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***  RKSBW  ***

elNémo ID: 200930151107113531

Job options:

ID        	=	 200930151107113531
JOBID     	=	 RKSBW
USERID    	=	 CThomp
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER RKSBW

REMARK Date 2020-09-28 Time 22:40:15 BST +0100 (1601329215.03 s)
REMARK PHENIX refinement
REMARK 
REMARK ****************** INPUT FILES AND LABELS ******************************
REMARK Reflections:
REMARK   file name      : /Users/changjiang/RimK/Refine_3/RimK_refine_3.mtz
REMARK   labels         : ['F-obs,SIGF-obs']
REMARK R-free flags:
REMARK   file name      : /Users/changjiang/RimK/Refine_3/RimK_refine_3.mtz
REMARK   label          : R-free-flags
REMARK   test_flag_value: 0
REMARK Model file name(s): 
REMARK   /Users/changjiang/RimK/Refine_6/RimK_refine_6-coot-1.pdb
REMARK 
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS *******************
REMARK Start: r_work = 0.1991 r_free = 0.2126 bonds = 0.009 angles = 1.170
REMARK Final: r_work = 0.1960 r_free = 0.2123 bonds = 0.008 angles = 0.915
REMARK ************************************************************************
REMARK 
REMARK Rigid body refinement target: auto
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_rbr: rigid body refinement                                            
REMARK 1_gbr: group B-factor refinement                                        
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    : 0.6069 0.6978 0.009  1.17  31.9 128.3  58.0  75      0.000
REMARK       1_bss: 0.1991 0.2126 0.009  1.17  31.9 128.2  57.9  75      0.000
REMARK 1_settarget: 0.1991 0.2126 0.009  1.17  31.9 128.2  57.9  75      0.000
REMARK       1_nqh: 0.1991 0.2126 0.009  1.17  31.9 128.2  57.9  75      0.000
REMARK       1_rbr: 0.1991 0.2144 0.009  1.17  31.9 128.2  57.9  75      0.014
REMARK    1_weight: 0.1991 0.2144 0.009  1.17  31.9 128.2  57.9  75      0.014
REMARK    1_xyzrec: 0.1985 0.2225 0.008  0.97  31.9 128.2  57.9  75      0.083
REMARK       1_adp: 0.1972 0.2243 0.008  0.97  33.2 147.5  59.5  75      0.083
REMARK       2_bss: 0.1973 0.2250 0.008  0.97  33.2 147.5  59.4  75      0.083
REMARK 2_settarget: 0.1973 0.2250 0.008  0.97  33.2 147.5  59.4  75      0.083
REMARK 2_updatecdl: 0.1973 0.2250 0.008  0.98  33.2 147.5  59.4  75      0.083
REMARK       2_nqh: 0.1976 0.2251 0.008  0.98  33.2 147.5  59.4  75      0.085
REMARK   2_realsrl: 0.2020 0.2221 0.008  1.13  33.2 147.5  59.4  75      0.132
REMARK    2_weight: 0.2020 0.2221 0.008  1.13  33.2 147.5  59.4  75      0.132
REMARK    2_xyzrec: 0.1976 0.2135 0.009  0.95  33.2 147.5  59.4  75      0.095
REMARK  2_realsrl2: 0.1975 0.2139 0.009  0.95  33.2 147.5  59.4  75      0.096
REMARK       2_adp: 0.1977 0.2142 0.009  0.95  30.9 133.0  59.2  75      0.096
REMARK       3_bss: 0.1973 0.2148 0.009  0.95  29.8 131.9  58.1  75      0.096
REMARK 3_settarget: 0.1973 0.2148 0.009  0.95  29.8 131.9  58.1  75      0.096
REMARK 3_updatecdl: 0.1973 0.2148 0.009  0.96  29.8 131.9  58.1  75      0.096
REMARK     3_setrh: 0.1973 0.2148 0.009  0.96  29.8 131.9  58.1  75      0.096
REMARK       3_nqh: 0.1973 0.2148 0.009  0.96  29.8 131.9  58.1  75      0.096
REMARK   3_realsrl: 0.1995 0.2175 0.009  1.01  29.8 131.9  58.1  75      0.095
REMARK    3_weight: 0.1995 0.2175 0.009  1.01  29.8 131.9  58.1  75      0.095
REMARK    3_xyzrec: 0.1965 0.2158 0.008  0.92  29.8 131.9  58.1  75      0.088
REMARK  3_realsrl2: 0.1965 0.2158 0.008  0.92  29.8 131.9  58.1  75      0.088
REMARK       3_adp: 0.1963 0.2149 0.008  0.92  30.7 128.2  57.1  75      0.088
REMARK         end: 0.1960 0.2123 0.008  0.92  31.1 128.6  57.5  75      0.088
REMARK ------------------------------------------------------------------------
REMARK MODEL CONTENT.
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM
REMARK        C                     1318         1318.00
REMARK        S                       15           15.00
REMARK        O                      457          457.00
REMARK        N                      374          374.00
REMARK    TOTAL                     2164         2164.00
REMARK -----------------------------------------------------------------------
REMARK r_free_flags.md5.hexdigest 14b46078f54aac197ce609a94effe456
REMARK 
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.14_3260: ???)
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty,
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini,
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart
REMARK   3
REMARK   3  X-RAY DATA.
REMARK   3  
REMARK   3  REFINEMENT TARGET : ML
REMARK   3  
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.030   
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.260  
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.96 
REMARK   3   NUMBER OF REFLECTIONS             : 27688     
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 27688     
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1968
REMARK   3   R VALUE            (WORKING SET) : 0.1960
REMARK   3   FREE R VALUE                     : 0.2123
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.76  
REMARK   3   FREE R VALUE TEST SET COUNT      : 1318      
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 44.2701 -  4.2218    1.00     3098   154  0.1698 0.1717   0.931  0.931
REMARK   3     2  4.2218 -  3.3513    1.00     2970   149  0.1831 0.1882   0.922  0.894
REMARK   3     3  3.3513 -  2.9278    1.00     2906   157  0.2114 0.2605   0.887  0.790
REMARK   3     4  2.9278 -  2.6601    1.00     2934   141  0.2251 0.2439   0.862  0.856
REMARK   3     5  2.6601 -  2.4695    1.00     2897   142  0.2171 0.2551   0.872  0.827
REMARK   3     6  2.4695 -  2.3239    1.00     2927   114  0.2192 0.2620   0.866  0.797
REMARK   3     7  2.3239 -  2.2075    1.00     2876   157  0.2262 0.2486   0.856  0.846
REMARK   3     8  2.2075 -  2.1114    1.00     2876   142  0.2631 0.3118   0.791  0.629
REMARK   3     9  2.1114 -  2.0301    1.00     2886   162  0.2981 0.3330   0.711  0.653
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)     : 0.26    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.14   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  
REMARK   3  
REMARK   3  GEOMETRY RESTRAINTS LIBRARY: CDL v1.2
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND      :  0.008   0.088   2118
REMARK   3    ANGLE     :  0.915   8.252   2857
REMARK   3    CHIRALITY :  0.055   0.229    336
REMARK   3    PLANARITY :  0.006   0.033    369
REMARK   3    DIHEDRAL  :  3.397  43.512   1304
REMARK   3    MIN NONBONDED DISTANCE : 2.126 
REMARK   3  REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3    ALL-ATOM CLASHSCORE : 3.05
REMARK   3    RAMACHANDRAN PLOT:
REMARK   3      OUTLIERS : 0.00  %
REMARK   3      ALLOWED  : 2.94  %
REMARK   3      FAVORED  : 97.06 %
REMARK   3    ROTAMER OUTLIERS : 0.00 %
REMARK   3    CBETA DEVIATIONS : 0
REMARK   3    PEPTIDE PLANE:
REMARK   3      CIS-PROLINE     : 0.0
REMARK   3      CIS-GENERAL     : 0.0
REMARK   3      TWISTED PROLINE : 0.0
REMARK   3      TWISTED GENERAL : 0.383141762452
REMARK   3  
REMARK   3                  min    max   mean    iso aniso
REMARK   3     Overall:   31.09 128.58  57.52   5.30  2164  2164
REMARK   3     Protein:   31.09 128.58  57.59   5.30  2089  2089
REMARK   3     Water:     35.48  72.39  55.75    N/A    75    75
REMARK   3     Chain  A:  31.09 128.58  57.59    N/A  2089  2089
REMARK   3     Chain  S:  35.48  72.39  55.75    N/A    75    75
REMARK   3     Histogram:
REMARK   3         Values      Number of atoms
REMARK   3      31.09 - 40.84       205
REMARK   3      40.84 - 50.59       669
REMARK   3      50.59 - 60.34       560
REMARK   3      60.34 - 70.09       348
REMARK   3      70.09 - 79.84       142
REMARK   3      79.84 - 89.59       112
REMARK   3      89.59 - 99.34        78
REMARK   3      99.34 - 109.09       36
REMARK   3     109.09 - 118.83        8
REMARK   3     118.83 - 128.58        6
REMARK   3  
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):  -1.0902  29.5189  18.6121
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.3041 T22:   0.2807                       
REMARK   3      T33:   0.3776 T12:   0.0268                       
REMARK   3      T13:  -0.0342 T23:   0.0185                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   1.2351 L22:   0.8733                       
REMARK   3      L33:   2.5687 L12:  -0.0222                       
REMARK   3      L13:  -0.0285 L23:   0.4012                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0072 S12:   0.1116 S13:  -0.1179         
REMARK   3      S21:   0.0184 S22:  -0.0496 S23:  -0.2461         
REMARK   3      S31:  -0.0056 S32:   0.1382 S33:   0.0356         
REMARK   3
CRYST1   79.030   79.030  116.050  90.00  90.00 120.00 P 31 2 1
SCALE1      0.012653  0.007305  0.000000        0.00000
SCALE2      0.000000  0.014611  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008617        0.00000
ATOM      1  N   MET A   1      -2.504  42.467  40.974  1.00 41.82           N
ANISOU    1  N   MET A   1     6222   4836   4833   -151  -1321   -213       N
ATOM      2  CA  MET A   1      -3.467  41.413  40.684  1.00 45.13           C
ANISOU    2  CA  MET A   1     6585   5318   5244    -68  -1256   -156       C
ATOM      3  C   MET A   1      -2.869  40.091  41.085  1.00 44.10           C
ANISOU    3  C   MET A   1     6355   5274   5126    -96  -1289    -69       C
ATOM      4  O   MET A   1      -1.642  39.967  41.189  1.00 41.85           O
ANISOU    4  O   MET A   1     6018   4996   4887   -163  -1354    -42       O
ATOM      5  CB  MET A   1      -3.818  41.391  39.185  1.00 46.71           C
ANISOU    5  CB  MET A   1     6763   5449   5534    -27  -1184   -126       C
ATOM      6  CG  MET A   1      -4.330  42.717  38.639  1.00 56.73           C
ANISOU    6  CG  MET A   1     8143   6614   6796     14  -1155   -197       C
ATOM      7  SD  MET A   1      -4.489  42.623  36.827  1.00 59.41           S
ANISOU    7  SD  MET A   1     8449   6884   7238     49  -1085   -144       S
ATOM      8  CE  MET A   1      -5.357  41.104  36.716  1.00 44.03           C
ANISOU    8  CE  MET A   1     6390   5059   5281    110  -1034    -87       C
ATOM      9  N   LYS A   2      -3.722  39.100  41.308  1.00 39.29           N
ANISOU    9  N   LYS A   2     5720   4735   4474    -45  -1246    -24       N
ATOM     10  CA  LYS A   2      -3.281  37.725  41.495  1.00 42.78           C
ANISOU   10  CA  LYS A   2     6087   5231   4936    -56  -1264     73       C
ATOM     11  C   LYS A   2      -3.467  36.985  40.171  1.00 44.79           C
ANISOU   11  C   LYS A   2     6280   5443   5294    -30  -1198    128       C
ATOM     12  O   LYS A   2      -4.583  36.945  39.626  1.00 41.70           O
ANISOU   12  O   LYS A   2     5901   5049   4892     14  -1121    111       O
ATOM     13  CB  LYS A   2      -4.060  37.052  42.623  1.00 43.95           C
ANISOU   13  CB  LYS A   2     6264   5472   4963    -38  -1255     94       C
ATOM     14  CG  LYS A   2      -3.434  35.731  43.092  1.00 46.24           C
ANISOU   14  CG  LYS A   2     6512   5804   5254    -51  -1296    198       C
ATOM     15  CD  LYS A   2      -4.288  35.090  44.200  1.00 51.99           C
ANISOU   15  CD  LYS A   2     7286   6618   5848    -46  -1276    227       C
ATOM     16  CE  LYS A   2      -3.733  33.734  44.638  1.00 55.71           C
ANISOU   16  CE  LYS A   2     7743   7110   6313    -50  -1314    344       C
ATOM     17  NZ  LYS A   2      -4.649  33.078  45.613  1.00 56.47           N
ANISOU   17  NZ  LYS A   2     7898   7281   6276    -59  -1277    383       N
ATOM     18  N   ILE A   3      -2.377  36.441  39.627  1.00 40.04           N
ANISOU   18  N   ILE A   3     5607   4819   4788    -52  -1228    185       N
ATOM     19  CA  ILE A   3      -2.383  35.918  38.260  1.00 40.07           C
ANISOU   19  CA  ILE A   3     5555   4775   4895    -31  -1168    221       C
ATOM     20  C   ILE A   3      -1.815  34.509  38.279  1.00 41.38           C
ANISOU   20  C   ILE A   3     5659   4961   5101    -18  -1186    307       C
ATOM     21  O   ILE A   3      -0.704  34.296  38.772  1.00 40.28           O
ANISOU   21  O   ILE A   3     5481   4848   4976    -33  -1261    336       O
ATOM     22  CB  ILE A   3      -1.571  36.796  37.295  1.00 41.93           C
ANISOU   22  CB  ILE A   3     5767   4950   5216    -64  -1173    193       C
ATOM     23  CG1 ILE A   3      -2.074  38.241  37.324  1.00 39.21           C
ANISOU   23  CG1 ILE A   3     5512   4558   4826    -73  -1162    111       C
ATOM     24  CG2 ILE A   3      -1.589  36.190  35.868  1.00 38.81           C
ANISOU   24  CG2 ILE A   3     5312   4520   4915    -38  -1108    229       C
ATOM     25  CD1 ILE A   3      -1.059  39.244  36.811  1.00 37.08           C
ANISOU   25  CD1 ILE A   3     5247   4227   4616   -142  -1188     83       C
ATOM     26  N   ALA A   4      -2.579  33.548  37.764  1.00 38.06           N
ANISOU   26  N   ALA A   4     5234   4529   4697     13  -1120    343       N
ATOM     27  CA  ALA A   4      -2.081  32.189  37.590  1.00 37.58           C
ANISOU   27  CA  ALA A   4     5136   4456   4688     34  -1126    421       C
ATOM     28  C   ALA A   4      -1.349  32.072  36.261  1.00 38.94           C
ANISOU   28  C   ALA A   4     5234   4583   4978     49  -1106    424       C
ATOM     29  O   ALA A   4      -1.775  32.636  35.255  1.00 39.71           O
ANISOU   29  O   ALA A   4     5324   4653   5110     46  -1049    382       O
ATOM     30  CB  ALA A   4      -3.237  31.186  37.622  1.00 36.09           C
ANISOU   30  CB  ALA A   4     4987   4266   4460     41  -1060    452       C
ATOM     31  N   VAL A   5      -0.236  31.348  36.252  1.00 41.90           N
ANISOU   31  N   VAL A   5     5553   4960   5409     73  -1154    474       N
ATOM     32  CA  VAL A   5       0.457  31.049  35.004  1.00 45.13           C
ANISOU   32  CA  VAL A   5     5884   5340   5924     96  -1126    478       C
ATOM     33  C   VAL A   5       0.349  29.542  34.799  1.00 45.61           C
ANISOU   33  C   VAL A   5     5952   5362   6015    152  -1104    536       C
ATOM     34  O   VAL A   5       0.864  28.764  35.612  1.00 42.38           O
ANISOU   34  O   VAL A   5     5553   4961   5587    189  -1163    593       O
ATOM     35  CB  VAL A   5       1.919  31.517  35.016  1.00 44.57           C
ANISOU   35  CB  VAL A   5     5724   5311   5899     83  -1194    471       C
ATOM     36  CG1 VAL A   5       2.527  31.314  33.632  1.00 42.29           C
ANISOU   36  CG1 VAL A   5     5351   5007   5712    101  -1148    465       C
ATOM     37  CG2 VAL A   5       2.028  33.003  35.430  1.00 42.43           C
ANISOU   37  CG2 VAL A   5     5472   5063   5586      7  -1225    412       C
ATOM     38  N   LEU A   6      -0.379  29.119  33.763  1.00 43.31           N
ANISOU   38  N   LEU A   6     5670   5026   5761    158  -1021    522       N
ATOM     39  CA  LEU A   6      -0.567  27.686  33.516  1.00 43.20           C
ANISOU   39  CA  LEU A   6     5682   4955   5775    198   -992    566       C
ATOM     40  C   LEU A   6       0.638  27.169  32.752  1.00 48.40           C
ANISOU   40  C   LEU A   6     6263   5599   6529    261  -1008    578       C
ATOM     41  O   LEU A   6       0.775  27.433  31.550  1.00 50.58           O
ANISOU   41  O   LEU A   6     6483   5871   6865    262   -958    536       O
ATOM     42  CB  LEU A   6      -1.837  27.422  32.718  1.00 38.85           C
ANISOU   42  CB  LEU A   6     5166   4375   5219    170   -900    533       C
ATOM     43  CG  LEU A   6      -3.158  27.972  33.247  1.00 46.93           C
ANISOU   43  CG  LEU A   6     6243   5438   6150    117   -868    504       C
ATOM     44  CD1 LEU A   6      -4.287  27.437  32.412  1.00 42.78           C
ANISOU   44  CD1 LEU A   6     5730   4898   5626     94   -784    475       C
ATOM     45  CD2 LEU A   6      -3.368  27.613  34.719  1.00 45.01           C
ANISOU   45  CD2 LEU A   6     6068   5213   5821     98   -909    554       C
ATOM     46  N   SER A   7       1.510  26.439  33.432  1.00 47.34           N
ANISOU   46  N   SER A   7     6123   5463   6401    322  -1076    633       N
ATOM     47  CA  SER A   7       2.730  25.976  32.794  1.00 50.89           C
ANISOU   47  CA  SER A   7     6482   5919   6935    399  -1098    638       C
ATOM     48  C   SER A   7       3.202  24.725  33.496  1.00 47.45           C
ANISOU   48  C   SER A   7     6091   5442   6495    492  -1154    710       C
ATOM     49  O   SER A   7       3.150  24.631  34.728  1.00 48.12           O
ANISOU   49  O   SER A   7     6235   5542   6506    492  -1217    761       O
ATOM     50  CB  SER A   7       3.824  27.051  32.832  1.00 58.56           C
ANISOU   50  CB  SER A   7     7336   6989   7923    379  -1151    607       C
ATOM     51  OG  SER A   7       5.073  26.552  32.391  1.00 67.63           O
ANISOU   51  OG  SER A   7     8380   8175   9141    460  -1180    613       O
ATOM     52  N   ARG A   8       3.714  23.782  32.718  1.00 44.37           N
ANISOU   52  N   ARG A   8     5677   5002   6179    581  -1134    715       N
ATOM     53  CA  ARG A   8       4.195  22.550  33.324  1.00 51.57           C
ANISOU   53  CA  ARG A   8     6649   5855   7089    692  -1189    786       C
ATOM     54  C   ARG A   8       5.642  22.651  33.784  1.00 57.68           C
ANISOU   54  C   ARG A   8     7311   6728   7878    788  -1290    805       C
ATOM     55  O   ARG A   8       6.178  21.675  34.321  1.00 57.60           O
ANISOU   55  O   ARG A   8     7340   6682   7862    908  -1352    868       O
ATOM     56  CB  ARG A   8       3.998  21.384  32.348  1.00 63.29           C
ANISOU   56  CB  ARG A   8     8186   7222   8640    755  -1122    778       C
ATOM     57  CG  ARG A   8       2.524  20.978  32.246  1.00 75.09           C
ANISOU   57  CG  ARG A   8     9817   8615  10098    660  -1041    779       C
ATOM     58  CD  ARG A   8       2.280  19.673  31.486  1.00 74.67           C
ANISOU   58  CD  ARG A   8     9850   8424  10098    710   -984    775       C
ATOM     59  NE  ARG A   8       2.920  18.512  32.097  1.00 79.14           N
ANISOU   59  NE  ARG A   8    10503   8897  10669    833  -1044    851       N
ATOM     60  CZ  ARG A   8       3.477  17.526  31.400  1.00 81.36           C
ANISOU   60  CZ  ARG A   8    10805   9087  11021    951  -1032    840       C
ATOM     61  NH1 ARG A   8       3.455  17.563  30.073  1.00 82.63           N
ANISOU   61  NH1 ARG A   8    10898   9248  11248    948   -959    752       N
ATOM     62  NH2 ARG A   8       4.043  16.504  32.025  1.00 79.92           N
ANISOU   62  NH2 ARG A   8    10718   8812  10836   1078  -1093    915       N
ATOM     63  N   ASN A   9       6.270  23.821  33.644  1.00 59.48           N
ANISOU   63  N   ASN A   9     7403   7082   8116    736  -1313    754       N
ATOM     64  CA  ASN A   9       7.622  23.982  34.166  1.00 60.35           C
ANISOU   64  CA  ASN A   9     7389   7314   8228    806  -1415    763       C
ATOM     65  C   ASN A   9       7.929  25.452  34.454  1.00 56.31           C
ANISOU   65  C   ASN A   9     6785   6925   7687    685  -1446    713       C
ATOM     66  O   ASN A   9       8.024  26.278  33.532  1.00 52.90           O
ANISOU   66  O   ASN A   9     6274   6527   7299    606  -1386    649       O
ATOM     67  CB  ASN A   9       8.628  23.376  33.184  1.00 66.46           C
ANISOU   67  CB  ASN A   9     8045   8114   9092    925  -1402    738       C
ATOM     68  CG  ASN A   9      10.065  23.526  33.643  1.00 67.99           C
ANISOU   68  CG  ASN A   9     8080   8464   9290   1004  -1505    738       C
ATOM     69  OD1 ASN A   9      10.334  23.895  34.781  1.00 67.56           O
ANISOU   69  OD1 ASN A   9     8019   8485   9167    986  -1600    767       O
ATOM     70  ND2 ASN A   9      10.996  23.228  32.750  1.00 71.28           N
ANISOU   70  ND2 ASN A   9     8359   8944   9781   1093  -1487    698       N
ATOM     71  N   PRO A  10       8.099  25.810  35.732  1.00 53.62           N
ANISOU   71  N   PRO A  10     6461   6649   7265    663  -1539    740       N
ATOM     72  CA  PRO A  10       8.368  27.216  36.082  1.00 56.17           C
ANISOU   72  CA  PRO A  10     6716   7074   7553    538  -1572    684       C
ATOM     73  C   PRO A  10       9.733  27.716  35.634  1.00 62.50           C
ANISOU   73  C   PRO A  10     7325   8012   8409    532  -1608    635       C
ATOM     74  O   PRO A  10       9.945  28.935  35.619  1.00 57.98           O
ANISOU   74  O   PRO A  10     6699   7504   7826    403  -1611    577       O
ATOM     75  CB  PRO A  10       8.258  27.223  37.611  1.00 56.02           C
ANISOU   75  CB  PRO A  10     6768   7092   7425    539  -1669    728       C
ATOM     76  CG  PRO A  10       8.496  25.784  38.019  1.00 56.98           C
ANISOU   76  CG  PRO A  10     6939   7174   7538    696  -1716    816       C
ATOM     77  CD  PRO A  10       7.970  24.939  36.916  1.00 55.39           C
ANISOU   77  CD  PRO A  10     6790   6842   7414    746  -1614    825       C
ATOM     78  N   ARG A  11      10.659  26.826  35.273  1.00 60.94           N
ANISOU   78  N   ARG A  11     7027   7862   8266    666  -1634    653       N
ATOM     79  CA  ARG A  11      12.005  27.225  34.896  1.00 56.60           C
ANISOU   79  CA  ARG A  11     6272   7473   7760    666  -1670    605       C
ATOM     80  C   ARG A  11      12.149  27.530  33.413  1.00 55.67           C
ANISOU   80  C   ARG A  11     6072   7352   7727    619  -1559    549       C
ATOM     81  O   ARG A  11      13.186  28.074  33.014  1.00 64.74           O
ANISOU   81  O   ARG A  11     7047   8643   8907    575  -1568    499       O
ATOM     82  CB  ARG A  11      13.008  26.137  35.301  1.00 63.47           C
ANISOU   82  CB  ARG A  11     7054   8425   8636    855  -1763    646       C
ATOM     83  CG  ARG A  11      12.816  25.637  36.729  1.00 78.33           C
ANISOU   83  CG  ARG A  11     9043  10294  10425    927  -1871    721       C
ATOM     84  CD  ARG A  11      14.065  24.979  37.299  1.00 94.56           C
ANISOU   84  CD  ARG A  11    10971  12492  12466   1093  -1995    750       C
ATOM     85  NE  ARG A  11      14.907  25.920  38.043  1.00105.91           N
ANISOU   85  NE  ARG A  11    12265  14127  13849   1009  -2097    706       N
ATOM     86  CZ  ARG A  11      14.919  26.032  39.372  1.00106.70           C
ANISOU   86  CZ  ARG A  11    12415  14283  13844   1009  -2210    743       C
ATOM     87  NH1 ARG A  11      14.128  25.266  40.112  1.00103.90           N
ANISOU   87  NH1 ARG A  11    12255  13800  13423   1088  -2230    833       N
ATOM     88  NH2 ARG A  11      15.719  26.912  39.963  1.00107.40           N
ANISOU   88  NH2 ARG A  11    12362  14561  13886    920  -2301    687       N
ATOM     89  N   LEU A  12      11.149  27.206  32.592  1.00 51.15           N
ANISOU   89  N   LEU A  12     5614   6637   7185    620  -1455    553       N
ATOM     90  CA  LEU A  12      11.226  27.542  31.177  1.00 58.18           C
ANISOU   90  CA  LEU A  12     6438   7528   8139    572  -1348    502       C
ATOM     91  C   LEU A  12      11.283  29.051  31.006  1.00 57.28           C
ANISOU   91  C   LEU A  12     6287   7466   8009    388  -1326    454       C
ATOM     92  O   LEU A  12      10.637  29.793  31.750  1.00 57.49           O
ANISOU   92  O   LEU A  12     6415   7451   7977    294  -1352    457       O
ATOM     93  CB  LEU A  12      10.031  26.977  30.404  1.00 62.45           C
ANISOU   93  CB  LEU A  12     7119   7911   8699    595  -1249    512       C
ATOM     94  CG  LEU A  12       9.696  25.488  30.486  1.00 70.79           C
ANISOU   94  CG  LEU A  12     8265   8864   9769    748  -1251    557       C
ATOM     95  CD1 LEU A  12       8.205  25.270  30.197  1.00 71.56           C
ANISOU   95  CD1 LEU A  12     8532   8810   9848    701  -1173    565       C
ATOM     96  CD2 LEU A  12      10.571  24.671  29.531  1.00 66.72           C
ANISOU   96  CD2 LEU A  12     7639   8386   9327    876  -1221    532       C
ATOM     97  N   TYR A  13      12.061  29.493  30.011  1.00 52.78           N
ANISOU   97  N   TYR A  13     5581   6986   7487    338  -1273    410       N
ATOM     98  CA  TYR A  13      12.336  30.914  29.833  1.00 49.66           C
ANISOU   98  CA  TYR A  13     5145   6645   7079    155  -1254    368       C
ATOM     99  C   TYR A  13      11.056  31.734  29.880  1.00 47.60           C
ANISOU   99  C   TYR A  13     5066   6243   6777     54  -1211    369       C
ATOM    100  O   TYR A  13      10.938  32.676  30.674  1.00 48.46           O
ANISOU  100  O   TYR A  13     5225   6351   6836    -53  -1259    355       O
ATOM    101  CB  TYR A  13      13.066  31.160  28.508  1.00 53.04           C
ANISOU  101  CB  TYR A  13     5439   7154   7560    111  -1168    330       C
ATOM    102  CG  TYR A  13      13.361  32.633  28.254  1.00 54.14           C
ANISOU  102  CG  TYR A  13     5554   7332   7683    -95  -1138    294       C
ATOM    103  CD1 TYR A  13      14.589  33.183  28.607  1.00 55.10           C
ANISOU  103  CD1 TYR A  13     5512   7619   7803   -189  -1192    260       C
ATOM    104  CD2 TYR A  13      12.397  33.482  27.688  1.00 52.06           C
ANISOU  104  CD2 TYR A  13     5440   6938   7401   -197  -1061    295       C
ATOM    105  CE1 TYR A  13      14.871  34.534  28.394  1.00 55.26           C
ANISOU  105  CE1 TYR A  13     5529   7661   7808   -399  -1163    227       C
ATOM    106  CE2 TYR A  13      12.664  34.841  27.478  1.00 46.04           C
ANISOU  106  CE2 TYR A  13     4686   6185   6621   -384  -1035    269       C
ATOM    107  CZ  TYR A  13      13.906  35.356  27.830  1.00 54.67           C
ANISOU  107  CZ  TYR A  13     5627   7429   7717   -494  -1083    235       C
ATOM    108  OH  TYR A  13      14.191  36.691  27.615  1.00 55.01           O
ANISOU  108  OH  TYR A  13     5692   7468   7742   -699  -1054    208       O
ATOM    109  N   SER A  14      10.084  31.391  29.031  1.00 51.49           N
ANISOU  109  N   SER A  14     5657   6622   7284     93  -1122    380       N
ATOM    110  CA  SER A  14       8.897  32.231  28.897  1.00 49.58           C
ANISOU  110  CA  SER A  14     5567   6268   7003      9  -1074    374       C
ATOM    111  C   SER A  14       8.085  32.259  30.182  1.00 46.89           C
ANISOU  111  C   SER A  14     5349   5870   6598     18  -1138    392       C
ATOM    112  O   SER A  14       7.564  33.311  30.569  1.00 44.23           O
ANISOU  112  O   SER A  14     5100   5493   6214    -75  -1144    372       O
ATOM    113  CB  SER A  14       8.030  31.753  27.733  1.00 45.14           C
ANISOU  113  CB  SER A  14     5066   5622   6462     61   -974    377       C
ATOM    114  OG  SER A  14       8.750  31.852  26.519  1.00 49.76           O
ANISOU  114  OG  SER A  14     5547   6267   7094     42   -907    356       O
ATOM    115  N   THR A  15       7.953  31.115  30.849  1.00 44.76           N
ANISOU  115  N   THR A  15     5096   5591   6319    130  -1184    431       N
ATOM    116  CA  THR A  15       7.241  31.080  32.120  1.00 44.96           C
ANISOU  116  CA  THR A  15     5232   5579   6271    135  -1243    454       C
ATOM    117  C   THR A  15       7.975  31.898  33.177  1.00 52.26           C
ANISOU  117  C   THR A  15     6114   6591   7150     61  -1338    435       C
ATOM    118  O   THR A  15       7.362  32.697  33.897  1.00 54.50           O
ANISOU  118  O   THR A  15     6493   6846   7369     -9  -1358    416       O
ATOM    119  CB  THR A  15       7.074  29.632  32.583  1.00 48.57           C
ANISOU  119  CB  THR A  15     5722   6008   6726    264  -1271    510       C
ATOM    120  OG1 THR A  15       6.255  28.936  31.638  1.00 53.11           O
ANISOU  120  OG1 THR A  15     6355   6489   7334    309  -1181    516       O
ATOM    121  CG2 THR A  15       6.415  29.579  33.947  1.00 45.00           C
ANISOU  121  CG2 THR A  15     5379   5533   6184    260  -1331    542       C
ATOM    122  N   ARG A  16       9.289  31.699  33.290  1.00 45.97           N
ANISOU  122  N   ARG A  16     5169   5913   6383     81  -1399    432       N
ATOM    123  CA  ARG A  16      10.073  32.443  34.264  1.00 48.03           C
ANISOU  123  CA  ARG A  16     5370   6279   6599      2  -1495    404       C
ATOM    124  C   ARG A  16       9.944  33.945  34.029  1.00 47.55           C
ANISOU  124  C   ARG A  16     5347   6195   6526   -166  -1463    344       C
ATOM    125  O   ARG A  16       9.799  34.723  34.980  1.00 44.83           O
ANISOU  125  O   ARG A  16     5065   5854   6115   -245  -1520    316       O
ATOM    126  CB  ARG A  16      11.543  32.007  34.181  1.00 47.64           C
ANISOU  126  CB  ARG A  16     5125   6385   6592     49  -1553    400       C
ATOM    127  CG  ARG A  16      12.498  32.758  35.087  1.00 61.85           C
ANISOU  127  CG  ARG A  16     6827   8325   8347    -44  -1658    360       C
ATOM    128  CD  ARG A  16      13.933  32.201  34.984  1.00 64.87           C
ANISOU  128  CD  ARG A  16     6991   8888   8767     26  -1717    354       C
ATOM    129  NE  ARG A  16      14.483  32.352  33.636  1.00 64.64           N
ANISOU  129  NE  ARG A  16     6842   8900   8819    -12  -1625    323       N
ATOM    130  CZ  ARG A  16      14.980  33.486  33.148  1.00 71.20           C
ANISOU  130  CZ  ARG A  16     7601   9787   9663   -191  -1588    265       C
ATOM    131  NH1 ARG A  16      15.020  34.582  33.895  1.00 68.20           N
ANISOU  131  NH1 ARG A  16     7262   9422   9230   -350  -1640    225       N
ATOM    132  NH2 ARG A  16      15.449  33.521  31.909  1.00 73.52           N
ANISOU  132  NH2 ARG A  16     7791  10122  10020   -218  -1497    247       N
ATOM    133  N   ARG A  17      10.010  34.364  32.763  1.00 39.36           N
ANISOU  133  N   ARG A  17     4282   5127   5545   -221  -1370    325       N
ATOM    134  CA  ARG A  17      10.007  35.784  32.441  1.00 47.37           C
ANISOU  134  CA  ARG A  17     5341   6108   6551   -382  -1336    277       C
ATOM    135  C   ARG A  17       8.660  36.413  32.766  1.00 48.99           C
ANISOU  135  C   ARG A  17     5740   6175   6699   -400  -1311    269       C
ATOM    136  O   ARG A  17       8.597  37.546  33.260  1.00 44.85           O
ANISOU  136  O   ARG A  17     5290   5621   6132   -511  -1336    225       O
ATOM    137  CB  ARG A  17      10.355  35.977  30.962  1.00 46.24           C
ANISOU  137  CB  ARG A  17     5133   5964   6472   -423  -1236    272       C
ATOM    138  CG  ARG A  17      11.841  35.808  30.676  1.00 54.80           C
ANISOU  138  CG  ARG A  17     6010   7212   7601   -458  -1258    256       C
ATOM    139  CD  ARG A  17      12.631  37.057  31.100  1.00 58.46           C
ANISOU  139  CD  ARG A  17     6432   7739   8040   -648  -1300    204       C
ATOM    140  NE  ARG A  17      12.098  38.233  30.425  1.00 60.55           N
ANISOU  140  NE  ARG A  17     6831   7879   8298   -780  -1220    189       N
ATOM    141  CZ  ARG A  17      11.708  39.345  31.036  1.00 55.58           C
ANISOU  141  CZ  ARG A  17     6338   7161   7618   -894  -1246    156       C
ATOM    142  NH1 ARG A  17      11.804  39.450  32.352  1.00 57.83           N
ANISOU  142  NH1 ARG A  17     6637   7483   7854   -905  -1350    129       N
ATOM    143  NH2 ARG A  17      11.204  40.346  30.319  1.00 50.60           N
ANISOU  143  NH2 ARG A  17     5843   6401   6981   -988  -1169    151       N
ATOM    144  N   LEU A  18       7.569  35.687  32.498  1.00 46.03           N
ANISOU  144  N   LEU A  18     5448   5721   6320   -292  -1261    303       N
ATOM    145  CA  LEU A  18       6.245  36.215  32.816  1.00 45.39           C
ANISOU  145  CA  LEU A  18     5531   5536   6179   -293  -1236    291       C
ATOM    146  C   LEU A  18       6.065  36.347  34.325  1.00 45.10           C
ANISOU  146  C   LEU A  18     5550   5524   6063   -297  -1324    278       C
ATOM    147  O   LEU A  18       5.466  37.316  34.803  1.00 41.14           O
ANISOU  147  O   LEU A  18     5159   4968   5503   -350  -1329    236       O
ATOM    148  CB  LEU A  18       5.163  35.317  32.216  1.00 43.15           C
ANISOU  148  CB  LEU A  18     5297   5191   5905   -187  -1166    325       C
ATOM    149  CG  LEU A  18       5.033  35.422  30.702  1.00 41.28           C
ANISOU  149  CG  LEU A  18     5045   4915   5723   -189  -1072    325       C
ATOM    150  CD1 LEU A  18       4.211  34.251  30.143  1.00 46.14           C
ANISOU  150  CD1 LEU A  18     5676   5500   6356    -83  -1017    354       C
ATOM    151  CD2 LEU A  18       4.392  36.773  30.314  1.00 38.23           C
ANISOU  151  CD2 LEU A  18     4772   4450   5305   -259  -1030    291       C
ATOM    152  N   VAL A  19       6.583  35.387  35.092  1.00 37.92           N
ANISOU  152  N   VAL A  19     4570   4695   5142   -232  -1395    313       N
ATOM    153  CA  VAL A  19       6.556  35.510  36.551  1.00 39.21           C
ANISOU  153  CA  VAL A  19     4777   4903   5218   -240  -1487    305       C
ATOM    154  C   VAL A  19       7.368  36.720  37.005  1.00 47.18           C
ANISOU  154  C   VAL A  19     5759   5962   6204   -371  -1547    238       C
ATOM    155  O   VAL A  19       6.894  37.534  37.806  1.00 47.67           O
ANISOU  155  O   VAL A  19     5926   5994   6191   -425  -1575    192       O
ATOM    156  CB  VAL A  19       7.076  34.221  37.211  1.00 42.68           C
ANISOU  156  CB  VAL A  19     5147   5423   5647   -137  -1557    366       C
ATOM    157  CG1 VAL A  19       7.312  34.446  38.702  1.00 39.66           C
ANISOU  157  CG1 VAL A  19     4788   5116   5166   -157  -1665    356       C
ATOM    158  CG2 VAL A  19       6.098  33.094  36.983  1.00 46.26           C
ANISOU  158  CG2 VAL A  19     5671   5803   6103    -30  -1499    427       C
ATOM    159  N   GLU A  20       8.614  36.841  36.518  1.00 39.55           N
ANISOU  159  N   GLU A  20     4651   5079   5299   -429  -1567    226       N
ATOM    160  CA  GLU A  20       9.465  37.976  36.888  1.00 48.28           C
ANISOU  160  CA  GLU A  20     5719   6240   6386   -581  -1621    157       C
ATOM    161  C   GLU A  20       8.803  39.301  36.544  1.00 51.18           C
ANISOU  161  C   GLU A  20     6233   6475   6740   -689  -1561    103       C
