANISOU 6244  CG  LEU D  99     6861   6349   6572   -153     73   -714       C
ATOM   6245  CD1 LEU D  99      -7.586 -18.274 -69.469  1.00 44.66           C
ANISOU 6245  CD1 LEU D  99     5939   5408   5622   -182     91   -722       C
ATOM   6246  CD2 LEU D  99      -6.593 -16.095 -68.599  1.00 42.70           C
ANISOU 6246  CD2 LEU D  99     5569   5236   5419   -167     81   -727       C
ATOM   6247  N   GLU D 100     -10.721 -15.122 -67.205  1.00 53.82           N
ANISOU 6247  N   GLU D 100     7061   6572   6818   -331    135   -580       N
ATOM   6248  CA  GLU D 100     -11.599 -14.211 -67.934  1.00 48.05           C
ANISOU 6248  CA  GLU D 100     6278   5883   6097   -389    157   -558       C
ATOM   6249  C   GLU D 100     -11.357 -12.771 -67.507  1.00 53.75           C
ANISOU 6249  C   GLU D 100     6945   6637   6840   -388    154   -541       C
ATOM   6250  O   GLU D 100     -11.234 -11.872 -68.347  1.00 62.18           O
ANISOU 6250  O   GLU D 100     7962   7748   7916   -406    166   -538       O
ATOM   6251  CB  GLU D 100     -13.058 -14.603 -67.712  1.00 49.62           C
ANISOU 6251  CB  GLU D 100     6515   6059   6280   -440    175   -541       C
ATOM   6252  CG  GLU D 100     -14.077 -13.524 -68.063  1.00 50.98           C
ANISOU 6252  CG  GLU D 100     6636   6275   6459   -484    188   -520       C
ATOM   6253  CD  GLU D 100     -15.499 -13.937 -67.694  1.00 64.73           C
ANISOU 6253  CD  GLU D 100     8407   8002   8186   -534    205   -519       C
ATOM   6254  OE1 GLU D 100     -15.752 -15.146 -67.537  1.00 74.78           O
ANISOU 6254  OE1 GLU D 100     9740   9233   9440   -549    217   -535       O
ATOM   6255  OE2 GLU D 100     -16.368 -13.060 -67.538  1.00 74.47           O
ANISOU 6255  OE2 GLU D 100     9606   9266   9424   -559    208   -506       O
ATOM   6256  N   ASN D 101     -11.259 -12.540 -66.195  1.00 48.75           N
ANISOU 6256  N   ASN D 101     6330   5980   6211   -366    140   -530       N
ATOM   6257  CA  ASN D 101     -11.026 -11.189 -65.705  1.00 46.43           C
ANISOU 6257  CA  ASN D 101     5990   5715   5938   -365    138   -516       C
ATOM   6258  C   ASN D 101      -9.586 -10.759 -65.958  1.00 45.23           C
ANISOU 6258  C   ASN D 101     5790   5594   5801   -331    132   -549       C
ATOM   6259  O   ASN D 101      -9.335  -9.610 -66.326  1.00 49.40           O
ANISOU 6259  O   ASN D 101     6270   6159   6343   -352    147   -546       O
ATOM   6260  CB  ASN D 101     -11.391 -11.123 -64.222  1.00 50.26           C
ANISOU 6260  CB  ASN D 101     6510   6164   6421   -353    126   -497       C
ATOM   6261  CG  ASN D 101     -12.891 -11.086 -64.003  1.00 48.92           C
ANISOU 6261  CG  ASN D 101     6362   5982   6242   -404    142   -469       C
ATOM   6262  OD1 ASN D 101     -13.508 -10.038 -64.164  1.00 47.86           O
ANISOU 6262  OD1 ASN D 101     6188   5880   6117   -432    151   -449       O
ATOM   6263  ND2 ASN D 101     -13.496 -12.236 -63.671  1.00 42.66           N
ANISOU 6263  ND2 ASN D 101     5637   5145   5428   -416    149   -472       N
ATOM   6264  N   GLN D 102      -8.633 -11.682 -65.813  1.00 48.62           N
ANISOU 6264  N   GLN D 102     6237   6012   6225   -280    112   -588       N
ATOM   6265  CA  GLN D 102      -7.239 -11.388 -66.145  1.00 49.30           C
ANISOU 6265  CA  GLN D 102     6267   6139   6324   -249    107   -637       C
ATOM   6266  C   GLN D 102      -7.067 -10.982 -67.605  1.00 53.81           C
ANISOU 6266  C   GLN D 102     6794   6751   6899   -291    138   -648       C
ATOM   6267  O   GLN D 102      -6.310 -10.051 -67.911  1.00 60.77           O
ANISOU 6267  O   GLN D 102     7621   7675   7796   -304    156   -671       O
ATOM   6268  CB  GLN D 102      -6.368 -12.611 -65.839  1.00 58.27           C
ANISOU 6268  CB  GLN D 102     7435   7257   7448   -178     74   -683       C
ATOM   6269  CG  GLN D 102      -4.881 -12.341 -65.859  1.00 57.98           C
ANISOU 6269  CG  GLN D 102     7334   7270   7425   -133     61   -750       C
ATOM   6270  CD  GLN D 102      -4.503 -11.279 -64.858  1.00 60.71           C
ANISOU 6270  CD  GLN D 102     7641   7637   7790   -124     55   -755       C
ATOM   6271  OE1 GLN D 102      -4.845 -11.379 -63.689  1.00 66.95           O
ANISOU 6271  OE1 GLN D 102     8474   8391   8572    -95     31   -732       O
ATOM   6272  NE2 GLN D 102      -3.825 -10.241 -65.317  1.00 60.97           N
ANISOU 6272  NE2 GLN D 102     7597   7726   7843   -156     81   -784       N
ATOM   6273  N   ALA D 103      -7.725 -11.698 -68.529  1.00 52.34           N
ANISOU 6273  N   ALA D 103     6635   6553   6698   -314    148   -636       N
ATOM   6274  CA  ALA D 103      -7.520 -11.446 -69.952  1.00 45.11           C
ANISOU 6274  CA  ALA D 103     5687   5672   5779   -346    175   -649       C
ATOM   6275  C   ALA D 103      -8.073 -10.088 -70.370  1.00 48.93           C
ANISOU 6275  C   ALA D 103     6149   6178   6264   -396    203   -615       C
ATOM   6276  O   ALA D 103      -7.504  -9.425 -71.249  1.00 49.41           O
ANISOU 6276  O   ALA D 103     6180   6270   6324   -419    230   -632       O
ATOM   6277  CB  ALA D 103      -8.165 -12.555 -70.785  1.00 49.74           C
ANISOU 6277  CB  ALA D 103     6311   6241   6347   -356    177   -644       C
ATOM   6278  N   MET D 104      -9.198  -9.660 -69.787  1.00 41.80           N
ANISOU 6278  N   MET D 104     5268   5256   5358   -413    198   -570       N
ATOM   6279  CA  MET D 104      -9.641  -8.305 -70.095  1.00 53.66           C
ANISOU 6279  CA  MET D 104     6756   6777   6857   -446    218   -542       C
ATOM   6280  C   MET D 104      -8.659  -7.280 -69.545  1.00 51.57           C
ANISOU 6280  C   MET D 104     6459   6527   6608   -443    229   -557       C
ATOM   6281  O   MET D 104      -8.386  -6.260 -70.191  1.00 59.71           O
ANISOU 6281  O   MET D 104     7478   7577   7632   -473    259   -557       O
ATOM   6282  CB  MET D 104     -11.045  -8.047 -69.556  1.00 57.25           C
ANISOU 6282  CB  MET D 104     7234   7215   7304   -458    208   -500       C
ATOM   6283  CG  MET D 104     -11.548  -6.635 -69.866  1.00 54.73           C
ANISOU 6283  CG  MET D 104     6909   6912   6974   -480    222   -472       C
ATOM   6284  SD  MET D 104     -11.958  -6.281 -71.610  1.00 62.07           S
ANISOU 6284  SD  MET D 104     7850   7864   7870   -502    242   -469       S
ATOM   6285  CE  MET D 104     -13.516  -7.155 -71.782  1.00 53.47           C
ANISOU 6285  CE  MET D 104     6775   6774   6765   -504    220   -460       C
ATOM   6286  N   ASP D 105      -8.097  -7.547 -68.369  1.00 40.82           N
ANISOU 6286  N   ASP D 105     5089   5157   5265   -409    207   -574       N
ATOM   6287  CA  ASP D 105      -7.079  -6.651 -67.824  1.00 59.11           C
ANISOU 6287  CA  ASP D 105     7366   7495   7598   -406    217   -602       C
ATOM   6288  C   ASP D 105      -5.856  -6.591 -68.727  1.00 58.40           C
ANISOU 6288  C   ASP D 105     7236   7442   7510   -416    243   -659       C
ATOM   6289  O   ASP D 105      -5.312  -5.512 -68.976  1.00 56.77           O
ANISOU 6289  O   ASP D 105     7004   7259   7306   -451    278   -675       O
ATOM   6290  CB  ASP D 105      -6.672  -7.099 -66.421  1.00 68.07           C
ANISOU 6290  CB  ASP D 105     8501   8617   8747   -355    181   -618       C
ATOM   6291  CG  ASP D 105      -7.577  -6.544 -65.351  1.00 71.19           C
ANISOU 6291  CG  ASP D 105     8918   8985   9145   -359    170   -571       C
ATOM   6292  OD1 ASP D 105      -8.661  -6.034 -65.714  1.00 70.92           O
ANISOU 6292  OD1 ASP D 105     8902   8943   9100   -395    183   -526       O
ATOM   6293  OD2 ASP D 105      -7.206  -6.630 -64.156  1.00 76.82           O
ANISOU 6293  OD2 ASP D 105     9631   9689   9868   -322    145   -582       O
ATOM   6294  N   THR D 106      -5.394  -7.750 -69.206  1.00 61.05           N
ANISOU 6294  N   THR D 106     7569   7784   7842   -389    230   -695       N
ATOM   6295  CA  THR D 106      -4.254  -7.786 -70.126  1.00 56.93           C
ANISOU 6295  CA  THR D 106     7005   7302   7321   -400    256   -756       C
ATOM   6296  C   THR D 106      -4.587  -7.116 -71.451  1.00 59.05           C
ANISOU 6296  C   THR D 106     7286   7579   7572   -461    302   -736       C
ATOM   6297  O   THR D 106      -3.761  -6.387 -72.013  1.00 58.39           O
ANISOU 6297  O   THR D 106     7173   7526   7486   -498    344   -774       O
ATOM   6298  CB  THR D 106      -3.824  -9.228 -70.379  1.00 47.40           C
ANISOU 6298  CB  THR D 106     5802   6097   6112   -352    228   -795       C
ATOM   6299  OG1 THR D 106      -3.394  -9.820 -69.155  1.00 42.26           O
ANISOU 6299  OG1 THR D 106     5152   5436   5470   -285    183   -820       O
ATOM   6300  CG2 THR D 106      -2.693  -9.281 -71.392  1.00 58.67           C
ANISOU 6300  CG2 THR D 106     7181   7571   7539   -365    256   -864       C
ATOM   6301  N   ARG D 107      -5.786  -7.377 -71.972  1.00 59.60           N
ANISOU 6301  N   ARG D 107     7401   7621   7622   -471    296   -682       N
ATOM   6302  CA  ARG D 107      -6.230  -6.717 -73.190  1.00 53.78           C
ANISOU 6302  CA  ARG D 107     6688   6888   6859   -517    332   -659       C
ATOM   6303  C   ARG D 107      -6.209  -5.207 -73.027  1.00 62.47           C
ANISOU 6303  C   ARG D 107     7795   7987   7952   -552    364   -641       C
ATOM   6304  O   ARG D 107      -5.716  -4.485 -73.898  1.00 75.98           O
ANISOU 6304  O   ARG D 107     9514   9711   9646   -593    410   -657       O
ATOM   6305  CB  ARG D 107      -7.629  -7.202 -73.559  1.00 41.80           C
ANISOU 6305  CB  ARG D 107     5212   5347   5322   -512    311   -610       C
ATOM   6306  CG  ARG D 107      -8.345  -6.328 -74.590  1.00 42.50           C
ANISOU 6306  CG  ARG D 107     5336   5436   5378   -544    335   -577       C
ATOM   6307  CD  ARG D 107      -9.835  -6.673 -74.675  1.00 52.96           C
ANISOU 6307  CD  ARG D 107     6689   6747   6686   -533    307   -538       C
ATOM   6308  NE  ARG D 107     -10.082  -8.115 -74.696  1.00 62.07           N
ANISOU 6308  NE  ARG D 107     7839   7896   7848   -516    283   -552       N
ATOM   6309  CZ  ARG D 107      -9.973  -8.870 -75.782  1.00 62.63           C
ANISOU 6309  CZ  ARG D 107     7915   7978   7906   -520    290   -572       C
ATOM   6310  NH1 ARG D 107      -9.624  -8.315 -76.932  1.00 64.17           N
ANISOU 6310  NH1 ARG D 107     8117   8188   8078   -540    320   -579       N
ATOM   6311  NH2 ARG D 107     -10.213 -10.175 -75.720  1.00 65.56           N
ANISOU 6311  NH2 ARG D 107     8289   8337   8282   -505    271   -585       N
ATOM   6312  N   LEU D 108      -6.728  -4.708 -71.904  1.00 62.74           N
ANISOU 6312  N   LEU D 108     7835   8004   7998   -539    344   -609       N
ATOM   6313  CA  LEU D 108      -6.796  -3.262 -71.703  1.00 63.76           C
ANISOU 6313  CA  LEU D 108     7980   8128   8119   -570    372   -588       C
ATOM   6314  C   LEU D 108      -5.432  -2.666 -71.373  1.00 71.18           C
ANISOU 6314  C   LEU D 108     8878   9092   9075   -594    406   -644       C
ATOM   6315  O   LEU D 108      -5.158  -1.522 -71.745  1.00 71.85           O
ANISOU 6315  O   LEU D 108     8982   9175   9143   -640    453   -645       O
ATOM   6316  CB  LEU D 108      -7.808  -2.928 -70.608  1.00 54.18           C
ANISOU 6316  CB  LEU D 108     6782   6891   6911   -549    339   -539       C
ATOM   6317  CG  LEU D 108      -9.214  -2.745 -71.175  1.00 53.15           C