ATOM    162  O   GLU A  20       8.757  40.220  37.367  1.00 45.14           O
ANISOU  162  O   GLU A  20     5549   5691   5911   -778  -1611     42       O
ATOM    163  CB  GLU A  20      10.810  37.890  36.174  1.00 52.50           C
ANISOU  163  CB  GLU A  20     6065   6887   6993   -636  -1624    152       C
ATOM    164  CG  GLU A  20      11.697  36.752  36.615  1.00 62.43           C
ANISOU  164  CG  GLU A  20     7162   8299   8259   -529  -1704    188       C
ATOM    165  CD  GLU A  20      12.946  36.642  35.754  1.00 68.14           C
ANISOU  165  CD  GLU A  20     7687   9146   9059   -566  -1689    177       C
ATOM    166  OE1 GLU A  20      13.083  37.433  34.787  1.00 64.11           O
ANISOU  166  OE1 GLU A  20     7172   8595   8592   -688  -1607    147       O
ATOM    167  OE2 GLU A  20      13.780  35.760  36.046  1.00 69.58           O
ANISOU  167  OE2 GLU A  20     7718   9470   9250   -468  -1757    199       O
ATOM    168  N   ALA A  21       8.324  39.434  35.309  1.00 45.45           N
ANISOU  168  N   ALA A  21     5547   5653   6068   -680  -1457    123       N
ATOM    169  CA  ALA A  21       7.700  40.685  34.893  1.00 44.87           C
ANISOU  169  CA  ALA A  21     5624   5444   5980   -762  -1400     82       C
ATOM    170  C   ALA A  21       6.482  41.007  35.755  1.00 45.68           C
ANISOU  170  C   ALA A  21     5891   5465   5999   -706  -1414     56       C
ATOM    171  O   ALA A  21       6.243  42.170  36.098  1.00 43.92           O
ANISOU  171  O   ALA A  21     5792   5162   5733   -785  -1423     -6       O
ATOM    172  CB  ALA A  21       7.301  40.603  33.418  1.00 43.57           C
ANISOU  172  CB  ALA A  21     5474   5205   5876   -730  -1290    120       C
ATOM    173  N   GLY A  22       5.693  39.988  36.104  1.00 41.15           N
ANISOU  173  N   GLY A  22     5324   4911   5399   -570  -1411     98       N
ATOM    174  CA  GLY A  22       4.529  40.229  36.943  1.00 41.36           C
ANISOU  174  CA  GLY A  22     5487   4889   5338   -517  -1417     72       C
ATOM    175  C   GLY A  22       4.911  40.693  38.336  1.00 46.54           C
ANISOU  175  C   GLY A  22     6169   5600   5913   -576  -1514     18       C
ATOM    176  O   GLY A  22       4.333  41.647  38.868  1.00 45.49           O
ANISOU  176  O   GLY A  22     6167   5402   5714   -605  -1520    -48       O
ATOM    177  N   VAL A  23       5.896  40.026  38.943  1.00 45.92           N
ANISOU  177  N   VAL A  23     5967   5647   5832   -585  -1595     41       N
ATOM    178  CA  VAL A  23       6.340  40.388  40.290  1.00 44.77           C
ANISOU  178  CA  VAL A  23     5831   5579   5600   -640  -1699    -10       C
ATOM    179  C   VAL A  23       6.912  41.806  40.304  1.00 47.06           C
ANISOU  179  C   VAL A  23     6164   5827   5888   -800  -1721   -102       C
ATOM    180  O   VAL A  23       6.661  42.585  41.234  1.00 44.04           O
ANISOU  180  O   VAL A  23     5887   5426   5421   -848  -1767   -177       O
ATOM    181  CB  VAL A  23       7.360  39.349  40.803  1.00 45.58           C
ANISOU  181  CB  VAL A  23     5777   5835   5704   -604  -1786     41       C
ATOM    182  CG1 VAL A  23       7.956  39.770  42.158  1.00 46.57           C
ANISOU  182  CG1 VAL A  23     5896   6066   5734   -670  -1906    -16       C
ATOM    183  CG2 VAL A  23       6.712  37.980  40.923  1.00 45.55           C
ANISOU  183  CG2 VAL A  23     5775   5844   5690   -451  -1766    132       C
ATOM    184  N   GLU A  24       7.682  42.169  39.272  1.00 47.41           N
ANISOU  184  N   GLU A  24     6137   5854   6021   -891  -1685   -102       N
ATOM    185  CA  GLU A  24       8.271  43.508  39.218  1.00 49.61           C
ANISOU  185  CA  GLU A  24     6466   6081   6301  -1068  -1699   -184       C
ATOM    186  C   GLU A  24       7.208  44.601  39.280  1.00 49.00           C
ANISOU  186  C   GLU A  24     6611   5831   6178  -1077  -1654   -242       C
ATOM    187  O   GLU A  24       7.500  45.732  39.696  1.00 48.08           O
ANISOU  187  O   GLU A  24     6586   5655   6025  -1209  -1687   -328       O
ATOM    188  CB  GLU A  24       9.065  43.694  37.924  1.00 66.25           C
ANISOU  188  CB  GLU A  24     8482   8182   8509  -1160  -1638   -160       C
ATOM    189  CG  GLU A  24      10.392  42.988  37.808  1.00 82.61           C
ANISOU  189  CG  GLU A  24    10324  10435  10628  -1197  -1685   -136       C
ATOM    190  CD  GLU A  24      11.026  43.211  36.435  1.00 90.12           C
ANISOU  190  CD  GLU A  24    11195  11376  11669  -1285  -1602   -114       C
ATOM    191  OE1 GLU A  24      10.462  44.000  35.641  1.00 87.41           O
ANISOU  191  OE1 GLU A  24    10993  10875  11344  -1332  -1517   -116       O
ATOM    192  OE2 GLU A  24      12.077  42.593  36.147  1.00 93.12           O
ANISOU  192  OE2 GLU A  24    11374  11912  12097  -1298  -1622    -93       O
ATOM    193  N   ARG A  25       5.996  44.304  38.806  1.00 48.28           N
ANISOU  193  N   ARG A  25     6605   5654   6086   -939  -1577   -201       N
ATOM    194  CA  ARG A  25       4.906  45.266  38.718  1.00 52.14           C
ANISOU  194  CA  ARG A  25     7292   5985   6534   -909  -1527   -250       C
ATOM    195  C   ARG A  25       3.926  45.151  39.879  1.00 52.05           C
ANISOU  195  C   ARG A  25     7367   5994   6417   -806  -1557   -288       C
ATOM    196  O   ARG A  25       2.864  45.781  39.839  1.00 49.97           O
ANISOU  196  O   ARG A  25     7252   5622   6111   -739  -1511   -327       O
ATOM    197  CB  ARG A  25       4.157  45.103  37.383  1.00 46.43           C
ANISOU  197  CB  ARG A  25     6600   5172   5868   -820  -1421   -189       C
ATOM    198  CG  ARG A  25       4.982  45.457  36.142  1.00 47.86           C
ANISOU  198  CG  ARG A  25     6737   5310   6139   -927  -1374   -158       C
ATOM    199  CD  ARG A  25       4.112  45.406  34.849  1.00 42.92           C
ANISOU  199  CD  ARG A  25     6169   4590   5549   -829  -1273   -104       C
ATOM    200  NE  ARG A  25       4.599  46.335  33.848  1.00 64.20           N
ANISOU  200  NE  ARG A  25     8926   7180   8286   -943  -1224   -100       N
ATOM    201  CZ  ARG A  25       4.005  47.474  33.525  1.00 66.75           C
ANISOU  201  CZ  ARG A  25     9444   7337   8582   -949  -1189   -129       C
ATOM    202  NH1 ARG A  25       2.867  47.825  34.106  1.00 66.88           N
ANISOU  202  NH1 ARG A  25     9598   7285   8529   -831  -1197   -173       N
ATOM    203  NH2 ARG A  25       4.551  48.256  32.609  1.00 78.08           N
ANISOU  203  NH2 ARG A  25    10938   8677  10053  -1068  -1144   -112       N
ATOM    204  N   GLY A  26       4.256  44.369  40.908  1.00 48.85           N
ANISOU  204  N   GLY A  26     6872   5730   5960   -787  -1631   -277       N
ATOM    205  CA  GLY A  26       3.446  44.286  42.107  1.00 44.91           C
ANISOU  205  CA  GLY A  26     6450   5269   5345   -712  -1663   -315       C
ATOM    206  C   GLY A  26       2.372  43.213  42.109  1.00 50.88           C
ANISOU  206  C   GLY A  26     7190   6065   6076   -561  -1610   -244       C
ATOM    207  O   GLY A  26       1.524  43.209  43.015  1.00 45.45           O
ANISOU  207  O   GLY A  26     6578   5406   5285   -498  -1615   -277       O
ATOM    208  N   HIS A  27       2.395  42.291  41.149  1.00 39.10           N
ANISOU  208  N   HIS A  27     5603   4584   4670   -510  -1559   -153       N
ATOM    209  CA  HIS A  27       1.398  41.233  41.061  1.00 41.72           C
ANISOU  209  CA  HIS A  27     5921   4947   4985   -388  -1505    -88       C
ATOM    210  C   HIS A  27       1.819  39.997  41.844  1.00 47.32           C
ANISOU  210  C   HIS A  27     6538   5778   5662   -358  -1563    -20       C
ATOM    211  O   HIS A  27       3.007  39.744  42.076  1.00 42.81           O
ANISOU  211  O   HIS A  27     5873   5275   5116   -409  -1637     -1       O
ATOM    212  CB  HIS A  27       1.154  40.866  39.594  1.00 41.87           C
ANISOU  212  CB  HIS A  27     5897   4904   5106   -348  -1419    -34       C
ATOM    213  CG  HIS A  27       0.717  42.032  38.767  1.00 44.49           C
ANISOU  213  CG  HIS A  27     6329   5113   5462   -362  -1363    -85       C
ATOM    214  ND1 HIS A  27      -0.497  42.660  38.957  1.00 44.15           N
ANISOU  214  ND1 HIS A  27     6408   5017   5350   -293  -1324   -139       N
ATOM    215  CD2 HIS A  27       1.345  42.715  37.780  1.00 44.21           C
ANISOU  215  CD2 HIS A  27     6296   4999   5502   -434  -1341    -89       C
ATOM    216  CE1 HIS A  27      -0.611  43.662  38.102  1.00 46.42           C
ANISOU  216  CE1 HIS A  27     6779   5186   5673   -307  -1285   -169       C
ATOM    217  NE2 HIS A  27       0.492  43.718  37.374  1.00 44.14           N
ANISOU  217  NE2 HIS A  27     6426   4875   5469   -401  -1292   -136       N
ATOM    218  N   GLU A  28       0.820  39.223  42.246  1.00 42.90           N
ANISOU  218  N   GLU A  28     6009   5251   5042   -274  -1528     19       N
ATOM    219  CA  GLU A  28       1.019  37.935  42.905  1.00 45.94           C
ANISOU  219  CA  GLU A  28     6337   5725   5391   -232  -1566    103       C
ATOM    220  C   GLU A  28       0.928  36.846  41.840  1.00 48.87           C
ANISOU  220  C   GLU A  28     6641   6066   5860   -178  -1505    188       C
ATOM    221  O   GLU A  28      -0.161  36.576  41.319  1.00 49.26           O
ANISOU  221  O   GLU A  28     6728   6075   5914   -133  -1418    199       O
ATOM    222  CB  GLU A  28      -0.031  37.726  43.995  1.00 47.91           C
ANISOU  222  CB  GLU A  28     6672   6026   5507   -192  -1555     96       C
ATOM    223  CG  GLU A  28       0.152  36.472  44.823  1.00 59.92           C
ANISOU  223  CG  GLU A  28     8167   7631   6967   -158  -1599    189       C
ATOM    224  CD  GLU A  28      -0.954  36.302  45.857  1.00 64.30           C
ANISOU  224  CD  GLU A  28     8810   8243   7380   -134  -1571    184       C
ATOM    225  OE1 GLU A  28      -1.707  37.275  46.099  1.00 66.35           O
ANISOU  225  OE1 GLU A  28     9139   8495   7577   -142  -1538     91       O
ATOM    226  OE2 GLU A  28      -1.057  35.201  46.436  1.00 67.38           O
ANISOU  226  OE2 GLU A  28     9204   8684   7714   -107  -1582    274       O
ATOM    227  N   MET A  29       2.065  36.217  41.527  1.00 45.77           N
ANISOU  227  N   MET A  29     6146   5704   5542   -179  -1550    241       N
ATOM    228  CA  MET A  29       2.172  35.274  40.422  1.00 50.48           C
ANISOU  228  CA  MET A  29     6676   6265   6241   -129  -1496    307       C
ATOM    229  C   MET A  29       2.226  33.854  40.962  1.00 52.37           C
ANISOU  229  C   MET A  29     6901   6543   6454    -58  -1524    398       C
ATOM    230  O   MET A  29       3.056  33.551  41.820  1.00 51.65           O
ANISOU  230  O   MET A  29     6776   6527   6323    -48  -1617    427       O
ATOM    231  CB  MET A  29       3.422  35.551  39.583  1.00 45.50           C
ANISOU  231  CB  MET A  29     5936   5640   5713   -168  -1518    297       C
ATOM    232  CG  MET A  29       3.548  36.978  39.033  1.00 40.40           C
ANISOU  232  CG  MET A  29     5313   4943   5093   -259  -1495    216       C
ATOM    233  SD  MET A  29       2.179  37.625  38.036  1.00 44.15           S
ANISOU  233  SD  MET A  29     5893   5300   5581   -241  -1378    183       S
ATOM    234  CE  MET A  29       2.361  36.689  36.496  1.00 41.69           C
ANISOU  234  CE  MET A  29     5490   4964   5386   -193  -1303    245       C
ATOM    235  N   VAL A  30       1.351  32.982  40.459  1.00 46.06           N
ANISOU  235  N   VAL A  30     6135   5693   5674    -10  -1445    445       N
ATOM    236  CA  VAL A  30       1.325  31.575  40.876  1.00 44.79           C
ANISOU  236  CA  VAL A  30     5989   5536   5492     52  -1458    538       C
ATOM    237  C   VAL A  30       1.425  30.703  39.627  1.00 47.92           C
ANISOU  237  C   VAL A  30     6339   5865   6002     98  -1398    576       C
ATOM    238  O   VAL A  30       0.574  30.794  38.735  1.00 46.22           O
ANISOU  238  O   VAL A  30     6142   5596   5822     86  -1308    548       O
ATOM    239  CB  VAL A  30       0.047  31.230  41.659  1.00 44.62           C
ANISOU  239  CB  VAL A  30     6074   5519   5360     46  -1416    559       C
ATOM    240  CG1 VAL A  30       0.133  29.829  42.226  1.00 50.90           C
ANISOU  240  CG1 VAL A  30     6909   6309   6122     95  -1439    665       C
ATOM    241  CG2 VAL A  30      -0.206  32.249  42.755  1.00 46.80           C
ANISOU  241  CG2 VAL A  30     6400   5862   5520      3  -1456    499       C
ATOM    242  N   VAL A  31       2.442  29.850  39.571  1.00 44.70           N
ANISOU  242  N   VAL A  31     5873   5468   5644    159  -1452    633       N
ATOM    243  CA  VAL A  31       2.602  28.907  38.469  1.00 50.24           C
ANISOU  243  CA  VAL A  31     6539   6104   6446    217  -1400    665       C
ATOM    244  C   VAL A  31       1.787  27.659  38.788  1.00 51.51           C
ANISOU  244  C   VAL A  31     6803   6200   6569    254  -1365    738       C
ATOM    245  O   VAL A  31       2.000  27.015  39.820  1.00 50.58           O
ANISOU  245  O   VAL A  31     6738   6098   6383    291  -1427    806       O
ATOM    246  CB  VAL A  31       4.080  28.554  38.250  1.00 51.72           C
ANISOU  246  CB  VAL A  31     6612   6336   6701    283  -1471    685       C
ATOM    247  CG1 VAL A  31       4.221  27.596  37.091  1.00 50.93           C
ANISOU  247  CG1 VAL A  31     6483   6168   6702    352  -1412    706       C
ATOM    248  CG2 VAL A  31       4.892  29.826  38.008  1.00 53.50           C
ANISOU  248  CG2 VAL A  31     6735   6637   6955    215  -1503    612       C
ATOM    249  N   ILE A  32       0.857  27.312  37.912  1.00 46.96           N
ANISOU  249  N   ILE A  32     6261   5553   6029    237  -1266    724       N
ATOM    250  CA  ILE A  32      -0.009  26.160  38.127  1.00 49.83           C
ANISOU  250  CA  ILE A  32     6727   5849   6358    240  -1218    782       C
ATOM    251  C   ILE A  32       0.386  25.087  37.122  1.00 56.14           C
ANISOU  251  C   ILE A  32     7511   6561   7258    305  -1188    808       C
ATOM    252  O   ILE A  32       0.240  25.276  35.907  1.00 51.87           O
ANISOU  252  O   ILE A  32     6917   5997   6793    297  -1125    752       O
ATOM    253  CB  ILE A  32      -1.495  26.520  37.987  1.00 46.46           C
ANISOU  253  CB  ILE A  32     6350   5424   5879    160  -1127    737       C
ATOM    254  CG1 ILE A  32      -1.903  27.569  39.025  1.00 43.10           C
ANISOU  254  CG1 ILE A  32     5947   5085   5346    112  -1155    704       C
ATOM    255  CG2 ILE A  32      -2.336  25.257  38.128  1.00 42.20           C
ANISOU  255  CG2 ILE A  32     5907   4818   5308    140  -1072    796       C
ATOM    256  CD1 ILE A  32      -1.649  27.128  40.470  1.00 44.55           C
ANISOU  256  CD1 ILE A  32     6198   5304   5427    121  -1226    776       C
ATOM    257  N   ASP A  33       0.880  23.955  37.623  1.00 54.99           N
ANISOU  257  N   ASP A  33     7422   6365   7107    377  -1234    891       N
ATOM    258  CA  ASP A  33       1.101  22.798  36.762  1.00 53.98           C
ANISOU  258  CA  ASP A  33     7314   6131   7063    445  -1199    914       C
ATOM    259  C   ASP A  33      -0.257  22.291  36.284  1.00 52.13           C
ANISOU  259  C   ASP A  33     7169   5818   6820    364  -1093    900       C
ATOM    260  O   ASP A  33      -1.051  21.737  37.054  1.00 57.78           O
ANISOU  260  O   ASP A  33     8001   6497   7455    312  -1074    953       O
ATOM    261  CB  ASP A  33       1.899  21.710  37.500  1.00 54.21           C
ANISOU  261  CB  ASP A  33     7408   6111   7079    555  -1278   1012       C
ATOM    262  CG  ASP A  33       2.390  20.581  36.569  1.00 68.47           C
ANISOU  262  CG  ASP A  33     9227   7806   8984    658  -1256   1024       C
ATOM    263  OD1 ASP A  33       1.804  20.363  35.481  1.00 68.61           O
ANISOU  263  OD1 ASP A  33     9248   7760   9062    619  -1164    970       O
ATOM    264  OD2 ASP A  33       3.354  19.879  36.964  1.00 78.19           O
ANISOU  264  OD2 ASP A  33    10469   9015  10224    787  -1335   1086       O
ATOM    265  N   THR A  34      -0.493  22.462  34.989  1.00 44.18           N
ANISOU  265  N   THR A  34     6102   4795   5890    349  -1023    828       N
ATOM    266  CA  THR A  34      -1.809  22.308  34.388  1.00 47.95           C
ANISOU  266  CA  THR A  34     6622   5242   6355    259   -924    785       C
ATOM    267  C   THR A  34      -2.426  20.941  34.655  1.00 58.15           C
ANISOU  267  C   THR A  34     8050   6421   7623    231   -887    842       C
ATOM    268  O   THR A  34      -3.595  20.841  35.055  1.00 52.07           O
ANISOU  268  O   THR A  34     7345   5662   6779    127   -835    844       O
ATOM    269  CB  THR A  34      -1.664  22.536  32.896  1.00 57.27           C
ANISOU  269  CB  THR A  34     7715   6419   7627    277   -873    709       C
ATOM    270  OG1 THR A  34      -0.817  23.685  32.699  1.00 58.37           O
ANISOU  270  OG1 THR A  34     7741   6644   7793    307   -916    674       O
ATOM    271  CG2 THR A  34      -3.016  22.741  32.287  1.00 50.57           C
ANISOU  271  CG2 THR A  34     6877   5587   6752    184   -785    648       C
ATOM    272  N   LEU A  35      -1.671  19.872  34.394  1.00 52.96           N
ANISOU  272  N   LEU A  35     7439   5654   7028    320   -909    885       N
ATOM    273  CA  LEU A  35      -2.203  18.530  34.566  1.00 47.94           C
ANISOU  273  CA  LEU A  35     6957   4880   6377    291   -872    939       C
ATOM    274  C   LEU A  35      -2.478  18.191  36.020  1.00 49.51           C
ANISOU  274  C   LEU A  35     7277   5067   6467    255   -908   1040       C
ATOM    275  O   LEU A  35      -3.137  17.176  36.289  1.00 54.28           O
ANISOU  275  O   LEU A  35     8028   5562   7036    191   -864   1091       O
ATOM    276  CB  LEU A  35      -1.241  17.492  33.977  1.00 51.91           C
ANISOU  276  CB  LEU A  35     7496   5256   6970    421   -894    959       C
ATOM    277  CG  LEU A  35      -0.904  17.658  32.493  1.00 59.52           C
ANISOU  277  CG  LEU A  35     8350   6227   8036    464   -852    862       C
ATOM    278  CD1 LEU A  35       0.075  16.563  32.033  1.00 59.28           C
ANISOU  278  CD1 LEU A  35     8364   6075   8086    611   -876    880       C
ATOM    279  CD2 LEU A  35      -2.171  17.640  31.651  1.00 63.22           C
ANISOU  279  CD2 LEU A  35     8831   6687   8502    334   -750    785       C
ATOM    280  N   ARG A  36      -1.983  18.989  36.961  1.00 45.12           N
ANISOU  280  N   ARG A  36     6673   4618   5853    287   -985   1069       N
ATOM    281  CA  ARG A  36      -2.207  18.706  38.374  1.00 46.13           C
ANISOU  281  CA  ARG A  36     6915   4750   5862    258  -1023   1166       C
ATOM    282  C   ARG A  36      -3.386  19.474  38.962  1.00 51.48           C
ANISOU  282  C   ARG A  36     7587   5538   6433    119   -972   1135       C
ATOM    283  O   ARG A  36      -3.771  19.213  40.112  1.00 53.56           O
ANISOU  283  O   ARG A  36     7952   5816   6583     70   -982   1210       O
ATOM    284  CB  ARG A  36      -0.942  19.008  39.175  1.00 50.97           C
ANISOU  284  CB  ARG A  36     7489   5423   6456    381  -1147   1219       C
ATOM    285  CG  ARG A  36       0.119  17.920  39.011  1.00 63.52           C
ANISOU  285  CG  ARG A  36     9131   6895   8109    533  -1206   1286       C
ATOM    286  CD  ARG A  36       1.500  18.460  39.313  1.00 67.42           C
ANISOU  286  CD  ARG A  36     9502   7492   8621    666  -1323   1289       C
ATOM    287  NE  ARG A  36       1.821  18.320  40.726  1.00 82.85           N
ANISOU  287  NE  ARG A  36    11533   9487  10461    705  -1416   1388       N
ATOM    288  CZ  ARG A  36       2.978  18.688  41.264  1.00 90.69           C
ANISOU  288  CZ  ARG A  36    12435  10583  11438    814  -1534   1406       C
ATOM    289  NH1 ARG A  36       3.920  19.227  40.497  1.00 91.06           N
ANISOU  289  NH1 ARG A  36    12309  10707  11583    884  -1565   1329       N
ATOM    290  NH2 ARG A  36       3.189  18.521  42.564  1.00 90.10           N
ANISOU  290  NH2 ARG A  36    12440  10550  11244    847  -1619   1498       N
ATOM    291  N   ALA A  37      -3.952  20.417  38.215  1.00 51.29           N
ANISOU  291  N   ALA A  37     7451   5600   6437     65   -919   1028       N
ATOM    292  CA  ALA A  37      -5.178  21.067  38.631  1.00 42.26           C
ANISOU  292  CA  ALA A  37     6299   4561   5198    -51   -859    985       C
ATOM    293  C   ALA A  37      -6.346  20.144  38.326  1.00 50.67           C
ANISOU  293  C   ALA A  37     7443   5566   6242   -166   -758    988       C
ATOM    294  O   ALA A  37      -6.363  19.457  37.297  1.00 49.89           O
ANISOU  294  O   ALA A  37     7355   5371   6232   -165   -717    964       O
ATOM    295  CB  ALA A  37      -5.343  22.405  37.914  1.00 39.48           C
ANISOU  295  CB  ALA A  37     5808   4313   4880    -47   -845    873       C
ATOM    296  N   TYR A  38      -7.292  20.077  39.255  1.00 51.95           N
ANISOU  296  N   TYR A  38     7667   5789   6282   -272   -718   1016       N
ATOM    297  CA  TYR A  38      -8.494  19.281  39.068  1.00 49.48           C
ANISOU  297  CA  TYR A  38     7418   5449   5932   -412   -615   1012       C
ATOM    298  C   TYR A  38      -9.695  20.138  39.450  1.00 53.85           C
ANISOU  298  C   TYR A  38     7898   6181   6382   -508   -555    943       C
ATOM    299  O   TYR A  38      -9.561  21.164  40.127  1.00 49.37           O
ANISOU  299  O   TYR A  38     7277   5728   5752   -465   -598    924       O
ATOM    300  CB  TYR A  38      -8.445  17.962  39.860  1.00 40.65           C
ANISOU  300  CB  TYR A  38     6484   4201   4761   -461   -612   1140       C
ATOM    301  CG  TYR A  38      -7.999  18.064  41.300  1.00 43.88           C
ANISOU  301  CG  TYR A  38     6969   4645   5059   -427   -681   1241       C
ATOM    302  CD1 TYR A  38      -8.916  17.914  42.327  1.00 50.29           C
ANISOU  302  CD1 TYR A  38     7854   5529   5724   -555   -629   1286       C
ATOM    303  CD2 TYR A  38      -6.660  18.263  41.640  1.00 49.25           C
ANISOU  303  CD2 TYR A  38     7644   5298   5770   -272   -798   1291       C
ATOM    304  CE1 TYR A  38      -8.539  17.989  43.656  1.00 59.02           C
ANISOU  304  CE1 TYR A  38     9037   6676   6713   -527   -691   1380       C
ATOM    305  CE2 TYR A  38      -6.261  18.341  42.989  1.00 59.58           C
ANISOU  305  CE2 TYR A  38     9023   6653   6963   -241   -869   1382       C
ATOM    306  CZ  TYR A  38      -7.219  18.210  43.991  1.00 60.13           C
ANISOU  306  CZ  TYR A  38     9175   6789   6883   -369   -814   1427       C
ATOM    307  OH  TYR A  38      -6.885  18.287  45.329  1.00 56.73           O
ANISOU  307  OH  TYR A  38     8818   6415   6321   -344   -879   1516       O
ATOM    308  N   MET A  39     -10.870  19.731  38.975  1.00 44.28           N
ANISOU  308  N   MET A  39     6676   4998   5150   -635   -457    894       N
ATOM    309  CA  MET A  39     -11.987  20.655  38.831  1.00 54.23           C
ANISOU  309  CA  MET A  39     7813   6441   6349   -690   -398    789       C
ATOM    310  C   MET A  39     -13.273  20.068  39.375  1.00 45.05           C
ANISOU  310  C   MET A  39     6688   5356   5072   -862   -302    796       C
ATOM    311  O   MET A  39     -13.577  18.889  39.178  1.00 42.52           O
ANISOU  311  O   MET A  39     6459   4933   4762   -972   -250    838       O
ATOM    312  CB  MET A  39     -12.264  21.004  37.374  1.00 52.83           C
ANISOU  312  CB  MET A  39     7522   6284   6267   -665   -369    680       C
ATOM    313  CG  MET A  39     -11.215  21.788  36.675  1.00 62.77           C
ANISOU  313  CG  MET A  39     8714   7507   7628   -516   -441    649       C
ATOM    314  SD  MET A  39     -11.559  21.542  34.932  1.00 62.53           S
ANISOU  314  SD  MET A  39     8609   7450   7701   -524   -389    557       S
ATOM    315  CE  MET A  39     -10.161  20.529  34.449  1.00 59.64           C
ANISOU  315  CE  MET A  39     8330   6872   7458   -448   -439    628       C
ATOM    316  N   ASN A  40     -14.066  20.929  39.978  1.00 42.47           N
ANISOU  316  N   ASN A  40     6283   5216   4637   -888   -273    743       N
ATOM    317  CA  ASN A  40     -15.422  20.611  40.377  1.00 48.43           C
ANISOU  317  CA  ASN A  40     7020   6104   5276  -1050   -170    717       C
ATOM    318  C   ASN A  40     -16.353  21.377  39.455  1.00 44.81           C
ANISOU  318  C   ASN A  40     6392   5804   4830  -1044   -123    574       C
ATOM    319  O   ASN A  40     -16.216  22.585  39.292  1.00 45.09           O
ANISOU  319  O   ASN A  40     6334   5925   4875   -917   -165    504       O
ATOM    320  CB  ASN A  40     -15.657  21.008  41.842  1.00 50.86           C
ANISOU  320  CB  ASN A  40     7361   6532   5431  -1073   -169    760       C
ATOM    321  CG  ASN A  40     -16.967  20.526  42.373  1.00 65.87           C
ANISOU  321  CG  ASN A  40     9257   8569   7200  -1257    -57    753       C
ATOM    322  OD1 ASN A  40     -17.946  20.375  41.640  1.00 73.72           O
ANISOU  322  OD1 ASN A  40    10156   9652   8201  -1350     22    668       O
ATOM    323  ND2 ASN A  40     -17.007  20.290  43.669  1.00 82.54           N
ANISOU  323  ND2 ASN A  40    11464  10715   9180  -1317    -47    840       N
ATOM    324  N   ILE A  41     -17.287  20.675  38.847  1.00 41.85           N
ANISOU  324  N   ILE A  41     5985   5465   4452  -1182    -39    531       N
ATOM    325  CA  ILE A  41     -18.404  21.294  38.153  1.00 60.36           C
ANISOU  325  CA  ILE A  41     8159   8004   6769  -1198     16    397       C
ATOM    326  C   ILE A  41     -19.677  21.062  38.949  1.00 72.10           C
ANISOU  326  C   ILE A  41     9607   9682   8108  -1360    112    377       C
ATOM    327  O   ILE A  41     -20.000  19.928  39.326  1.00 74.31           O
ANISOU  327  O   ILE A  41     9980   9909   8346  -1539    173    442       O
ATOM    328  CB  ILE A  41     -18.557  20.735  36.735  1.00 63.22           C
ANISOU  328  CB  ILE A  41     8484   8302   7236  -1234     37    340       C
ATOM    329  CG1 ILE A  41     -17.466  21.301  35.865  1.00 71.20           C
ANISOU  329  CG1 ILE A  41     9484   9195   8375  -1055    -48    330       C
ATOM    330  CG2 ILE A  41     -19.906  21.068  36.171  1.00 63.32           C
ANISOU  330  CG2 ILE A  41     8330   8538   7190  -1298    106    213       C
ATOM    331  CD1 ILE A  41     -17.135  20.409  34.805  1.00 78.76           C
ANISOU  331  CD1 ILE A  41    10482  10005   9437  -1088    -43    328       C
ATOM    332  N   ALA A  42     -20.375  22.146  39.228  1.00 67.44           N
ANISOU  332  N   ALA A  42     8883   9310   7433  -1296    126    288       N
ATOM    333  CA  ALA A  42     -21.762  22.113  39.634  1.00 81.73           C
ANISOU  333  CA  ALA A  42    10586  11360   9107  -1427    225    221       C
ATOM    334  C   ALA A  42     -22.428  23.212  38.838  1.00 90.23           C
ANISOU  334  C   ALA A  42    11476  12622  10187  -1301    221     76       C
ATOM    335  O   ALA A  42     -21.748  24.035  38.223  1.00101.37           O
ANISOU  335  O   ALA A  42    12872  13956  11686  -1120    142     50       O
ATOM    336  CB  ALA A  42     -21.912  22.299  41.149  1.00 79.53           C
ANISOU  336  CB  ALA A  42    10359  11176   8684  -1462    249    275       C
ATOM    337  N   SER A  43     -23.754  23.207  38.809  1.00 93.65           N
ANISOU  337  N   SER A  43    11764  13298  10522  -1398    307    -16       N
ATOM    338  CA  SER A  43     -24.457  24.389  38.332  1.00 82.13           C
ANISOU  338  CA  SER A  43    10128  12049   9030  -1247    299   -151       C
ATOM    339  C   SER A  43     -24.071  25.572  39.211  1.00 79.29           C
ANISOU  339  C   SER A  43     9792  11719   8617  -1071    248   -153       C
ATOM    340  O   SER A  43     -24.212  25.510  40.441  1.00 59.00           O
ANISOU  340  O   SER A  43     7267   9215   5936  -1132    283   -113       O
ATOM    341  CB  SER A  43     -25.966  24.150  38.350  1.00 77.49           C
ANISOU  341  CB  SER A  43     9369  11751   8324  -1383    402   -249       C
ATOM    342  OG  SER A  43     -26.314  23.177  37.386  1.00 74.67           O
ANISOU  342  OG  SER A  43     8980  11368   8023  -1537    438   -269       O
ATOM    343  N   HIS A  44     -23.539  26.629  38.581  1.00 73.38           N
ANISOU  343  N   HIS A  44     9028  10908   7944   -862    167   -195       N
ATOM    344  CA  HIS A  44     -22.861  27.695  39.313  1.00 77.59           C
ANISOU  344  CA  HIS A  44     9629  11392   8460   -701    100   -185       C
ATOM    345  C   HIS A  44     -21.745  27.094  40.169  1.00 78.29           C
ANISOU  345  C   HIS A  44     9891  11286   8571   -767     63    -49       C
ATOM    346  O   HIS A  44     -21.298  25.974  39.900  1.00 76.80           O
ANISOU  346  O   HIS A  44     9780  10949   8450   -887     69     37       O
ATOM    347  CB  HIS A  44     -23.879  28.493  40.133  1.00 83.60           C
ANISOU  347  CB  HIS A  44    10290  12408   9067   -648    148   -279       C
ATOM    348  CG  HIS A  44     -25.186  28.685  39.420  1.00 89.06           C
ANISOU  348  CG  HIS A  44    10792  13338   9710   -634    206   -402       C
ATOM    349  ND1 HIS A  44     -26.312  27.943  39.710  1.00 91.55           N
ANISOU  349  ND1 HIS A  44    10998  13867   9920   -807    309   -437       N
ATOM    350  CD2 HIS A  44     -25.531  29.505  38.398  1.00 89.40           C
ANISOU  350  CD2 HIS A  44    10734  13444   9790   -471    174   -497       C
ATOM    351  CE1 HIS A  44     -27.299  28.309  38.910  1.00 92.36           C
ANISOU  351  CE1 HIS A  44    10924  14171   9998   -747    334   -556       C
ATOM    352  NE2 HIS A  44     -26.852  29.258  38.105  1.00 91.00           N
ANISOU  352  NE2 HIS A  44    10759  13909   9910   -534    250   -591       N
ATOM    353  N   LYS A  45     -21.251  27.834  41.168  1.00 89.11           N
ANISOU  353  N   LYS A  45    11326  12646   9885   -679     18    -34       N
ATOM    354  CA  LYS A  45     -20.195  27.395  42.093  1.00 83.68           C
ANISOU  354  CA  LYS A  45    10794  11804   9198   -719    -29     88       C
ATOM    355  C   LYS A  45     -19.052  26.569  41.483  1.00 79.65           C
ANISOU  355  C   LYS A  45    10384  11047   8830   -746    -86    192       C
ATOM    356  O   LYS A  45     -18.686  25.533  42.052  1.00 83.51           O
ANISOU  356  O   LYS A  45    10981  11445   9304   -859    -77    302       O
ATOM    357  CB  LYS A  45     -20.821  26.586  43.233  1.00 75.75           C
ANISOU  357  CB  LYS A  45     9821  10909   8049   -885     51    141       C
ATOM    358  CG  LYS A  45     -21.750  27.374  44.144  1.00 79.57           C
ANISOU  358  CG  LYS A  45    10226  11637   8369   -856    102     53       C
ATOM    359  CD  LYS A  45     -23.058  26.622  44.437  1.00 80.57           C
ANISOU  359  CD  LYS A  45    10268  11971   8376  -1037    230     32       C
ATOM    360  CE  LYS A  45     -22.980  25.820  45.733  1.00 82.38           C
ANISOU  360  CE  LYS A  45    10615  12205   8483  -1191    272    144       C
ATOM    361  NZ  LYS A  45     -24.278  25.852  46.508  1.00 81.34           N
ANISOU  361  NZ  LYS A  45    10377  12362   8166  -1292    390     79       N
ATOM    362  N   PRO A  46     -18.437  26.978  40.370  1.00 75.88           N
ANISOU  362  N   PRO A  46     9887  10458   8487   -639   -143    166       N
ATOM    363  CA  PRO A  46     -17.322  26.187  39.823  1.00 70.01           C
ANISOU  363  CA  PRO A  46     9232   9496   7873   -653   -193    258       C
ATOM    364  C   PRO A  46     -16.035  26.400  40.612  1.00 72.60           C
ANISOU  364  C   PRO A  46     9668   9700   8218   -588   -283    340       C
ATOM    365  O   PRO A  46     -15.707  27.520  41.014  1.00 68.24           O
ANISOU  365  O   PRO A  46     9106   9181   7639   -483   -335    299       O
ATOM    366  CB  PRO A  46     -17.179  26.707  38.383  1.00 65.68           C
ANISOU  366  CB  PRO A  46     8608   8908   7441   -556   -216    189       C
ATOM    367  CG  PRO A  46     -18.225  27.814  38.218  1.00 68.72           C
ANISOU  367  CG  PRO A  46     8874   9484   7753   -479   -187     67       C
ATOM    368  CD  PRO A  46     -18.651  28.211  39.592  1.00 72.00           C
ANISOU  368  CD  PRO A  46     9303  10025   8030   -489   -168     58       C
ATOM    369  N   GLN A  47     -15.296  25.302  40.824  1.00 64.10           N
ANISOU  369  N   GLN A  47     8697   8477   7182   -649   -304    453       N
ATOM    370  CA  GLN A  47     -14.100  25.305  41.657  1.00 57.43           C
ANISOU  370  CA  GLN A  47     7951   7533   6338   -597   -391    542       C
ATOM    371  C   GLN A  47     -12.927  24.682  40.916  1.00 58.47           C
ANISOU  371  C   GLN A  47     8131   7474   6612   -552   -451    607       C
ATOM    372  O   GLN A  47     -13.104  23.801  40.071  1.00 52.49           O
ANISOU  372  O   GLN A  47     7379   6639   5926   -606   -409    619       O
ATOM    373  CB  GLN A  47     -14.318  24.528  42.950  1.00 67.32           C
ANISOU  373  CB  GLN A  47     9305   8811   7463   -699   -367    635       C
ATOM    374  CG  GLN A  47     -15.689  24.721  43.566  1.00 83.65           C
ANISOU  374  CG  GLN A  47    11323  11078   9384   -790   -273    579       C
ATOM    375  CD  GLN A  47     -15.664  25.706  44.709  1.00 93.72           C
ANISOU  375  CD  GLN A  47    12598  12473  10536   -730   -305    549       C
ATOM    376  OE1 GLN A  47     -14.702  26.456  44.874  1.00100.27           O
ANISOU  376  OE1 GLN A  47    13447  13247  11405   -615   -399    544       O
ATOM    377  NE2 GLN A  47     -16.723  25.711  45.509  1.00 96.97           N
ANISOU  377  NE2 GLN A  47    12989  13059  10797   -813   -224    523       N
ATOM    378  N   ILE A  48     -11.720  25.140  41.251  1.00 51.98           N
ANISOU  378  N   ILE A  48     7337   6586   5826   -456   -548    642       N
ATOM    379  CA  ILE A  48     -10.478  24.483  40.853  1.00 50.89           C