ANISOU 6317  CG  LEU D 108     6699   6745   6751   -549    327   -488       C
ATOM   6318  CD1 LEU D 108     -10.261  -3.075 -70.153  1.00 39.79           C
ANISOU 6318  CD1 LEU D 108     5009   5040   5071   -522    286   -458       C
ATOM   6319  CD2 LEU D 108      -9.376  -1.323 -71.672  1.00 63.66           C
ANISOU 6319  CD2 LEU D 108     8071   8067   8051   -575    360   -466       C
ATOM   6320  N   ASP D 109      -4.574  -3.413 -70.669  1.00 78.91           N
ANISOU 6320  N   ASP D 109     9803  10094  10084   -561    384   -695       N
ATOM   6321  CA  ASP D 109      -3.174  -3.014 -70.546  1.00 79.77           C
ANISOU 6321  CA  ASP D 109     9858  10243  10209   -582    416   -770       C
ATOM   6322  C   ASP D 109      -2.557  -2.776 -71.920  1.00 77.76           C
ANISOU 6322  C   ASP D 109     9604  10008   9932   -636    474   -808       C
ATOM   6323  O   ASP D 109      -1.791  -1.827 -72.110  1.00 72.76           O
ANISOU 6323  O   ASP D 109     8957   9393   9295   -691    530   -848       O
ATOM   6324  CB  ASP D 109      -2.376  -4.083 -69.789  1.00 83.19           C
ANISOU 6324  CB  ASP D 109    10236  10703  10668   -521    373   -829       C
ATOM   6325  CG  ASP D 109      -2.558  -4.007 -68.280  1.00 85.32           C
ANISOU 6325  CG  ASP D 109    10498  10960  10957   -477    330   -815       C
ATOM   6326  OD1 ASP D 109      -2.903  -2.920 -67.774  1.00 86.80           O
ANISOU 6326  OD1 ASP D 109    10698  11135  11147   -506    347   -783       O
ATOM   6327  OD2 ASP D 109      -2.345  -5.039 -67.601  1.00 84.91           O
ANISOU 6327  OD2 ASP D 109    10436  10910  10916   -412    281   -836       O
ATOM   6328  N   PHE D 110      -2.894  -3.625 -72.897  1.00 80.63           N
ANISOU 6328  N   PHE D 110     9988  10366  10280   -627    466   -797       N
ATOM   6329  CA  PHE D 110      -2.349  -3.467 -74.244  1.00 81.03           C
ANISOU 6329  CA  PHE D 110    10046  10434  10307   -677    521   -831       C
ATOM   6330  C   PHE D 110      -3.045  -2.352 -75.009  1.00 64.58           C
ANISOU 6330  C   PHE D 110     8040   8316   8182   -728    564   -776       C
ATOM   6331  O   PHE D 110      -2.387  -1.487 -75.587  1.00 64.40           O
ANISOU 6331  O   PHE D 110     8031   8298   8138   -790    630   -807       O
ATOM   6332  CB  PHE D 110      -2.461  -4.775 -75.030  1.00 83.58           C
ANISOU 6332  CB  PHE D 110    10367  10764  10626   -647    496   -839       C
ATOM   6333  CG  PHE D 110      -1.857  -4.709 -76.408  1.00 79.81           C
ANISOU 6333  CG  PHE D 110     9893  10306  10123   -697    551   -879       C
ATOM   6334  CD1 PHE D 110      -2.516  -4.080 -77.450  1.00 80.74           C
ANISOU 6334  CD1 PHE D 110    10083  10396  10199   -737    587   -832       C
ATOM   6335  CD2 PHE D 110      -0.633  -5.282 -76.660  1.00 82.08           C
ANISOU 6335  CD2 PHE D 110    10117  10643  10427   -698    566   -967       C
ATOM   6336  CE1 PHE D 110      -1.959  -4.022 -78.710  1.00 84.04           C
ANISOU 6336  CE1 PHE D 110    10514  10828  10590   -784    641   -867       C
ATOM   6337  CE2 PHE D 110      -0.078  -5.223 -77.913  1.00 81.70           C
ANISOU 6337  CE2 PHE D 110    10072  10615  10356   -748    621  -1007       C
ATOM   6338  CZ  PHE D 110      -0.743  -4.590 -78.941  1.00 82.49           C
ANISOU 6338  CZ  PHE D 110    10250  10680  10412   -795    661   -954       C
ATOM   6339  N   ALA D 111      -4.374  -2.379 -75.053  1.00 65.84           N
ANISOU 6339  N   ALA D 111     8253   8439   8323   -701    530   -701       N
ATOM   6340  CA  ALA D 111      -5.118  -1.427 -75.866  1.00 66.55           C
ANISOU 6340  CA  ALA D 111     8424   8497   8365   -729    559   -652       C
ATOM   6341  C   ALA D 111      -4.949   0.013 -75.400  1.00 78.39           C
ANISOU 6341  C   ALA D 111     9957   9977   9852   -767    598   -642       C
ATOM   6342  O   ALA D 111      -5.212   0.935 -76.181  1.00 87.36           O
ANISOU 6342  O   ALA D 111    11170  11083  10939   -799    638   -617       O
ATOM   6343  CB  ALA D 111      -6.602  -1.796 -75.876  1.00 55.68           C
ANISOU 6343  CB  ALA D 111     7084   7097   6974   -683    504   -587       C
ATOM   6344  N   ARG D 112      -4.513   0.241 -74.159  1.00 77.87           N
ANISOU 6344  N   ARG D 112     9841   9923   9824   -760    587   -661       N
ATOM   6345  CA  ARG D 112      -4.393   1.613 -73.679  1.00 83.54           C
ANISOU 6345  CA  ARG D 112    10592  10620  10531   -797    624   -652       C
ATOM   6346  C   ARG D 112      -3.081   2.269 -74.081  1.00 89.00           C
ANISOU 6346  C   ARG D 112    11272  11329  11215   -872    705   -721       C
ATOM   6347  O   ARG D 112      -2.970   3.497 -73.997  1.00 93.18           O
ANISOU 6347  O   ARG D 112    11853  11832  11720   -919    754   -715       O
ATOM   6348  CB  ARG D 112      -4.564   1.668 -72.161  1.00 82.41           C
ANISOU 6348  CB  ARG D 112    10404  10481  10428   -761    580   -642       C
ATOM   6349  CG  ARG D 112      -6.000   1.909 -71.737  1.00 85.67           C
ANISOU 6349  CG  ARG D 112    10864  10859  10828   -720    533   -564       C
ATOM   6350  CD  ARG D 112      -6.096   2.177 -70.258  1.00 91.18           C
ANISOU 6350  CD  ARG D 112    11527  11557  11560   -696    503   -555       C
ATOM   6351  NE  ARG D 112      -5.048   1.474 -69.531  1.00 92.25           N
ANISOU 6351  NE  ARG D 112    11582  11730  11740   -685    492   -617       N
ATOM   6352  CZ  ARG D 112      -5.214   0.294 -68.947  1.00 91.42           C
ANISOU 6352  CZ  ARG D 112    11439  11636  11661   -631    437   -620       C
ATOM   6353  NH1 ARG D 112      -6.394  -0.312 -68.998  1.00 85.98           N
ANISOU 6353  NH1 ARG D 112    10780  10926  10963   -597    395   -567       N