ANISOU  379  CA  ILE A  48     7249   6288   5800   -404   -613    717       C
ATOM    380  C   ILE A  48      -9.669  24.206  42.108  1.00 51.23           C
ANISOU  380  C   ILE A  48     7386   6305   5775   -383   -688    816       C
ATOM    381  O   ILE A  48      -9.420  25.125  42.898  1.00 56.03           O
ANISOU  381  O   ILE A  48     7979   6995   6313   -343   -740    792       O
ATOM    382  CB  ILE A  48      -9.644  25.324  39.880  1.00 54.03           C
ANISOU  382  CB  ILE A  48     7566   6646   6317   -298   -667    659       C
ATOM    383  CG1 ILE A  48     -10.419  25.589  38.601  1.00 50.36           C
ANISOU  383  CG1 ILE A  48     7016   6208   5910   -307   -599    568       C
ATOM    384  CG2 ILE A  48      -8.336  24.602  39.569  1.00 52.11           C
ANISOU  384  CG2 ILE A  48     7360   6262   6176   -240   -732    735       C
ATOM    385  CD1 ILE A  48      -9.773  26.632  37.691  1.00 49.31           C
ANISOU  385  CD1 ILE A  48     6809   6058   5868   -212   -640    506       C
ATOM    386  N   HIS A  49      -9.256  22.953  42.291  1.00 47.42           N
ANISOU  386  N   HIS A  49     7006   5704   5308   -405   -698    925       N
ATOM    387  CA  HIS A  49      -8.343  22.582  43.365  1.00 47.79           C
ANISOU  387  CA  HIS A  49     7146   5711   5300   -360   -784   1032       C
ATOM    388  C   HIS A  49      -6.983  22.199  42.798  1.00 53.64           C
ANISOU  388  C   HIS A  49     7888   6325   6169   -246   -868   1075       C
ATOM    389  O   HIS A  49      -6.845  21.886  41.613  1.00 50.68           O
ANISOU  389  O   HIS A  49     7473   5866   5916   -225   -842   1042       O
ATOM    390  CB  HIS A  49      -8.874  21.419  44.210  1.00 53.71           C
ANISOU  390  CB  HIS A  49     8040   6425   5944   -457   -740   1143       C
ATOM    391  CG  HIS A  49      -9.985  21.784  45.149  1.00 53.37           C
ANISOU  391  CG  HIS A  49     8004   6536   5740   -561   -675   1123       C
ATOM    392  ND1 HIS A  49     -11.019  22.623  44.798  1.00 58.08           N
ANISOU  392  ND1 HIS A  49     8488   7268   6312   -607   -601   1000       N
ATOM    393  CD2 HIS A  49     -10.248  21.374  46.413  1.00 58.30           C
ANISOU  393  CD2 HIS A  49     8736   7205   6211   -625   -667   1211       C
ATOM    394  CE1 HIS A  49     -11.860  22.735  45.810  1.00 57.39           C
ANISOU  394  CE1 HIS A  49     8427   7313   6067   -691   -549   1005       C
ATOM    395  NE2 HIS A  49     -11.414  21.988  46.803  1.00 63.74           N
ANISOU  395  NE2 HIS A  49     9366   8065   6788   -712   -585   1134       N
ATOM    396  N   TYR A  50      -5.983  22.204  43.683  1.00 46.23           N
ANISOU  396  N   TYR A  50     6990   5387   5189   -171   -971   1146       N
ATOM    397  CA  TYR A  50      -4.583  22.005  43.313  1.00 47.64           C
ANISOU  397  CA  TYR A  50     7141   5489   5471    -46  -1067   1178       C
ATOM    398  C   TYR A  50      -3.855  21.534  44.557  1.00 56.49           C
ANISOU  398  C   TYR A  50     8356   6610   6498      9  -1161   1292       C
ATOM    399  O   TYR A  50      -3.942  22.197  45.596  1.00 52.40           O
ANISOU  399  O   TYR A  50     7841   6208   5860    -11  -1199   1288       O
ATOM    400  CB  TYR A  50      -3.979  23.305  42.801  1.00 46.71           C
ANISOU  400  CB  TYR A  50     6879   5448   5422      8  -1112   1074       C
ATOM    401  CG  TYR A  50      -2.605  23.211  42.169  1.00 51.23           C
ANISOU  401  CG  TYR A  50     7384   5968   6115    120  -1190   1080       C
ATOM    402  CD1 TYR A  50      -2.436  22.665  40.909  1.00 54.66           C
ANISOU  402  CD1 TYR A  50     7787   6304   6677    152  -1148   1062       C
ATOM    403  CD2 TYR A  50      -1.485  23.725  42.816  1.00 55.04           C
ANISOU  403  CD2 TYR A  50     7818   6517   6577    190  -1304   1092       C
ATOM    404  CE1 TYR A  50      -1.187  22.610  40.314  1.00 55.18           C
ANISOU  404  CE1 TYR A  50     7775   6343   6847    257  -1211   1059       C
ATOM    405  CE2 TYR A  50      -0.231  23.671  42.232  1.00 52.19           C
ANISOU  405  CE2 TYR A  50     7371   6136   6321    288  -1371   1089       C
ATOM    406  CZ  TYR A  50      -0.089  23.117  40.983  1.00 57.81           C
ANISOU  406  CZ  TYR A  50     8051   6754   7158    324  -1321   1073       C
ATOM    407  OH  TYR A  50       1.143  23.059  40.386  1.00 63.11           O
ANISOU  407  OH  TYR A  50     8627   7424   7929    422  -1379   1064       O
ATOM    408  N   ARG A  51      -3.175  20.389  44.465  1.00 60.57           N
ANISOU  408  N   ARG A  51     8957   6998   7061     85  -1200   1390       N
ATOM    409  CA  ARG A  51      -2.406  19.823  45.583  1.00 66.47           C
ANISOU  409  CA  ARG A  51     9803   7734   7720    165  -1301   1513       C
ATOM    410  C   ARG A  51      -3.202  19.833  46.886  1.00 65.18           C
ANISOU  410  C   ARG A  51     9746   7647   7373     68  -1280   1571       C
ATOM    411  O   ARG A  51      -2.669  20.113  47.963  1.00 62.79           O
ANISOU  411  O   ARG A  51     9463   7432   6962    115  -1372   1618       O
ATOM    412  CB  ARG A  51      -1.073  20.557  45.755  1.00 63.20           C
ANISOU  412  CB  ARG A  51     9268   7409   7335    288  -1431   1484       C
ATOM    413  CG  ARG A  51      -0.182  20.514  44.517  1.00 66.88           C
ANISOU  413  CG  ARG A  51     9622   7818   7973    386  -1452   1433       C
ATOM    414  CD  ARG A  51       1.077  21.363  44.681  1.00 75.17           C
ANISOU  414  CD  ARG A  51    10529   8987   9046    476  -1570   1389       C
ATOM    415  NE  ARG A  51       2.286  20.544  44.690  1.00 83.91           N
ANISOU  415  NE  ARG A  51    11635  10049  10197    634  -1666   1464       N
ATOM    416  CZ  ARG A  51       2.950  20.192  45.787  1.00 91.53           C
ANISOU  416  CZ  ARG A  51    12653  11059  11064    721  -1778   1557       C
ATOM    417  NH1 ARG A  51       2.530  20.594  46.981  1.00 94.56           N
ANISOU  417  NH1 ARG A  51    13099  11534  11294    653  -1806   1585       N
ATOM    418  NH2 ARG A  51       4.038  19.440  45.689  1.00 94.88           N
ANISOU  418  NH2 ARG A  51    13067  11447  11536    885  -1865   1618       N
ATOM    419  N   GLY A  52      -4.500  19.542  46.785  1.00 64.12           N
ANISOU  419  N   GLY A  52     9671   7496   7195    -73  -1155   1562       N
ATOM    420  CA  GLY A  52      -5.348  19.374  47.949  1.00 59.41           C
ANISOU  420  CA  GLY A  52     9184   6968   6421   -181  -1112   1625       C
ATOM    421  C   GLY A  52      -6.098  20.606  48.402  1.00 59.95           C
ANISOU  421  C   GLY A  52     9157   7224   6395   -256  -1075   1518       C
ATOM    422  O   GLY A  52      -6.883  20.512  49.353  1.00 60.96           O
ANISOU  422  O   GLY A  52     9363   7432   6367   -352  -1025   1557       O
ATOM    423  N   LYS A  53      -5.899  21.749  47.755  1.00 57.29           N
ANISOU  423  N   LYS A  53     8665   6958   6143   -215  -1092   1386       N
ATOM    424  CA  LYS A  53      -6.478  23.000  48.224  1.00 64.90           C
ANISOU  424  CA  LYS A  53     9552   8088   7020   -257  -1072   1279       C
ATOM    425  C   LYS A  53      -7.135  23.765  47.085  1.00 62.48           C
ANISOU  425  C   LYS A  53     9122   7804   6813   -283   -996   1142       C
ATOM    426  O   LYS A  53      -6.691  23.682  45.933  1.00 55.24           O
ANISOU  426  O   LYS A  53     8145   6796   6048   -235  -1001   1113       O
ATOM    427  CB  LYS A  53      -5.405  23.886  48.875  1.00 65.94           C
ANISOU  427  CB  LYS A  53     9636   8298   7120   -165  -1202   1254       C
ATOM    428  CG  LYS A  53      -4.682  23.220  50.043  1.00 66.68           C
ANISOU  428  CG  LYS A  53     9840   8394   7100   -119  -1297   1386       C
ATOM    429  CD  LYS A  53      -3.218  23.644  50.102  1.00 70.81           C
ANISOU  429  CD  LYS A  53    10292   8932   7679      3  -1443   1378       C
ATOM    430  CE  LYS A  53      -2.446  22.815  51.121  1.00 77.43           C
ANISOU  430  CE  LYS A  53    11239   9763   8417     74  -1546   1521       C
ATOM    431  NZ  LYS A  53      -3.090  22.860  52.467  1.00 76.16           N
ANISOU  431  NZ  LYS A  53    11181   9711   8045      5  -1533   1566       N
ATOM    432  N   PRO A  54      -8.184  24.534  47.380  1.00 58.24           N
ANISOU  432  N   PRO A  54     8545   7398   6186   -348   -926   1055       N
ATOM    433  CA  PRO A  54      -8.837  25.329  46.336  1.00 53.97           C
ANISOU  433  CA  PRO A  54     7890   6889   5726   -353   -862    925       C
ATOM    434  C   PRO A  54      -7.974  26.499  45.902  1.00 59.11           C
ANISOU  434  C   PRO A  54     8455   7542   6463   -258   -942    840       C
ATOM    435  O   PRO A  54      -7.277  27.117  46.710  1.00 58.18           O
ANISOU  435  O   PRO A  54     8346   7472   6288   -216  -1029    834       O
ATOM    436  CB  PRO A  54     -10.125  25.830  47.006  1.00 53.84           C
ANISOU  436  CB  PRO A  54     7862   7030   5563   -426   -779    861       C
ATOM    437  CG  PRO A  54     -10.063  25.400  48.436  1.00 58.08           C
ANISOU  437  CG  PRO A  54     8506   7623   5939   -465   -802    953       C
ATOM    438  CD  PRO A  54      -8.692  24.865  48.721  1.00 62.45           C
ANISOU  438  CD  PRO A  54     9127   8068   6533   -394   -919   1061       C
ATOM    439  N   LEU A  55      -8.038  26.809  44.608  1.00 51.63           N
ANISOU  439  N   LEU A  55     7427   6544   5646   -234   -911    772       N
ATOM    440  CA  LEU A  55      -7.393  27.997  44.062  1.00 50.66           C
ANISOU  440  CA  LEU A  55     7226   6419   5602   -165   -964    685       C
ATOM    441  C   LEU A  55      -8.396  29.145  44.113  1.00 52.82           C
ANISOU  441  C   LEU A  55     7463   6797   5811   -173   -912    568       C
ATOM    442  O   LEU A  55      -9.431  29.101  43.444  1.00 61.72           O
ANISOU  442  O   LEU A  55     8552   7950   6948   -198   -823    521       O
ATOM    443  CB  LEU A  55      -6.916  27.746  42.635  1.00 47.79           C
ANISOU  443  CB  LEU A  55     6805   5951   5402   -131   -956    678       C
ATOM    444  CG  LEU A  55      -5.806  26.716  42.431  1.00 48.56           C
ANISOU  444  CG  LEU A  55     6926   5944   5581    -92  -1013    775       C
ATOM    445  CD1 LEU A  55      -5.461  26.644  40.956  1.00 54.01           C
ANISOU  445  CD1 LEU A  55     7547   6554   6420    -58   -990    742       C
ATOM    446  CD2 LEU A  55      -4.556  27.050  43.256  1.00 49.84           C
ANISOU  446  CD2 LEU A  55     7091   6127   5720    -38  -1132    807       C
ATOM    447  N   GLU A  56      -8.090  30.175  44.895  1.00 51.61           N
ANISOU  447  N   GLU A  56     7318   6703   5587   -145   -970    514       N
ATOM    448  CA  GLU A  56      -9.036  31.248  45.167  1.00 61.83           C
ANISOU  448  CA  GLU A  56     8600   8097   6798   -136   -926    403       C
ATOM    449  C   GLU A  56      -8.370  32.608  44.988  1.00 49.74           C
ANISOU  449  C   GLU A  56     7053   6537   5308    -80   -992    315       C
ATOM    450  O   GLU A  56      -7.150  32.753  45.109  1.00 50.99           O
ANISOU  450  O   GLU A  56     7216   6642   5516    -70  -1082    341       O
ATOM    451  CB  GLU A  56      -9.611  31.130  46.591  1.00 68.69           C
ANISOU  451  CB  GLU A  56     9525   9086   7488   -175   -912    414       C
ATOM    452  CG  GLU A  56     -10.282  29.797  46.879  1.00 79.86           C
ANISOU  452  CG  GLU A  56    10973  10527   8843   -254   -841    509       C
ATOM    453  CD  GLU A  56     -10.925  29.746  48.256  1.00 88.38           C
ANISOU  453  CD  GLU A  56    12106  11742   9732   -302   -813    518       C
ATOM    454  OE1 GLU A  56     -10.226  30.023  49.256  1.00 89.91           O
ANISOU  454  OE1 GLU A  56    12353  11961   9845   -283   -894    538       O
ATOM    455  OE2 GLU A  56     -12.130  29.423  48.333  1.00 91.13           O
ANISOU  455  OE2 GLU A  56    12437  12184  10004   -363   -708    501       O
ATOM    456  N   GLY A  57      -9.194  33.607  44.682  1.00 56.14           N
ANISOU  456  N   GLY A  57     7846   7386   6097    -43   -945    207       N
ATOM    457  CA  GLY A  57      -8.721  34.978  44.620  1.00 56.36           C
ANISOU  457  CA  GLY A  57     7892   7379   6145      3   -998    116       C
ATOM    458  C   GLY A  57      -8.033  35.385  43.336  1.00 56.69           C
ANISOU  458  C   GLY A  57     7900   7303   6338     26  -1018    107       C
ATOM    459  O   GLY A  57      -7.461  36.482  43.279  1.00 49.79           O
ANISOU  459  O   GLY A  57     7052   6378   5487     43  -1067     45       O
ATOM    460  N   PHE A  58      -8.080  34.566  42.291  1.00 54.79           N
ANISOU  460  N   PHE A  58     7608   7016   6195     20   -976    163       N
ATOM    461  CA  PHE A  58      -7.345  34.909  41.080  1.00 48.93           C
ANISOU  461  CA  PHE A  58     6832   6172   5588     37   -993    161       C
ATOM    462  C   PHE A  58      -8.077  35.970  40.277  1.00 48.79           C
ANISOU  462  C   PHE A  58     6818   6139   5583     92   -948     73       C
ATOM    463  O   PHE A  58      -9.293  35.900  40.084  1.00 48.46           O
ANISOU  463  O   PHE A  58     6759   6163   5492    123   -878     38       O
ATOM    464  CB  PHE A  58      -7.080  33.662  40.235  1.00 41.39           C
ANISOU  464  CB  PHE A  58     5827   5172   4727     19   -967    244       C
ATOM    465  CG  PHE A  58      -5.939  32.828  40.771  1.00 45.63           C
ANISOU  465  CG  PHE A  58     6365   5685   5288     -6  -1036    332       C
ATOM    466  CD1 PHE A  58      -4.642  33.090  40.390  1.00 38.75           C
ANISOU  466  CD1 PHE A  58     5461   4758   4506     -1  -1102    344       C
ATOM    467  CD2 PHE A  58      -6.169  31.824  41.696  1.00 40.87           C
ANISOU  467  CD2 PHE A  58     5799   5124   4608    -32  -1037    400       C
ATOM    468  CE1 PHE A  58      -3.596  32.354  40.900  1.00 41.16           C
ANISOU  468  CE1 PHE A  58     5755   5061   4825     -3  -1172    417       C
ATOM    469  CE2 PHE A  58      -5.123  31.089  42.213  1.00 50.98           C
ANISOU  469  CE2 PHE A  58     7089   6381   5899    -32  -1109    484       C
ATOM    470  CZ  PHE A  58      -3.835  31.350  41.810  1.00 45.49           C
ANISOU  470  CZ  PHE A  58     6346   5642   5296     -9  -1180    490       C
ATOM    471  N   ASP A  59      -7.318  36.968  39.813  1.00 39.59           N
ANISOU  471  N   ASP A  59     5674   4890   4479    103   -990     38       N
ATOM    472  CA  ASP A  59      -7.848  37.994  38.932  1.00 39.29           C
ANISOU  472  CA  ASP A  59     5659   4807   4462    162   -955    -30       C
ATOM    473  C   ASP A  59      -7.653  37.634  37.467  1.00 42.43           C
ANISOU  473  C   ASP A  59     6003   5146   4972    168   -921     10       C
ATOM    474  O   ASP A  59      -8.508  37.948  36.638  1.00 39.71           O
ANISOU  474  O   ASP A  59     5652   4806   4627    228   -869    -23       O
ATOM    475  CB  ASP A  59      -7.171  39.341  39.221  1.00 43.34           C
ANISOU  475  CB  ASP A  59     6251   5245   4972    158  -1013    -90       C
ATOM    476  CG  ASP A  59      -7.368  39.798  40.651  1.00 53.38           C
ANISOU  476  CG  ASP A  59     7584   6573   6124    157  -1048   -148       C
ATOM    477  OD1 ASP A  59      -8.539  40.000  41.027  1.00 53.13           O
ANISOU  477  OD1 ASP A  59     7573   6615   6001    221  -1003   -203       O
ATOM    478  OD2 ASP A  59      -6.363  39.956  41.392  1.00 46.82           O
ANISOU  478  OD2 ASP A  59     6775   5729   5285     94  -1122   -143       O
ATOM    479  N   ALA A  60      -6.540  36.994  37.106  1.00 39.73           N
ANISOU  479  N   ALA A  60     5618   4760   4719    116   -951     78       N
ATOM    480  CA  ALA A  60      -6.315  36.701  35.692  1.00 37.45           C
ANISOU  480  CA  ALA A  60     5280   4420   4529    124   -915    107       C
ATOM    481  C   ALA A  60      -5.517  35.415  35.570  1.00 38.11           C
ANISOU  481  C   ALA A  60     5300   4501   4679     85   -928    185       C
ATOM    482  O   ALA A  60      -5.039  34.851  36.561  1.00 43.88           O
ANISOU  482  O   ALA A  60     6031   5258   5382     57   -974    222       O
ATOM    483  CB  ALA A  60      -5.617  37.877  34.972  1.00 36.36           C
ANISOU  483  CB  ALA A  60     5176   4194   4444    120   -934     80       C
ATOM    484  N   VAL A  61      -5.419  34.912  34.349  1.00 36.35           N
ANISOU  484  N   VAL A  61     5029   4248   4536     95   -888    209       N
ATOM    485  CA  VAL A  61      -4.717  33.656  34.102  1.00 35.05           C
ANISOU  485  CA  VAL A  61     4811   4071   4438     78   -893    274       C
ATOM    486  C   VAL A  61      -3.978  33.801  32.783  1.00 40.47           C
ANISOU  486  C   VAL A  61     5449   4708   5220     82   -876    279       C
ATOM    487  O   VAL A  61      -4.539  34.309  31.808  1.00 39.24           O
ANISOU  487  O   VAL A  61     5297   4540   5072    105   -828    247       O
ATOM    488  CB  VAL A  61      -5.673  32.433  34.118  1.00 33.96           C
ANISOU  488  CB  VAL A  61     4667   3964   4274     79   -841    297       C
ATOM    489  CG1 VAL A  61      -6.881  32.573  33.156  1.00 31.09           C
ANISOU  489  CG1 VAL A  61     4290   3626   3897    102   -767    250       C
ATOM    490  CG2 VAL A  61      -4.927  31.116  33.868  1.00 36.16           C
ANISOU  490  CG2 VAL A  61     4916   4202   4623     72   -848    363       C
ATOM    491  N   ILE A  62      -2.702  33.423  32.774  1.00 38.18           N
ANISOU  491  N   ILE A  62     5111   4402   4994     65   -918    317       N
ATOM    492  CA  ILE A  62      -1.886  33.399  31.568  1.00 41.57           C
ANISOU  492  CA  ILE A  62     5479   4804   5511     65   -898    325       C
ATOM    493  C   ILE A  62      -1.715  31.940  31.150  1.00 41.08           C
ANISOU  493  C   ILE A  62     5371   4737   5501     96   -876    366       C
ATOM    494  O   ILE A  62      -1.024  31.179  31.839  1.00 39.89           O
ANISOU  494  O   ILE A  62     5201   4592   5363    107   -924    408       O
ATOM    495  CB  ILE A  62      -0.529  34.076  31.792  1.00 42.78           C
ANISOU  495  CB  ILE A  62     5595   4960   5699     23   -957    327       C
ATOM    496  CG1 ILE A  62      -0.719  35.574  32.096  1.00 41.11           C
ANISOU  496  CG1 ILE A  62     5453   4728   5440    -18   -972    278       C
ATOM    497  CG2 ILE A  62       0.371  33.877  30.568  1.00 44.70           C
ANISOU  497  CG2 ILE A  62     5757   5198   6029     20   -927    339       C
ATOM    498  CD1 ILE A  62       0.533  36.224  32.739  1.00 41.01           C
ANISOU  498  CD1 ILE A  62     5415   4730   5437    -87  -1045    270       C
ATOM    499  N   PRO A  63      -2.326  31.496  30.053  1.00 38.29           N
ANISOU  499  N   PRO A  63     5007   4368   5172    117   -808    353       N
ATOM    500  CA  PRO A  63      -2.121  30.112  29.604  1.00 42.29           C
ANISOU  500  CA  PRO A  63     5485   4853   5731    144   -785    381       C
ATOM    501  C   PRO A  63      -0.813  29.979  28.834  1.00 49.34           C
ANISOU  501  C   PRO A  63     6301   5741   6707    165   -792    391       C
ATOM    502  O   PRO A  63      -0.555  30.723  27.886  1.00 50.66           O
ANISOU  502  O   PRO A  63     6435   5917   6898    153   -762    365       O
ATOM    503  CB  PRO A  63      -3.324  29.856  28.695  1.00 42.66           C
ANISOU  503  CB  PRO A  63     5547   4901   5761    147   -711    346       C
ATOM    504  CG  PRO A  63      -3.671  31.181  28.174  1.00 43.91           C
ANISOU  504  CG  PRO A  63     5710   5080   5892    144   -695    307       C
ATOM    505  CD  PRO A  63      -3.337  32.193  29.248  1.00 36.69           C
ANISOU  505  CD  PRO A  63     4829   4172   4940    123   -753    309       C
ATOM    506  N   ARG A  64       0.012  29.033  29.249  1.00 39.38           N
ANISOU  506  N   ARG A  64     5011   4470   5482    200   -831    429       N
ATOM    507  CA  ARG A  64       1.191  28.610  28.491  1.00 49.60           C
ANISOU  507  CA  ARG A  64     6219   5772   6855    241   -830    433       C
ATOM    508  C   ARG A  64       1.038  27.108  28.258  1.00 53.68           C
ANISOU  508  C   ARG A  64     6759   6234   7403    302   -807    452       C
ATOM    509  O   ARG A  64       1.754  26.289  28.831  1.00 53.43           O
ANISOU  509  O   ARG A  64     6720   6187   7393    359   -856    491       O
ATOM    510  CB  ARG A  64       2.495  28.937  29.228  1.00 51.42           C
ANISOU  510  CB  ARG A  64     6383   6055   7100    244   -909    455       C
ATOM    511  CG  ARG A  64       2.716  30.420  29.527  1.00 56.93           C
ANISOU  511  CG  ARG A  64     7071   6793   7767    166   -935    430       C
ATOM    512  CD  ARG A  64       2.930  31.233  28.255  1.00 58.64           C
ANISOU  512  CD  ARG A  64     7247   7018   8016    126   -875    396       C
ATOM    513  NE  ARG A  64       4.076  30.753  27.484  1.00 63.20           N
ANISOU  513  NE  ARG A  64     7711   7640   8663    156   -862    397       N
ATOM    514  CZ  ARG A  64       4.516  31.335  26.371  1.00 64.78           C
ANISOU  514  CZ  ARG A  64     7856   7865   8891    118   -808    375       C
ATOM    515  NH1 ARG A  64       3.898  32.415  25.895  1.00 54.83           N
ANISOU  515  NH1 ARG A  64     6660   6575   7596     54   -768    358       N
ATOM    516  NH2 ARG A  64       5.556  30.827  25.724  1.00 65.84           N
ANISOU  516  NH2 ARG A  64     7877   8057   9081    152   -792    370       N
ATOM    517  N   ILE A  65       0.064  26.751  27.432  1.00 53.05           N
ANISOU  517  N   ILE A  65     6717   6122   7319    291   -736    421       N
ATOM    518  CA  ILE A  65      -0.344  25.363  27.270  1.00 57.97           C
ANISOU  518  CA  ILE A  65     7393   6675   7959    322   -708    429       C
ATOM    519  C   ILE A  65       0.489  24.745  26.152  1.00 64.19           C
ANISOU  519  C   ILE A  65     8120   7447   8822    388   -678    405       C
ATOM    520  O   ILE A  65       0.393  25.163  24.994  1.00 72.23           O
ANISOU  520  O   ILE A  65     9094   8497   9855    376   -624    357       O
ATOM    521  CB  ILE A  65      -1.846  25.262  26.979  1.00 55.15           C
ANISOU  521  CB  ILE A  65     7097   6306   7552    264   -648    395       C
ATOM    522  CG1 ILE A  65      -2.649  25.887  28.125  1.00 48.99           C
ANISOU  522  CG1 ILE A  65     6364   5559   6689    210   -673    412       C
ATOM    523  CG2 ILE A  65      -2.247  23.813  26.773  1.00 60.29           C
ANISOU  523  CG2 ILE A  65     7811   6875   8221    271   -615    397       C
ATOM    524  CD1 ILE A  65      -4.088  26.174  27.743  1.00 49.95           C
ANISOU  524  CD1 ILE A  65     6508   5716   6754    158   -616    364       C
ATOM    525  N   GLY A  66       1.316  23.757  26.502  1.00 62.58           N
ANISOU  525  N   GLY A  66     7918   7200   8660    466   -715    437       N
ATOM    526  CA  GLY A  66       2.022  22.997  25.487  1.00 67.65           C
ANISOU  526  CA  GLY A  66     8515   7820   9369    546   -682    406       C
ATOM    527  C   GLY A  66       1.067  22.329  24.517  1.00 69.80           C
ANISOU  527  C   GLY A  66     8847   8031   9643    524   -604    355       C
ATOM    528  O   GLY A  66      -0.113  22.121  24.805  1.00 66.73           O
ANISOU  528  O   GLY A  66     8544   7601   9208    455   -583    355       O
ATOM    529  N   ALA A  67       1.585  22.011  23.325  1.00 74.08           N
ANISOU  529  N   ALA A  67     9332   8583  10232    577   -558    304       N
ATOM    530  CA  ALA A  67       0.739  21.345  22.334  1.00 75.42           C
ANISOU  530  CA  ALA A  67     9555   8702  10400    556   -486    243       C
ATOM    531  C   ALA A  67       0.372  19.932  22.770  1.00 69.51           C
ANISOU  531  C   ALA A  67     8930   7817   9664    579   -489    255       C
ATOM    532  O   ALA A  67      -0.693  19.427  22.397  1.00 74.42           O
ANISOU  532  O   ALA A  67     9627   8387  10262    511   -441    216       O
ATOM    533  CB  ALA A  67       1.424  21.321  20.968  1.00 72.96           C
ANISOU  533  CB  ALA A  67     9158   8438  10127    611   -435    180       C
ATOM    534  N   SER A  68       1.231  19.293  23.568  1.00 64.81           N
ANISOU  534  N   SER A  68     8360   7162   9101    669   -547    310       N
ATOM    535  CA  SER A  68       0.925  17.972  24.114  1.00 69.88           C
ANISOU  535  CA  SER A  68     9149   7653   9749    693   -556    341       C
ATOM    536  C   SER A  68      -0.367  17.979  24.921  1.00 67.68           C
ANISOU  536  C   SER A  68     8974   7339   9403    563   -550    375       C
ATOM    537  O   SER A  68      -1.072  16.964  24.981  1.00 68.20           O
ANISOU  537  O   SER A  68     9167   7285   9460    520   -520    372       O
ATOM    538  CB  SER A  68       2.085  17.491  24.996  1.00 70.83           C
ANISOU  538  CB  SER A  68     9277   7737   9900    825   -635    411       C
ATOM    539  OG  SER A  68       2.671  18.579  25.707  1.00 79.46           O
ANISOU  539  OG  SER A  68    10264   8955  10970    823   -697    455       O
ATOM    540  N   VAL A  69      -0.688  19.104  25.550  1.00 60.96           N
ANISOU  540  N   VAL A  69     8071   6591   8499    496   -576    403       N
ATOM    541  CA  VAL A  69      -1.682  19.153  26.614  1.00 61.87           C
ANISOU  541  CA  VAL A  69     8270   6694   8542    397   -585    449       C
ATOM    542  C   VAL A  69      -2.841  20.086  26.252  1.00 67.52           C
ANISOU  542  C   VAL A  69     8943   7510   9203    286   -538    397       C
ATOM    543  O   VAL A  69      -3.535  20.589  27.133  1.00 62.48           O
ANISOU  543  O   VAL A  69     8326   6917   8497    217   -551    425       O
ATOM    544  CB  VAL A  69      -1.022  19.554  27.950  1.00 59.00           C
ANISOU  544  CB  VAL A  69     7904   6360   8152    436   -670    534       C
ATOM    545  CG1 VAL A  69      -0.103  18.423  28.457  1.00 60.67           C
ANISOU  545  CG1 VAL A  69     8190   6463   8400    551   -721    597       C
ATOM    546  CG2 VAL A  69      -0.206  20.833  27.788  1.00 56.76           C
ANISOU  546  CG2 VAL A  69     7480   6204   7882    469   -705    518       C
ATOM    547  N   THR A  70      -3.066  20.304  24.951  1.00 61.43           N
ANISOU  547  N   THR A  70     8111   6777   8451    280   -484    318       N
ATOM    548  CA  THR A  70      -4.086  21.258  24.515  1.00 62.37           C
ANISOU  548  CA  THR A  70     8181   7003   8515    203   -449    269       C
ATOM    549  C   THR A  70      -5.455  20.934  25.107  1.00 59.48           C
ANISOU  549  C   THR A  70     7883   6637   8079     95   -423    266       C
ATOM    550  O   THR A  70      -6.156  21.838  25.586  1.00 59.03           O
ANISOU  550  O   THR A  70     7798   6673   7958     50   -428    267       O
ATOM    551  CB  THR A  70      -4.154  21.300  22.984  1.00 61.23           C
ANISOU  551  CB  THR A  70     7979   6891   8393    217   -395    188       C
ATOM    552  OG1 THR A  70      -2.915  21.803  22.470  1.00 64.61           O
ANISOU  552  OG1 THR A  70     8328   7349   8871    303   -411    192       O
ATOM    553  CG2 THR A  70      -5.290  22.209  22.514  1.00 56.77           C
ANISOU  553  CG2 THR A  70     7372   6437   7760    153   -363    139       C
ATOM    554  N   PHE A  71      -5.849  19.654  25.101  1.00 55.32           N
ANISOU  554  N   PHE A  71     7448   6009   7561     50   -392    261       N
ATOM    555  CA  PHE A  71      -7.181  19.289  25.578  1.00 52.87           C
ANISOU  555  CA  PHE A  71     7194   5713   7181    -78   -356    251       C
ATOM    556  C   PHE A  71      -7.365  19.627  27.053  1.00 47.08           C
ANISOU  556  C   PHE A  71     6497   5004   6387   -109   -393    329       C
ATOM    557  O   PHE A  71      -8.269  20.388  27.417  1.00 41.31           O
ANISOU  557  O   PHE A  71     5723   4389   5583   -170   -380    311       O
ATOM    558  CB  PHE A  71      -7.467  17.802  25.375  1.00 62.63           C
ANISOU  558  CB  PHE A  71     8545   6812   8439   -137   -317    238       C
ATOM    559  CG  PHE A  71      -8.773  17.375  26.000  1.00 65.52           C
ANISOU  559  CG  PHE A  71     8972   7194   8729   -293   -276    238       C
ATOM    560  CD1 PHE A  71      -9.980  17.694  25.387  1.00 63.08           C
ANISOU  560  CD1 PHE A  71     8590   7011   8366   -391   -225    151       C
ATOM    561  CD2 PHE A  71      -8.801  16.715  27.221  1.00 62.14           C
ANISOU  561  CD2 PHE A  71     8664   6675   8272   -340   -289    327       C
ATOM    562  CE1 PHE A  71     -11.188  17.336  25.959  1.00 64.86           C
ANISOU  562  CE1 PHE A  71     8848   7281   8516   -543   -184    143       C
ATOM    563  CE2 PHE A  71     -10.010  16.348  27.800  1.00 68.00           C
ANISOU  563  CE2 PHE A  71     9456   7448   8935   -500   -242    327       C
ATOM    564  CZ  PHE A  71     -11.204  16.659  27.169  1.00 68.06           C
ANISOU  564  CZ  PHE A  71     9374   7591   8893   -606   -187    231       C
ATOM    565  N   TYR A  72      -6.549  19.028  27.930  1.00 45.17           N
ANISOU  565  N   TYR A  72     6338   4658   6166    -62   -439    414       N
ATOM    566  CA  TYR A  72      -6.785  19.239  29.355  1.00 46.50           C
ANISOU  566  CA  TYR A  72     6554   4851   6262   -100   -471    489       C
ATOM    567  C   TYR A  72      -6.482  20.678  29.771  1.00 51.99           C
ANISOU  567  C   TYR A  72     7154   5672   6929    -54   -518    491       C
ATOM    568  O   TYR A  72      -7.188  21.235  30.624  1.00 45.82           O
ANISOU  568  O   TYR A  72     6373   4973   6065   -112   -518    502       O
ATOM    569  CB  TYR A  72      -5.978  18.259  30.202  1.00 45.09           C
ANISOU  569  CB  TYR A  72     6496   4536   6101    -50   -517    586       C
ATOM    570  CG  TYR A  72      -6.500  18.237  31.615  1.00 50.51           C
ANISOU  570  CG  TYR A  72     7258   5243   6692   -123   -531    661       C
ATOM    571  CD1 TYR A  72      -7.698  17.598  31.919  1.00 52.36           C
ANISOU  571  CD1 TYR A  72     7574   5461   6860   -268   -466    663       C
ATOM    572  CD2 TYR A  72      -5.838  18.928  32.635  1.00 49.39           C
ANISOU  572  CD2 TYR A  72     7095   5157   6514    -59   -606    722       C
ATOM    573  CE1 TYR A  72      -8.205  17.613  33.207  1.00 58.84           C
ANISOU  573  CE1 TYR A  72     8457   6319   7579   -343   -469    730       C
ATOM    574  CE2 TYR A  72      -6.328  18.936  33.923  1.00 48.98           C
ANISOU  574  CE2 TYR A  72     7112   5138   6361   -125   -616    786       C
ATOM    575  CZ  TYR A  72      -7.512  18.277  34.202  1.00 53.67           C
ANISOU  575  CZ  TYR A  72     7790   5716   6888   -265   -544    793       C
ATOM    576  OH  TYR A  72      -8.013  18.291  35.472  1.00 50.03           O
ANISOU  576  OH  TYR A  72     7393   5301   6316   -337   -546    857       O
ATOM    577  N   GLY A  73      -5.468  21.302  29.168  1.00 49.16           N
ANISOU  577  N   GLY A  73     6715   5331   6634     43   -552    475       N
ATOM    578  CA  GLY A  73      -5.150  22.676  29.513  1.00 45.72           C
ANISOU  578  CA  GLY A  73     6203   4995   6174     72   -594    472       C
ATOM    579  C   GLY A  73      -6.274  23.631  29.171  1.00 48.91           C
ANISOU  579  C   GLY A  73     6558   5506   6520     18   -553    406       C
ATOM    580  O   GLY A  73      -6.574  24.550  29.942  1.00 40.15           O
ANISOU  580  O   GLY A  73     5438   4470   5348      5   -576    410       O
ATOM    581  N   CYS A  74      -6.913  23.425  28.010  1.00 39.11           N
ANISOU  581  N   CYS A  74     5287   4280   5294     -6   -493    341       N
ATOM    582  CA  CYS A  74      -8.052  24.263  27.654  1.00 42.26           C
ANISOU  582  CA  CYS A  74     5635   4791   5629    -42   -458    277       C
ATOM    583  C   CYS A  74      -9.212  24.043  28.609  1.00 41.89           C
ANISOU  583  C   CYS A  74     5625   4799   5494   -127   -435    280       C
ATOM    584  O   CYS A  74      -9.958  24.989  28.894  1.00 43.56           O
ANISOU  584  O   CYS A  74     5796   5118   5635   -130   -431    248       O
ATOM    585  CB  CYS A  74      -8.470  24.014  26.193  1.00 42.86           C
ANISOU  585  CB  CYS A  74     5668   4885   5731    -46   -406    206       C
ATOM    586  SG  CYS A  74      -7.376  24.946  25.004  1.00 51.61           S
ANISOU  586  SG  CYS A  74     6707   6000   6902     53   -422    188       S
ATOM    587  N   ALA A  75      -9.345  22.828  29.152  1.00 41.06           N
ANISOU  587  N   ALA A  75     5599   4619   5384   -192   -419    322       N
ATOM    588  CA  ALA A  75     -10.401  22.572  30.133  1.00 42.55           C
ANISOU  588  CA  ALA A  75     5824   4864   5479   -291   -390    334       C
ATOM    589  C   ALA A  75     -10.144  23.316  31.444  1.00 43.27           C
ANISOU  589  C   ALA A  75     5931   4997   5510   -264   -439    385       C
ATOM    590  O   ALA A  75     -11.068  23.891  32.032  1.00 41.27           O
ANISOU  590  O   ALA A  75     5652   4860   5167   -304   -419    358       O
ATOM    591  CB  ALA A  75     -10.522  21.073  30.389  1.00 40.99           C
ANISOU  591  CB  ALA A  75     5731   4552   5290   -377   -360    377       C
ATOM    592  N   VAL A  76      -8.900  23.300  31.932  1.00 41.81           N
ANISOU  592  N   VAL A  76     5785   4731   5369   -194   -506    452       N
ATOM    593  CA  VAL A  76      -8.561  24.077  33.125  1.00 40.99           C
ANISOU  593  CA  VAL A  76     5692   4675   5207   -167   -562    490       C
ATOM    594  C   VAL A  76      -8.756  25.572  32.862  1.00 38.28           C
ANISOU  594  C   VAL A  76     5269   4431   4844   -122   -572    423       C
ATOM    595  O   VAL A  76      -9.364  26.295  33.660  1.00 40.84           O
ANISOU  595  O   VAL A  76     5591   4845   5080   -137   -574    404       O
ATOM    596  CB  VAL A  76      -7.123  23.758  33.563  1.00 40.87           C
ANISOU  596  CB  VAL A  76     5715   4567   5245    -95   -638    566       C
ATOM    597  CG1 VAL A  76      -6.704  24.687  34.683  1.00 41.28           C
ANISOU  597  CG1 VAL A  76     5764   4682   5238    -67   -704    589       C
ATOM    598  CG2 VAL A  76      -7.009  22.262  33.987  1.00 35.28           C
ANISOU  598  CG2 VAL A  76     5117   3747   4541   -125   -632    644       C
ATOM    599  N   LEU A  77      -8.241  26.058  31.738  1.00 40.14           N
ANISOU  599  N   LEU A  77     5448   4648   5155    -64   -577    385       N
ATOM    600  CA  LEU A  77      -8.406  27.471  31.406  1.00 37.35           C
ANISOU  600  CA  LEU A  77     5042   4364   4783    -20   -586    329       C
ATOM    601  C   LEU A  77      -9.881  27.840  31.316  1.00 37.69           C
ANISOU  601  C   LEU A  77     5060   4517   4745    -48   -532    264       C
ATOM    602  O   LEU A  77     -10.313  28.860  31.867  1.00 39.49           O
ANISOU  602  O   LEU A  77     5283   4817   4905    -23   -544    233       O
ATOM    603  CB  LEU A  77      -7.699  27.778  30.089  1.00 40.41           C
ANISOU  603  CB  LEU A  77     5383   4713   5258     31   -585    307       C
ATOM    604  CG  LEU A  77      -7.814  29.207  29.567  1.00 40.48           C
ANISOU  604  CG  LEU A  77     5360   4769   5253     76   -590    259       C
ATOM    605  CD1 LEU A  77      -7.185  30.177  30.562  1.00 34.18           C
ANISOU  605  CD1 LEU A  77     4588   3967   4430     91   -651    276       C
ATOM    606  CD2 LEU A  77      -7.119  29.287  28.240  1.00 37.51           C
ANISOU  606  CD2 LEU A  77     4944   4353   4954    109   -578    249       C
ATOM    607  N   ARG A  78     -10.676  27.016  30.615  1.00 38.94           N
ANISOU  607  N   ARG A  78     5196   4695   4904    -97   -473    236       N
ATOM    608  CA  ARG A  78     -12.112  27.273  30.550  1.00 37.77           C
ANISOU  608  CA  ARG A  78     5001   4678   4671   -128   -423    169       C
ATOM    609  C   ARG A  78     -12.705  27.313  31.948  1.00 37.10           C
ANISOU  609  C   ARG A  78     4945   4664   4489   -175   -418    184       C
ATOM    610  O   ARG A  78     -13.616  28.105  32.227  1.00 40.39           O
ANISOU  610  O   ARG A  78     5319   5205   4823   -153   -401    127       O
ATOM    611  CB  ARG A  78     -12.812  26.191  29.701  1.00 39.78           C
ANISOU  611  CB  ARG A  78     5231   4945   4940   -203   -363    136       C
ATOM    612  CG  ARG A  78     -13.981  26.655  28.842  1.00 45.95           C
ANISOU  612  CG  ARG A  78     5923   5865   5672   -192   -324     45       C
ATOM    613  CD  ARG A  78     -14.247  25.664  27.669  1.00 39.56           C
ANISOU  613  CD  ARG A  78     5089   5039   4905   -250   -282      8       C
ATOM    614  NE  ARG A  78     -14.050  24.310  28.123  1.00 52.39           N
ANISOU  614  NE  ARG A  78     6786   6564   6555   -356   -261     55       N
ATOM    615  CZ  ARG A  78     -13.267  23.415  27.543  1.00 43.83           C
ANISOU  615  CZ  ARG A  78     5754   5343   5556   -366   -262     79       C
ATOM    616  NH1 ARG A  78     -12.602  23.697  26.414  1.00 43.67           N
ANISOU  616  NH1 ARG A  78     5705   5285   5603   -284   -277     56       N
ATOM    617  NH2 ARG A  78     -13.177  22.220  28.102  1.00 40.60           N
ANISOU  617  NH2 ARG A  78     5432   4835   5158   -456   -244    126       N
ATOM    618  N   GLN A  79     -12.200  26.464  32.857  1.00 36.69           N
ANISOU  618  N   GLN A  79     4967   4538   4436   -230   -433    261       N
ATOM    619  CA  GLN A  79     -12.736  26.486  34.214  1.00 38.88           C
ANISOU  619  CA  GLN A  79     5277   4889   4607   -280   -426    281       C
ATOM    620  C   GLN A  79     -12.429  27.817  34.904  1.00 43.94           C
ANISOU  620  C   GLN A  79     5916   5575   5205   -198   -478    263       C
ATOM    621  O   GLN A  79     -13.297  28.393  35.572  1.00 38.74           O
ANISOU  621  O   GLN A  79     5237   5036   4444   -200   -455    218       O
ATOM    622  CB  GLN A  79     -12.199  25.302  35.027  1.00 41.10           C
ANISOU  622  CB  GLN A  79     5656   5072   4890   -347   -437    380       C
ATOM    623  CG  GLN A  79     -12.873  25.143  36.388  1.00 40.83           C
ANISOU  623  CG  GLN A  79     5663   5120   4728   -422   -414    409       C
ATOM    624  CD  GLN A  79     -14.258  24.495  36.308  1.00 44.66           C
ANISOU  624  CD  GLN A  79     6121   5704   5145   -547   -320    372       C
ATOM    625  OE1 GLN A  79     -14.798  24.270  35.224  1.00 46.85           O
ANISOU  625  OE1 GLN A  79     6336   6003   5464   -572   -277    312       O
ATOM    626  NE2 GLN A  79     -14.832  24.193  37.465  1.00 40.06           N
ANISOU  626  NE2 GLN A  79     5580   5194   4449   -634   -287    407       N
ATOM    627  N   PHE A  80     -11.202  28.330  34.754  1.00 37.16           N
ANISOU  627  N   PHE A  80     5077   4625   4419   -128   -545    289       N
ATOM    628  CA  PHE A  80     -10.911  29.659  35.293  1.00 36.45           C
ANISOU  628  CA  PHE A  80     4992   4565   4292    -62   -594    258       C
ATOM    629  C   PHE A  80     -11.866  30.697  34.715  1.00 39.38           C
ANISOU  629  C   PHE A  80     5312   5024   4625     -6   -561    166       C
ATOM    630  O   PHE A  80     -12.314  31.603  35.423  1.00 39.13           O
ANISOU  630  O   PHE A  80     5292   5065   4513     31   -569    120       O
ATOM    631  CB  PHE A  80      -9.476  30.071  34.978  1.00 31.73           C
ANISOU  631  CB  PHE A  80     4406   3864   3786    -14   -662    287       C
ATOM    632  CG  PHE A  80      -8.447  29.595  35.994  1.00 38.56           C
ANISOU  632  CG  PHE A  80     5320   4679   4652    -30   -726    363       C
ATOM    633  CD1 PHE A  80      -7.589  28.553  35.679  1.00 38.48           C
ANISOU  633  CD1 PHE A  80     5318   4582   4721    -35   -744    430       C
ATOM    634  CD2 PHE A  80      -8.304  30.229  37.232  1.00 38.99           C
ANISOU  634  CD2 PHE A  80     5413   4778   4624    -28   -773    362       C
ATOM    635  CE1 PHE A  80      -6.628  28.122  36.590  1.00 46.98           C
ANISOU  635  CE1 PHE A  80     6435   5622   5792    -29   -812    502       C
ATOM    636  CE2 PHE A  80      -7.345  29.811  38.142  1.00 42.05           C
ANISOU  636  CE2 PHE A  80     5840   5135   5002    -36   -840    431       C
ATOM    637  CZ  PHE A  80      -6.498  28.763  37.824  1.00 45.42           C
ANISOU  637  CZ  PHE A  80     6269   5481   5508    -32   -863    504       C
ATOM    638  N   GLU A  81     -12.155  30.604  33.411  1.00 38.49           N
ANISOU  638  N   GLU A  81     5149   4908   4567     13   -529    135       N
ATOM    639  CA  GLU A  81     -13.047  31.586  32.792  1.00 36.04           C
ANISOU  639  CA  GLU A  81     4794   4684   4218     87   -506     54       C
ATOM    640  C   GLU A  81     -14.440  31.529  33.399  1.00 42.41           C
ANISOU  640  C   GLU A  81     5557   5646   4909     67   -456     -0       C
ATOM    641  O   GLU A  81     -15.040  32.575  33.669  1.00 47.19           O
ANISOU  641  O   GLU A  81     6153   6332   5444    147   -458    -63       O
ATOM    642  CB  GLU A  81     -13.110  31.368  31.274  1.00 35.11           C
ANISOU  642  CB  GLU A  81     4627   4546   4167    106   -482     36       C
ATOM    643  CG  GLU A  81     -11.764  31.588  30.596  1.00 41.88           C
ANISOU  643  CG  GLU A  81     5514   5272   5128    134   -523     78       C
ATOM    644  CD  GLU A  81     -11.797  31.270  29.098  1.00 46.16           C
ANISOU  644  CD  GLU A  81     6011   5801   5726    148   -494     63       C
ATOM    645  OE1 GLU A  81     -12.895  31.211  28.507  1.00 53.12           O
ANISOU  645  OE1 GLU A  81     6841   6781   6562    159   -454      8       O
ATOM    646  OE2 GLU A  81     -10.717  31.052  28.526  1.00 48.58           O
ANISOU  646  OE2 GLU A  81     6328   6012   6117    146   -511    101       O
ATOM    647  N   MET A  82     -14.971  30.315  33.638  1.00 44.34           N
ANISOU  647  N   MET A  82     5781   5937   5129    -41   -407     21       N
ATOM    648  CA  MET A  82     -16.286  30.205  34.267  1.00 44.34           C
ANISOU  648  CA  MET A  82     5728   6107   5013    -82   -350    -29       C
ATOM    649  C   MET A  82     -16.295  30.840  35.646  1.00 45.76           C
ANISOU  649  C   MET A  82     5952   6334   5103    -60   -370    -31       C
ATOM    650  O   MET A  82     -17.348  31.254  36.136  1.00 48.38           O
ANISOU  650  O   MET A  82     6232   6823   5328    -41   -331    -98       O
ATOM    651  CB  MET A  82     -16.725  28.737  34.403  1.00 50.87           C
ANISOU  651  CB  MET A  82     6547   6953   5827   -234   -293      7       C
ATOM    652  CG  MET A  82     -16.395  27.799  33.247  1.00 59.31           C
ANISOU  652  CG  MET A  82     7613   7925   6997   -284   -281     28       C
ATOM    653  SD  MET A  82     -17.561  27.878  31.868  1.00 74.90           S
ANISOU  653  SD  MET A  82     9461  10037   8960   -272   -233    -76       S
ATOM    654  CE  MET A  82     -16.690  28.931  30.700  1.00 68.55           C
ANISOU  654  CE  MET A  82     8661   9139   8245   -114   -294    -87       C
ATOM    655  N   MET A  83     -15.150  30.877  36.310  1.00 44.41           N
ANISOU  655  N   MET A  83     5867   6042   4964    -62   -428     36       N
ATOM    656  CA  MET A  83     -15.079  31.455  37.640  1.00 47.06           C
ANISOU  656  CA  MET A  83     6252   6420   5208    -46   -453     32       C
ATOM    657  C   MET A  83     -14.910  32.964  37.609  1.00 48.13           C
ANISOU  657  C   MET A  83     6404   6548   5335     80   -498    -37       C
ATOM    658  O   MET A  83     -14.793  33.578  38.672  1.00 47.13           O
ANISOU  658  O   MET A  83     6326   6447   5133    104   -525    -56       O
ATOM    659  CB  MET A  83     -13.926  30.829  38.419  1.00 41.34           C
ANISOU  659  CB  MET A  83     5613   5585   4510   -102   -505    132       C
ATOM    660  CG  MET A  83     -14.113  29.341  38.675  1.00 55.44           C
ANISOU  660  CG  MET A  83     7419   7362   6286   -224   -463    209       C
ATOM    661  SD  MET A  83     -12.579  28.578  39.258  1.00 58.36           S
ANISOU  661  SD  MET A  83     7890   7573   6713   -247   -540    334       S
ATOM    662  CE  MET A  83     -12.053  29.687  40.562  1.00 65.57           C
ANISOU  662  CE  MET A  83     8848   8526   7540   -190   -613    319       C
ATOM    663  N   GLY A  84     -14.889  33.569  36.430  1.00 50.89           N
ANISOU  663  N   GLY A  84     6727   6856   5752    159   -505    -74       N
ATOM    664  CA  GLY A  84     -14.723  35.004  36.335  1.00 50.59           C
ANISOU  664  CA  GLY A  84     6731   6784   5708    276   -546   -133       C
ATOM    665  C   GLY A  84     -13.287  35.464  36.302  1.00 48.06           C
ANISOU  665  C   GLY A  84     6487   6302   5471    277   -618    -88       C
ATOM    666  O   GLY A  84     -13.041  36.672  36.394  1.00 51.07           O
ANISOU  666  O   GLY A  84     6927   6635   5843    350   -655   -133       O
ATOM    667  N   VAL A  85     -12.333  34.545  36.176  1.00 43.88           N
ANISOU  667  N   VAL A  85     5961   5690   5022    198   -639     -5       N
ATOM    668  CA  VAL A  85     -10.925  34.914  36.049  1.00 42.75           C
ANISOU  668  CA  VAL A  85     5864   5417   4962    193   -705     35       C
ATOM    669  C   VAL A  85     -10.646  35.348  34.610  1.00 49.51           C
ANISOU  669  C   VAL A  85     6702   6202   5907    236   -699     27       C
ATOM    670  O   VAL A  85     -11.008  34.649  33.652  1.00 44.88           O
ANISOU  670  O   VAL A  85     6061   5632   5361    229   -656     39       O
ATOM    671  CB  VAL A  85     -10.026  33.746  36.474  1.00 42.66           C
ANISOU  671  CB  VAL A  85     5853   5362   4994    113   -731    124       C
ATOM    672  CG1 VAL A  85      -8.584  34.157  36.388  1.00 41.29           C
ANISOU  672  CG1 VAL A  85     5702   5088   4898    111   -802    154       C
ATOM    673  CG2 VAL A  85     -10.358  33.326  37.914  1.00 39.57           C
ANISOU  673  CG2 VAL A  85     5492   5045   4496     70   -736    141       C
ATOM    674  N   PHE A  86     -10.001  36.506  34.454  1.00 42.96           N
ANISOU  674  N   PHE A  86     5928   5293   5102    273   -740      5       N
ATOM    675  CA  PHE A  86      -9.769  37.084  33.122  1.00 38.44           C
ANISOU  675  CA  PHE A  86     5357   4651   4595    315   -731      1       C
ATOM    676  C   PHE A  86      -8.628  36.361  32.407  1.00 35.72           C
ANISOU  676  C   PHE A  86     4975   4238   4358    255   -741     68       C
ATOM    677  O   PHE A  86      -7.506  36.342  32.922  1.00 36.66           O
ANISOU  677  O   PHE A  86     5108   4307   4514    204   -790    102       O
ATOM    678  CB  PHE A  86      -9.450  38.571  33.243  1.00 40.88           C
ANISOU  678  CB  PHE A  86     5759   4883   4889    358   -768    -41       C
ATOM    679  CG  PHE A  86      -9.264  39.252  31.924  1.00 47.76           C
ANISOU  679  CG  PHE A  86     6656   5679   5811    400   -756    -38       C
ATOM    680  CD1 PHE A  86     -10.359  39.747  31.215  1.00 48.92           C
ANISOU  680  CD1 PHE A  86     6812   5862   5913    504   -721    -79       C
ATOM    681  CD2 PHE A  86      -8.002  39.392  31.385  1.00 42.65           C
ANISOU  681  CD2 PHE A  86     6019   4936   5249    336   -778      8       C
ATOM    682  CE1 PHE A  86     -10.185  40.378  29.983  1.00 48.90           C
ANISOU  682  CE1 PHE A  86     6847   5788   5945    547   -711    -66       C
ATOM    683  CE2 PHE A  86      -7.814  40.008  30.158  1.00 46.32           C
ANISOU  683  CE2 PHE A  86     6515   5334   5752    363   -759     19       C
ATOM    684  CZ  PHE A  86      -8.908  40.505  29.454  1.00 45.57           C
ANISOU  684  CZ  PHE A  86     6446   5261   5606    469   -727    -13       C
ATOM    685  N   PRO A  87      -8.857  35.768  31.239  1.00 38.48           N
ANISOU  685  N   PRO A  87     5272   4596   4753    264   -698     82       N
ATOM    686  CA  PRO A  87      -7.770  35.033  30.568  1.00 35.57           C
ANISOU  686  CA  PRO A  87     4863   4169   4481    218   -702    137       C
ATOM    687  C   PRO A  87      -6.996  35.899  29.583  1.00 39.93           C
ANISOU  687  C   PRO A  87     5433   4650   5088    229   -708    142       C
ATOM    688  O   PRO A  87      -7.560  36.740  28.880  1.00 39.32           O
ANISOU  688  O   PRO A  87     5389   4568   4985    283   -687    111       O
ATOM    689  CB  PRO A  87      -8.529  33.922  29.829  1.00 37.94           C
ANISOU  689  CB  PRO A  87     5105   4520   4789    216   -647    137       C
ATOM    690  CG  PRO A  87      -9.862  34.632  29.436  1.00 37.05           C
ANISOU  690  CG  PRO A  87     4994   4481   4602    284   -614     74       C
ATOM    691  CD  PRO A  87     -10.157  35.619  30.547  1.00 37.66           C
ANISOU  691  CD  PRO A  87     5130   4573   4606    315   -644     41       C
ATOM    692  N   LEU A  88      -5.678  35.680  29.517  1.00 36.99           N
ANISOU  692  N   LEU A  88     5037   4229   4788    178   -736    183       N
ATOM    693  CA  LEU A  88      -4.860  36.435  28.562  1.00 40.97           C
ANISOU  693  CA  LEU A  88     5549   4676   5343    165   -732    192       C
ATOM    694  C   LEU A  88      -5.298  36.152  27.126  1.00 44.56           C
ANISOU  694  C   LEU A  88     5973   5142   5816    202   -674    192       C
ATOM    695  O   LEU A  88      -5.510  37.079  26.334  1.00 37.83           O
ANISOU  695  O   LEU A  88     5166   4262   4945    232   -655    182       O
ATOM    696  CB  LEU A  88      -3.377  36.092  28.735  1.00 37.42           C
ANISOU  696  CB  LEU A  88     5048   4205   4964    102   -767    231       C
ATOM    697  CG  LEU A  88      -2.452  36.846  27.767  1.00 41.05           C
ANISOU  697  CG  LEU A  88     5502   4621   5472     65   -755    241       C
ATOM    698  CD1 LEU A  88      -2.443  38.340  28.088  1.00 39.20           C
ANISOU  698  CD1 LEU A  88     5368   4327   5198     39   -778    215       C
ATOM    699  CD2 LEU A  88      -1.033  36.264  27.751  1.00 40.87           C
ANISOU  699  CD2 LEU A  88     5389   4617   5524     13   -777    273       C
ATOM    700  N   ASN A  89      -5.390  34.867  26.770  1.00 40.99           N
ANISOU  700  N   ASN A  89     5453   4726   5396    200   -647    206       N
ATOM    701  CA  ASN A  89      -6.085  34.378  25.583  1.00 39.70           C
ANISOU  701  CA  ASN A  89     5257   4597   5230    234   -592    189       C
ATOM    702  C   ASN A  89      -7.233  33.487  26.037  1.00 37.31           C
ANISOU  702  C   ASN A  89     4936   4357   4883    241   -575    165       C
ATOM    703  O   ASN A  89      -7.090  32.750  27.020  1.00 40.93           O
ANISOU  703  O   ASN A  89     5391   4815   5346    205   -594    183       O
ATOM    704  CB  ASN A  89      -5.130  33.575  24.675  1.00 34.20           C
ANISOU  704  CB  ASN A  89     4501   3884   4612    213   -569    214       C
ATOM    705  CG  ASN A  89      -4.209  34.483  23.866  1.00 37.62           C
ANISOU  705  CG  ASN A  89     4940   4281   5073    200   -563    232       C
ATOM    706  OD1 ASN A  89      -4.620  35.558  23.425  1.00 39.69           O
ANISOU  706  OD1 ASN A  89     5259   4531   5292    223   -554    223       O
ATOM    707  ND2 ASN A  89      -2.969  34.060  23.684  1.00 32.41           N
ANISOU  707  ND2 ASN A  89     4223   3609   4481    165   -566    258       N
ATOM    708  N   GLU A  90      -8.366  33.552  25.342  1.00 37.99           N
ANISOU  708  N   GLU A  90     5009   4506   4919    282   -538    124       N
ATOM    709  CA  GLU A  90      -9.525  32.735  25.711  1.00 36.86           C
ANISOU  709  CA  GLU A  90     4835   4443   4727    269   -514     92       C
ATOM    710  C   GLU A  90      -9.331  31.299  25.243  1.00 39.51           C
ANISOU  710  C   GLU A  90     5130   4768   5115    217   -484    101       C
ATOM    711  O   GLU A  90      -8.769  31.054  24.171  1.00 34.41           O
ANISOU  711  O   GLU A  90     4462   4092   4519    225   -467    106       O
ATOM    712  CB  GLU A  90     -10.805  33.305  25.094  1.00 40.36           C
ANISOU  712  CB  GLU A  90     5262   4979   5094    334   -490     36       C
ATOM    713  CG  GLU A  90     -11.296  34.589  25.769  1.00 40.59           C
ANISOU  713  CG  GLU A  90     5342   5027   5054    401   -517     13       C
ATOM    714  CD  GLU A  90     -12.486  35.234  25.064  1.00 49.87           C
ANISOU  714  CD  GLU A  90     6500   6296   6151    497   -501    -41       C
ATOM    715  OE1 GLU A  90     -12.789  34.896  23.890  1.00 53.46           O
ANISOU  715  OE1 GLU A  90     6910   6795   6607    514   -476    -54       O
ATOM    716  OE2 GLU A  90     -13.133  36.078  25.703  1.00 57.90           O
ANISOU  716  OE2 GLU A  90     7549   7351   7101    564   -517    -74       O
ATOM    717  N   SER A  91      -9.824  30.340  26.042  1.00 35.77           N
ANISOU  717  N   SER A  91     4653   4315   4622    163   -474    102       N
ATOM    718  CA  SER A  91      -9.701  28.927  25.660  1.00 37.10           C
ANISOU  718  CA  SER A  91     4808   4451   4838    111   -445    109       C
ATOM    719  C   SER A  91     -10.310  28.634  24.283  1.00 35.40           C
ANISOU  719  C   SER A  91     4547   4285   4618    117   -401     54       C
ATOM    720  O   SER A  91      -9.810  27.769  23.552  1.00 35.40           O
ANISOU  720  O   SER A  91     4541   4234   4676    100   -381     54       O
ATOM    721  CB  SER A  91     -10.358  28.022  26.712  1.00 39.42           C
ANISOU  721  CB  SER A  91     5124   4762   5092     38   -433    118       C
ATOM    722  OG  SER A  91     -11.739  28.307  26.798  1.00 52.84           O
ANISOU  722  OG  SER A  91     6790   6583   6704     24   -403     62       O
ATOM    723  N   VAL A  92     -11.420  29.285  23.925  1.00 36.81           N
ANISOU  723  N   VAL A  92     4693   4572   4722    147   -386      1       N
ATOM    724  CA  VAL A  92     -11.996  28.995  22.606  1.00 48.43           C
ANISOU  724  CA  VAL A  92     6115   6108   6179    155   -352    -53       C
ATOM    725  C   VAL A  92     -11.016  29.379  21.509  1.00 47.20           C
ANISOU  725  C   VAL A  92     5965   5895   6074    207   -355    -35       C
ATOM    726  O   VAL A  92     -10.845  28.650  20.523  1.00 47.70           O
ANISOU  726  O   VAL A  92     6007   5952   6166    191   -327    -59       O
ATOM    727  CB  VAL A  92     -13.345  29.701  22.401  1.00 44.78           C
ANISOU  727  CB  VAL A  92     5605   5792   5618    200   -346   -113       C
ATOM    728  CG1 VAL A  92     -14.415  29.066  23.282  1.00 49.45           C
ANISOU  728  CG1 VAL A  92     6164   6472   6153    124   -324   -147       C
ATOM    729  CG2 VAL A  92     -13.203  31.185  22.668  1.00 39.43           C
ANISOU  729  CG2 VAL A  92     4963   5109   4908    298   -382    -93       C
ATOM    730  N   ALA A  93     -10.336  30.516  21.678  1.00 39.97           N
ANISOU  730  N   ALA A  93     5084   4937   5167    261   -386      6       N
ATOM    731  CA  ALA A  93      -9.432  30.984  20.635  1.00 41.48           C
ANISOU  731  CA  ALA A  93     5281   5086   5395    296   -381     27       C
ATOM    732  C   ALA A  93      -8.177  30.135  20.579  1.00 41.54           C
ANISOU  732  C   ALA A  93     5281   5009   5492    258   -376     59       C
ATOM    733  O   ALA A  93      -7.664  29.857  19.488  1.00 41.79           O
ANISOU  733  O   ALA A  93     5290   5036   5553    268   -348     51       O
ATOM    734  CB  ALA A  93      -9.086  32.459  20.850  1.00 38.67           C
ANISOU  734  CB  ALA A  93     4976   4700   5017    345   -411     60       C
ATOM    735  N   ILE A  94      -7.664  29.699  21.736  1.00 39.18           N
ANISOU  735  N   ILE A  94     5001   4654   5233    224   -403     94       N
ATOM    736  CA  ILE A  94      -6.504  28.801  21.724  1.00 37.46           C
ANISOU  736  CA  ILE A  94     4772   4364   5098    210   -404    121       C
ATOM    737  C   ILE A  94      -6.860  27.492  21.036  1.00 44.17           C
ANISOU  737  C   ILE A  94     5608   5209   5965    191   -363     80       C
ATOM    738  O   ILE A  94      -6.074  26.945  20.250  1.00 42.46           O
ANISOU  738  O   ILE A  94     5370   4960   5801    209   -342     73       O
ATOM    739  CB  ILE A  94      -5.996  28.532  23.152  1.00 39.83           C
ANISOU  739  CB  ILE A  94     5099   4613   5421    188   -450    169       C
ATOM    740  CG1 ILE A  94      -5.452  29.810  23.798  1.00 41.98           C
ANISOU  740  CG1 ILE A  94     5386   4883   5683    198   -494    200       C
ATOM    741  CG2 ILE A  94      -4.916  27.431  23.133  1.00 42.20           C
ANISOU  741  CG2 ILE A  94     5389   4846   5801    196   -454    194       C
ATOM    742  CD1 ILE A  94      -5.174  29.638  25.289  1.00 45.33           C
ANISOU  742  CD1 ILE A  94     5839   5281   6103    177   -544    238       C
ATOM    743  N   ALA A  95      -8.024  26.932  21.384  1.00 43.11           N
ANISOU  743  N   ALA A  95     5487   5109   5785    147   -349     48       N
ATOM    744  CA  ALA A  95      -8.440  25.668  20.787  1.00 48.73           C
ANISOU  744  CA  ALA A  95     6199   5807   6508    107   -309      1       C
ATOM    745  C   ALA A  95      -8.590  25.816  19.286  1.00 43.78           C
ANISOU  745  C   ALA A  95     5530   5237   5866    135   -275    -55       C
ATOM    746  O   ALA A  95      -8.167  24.945  18.521  1.00 44.43           O
ANISOU  746  O   ALA A  95     5612   5279   5991    134   -247    -85       O
ATOM    747  CB  ALA A  95      -9.760  25.185  21.409  1.00 42.10           C
ANISOU  747  CB  ALA A  95     5372   5017   5609     31   -295    -29       C
ATOM    748  N   ARG A  96      -9.191  26.921  18.852  1.00 46.15           N
ANISOU  748  N   ARG A  96     5803   5631   6101    169   -279    -71       N
ATOM    749  CA  ARG A  96      -9.349  27.180  17.428  1.00 47.18           C
ANISOU  749  CA  ARG A  96     5900   5827   6199    205   -252   -114       C
ATOM    750  C   ARG A  96      -7.994  27.240  16.732  1.00 55.28           C
ANISOU  750  C   ARG A  96     6924   6796   7285    241   -240    -86       C
ATOM    751  O   ARG A  96      -7.760  26.533  15.747  1.00 54.47           O
ANISOU  751  O   ARG A  96     6804   6696   7197    243   -205   -129       O
ATOM    752  CB  ARG A  96     -10.112  28.481  17.250  1.00 43.45           C
ANISOU  752  CB  ARG A  96     5418   5449   5644    257   -269   -115       C
ATOM    753  CG  ARG A  96     -10.345  28.915  15.828  1.00 50.51           C
ANISOU  753  CG  ARG A  96     6288   6419   6483    308   -251   -146       C
ATOM    754  CD  ARG A  96     -10.873  30.321  15.862  1.00 49.47           C
ANISOU  754  CD  ARG A  96     6175   6343   6278    381   -278   -123       C
ATOM    755  NE  ARG A  96     -12.276  30.364  16.244  1.00 48.80           N
ANISOU  755  NE  ARG A  96     6056   6368   6118    389   -291   -173       N
ATOM    756  CZ  ARG A  96     -12.747  31.073  17.260  1.00 51.27           C
ANISOU  756  CZ  ARG A  96     6386   6692   6401    417   -320   -158       C
ATOM    757  NH1 ARG A  96     -11.924  31.795  18.019  1.00 50.70           N
ANISOU  757  NH1 ARG A  96     6376   6518   6370    431   -342    -94       N
ATOM    758  NH2 ARG A  96     -14.040  31.051  17.530  1.00 47.43           N
ANISOU  758  NH2 ARG A  96     5850   6331   5840    427   -324   -213       N
ATOM    759  N   SER A  97      -7.066  28.048  17.272  1.00 44.92           N
ANISOU  759  N   SER A  97     5625   5437   6007    264   -267    -20       N
ATOM    760  CA  SER A  97      -5.781  28.270  16.624  1.00 43.62           C
ANISOU  760  CA  SER A  97     5440   5244   5887    288   -251      7       C
ATOM    761  C   SER A  97      -4.949  27.005  16.528  1.00 43.88           C
ANISOU  761  C   SER A  97     5456   5221   5997    287   -234     -8       C
ATOM    762  O   SER A  97      -4.088  26.910  15.651  1.00 47.44           O
ANISOU  762  O   SER A  97     5872   5680   6474    313   -203    -16       O
ATOM    763  CB  SER A  97      -4.979  29.347  17.371  1.00 41.92           C
ANISOU  763  CB  SER A  97     5240   4996   5693    289   -287     74       C
ATOM    764  OG  SER A  97      -4.466  28.829  18.586  1.00 47.31           O
ANISOU  764  OG  SER A  97     5927   5618   6431    270   -323    102       O
ATOM    765  N   ARG A  98      -5.155  26.033  17.411  1.00 43.32           N
ANISOU  765  N   ARG A  98     5412   5090   5959    263   -251    -11       N
ATOM    766  CA  ARG A  98      -4.342  24.827  17.322  1.00 41.52           C
ANISOU  766  CA  ARG A  98     5184   4789   5802    283   -238    -23       C
ATOM    767  C   ARG A  98      -4.916  23.808  16.350  1.00 45.24           C
ANISOU  767  C   ARG A  98     5667   5260   6261    271   -192   -103       C
ATOM    768  O   ARG A  98      -4.254  22.806  16.066  1.00 44.64           O
ANISOU  768  O   ARG A  98     5601   5119   6241    301   -174   -128       O
ATOM    769  CB  ARG A  98      -4.170  24.184  18.702  1.00 51.29           C
ANISOU  769  CB  ARG A  98     6468   5942   7079    270   -280     22       C
ATOM    770  CG  ARG A  98      -3.545  25.150  19.701  1.00 65.31           C
ANISOU  770  CG  ARG A  98     8230   7724   8861    279   -332     92       C
ATOM    771  CD  ARG A  98      -2.055  24.949  19.870  1.00 65.77           C
ANISOU  771  CD  ARG A  98     8249   7751   8990    332   -354    126       C
ATOM    772  NE  ARG A  98      -1.782  24.241  21.116  1.00 82.73           N
ANISOU  772  NE  ARG A  98    10439   9828  11166    342   -402    171       N
ATOM    773  CZ  ARG A  98      -1.394  24.823  22.248  1.00 84.21           C
ANISOU  773  CZ  ARG A  98    10626  10022  11348    336   -461    227       C
ATOM    774  NH1 ARG A  98      -1.214  26.139  22.312  1.00 89.30           N
ANISOU  774  NH1 ARG A  98    11234  10728  11967    311   -476    240       N
ATOM    775  NH2 ARG A  98      -1.185  24.079  23.322  1.00 81.08           N
ANISOU  775  NH2 ARG A  98    10277   9565  10966    352   -504    271       N
ATOM    776  N   ASP A  99      -6.126  24.043  15.849  1.00 43.17           N
ANISOU  776  N   ASP A  99     5403   5073   5925    233   -175   -151       N
ATOM    777  CA  ASP A  99      -6.757  23.216  14.815  1.00 43.68           C
ANISOU  777  CA  ASP A  99     5469   5165   5963    209   -134   -241       C
ATOM    778  C   ASP A  99      -6.375  23.864  13.479  1.00 41.05           C
ANISOU  778  C   ASP A  99     5087   4915   5594    259   -104   -264       C
ATOM    779  O   ASP A  99      -6.998  24.843  13.055  1.00 36.68           O
ANISOU  779  O   ASP A  99     4511   4459   4965    266   -109   -261       O
ATOM    780  CB  ASP A  99      -8.263  23.176  15.066  1.00 38.06           C
ANISOU  780  CB  ASP A  99     4763   4517   5179    137   -138   -280       C
ATOM    781  CG  ASP A  99      -9.043  22.319  14.057  1.00 46.65           C
ANISOU  781  CG  ASP A  99     5847   5649   6229     90   -101   -385       C
ATOM    782  OD1 ASP A  99      -8.490  21.910  13.012  1.00 48.37           O
ANISOU  782  OD1 ASP A  99     6059   5858   6461    123    -70   -432       O
ATOM    783  OD2 ASP A  99     -10.245  22.070  14.342  1.00 48.08           O
ANISOU  783  OD2 ASP A  99     6026   5885   6359     12   -101   -426       O
ATOM    784  N   LYS A 100      -5.313  23.358  12.841  1.00 43.71           N
ANISOU  784  N   LYS A 100     5410   5217   5980    304    -75   -281       N
ATOM    785  CA  LYS A 100      -4.788  24.076  11.682  1.00 46.87           C
ANISOU  785  CA  LYS A 100     5763   5701   6343    346    -42   -285       C
ATOM    786  C   LYS A 100      -5.794  24.107  10.537  1.00 47.03           C
ANISOU  786  C   LYS A 100     5777   5822   6270    331    -17   -359       C
ATOM    787  O   LYS A 100      -5.917  25.128   9.849  1.00 40.58           O
ANISOU  787  O   LYS A 100     4940   5097   5383    353    -11   -336       O
ATOM    788  CB  LYS A 100      -3.467  23.479  11.209  1.00 50.75           C
ANISOU  788  CB  LYS A 100     6227   6158   6899    399     -8   -301       C
ATOM    789  CG  LYS A 100      -2.700  24.421  10.245  1.00 69.22           C
ANISOU  789  CG  LYS A 100     8511   8589   9201    429     28   -278       C
ATOM    790  CD  LYS A 100      -2.346  25.785  10.911  1.00 80.07           C
ANISOU  790  CD  LYS A 100     9874   9977  10573    413     -5   -178       C
ATOM    791  CE  LYS A 100      -2.979  27.013  10.168  1.00 80.43           C
ANISOU  791  CE  LYS A 100     9934  10109  10516    400      5   -154       C
ATOM    792  NZ  LYS A 100      -2.681  28.375  10.770  1.00 67.24           N
ANISOU  792  NZ  LYS A 100     8280   8429   8838    380    -24    -62       N
ATOM    793  N   LEU A 101      -6.538  23.016  10.333  1.00 43.33           N
ANISOU  793  N   LEU A 101     5332   5340   5794    290     -5   -445       N
ATOM    794  CA  LEU A 101      -7.566  22.995   9.298  1.00 40.67           C
ANISOU  794  CA  LEU A 101     4977   5116   5360    268     10   -526       C
ATOM    795  C   LEU A 101      -8.583  24.096   9.526  1.00 47.16           C
ANISOU  795  C   LEU A 101     5780   6040   6100    263    -26   -490       C
ATOM    796  O   LEU A 101      -8.916  24.861   8.612  1.00 40.13           O
ANISOU  796  O   LEU A 101     4864   5263   5120    301    -23   -496       O
ATOM    797  CB  LEU A 101      -8.252  21.623   9.291  1.00 46.66           C
ANISOU  797  CB  LEU A 101     5769   5829   6129    197     22   -625       C
ATOM    798  CG  LEU A 101      -8.923  21.168   7.997  1.00 56.31           C
ANISOU  798  CG  LEU A 101     6974   7150   7270    172     49   -742       C
ATOM    799  CD1 LEU A 101      -9.151  19.661   7.944  1.00 52.43           C
ANISOU  799  CD1 LEU A 101     6539   6565   6818    102     73   -844       C
ATOM    800  CD2 LEU A 101     -10.217  21.895   7.794  1.00 57.88           C
ANISOU  800  CD2 LEU A 101     7127   7504   7362    145     21   -758       C
ATOM    801  N   ARG A 102      -9.120  24.158  10.744  1.00 41.62           N
ANISOU  801  N   ARG A 102     5093   5301   5419    224    -61   -456       N
ATOM    802  CA  ARG A 102     -10.153  25.130  11.066  1.00 39.21           C
ANISOU  802  CA  ARG A 102     4767   5094   5036    231    -96   -435       C
ATOM    803  C   ARG A 102      -9.603  26.549  11.017  1.00 34.51           C
ANISOU  803  C   ARG A 102     4178   4512   4421    307   -112   -346       C
ATOM    804  O   ARG A 102     -10.313  27.478  10.617  1.00 32.88           O
ANISOU  804  O   ARG A 102     3961   4405   4125    352   -130   -340       O
ATOM    805  CB  ARG A 102     -10.721  24.805  12.455  1.00 35.66           C
ANISOU  805  CB  ARG A 102     4333   4598   4617    170   -120   -419       C
ATOM    806  CG  ARG A 102     -11.779  25.750  12.999  1.00 36.67           C
ANISOU  806  CG  ARG A 102     4436   4828   4671    184   -154   -403       C
ATOM    807  CD  ARG A 102     -12.195  25.277  14.409  1.00 39.99           C
ANISOU  807  CD  ARG A 102     4874   5198   5122    111   -166   -388       C
ATOM    808  NE  ARG A 102     -13.104  26.251  14.995  1.00 43.32           N
ANISOU  808  NE  ARG A 102     5266   5720   5473    140   -195   -373       N
ATOM    809  CZ  ARG A 102     -13.311  26.396  16.296  1.00 40.24           C
ANISOU  809  CZ  ARG A 102     4894   5302   5095    114   -212   -335       C
ATOM    810  NH1 ARG A 102     -12.678  25.602  17.153  1.00 39.24           N
ANISOU  810  NH1 ARG A 102     4818   5048   5045     54   -206   -298       N
ATOM    811  NH2 ARG A 102     -14.165  27.318  16.721  1.00 43.17           N
ANISOU  811  NH2 ARG A 102     5233   5777   5392    158   -236   -336       N
ATOM    812  N   SER A 103      -8.347  26.741  11.444  1.00 35.03           N
ANISOU  812  N   SER A 103     4265   4478   4566    321   -108   -278       N
ATOM    813  CA  SER A 103      -7.737  28.074  11.394  1.00 40.53           C
ANISOU  813  CA  SER A 103     4977   5174   5247    367   -118   -196       C
ATOM    814  C   SER A 103      -7.608  28.570   9.961  1.00 33.82           C
ANISOU  814  C   SER A 103     4121   4405   4324    408    -86   -203       C