ATOM   6354  NH2 ARG D 112      -4.199  -0.276 -68.309  1.00 93.95           N
ANISOU 6354  NH2 ARG D 112    11695  11990  12013   -611    424   -681       N
ATOM   6355  N   VAL D 113      -2.090   1.487 -74.510  1.00 88.57           N
ANISOU 6355  N   VAL D 113    11154  11319  11178   -886    722   -793       N
ATOM   6356  CA  VAL D 113      -0.923   2.075 -75.158  1.00 88.73           C
ANISOU 6356  CA  VAL D 113    11170  11360  11182   -968    808   -867       C
ATOM   6357  C   VAL D 113      -1.236   2.440 -76.609  1.00 95.41           C
ANISOU 6357  C   VAL D 113    12114  12169  11967  -1012    859   -839       C
ATOM   6358  O   VAL D 113      -0.682   3.407 -77.142  1.00 99.10           O
ANISOU 6358  O   VAL D 113    12635  12620  12398  -1091    943   -866       O
ATOM   6359  CB  VAL D 113       0.279   1.119 -75.078  1.00 80.99           C
ANISOU 6359  CB  VAL D 113    10080  10450  10242   -964    806   -966       C
ATOM   6360  CG1 VAL D 113       1.554   1.825 -75.506  1.00 80.75           C
ANISOU 6360  CG1 VAL D 113    10027  10453  10203  -1057    900  -1059       C
ATOM   6361  CG2 VAL D 113       0.414   0.550 -73.680  1.00 85.08           C
ANISOU 6361  CG2 VAL D 113    10517  10998  10813   -895    737   -983       C
ATOM   6362  N   CYS D 114      -2.134   1.690 -77.259  1.00 95.26           N
ANISOU 6362  N   CYS D 114    12128  12134  11931   -962    812   -786       N
ATOM   6363  CA  CYS D 114      -2.390   1.867 -78.684  1.00 91.93           C
ANISOU 6363  CA  CYS D 114    11794  11684  11450   -991    853   -767       C
ATOM   6364  C   CYS D 114      -3.334   3.022 -78.963  1.00 93.54           C
ANISOU 6364  C   CYS D 114    12124  11824  11595   -994    866   -693       C
ATOM   6365  O   CYS D 114      -3.268   3.619 -80.045  1.00 88.66           O
ANISOU 6365  O   CYS D 114    11600  11172  10914  -1038    925   -689       O
ATOM   6366  CB  CYS D 114      -2.958   0.580 -79.281  1.00 90.01           C
ANISOU 6366  CB  CYS D 114    11531  11455  11212   -934    796   -748       C
ATOM   6367  SG  CYS D 114      -1.765  -0.779 -79.383  1.00 88.86           S
ANISOU 6367  SG  CYS D 114    11268  11378  11115   -932    792   -840       S
ATOM   6368  N   TYR D 115      -4.221   3.339 -78.019  1.00 99.36           N
ANISOU 6368  N   TYR D 115    12868  12541  12344   -944    812   -639       N
ATOM   6369  CA  TYR D 115      -5.058   4.527 -78.120  1.00107.82           C
ANISOU 6369  CA  TYR D 115    14054  13554  13359   -939    820   -577       C
ATOM   6370  C   TYR D 115      -4.365   5.770 -77.575  1.00107.38           C
ANISOU 6370  C   TYR D 115    14029  13475  13295  -1003    886   -599       C
ATOM   6371  O   TYR D 115      -4.794   6.888 -77.884  1.00111.85           O
ANISOU 6371  O   TYR D 115    14714  13984  13801  -1017    917   -560       O
ATOM   6372  CB  TYR D 115      -6.386   4.311 -77.379  1.00115.60           C
ANISOU 6372  CB  TYR D 115    15030  14533  14359   -856    732   -515       C
ATOM   6373  CG  TYR D 115      -7.397   3.474 -78.145  1.00121.53           C
ANISOU 6373  CG  TYR D 115    15796  15289  15089   -798    677   -482       C
ATOM   6374  CD1 TYR D 115      -8.767   3.634 -77.945  1.00123.07           C
ANISOU 6374  CD1 TYR D 115    16027  15470  15265   -733    615   -427       C
ATOM   6375  CD2 TYR D 115      -6.980   2.523 -79.065  1.00122.37           C
ANISOU 6375  CD2 TYR D 115    15877  15422  15198   -809    687   -514       C
ATOM   6376  CE1 TYR D 115      -9.685   2.869 -78.646  1.00121.86           C
ANISOU 6376  CE1 TYR D 115    15879  15330  15093   -684    568   -409       C
ATOM   6377  CE2 TYR D 115      -7.884   1.757 -79.766  1.00121.55           C
ANISOU 6377  CE2 TYR D 115    15784  15325  15075   -760    639   -490       C
ATOM   6378  CZ  TYR D 115      -9.232   1.930 -79.561  1.00120.35           C
ANISOU 6378  CZ  TYR D 115    15663  15160  14903   -699    581   -440       C
ATOM   6379  OH  TYR D 115     -10.113   1.150 -80.278  1.00116.53           O
ANISOU 6379  OH  TYR D 115    15182  14692  14402   -655    536   -427       O
ATOM   6380  N   ASN D 116      -3.308   5.593 -76.782  1.00102.13           N
ANISOU 6380  N   ASN D 116    13263  12854  12686  -1039    907   -665       N
ATOM   6381  CA  ASN D 116      -2.556   6.719 -76.236  1.00104.06           C
ANISOU 6381  CA  ASN D 116    13523  13087  12929  -1109    975   -701       C
ATOM   6382  C   ASN D 116      -1.873   7.481 -77.365  1.00108.46           C
ANISOU 6382  C   ASN D 116    14173  13612  13424  -1202   1081   -735       C
ATOM   6383  O   ASN D 116      -1.184   6.864 -78.190  1.00109.73           O
ANISOU 6383  O   ASN D 116    14304  13805  13583  -1238   1116   -788       O
ATOM   6384  CB  ASN D 116      -1.508   6.209 -75.243  1.00106.14           C
ANISOU 6384  CB  ASN D 116    13645  13419  13266  -1121    971   -780       C
ATOM   6385  CG  ASN D 116      -1.179   7.214 -74.144  1.00109.85           C
ANISOU 6385  CG  ASN D 116    14105  13882  13752  -1153    996   -796       C
ATOM   6386  OD1 ASN D 116      -1.651   8.348 -74.152  1.00116.52           O
ANISOU 6386  OD1 ASN D 116    15054  14667  14553  -1176   1026   -750       O
ATOM   6387  ND2 ASN D 116      -0.340   6.798 -73.202  1.00106.09           N
ANISOU 6387  ND2 ASN D 116    13506  13467  13337  -1151    982   -866       N
ATOM   6388  N   PRO D 117      -2.030   8.807 -77.444  1.00107.17           N
ANISOU 6388  N   PRO D 117    14131  13385  13204  -1246   1138   -708       N
ATOM   6389  CA  PRO D 117      -1.219   9.579 -78.399  1.00110.43           C
ANISOU 6389  CA  PRO D 117    14638  13764  13556  -1352   1255   -752       C
ATOM   6390  C   PRO D 117       0.269   9.460 -78.128  1.00114.38           C