ATOM    815  O   SER A 103      -7.911  29.730   9.669  1.00 39.14           O
ANISOU  815  O   SER A 103     4822   5123   4926    450   -101   -158       O
ATOM    816  CB  SER A 103      -6.355  28.049  12.061  1.00 43.62           C
ANISOU  816  CB  SER A 103     5374   5463   5738    357   -117   -136       C
ATOM    817  OG  SER A 103      -6.483  27.809  13.452  1.00 51.84           O
ANISOU  817  OG  SER A 103     6432   6436   6828    329   -155   -113       O
ATOM    818  N   LEU A 104      -7.143  27.708   9.051  1.00 40.35           N
ANISOU  818  N   LEU A 104     4921   5247   5161    402    -42   -259       N
ATOM    819  CA  LEU A 104      -7.017  28.120   7.650  1.00 38.83           C
ANISOU  819  CA  LEU A 104     4724   5145   4885    438     -7   -269       C
ATOM    820  C   LEU A 104      -8.378  28.454   7.052  1.00 43.06           C
ANISOU  820  C   LEU A 104     5260   5800   5302    466    -31   -308       C
ATOM    821  O   LEU A 104      -8.521  29.442   6.326  1.00 38.62           O
ANISOU  821  O   LEU A 104     4721   5303   4648    516    -32   -266       O
ATOM    822  CB  LEU A 104      -6.322  27.021   6.840  1.00 39.13           C
ANISOU  822  CB  LEU A 104     4731   5184   4953    430     47   -339       C
ATOM    823  CG  LEU A 104      -4.814  26.995   7.089  1.00 48.24           C
ANISOU  823  CG  LEU A 104     5868   6266   6196    432     76   -291       C
ATOM    824  CD1 LEU A 104      -4.187  25.651   6.711  1.00 48.75           C
ANISOU  824  CD1 LEU A 104     5903   6301   6318    440    118   -374       C
ATOM    825  CD2 LEU A 104      -4.141  28.142   6.327  1.00 54.62           C
ANISOU  825  CD2 LEU A 104     6678   7129   6947    448    109   -222       C
ATOM    826  N   GLN A 105      -9.396  27.649   7.363  1.00 33.70           N
ANISOU  826  N   GLN A 105     4048   4647   4109    432    -51   -388       N
ATOM    827  CA  GLN A 105     -10.725  27.907   6.837  1.00 41.39           C
ANISOU  827  CA  GLN A 105     4998   5762   4967    458    -79   -438       C
ATOM    828  C   GLN A 105     -11.253  29.241   7.321  1.00 42.59           C
ANISOU  828  C   GLN A 105     5176   5940   5066    523   -124   -362       C
ATOM    829  O   GLN A 105     -11.871  29.980   6.550  1.00 39.58           O
ANISOU  829  O   GLN A 105     4798   5668   4572    595   -144   -357       O
ATOM    830  CB  GLN A 105     -11.681  26.788   7.243  1.00 44.99           C
ANISOU  830  CB  GLN A 105     5413   6248   5433    384    -89   -537       C
ATOM    831  CG  GLN A 105     -11.540  25.504   6.431  1.00 43.44           C
ANISOU  831  CG  GLN A 105     5201   6057   5245    329    -50   -642       C
ATOM    832  CD  GLN A 105     -12.485  24.444   6.951  1.00 49.66           C
ANISOU  832  CD  GLN A 105     5966   6853   6047    231    -58   -732       C
ATOM    833  OE1 GLN A 105     -12.496  24.154   8.155  1.00 43.42           O
ANISOU  833  OE1 GLN A 105     5196   5968   5334    182    -67   -701       O
ATOM    834  NE2 GLN A 105     -13.290  23.862   6.057  1.00 39.77           N
ANISOU  834  NE2 GLN A 105     4674   5721   4715    193    -54   -845       N
ATOM    835  N   LEU A 106     -11.034  29.559   8.611  1.00 35.80           N
ANISOU  835  N   LEU A 106     4341   4981   4281    508   -146   -306       N
ATOM    836  CA  LEU A 106     -11.512  30.826   9.155  1.00 38.96           C
ANISOU  836  CA  LEU A 106     4778   5390   4634    575   -188   -243       C
ATOM    837  C   LEU A 106     -10.712  32.007   8.604  1.00 40.08           C
ANISOU  837  C   LEU A 106     4993   5487   4750    631   -179   -151       C
ATOM    838  O   LEU A 106     -11.278  33.057   8.281  1.00 35.98           O
ANISOU  838  O   LEU A 106     4517   5014   4138    716   -208   -116       O
ATOM    839  CB  LEU A 106     -11.431  30.788  10.687  1.00 40.21           C
ANISOU  839  CB  LEU A 106     4948   5455   4876    534   -209   -217       C
ATOM    840  CG  LEU A 106     -12.411  29.781  11.305  1.00 64.17           C
ANISOU  840  CG  LEU A 106     7923   8545   7915    473   -217   -297       C
ATOM    841  CD1 LEU A 106     -12.455  29.922  12.814  1.00 73.26           C
ANISOU  841  CD1 LEU A 106     9093   9625   9119    446   -239   -262       C
ATOM    842  CD2 LEU A 106     -13.817  29.938  10.724  1.00 66.15           C
ANISOU  842  CD2 LEU A 106     8116   8970   8047    518   -238   -366       C
ATOM    843  N   LEU A 107      -9.391  31.872   8.543  1.00 38.54           N
ANISOU  843  N   LEU A 107     4816   5198   4631    583   -141   -109       N
ATOM    844  CA  LEU A 107      -8.569  32.927   7.954  1.00 40.32           C
ANISOU  844  CA  LEU A 107     5106   5385   4827    607   -121    -23       C
ATOM    845  C   LEU A 107      -8.971  33.176   6.506  1.00 45.31           C
ANISOU  845  C   LEU A 107     5749   6129   5336    664   -104    -33       C
ATOM    846  O   LEU A 107      -9.049  34.329   6.059  1.00 41.93           O
ANISOU  846  O   LEU A 107     5401   5702   4829    722   -113     39       O
ATOM    847  CB  LEU A 107      -7.091  32.544   8.037  1.00 37.73           C
ANISOU  847  CB  LEU A 107     4761   4978   4599    536    -75      3       C
ATOM    848  CG  LEU A 107      -6.421  32.542   9.410  1.00 42.66           C
ANISOU  848  CG  LEU A 107     5385   5490   5334    486    -96     37       C
ATOM    849  CD1 LEU A 107      -5.092  31.809   9.360  1.00 40.37           C
ANISOU  849  CD1 LEU A 107     5041   5163   5134    433    -53     33       C
ATOM    850  CD2 LEU A 107      -6.217  33.955   9.921  1.00 47.03           C
ANISOU  850  CD2 LEU A 107     6022   5975   5873    493   -121    122       C
ATOM    851  N   SER A 108      -9.252  32.095   5.772  1.00 37.85           N
ANISOU  851  N   SER A 108     4737   5275   4370    648    -82   -122       N
ATOM    852  CA  SER A 108      -9.669  32.191   4.378  1.00 47.33           C
ANISOU  852  CA  SER A 108     5937   6601   5443    699    -69   -147       C
ATOM    853  C   SER A 108     -10.986  32.946   4.240  1.00 51.75           C
ANISOU  853  C   SER A 108     6518   7259   5886    795   -129   -144       C
ATOM    854  O   SER A 108     -11.116  33.859   3.411  1.00 40.36           O
ANISOU  854  O   SER A 108     5139   5862   4333    872   -136    -86       O
ATOM    855  CB  SER A 108      -9.793  30.784   3.795  1.00 54.22           C
ANISOU  855  CB  SER A 108     6731   7546   6323    653    -40   -265       C
ATOM    856  OG  SER A 108     -10.407  30.831   2.535  1.00 75.90           O
ANISOU  856  OG  SER A 108     9468  10437   8933    703    -41   -306       O
ATOM    857  N   ARG A 109     -11.993  32.544   5.017  1.00 41.88           N
ANISOU  857  N   ARG A 109     5212   6051   4650    796   -172   -209       N
ATOM    858  CA  ARG A 109     -13.279  33.236   4.982  1.00 44.61           C
ANISOU  858  CA  ARG A 109     5555   6509   4886    900   -233   -217       C
ATOM    859  C   ARG A 109     -13.131  34.721   5.298  1.00 45.26           C
ANISOU  859  C   ARG A 109     5751   6507   4939    991   -259   -103       C
ATOM    860  O   ARG A 109     -13.870  35.547   4.760  1.00 42.86           O
ANISOU  860  O   ARG A 109     5486   6284   4514   1112   -299    -79       O
ATOM    861  CB  ARG A 109     -14.251  32.579   5.967  1.00 53.98           C
ANISOU  861  CB  ARG A 109     6656   7747   6107    865   -264   -301       C
ATOM    862  CG  ARG A 109     -15.602  33.250   6.048  1.00 59.39           C
ANISOU  862  CG  ARG A 109     7312   8571   6682    978   -325   -323       C
ATOM    863  CD  ARG A 109     -16.434  32.710   7.206  1.00 70.10           C
ANISOU  863  CD  ARG A 109     8585   9969   8081    928   -344   -393       C
ATOM    864  NE  ARG A 109     -17.840  32.613   6.822  1.00 88.12           N
ANISOU  864  NE  ARG A 109    10766  12471  10246    986   -386   -481       N
ATOM    865  CZ  ARG A 109     -18.785  32.023   7.549  1.00 92.86           C
ANISOU  865  CZ  ARG A 109    11261  13173  10847    931   -398   -566       C
ATOM    866  NH1 ARG A 109     -18.488  31.480   8.721  1.00 87.18           N
ANISOU  866  NH1 ARG A 109    10543  12343  10240    822   -371   -566       N
ATOM    867  NH2 ARG A 109     -20.035  31.988   7.103  1.00 94.97           N
ANISOU  867  NH2 ARG A 109    11420  13665  10997    985   -436   -651       N
ATOM    868  N   ARG A 110     -12.190  35.091   6.172  1.00 37.94           N
ANISOU  868  N   ARG A 110     4884   5414   4117    937   -242    -35       N
ATOM    869  CA  ARG A 110     -12.059  36.522   6.430  1.00 43.77           C
ANISOU  869  CA  ARG A 110     5747   6059   4823   1013   -266     66       C
ATOM    870  C   ARG A 110     -11.227  37.250   5.382  1.00 52.14           C
ANISOU  870  C   ARG A 110     6909   7074   5829   1021   -229    157       C
ATOM    871  O   ARG A 110     -11.034  38.460   5.512  1.00 52.71           O
ANISOU  871  O   ARG A 110     7108   7046   5872   1069   -242    249       O
ATOM    872  CB  ARG A 110     -11.462  36.778   7.807  1.00 51.29           C
ANISOU  872  CB  ARG A 110     6733   6861   5893    951   -269    100       C
ATOM    873  CG  ARG A 110     -12.175  36.026   8.915  1.00 73.38           C
ANISOU  873  CG  ARG A 110     9440   9696   8745    926   -296     20       C
ATOM    874  CD  ARG A 110     -13.679  36.253   8.922  1.00 91.83           C
ANISOU  874  CD  ARG A 110    11738  12174  10980   1039   -346    -35       C
ATOM    875  NE  ARG A 110     -14.361  35.113   9.533  1.00103.23           N
ANISOU  875  NE  ARG A 110    13059  13706  12459    974   -349   -132       N
ATOM    876  CZ  ARG A 110     -15.672  35.041   9.741  1.00107.81           C
ANISOU  876  CZ  ARG A 110    13564  14433  12967   1035   -384   -202       C
ATOM    877  NH1 ARG A 110     -16.462  36.047   9.385  1.00109.52           N
ANISOU  877  NH1 ARG A 110    13811  14728  13072   1187   -428   -188       N
ATOM    878  NH2 ARG A 110     -16.194  33.958  10.306  1.00105.27           N
ANISOU  878  NH2 ARG A 110    13136  14180  12680    944   -375   -285       N
ATOM    879  N   GLY A 111     -10.724  36.559   4.363  1.00 51.55           N
ANISOU  879  N   GLY A 111     6788   7064   5735    970   -179    135       N
ATOM    880  CA  GLY A 111     -10.040  37.231   3.269  1.00 53.74           C
ANISOU  880  CA  GLY A 111     7156   7327   5935    977   -138    220       C
ATOM    881  C   GLY A 111      -8.563  37.466   3.486  1.00 52.38           C
ANISOU  881  C   GLY A 111     7025   7023   5855    863    -77    290       C
ATOM    882  O   GLY A 111      -7.966  38.295   2.791  1.00 57.44           O
ANISOU  882  O   GLY A 111     7767   7625   6434    854    -41    382       O
ATOM    883  N   ILE A 112      -7.952  36.745   4.404  1.00 44.06           N
ANISOU  883  N   ILE A 112     5894   5908   4938    771    -62    250       N
ATOM    884  CA  ILE A 112      -6.533  36.888   4.695  1.00 43.95           C
ANISOU  884  CA  ILE A 112     5890   5794   5016    662    -11    303       C
ATOM    885  C   ILE A 112      -5.715  36.093   3.689  1.00 47.18           C
ANISOU  885  C   ILE A 112     6225   6280   5421    608     63    272       C
ATOM    886  O   ILE A 112      -6.103  34.997   3.269  1.00 43.70           O
ANISOU  886  O   ILE A 112     5696   5935   4972    625     70    178       O
ATOM    887  CB  ILE A 112      -6.276  36.453   6.141  1.00 45.24           C
ANISOU  887  CB  ILE A 112     5999   5873   5316    608    -38    271       C
ATOM    888  CG1 ILE A 112      -6.891  37.514   7.056  1.00 51.32           C
ANISOU  888  CG1 ILE A 112     6866   6557   6075    658    -99    316       C
ATOM    889  CG2 ILE A 112      -4.799  36.269   6.414  1.00 44.33           C
ANISOU  889  CG2 ILE A 112     5847   5696   5302    498     11    298       C
ATOM    890  CD1 ILE A 112      -6.551  37.345   8.497  1.00 54.48           C
ANISOU  890  CD1 ILE A 112     7239   6869   6592    601   -126    303       C
ATOM    891  N   GLY A 113      -4.590  36.660   3.276  1.00 45.46           N
ANISOU  891  N   GLY A 113     6047   6024   5201    538    123    348       N
ATOM    892  CA  GLY A 113      -3.729  35.999   2.318  1.00 46.73           C
ANISOU  892  CA  GLY A 113     6136   6269   5351    490    202    321       C
ATOM    893  C   GLY A 113      -3.182  34.701   2.859  1.00 39.48           C
ANISOU  893  C   GLY A 113     5084   5358   4559    450    217    229       C
ATOM    894  O   GLY A 113      -2.677  34.663   3.983  1.00 45.49           O
ANISOU  894  O   GLY A 113     5819   6031   5435    404    196    238       O
ATOM    895  N   LEU A 114      -3.275  33.634   2.073  1.00 38.15           N
ANISOU  895  N   LEU A 114     4840   5290   4365    474    249    138       N
ATOM    896  CA  LEU A 114      -2.831  32.309   2.484  1.00 42.37           C
ANISOU  896  CA  LEU A 114     5267   5820   5010    456    263     43       C
ATOM    897  C   LEU A 114      -2.268  31.596   1.272  1.00 38.77           C
ANISOU  897  C   LEU A 114     4753   5469   4507    459    339    -18       C
ATOM    898  O   LEU A 114      -2.664  31.892   0.145  1.00 42.03           O
ANISOU  898  O   LEU A 114     5204   5977   4789    487    363    -14       O
ATOM    899  CB  LEU A 114      -3.988  31.472   3.041  1.00 41.01           C
ANISOU  899  CB  LEU A 114     5076   5642   4865    497    200    -43       C
ATOM    900  CG  LEU A 114      -4.780  32.002   4.212  1.00 47.76           C
ANISOU  900  CG  LEU A 114     5975   6421   5750    509    124     -7       C
ATOM    901  CD1 LEU A 114      -6.105  31.247   4.261  1.00 46.24           C
ANISOU  901  CD1 LEU A 114     5759   6283   5526    546     80    -99       C
ATOM    902  CD2 LEU A 114      -3.963  31.840   5.475  1.00 47.52           C
ANISOU  902  CD2 LEU A 114     5917   6281   5856    458    111     16       C
ATOM    903  N   PRO A 115      -1.406  30.602   1.470  1.00 42.86           N
ANISOU  903  N   PRO A 115     5183   5981   5123    443    375    -82       N
ATOM    904  CA  PRO A 115      -1.083  29.698   0.365  1.00 45.82           C
ANISOU  904  CA  PRO A 115     5501   6454   5453    468    441   -175       C
ATOM    905  C   PRO A 115      -2.312  28.888  -0.005  1.00 46.77           C
ANISOU  905  C   PRO A 115     5636   6613   5522    514    405   -278       C
ATOM    906  O   PRO A 115      -3.118  28.523   0.851  1.00 46.09           O
ANISOU  906  O   PRO A 115     5561   6459   5491    518    339   -307       O
ATOM    907  CB  PRO A 115       0.017  28.791   0.934  1.00 49.22           C
ANISOU  907  CB  PRO A 115     5841   6842   6017    462    469   -224       C
ATOM    908  CG  PRO A 115       0.297  29.289   2.320  1.00 49.62           C
ANISOU  908  CG  PRO A 115     5898   6783   6174    427    414   -148       C
ATOM    909  CD  PRO A 115      -0.873  30.121   2.756  1.00 42.34           C
ANISOU  909  CD  PRO A 115     5068   5814   5205    423    345    -90       C
ATOM    910  N   VAL A 116      -2.453  28.607  -1.300  1.00 46.68           N
ANISOU  910  N   VAL A 116     5619   6719   5396    538    452   -337       N
ATOM    911  CA  VAL A 116      -3.536  27.740  -1.751  1.00 45.45           C
ANISOU  911  CA  VAL A 116     5465   6617   5187    567    422   -456       C
ATOM    912  C   VAL A 116      -3.423  26.384  -1.068  1.00 44.38           C
ANISOU  912  C   VAL A 116     5289   6393   5182    561    414   -561       C
ATOM    913  O   VAL A 116      -2.348  25.767  -1.041  1.00 45.15           O
ANISOU  913  O   VAL A 116     5340   6457   5356    568    466   -594       O
ATOM    914  CB  VAL A 116      -3.498  27.599  -3.278  1.00 55.05           C
ANISOU  914  CB  VAL A 116     6677   7981   6258    591    481   -511       C
ATOM    915  CG1 VAL A 116      -4.634  26.707  -3.744  1.00 57.21           C
ANISOU  915  CG1 VAL A 116     6949   8319   6471    609    445   -645       C
ATOM    916  CG2 VAL A 116      -3.572  28.978  -3.941  1.00 62.15           C
ANISOU  916  CG2 VAL A 116     7638   8955   7020    599    490   -387       C
ATOM    917  N   THR A 117      -4.541  25.895  -0.543  1.00 45.58           N
ANISOU  917  N   THR A 117     5458   6511   5350    551    350   -617       N
ATOM    918  CA  THR A 117      -4.537  24.750   0.354  1.00 42.09           C
ANISOU  918  CA  THR A 117     5006   5950   5035    531    332   -687       C
ATOM    919  C   THR A 117      -5.723  23.845   0.060  1.00 44.32           C
ANISOU  919  C   THR A 117     5301   6265   5274    507    304   -812       C
ATOM    920  O   THR A 117      -6.845  24.315  -0.162  1.00 43.00           O
ANISOU  920  O   THR A 117     5141   6185   5010    499    260   -813       O
ATOM    921  CB  THR A 117      -4.584  25.203   1.830  1.00 49.07           C
ANISOU  921  CB  THR A 117     5904   6719   6020    509    276   -593       C
ATOM    922  OG1 THR A 117      -3.590  26.212   2.058  1.00 53.28           O
ANISOU  922  OG1 THR A 117     6429   7239   6576    514    295   -478       O
ATOM    923  CG2 THR A 117      -4.305  24.037   2.758  1.00 52.24           C
ANISOU  923  CG2 THR A 117     6305   6990   6554    495    266   -644       C
ATOM    924  N   GLY A 118      -5.478  22.545   0.098  1.00 40.62           N
ANISOU  924  N   GLY A 118     4836   5722   4876    496    327   -920       N
ATOM    925  CA  GLY A 118      -6.541  21.573  -0.048  1.00 47.66           C
ANISOU  925  CA  GLY A 118     5749   6617   5743    446    304  -1046       C
ATOM    926  C   GLY A 118      -6.522  20.593   1.111  1.00 51.30           C
ANISOU  926  C   GLY A 118     6246   6905   6340    406    285  -1071       C
ATOM    927  O   GLY A 118      -5.497  20.386   1.758  1.00 46.21           O
ANISOU  927  O   GLY A 118     5607   6145   5805    442    301  -1022       O
ATOM    928  N   PHE A 119      -7.684  20.006   1.372  1.00 45.15           N
ANISOU  928  N   PHE A 119     5489   6119   5546    329    249  -1145       N
ATOM    929  CA  PHE A 119      -7.828  19.022   2.437  1.00 40.38           C
ANISOU  929  CA  PHE A 119     4939   5350   5053    271    234  -1169       C
ATOM    930  C   PHE A 119      -8.591  17.829   1.915  1.00 45.26           C
ANISOU  930  C   PHE A 119     5597   5959   5641    192    244  -1326       C
ATOM    931  O   PHE A 119      -9.583  17.988   1.194  1.00 44.90           O
ANISOU  931  O   PHE A 119     5518   6062   5481    145    229  -1397       O
ATOM    932  CB  PHE A 119      -8.589  19.565   3.644  1.00 45.37           C
ANISOU  932  CB  PHE A 119     5567   5965   5708    219    177  -1081       C
ATOM    933  CG  PHE A 119      -7.849  20.587   4.414  1.00 67.22           C
ANISOU  933  CG  PHE A 119     8315   8699   8525    279    161   -935       C
ATOM    934  CD1 PHE A 119      -8.392  21.836   4.645  1.00 79.02           C
ANISOU  934  CD1 PHE A 119     9776  10289   9958    289    124   -850       C
ATOM    935  CD2 PHE A 119      -6.602  20.313   4.920  1.00 77.38           C
ANISOU  935  CD2 PHE A 119     9620   9862   9919    328    181   -886       C
ATOM    936  CE1 PHE A 119      -7.691  22.782   5.379  1.00 83.18           C
ANISOU  936  CE1 PHE A 119    10299  10772  10532    331    109   -723       C
ATOM    937  CE2 PHE A 119      -5.914  21.266   5.638  1.00 82.13           C
ANISOU  937  CE2 PHE A 119    10199  10444  10563    368    162   -759       C
ATOM    938  CZ  PHE A 119      -6.442  22.496   5.856  1.00 82.05           C
ANISOU  938  CZ  PHE A 119    10166  10515  10493    362    129   -680       C
ATOM    939  N   ALA A 120      -8.145  16.636   2.300  1.00 47.98           N
ANISOU  939  N   ALA A 120     6018   6127   6084    177    266  -1382       N
ATOM    940  CA  ALA A 120      -8.820  15.414   1.894  1.00 42.15           C
ANISOU  940  CA  ALA A 120     5344   5341   5329     85    278  -1536       C
ATOM    941  C   ALA A 120      -8.676  14.392   3.012  1.00 49.62           C
ANISOU  941  C   ALA A 120     6395   6058   6399     38    275  -1529       C
ATOM    942  O   ALA A 120      -7.896  14.571   3.951  1.00 54.25           O
ANISOU  942  O   ALA A 120     6998   6535   7081    102    265  -1414       O
ATOM    943  CB  ALA A 120      -8.263  14.882   0.571  1.00 43.87           C
ANISOU  943  CB  ALA A 120     5574   5594   5500    143    331  -1661       C
ATOM    944  N   HIS A 121      -9.472  13.337   2.924  1.00 49.58           N
ANISOU  944  N   HIS A 121     6465   5986   6386    -84    280  -1650       N
ATOM    945  CA  HIS A 121      -9.329  12.208   3.831  1.00 54.19           C
ANISOU  945  CA  HIS A 121     7183   6329   7078   -134    285  -1655       C
ATOM    946  C   HIS A 121      -9.303  10.940   3.004  1.00 55.48           C
ANISOU  946  C   HIS A 121     7450   6391   7239   -167    325  -1826       C
ATOM    947  O   HIS A 121      -8.275  10.261   2.922  1.00 56.61           O
ANISOU  947  O   HIS A 121     7675   6376   7457    -59    354  -1848       O
ATOM    948  CB  HIS A 121     -10.461  12.155   4.859  1.00 51.87           C
ANISOU  948  CB  HIS A 121     6905   6020   6784   -291    252  -1616       C
ATOM    949  CG  HIS A 121     -10.334  11.025   5.835  1.00 52.98           C
ANISOU  949  CG  HIS A 121     7199   5906   7024   -353    259  -1603       C
ATOM    950  ND1 HIS A 121     -10.563   9.710   5.490  1.00 55.56           N
ANISOU  950  ND1 HIS A 121     7660   6082   7367   -442    289  -1736       N
ATOM    951  CD2 HIS A 121      -9.998  11.017   7.148  1.00 55.18           C
ANISOU  951  CD2 HIS A 121     7533   6049   7386   -337    238  -1471       C
ATOM    952  CE1 HIS A 121     -10.374   8.939   6.547  1.00 59.64           C
ANISOU  952  CE1 HIS A 121     8316   6370   7973   -476    288  -1677       C
ATOM    953  NE2 HIS A 121     -10.028   9.707   7.564  1.00 58.98           N
ANISOU  953  NE2 HIS A 121     8184   6299   7928   -411    256  -1515       N
ATOM    954  N   SER A 122     -10.423  10.630   2.361  1.00 50.26           N
ANISOU  954  N   SER A 122     6781   5828   6487   -309    324  -1954       N
ATOM    955  CA  SER A 122     -10.536   9.453   1.503  1.00 48.06           C
ANISOU  955  CA  SER A 122     6603   5467   6189   -364    360  -2138       C
ATOM    956  C   SER A 122     -11.056   9.845   0.122  1.00 54.87           C
ANISOU  956  C   SER A 122     7365   6574   6909   -381    364  -2258       C
ATOM    957  O   SER A 122     -12.078   9.328  -0.344  1.00 58.88           O
ANISOU  957  O   SER A 122     7885   7143   7343   -536    358  -2396       O
ATOM    958  CB  SER A 122     -11.434   8.414   2.171  1.00 54.95           C
ANISOU  958  CB  SER A 122     7600   6182   7096   -562    357  -2198       C
ATOM    959  OG  SER A 122     -11.048   8.242   3.531  1.00 60.89           O
ANISOU  959  OG  SER A 122     8434   6740   7961   -546    346  -2057       O
ATOM    960  N   PRO A 123     -10.347  10.729  -0.586  1.00 61.51           N
ANISOU  960  N   PRO A 123     8109   7563   7701   -229    374  -2214       N
ATOM    961  CA  PRO A 123     -10.840  11.180  -1.893  1.00 60.67           C
ANISOU  961  CA  PRO A 123     7909   7701   7440   -235    373  -2311       C
ATOM    962  C   PRO A 123     -10.699  10.099  -2.949  1.00 66.73           C
ANISOU  962  C   PRO A 123     8760   8422   8171   -252    416  -2510       C
ATOM    963  O   PRO A 123      -9.781   9.276  -2.916  1.00 62.09           O
ANISOU  963  O   PRO A 123     8281   7638   7673   -176    458  -2552       O
ATOM    964  CB  PRO A 123      -9.950  12.386  -2.211  1.00 57.90           C
ANISOU  964  CB  PRO A 123     7460   7477   7062    -67    382  -2184       C
ATOM    965  CG  PRO A 123      -8.642  12.023  -1.587  1.00 60.85           C
ANISOU  965  CG  PRO A 123     7901   7645   7576     48    416  -2114       C
ATOM    966  CD  PRO A 123      -8.986  11.239  -0.316  1.00 61.21           C
ANISOU  966  CD  PRO A 123     8050   7470   7737    -48    393  -2088       C
ATOM    967  N   ASP A 124     -11.630  10.109  -3.901  1.00 71.92           N
ANISOU  967  N   ASP A 124     9365   9272   8689   -344    400  -2640       N
ATOM    968  CA  ASP A 124     -11.619   9.136  -4.989  1.00 64.96           C
ANISOU  968  CA  ASP A 124     8557   8375   7748   -375    436  -2848       C
ATOM    969  C   ASP A 124     -10.835   9.607  -6.206  1.00 67.35           C
ANISOU  969  C   ASP A 124     8802   8833   7955   -220    473  -2879       C
ATOM    970  O   ASP A 124     -10.618   8.816  -7.123  1.00 69.52           O
ANISOU  970  O   ASP A 124     9142   9089   8184   -213    511  -3050       O
ATOM    971  CB  ASP A 124     -13.053   8.793  -5.425  1.00 63.25           C
ANISOU  971  CB  ASP A 124     8315   8298   7420   -574    398  -2996       C
ATOM    972  CG  ASP A 124     -13.902   8.268  -4.281  1.00 62.93           C
ANISOU  972  CG  ASP A 124     8327   8124   7458   -758    372  -2981       C
ATOM    973  OD1 ASP A 124     -13.741   7.083  -3.918  1.00 68.52           O
ANISOU  973  OD1 ASP A 124     9197   8577   8261   -837    403  -3060       O
ATOM    974  OD2 ASP A 124     -14.728   9.037  -3.743  1.00 61.13           O
ANISOU  974  OD2 ASP A 124     7987   8045   7195   -822    324  -2888       O
ATOM    975  N   ASP A 125     -10.415  10.872  -6.245  1.00 70.26           N
ANISOU  975  N   ASP A 125     9057   9351   8286   -102    465  -2721       N
ATOM    976  CA  ASP A 125      -9.758  11.448  -7.424  1.00 66.32           C
ANISOU  976  CA  ASP A 125     8495   9029   7673     26    503  -2733       C
ATOM    977  C   ASP A 125      -8.624  12.343  -6.909  1.00 63.00           C
ANISOU  977  C   ASP A 125     8027   8580   7329    172    527  -2539       C
ATOM    978  O   ASP A 125      -8.785  13.562  -6.761  1.00 60.15           O
ANISOU  978  O   ASP A 125     7576   8358   6918    199    496  -2391       O
ATOM    979  CB  ASP A 125     -10.762  12.214  -8.292  1.00 65.08           C
ANISOU  979  CB  ASP A 125     8238   9162   7329    -21    458  -2759       C
ATOM    980  CG  ASP A 125     -10.188  12.657  -9.622  1.00 64.29           C
ANISOU  980  CG  ASP A 125     8096   9247   7087     90    500  -2794       C
ATOM    981  OD1 ASP A 125      -8.951  12.770  -9.743  1.00 62.85           O
ANISOU  981  OD1 ASP A 125     7924   9004   6952    217    564  -2740       O
ATOM    982  OD2 ASP A 125     -10.986  12.919 -10.551  1.00 69.48           O
ANISOU  982  OD2 ASP A 125     8700  10126   7572     50    469  -2872       O
ATOM    983  N   ILE A 126      -7.481  11.716  -6.607  1.00 66.75           N
ANISOU  983  N   ILE A 126     8567   8870   7925    265    579  -2544       N
ATOM    984  CA  ILE A 126      -6.316  12.471  -6.129  1.00 65.21           C
ANISOU  984  CA  ILE A 126     8317   8655   7804    396    604  -2377       C
ATOM    985  C   ILE A 126      -5.804  13.434  -7.188  1.00 56.40           C
ANISOU  985  C   ILE A 126     7106   7766   6557    481    644  -2339       C
ATOM    986  O   ILE A 126      -5.390  14.548  -6.829  1.00 51.70           O
ANISOU  986  O   ILE A 126     6439   7236   5970    527    638  -2168       O
ATOM    987  CB  ILE A 126      -5.240  11.517  -5.603  1.00 64.73           C
ANISOU  987  CB  ILE A 126     8337   8365   7892    487    645  -2405       C
ATOM    988  CG1 ILE A 126      -5.707  10.853  -4.309  1.00 63.68           C
ANISOU  988  CG1 ILE A 126     8300   8004   7892    404    597  -2375       C
ATOM    989  CG2 ILE A 126      -3.923  12.254  -5.344  1.00 59.79           C
ANISOU  989  CG2 ILE A 126     7630   7767   7322    628    679  -2265       C
ATOM    990  CD1 ILE A 126      -5.165   9.457  -4.125  1.00 62.50           C
ANISOU  990  CD1 ILE A 126     8290   7612   7846    451    629  -2489       C
ATOM    991  N   PRO A 127      -5.769  13.090  -8.491  1.00 58.15           N
ANISOU  991  N   PRO A 127     7330   8112   6652    503    688  -2485       N
ATOM    992  CA  PRO A 127      -5.419  14.111  -9.492  1.00 56.84           C
ANISOU  992  CA  PRO A 127     7078   8180   6338    566    723  -2429       C
ATOM    993  C   PRO A 127      -6.271  15.363  -9.390  1.00 58.19           C
ANISOU  993  C   PRO A 127     7187   8502   6418    515    659  -2291       C
ATOM    994  O   PRO A 127      -5.751  16.474  -9.554  1.00 59.10           O
ANISOU  994  O   PRO A 127     7246   8725   6486    573    678  -2147       O
ATOM    995  CB  PRO A 127      -5.645  13.382 -10.825  1.00 63.90           C
ANISOU  995  CB  PRO A 127     8003   9181   7095    560    760  -2636       C
ATOM    996  CG  PRO A 127      -5.412  11.951 -10.517  1.00 63.54           C
ANISOU  996  CG  PRO A 127     8060   8913   7168    558    781  -2790       C
ATOM    997  CD  PRO A 127      -5.923  11.757  -9.113  1.00 59.65           C
ANISOU  997  CD  PRO A 127     7611   8226   6826    478    716  -2707       C
ATOM    998  N   ASP A 128      -7.575  15.208  -9.120  1.00 56.03           N
ANISOU  998  N   ASP A 128     6927   8243   6117    406    584  -2334       N
ATOM    999  CA  ASP A 128      -8.439  16.370  -8.933  1.00 56.87           C
ANISOU  999  CA  ASP A 128     6975   8489   6144    377    516  -2207       C
ATOM   1000  C   ASP A 128      -8.038  17.148  -7.685  1.00 53.23           C
ANISOU 1000  C   ASP A 128     6497   7915   5812    404    496  -2012       C
ATOM   1001  O   ASP A 128      -8.036  18.383  -7.692  1.00 56.18           O
ANISOU 1001  O   ASP A 128     6827   8392   6125    444    478  -1865       O
ATOM   1002  CB  ASP A 128      -9.907  15.928  -8.867  1.00 61.82           C
ANISOU 1002  CB  ASP A 128     7603   9167   6720    254    443  -2314       C
ATOM   1003  CG  ASP A 128     -10.893  17.103  -8.901  1.00 67.69           C
ANISOU 1003  CG  ASP A 128     8273  10101   7345    249    369  -2212       C
ATOM   1004  OD1 ASP A 128     -10.652  18.089  -9.639  1.00 66.98           O
ANISOU 1004  OD1 ASP A 128     8150  10168   7131    334    377  -2127       O
ATOM   1005  OD2 ASP A 128     -11.930  17.023  -8.196  1.00 58.78           O
ANISOU 1005  OD2 ASP A 128     7124   8967   6242    161    305  -2220       O
ATOM   1006  N   LEU A 129      -7.664  16.445  -6.612  1.00 52.66           N
ANISOU 1006  N   LEU A 129     6470   7626   5911    385    500  -2007       N
ATOM   1007  CA  LEU A 129      -7.192  17.138  -5.416  1.00 49.66           C
ANISOU 1007  CA  LEU A 129     6075   7143   5652    412    481  -1830       C
ATOM   1008  C   LEU A 129      -5.911  17.913  -5.698  1.00 51.50           C
ANISOU 1008  C   LEU A 129     6267   7416   5884    515    538  -1722       C
ATOM   1009  O   LEU A 129      -5.742  19.046  -5.233  1.00 53.52           O
ANISOU 1009  O   LEU A 129     6489   7701   6145    533    519  -1562       O
ATOM   1010  CB  LEU A 129      -6.964  16.134  -4.285  1.00 49.59           C
ANISOU 1010  CB  LEU A 129     6130   6897   5814    382    476  -1853       C
ATOM   1011  CG  LEU A 129      -6.227  16.653  -3.051  1.00 48.99           C
ANISOU 1011  CG  LEU A 129     6043   6699   5871    425    464  -1688       C
ATOM   1012  CD1 LEU A 129      -7.040  17.734  -2.331  1.00 51.05           C
ANISOU 1012  CD1 LEU A 129     6267   7018   6110    378    399  -1558       C
ATOM   1013  CD2 LEU A 129      -5.889  15.508  -2.108  1.00 54.89           C
ANISOU 1013  CD2 LEU A 129     6869   7216   6770    416    465  -1725       C
ATOM   1014  N   ILE A 130      -4.995  17.317  -6.461  1.00 48.69           N
ANISOU 1014  N   ILE A 130     5914   7066   5519    578    613  -1812       N
ATOM   1015  CA  ILE A 130      -3.740  17.985  -6.773  1.00 55.61           C
ANISOU 1015  CA  ILE A 130     6738   8002   6389    662    678  -1722       C
ATOM   1016  C   ILE A 130      -3.985  19.204  -7.653  1.00 55.08           C
ANISOU 1016  C   ILE A 130     6634   8141   6155    663    684  -1640       C
ATOM   1017  O   ILE A 130      -3.388  20.263  -7.441  1.00 52.06           O
ANISOU 1017  O   ILE A 130     6216   7791   5773    684    699  -1488       O
ATOM   1018  CB  ILE A 130      -2.766  16.986  -7.426  1.00 53.83           C
ANISOU 1018  CB  ILE A 130     6517   7754   6182    737    760  -1858       C
ATOM   1019  CG1 ILE A 130      -2.348  15.917  -6.402  1.00 52.89           C
ANISOU 1019  CG1 ILE A 130     6447   7406   6243    763    750  -1901       C
ATOM   1020  CG2 ILE A 130      -1.564  17.716  -8.018  1.00 53.33           C
ANISOU 1020  CG2 ILE A 130     6377   7816   6069    810    840  -1785       C
ATOM   1021  CD1 ILE A 130      -1.655  14.684  -7.024  1.00 53.67           C
ANISOU 1021  CD1 ILE A 130     6581   7450   6362    845    817  -2074       C
ATOM   1022  N   ASP A 131      -4.870  19.081  -8.649  1.00 57.14           N
ANISOU 1022  N   ASP A 131     6907   8540   6262    637    670  -1739       N
ATOM   1023  CA  ASP A 131      -5.204  20.228  -9.486  1.00 57.91           C
ANISOU 1023  CA  ASP A 131     6986   8833   6186    648    664  -1654       C
ATOM   1024  C   ASP A 131      -5.771  21.381  -8.674  1.00 59.06           C
ANISOU 1024  C   ASP A 131     7131   8964   6347    629    593  -1485       C
ATOM   1025  O   ASP A 131      -5.674  22.534  -9.106  1.00 61.05           O
ANISOU 1025  O   ASP A 131     7381   9322   6493    656    599  -1361       O
ATOM   1026  CB  ASP A 131      -6.197  19.822 -10.583  1.00 69.04           C
ANISOU 1026  CB  ASP A 131     8407  10396   7428    625    641  -1798       C
ATOM   1027  CG  ASP A 131      -6.438  20.937 -11.592  1.00 77.65           C
ANISOU 1027  CG  ASP A 131     9487  11698   8317    658    641  -1715       C
ATOM   1028  OD1 ASP A 131      -5.453  21.570 -12.030  1.00 79.90           O
ANISOU 1028  OD1 ASP A 131     9763  12033   8560    703    713  -1622       O
ATOM   1029  OD2 ASP A 131      -7.607  21.182 -11.950  1.00 81.15           O
ANISOU 1029  OD2 ASP A 131     9932  12263   8640    638    568  -1740       O
ATOM   1030  N   MET A 132      -6.328  21.097  -7.489  1.00 57.25           N
ANISOU 1030  N   MET A 132     6911   8597   6243    584    529  -1474       N
ATOM   1031  CA  MET A 132      -6.905  22.155  -6.662  1.00 59.89           C
ANISOU 1031  CA  MET A 132     7245   8917   6592    574    461  -1327       C
ATOM   1032  C   MET A 132      -5.857  23.105  -6.118  1.00 63.29           C
ANISOU 1032  C   MET A 132     7673   9282   7093    605    492  -1161       C