ANISOU 6390  C   PRO D 117    15030  14328  14102  -1444   1327   -868       C
ATOM   6391  O   PRO D 117       1.071   9.764 -79.017  1.00116.34           O
ANISOU 6391  O   PRO D 117    15324  14570  14311  -1539   1425   -925       O
ATOM   6392  CB  PRO D 117      -1.708  11.021 -78.205  1.00105.92           C
ANISOU 6392  CB  PRO D 117    14213  13109  12923  -1371   1291   -701       C
ATOM   6393  CG  PRO D 117      -3.073  10.883 -77.595  1.00100.78           C
ANISOU 6393  CG  PRO D 117    13568  12443  12282  -1253   1180   -612       C
ATOM   6394  CD  PRO D 117      -3.003   9.654 -76.737  1.00101.98           C
ANISOU 6394  CD  PRO D 117    13544  12677  12528  -1199   1099   -635       C
ATOM   6395  N   ASP D 118       0.660   9.005 -76.942  1.00116.97           N
ANISOU 6395  N   ASP D 118    15214  14721  14509  -1417   1281   -909       N
ATOM   6396  CA  ASP D 118       2.059   8.809 -76.607  1.00122.26           C
ANISOU 6396  CA  ASP D 118    15762  15467  15226  -1487   1334  -1031       C
ATOM   6397  C   ASP D 118       2.570   7.422 -76.971  1.00125.27           C
ANISOU 6397  C   ASP D 118    16024  15923  15648  -1455   1297  -1088       C
ATOM   6398  O   ASP D 118       3.633   7.026 -76.477  1.00128.53           O
ANISOU 6398  O   ASP D 118    16307  16415  16112  -1477   1309  -1191       O
ATOM   6399  CB  ASP D 118       2.289   9.073 -75.124  1.00125.75           C
ANISOU 6399  CB  ASP D 118    16113  15942  15725  -1469   1302  -1056       C
ATOM   6400  CG  ASP D 118       2.252  10.547 -74.786  1.00127.51           C
ANISOU 6400  CG  ASP D 118    16435  16104  15909  -1537   1371  -1041       C
ATOM   6401  OD1 ASP D 118       3.340  11.148 -74.709  1.00127.66           O
ANISOU 6401  OD1 ASP D 118    16427  16148  15928  -1640   1465  -1136       O
ATOM   6402  OD2 ASP D 118       1.146  11.099 -74.582  1.00126.99           O
ANISOU 6402  OD2 ASP D 118    16470  15968  15812  -1487   1332   -940       O
ATOM   6403  N   PHE D 119       1.833   6.680 -77.811  1.00120.08           N
ANISOU 6403  N   PHE D 119    15409  15246  14969  -1398   1251  -1028       N
ATOM   6404  CA  PHE D 119       2.311   5.392 -78.303  1.00115.56           C
ANISOU 6404  CA  PHE D 119    14742  14736  14427  -1373   1224  -1081       C
ATOM   6405  C   PHE D 119       3.683   5.532 -78.937  1.00121.32           C
ANISOU 6405  C   PHE D 119    15433  15514  15150  -1479   1327  -1200       C
ATOM   6406  O   PHE D 119       4.481   4.586 -78.921  1.00125.20           O
ANISOU 6406  O   PHE D 119    15802  16084  15685  -1466   1311  -1285       O
ATOM   6407  CB  PHE D 119       1.314   4.821 -79.307  1.00110.00           C
ANISOU 6407  CB  PHE D 119    14117  13993  13684  -1319   1182   -999       C
ATOM   6408  CG  PHE D 119       1.703   3.475 -79.853  1.00104.80           C
ANISOU 6408  CG  PHE D 119    13374  13392  13054  -1289   1152  -1045       C
ATOM   6409  CD1 PHE D 119       1.569   2.336 -79.077  1.00101.25           C
ANISOU 6409  CD1 PHE D 119    12817  12988  12665  -1200   1058  -1048       C
ATOM   6410  CD2 PHE D 119       2.183   3.342 -81.146  1.00101.02           C
ANISOU 6410  CD2 PHE D 119    12931  12915  12535  -1347   1218  -1083       C
ATOM   6411  CE1 PHE D 119       1.915   1.094 -79.570  1.00 98.27           C
ANISOU 6411  CE1 PHE D 119    12372  12657  12309  -1168   1029  -1089       C
ATOM   6412  CE2 PHE D 119       2.531   2.105 -81.643  1.00 98.55           C
ANISOU 6412  CE2 PHE D 119    12542  12656  12248  -1316   1188  -1126       C
ATOM   6413  CZ  PHE D 119       2.398   0.978 -80.851  1.00 98.03           C
ANISOU 6413  CZ  PHE D 119    12370  12634  12243  -1225   1092  -1129       C
ATOM   6414  N   GLU D 120       3.951   6.701 -79.519  1.00120.63           N
ANISOU 6414  N   GLU D 120    15455  15377  15003  -1583   1435  -1211       N
ATOM   6415  CA  GLU D 120       5.277   7.178 -79.880  1.00118.76           C
ANISOU 6415  CA  GLU D 120    15189  15179  14755  -1710   1554  -1334       C
ATOM   6416  C   GLU D 120       6.344   6.724 -78.874  1.00106.55           C
ANISOU 6416  C   GLU D 120    13458  13738  13286  -1709   1538  -1454       C
ATOM   6417  O   GLU D 120       7.044   5.734 -79.111  1.00 94.21           O
ANISOU 6417  O   GLU D 120    11782  12255  11759  -1692   1521  -1536       O
ATOM   6418  CB  GLU D 120       5.227   8.715 -80.018  1.00128.77           C
ANISOU 6418  CB  GLU D 120    16604  16365  15957  -1809   1656  -1314       C
ATOM   6419  CG  GLU D 120       4.739   9.486 -78.777  1.00135.36           C
ANISOU 6419  CG  GLU D 120    17452  17169  16810  -1778   1621  -1264       C
ATOM   6420  CD  GLU D 120       4.023  10.796 -79.065  1.00139.51           C
ANISOU 6420  CD  GLU D 120    18172  17580  17254  -1815   1673  -1180       C
ATOM   6421  OE1 GLU D 120       4.354  11.468 -80.053  1.00139.68           O
ANISOU 6421  OE1 GLU D 120    18319  17551  17204  -1914   1781  -1199       O
ATOM   6422  OE2 GLU D 120       3.189  11.215 -78.234  1.00140.13           O
ANISOU 6422  OE2 GLU D 120    18284  17619  17340  -1749   1610  -1101       O
ATOM   6423  N   LYS D 121       6.469   7.435 -77.748  1.00105.48           N
ANISOU 6423  N   LYS D 121    13295  13607  13177  -1719   1538  -1467       N
ATOM   6424  CA  LYS D 121       7.488   7.256 -76.719  1.00105.98           C
ANISOU 6424  CA  LYS D 121    13197  13766  13303  -1723   1531  -1586       C
ATOM   6425  C   LYS D 121       7.207   6.092 -75.779  1.00103.98           C
ANISOU 6425  C   LYS D 121    12829  13564  13115  -1582   1394  -1568       C
ATOM   6426  O   LYS D 121       8.072   5.754 -74.963  1.00100.24           O
ANISOU 6426  O   LYS D 121    12216  13177  12693  -1563   1371  -1672       O