ATOM   1033  O   MET A 132      -6.172  24.267  -5.829  1.00 57.39           O
ANISOU 1033  O   MET A 132     6940   8560   6307    615    453  -1027       O
ATOM   1034  CB  MET A 132      -7.661  21.567  -5.482  1.00 62.52           C
ANISOU 1034  CB  MET A 132     7586   9123   7044    513    398  -1360       C
ATOM   1035  CG  MET A 132      -9.001  21.015  -5.812  1.00 67.59           C
ANISOU 1035  CG  MET A 132     8223   9855   7605    455    345  -1487       C
ATOM   1036  SD  MET A 132      -9.748  20.557  -4.242  1.00 79.44           S
ANISOU 1036  SD  MET A 132     9730  11202   9250    372    284  -1481       S
ATOM   1037  CE  MET A 132     -11.145  19.767  -4.928  1.00 73.13           C
ANISOU 1037  CE  MET A 132     8910  10539   8336    286    244  -1663       C
ATOM   1038  N   VAL A 133      -4.628  22.629  -5.927  1.00 58.10           N
ANISOU 1038  N   VAL A 133     6998   8539   6539    623    557  -1171       N
ATOM   1039  CA  VAL A 133      -3.571  23.472  -5.387  1.00 56.06           C
ANISOU 1039  CA  VAL A 133     6721   8230   6350    636    587  -1025       C
ATOM   1040  C   VAL A 133      -2.671  23.893  -6.535  1.00 50.65           C
ANISOU 1040  C   VAL A 133     6012   7676   5558    664    676  -1006       C
ATOM   1041  O   VAL A 133      -1.502  24.238  -6.325  1.00 56.00           O
ANISOU 1041  O   VAL A 133     6651   8332   6294    670    732   -934       O
ATOM   1042  CB  VAL A 133      -2.781  22.763  -4.269  1.00 63.07           C
ANISOU 1042  CB  VAL A 133     7588   8951   7425    640    592  -1034       C
ATOM   1043  CG1 VAL A 133      -3.542  22.856  -2.962  1.00 68.67           C
ANISOU 1043  CG1 VAL A 133     8326   9539   8227    601    507   -982       C
ATOM   1044  CG2 VAL A 133      -2.524  21.313  -4.622  1.00 61.48           C
ANISOU 1044  CG2 VAL A 133     7386   8709   7265    667    630  -1199       C
ATOM   1045  N   ASN A 134      -3.213  23.830  -7.759  1.00 56.30           N
ANISOU 1045  N   ASN A 134     6742   8539   6109    677    691  -1078       N
ATOM   1046  CA  ASN A 134      -2.580  24.377  -8.969  1.00 57.75           C
ANISOU 1046  CA  ASN A 134     6918   8877   6147    697    772  -1047       C
ATOM   1047  C   ASN A 134      -1.353  23.594  -9.376  1.00 58.55           C
ANISOU 1047  C   ASN A 134     6962   8994   6290    724    872  -1135       C
ATOM   1048  O   ASN A 134      -0.408  24.144  -9.948  1.00 66.97           O
ANISOU 1048  O   ASN A 134     7998  10152   7296    727    955  -1073       O
ATOM   1049  CB  ASN A 134      -2.222  25.856  -8.813  1.00 51.68           C
ANISOU 1049  CB  ASN A 134     6174   8122   5340    677    779   -851       C
ATOM   1050  CG  ASN A 134      -3.449  26.704  -8.634  1.00 60.12           C
ANISOU 1050  CG  ASN A 134     7308   9201   6334    679    686   -769       C
ATOM   1051  OD1 ASN A 134      -4.505  26.379  -9.182  1.00 65.96           O
ANISOU 1051  OD1 ASN A 134     8063  10028   6970    700    638   -853       O
ATOM   1052  ND2 ASN A 134      -3.341  27.765  -7.847  1.00 56.37           N
ANISOU 1052  ND2 ASN A 134     6868   8641   5909    660    656   -615       N
ATOM   1053  N   GLY A 135      -1.368  22.306  -9.108  1.00 55.09           N
ANISOU 1053  N   GLY A 135     6514   8470   5948    746    867  -1284       N
ATOM   1054  CA  GLY A 135      -0.411  21.429  -9.716  1.00 60.93           C
ANISOU 1054  CA  GLY A 135     7211   9245   6696    798    957  -1406       C
ATOM   1055  C   GLY A 135       0.743  21.081  -8.806  1.00 73.28           C
ANISOU 1055  C   GLY A 135     8719  10689   8435    832    987  -1384       C
ATOM   1056  O   GLY A 135       0.714  21.293  -7.586  1.00 60.10           O
ANISOU 1056  O   GLY A 135     7054   8883   6900    811    927  -1296       O
ATOM   1057  N   ALA A 136       1.817  20.661  -9.449  1.00 73.16           N
ANISOU 1057  N   ALA A 136     8642  10752   8402    891   1084  -1456       N
ATOM   1058  CA  ALA A 136       2.654  19.535  -9.080  1.00 81.94           C
ANISOU 1058  CA  ALA A 136     9717  11773   9645    974   1117  -1566       C
ATOM   1059  C   ALA A 136       3.723  19.813  -8.034  1.00 81.81           C
ANISOU 1059  C   ALA A 136     9622  11686   9777    996   1122  -1464       C
ATOM   1060  O   ALA A 136       3.970  18.938  -7.195  1.00103.96           O
ANISOU 1060  O   ALA A 136    12433  14338  12727   1055   1089  -1516       O
ATOM   1061  CB  ALA A 136       3.302  18.960 -10.345  1.00 88.98           C
ANISOU 1061  CB  ALA A 136    10568  12809  10430   1044   1223  -1708       C
ATOM   1062  N   PRO A 137       4.421  20.953  -8.045  1.00 83.50           N
ANISOU 1062  N   PRO A 137     9764  12003   9958    952   1162  -1324       N
ATOM   1063  CA  PRO A 137       5.300  21.216  -6.901  1.00 68.33           C
ANISOU 1063  CA  PRO A 137     7770  10006   8184    957   1145  -1231       C
ATOM   1064  C   PRO A 137       4.435  21.530  -5.695  1.00 61.09           C
ANISOU 1064  C   PRO A 137     6930   8924   7360    901   1029  -1137       C
ATOM   1065  O   PRO A 137       3.823  22.598  -5.648  1.00 65.29           O
ANISOU 1065  O   PRO A 137     7505   9475   7826    817    995  -1021       O
ATOM   1066  CB  PRO A 137       6.144  22.411  -7.358  1.00 66.63           C
ANISOU 1066  CB  PRO A 137     7473   9957   7887    893   1223  -1113       C
ATOM   1067  CG  PRO A 137       6.022  22.407  -8.851  1.00 67.98           C
ANISOU 1067  CG  PRO A 137     7654  10298   7877    896   1308  -1184       C
ATOM   1068  CD  PRO A 137       4.624  21.946  -9.113  1.00 67.77           C
ANISOU 1068  CD  PRO A 137     7750  10205   7797    899   1236  -1257       C
ATOM   1069  N   LEU A 138       4.338  20.612  -4.733  1.00 53.80           N
ANISOU 1069  N   LEU A 138     6032   7834   6575    952    969  -1187       N
ATOM   1070  CA  LEU A 138       3.381  20.832  -3.657  1.00 54.73           C
ANISOU 1070  CA  LEU A 138     6228   7806   6760    893    865  -1113       C
ATOM   1071  C   LEU A 138       3.868  20.228  -2.346  1.00 54.93           C
ANISOU 1071  C   LEU A 138     6241   7675   6954    942    814  -1099       C
ATOM   1072  O   LEU A 138       4.741  19.357  -2.315  1.00 55.67           O
ANISOU 1072  O   LEU A 138     6289   7746   7116   1041    847  -1178       O
ATOM   1073  CB  LEU A 138       1.993  20.283  -4.033  1.00 60.90           C
ANISOU 1073  CB  LEU A 138     7114   8546   7480    867    822  -1203       C
ATOM   1074  CG  LEU A 138       1.746  18.778  -4.138  1.00 70.92           C
ANISOU 1074  CG  LEU A 138     8439   9712   8796    924    820  -1369       C
ATOM   1075  CD1 LEU A 138       1.323  18.225  -2.808  1.00 80.66           C
ANISOU 1075  CD1 LEU A 138     9734  10746  10166    911    739  -1349       C
ATOM   1076  CD2 LEU A 138       0.661  18.505  -5.156  1.00 76.76           C
ANISOU 1076  CD2 LEU A 138     9240  10521   9403    884    821  -1475       C
ATOM   1077  N   VAL A 139       3.249  20.692  -1.261  1.00 47.67           N
ANISOU 1077  N   VAL A 139     5369   6651   6092    880    729  -1000       N
ATOM   1078  CA  VAL A 139       3.592  20.313   0.103  1.00 51.46           C
ANISOU 1078  CA  VAL A 139     5850   6987   6716    909    668   -959       C
ATOM   1079  C   VAL A 139       2.477  19.425   0.648  1.00 54.95           C
ANISOU 1079  C   VAL A 139     6408   7272   7200    896    603  -1015       C
ATOM   1080  O   VAL A 139       1.291  19.749   0.501  1.00 50.69           O
ANISOU 1080  O   VAL A 139     5931   6737   6592    817    571  -1008       O
ATOM   1081  CB  VAL A 139       3.791  21.558   0.985  1.00 50.80           C
ANISOU 1081  CB  VAL A 139     5731   6910   6660    838    626   -803       C
ATOM   1082  CG1 VAL A 139       3.926  21.165   2.437  1.00 53.49           C
ANISOU 1082  CG1 VAL A 139     6090   7103   7132    860    550   -760       C
ATOM   1083  CG2 VAL A 139       5.013  22.372   0.511  1.00 49.95           C
ANISOU 1083  CG2 VAL A 139     5506   6952   6521    832    696   -750       C
ATOM   1084  N   ILE A 140       2.856  18.302   1.262  1.00 52.00           N
ANISOU 1084  N   ILE A 140     6063   6762   6932    973    585  -1070       N
ATOM   1085  CA  ILE A 140       1.915  17.361   1.866  1.00 45.62           C
ANISOU 1085  CA  ILE A 140     5377   5784   6173    950    531  -1119       C
ATOM   1086  C   ILE A 140       2.172  17.321   3.363  1.00 51.96           C
ANISOU 1086  C   ILE A 140     6196   6457   7090    961    462  -1020       C
ATOM   1087  O   ILE A 140       3.320  17.153   3.797  1.00 46.28           O
ANISOU 1087  O   ILE A 140     5415   5724   6444   1055    464   -994       O
ATOM   1088  CB  ILE A 140       2.025  15.953   1.252  1.00 52.53           C
ANISOU 1088  CB  ILE A 140     6316   6581   7062   1029    569  -1277       C
ATOM   1089  CG1 ILE A 140       1.738  16.003  -0.236  1.00 50.79           C
ANISOU 1089  CG1 ILE A 140     6081   6503   6714   1014    635  -1382       C
ATOM   1090  CG2 ILE A 140       1.022  14.988   1.892  1.00 53.48           C
ANISOU 1090  CG2 ILE A 140     6578   6512   7229    977    517  -1323       C
ATOM   1091  CD1 ILE A 140       1.791  14.634  -0.890  1.00 57.90           C
ANISOU 1091  CD1 ILE A 140     7055   7325   7619   1085    675  -1555       C
ATOM   1092  N   LYS A 141       1.101  17.482   4.145  1.00 48.99           N
ANISOU 1092  N   LYS A 141     5894   6001   6719    867    399   -969       N
ATOM   1093  CA  LYS A 141       1.137  17.469   5.602  1.00 53.91           C
ANISOU 1093  CA  LYS A 141     6548   6503   7431    858    330   -873       C
ATOM   1094  C   LYS A 141      -0.030  16.630   6.113  1.00 58.25           C
ANISOU 1094  C   LYS A 141     7228   6910   7994    789    293   -912       C
ATOM   1095  O   LYS A 141      -1.051  16.475   5.439  1.00 50.90           O
ANISOU 1095  O   LYS A 141     6338   6009   6991    714    308   -986       O
ATOM   1096  CB  LYS A 141       1.038  18.884   6.194  1.00 58.46           C
ANISOU 1096  CB  LYS A 141     7067   7159   7985    790    293   -742       C
ATOM   1097  CG  LYS A 141       2.370  19.560   6.425  1.00 70.99           C
ANISOU 1097  CG  LYS A 141     8544   8820   9610    844    302   -670       C
ATOM   1098  CD  LYS A 141       2.224  20.933   7.085  1.00 74.26           C
ANISOU 1098  CD  LYS A 141     8926   9283  10005    763    262   -547       C
ATOM   1099  CE  LYS A 141       1.928  22.031   6.065  1.00 78.96           C
ANISOU 1099  CE  LYS A 141     9491  10016  10493    703    305   -531       C
ATOM   1100  NZ  LYS A 141       2.098  23.415   6.618  1.00 79.46           N
ANISOU 1100  NZ  LYS A 141     9526  10121  10544    640    277   -413       N
ATOM   1101  N   VAL A 142       0.119  16.103   7.322  1.00 57.48           N
ANISOU 1101  N   VAL A 142     7192   6666   7983    808    243   -859       N
ATOM   1102  CA  VAL A 142      -0.926  15.326   7.974  1.00 57.76           C
ANISOU 1102  CA  VAL A 142     7355   6557   8034    727    211   -876       C
ATOM   1103  C   VAL A 142      -1.371  16.076   9.220  1.00 60.07           C
ANISOU 1103  C   VAL A 142     7645   6843   8337    655    150   -750       C
ATOM   1104  O   VAL A 142      -0.543  16.651   9.935  1.00 71.52           O
ANISOU 1104  O   VAL A 142     9037   8310   9829    709    119   -655       O
ATOM   1105  CB  VAL A 142      -0.429  13.907   8.312  1.00 65.26           C
ANISOU 1105  CB  VAL A 142     8415   7316   9066    812    210   -925       C
ATOM   1106  CG1 VAL A 142      -1.256  13.297   9.418  1.00 70.42           C
ANISOU 1106  CG1 VAL A 142     9199   7805   9750    725    165   -885       C
ATOM   1107  CG2 VAL A 142      -0.468  13.046   7.075  1.00 62.96           C
ANISOU 1107  CG2 VAL A 142     8166   7008   8747    843    270  -1078       C
ATOM   1108  N   LEU A 143      -2.675  16.090   9.472  1.00 58.51           N
ANISOU 1108  N   LEU A 143     7502   6635   8093    531    133   -758       N
ATOM   1109  CA  LEU A 143      -3.240  16.855  10.574  1.00 67.18           C
ANISOU 1109  CA  LEU A 143     8594   7750   9183    459     82   -654       C
ATOM   1110  C   LEU A 143      -3.871  15.954  11.628  1.00 77.95           C
ANISOU 1110  C   LEU A 143    10075   8960  10581    391     54   -638       C
ATOM   1111  O   LEU A 143      -4.461  14.915  11.314  1.00 78.79           O
ANISOU 1111  O   LEU A 143    10273   8979  10684    335     78   -725       O
ATOM   1112  CB  LEU A 143      -4.293  17.833  10.073  1.00 62.50           C
ANISOU 1112  CB  LEU A 143     7946   7309   8493    375     85   -663       C
ATOM   1113  CG  LEU A 143      -3.807  18.660   8.900  1.00 63.90           C
ANISOU 1113  CG  LEU A 143     8032   7630   8616    428    120   -680       C
ATOM   1114  CD1 LEU A 143      -4.995  19.397   8.339  1.00 51.59           C
ANISOU 1114  CD1 LEU A 143     6446   6205   6951    356    118   -702       C
ATOM   1115  CD2 LEU A 143      -2.735  19.615   9.391  1.00 64.44           C
ANISOU 1115  CD2 LEU A 143     8033   7730   8721    489    102   -574       C
ATOM   1116  N   GLU A 144      -3.775  16.398  12.883  1.00 75.70           N
ANISOU 1116  N   GLU A 144     9794   8648  10322    383      5   -528       N
ATOM   1117  CA  GLU A 144      -4.318  15.663  14.026  1.00 80.33           C
ANISOU 1117  CA  GLU A 144    10493   9098  10930    315    -22   -488       C
ATOM   1118  C   GLU A 144      -3.794  14.228  14.044  1.00 86.17           C
ANISOU 1118  C   GLU A 144    11355   9651  11736    372    -10   -527       C
ATOM   1119  O   GLU A 144      -4.509  13.285  14.388  1.00 92.34           O
ANISOU 1119  O   GLU A 144    12262  10306  12519    284     -2   -551       O
ATOM   1120  CB  GLU A 144      -5.851  15.693  14.025  1.00 78.60           C
ANISOU 1120  CB  GLU A 144    10296   8931  10639    160    -10   -529       C
ATOM   1121  CG  GLU A 144      -6.458  17.089  14.106  1.00 81.09           C
ANISOU 1121  CG  GLU A 144    10505   9421  10885    122    -28   -490       C
ATOM   1122  CD  GLU A 144      -6.263  17.745  15.467  1.00 89.16           C
ANISOU 1122  CD  GLU A 144    11523  10434  11922    129    -77   -371       C
ATOM   1123  OE1 GLU A 144      -6.208  18.994  15.527  1.00 89.85           O
ANISOU 1123  OE1 GLU A 144    11527  10637  11977    153    -97   -326       O
ATOM   1124  OE2 GLU A 144      -6.169  17.015  16.477  1.00 94.03           O
ANISOU 1124  OE2 GLU A 144    12230  10922  12576    110    -97   -322       O
ATOM   1125  N   GLY A 145      -2.531  14.063  13.664  1.00 88.52           N
ANISOU 1125  N   GLY A 145    11616   9930  12086    521     -6   -534       N
ATOM   1126  CA  GLY A 145      -1.927  12.753  13.526  1.00 94.45           C
ANISOU 1126  CA  GLY A 145    12478  10511  12898    614      7   -583       C
ATOM   1127  C   GLY A 145      -1.141  12.331  14.754  1.00 98.13           C
ANISOU 1127  C   GLY A 145    13009  10848  13428    710    -49   -480       C
ATOM   1128  O   GLY A 145      -0.497  13.145  15.412  1.00 96.95           O
ANISOU 1128  O   GLY A 145    12765  10781  13289    764    -93   -387       O
ATOM   1129  N   THR A 146      -1.206  11.033  15.052  1.00102.52           N
ANISOU 1129  N   THR A 146    13736  11195  14020    729    -48   -498       N
ATOM   1130  CA  THR A 146      -0.458  10.462  16.165  1.00103.36           C
ANISOU 1130  CA  THR A 146    13932  11159  14181    840   -104   -401       C
ATOM   1131  C   THR A 146       0.986  10.132  15.795  1.00102.49           C
ANISOU 1131  C   THR A 146    13773  11039  14132   1065   -113   -424       C
ATOM   1132  O   THR A 146       1.840  10.061  16.686  1.00102.41           O
ANISOU 1132  O   THR A 146    13760  10992  14157   1190   -173   -333       O
ATOM   1133  CB  THR A 146      -1.155   9.189  16.673  1.00101.54           C
ANISOU 1133  CB  THR A 146    13933  10690  13959    765    -99   -401       C
ATOM   1134  OG1 THR A 146      -1.626   8.408  15.564  1.00100.17           O
ANISOU 1134  OG1 THR A 146    13838  10440  13781    717    -36   -541       O
ATOM   1135  CG2 THR A 146      -2.331   9.541  17.577  1.00 96.32           C
ANISOU 1135  CG2 THR A 146    13312  10045  13242    568   -111   -328       C
ATOM   1136  N   GLN A 147       1.271   9.938  14.508  1.00101.12           N
ANISOU 1136  N   GLN A 147    13550  10911  13961   1123    -56   -548       N
ATOM   1137  CA  GLN A 147       2.525   9.366  14.035  1.00 94.29           C
ANISOU 1137  CA  GLN A 147    12660  10017  13149   1340    -49   -600       C
ATOM   1138  C   GLN A 147       3.612  10.399  13.772  1.00 92.27           C
ANISOU 1138  C   GLN A 147    12176   9986  12896   1442    -56   -578       C
ATOM   1139  O   GLN A 147       4.714  10.010  13.373  1.00 95.01           O
ANISOU 1139  O   GLN A 147    12468  10350  13281   1627    -47   -624       O
ATOM   1140  CB  GLN A 147       2.275   8.558  12.753  1.00 93.24           C
ANISOU 1140  CB  GLN A 147    12598   9819  13008   1348     24   -759       C
ATOM   1141  CG  GLN A 147       1.423   7.308  12.949  1.00 95.24           C
ANISOU 1141  CG  GLN A 147    13100   9817  13272   1268     34   -799       C
ATOM   1142  CD  GLN A 147      -0.066   7.616  12.990  1.00 96.73           C
ANISOU 1142  CD  GLN A 147    13326  10029  13398   1011     52   -803       C
ATOM   1143  OE1 GLN A 147      -0.510   8.673  12.530  1.00 96.77           O
ANISOU 1143  OE1 GLN A 147    13179  10242  13347    913     69   -813       O
ATOM   1144  NE2 GLN A 147      -0.846   6.693  13.547  1.00 97.61           N
ANISOU 1144  NE2 GLN A 147    13644   9930  13514    903     49   -795       N
ATOM   1145  N   GLY A 148       3.337  11.689  13.979  1.00 90.31           N
ANISOU 1145  N   GLY A 148    11798   9910  12606   1327    -68   -513       N
ATOM   1146  CA  GLY A 148       4.312  12.743  13.748  1.00 87.79           C
ANISOU 1146  CA  GLY A 148    11273   9800  12285   1387    -69   -488       C
ATOM   1147  C   GLY A 148       4.942  12.703  12.367  1.00 86.69           C
ANISOU 1147  C   GLY A 148    11031   9770  12137   1471      4   -603       C
ATOM   1148  O   GLY A 148       6.171  12.724  12.231  1.00 82.74           O
ANISOU 1148  O   GLY A 148    10413   9356  11669   1621      3   -611       O
ATOM   1149  N   ILE A 149       4.105  12.640  11.329  1.00 85.63           N
ANISOU 1149  N   ILE A 149    10934   9649  11952   1375     68   -696       N
ATOM   1150  CA  ILE A 149       4.630  12.425   9.985  1.00 77.41           C
ANISOU 1150  CA  ILE A 149     9825   8695  10893   1458    142   -817       C
ATOM   1151  C   ILE A 149       5.337  13.677   9.469  1.00 77.26           C
ANISOU 1151  C   ILE A 149     9600   8917  10837   1453    171   -791       C
ATOM   1152  O   ILE A 149       6.322  13.580   8.726  1.00 82.34           O
ANISOU 1152  O   ILE A 149    10138   9663  11484   1571    219   -855       O
ATOM   1153  CB  ILE A 149       3.494  11.947   9.062  1.00 67.14           C
ANISOU 1153  CB  ILE A 149     8633   7339   9539   1351    195   -928       C
ATOM   1154  CG1 ILE A 149       3.141  10.494   9.389  1.00 70.83           C
ANISOU 1154  CG1 ILE A 149     9305   7554  10052   1387    182   -980       C
ATOM   1155  CG2 ILE A 149       3.894  12.038   7.613  1.00 66.47           C
ANISOU 1155  CG2 ILE A 149     8456   7393   9405   1400    275  -1045       C
ATOM   1156  CD1 ILE A 149       1.657  10.205   9.397  1.00 72.92           C
ANISOU 1156  CD1 ILE A 149     9706   7725  10276   1197    187  -1010       C
ATOM   1157  N   GLY A 150       4.892  14.862   9.884  1.00 70.66           N
ANISOU 1157  N   GLY A 150     8707   8173   9965   1319    145   -698       N
ATOM   1158  CA  GLY A 150       5.595  16.058   9.453  1.00 65.22           C
ANISOU 1158  CA  GLY A 150     7846   7692   9244   1302    173   -665       C
ATOM   1159  C   GLY A 150       5.291  16.410   8.004  1.00 64.16           C
ANISOU 1159  C   GLY A 150     7671   7678   9027   1251    257   -748       C
ATOM   1160  O   GLY A 150       4.231  16.081   7.467  1.00 70.83           O
ANISOU 1160  O   GLY A 150     8616   8472   9826   1180    278   -809       O
ATOM   1161  N   VAL A 151       6.253  17.069   7.353  1.00 60.94           N
ANISOU 1161  N   VAL A 151     7113   7446   8595   1284    307   -751       N
ATOM   1162  CA  VAL A 151       6.056  17.684   6.043  1.00 58.42           C
ANISOU 1162  CA  VAL A 151     6742   7272   8181   1221    385   -798       C
ATOM   1163  C   VAL A 151       6.769  16.877   4.963  1.00 55.73           C
ANISOU 1163  C   VAL A 151     6357   6988   7828   1345    463   -925       C
ATOM   1164  O   VAL A 151       7.908  16.428   5.151  1.00 49.58           O
ANISOU 1164  O   VAL A 151     5496   6234   7107   1479    469   -946       O
ATOM   1165  CB  VAL A 151       6.549  19.145   6.040  1.00 59.38           C
ANISOU 1165  CB  VAL A 151     6739   7556   8265   1138    396   -702       C
ATOM   1166  CG1 VAL A 151       6.251  19.789   4.710  1.00 54.77           C
ANISOU 1166  CG1 VAL A 151     6131   7109   7572   1069    475   -735       C
ATOM   1167  CG2 VAL A 151       5.879  19.935   7.155  1.00 58.62           C
ANISOU 1167  CG2 VAL A 151     6695   7397   8182   1031    318   -587       C
ATOM   1168  N   VAL A 152       6.104  16.719   3.818  1.00 50.06           N
ANISOU 1168  N   VAL A 152     5688   6306   7028   1306    521  -1014       N
ATOM   1169  CA  VAL A 152       6.665  16.056   2.647  1.00 55.38           C
ANISOU 1169  CA  VAL A 152     6324   7052   7665   1408    605  -1146       C
ATOM   1170  C   VAL A 152       6.504  16.983   1.445  1.00 54.75           C
ANISOU 1170  C   VAL A 152     6177   7164   7460   1320    678  -1154       C
ATOM   1171  O   VAL A 152       5.386  17.416   1.138  1.00 54.06           O
ANISOU 1171  O   VAL A 152     6164   7075   7300   1205    666  -1139       O
ATOM   1172  CB  VAL A 152       5.991  14.697   2.387  1.00 55.32           C
ANISOU 1172  CB  VAL A 152     6471   6876   7672   1458    603  -1273       C
ATOM   1173  CG1 VAL A 152       6.429  14.125   1.034  1.00 50.97           C
ANISOU 1173  CG1 VAL A 152     5891   6415   7061   1548    696  -1424       C
ATOM   1174  CG2 VAL A 152       6.289  13.713   3.529  1.00 53.83           C
ANISOU 1174  CG2 VAL A 152     6363   6486   7603   1563    538  -1261       C
ATOM   1175  N   LEU A 153       7.621  17.290   0.772  1.00 60.09           N
ANISOU 1175  N   LEU A 153     6713   8013   8105   1378    753  -1174       N
ATOM   1176  CA  LEU A 153       7.640  18.105  -0.443  1.00 52.14           C
ANISOU 1176  CA  LEU A 153     5643   7198   6969   1306    836  -1181       C
ATOM   1177  C   LEU A 153       7.759  17.193  -1.648  1.00 51.74           C
ANISOU 1177  C   LEU A 153     5605   7198   6857   1398    916  -1344       C
ATOM   1178  O   LEU A 153       8.699  16.399  -1.722  1.00 48.82           O
ANISOU 1178  O   LEU A 153     5174   6837   6537   1543    950  -1428       O
ATOM   1179  CB  LEU A 153       8.816  19.077  -0.457  1.00 56.41           C
ANISOU 1179  CB  LEU A 153     6017   7917   7500   1286    882  -1099       C
ATOM   1180  CG  LEU A 153       8.847  20.271   0.474  1.00 69.23           C
ANISOU 1180  CG  LEU A 153     7610   9542   9152   1168    825   -941       C
ATOM   1181  CD1 LEU A 153       9.288  19.852   1.864  1.00 72.61           C
ANISOU 1181  CD1 LEU A 153     8021   9853   9715   1235    740   -902       C
ATOM   1182  CD2 LEU A 153       9.786  21.297  -0.123  1.00 80.54           C
ANISOU 1182  CD2 LEU A 153     8902  11184  10517   1103    907   -889       C
ATOM   1183  N   CYS A 154       6.842  17.326  -2.606  1.00 48.70           N
ANISOU 1183  N   CYS A 154     5292   6856   6356   1324    944  -1392       N
ATOM   1184  CA  CYS A 154       6.861  16.489  -3.801  1.00 56.08           C
ANISOU 1184  CA  CYS A 154     6249   7844   7215   1399   1018  -1558       C
ATOM   1185  C   CYS A 154       7.118  17.345  -5.033  1.00 56.79           C
ANISOU 1185  C   CYS A 154     6256   8168   7153   1346   1110  -1551       C
ATOM   1186  O   CYS A 154       6.386  18.307  -5.288  1.00 58.00           O
ANISOU 1186  O   CYS A 154     6439   8380   7216   1221   1095  -1462       O
ATOM   1187  CB  CYS A 154       5.541  15.735  -3.969  1.00 62.31           C
ANISOU 1187  CB  CYS A 154     7201   8493   7982   1358    973  -1649       C
ATOM   1188  SG  CYS A 154       5.187  14.510  -2.703  1.00 59.77           S
ANISOU 1188  SG  CYS A 154     7010   7881   7819   1412    884  -1680       S
ATOM   1189  N   GLU A 155       8.141  16.980  -5.806  1.00 52.90           N
ANISOU 1189  N   GLU A 155     5663   7811   6624   1448   1205  -1645       N
ATOM   1190  CA  GLU A 155       8.429  17.728  -7.025  1.00 58.16           C
ANISOU 1190  CA  GLU A 155     6256   8710   7134   1396   1305  -1641       C
ATOM   1191  C   GLU A 155       7.316  17.567  -8.062  1.00 62.88           C
ANISOU 1191  C   GLU A 155     6967   9333   7592   1346   1315  -1724       C
ATOM   1192  O   GLU A 155       6.869  18.559  -8.649  1.00 64.36           O
ANISOU 1192  O   GLU A 155     7163   9640   7652   1237   1332  -1641       O
ATOM   1193  CB  GLU A 155       9.776  17.294  -7.603  1.00 54.84           C
ANISOU 1193  CB  GLU A 155     5693   8443   6701   1523   1411  -1738       C
ATOM   1194  CG  GLU A 155      10.184  18.076  -8.827  1.00 60.20           C
ANISOU 1194  CG  GLU A 155     6284   9376   7211   1461   1526  -1726       C
ATOM   1195  CD  GLU A 155      11.377  17.459  -9.561  1.00 72.06           C
ANISOU 1195  CD  GLU A 155     7653  11046   8682   1598   1643  -1861       C
ATOM   1196  OE1 GLU A 155      12.029  16.540  -9.014  1.00 73.40           O
ANISOU 1196  OE1 GLU A 155     7776  11138   8972   1752   1629  -1946       O
ATOM   1197  OE2 GLU A 155      11.656  17.900 -10.698  1.00 75.38           O
ANISOU 1197  OE2 GLU A 155     8016  11680   8947   1558   1749  -1882       O
ATOM   1198  N   THR A 156       6.846  16.339  -8.292  1.00 62.46           N
ANISOU 1198  N   THR A 156     7009   9166   7556   1421   1300  -1886       N
ATOM   1199  CA  THR A 156       5.910  16.043  -9.368  1.00 58.54           C
ANISOU 1199  CA  THR A 156     6604   8718   6921   1383   1316  -1998       C
ATOM   1200  C   THR A 156       4.542  15.635  -8.836  1.00 62.61           C
ANISOU 1200  C   THR A 156     7263   9049   7476   1311   1211  -2015       C
ATOM   1201  O   THR A 156       4.380  15.252  -7.669  1.00 58.89           O
ANISOU 1201  O   THR A 156     6840   8385   7151   1317   1136  -1977       O
ATOM   1202  CB  THR A 156       6.431  14.914 -10.257  1.00 62.71           C
ANISOU 1202  CB  THR A 156     7132   9285   7411   1514   1397  -2204       C
ATOM   1203  OG1 THR A 156       6.232  13.680  -9.566  1.00 66.54           O
ANISOU 1203  OG1 THR A 156     7717   9533   8031   1593   1341  -2307       O
ATOM   1204  CG2 THR A 156       7.911  15.097 -10.544  1.00 65.55           C
ANISOU 1204  CG2 THR A 156     7331   9809   7768   1613   1499  -2204       C
ATOM   1205  N   ALA A 157       3.552  15.705  -9.733  1.00 62.26           N
ANISOU 1205  N   ALA A 157     7284   9083   7289   1239   1207  -2078       N
ATOM   1206  CA  ALA A 157       2.198  15.297  -9.372  1.00 61.96           C
ANISOU 1206  CA  ALA A 157     7366   8911   7267   1158   1115  -2116       C
ATOM   1207  C   ALA A 157       2.099  13.787  -9.228  1.00 63.16           C
ANISOU 1207  C   ALA A 157     7614   8880   7504   1219   1107  -2293       C
ATOM   1208  O   ALA A 157       1.300  13.292  -8.425  1.00 62.98           O
ANISOU 1208  O   ALA A 157     7686   8677   7568   1161   1029  -2299       O
ATOM   1209  CB  ALA A 157       1.199  15.792 -10.417  1.00 60.91           C
ANISOU 1209  CB  ALA A 157     7260   8939   6946   1072   1110  -2142       C
ATOM   1210  N   THR A 158       2.906  13.040  -9.984  1.00 56.83           N
ANISOU 1210  N   THR A 158     6797   8120   6677   1336   1190  -2439       N
ATOM   1211  CA  THR A 158       2.846  11.586  -9.885  1.00 60.57           C
ANISOU 1211  CA  THR A 158     7385   8399   7228   1406   1185  -2616       C
ATOM   1212  C   THR A 158       3.400  11.098  -8.549  1.00 67.27           C
ANISOU 1212  C   THR A 158     8258   9027   8273   1482   1142  -2552       C
ATOM   1213  O   THR A 158       2.851  10.169  -7.946  1.00 68.74           O
ANISOU 1213  O   THR A 158     8582   8988   8550   1467   1088  -2614       O
ATOM   1214  CB  THR A 158       3.577  10.948 -11.067  1.00 66.50           C
ANISOU 1214  CB  THR A 158     8116   9257   7893   1527   1287  -2796       C
ATOM   1215  OG1 THR A 158       3.465   9.525 -10.985  1.00 72.81           O
ANISOU 1215  OG1 THR A 158     9053   9844   8767   1596   1280  -2975       O
ATOM   1216  CG2 THR A 158       5.035  11.315 -11.083  1.00 72.10           C
ANISOU 1216  CG2 THR A 158     8679  10087   8631   1659   1366  -2740       C
ATOM   1217  N   ALA A 159       4.468  11.724  -8.052  1.00 65.60           N
ANISOU 1217  N   ALA A 159     7921   8882   8123   1556   1164  -2426       N
ATOM   1218  CA  ALA A 159       4.939  11.411  -6.707  1.00 64.46           C
ANISOU 1218  CA  ALA A 159     7790   8551   8152   1622   1108  -2342       C
ATOM   1219  C   ALA A 159       3.892  11.781  -5.657  1.00 61.65           C
ANISOU 1219  C   ALA A 159     7508   8063   7853   1478   1005  -2214       C
ATOM   1220  O   ALA A 159       3.575  10.978  -4.770  1.00 59.37           O
ANISOU 1220  O   ALA A 159     7335   7548   7676   1486    946  -2225       O
ATOM   1221  CB  ALA A 159       6.256  12.137  -6.430  1.00 66.02           C
ANISOU 1221  CB  ALA A 159     7814   8887   8385   1708   1147  -2231       C
ATOM   1222  N   ALA A 160       3.351  13.002  -5.738  1.00 51.68           N
ANISOU 1222  N   ALA A 160     6185   6940   6510   1351    986  -2090       N
ATOM   1223  CA  ALA A 160       2.330  13.442  -4.789  1.00 53.72           C
ANISOU 1223  CA  ALA A 160     6500   7103   6809   1222    894  -1975       C
ATOM   1224  C   ALA A 160       1.157  12.465  -4.729  1.00 52.48           C
ANISOU 1224  C   ALA A 160     6494   6789   6658   1147    849  -2089       C
ATOM   1225  O   ALA A 160       0.645  12.150  -3.649  1.00 57.37           O
ANISOU 1225  O   ALA A 160     7192   7233   7373   1095    781  -2037       O
ATOM   1226  CB  ALA A 160       1.840  14.839  -5.170  1.00 58.09           C
ANISOU 1226  CB  ALA A 160     6982   7844   7245   1115    888  -1859       C
ATOM   1227  N   GLU A 161       0.716  11.979  -5.884  1.00 53.84           N
ANISOU 1227  N   GLU A 161     6708   7029   6720   1130    889  -2247       N
ATOM   1228  CA  GLU A 161      -0.348  10.982  -5.898  1.00 59.91           C
ANISOU 1228  CA  GLU A 161     7618   7654   7490   1045    853  -2376       C
ATOM   1229  C   GLU A 161       0.033   9.756  -5.070  1.00 60.72           C
ANISOU 1229  C   GLU A 161     7841   7486   7743   1117    839  -2428       C
ATOM   1230  O   GLU A 161      -0.752   9.300  -4.228  1.00 57.74           O
ANISOU 1230  O   GLU A 161     7571   6934   7433   1021    779  -2410       O
ATOM   1231  CB  GLU A 161      -0.677  10.591  -7.335  1.00 63.71           C
ANISOU 1231  CB  GLU A 161     8121   8260   7828   1033    904  -2558       C
ATOM   1232  CG  GLU A 161      -2.036   9.952  -7.485  1.00 67.55           C
ANISOU 1232  CG  GLU A 161     8718   8676   8270    887    858  -2674       C
ATOM   1233  CD  GLU A 161      -2.451   9.841  -8.931  1.00 75.29           C
ANISOU 1233  CD  GLU A 161     9693   9834   9079    858    896  -2833       C
ATOM   1234  OE1 GLU A 161      -1.830  10.517  -9.784  1.00 70.72           O
ANISOU 1234  OE1 GLU A 161     9013   9460   8397    932    953  -2815       O
ATOM   1235  OE2 GLU A 161      -3.387   9.065  -9.210  1.00 83.40           O
ANISOU 1235  OE2 GLU A 161    10818  10799  10069    753    871  -2979       O
ATOM   1236  N   SER A 162       1.250   9.226  -5.275  1.00 55.20           N
ANISOU 1236  N   SER A 162     7127   6754   7093   1292    895  -2487       N
ATOM   1237  CA  SER A 162       1.695   8.053  -4.520  1.00 56.64           C
ANISOU 1237  CA  SER A 162     7433   6673   7413   1395    879  -2533       C
ATOM   1238  C   SER A 162       1.809   8.352  -3.033  1.00 60.11           C
ANISOU 1238  C   SER A 162     7874   6989   7977   1386    808  -2351       C
ATOM   1239  O   SER A 162       1.444   7.519  -2.195  1.00 72.51           O
ANISOU 1239  O   SER A 162     9592   8318   9638   1364    762  -2353       O
ATOM   1240  CB  SER A 162       3.046   7.555  -5.045  1.00 57.94           C
ANISOU 1240  CB  SER A 162     7553   6864   7597   1613    952  -2625       C
ATOM   1241  OG  SER A 162       2.883   6.822  -6.231  1.00 65.82           O
ANISOU 1241  OG  SER A 162     8618   7882   8507   1636   1011  -2831       O
ATOM   1242  N   VAL A 163       2.327   9.526  -2.680  1.00 54.61           N
ANISOU 1242  N   VAL A 163     7021   6449   7281   1398    800  -2193       N
ATOM   1243  CA  VAL A 163       2.479   9.854  -1.271  1.00 48.80           C
ANISOU 1243  CA  VAL A 163     6278   5610   6653   1392    732  -2026       C
ATOM   1244  C   VAL A 163       1.109  10.046  -0.607  1.00 57.95           C
ANISOU 1244  C   VAL A 163     7521   6689   7807   1202    664  -1962       C
ATOM   1245  O   VAL A 163       0.875   9.556   0.504  1.00 57.56           O
ANISOU 1245  O   VAL A 163     7573   6445   7851   1182    609  -1904       O
ATOM   1246  CB  VAL A 163       3.373  11.094  -1.118  1.00 55.91           C
ANISOU 1246  CB  VAL A 163     6991   6706   7546   1435    743  -1887       C
ATOM   1247  CG1 VAL A 163       3.548  11.446   0.357  1.00 58.95           C
ANISOU 1247  CG1 VAL A 163     7368   6993   8037   1427    667  -1723       C
ATOM   1248  CG2 VAL A 163       4.730  10.866  -1.819  1.00 54.20           C
ANISOU 1248  CG2 VAL A 163     6672   6597   7326   1615    820  -1963       C
ATOM   1249  N   ILE A 164       0.183  10.753  -1.267  1.00 52.94           N
ANISOU 1249  N   ILE A 164     6845   6212   7057   1067    667  -1971       N
ATOM   1250  CA  ILE A 164      -1.164  10.895  -0.699  1.00 54.64           C