ATOM   6427  CB  LYS D 121       7.601   8.530 -75.867  1.00105.48           C
ANISOU 6427  CB  LYS D 121    13166  13676  13236  -1785   1582  -1594       C
ATOM   6428  CG  LYS D 121       7.384   9.841 -76.623  1.00106.95           C
ANISOU 6428  CG  LYS D 121    13528  13767  13343  -1900   1698  -1555       C
ATOM   6429  CD  LYS D 121       6.523  10.837 -75.805  1.00107.90           C
ANISOU 6429  CD  LYS D 121    13744  13807  13447  -1878   1677  -1458       C
ATOM   6430  CE  LYS D 121       5.974  11.973 -76.673  1.00107.19           C
ANISOU 6430  CE  LYS D 121    13864  13599  13263  -1951   1764  -1384       C
ATOM   6431  NZ  LYS D 121       5.722  13.241 -75.935  1.00105.12           N
ANISOU 6431  NZ  LYS D 121    13687  13276  12979  -1989   1800  -1352       N
ATOM   6432  N   LEU D 122       6.016   5.500 -75.837  1.00105.69           N
ANISOU 6432  N   LEU D 122    13103  13727  13328  -1482   1303  -1444       N
ATOM   6433  CA  LEU D 122       5.623   4.465 -74.890  1.00 99.06           C
ANISOU 6433  CA  LEU D 122    12180  12917  12541  -1354   1179  -1416       C
ATOM   6434  C   LEU D 122       5.845   3.058 -75.421  1.00 92.94           C
ANISOU 6434  C   LEU D 122    11339  12190  11784  -1292   1128  -1447       C
ATOM   6435  O   LEU D 122       6.088   2.147 -74.623  1.00 84.96           O
ANISOU 6435  O   LEU D 122    10230  11231  10819  -1204   1047  -1482       O
ATOM   6436  CB  LEU D 122       4.148   4.644 -74.508  1.00 96.15           C
ANISOU 6436  CB  LEU D 122    11909  12466  12159  -1285   1112  -1269       C
ATOM   6437  CG  LEU D 122       3.717   4.238 -73.103  1.00 94.41           C
ANISOU 6437  CG  LEU D 122    11629  12257  11986  -1188   1013  -1236       C
ATOM   6438  CD1 LEU D 122       4.877   4.394 -72.148  1.00 90.73           C
ANISOU 6438  CD1 LEU D 122    11045  11866  11562  -1203   1025  -1351       C
ATOM   6439  CD2 LEU D 122       2.554   5.120 -72.684  1.00 92.68           C
ANISOU 6439  CD2 LEU D 122    11513  11958  11743  -1177    999  -1124       C
ATOM   6440  N   LYS D 123       5.766   2.864 -76.744  1.00 97.57           N
ANISOU 6440  N   LYS D 123    11986  12756  12331  -1332   1172  -1436       N
ATOM   6441  CA  LYS D 123       6.042   1.557 -77.343  1.00 99.96           C
ANISOU 6441  CA  LYS D 123    12227  13103  12648  -1281   1131  -1473       C
ATOM   6442  C   LYS D 123       7.351   0.939 -76.862  1.00106.58           C
ANISOU 6442  C   LYS D 123    12914  14048  13533  -1266   1122  -1617       C
ATOM   6443  O   LYS D 123       7.351  -0.259 -76.533  1.00102.49           O
ANISOU 6443  O   LYS D 123    12331  13564  13046  -1164   1033  -1627       O
ATOM   6444  CB  LYS D 123       6.019   1.656 -78.876  1.00 97.05           C
ANISOU 6444  CB  LYS D 123    11941  12707  12227  -1352   1205  -1465       C
ATOM   6445  CG  LYS D 123       6.754   0.493 -79.557  1.00 95.15           C
ANISOU 6445  CG  LYS D 123    11617  12536  12002  -1334   1195  -1549       C
ATOM   6446  CD  LYS D 123       6.120   0.024 -80.866  1.00 93.42           C
ANISOU 6446  CD  LYS D 123    11483  12272  11741  -1332   1199  -1484       C
ATOM   6447  CE  LYS D 123       6.231   1.063 -81.981  1.00 97.71           C
ANISOU 6447  CE  LYS D 123    12138  12771  12219  -1451   1316  -1482       C
ATOM   6448  NZ  LYS D 123       5.585   0.588 -83.244  1.00 97.37           N
ANISOU 6448  NZ  LYS D 123    12180  12685  12130  -1439   1313  -1419       N
ATOM   6449  N   PRO D 124       8.480   1.667 -76.786  1.00112.96           N
ANISOU 6449  N   PRO D 124    13661  14913  14344  -1359   1207  -1738       N
ATOM   6450  CA  PRO D 124       9.683   1.054 -76.193  1.00108.69           C
ANISOU 6450  CA  PRO D 124    12963  14485  13849  -1325   1183  -1885       C
ATOM   6451  C   PRO D 124       9.480   0.567 -74.767  1.00101.43           C
ANISOU 6451  C   PRO D 124    11981  13583  12973  -1204   1072  -1869       C
ATOM   6452  O   PRO D 124      10.036  -0.471 -74.390  1.00100.63           O
ANISOU 6452  O   PRO D 124    11782  13552  12903  -1114   1002  -1943       O
ATOM   6453  CB  PRO D 124      10.720   2.184 -76.273  1.00105.88           C
ANISOU 6453  CB  PRO D 124    12571  14175  13484  -1461   1304  -2004       C
ATOM   6454  CG  PRO D 124      10.296   2.991 -77.444  1.00104.18           C
ANISOU 6454  CG  PRO D 124    12495  13879  13208  -1572   1404  -1941       C
ATOM   6455  CD  PRO D 124       8.793   2.979 -77.392  1.00110.06           C
ANISOU 6455  CD  PRO D 124    13367  14517  13933  -1502   1337  -1762       C
ATOM   6456  N   GLY D 125       8.693   1.276 -73.961  1.00 96.92           N
ANISOU 6456  N   GLY D 125    11473  12951  12403  -1194   1052  -1776       N
ATOM   6457  CA  GLY D 125       8.496   0.841 -72.588  1.00 96.00           C
ANISOU 6457  CA  GLY D 125    11305  12847  12323  -1084    952  -1761       C
ATOM   6458  C   GLY D 125       7.622  -0.395 -72.488  1.00 93.17           C
ANISOU 6458  C   GLY D 125    10979  12450  11970   -963    846  -1670       C
ATOM   6459  O   GLY D 125       7.994  -1.385 -71.848  1.00 87.85           O
ANISOU 6459  O   GLY D 125    10233  11823  11322   -863    766  -1719       O
ATOM   6460  N   PHE D 126       6.446  -0.351 -73.124  1.00 93.40           N
ANISOU 6460  N   PHE D 126    11123  12395  11971   -972    846  -1541       N
ATOM   6461  CA  PHE D 126       5.509  -1.471 -73.077  1.00 87.86           C
ANISOU 6461  CA  PHE D 126    10461  11652  11271   -873    756  -1453       C
ATOM   6462  C   PHE D 126       6.142  -2.763 -73.579  1.00 87.80           C
ANISOU 6462  C   PHE D 126    10391  11696  11271   -819    723  -1525       C
ATOM   6463  O   PHE D 126       5.797  -3.852 -73.101  1.00 88.73           O
ANISOU 6463  O   PHE D 126    10505  11805  11402   -717    636  -1498       O
ATOM   6464  CB  PHE D 126       4.261  -1.137 -73.899  1.00 86.04           C
ANISOU 6464  CB  PHE D 126    10352  11336  11003   -905    775  -1328       C
ATOM   6465  CG  PHE D 126       3.212  -2.210 -73.873  1.00 83.92           C
ANISOU 6465  CG  PHE D 126    10125  11026  10735   -818    693  -1240       C
ATOM   6466  CD1 PHE D 126       2.490  -2.464 -72.715  1.00 81.72           C
ANISOU 6466  CD1 PHE D 126     9857  10718  10474   -745    620  -1180       C
ATOM   6467  CD2 PHE D 126       2.950  -2.972 -75.007  1.00 86.90           C
ANISOU 6467  CD2 PHE D 126    10533  11394  11092   -814    693  -1223       C
ATOM   6468  CE1 PHE D 126       1.523  -3.457 -72.681  1.00 85.10           C
ANISOU 6468  CE1 PHE D 126    10327  11108  10901   -676    554  -1108       C
ATOM   6469  CE2 PHE D 126       1.981  -3.968 -74.988  1.00 87.31           C
ANISOU 6469  CE2 PHE D 126    10621  11408  11143   -742    623  -1150       C
ATOM   6470  CZ  PHE D 126       1.265  -4.212 -73.821  1.00 88.26           C
ANISOU 6470  CZ  PHE D 126    10753  11499  11281   -676    556  -1094       C
ATOM   6471  N   LEU D 127       7.076  -2.665 -74.527  1.00 84.57           N
ANISOU 6471  N   LEU D 127     9939  11340  10853   -887    792  -1620       N
ATOM   6472  CA  LEU D 127       7.674  -3.866 -75.101  1.00 76.84           C
ANISOU 6472  CA  LEU D 127     8903  10412   9879   -838    764  -1691       C
ATOM   6473  C   LEU D 127       8.518  -4.630 -74.085  1.00 77.81           C
ANISOU 6473  C   LEU D 127     8920  10607  10035   -738    690  -1791       C
ATOM   6474  O   LEU D 127       8.601  -5.860 -74.157  1.00 76.42           O
ANISOU 6474  O   LEU D 127     8727  10445   9863   -647    624  -1808       O
ATOM   6475  CB  LEU D 127       8.495  -3.498 -76.339  1.00 72.39           C
ANISOU 6475  CB  LEU D 127     8316   9892   9296   -943    863  -1777       C
ATOM   6476  CG  LEU D 127       7.693  -3.489 -77.647  1.00 63.47           C
ANISOU 6476  CG  LEU D 127     7292   8696   8127   -993    902  -1686       C
ATOM   6477  CD1 LEU D 127       8.171  -2.451 -78.650  1.00 54.45           C
ANISOU 6477  CD1 LEU D 127     6181   7557   6951  -1130   1025  -1728       C
ATOM   6478  CD2 LEU D 127       7.732  -4.880 -78.259  1.00 68.51           C
ANISOU 6478  CD2 LEU D 127     7910   9353   8767   -922    850  -1700       C
ATOM   6479  N   LYS D 128       9.134  -3.930 -73.126  1.00 83.49           N
ANISOU 6479  N   LYS D 128     9576  11372  10774   -747    699  -1859       N
ATOM   6480  CA  LYS D 128       9.895  -4.598 -72.074  1.00 80.61           C
ANISOU 6480  CA  LYS D 128     9118  11076  10436   -639    621  -1954       C
ATOM   6481  C   LYS D 128       9.004  -5.366 -71.105  1.00 82.27           C
ANISOU 6481  C   LYS D 128     9387  11224  10650   -518    515  -1855       C
ATOM   6482  O   LYS D 128       9.481  -6.297 -70.445  1.00 75.11           O
ANISOU 6482  O   LYS D 128     8434  10354   9751   -403    435  -1916       O
ATOM   6483  CB  LYS D 128      10.721  -3.578 -71.287  1.00 81.04           C
ANISOU 6483  CB  LYS D 128     9089  11194  10508   -685    659  -2052       C
ATOM   6484  CG  LYS D 128      11.070  -2.321 -72.054  1.00 80.17           C
ANISOU 6484  CG  LYS D 128     8980  11095  10386   -844    787  -2088       C
ATOM   6485  N   GLU D 129       7.727  -4.996 -70.991  1.00 85.77           N
ANISOU 6485  N   GLU D 129     9934  11572  11082   -539    514  -1710       N
ATOM   6486  CA  GLU D 129       6.857  -5.637 -70.015  1.00 84.71           C
ANISOU 6486  CA  GLU D 129     9858  11378  10950   -440    426  -1621       C
ATOM   6487  C   GLU D 129       6.250  -6.938 -70.523  1.00 81.33           C
ANISOU 6487  C   GLU D 129     9489  10906  10506   -375    375  -1565       C
ATOM   6488  O   GLU D 129       5.900  -7.800 -69.710  1.00 88.14           O
ANISOU 6488  O   GLU D 129    10384  11738  11368   -275    296  -1535       O
ATOM   6489  CB  GLU D 129       5.747  -4.676 -69.606  1.00 88.89           C
ANISOU 6489  CB  GLU D 129    10465  11834  11476   -489    445  -1502       C
ATOM   6490  CG  GLU D 129       6.247  -3.315 -69.179  1.00 96.82           C
ANISOU 6490  CG  GLU D 129    11428  12870  12491   -564    505  -1546       C
ATOM   6491  CD  GLU D 129       5.221  -2.226 -69.408  1.00104.68           C
ANISOU 6491  CD  GLU D 129    12511  13792  13470   -646    555  -1435       C
ATOM   6492  OE1 GLU D 129       5.617  -1.040 -69.476  1.00108.82           O
ANISOU 6492  OE1 GLU D 129    13022  14332  13993   -735    628  -1468       O
ATOM   6493  OE2 GLU D 129       4.019  -2.555 -69.523  1.00104.93           O
ANISOU 6493  OE2 GLU D 129    12627  13753  13489   -621    523  -1321       O
ATOM   6494  N   ILE D 130       6.131  -7.098 -71.836  1.00 73.79           N
ANISOU 6494  N   ILE D 130     8555   9945   9536   -431    421  -1554       N
ATOM   6495  CA  ILE D 130       5.523  -8.272 -72.462  1.00 68.90           C
ANISOU 6495  CA  ILE D 130     7994   9284   8902   -385    383  -1502       C
ATOM   6496  C   ILE D 130       6.098  -9.599 -71.962  1.00 76.26           C
ANISOU 6496  C   ILE D 130     8898  10243   9836   -263    303  -1567       C
ATOM   6497  O   ILE D 130       5.318 -10.536 -71.732  1.00 80.16           O
ANISOU 6497  O   ILE D 130     9465  10675  10318   -198    247  -1496       O
ATOM   6498  CB  ILE D 130       5.634  -8.174 -73.992  1.00 58.52           C
ANISOU 6498  CB  ILE D 130     6683   7981   7571   -466    451  -1513       C
ATOM   6499  CG1 ILE D 130       4.898  -6.930 -74.493  1.00 54.43           C
ANISOU 6499  CG1 ILE D 130     6225   7419   7038   -571    522  -1433       C