ANISOU 1250  CA  ILE A 164     7125   6377   7259    894    606  -1930       C
ATOM   1251  C   ILE A 164      -1.821   9.529  -0.544  1.00 57.85           C
ANISOU 1251  C   ILE A 164     7708   6568   7706    836    595  -2054       C
ATOM   1252  O   ILE A 164      -2.448   9.239   0.483  1.00 59.96           O
ANISOU 1252  O   ILE A 164     8063   6687   8034    744    545  -1995       O
ATOM   1253  CB  ILE A 164      -2.039  11.834  -1.553  1.00 55.58           C
ANISOU 1253  CB  ILE A 164     7164   6718   7234    785    609  -1935       C
ATOM   1254  CG1 ILE A 164      -1.472  13.259  -1.559  1.00 54.81           C
ANISOU 1254  CG1 ILE A 164     6923   6801   7102    821    613  -1788       C
ATOM   1255  CG2 ILE A 164      -3.496  11.838  -1.032  1.00 48.37           C
ANISOU 1255  CG2 ILE A 164     6310   5768   6301    613    548  -1923       C
ATOM   1256  CD1 ILE A 164      -1.946  14.080  -2.744  1.00 55.67           C
ANISOU 1256  CD1 ILE A 164     6961   7137   7053    775    639  -1813       C
ATOM   1257  N   GLU A 165      -1.678   8.665  -1.556  1.00 56.69           N
ANISOU 1257  N   GLU A 165     7624   6396   7519    882    647  -2231       N
ATOM   1258  CA  GLU A 165      -2.208   7.307  -1.458  1.00 63.40           C
ANISOU 1258  CA  GLU A 165     8663   7017   8409    826    644  -2361       C
ATOM   1259  C   GLU A 165      -1.654   6.577  -0.240  1.00 67.27           C
ANISOU 1259  C   GLU A 165     9271   7245   9044    908    615  -2289       C
ATOM   1260  O   GLU A 165      -2.365   5.793   0.399  1.00 66.14           O
ANISOU 1260  O   GLU A 165     9286   6898   8947    799    585  -2305       O
ATOM   1261  CB  GLU A 165      -1.892   6.520  -2.731  1.00 65.79           C
ANISOU 1261  CB  GLU A 165     9015   7327   8653    900    708  -2566       C
ATOM   1262  CG  GLU A 165      -2.670   6.969  -3.951  1.00 75.82           C
ANISOU 1262  CG  GLU A 165    10215   8825   9767    793    729  -2667       C
ATOM   1263  CD  GLU A 165      -2.788   5.894  -5.007  1.00 85.39           C
ANISOU 1263  CD  GLU A 165    11539   9982  10924    799    776  -2898       C
ATOM   1264  OE1 GLU A 165      -2.121   4.845  -4.875  1.00 90.99           O
ANISOU 1264  OE1 GLU A 165    12375  10479  11718    915    802  -2981       O
ATOM   1265  OE2 GLU A 165      -3.543   6.107  -5.978  1.00 88.10           O
ANISOU 1265  OE2 GLU A 165    11845  10497  11132    695    784  -2999       O
ATOM   1266  N   ALA A 166      -0.383   6.818   0.094  1.00 66.15           N
ANISOU 1266  N   ALA A 166     9054   7113   8968   1095    622  -2207       N
ATOM   1267  CA  ALA A 166       0.210   6.165   1.255  1.00 63.77           C
ANISOU 1267  CA  ALA A 166     8855   6581   8794   1198    586  -2130       C
ATOM   1268  C   ALA A 166      -0.394   6.688   2.549  1.00 64.11           C
ANISOU 1268  C   ALA A 166     8902   6579   8876   1074    517  -1958       C
ATOM   1269  O   ALA A 166      -0.739   5.907   3.446  1.00 63.03           O
ANISOU 1269  O   ALA A 166     8929   6212   8807   1031    482  -1928       O
ATOM   1270  CB  ALA A 166       1.724   6.367   1.256  1.00 64.05           C
ANISOU 1270  CB  ALA A 166     8776   6684   8878   1432    606  -2091       C
ATOM   1271  N   PHE A 167      -0.514   8.016   2.675  1.00 62.20           N
ANISOU 1271  N   PHE A 167     8492   6552   8589   1018    499  -1841       N
ATOM   1272  CA  PHE A 167      -1.039   8.593   3.908  1.00 62.24           C
ANISOU 1272  CA  PHE A 167     8492   6532   8626    914    436  -1682       C
ATOM   1273  C   PHE A 167      -2.501   8.229   4.120  1.00 57.11           C
ANISOU 1273  C   PHE A 167     7951   5807   7940    704    417  -1718       C
ATOM   1274  O   PHE A 167      -2.963   8.177   5.265  1.00 55.10           O
ANISOU 1274  O   PHE A 167     7762   5446   7729    622    371  -1617       O
ATOM   1275  CB  PHE A 167      -0.850  10.112   3.900  1.00 60.03           C
ANISOU 1275  CB  PHE A 167     8019   6491   8297    904    426  -1566       C
ATOM   1276  CG  PHE A 167       0.590  10.532   4.013  1.00 67.47           C
ANISOU 1276  CG  PHE A 167     8846   7502   9287   1079    435  -1500       C
ATOM   1277  CD1 PHE A 167       1.556   9.620   4.418  1.00 69.07           C
ANISOU 1277  CD1 PHE A 167     9111   7551   9580   1242    432  -1517       C
ATOM   1278  CD2 PHE A 167       0.981  11.830   3.721  1.00 67.72           C
ANISOU 1278  CD2 PHE A 167     8708   7752   9269   1082    446  -1424       C
ATOM   1279  CE1 PHE A 167       2.886   9.995   4.530  1.00 69.27           C
ANISOU 1279  CE1 PHE A 167     9009   7666   9645   1404    439  -1465       C
ATOM   1280  CE2 PHE A 167       2.311  12.208   3.827  1.00 66.61           C
ANISOU 1280  CE2 PHE A 167     8451   7689   9169   1221    459  -1371       C
ATOM   1281  CZ  PHE A 167       3.263  11.289   4.234  1.00 61.67           C
ANISOU 1281  CZ  PHE A 167     7865   6935   8633   1382    454  -1394       C
ATOM   1282  N   MET A 168      -3.239   7.994   3.031  1.00 53.43           N
ANISOU 1282  N   MET A 168     7499   5415   7388    610    451  -1863       N
ATOM   1283  CA  MET A 168      -4.598   7.481   3.136  1.00 60.52           C
ANISOU 1283  CA  MET A 168     8500   6245   8250    405    439  -1928       C
ATOM   1284  C   MET A 168      -4.608   6.114   3.812  1.00 67.19           C
ANISOU 1284  C   MET A 168     9563   6784   9182    387    435  -1961       C
ATOM   1285  O   MET A 168      -5.466   5.838   4.661  1.00 72.65           O
ANISOU 1285  O   MET A 168    10343   7371   9889    230    407  -1914       O
ATOM   1286  CB  MET A 168      -5.233   7.405   1.741  1.00 56.93           C
ANISOU 1286  CB  MET A 168     8014   5935   7682    329    475  -2097       C
ATOM   1287  CG  MET A 168      -5.729   8.769   1.203  1.00 51.94           C
ANISOU 1287  CG  MET A 168     7197   5600   6938    281    464  -2051       C
ATOM   1288  SD  MET A 168      -6.203   8.715  -0.552  1.00 61.18           S
ANISOU 1288  SD  MET A 168     8321   6965   7961    243    505  -2245       S
ATOM   1289  CE  MET A 168      -7.531   7.503  -0.551  1.00 55.99           C
ANISOU 1289  CE  MET A 168     7816   6173   7285     25    496  -2401       C
ATOM   1290  N   GLY A 169      -3.644   5.250   3.464  1.00 64.68           N
ANISOU 1290  N   GLY A 169     9339   6318   8920    552    465  -2040       N
ATOM   1291  CA  GLY A 169      -3.532   3.959   4.131  1.00 59.80           C
ANISOU 1291  CA  GLY A 169     8950   5382   8388    568    459  -2058       C
ATOM   1292  C   GLY A 169      -3.428   4.077   5.640  1.00 61.47           C
ANISOU 1292  C   GLY A 169     9207   5474   8674    567    405  -1871       C
ATOM   1293  O   GLY A 169      -3.818   3.161   6.368  1.00 68.00           O
ANISOU 1293  O   GLY A 169    10233   6057   9546    489    392  -1856       O
ATOM   1294  N   LEU A 170      -2.939   5.213   6.135  1.00 61.68           N
ANISOU 1294  N   LEU A 170     9060   5671   8706    641    374  -1726       N
ATOM   1295  CA  LEU A 170      -2.831   5.446   7.568  1.00 63.83           C
ANISOU 1295  CA  LEU A 170     9355   5862   9034    641    318  -1548       C
ATOM   1296  C   LEU A 170      -4.033   6.201   8.129  1.00 67.63           C
ANISOU 1296  C   LEU A 170     9777   6459   9460    425    294  -1471       C
ATOM   1297  O   LEU A 170      -3.998   6.628   9.289  1.00 65.16           O
ANISOU 1297  O   LEU A 170     9450   6132   9175    415    249  -1321       O
ATOM   1298  CB  LEU A 170      -1.529   6.193   7.878  1.00 66.50           C
ANISOU 1298  CB  LEU A 170     9546   6307   9415    850    294  -1441       C
ATOM   1299  CG  LEU A 170      -0.261   5.667   7.180  1.00 70.85           C
ANISOU 1299  CG  LEU A 170    10090   6824  10005   1085    325  -1526       C
ATOM   1300  CD1 LEU A 170       0.971   6.344   7.732  1.00 72.71           C
ANISOU 1300  CD1 LEU A 170    10181   7159  10286   1266    292  -1406       C
ATOM   1301  CD2 LEU A 170      -0.121   4.158   7.278  1.00 72.11           C
ANISOU 1301  CD2 LEU A 170    10491   6684  10223   1154    333  -1607       C
ATOM   1302  N   LYS A 171      -5.090   6.372   7.327  1.00 71.14           N
ANISOU 1302  N   LYS A 171    10180   7030   9820    259    320  -1576       N
ATOM   1303  CA  LYS A 171      -6.363   6.936   7.787  1.00 69.76           C
ANISOU 1303  CA  LYS A 171     9955   6966   9585     50    300  -1531       C
ATOM   1304  C   LYS A 171      -6.178   8.325   8.392  1.00 63.24           C
ANISOU 1304  C   LYS A 171     8957   6324   8745     94    261  -1380       C
ATOM   1305  O   LYS A 171      -6.823   8.691   9.378  1.00 65.53           O
ANISOU 1305  O   LYS A 171     9242   6627   9027    -13    231  -1281       O
ATOM   1306  CB  LYS A 171      -7.053   5.993   8.774  1.00 69.55           C
ANISOU 1306  CB  LYS A 171    10117   6717   9590   -100    292  -1502       C
ATOM   1307  CG  LYS A 171      -7.393   4.629   8.174  1.00 71.01           C
ANISOU 1307  CG  LYS A 171    10492   6706   9781   -184    332  -1660       C
ATOM   1308  CD  LYS A 171      -8.293   4.774   6.946  1.00 72.85           C
ANISOU 1308  CD  LYS A 171    10641   7122   9917   -320    362  -1824       C
ATOM   1309  CE  LYS A 171      -8.869   3.431   6.522  1.00 81.13           C
ANISOU 1309  CE  LYS A 171    11888   7975  10963   -465    398  -1982       C
ATOM   1310  NZ  LYS A 171      -9.628   3.520   5.244  1.00 85.53           N
ANISOU 1310  NZ  LYS A 171    12359   8718  11420   -579    422  -2158       N
ATOM   1311  N   GLN A 172      -5.295   9.109   7.787  1.00 63.31           N
ANISOU 1311  N   GLN A 172     8828   6479   8746    245    267  -1366       N
ATOM   1312  CA  GLN A 172      -4.957  10.435   8.283  1.00 63.76           C
ANISOU 1312  CA  GLN A 172     8735   6694   8795    296    234  -1231       C
ATOM   1313  C   GLN A 172      -5.751  11.516   7.553  1.00 51.59           C
ANISOU 1313  C   GLN A 172     7055   5397   7151    214    239  -1255       C
ATOM   1314  O   GLN A 172      -6.211  11.336   6.424  1.00 54.32           O
ANISOU 1314  O   GLN A 172     7385   5827   7428    171    271  -1381       O
ATOM   1315  CB  GLN A 172      -3.456  10.690   8.122  1.00 68.39           C
ANISOU 1315  CB  GLN A 172     9253   7296   9435    501    238  -1191       C
ATOM   1316  CG  GLN A 172      -2.577   9.559   8.650  1.00 77.72           C
ANISOU 1316  CG  GLN A 172    10567   8251  10713    625    231  -1187       C
ATOM   1317  CD  GLN A 172      -2.395   9.599  10.160  1.00 85.14           C
ANISOU 1317  CD  GLN A 172    11557   9083  11711    634    173  -1037       C
ATOM   1318  OE1 GLN A 172      -2.169  10.659  10.748  1.00 85.34           O
ANISOU 1318  OE1 GLN A 172    11465   9230  11730    645    138   -924       O
ATOM   1319  NE2 GLN A 172      -2.487   8.437  10.793  1.00 89.87           N
ANISOU 1319  NE2 GLN A 172    12342   9446  12360    628    162  -1035       N
ATOM   1320  N   ASN A 173      -5.925  12.640   8.231  1.00 49.93           N
ANISOU 1320  N   ASN A 173     6751   5297   6922    198    202  -1134       N
ATOM   1321  CA  ASN A 173      -6.379  13.857   7.583  1.00 55.99           C
ANISOU 1321  CA  ASN A 173     7383   6291   7598    177    201  -1127       C
ATOM   1322  C   ASN A 173      -5.204  14.492   6.842  1.00 61.45           C
ANISOU 1322  C   ASN A 173     7985   7075   8290    321    224  -1111       C
ATOM   1323  O   ASN A 173      -4.134  14.698   7.423  1.00 52.46           O
ANISOU 1323  O   ASN A 173     6826   5885   7221    422    212  -1025       O
ATOM   1324  CB  ASN A 173      -6.971  14.795   8.629  1.00 56.68           C
ANISOU 1324  CB  ASN A 173     7425   6442   7671    116    155  -1009       C
ATOM   1325  CG  ASN A 173      -7.815  14.035   9.651  1.00 69.76           C
ANISOU 1325  CG  ASN A 173     9181   7975   9349    -11    138  -1000       C
ATOM   1326  OD1 ASN A 173      -8.903  13.543   9.328  1.00 61.14           O
ANISOU 1326  OD1 ASN A 173     8117   6909   8205   -142    152  -1091       O
ATOM   1327  ND2 ASN A 173      -7.289  13.883  10.871  1.00 65.99           N
ANISOU 1327  ND2 ASN A 173     8761   7368   8946     22    110   -893       N
ATOM   1328  N   ILE A 174      -5.401  14.775   5.555  1.00 55.92           N
ANISOU 1328  N   ILE A 174     7226   6518   7502    324    257  -1197       N
ATOM   1329  CA  ILE A 174      -4.327  15.121   4.631  1.00 46.73           C
ANISOU 1329  CA  ILE A 174     5992   5439   6323    444    298  -1213       C
ATOM   1330  C   ILE A 174      -4.501  16.560   4.173  1.00 50.59           C
ANISOU 1330  C   ILE A 174     6372   6127   6723    440    294  -1145       C
ATOM   1331  O   ILE A 174      -5.544  16.926   3.616  1.00 55.18           O
ANISOU 1331  O   ILE A 174     6935   6826   7206    367    286  -1185       O
ATOM   1332  CB  ILE A 174      -4.307  14.166   3.433  1.00 45.44           C
ANISOU 1332  CB  ILE A 174     5872   5270   6123    461    350  -1375       C
ATOM   1333  CG1 ILE A 174      -3.962  12.752   3.911  1.00 49.53           C
ANISOU 1333  CG1 ILE A 174     6520   5560   6740    489    356  -1435       C
ATOM   1334  CG2 ILE A 174      -3.334  14.657   2.355  1.00 44.47           C
ANISOU 1334  CG2 ILE A 174     5659   5283   5955    571    401  -1396       C
ATOM   1335  CD1 ILE A 174      -4.243  11.677   2.875  1.00 54.29           C
ANISOU 1335  CD1 ILE A 174     7203   6121   7306    471    399  -1614       C
ATOM   1336  N   MET A 175      -3.477  17.372   4.394  1.00 42.93           N
ANISOU 1336  N   MET A 175     5333   5194   5783    518    297  -1044       N
ATOM   1337  CA  MET A 175      -3.412  18.707   3.832  1.00 47.09           C
ANISOU 1337  CA  MET A 175     5777   5888   6226    524    306   -980       C
ATOM   1338  C   MET A 175      -2.438  18.715   2.663  1.00 47.88           C
ANISOU 1338  C   MET A 175     5824   6077   6289    603    373  -1029       C
ATOM   1339  O   MET A 175      -1.371  18.093   2.723  1.00 48.60           O
ANISOU 1339  O   MET A 175     5907   6105   6455    683    403  -1053       O
ATOM   1340  CB  MET A 175      -2.967  19.725   4.882  1.00 47.29           C
ANISOU 1340  CB  MET A 175     5766   5902   6300    531    267   -832       C
ATOM   1341  CG  MET A 175      -2.877  21.150   4.364  1.00 60.21           C
ANISOU 1341  CG  MET A 175     7342   7682   7854    531    276   -756       C
ATOM   1342  SD  MET A 175      -2.062  22.309   5.492  1.00 68.75           S
ANISOU 1342  SD  MET A 175     8386   8738   8998    537    242   -600       S
ATOM   1343  CE  MET A 175      -2.999  22.042   6.966  1.00 65.48           C
ANISOU 1343  CE  MET A 175     8033   8207   8638    483    168   -566       C
ATOM   1344  N   VAL A 176      -2.815  19.400   1.590  1.00 47.06           N
ANISOU 1344  N   VAL A 176     5687   6130   6064    587    397  -1045       N
ATOM   1345  CA  VAL A 176      -1.895  19.686   0.493  1.00 47.47           C
ANISOU 1345  CA  VAL A 176     5680   6297   6059    649    467  -1065       C
ATOM   1346  C   VAL A 176      -1.845  21.199   0.323  1.00 47.87           C
ANISOU 1346  C   VAL A 176     5686   6468   6036    628    464   -940       C
ATOM   1347  O   VAL A 176      -2.864  21.880   0.464  1.00 50.05           O
ANISOU 1347  O   VAL A 176     5985   6780   6250    578    417   -895       O
ATOM   1348  CB  VAL A 176      -2.292  18.977  -0.820  1.00 47.01           C
ANISOU 1348  CB  VAL A 176     5643   6316   5905    654    511  -1215       C
ATOM   1349  CG1 VAL A 176      -2.234  17.445  -0.659  1.00 49.94           C
ANISOU 1349  CG1 VAL A 176     6079   6540   6354    676    519  -1345       C
ATOM   1350  CG2 VAL A 176      -3.668  19.411  -1.272  1.00 44.80           C
ANISOU 1350  CG2 VAL A 176     5382   6134   5505    580    473  -1233       C
ATOM   1351  N   GLN A 177      -0.651  21.725   0.064  1.00 41.61           N
ANISOU 1351  N   GLN A 177     4829   5731   5249    667    514   -885       N
ATOM   1352  CA  GLN A 177      -0.453  23.161  -0.063  1.00 44.64           C
ANISOU 1352  CA  GLN A 177     5187   6203   5570    637    519   -759       C
ATOM   1353  C   GLN A 177       0.447  23.431  -1.255  1.00 47.76           C
ANISOU 1353  C   GLN A 177     5527   6735   5884    663    609   -773       C
ATOM   1354  O   GLN A 177       1.362  22.648  -1.535  1.00 44.01           O
ANISOU 1354  O   GLN A 177     5000   6268   5453    718    663   -848       O
ATOM   1355  CB  GLN A 177       0.177  23.767   1.202  1.00 46.10           C
ANISOU 1355  CB  GLN A 177     5349   6306   5860    620    483   -642       C
ATOM   1356  CG  GLN A 177      -0.802  24.274   2.216  1.00 62.54           C
ANISOU 1356  CG  GLN A 177     7487   8312   7962    574    401   -573       C
ATOM   1357  CD  GLN A 177      -0.167  25.259   3.181  1.00 67.86           C
ANISOU 1357  CD  GLN A 177     8142   8946   8694    547    374   -448       C
ATOM   1358  OE1 GLN A 177       1.055  25.288   3.349  1.00 75.21           O
ANISOU 1358  OE1 GLN A 177     9008   9883   9684    561    406   -423       O
ATOM   1359  NE2 GLN A 177      -0.994  26.074   3.817  1.00 64.05           N
ANISOU 1359  NE2 GLN A 177     7711   8432   8192    509    315   -377       N
ATOM   1360  N   GLU A 178       0.174  24.516  -1.975  1.00 43.04           N
ANISOU 1360  N   GLU A 178     4945   6247   5163    629    626   -703       N
ATOM   1361  CA  GLU A 178       1.088  24.907  -3.040  1.00 42.88           C
ANISOU 1361  CA  GLU A 178     4875   6362   5057    636    718   -693       C
ATOM   1362  C   GLU A 178       2.465  25.146  -2.440  1.00 47.06           C
ANISOU 1362  C   GLU A 178     5322   6873   5686    631    753   -632       C
ATOM   1363  O   GLU A 178       2.586  25.572  -1.286  1.00 48.53           O
ANISOU 1363  O   GLU A 178     5509   6963   5967    601    698   -548       O
ATOM   1364  CB  GLU A 178       0.592  26.169  -3.748  1.00 46.08           C
ANISOU 1364  CB  GLU A 178     5332   6862   5314    595    723   -596       C
ATOM   1365  CG  GLU A 178       0.655  27.423  -2.858  1.00 52.32           C
ANISOU 1365  CG  GLU A 178     6154   7583   6141    540    680   -440       C
ATOM   1366  CD  GLU A 178       0.272  28.704  -3.598  1.00 56.75           C
ANISOU 1366  CD  GLU A 178     6788   8221   6552    510    691   -334       C
ATOM   1367  OE1 GLU A 178       0.646  28.860  -4.784  1.00 58.02           O
ANISOU 1367  OE1 GLU A 178     6942   8509   6593    510    767   -340       O
ATOM   1368  OE2 GLU A 178      -0.405  29.546  -2.984  1.00 56.05           O
ANISOU 1368  OE2 GLU A 178     6770   8063   6461    495    623   -245       O
ATOM   1369  N   TYR A 179       3.511  24.825  -3.205  1.00 54.08           N
ANISOU 1369  N   TYR A 179     6130   7868   6551    663    845   -684       N
ATOM   1370  CA  TYR A 179       4.875  25.109  -2.776  1.00 60.12           C
ANISOU 1370  CA  TYR A 179     6790   8663   7392    654    887   -633       C
ATOM   1371  C   TYR A 179       5.269  26.512  -3.220  1.00 55.48           C
ANISOU 1371  C   TYR A 179     6197   8174   6710    558    936   -506       C
ATOM   1372  O   TYR A 179       5.145  26.857  -4.398  1.00 55.83           O
ANISOU 1372  O   TYR A 179     6264   8337   6611    540   1001   -507       O
ATOM   1373  CB  TYR A 179       5.880  24.092  -3.330  1.00 58.15           C
ANISOU 1373  CB  TYR A 179     6439   8493   7163    741    967   -754       C
ATOM   1374  CG  TYR A 179       7.297  24.407  -2.878  1.00 65.90           C
ANISOU 1374  CG  TYR A 179     7287   9535   8216    734   1008   -706       C
ATOM   1375  CD1 TYR A 179       7.636  24.376  -1.527  1.00 70.96           C
ANISOU 1375  CD1 TYR A 179     7898  10068   8997    738    935   -657       C
ATOM   1376  CD2 TYR A 179       8.278  24.778  -3.788  1.00 66.85           C
ANISOU 1376  CD2 TYR A 179     7306   9837   8255    711   1118   -707       C
ATOM   1377  CE1 TYR A 179       8.921  24.682  -1.099  1.00 71.29           C
ANISOU 1377  CE1 TYR A 179     7804  10185   9099    726    964   -618       C
ATOM   1378  CE2 TYR A 179       9.578  25.088  -3.367  1.00 69.82           C
ANISOU 1378  CE2 TYR A 179     7540  10294   8694    690   1156   -668       C
ATOM   1379  CZ  TYR A 179       9.887  25.038  -2.025  1.00 67.86           C
ANISOU 1379  CZ  TYR A 179     7257   9940   8587    699   1075   -626       C
ATOM   1380  OH  TYR A 179      11.158  25.341  -1.598  1.00 72.45           O
ANISOU 1380  OH  TYR A 179     7685  10619   9224    676   1104   -596       O
ATOM   1381  N   ILE A 180       5.753  27.313  -2.278  1.00 54.93           N
ANISOU 1381  N   ILE A 180     6106   8052   6713    491    906   -398       N
ATOM   1382  CA  ILE A 180       6.172  28.679  -2.559  1.00 64.25           C
ANISOU 1382  CA  ILE A 180     7299   9296   7818    380    950   -271       C
ATOM   1383  C   ILE A 180       7.600  28.870  -2.064  1.00 68.50           C
ANISOU 1383  C   ILE A 180     7702   9887   8439    333    993   -244       C
ATOM   1384  O   ILE A 180       7.884  28.689  -0.873  1.00 75.03           O
ANISOU 1384  O   ILE A 180     8488  10626   9395    342    926   -235       O
ATOM   1385  CB  ILE A 180       5.238  29.709  -1.904  1.00 72.17           C
ANISOU 1385  CB  ILE A 180     8431  10178   8811    322    865   -158       C
ATOM   1386  CG1 ILE A 180       3.780  29.401  -2.244  1.00 68.55           C
ANISOU 1386  CG1 ILE A 180     8080   9681   8285    383    808   -200       C
ATOM   1387  CG2 ILE A 180       5.593  31.119  -2.374  1.00 76.15           C
ANISOU 1387  CG2 ILE A 180     8985  10731   9216    209    917    -28       C
ATOM   1388  CD1 ILE A 180       2.793  30.240  -1.485  1.00 60.54           C
ANISOU 1388  CD1 ILE A 180     7177   8552   7273    358    717   -111       C
ATOM   1389  N   LYS A 181       8.495  29.230  -2.971  1.00 71.02           N
ANISOU 1389  N   LYS A 181     7945  10365   8675    280   1103   -233       N
ATOM   1390  CA  LYS A 181       9.728  29.905  -2.585  1.00 80.48           C
ANISOU 1390  CA  LYS A 181     9034  11633   9914    177   1147   -167       C
ATOM   1391  C   LYS A 181      10.169  30.712  -3.790  1.00 87.19           C
ANISOU 1391  C   LYS A 181     9884  12633  10612     74   1266   -111       C
ATOM   1392  O   LYS A 181      10.411  30.148  -4.861  1.00 87.49           O
ANISOU 1392  O   LYS A 181     9868  12810  10565    127   1354   -190       O
ATOM   1393  CB  LYS A 181      10.830  28.936  -2.139  1.00 82.23           C
ANISOU 1393  CB  LYS A 181     9071  11926  10248    257   1163   -264       C
ATOM   1394  CG  LYS A 181      12.097  29.666  -1.682  1.00 88.51           C
ANISOU 1394  CG  LYS A 181     9731  12815  11084    139   1201   -202       C
ATOM   1395  CD  LYS A 181      13.362  29.146  -2.352  1.00 87.52           C
ANISOU 1395  CD  LYS A 181     9407  12907  10939    172   1313   -286       C
ATOM   1396  CE  LYS A 181      14.576  29.368  -1.466  1.00 88.43           C
ANISOU 1396  CE  LYS A 181     9348  13099  11152    117   1305   -270       C
ATOM   1397  NZ  LYS A 181      15.859  29.097  -2.178  1.00 86.31           N
ANISOU 1397  NZ  LYS A 181     8868  13080  10846    122   1427   -339       N
ATOM   1398  N   GLU A 182      10.226  32.025  -3.621  1.00 84.54           N
ANISOU 1398  N   GLU A 182     9626  12260  10236    -74   1270     25       N
ATOM   1399  CA  GLU A 182      10.598  32.956  -4.677  1.00101.12           C
ANISOU 1399  CA  GLU A 182    11761  14473  12185   -198   1379    109       C
ATOM   1400  C   GLU A 182      11.849  33.721  -4.247  1.00113.87           C
ANISOU 1400  C   GLU A 182    13271  16153  13840   -362   1434    176       C
ATOM   1401  O   GLU A 182      12.374  33.519  -3.147  1.00119.70           O
ANISOU 1401  O   GLU A 182    13907  16854  14719   -365   1377    152       O
ATOM   1402  CB  GLU A 182       9.432  33.901  -4.999  1.00101.77           C
ANISOU 1402  CB  GLU A 182    12069  14441  12158   -231   1337    220       C
ATOM   1403  CG  GLU A 182       8.101  33.180  -5.252  1.00100.02           C
ANISOU 1403  CG  GLU A 182    11939  14157  11906    -78   1263    150       C
ATOM   1404  CD  GLU A 182       6.938  33.798  -4.482  1.00 99.42           C
ANISOU 1404  CD  GLU A 182    12025  13894  11856    -64   1141    224       C
ATOM   1405  OE1 GLU A 182       7.168  34.311  -3.365  1.00 98.77           O
ANISOU 1405  OE1 GLU A 182    11949  13699  11880   -127   1086    280       O
ATOM   1406  OE2 GLU A 182       5.791  33.762  -4.984  1.00 99.08           O
ANISOU 1406  OE2 GLU A 182    12096  13827  11722     13   1099    220       O
ATOM   1407  N   ALA A 183      12.325  34.607  -5.128  1.00123.30           N
ANISOU 1407  N   ALA A 183    14494  17451  14903   -507   1545    261       N
ATOM   1408  CA  ALA A 183      13.518  35.411  -4.877  1.00122.36           C
ANISOU 1408  CA  ALA A 183    14279  17413  14799   -699   1614    327       C
ATOM   1409  C   ALA A 183      13.402  36.188  -3.570  1.00125.47           C
ANISOU 1409  C   ALA A 183    14746  17625  15302   -790   1511    404       C
ATOM   1410  O   ALA A 183      14.143  35.922  -2.617  1.00128.58           O
ANISOU 1410  O   ALA A 183    14988  18043  15825   -807   1474    359       O
ATOM   1411  CB  ALA A 183      13.768  36.372  -6.044  1.00118.83           C
ANISOU 1411  CB  ALA A 183    13917  17059  14172   -856   1742    431       C
ATOM   1412  N   GLY A 184      12.487  37.154  -3.517  1.00121.97           N
ANISOU 1412  N   GLY A 184    14535  17007  14802   -840   1461    518       N
ATOM   1413  CA  GLY A 184      12.172  37.813  -2.264  1.00118.05           C
ANISOU 1413  CA  GLY A 184    14133  16317  14405   -892   1350    575       C
ATOM   1414  C   GLY A 184      11.176  37.001  -1.464  1.00116.57           C
ANISOU 1414  C   GLY A 184    13974  16003  14316   -704   1217    504       C
ATOM   1415  O   GLY A 184       9.988  36.961  -1.804  1.00115.17           O
ANISOU 1415  O   GLY A 184    13947  15735  14077   -600   1171    517       O
ATOM   1416  N   GLY A 185      11.646  36.338  -0.406  1.00108.92           N
ANISOU 1416  N   GLY A 185    12858  15034  13491   -660   1156    429       N
ATOM   1417  CA  GLY A 185      10.791  35.454   0.366  1.00105.72           C
ANISOU 1417  CA  GLY A 185    12471  14520  13180   -490   1041    359       C
ATOM   1418  C   GLY A 185      11.229  35.216   1.798  1.00100.49           C
ANISOU 1418  C   GLY A 185    11714  13802  12666   -489    952    330       C
ATOM   1419  O   GLY A 185      11.357  34.065   2.232  1.00103.95           O
ANISOU 1419  O   GLY A 185    12038  14268  13192   -358    912    236       O
ATOM   1420  N   ALA A 186      11.454  36.293   2.546  1.00 95.72           N
ANISOU 1420  N   ALA A 186    11170  13113  12085   -632    918    411       N
ATOM   1421  CA  ALA A 186      11.801  36.161   3.952  1.00 85.40           C
ANISOU 1421  CA  ALA A 186     9790  11752  10905   -637    823    388       C
ATOM   1422  C   ALA A 186      10.616  35.616   4.745  1.00 84.37           C
ANISOU 1422  C   ALA A 186     9759  11466  10831   -489    707    362       C
ATOM   1423  O   ALA A 186       9.448  35.831   4.400  1.00 85.56           O
ANISOU 1423  O   ALA A 186    10074  11516  10920   -435    685    391       O
ATOM   1424  CB  ALA A 186      12.253  37.510   4.525  1.00 74.37           C
ANISOU 1424  CB  ALA A 186     8455  10293   9508   -839    815    474       C
ATOM   1425  N   ASP A 187      10.929  34.876   5.804  1.00 86.29           N
ANISOU 1425  N   ASP A 187     9895  11704  11186   -421    632    305       N
ATOM   1426  CA  ASP A 187       9.934  34.388   6.748  1.00 76.23           C
ANISOU 1426  CA  ASP A 187     8704  10288   9972   -308    522    286       C
ATOM   1427  C   ASP A 187      10.063  35.197   8.030  1.00 69.34           C
ANISOU 1427  C   ASP A 187     7872   9322   9152   -402    440    333       C
ATOM   1428  O   ASP A 187      11.113  35.167   8.681  1.00 73.69           O
ANISOU 1428  O   ASP A 187     8287   9947   9767   -457    424    318       O
ATOM   1429  CB  ASP A 187      10.120  32.896   7.020  1.00 77.61           C
ANISOU 1429  CB  ASP A 187     8757  10507  10224   -152    495    191       C
ATOM   1430  CG  ASP A 187       9.348  32.030   6.046  1.00 81.13           C
ANISOU 1430  CG  ASP A 187     9246  10959  10621    -30    533    135       C
ATOM   1431  OD1 ASP A 187       9.881  31.727   4.955  1.00 83.71           O
ANISOU 1431  OD1 ASP A 187     9493  11414  10897    -18    627     97       O
ATOM   1432  OD2 ASP A 187       8.199  31.660   6.370  1.00 84.50           O
ANISOU 1432  OD2 ASP A 187     9783  11269  11053     47    470    123       O
ATOM   1433  N   ILE A 188       9.007  35.933   8.383  1.00 57.74           N
ANISOU 1433  N   ILE A 188     6585   7702   7651   -415    388    385       N
ATOM   1434  CA  ILE A 188       9.047  36.787   9.561  1.00 55.57           C
ANISOU 1434  CA  ILE A 188     6372   7328   7413   -505    313    425       C
ATOM   1435  C   ILE A 188       8.031  36.292  10.586  1.00 56.04           C
ANISOU 1435  C   ILE A 188     6500   7275   7517   -388    210    401       C
ATOM   1436  O   ILE A 188       7.080  35.574  10.268  1.00 58.06           O
ANISOU 1436  O   ILE A 188     6800   7504   7756   -264    202    371       O
ATOM   1437  CB  ILE A 188       8.810  38.273   9.223  1.00 57.28           C
ANISOU 1437  CB  ILE A 188     6757   7457   7551   -638    341    509       C
ATOM   1438  CG1 ILE A 188       7.334  38.543   8.944  1.00 62.09           C
ANISOU 1438  CG1 ILE A 188     7555   7943   8094   -542    314    537       C
ATOM   1439  CG2 ILE A 188       9.664  38.699   8.032  1.00 60.26           C
ANISOU 1439  CG2 ILE A 188     7087   7946   7862   -754    459    542       C
ATOM   1440  CD1 ILE A 188       7.081  39.959   8.447  1.00 68.55           C
ANISOU 1440  CD1 ILE A 188     8557   8668   8822   -644    346    626       C
ATOM   1441  N   ARG A 189       8.266  36.674  11.838  1.00 53.95           N
ANISOU 1441  N   ARG A 189     6238   6955   7306   -440    133    409       N
ATOM   1442  CA  ARG A 189       7.390  36.353  12.957  1.00 50.21           C
ANISOU 1442  CA  ARG A 189     5832   6380   6867   -355     37    394       C
ATOM   1443  C   ARG A 189       6.993  37.667  13.615  1.00 50.57           C
ANISOU 1443  C   ARG A 189     6026   6306   6884   -446     -7    441       C
ATOM   1444  O   ARG A 189       7.857  38.430  14.060  1.00 52.17           O
ANISOU 1444  O   ARG A 189     6206   6514   7102   -579    -14    459       O
ATOM   1445  CB  ARG A 189       8.079  35.416  13.956  1.00 59.37           C
ANISOU 1445  CB  ARG A 189     6850   7593   8114   -308    -23    350       C
ATOM   1446  CG  ARG A 189       7.329  35.229  15.290  1.00 69.57           C
ANISOU 1446  CG  ARG A 189     8214   8786   9434   -253   -124    345       C
ATOM   1447  CD  ARG A 189       7.037  33.762  15.603  1.00 75.98           C
ANISOU 1447  CD  ARG A 189     8970   9607  10292   -110   -155    302       C
ATOM   1448  NE  ARG A 189       8.130  32.876  15.205  1.00 83.28           N
ANISOU 1448  NE  ARG A 189     9732  10648  11262    -67   -123    267       N
ATOM   1449  CZ  ARG A 189       8.041  31.550  15.171  1.00 89.23           C
ANISOU 1449  CZ  ARG A 189    10440  11410  12054     62   -129    225       C
ATOM   1450  NH1 ARG A 189       6.905  30.949  15.504  1.00 94.44           N
ANISOU 1450  NH1 ARG A 189    11202  11972  12709    138   -162    216       N
ATOM   1451  NH2 ARG A 189       9.085  30.822  14.808  1.00 87.09           N
ANISOU 1451  NH2 ARG A 189    10024  11245  11821    115   -100    189       N
ATOM   1452  N   CYS A 190       5.693  37.945  13.638  1.00 44.46           N
ANISOU 1452  N   CYS A 190     5403   5429   6063   -375    -33    454       N
ATOM   1453  CA  CYS A 190       5.141  39.146  14.256  1.00 46.64           C
ANISOU 1453  CA  CYS A 190     5840   5578   6305   -425    -77    490       C
ATOM   1454  C   CYS A 190       4.532  38.792  15.599  1.00 52.81           C
ANISOU 1454  C   CYS A 190     6636   6305   7123   -357   -169    457       C
ATOM   1455  O   CYS A 190       3.747  37.842  15.694  1.00 45.39           O
ANISOU 1455  O   CYS A 190     5676   5380   6191   -238   -189    425       O
ATOM   1456  CB  CYS A 190       4.087  39.798  13.357  1.00 45.89           C
ANISOU 1456  CB  CYS A 190     5903   5414   6118   -376    -46    528       C
ATOM   1457  SG  CYS A 190       4.792  40.328  11.787  1.00 55.67           S
ANISOU 1457  SG  CYS A 190     7151   6710   7291   -468     66    582       S
ATOM   1458  N   PHE A 191       4.887  39.562  16.621  1.00 46.68           N
ANISOU 1458  N   PHE A 191     5902   5471   6365   -442   -222    463       N
ATOM   1459  CA  PHE A 191       4.425  39.322  17.981  1.00 43.33           C
ANISOU 1459  CA  PHE A 191     5493   5005   5965   -394   -309    433       C
ATOM   1460  C   PHE A 191       3.302  40.311  18.279  1.00 48.36           C
ANISOU 1460  C   PHE A 191     6316   5519   6541   -366   -336    445       C
ATOM   1461  O   PHE A 191       3.531  41.524  18.351  1.00 51.68           O
ANISOU 1461  O   PHE A 191     6847   5856   6934   -459   -335    469       O
ATOM   1462  CB  PHE A 191       5.584  39.456  18.969  1.00 48.28           C
ANISOU 1462  CB  PHE A 191     6031   5668   6644   -498   -357    419       C
ATOM   1463  CG  PHE A 191       5.417  38.622  20.200  1.00 51.13           C
ANISOU 1463  CG  PHE A 191     6336   6049   7041   -425   -436    387       C
ATOM   1464  CD1 PHE A 191       6.154  37.457  20.381  1.00 50.05           C
ANISOU 1464  CD1 PHE A 191     6040   6017   6961   -383   -449    369       C
ATOM   1465  CD2 PHE A 191       4.491  38.992  21.174  1.00 62.67           C
ANISOU 1465  CD2 PHE A 191     7914   7425   8471   -389   -495    377       C
ATOM   1466  CE1 PHE A 191       5.984  36.687  21.527  1.00 62.83           C
ANISOU 1466  CE1 PHE A 191     7627   7642   8602   -313   -524    353       C
ATOM   1467  CE2 PHE A 191       4.312  38.222  22.322  1.00 67.77           C
ANISOU 1467  CE2 PHE A 191     8518   8093   9137   -329   -563    355       C