ATOM   6500  CG2 ILE D 130       5.092  -9.426 -74.651  1.00 53.22           C
ANISOU 6500  CG2 ILE D 130     6062   7274   6884   -416    412  -1470       C
ATOM   6501  CD1 ILE D 130       4.488  -6.998 -75.928  1.00 56.11           C
ANISOU 6501  CD1 ILE D 130     6488   7608   7223   -630    569  -1396       C
ATOM   6502  N   PRO D 131       7.422  -9.752 -71.788  1.00 76.73           N
ANISOU 6502  N   PRO D 131     8858  10389   9906   -226    294  -1703       N
ATOM   6503  CA  PRO D 131       7.943 -11.081 -71.402  1.00 78.58           C
ANISOU 6503  CA  PRO D 131     9079  10644  10133    -95    210  -1766       C
ATOM   6504  C   PRO D 131       7.376 -11.627 -70.104  1.00 79.89           C
ANISOU 6504  C   PRO D 131     9312  10751  10292      8    128  -1707       C
ATOM   6505  O   PRO D 131       6.990 -12.800 -70.050  1.00 82.95           O
ANISOU 6505  O   PRO D 131     9769  11089  10658     88     72  -1673       O
ATOM   6506  CB  PRO D 131       9.454 -10.838 -71.299  1.00 78.84           C
ANISOU 6506  CB  PRO D 131     8982  10795  10180    -81    219  -1932       C
ATOM   6507  CG  PRO D 131       9.713  -9.758 -72.257  1.00 77.62           C
ANISOU 6507  CG  PRO D 131     8783  10676  10034   -223    325  -1957       C
ATOM   6508  CD  PRO D 131       8.527  -8.842 -72.149  1.00 76.08           C
ANISOU 6508  CD  PRO D 131     8674  10396   9837   -303    363  -1818       C
ATOM   6509  N   GLU D 132       7.325 -10.815 -69.048  1.00 79.85           N
ANISOU 6509  N   GLU D 132     9294  10746  10299      5    123  -1697       N
ATOM   6510  CA  GLU D 132       6.829 -11.308 -67.768  1.00 86.32           C
ANISOU 6510  CA  GLU D 132    10181  11509  11107    102     48  -1646       C
ATOM   6511  C   GLU D 132       5.318 -11.513 -67.766  1.00 76.38           C
ANISOU 6511  C   GLU D 132     9042  10143   9835     74     48  -1496       C
ATOM   6512  O   GLU D 132       4.814 -12.282 -66.942  1.00 62.34           O
ANISOU 6512  O   GLU D 132     7342   8304   8038    154    -12  -1450       O
ATOM   6513  CB  GLU D 132       7.252 -10.361 -66.645  1.00 96.76           C
ANISOU 6513  CB  GLU D 132    11448  12869  12446    106     42  -1685       C
ATOM   6514  CG  GLU D 132       8.750 -10.064 -66.648  1.00110.12           C
ANISOU 6514  CG  GLU D 132    13007  14681  14153    123     49  -1848       C
ATOM   6515  CD  GLU D 132       9.387 -10.199 -65.271  1.00123.33           C
ANISOU 6515  CD  GLU D 132    14646  16391  15824    237    -26  -1921       C
ATOM   6516  OE1 GLU D 132       9.900  -9.182 -64.743  1.00127.10           O
ANISOU 6516  OE1 GLU D 132    15045  16926  16323    199      0  -1980       O
ATOM   6517  OE2 GLU D 132       9.373 -11.327 -64.717  1.00125.54           O
ANISOU 6517  OE2 GLU D 132    14983  16640  16077    368   -110  -1922       O
ATOM   6518  N   LYS D 133       4.592 -10.855 -68.672  1.00 81.18           N
ANISOU 6518  N   LYS D 133     9670  10727  10449    -37    115  -1425       N
ATOM   6519  CA  LYS D 133       3.171 -11.145 -68.850  1.00 77.61           C
ANISOU 6519  CA  LYS D 133     9320  10186   9983    -62    116  -1300       C
ATOM   6520  C   LYS D 133       2.970 -12.551 -69.399  1.00 76.62           C
ANISOU 6520  C   LYS D 133     9248  10028   9835     -9     82  -1293       C
ATOM   6521  O   LYS D 133       2.285 -13.385 -68.792  1.00 74.81           O
ANISOU 6521  O   LYS D 133     9104   9734   9588     48     37  -1240       O
ATOM   6522  CB  LYS D 133       2.545 -10.111 -69.781  1.00 66.32           C
ANISOU 6522  CB  LYS D 133     7894   8748   8558   -181    190  -1241       C
ATOM   6523  CG  LYS D 133       2.158  -8.846 -69.073  1.00 64.28           C
ANISOU 6523  CG  LYS D 133     7634   8478   8311   -229    214  -1199       C
ATOM   6524  CD  LYS D 133       1.637  -7.826 -70.031  1.00 66.25           C
ANISOU 6524  CD  LYS D 133     7897   8718   8556   -334    285  -1150       C
ATOM   6525  CE  LYS D 133       1.044  -6.648 -69.303  1.00 64.93           C
ANISOU 6525  CE  LYS D 133     7749   8525   8395   -374    302  -1093       C
ATOM   6526  NZ  LYS D 133       1.399  -5.398 -70.017  1.00 76.41           N
ANISOU 6526  NZ  LYS D 133     9181  10005   9848   -468    378  -1113       N
ATOM   6527  N   MET D 134       3.570 -12.830 -70.553  1.00 72.68           N
ANISOU 6527  N   MET D 134     8707   9573   9335    -30    109  -1350       N
ATOM   6528  CA  MET D 134       3.521 -14.177 -71.105  1.00 70.96           C
ANISOU 6528  CA  MET D 134     8534   9332   9097     25     77  -1357       C
ATOM   6529  C   MET D 134       3.963 -15.206 -70.075  1.00 81.63           C
ANISOU 6529  C   MET D 134     9917  10667  10430    154     -2  -1399       C
ATOM   6530  O   MET D 134       3.334 -16.262 -69.928  1.00 88.45           O
ANISOU 6530  O   MET D 134    10876  11462  11269    203    -37  -1351       O
ATOM   6531  CB  MET D 134       4.382 -14.237 -72.367  1.00 57.59           C
ANISOU 6531  CB  MET D 134     6769   7705   7406     -8    115  -1437       C
ATOM   6532  CG  MET D 134       4.018 -13.144 -73.365  1.00 54.02           C
ANISOU 6532  CG  MET D 134     6298   7264   6963   -134    197  -1399       C
ATOM   6533  SD  MET D 134       2.277 -13.255 -73.874  1.00 67.88           S
ANISOU 6533  SD  MET D 134     8162   8928   8702   -187    212  -1256       S
ATOM   6534  CE  MET D 134       1.503 -11.852 -73.061  1.00 64.30           C
ANISOU 6534  CE  MET D 134     7725   8447   8260   -244    235  -1180       C
ATOM   6535  N   LYS D 135       5.023 -14.896 -69.325  1.00 84.92           N
ANISOU 6535  N   LYS D 135    10263  11147  10857    212    -30  -1490       N
ATOM   6536  CA  LYS D 135       5.493 -15.813 -68.295  1.0