ATOM   1468  CZ  PHE A 191       5.055  37.070  22.496  1.00 66.91           C
ANISOU 1468  CZ  PHE A 191     8264   8077   9083   -294   -579    348       C
ATOM   1469  N   VAL A 192       2.082  39.801  18.429  1.00 38.00           N
ANISOU 1469  N   VAL A 192     5041   4195   5203   -237   -357    424       N
ATOM   1470  CA  VAL A 192       0.897  40.641  18.575  1.00 38.70           C
ANISOU 1470  CA  VAL A 192     5287   4191   5224   -175   -377    428       C
ATOM   1471  C   VAL A 192       0.468  40.630  20.031  1.00 43.43           C
ANISOU 1471  C   VAL A 192     5910   4759   5832   -149   -451    392       C
ATOM   1472  O   VAL A 192       0.318  39.561  20.626  1.00 44.73           O
ANISOU 1472  O   VAL A 192     5982   4986   6029   -104   -477    365       O
ATOM   1473  CB  VAL A 192      -0.255  40.145  17.681  1.00 46.75           C
ANISOU 1473  CB  VAL A 192     6321   5247   6193    -49   -346    422       C
ATOM   1474  CG1 VAL A 192      -1.493  40.958  17.926  1.00 44.30           C
ANISOU 1474  CG1 VAL A 192     6153   4867   5813     37   -376    417       C
ATOM   1475  CG2 VAL A 192       0.147  40.194  16.196  1.00 50.51           C
ANISOU 1475  CG2 VAL A 192     6785   5762   6646    -71   -272    457       C
ATOM   1476  N   VAL A 193       0.249  41.814  20.593  1.00 45.97           N
ANISOU 1476  N   VAL A 193     6369   4981   6118   -177   -482    391       N
ATOM   1477  CA  VAL A 193      -0.331  41.977  21.920  1.00 45.60           C
ANISOU 1477  CA  VAL A 193     6370   4901   6056   -140   -547    351       C
ATOM   1478  C   VAL A 193      -1.424  43.026  21.791  1.00 47.93           C
ANISOU 1478  C   VAL A 193     6835   5103   6275    -58   -550    347       C
ATOM   1479  O   VAL A 193      -1.145  44.174  21.419  1.00 46.13           O
ANISOU 1479  O   VAL A 193     6734   4770   6022   -110   -537    373       O
ATOM   1480  CB  VAL A 193       0.713  42.409  22.967  1.00 48.18           C
ANISOU 1480  CB  VAL A 193     6688   5203   6418   -264   -596    337       C
ATOM   1481  CG1 VAL A 193       0.036  42.649  24.324  1.00 48.33           C
ANISOU 1481  CG1 VAL A 193     6772   5189   6403   -218   -661    291       C
ATOM   1482  CG2 VAL A 193       1.839  41.390  23.079  1.00 41.35           C
ANISOU 1482  CG2 VAL A 193     5645   4444   5623   -325   -600    341       C
ATOM   1483  N   GLY A 194      -2.661  42.647  22.099  1.00 45.04           N
ANISOU 1483  N   GLY A 194     6472   4773   5867     70   -566    314       N
ATOM   1484  CA  GLY A 194      -3.743  43.603  21.905  1.00 45.63           C
ANISOU 1484  CA  GLY A 194     6692   4780   5864    177   -570    305       C
ATOM   1485  C   GLY A 194      -3.880  43.911  20.425  1.00 54.89           C
ANISOU 1485  C   GLY A 194     7912   5940   7005    212   -519    354       C
ATOM   1486  O   GLY A 194      -3.733  43.032  19.569  1.00 51.96           O
ANISOU 1486  O   GLY A 194     7431   5658   6652    211   -479    371       O
ATOM   1487  N   ASP A 195      -4.141  45.173  20.094  1.00 53.24           N
ANISOU 1487  N   ASP A 195     7877   5611   6739    245   -518    377       N
ATOM   1488  CA  ASP A 195      -4.261  45.533  18.686  1.00 60.24           C
ANISOU 1488  CA  ASP A 195     8828   6481   7581    281   -472    435       C
ATOM   1489  C   ASP A 195      -3.006  46.213  18.159  1.00 52.11           C
ANISOU 1489  C   ASP A 195     7866   5358   6574    124   -435    497       C
ATOM   1490  O   ASP A 195      -3.084  47.095  17.298  1.00 55.76           O
ANISOU 1490  O   ASP A 195     8476   5731   6980    139   -408    553       O
ATOM   1491  CB  ASP A 195      -5.496  46.399  18.443  1.00 69.80           C
ANISOU 1491  CB  ASP A 195    10190   7634   8697    450   -492    433       C
ATOM   1492  CG  ASP A 195      -5.689  47.448  19.504  1.00 85.68           C
ANISOU 1492  CG  ASP A 195    12353   9511  10691    470   -539    400       C
ATOM   1493  OD1 ASP A 195      -6.042  47.080  20.645  1.00 92.23           O
ANISOU 1493  OD1 ASP A 195    13118  10388  11535    494   -576    333       O
ATOM   1494  OD2 ASP A 195      -5.488  48.642  19.196  1.00 93.56           O
ANISOU 1494  OD2 ASP A 195    13543  10350  11653    459   -535    441       O
ATOM   1495  N   LYS A 196      -1.841  45.805  18.653  1.00 48.54           N
ANISOU 1495  N   LYS A 196     7308   4935   6200    -29   -433    489       N
ATOM   1496  CA  LYS A 196      -0.570  46.319  18.169  1.00 51.24           C
ANISOU 1496  CA  LYS A 196     7673   5227   6568   -201   -391    538       C
ATOM   1497  C   LYS A 196       0.361  45.154  17.892  1.00 54.31           C
ANISOU 1497  C   LYS A 196     7848   5762   7025   -281   -359    536       C
ATOM   1498  O   LYS A 196       0.387  44.172  18.641  1.00 49.91           O
ANISOU 1498  O   LYS A 196     7150   5295   6518   -256   -393    489       O
ATOM   1499  CB  LYS A 196       0.079  47.272  19.178  1.00 56.56           C
ANISOU 1499  CB  LYS A 196     8447   5779   7264   -329   -429    520       C
ATOM   1500  CG  LYS A 196      -0.801  48.472  19.525  1.00 64.30           C
ANISOU 1500  CG  LYS A 196     9660   6594   8178   -242   -462    512       C
ATOM   1501  CD  LYS A 196      -0.180  49.379  20.591  1.00 75.67           C
ANISOU 1501  CD  LYS A 196    11205   7907   9638   -374   -503    477       C
ATOM   1502  CE  LYS A 196      -1.222  50.354  21.153  1.00 86.08           C
ANISOU 1502  CE  LYS A 196    12735   9078  10892   -243   -547    442       C
ATOM   1503  NZ  LYS A 196      -2.406  49.652  21.754  1.00 92.80           N
ANISOU 1503  NZ  LYS A 196    13505  10033  11722    -50   -587    383       N
ATOM   1504  N   VAL A 197       1.101  45.248  16.794  1.00 51.77           N
ANISOU 1504  N   VAL A 197     7507   5465   6698   -367   -291    588       N
ATOM   1505  CA  VAL A 197       2.274  44.404  16.617  1.00 51.43           C
ANISOU 1505  CA  VAL A 197     7272   5547   6721   -472   -258    582       C
ATOM   1506  C   VAL A 197       3.378  45.050  17.441  1.00 55.14           C
ANISOU 1506  C   VAL A 197     7744   5973   7235   -647   -280    573       C
ATOM   1507  O   VAL A 197       3.856  46.131  17.098  1.00 54.39           O
ANISOU 1507  O   VAL A 197     7771   5784   7112   -772   -249    615       O
ATOM   1508  CB  VAL A 197       2.678  44.279  15.144  1.00 53.72           C
ANISOU 1508  CB  VAL A 197     7531   5900   6979   -503   -170    633       C
ATOM   1509  CG1 VAL A 197       4.076  43.678  15.028  1.00 51.55           C
ANISOU 1509  CG1 VAL A 197     7069   5747   6769   -633   -132    623       C
ATOM   1510  CG2 VAL A 197       1.671  43.434  14.393  1.00 50.34           C
ANISOU 1510  CG2 VAL A 197     7066   5549   6514   -337   -156    623       C
ATOM   1511  N   ILE A 198       3.774  44.401  18.542  1.00 56.52           N
ANISOU 1511  N   ILE A 198     7790   6214   7472   -662   -337    520       N
ATOM   1512  CA  ILE A 198       4.707  45.034  19.475  1.00 59.49           C
ANISOU 1512  CA  ILE A 198     8166   6556   7880   -819   -376    498       C
ATOM   1513  C   ILE A 198       6.152  44.637  19.221  1.00 56.55           C
ANISOU 1513  C   ILE A 198     7611   6315   7560   -962   -343    500       C
ATOM   1514  O   ILE A 198       7.058  45.243  19.810  1.00 63.31           O
ANISOU 1514  O   ILE A 198     8455   7164   8437  -1123   -365    483       O
ATOM   1515  CB  ILE A 198       4.306  44.730  20.935  1.00 54.85           C
ANISOU 1515  CB  ILE A 198     7563   5966   7312   -757   -468    439       C
ATOM   1516  CG1 ILE A 198       4.304  43.221  21.195  1.00 45.34           C
ANISOU 1516  CG1 ILE A 198     6168   4905   6153   -657   -487    416       C
ATOM   1517  CG2 ILE A 198       2.925  45.288  21.214  1.00 58.72           C
ANISOU 1517  CG2 ILE A 198     8235   6335   7742   -628   -495    430       C
ATOM   1518  CD1 ILE A 198       5.588  42.677  21.763  1.00 54.55           C
ANISOU 1518  CD1 ILE A 198     7158   6187   7381   -752   -516    394       C
ATOM   1519  N   ALA A 199       6.399  43.656  18.355  1.00 56.26           N
ANISOU 1519  N   ALA A 199     7428   6405   7541   -908   -290    511       N
ATOM   1520  CA  ALA A 199       7.758  43.248  18.029  1.00 49.12           C
ANISOU 1520  CA  ALA A 199     6336   5646   6682  -1022   -250    507       C
ATOM   1521  C   ALA A 199       7.698  42.317  16.834  1.00 53.17           C
ANISOU 1521  C   ALA A 199     6749   6263   7190   -928   -178    521       C
ATOM   1522  O   ALA A 199       6.697  41.628  16.627  1.00 50.82           O
ANISOU 1522  O   ALA A 199     6476   5954   6880   -766   -185    514       O
ATOM   1523  CB  ALA A 199       8.435  42.542  19.208  1.00 55.37           C
ANISOU 1523  CB  ALA A 199     6962   6538   7538  -1025   -327    453       C
ATOM   1524  N   ALA A 200       8.770  42.302  16.050  1.00 44.57           N
ANISOU 1524  N   ALA A 200     5545   5283   6107  -1038   -104    535       N
ATOM   1525  CA  ALA A 200       8.848  41.358  14.944  1.00 56.68           C
ANISOU 1525  CA  ALA A 200     6966   6933   7635   -951    -33    535       C
ATOM   1526  C   ALA A 200      10.308  41.022  14.681  1.00 59.12           C
ANISOU 1526  C   ALA A 200     7065   7416   7983  -1057     14    514       C
ATOM   1527  O   ALA A 200      11.208  41.777  15.051  1.00 66.81           O
ANISOU 1527  O   ALA A 200     8007   8411   8965  -1233     13    517       O
ATOM   1528  CB  ALA A 200       8.179  41.910  13.682  1.00 57.10           C
ANISOU 1528  CB  ALA A 200     7169   6922   7604   -938     43    592       C
ATOM   1529  N   MET A 201      10.535  39.871  14.046  1.00 56.11           N
ANISOU 1529  N   MET A 201     6534   7165   7620   -949     54    485       N
ATOM   1530  CA  MET A 201      11.894  39.406  13.797  1.00 60.10           C
ANISOU 1530  CA  MET A 201     6815   7859   8161  -1011     97    453       C
ATOM   1531  C   MET A 201      11.895  38.468  12.602  1.00 60.06           C
ANISOU 1531  C   MET A 201     6723   7958   8138   -898    180    436       C
ATOM   1532  O   MET A 201      10.872  37.865  12.277  1.00 53.58           O
ANISOU 1532  O   MET A 201     5982   7073   7301   -748    174    430       O
ATOM   1533  CB  MET A 201      12.460  38.688  15.026  1.00 62.67           C
ANISOU 1533  CB  MET A 201     6989   8258   8565   -958      3    399       C
ATOM   1534  CG  MET A 201      11.779  37.353  15.288  1.00 66.54           C
ANISOU 1534  CG  MET A 201     7455   8734   9091   -738    -44    365       C
ATOM   1535  SD  MET A 201      12.259  36.563  16.838  1.00 70.36           S
ANISOU 1535  SD  MET A 201     7816   9267   9652   -660   -169    323       S
ATOM   1536  CE  MET A 201      13.879  35.939  16.393  1.00 76.19           C
ANISOU 1536  CE  MET A 201     8275  10247  10428   -670   -124    278       C
ATOM   1537  N   LYS A 202      13.053  38.344  11.954  1.00 66.23           N
ANISOU 1537  N   LYS A 202     7334   8912   8918   -976    258    419       N
ATOM   1538  CA  LYS A 202      13.231  37.301  10.948  1.00 72.42           C
ANISOU 1538  CA  LYS A 202     8001   9822   9693   -854    331    380       C
ATOM   1539  C   LYS A 202      13.303  35.937  11.620  1.00 74.40           C
ANISOU 1539  C   LYS A 202     8127  10117  10023   -670    260    312       C
ATOM   1540  O   LYS A 202      13.897  35.790  12.692  1.00 80.82           O
ANISOU 1540  O   LYS A 202     8841  10969  10898   -677    183    289       O
ATOM   1541  CB  LYS A 202      14.497  37.542  10.120  1.00 82.11           C
ANISOU 1541  CB  LYS A 202     9065  11240  10891   -986    439    374       C
ATOM   1542  CG  LYS A 202      14.239  38.057   8.708  1.00 93.42           C
ANISOU 1542  CG  LYS A 202    10596  12678  12223  -1050    558    423       C
ATOM   1543  CD  LYS A 202      15.529  38.426   7.970  1.00 97.54           C
ANISOU 1543  CD  LYS A 202    10959  13395  12706  -1216    672    424       C
ATOM   1544  CE  LYS A 202      16.238  39.567   8.665  1.00 97.60           C
ANISOU 1544  CE  LYS A 202    10965  13393  12724  -1450    655    460       C
ATOM   1545  NZ  LYS A 202      17.094  40.384   7.766  1.00100.12           N
ANISOU 1545  NZ  LYS A 202    11244  13830  12969  -1673    783    501       N
ATOM   1546  N   ARG A 203      12.693  34.936  10.990  1.00 68.62           N
ANISOU 1546  N   ARG A 203     7410   9378   9285   -505    284    279       N
ATOM   1547  CA  ARG A 203      12.599  33.603  11.568  1.00 78.47           C
ANISOU 1547  CA  ARG A 203     8585  10627  10602   -323    220    220       C
ATOM   1548  C   ARG A 203      13.585  32.649  10.901  1.00 91.31           C
ANISOU 1548  C   ARG A 203    10016  12429  12249   -237    283    154       C
ATOM   1549  O   ARG A 203      13.757  32.678   9.679  1.00 93.81           O
ANISOU 1549  O   ARG A 203    10305  12830  12508   -255    388    143       O
ATOM   1550  CB  ARG A 203      11.180  33.054  11.438  1.00 80.41           C
ANISOU 1550  CB  ARG A 203     8992  10729  10832   -199    195    217       C
ATOM   1551  CG  ARG A 203      10.916  31.856  12.336  1.00 86.82           C
ANISOU 1551  CG  ARG A 203     9783  11489  11714    -45    111    176       C
ATOM   1552  CD  ARG A 203      10.168  30.759  11.599  1.00 92.49           C
ANISOU 1552  CD  ARG A 203    10547  12171  12422     95    143    127       C
ATOM   1553  NE  ARG A 203       9.056  31.296  10.819  1.00 92.35           N
ANISOU 1553  NE  ARG A 203    10678  12084  12327     60    183    152       N
ATOM   1554  CZ  ARG A 203       8.708  30.847   9.618  1.00 96.08           C
ANISOU 1554  CZ  ARG A 203    11165  12592  12748    113    256    115       C
ATOM   1555  NH1 ARG A 203       9.389  29.850   9.062  1.00 95.71           N
ANISOU 1555  NH1 ARG A 203    11001  12639  12725    202    303     47       N
ATOM   1556  NH2 ARG A 203       7.684  31.397   8.974  1.00 97.35           N
ANISOU 1556  NH2 ARG A 203    11458  12699  12829     86    279    142       N
ATOM   1557  N   GLN A 204      14.209  31.796  11.721  1.00 96.80           N
ANISOU 1557  N   GLN A 204    10581  13180  13018   -130    215    110       N
ATOM   1558  CA  GLN A 204      15.230  30.814  11.328  1.00102.79           C
ANISOU 1558  CA  GLN A 204    11140  14107  13808    -13    253     38       C
ATOM   1559  C   GLN A 204      16.034  31.202  10.080  1.00103.44           C
ANISOU 1559  C   GLN A 204    11100  14369  13833   -102    384     20       C
ATOM   1560  O   GLN A 204      17.171  30.768   9.898  1.00102.07           O
ANISOU 1560  O   GLN A 204    10718  14385  13679    -60    418    -35       O
ATOM   1561  CB  GLN A 204      14.574  29.442  11.109  1.00103.58           C
ANISOU 1561  CB  GLN A 204    11297  14123  13934    199    242    -14       C
ATOM   1562  CG  GLN A 204      13.797  29.290   9.825  1.00106.06           C
ANISOU 1562  CG  GLN A 204    11714  14399  14183    218    333    -31       C
ATOM   1563  CD  GLN A 204      13.925  27.893   9.242  1.00110.64           C
ANISOU 1563  CD  GLN A 204    12240  15013  14785    410    366   -120       C
ATOM   1564  OE1 GLN A 204      13.609  26.907   9.907  1.00114.32           O
ANISOU 1564  OE1 GLN A 204    12748  15378  15311    551    293   -147       O
ATOM   1565  NE2 GLN A 204      14.393  27.801   7.995  1.00108.36           N
ANISOU 1565  NE2 GLN A 204    11869  14860  14444    413    479   -167       N
ATOM   1566  N   SER A 221      18.764  39.107  12.595  1.00 79.45           N
ANISOU 1566  N   SER A 221     8145  11367  10675  -1551    356    293       N
ATOM   1567  CA  SER A 221      17.416  38.615  12.868  1.00 81.49           C
ANISOU 1567  CA  SER A 221     8596  11420  10948  -1353    289    312       C
ATOM   1568  C   SER A 221      16.422  39.774  13.054  1.00 83.73           C
ANISOU 1568  C   SER A 221     9163  11461  11188  -1458    269    382       C
ATOM   1569  O   SER A 221      15.233  39.558  13.234  1.00 73.15           O
ANISOU 1569  O   SER A 221     7994   9953   9846  -1319    221    401       O
ATOM   1570  CB  SER A 221      17.418  37.707  14.100  1.00 78.45           C
ANISOU 1570  CB  SER A 221     8123  11045  10639  -1186    158    262       C
ATOM   1571  OG  SER A 221      16.409  36.715  14.000  1.00 81.68           O
ANISOU 1571  OG  SER A 221     8623  11348  11064   -956    131    256       O
ATOM   1572  N   LEU A 222      16.925  41.003  13.000  1.00 89.97           N
ANISOU 1572  N   LEU A 222    10003  12238  11941  -1705    308    417       N
ATOM   1573  CA  LEU A 222      16.078  42.186  13.011  1.00 92.90           C
ANISOU 1573  CA  LEU A 222    10658  12378  12263  -1809    306    486       C
ATOM   1574  C   LEU A 222      15.388  42.358  11.660  1.00 93.11           C
ANISOU 1574  C   LEU A 222    10834  12335  12210  -1773    409    550       C
ATOM   1575  O   LEU A 222      15.921  41.970  10.615  1.00 99.22           O
ANISOU 1575  O   LEU A 222    11484  13264  12950  -1780    511    548       O
ATOM   1576  CB  LEU A 222      16.914  43.431  13.311  1.00 91.92           C
ANISOU 1576  CB  LEU A 222    10550  12254  12121  -2101    324    502       C
ATOM   1577  CG  LEU A 222      17.356  43.705  14.749  1.00 86.69           C
ANISOU 1577  CG  LEU A 222     9832  11593  11514  -2183    208    450       C
ATOM   1578  CD1 LEU A 222      18.338  44.863  14.750  1.00 84.79           C
ANISOU 1578  CD1 LEU A 222     9575  11394  11246  -2501    256    457       C
ATOM   1579  CD2 LEU A 222      16.148  43.991  15.643  1.00 80.87           C
ANISOU 1579  CD2 LEU A 222     9328  10615  10785  -2079    104    463       C
ATOM   1580  N   ILE A 223      14.197  42.962  11.683  1.00 91.22           N
ANISOU 1580  N   ILE A 223    10858  11871  11931  -1729    379    604       N
ATOM   1581  CA  ILE A 223      13.527  43.413  10.464  1.00 82.30           C
ANISOU 1581  CA  ILE A 223     9906  10657  10709  -1721    465    678       C
ATOM   1582  C   ILE A 223      12.773  44.711  10.731  1.00 81.08           C
ANISOU 1582  C   ILE A 223    10041  10259  10507  -1801    435    746       C
ATOM   1583  O   ILE A 223      12.667  45.181  11.867  1.00 80.04           O
ANISOU 1583  O   ILE A 223     9975  10018  10417  -1843    346    726       O
ATOM   1584  CB  ILE A 223      12.559  42.353   9.873  1.00 79.78           C
ANISOU 1584  CB  ILE A 223     9591  10346  10375  -1470    464    661       C
ATOM   1585  CG1 ILE A 223      11.685  41.693  10.941  1.00 79.96           C
ANISOU 1585  CG1 ILE A 223     9637  10281  10462  -1286    342    614       C
ATOM   1586  CG2 ILE A 223      13.279  41.343   9.019  1.00 81.42           C
ANISOU 1586  CG2 ILE A 223     9580  10773  10583  -1418    546    618       C
ATOM   1587  CD1 ILE A 223      10.603  42.577  11.428  1.00 79.97           C
ANISOU 1587  CD1 ILE A 223     9886  10065  10434  -1273    280    657       C
ATOM   1588  N   LYS A 224      12.254  45.292   9.650  1.00 80.05           N
ANISOU 1588  N   LYS A 224    10090  10045  10282  -1812    510    826       N
ATOM   1589  CA  LYS A 224      11.165  46.254   9.683  1.00 75.02           C
ANISOU 1589  CA  LYS A 224     9750   9168   9587  -1779    476    892       C
ATOM   1590  C   LYS A 224      10.050  45.673   8.829  1.00 69.29           C
ANISOU 1590  C   LYS A 224     9090   8435   8802  -1557    487    912       C
ATOM   1591  O   LYS A 224      10.307  45.169   7.730  1.00 67.16           O
ANISOU 1591  O   LYS A 224     8731   8303   8484  -1537    574    924       O
ATOM   1592  CB  LYS A 224      11.602  47.624   9.165  1.00 81.37           C
ANISOU 1592  CB  LYS A 224    10737   9864  10316  -2011    552    982       C
ATOM   1593  CG  LYS A 224      12.448  48.389  10.168  1.00 93.32           C
ANISOU 1593  CG  LYS A 224    12246  11329  11882  -2237    520    957       C
ATOM   1594  CD  LYS A 224      11.636  48.734  11.413  1.00 95.76           C
ANISOU 1594  CD  LYS A 224    12700  11451  12235  -2146    393    923       C
ATOM   1595  CE  LYS A 224      12.125  50.020  12.066  1.00 94.27           C
ANISOU 1595  CE  LYS A 224    12665  11108  12046  -2385    378    936       C
ATOM   1596  NZ  LYS A 224      12.156  49.893  13.551  1.00 93.57           N
ANISOU 1596  NZ  LYS A 224    12515  10999  12039  -2369    259    845       N
ATOM   1597  N   ILE A 225       8.838  45.682   9.348  1.00 66.53           N
ANISOU 1597  N   ILE A 225     8875   7949   8454  -1389    399    904       N
ATOM   1598  CA  ILE A 225       7.709  45.134   8.609  1.00 62.63           C
ANISOU 1598  CA  ILE A 225     8434   7459   7902  -1180    397    912       C
ATOM   1599  C   ILE A 225       7.009  46.259   7.862  1.00 62.43           C
ANISOU 1599  C   ILE A 225     8677   7282   7763  -1181    425   1011       C
ATOM   1600  O   ILE A 225       7.004  47.420   8.291  1.00 58.67           O
ANISOU 1600  O   ILE A 225     8388   6634   7270  -1282    405   1059       O
ATOM   1601  CB  ILE A 225       6.727  44.375   9.523  1.00 59.05           C
ANISOU 1601  CB  ILE A 225     7951   6978   7508   -986    291    841       C
ATOM   1602  CG1 ILE A 225       6.145  45.276  10.607  1.00 53.44           C
ANISOU 1602  CG1 ILE A 225     7414   6081   6811   -987    206    848       C
ATOM   1603  CG2 ILE A 225       7.391  43.166  10.146  1.00 61.74           C
ANISOU 1603  CG2 ILE A 225     8042   7465   7950   -964    267    754       C
ATOM   1604  CD1 ILE A 225       5.129  44.520  11.491  1.00 58.02           C
ANISOU 1604  CD1 ILE A 225     7960   6649   7434   -801    111    780       C
ATOM   1605  N   THR A 226       6.428  45.908   6.715  1.00 57.61           N
ANISOU 1605  N   THR A 226     8091   6732   7065  -1063    469   1040       N
ATOM   1606  CA  THR A 226       5.643  46.851   5.941  1.00 50.39           C
ANISOU 1606  CA  THR A 226     7427   5689   6028  -1018    485   1136       C
ATOM   1607  C   THR A 226       4.308  47.105   6.636  1.00 47.88           C
ANISOU 1607  C   THR A 226     7254   5230   5709   -836    376   1121       C
ATOM   1608  O   THR A 226       3.868  46.303   7.469  1.00 44.41           O
ANISOU 1608  O   THR A 226     6694   4831   5348   -725    304   1032       O
ATOM   1609  CB  THR A 226       5.404  46.301   4.538  1.00 51.59           C
ANISOU 1609  CB  THR A 226     7542   5978   6080   -934    556   1160       C
ATOM   1610  OG1 THR A 226       4.634  45.091   4.623  1.00 49.13           O
ANISOU 1610  OG1 THR A 226     7095   5770   5802   -738    503   1070       O
ATOM   1611  CG2 THR A 226       6.732  46.018   3.837  1.00 47.87           C
ANISOU 1611  CG2 THR A 226     6915   5670   5604  -1106    672   1167       C
ATOM   1612  N   PRO A 227       3.628  48.203   6.300  1.00 48.35           N
ANISOU 1612  N   PRO A 227     7571   5125   5673   -795    365   1206       N
ATOM   1613  CA  PRO A 227       2.259  48.382   6.823  1.00 53.75           C
ANISOU 1613  CA  PRO A 227     8375   5708   6340   -587    266   1184       C
ATOM   1614  C   PRO A 227       1.330  47.225   6.493  1.00 48.00           C
ANISOU 1614  C   PRO A 227     7508   5131   5598   -384    234   1118       C
ATOM   1615  O   PRO A 227       0.454  46.895   7.307  1.00 50.17           O
ANISOU 1615  O   PRO A 227     7757   5391   5912   -246    151   1051       O
ATOM   1616  CB  PRO A 227       1.800  49.688   6.158  1.00 51.07           C
ANISOU 1616  CB  PRO A 227     8331   5196   5876   -565    279   1300       C
ATOM   1617  CG  PRO A 227       3.095  50.447   5.905  1.00 55.21           C
ANISOU 1617  CG  PRO A 227     8923   5656   6397   -831    367   1373       C
ATOM   1618  CD  PRO A 227       4.086  49.376   5.527  1.00 57.20           C
ANISOU 1618  CD  PRO A 227     8898   6135   6699   -939    439   1326       C
ATOM   1619  N   GLU A 228       1.502  46.593   5.323  1.00 43.37           N
ANISOU 1619  N   GLU A 228     6830   4696   4952   -371    302   1130       N
ATOM   1620  CA  GLU A 228       0.643  45.472   4.930  1.00 42.51           C
ANISOU 1620  CA  GLU A 228     6593   4733   4824   -196    276   1059       C
ATOM   1621  C   GLU A 228       0.905  44.232   5.783  1.00 45.30           C
ANISOU 1621  C   GLU A 228     6718   5187   5309   -195    248    944       C
ATOM   1622  O   GLU A 228      -0.033  43.505   6.157  1.00 46.09           O
ANISOU 1622  O   GLU A 228     6754   5330   5429    -53    186    872       O
ATOM   1623  CB  GLU A 228       0.863  45.168   3.449  1.00 39.91           C
ANISOU 1623  CB  GLU A 228     6236   4536   4390   -200    361   1097       C
ATOM   1624  CG  GLU A 228       0.411  46.290   2.509  1.00 43.03           C
ANISOU 1624  CG  GLU A 228     6871   4846   4633   -164    380   1217       C
ATOM   1625  CD  GLU A 228       1.431  47.423   2.398  1.00 56.29           C
ANISOU 1625  CD  GLU A 228     8696   6399   6292   -365    448   1324       C
ATOM   1626  OE1 GLU A 228       2.605  47.226   2.791  1.00 55.42           O
ANISOU 1626  OE1 GLU A 228     8461   6324   6273   -548    499   1299       O
ATOM   1627  OE2 GLU A 228       1.056  48.513   1.922  1.00 52.56           O
ANISOU 1627  OE2 GLU A 228     8466   5795   5711   -343    449   1432       O
ATOM   1628  N   GLU A 229       2.176  43.950   6.074  1.00 45.81           N
ANISOU 1628  N   GLU A 229     6653   5296   5456   -351    294    927       N
ATOM   1629  CA  GLU A 229       2.492  42.848   6.987  1.00 45.79           C
ANISOU 1629  CA  GLU A 229     6453   5367   5577   -343    259    829       C
ATOM   1630  C   GLU A 229       1.905  43.104   8.370  1.00 43.97           C
ANISOU 1630  C   GLU A 229     6276   5021   5409   -298    162    798       C
ATOM   1631  O   GLU A 229       1.281  42.218   8.966  1.00 42.33           O
ANISOU 1631  O   GLU A 229     5979   4854   5249   -191    107    725       O
ATOM   1632  CB  GLU A 229       4.007  42.661   7.059  1.00 46.32           C
ANISOU 1632  CB  GLU A 229     6379   5508   5711   -513    321    823       C
ATOM   1633  CG  GLU A 229       4.592  41.897   5.864  1.00 48.23           C
ANISOU 1633  CG  GLU A 229     6489   5919   5916   -524    414    808       C
ATOM   1634  CD  GLU A 229       5.984  42.373   5.475  1.00 54.22           C
ANISOU 1634  CD  GLU A 229     7195   6734   6671   -717    505    851       C
ATOM   1635  OE1 GLU A 229       6.557  43.197   6.213  1.00 56.54           O
ANISOU 1635  OE1 GLU A 229     7537   6940   7006   -856    490    883       O
ATOM   1636  OE2 GLU A 229       6.507  41.918   4.434  1.00 52.89           O
ANISOU 1636  OE2 GLU A 229     6933   6707   6455   -737    593    847       O
ATOM   1637  N   ARG A 230       2.063  44.330   8.875  1.00 50.49           N
ANISOU 1637  N   ARG A 230     7260   5699   6227   -380    143    852       N
ATOM   1638  CA  ARG A 230       1.520  44.702  10.179  1.00 49.86           C
ANISOU 1638  CA  ARG A 230     7248   5504   6192   -338     54    821       C
ATOM   1639  C   ARG A 230       0.015  44.485  10.226  1.00 47.66           C
ANISOU 1639  C   ARG A 230     7024   5221   5865   -136     -4    792       C
ATOM   1640  O   ARG A 230      -0.510  43.823  11.133  1.00 49.93           O
ANISOU 1640  O   ARG A 230     7229   5535   6206    -60    -64    721       O
ATOM   1641  CB  ARG A 230       1.869  46.168  10.472  1.00 48.50           C
ANISOU 1641  CB  ARG A 230     7275   5158   5995   -454     54    886       C
ATOM   1642  CG  ARG A 230       1.299  46.717  11.779  1.00 61.76           C
ANISOU 1642  CG  ARG A 230     9055   6704   7705   -409    -34    850       C
ATOM   1643  CD  ARG A 230       1.735  48.173  12.029  1.00 61.85           C
ANISOU 1643  CD  ARG A 230     9279   6528   7695   -541    -30    907       C
ATOM   1644  NE  ARG A 230       3.185  48.347  11.916  1.00 59.48           N
ANISOU 1644  NE  ARG A 230     8909   6254   7435   -775     30    929       N
ATOM   1645  CZ  ARG A 230       4.041  48.196  12.926  1.00 63.06           C
ANISOU 1645  CZ  ARG A 230     9250   6732   7977   -905      3    875       C
ATOM   1646  NH1 ARG A 230       3.602  47.865  14.136  1.00 64.71           N
ANISOU 1646  NH1 ARG A 230     9415   6931   8240   -825    -81    802       N
ATOM   1647  NH2 ARG A 230       5.341  48.367  12.725  1.00 57.63           N
ANISOU 1647  NH2 ARG A 230     8485   6096   7318  -1117     62    893       N
ATOM   1648  N   MET A 231      -0.695  45.028   9.238  1.00 45.44           N
ANISOU 1648  N   MET A 231     6876   4917   5472    -47     12    847       N
ATOM   1649  CA  MET A 231      -2.138  44.843   9.153  1.00 47.56           C
ANISOU 1649  CA  MET A 231     7179   5211   5679    150    -42    817       C
ATOM   1650  C   MET A 231      -2.507  43.367   9.067  1.00 49.69           C
ANISOU 1650  C   MET A 231     7248   5647   5984    218    -47    731       C
ATOM   1651  O   MET A 231      -3.471  42.916   9.704  1.00 40.84           O
ANISOU 1651  O   MET A 231     6087   4556   4876    327   -106    668       O
ATOM   1652  CB  MET A 231      -2.679  45.598   7.938  1.00 52.23           C
ANISOU 1652  CB  MET A 231     7930   5779   6135    231    -19    897       C
ATOM   1653  CG  MET A 231      -4.119  45.280   7.622  1.00 65.87           C
ANISOU 1653  CG  MET A 231     9655   7587   7786    437    -70    860       C
ATOM   1654  SD  MET A 231      -5.206  46.255   8.674  1.00 83.67           S
ANISOU 1654  SD  MET A 231    12067   9703  10020    577   -162    849       S
ATOM   1655  CE  MET A 231      -4.833  47.898   8.061  1.00 87.74           C
ANISOU 1655  CE  MET A 231    12871  10021  10446    544   -136    981       C
ATOM   1656  N   THR A 232      -1.761  42.600   8.272  1.00 45.03           N
ANISOU 1656  N   THR A 232     6536   5167   5406    152     19    725       N
ATOM   1657  CA  THR A 232      -2.080  41.189   8.109  1.00 37.80           C
ANISOU 1657  CA  THR A 232     5451   4389   4521    213     19    640       C
ATOM   1658  C   THR A 232      -1.913  40.430   9.429  1.00 49.65           C
ANISOU 1658  C   THR A 232     6839   5884   6140    191    -26    572       C
ATOM   1659  O   THR A 232      -2.729  39.565   9.769  1.00 44.68           O
ANISOU 1659  O   THR A 232     6139   5311   5527    275    -62    504       O
ATOM   1660  CB  THR A 232      -1.204  40.575   7.018  1.00 40.63           C
ANISOU 1660  CB  THR A 232     5712   4856   4868    148    103    642       C
ATOM   1661  OG1 THR A 232      -1.535  41.161   5.751  1.00 40.14           O
ANISOU 1661  OG1 THR A 232     5755   4820   4677    187    141    703       O
ATOM   1662  CG2 THR A 232      -1.441  39.070   6.936  1.00 36.38           C
ANISOU 1662  CG2 THR A 232     5012   4438   4374    204    103    544       C
ATOM   1663  N   ALA A 233      -0.857  40.739  10.180  1.00 44.71           N
ANISOU 1663  N   ALA A 233     6197   5198   5592     71    -24    589       N
ATOM   1664  CA  ALA A 233      -0.624  40.055  11.447  1.00 43.01           C
ANISOU 1664  CA  ALA A 233     5882   4980   5479     52    -71    534       C
ATOM   1665  C   ALA A 233      -1.757  40.326  12.426  1.00 46.84           C
ANISOU 1665  C   ALA A 233     6440   5403   5952    139   -145    509       C
ATOM   1666  O   ALA A 233      -2.291  39.403  13.058  1.00 45.62           O
ANISOU 1666  O   ALA A 233     6205   5293   5835    194   -180    449       O
ATOM   1667  CB  ALA A 233       0.721  40.501  12.027  1.00 42.77           C
ANISOU 1667  CB  ALA A 233     5827   4908   5516    -94    -61    560       C
ATOM   1668  N   LEU A 234      -2.170  41.593  12.523  1.00 43.57           N
ANISOU 1668  N   LEU A 234     6189   4886   5480    157   -167    553       N
ATOM   1669  CA  LEU A 234      -3.231  41.983  13.443  1.00 45.63           C
ANISOU 1669  CA  LEU A 234     6525   5092   5721    251   -234    525       C
ATOM   1670  C   LEU A 234      -4.567  41.374  13.045  1.00 50.42           C
ANISOU 1670  C   LEU A 234     7095   5793   6268    395   -250    481       C
ATOM   1671  O   LEU A 234      -5.338  40.941  13.909  1.00 43.07           O
ANISOU 1671  O   LEU A 234     6123   4892   5352    454   -294    425       O
ATOM   1672  CB  LEU A 234      -3.332  43.512  13.492  1.00 48.78           C
ANISOU 1672  CB  LEU A 234     7122   5348   6063    251   -248    582       C
ATOM   1673  CG  LEU A 234      -2.172  44.268  14.149  1.00 45.10           C
ANISOU 1673  CG  LEU A 234     6714   4770   5652     96   -246    610       C
ATOM   1674  CD1 LEU A 234      -2.275  45.809  13.911  1.00 44.87           C
ANISOU 1674  CD1 LEU A 234     6915   4579   5554     89   -246    674       C
ATOM   1675  CD2 LEU A 234      -2.143  43.916  15.651  1.00 48.01           C
ANISOU 1675  CD2 LEU A 234     7018   5132   6093     78   -306    548       C
ATOM   1676  N   ARG A 235      -4.870  41.352  11.742  1.00 43.12           N
ANISOU 1676  N   ARG A 235     6185   4931   5269    446   -213    504       N
ATOM   1677  CA  ARG A 235      -6.111  40.734  11.285  1.00 43.39           C
ANISOU 1677  CA  ARG A 235     6168   5080   5240    572   -230    453       C
ATOM   1678  C   ARG A 235      -6.111  39.247  11.596  1.00 38.06           C
ANISOU 1678  C   ARG A 235     5326   4500   4634    543   -225    377       C
ATOM   1679  O   ARG A 235      -7.146  38.685  11.975  1.00 43.51           O
ANISOU 1679  O   ARG A 235     5965   5258   5310    611   -257    316       O
ATOM   1680  CB  ARG A 235      -6.300  40.936   9.776  1.00 43.54           C
ANISOU 1680  CB  ARG A 235     6226   5159   5159    621   -193    490       C
ATOM   1681  CG  ARG A 235      -6.967  42.218   9.346  1.00 44.16           C
ANISOU 1681  CG  ARG A 235     6474   5177   5127    726   -217    551       C
ATOM   1682  CD  ARG A 235      -7.047  42.237   7.815  1.00 44.61           C
ANISOU 1682  CD  ARG A 235     6554   5314   5080    766   -177    590       C
ATOM   1683  NE  ARG A 235      -7.585  43.494   7.308  1.00 55.88           N
ANISOU 1683  NE  ARG A 235     8166   6674   6394    872   -200    666       N
ATOM   1684  CZ  ARG A 235      -7.304  44.033   6.117  1.00 61.70           C
ANISOU 1684  CZ  ARG A 235     9003   7405   7035    875   -160    748       C
ATOM   1685  NH1 ARG A 235      -6.456  43.445   5.269  1.00 45.56           N
ANISOU 1685  NH1 ARG A 235     6884   5432   4995    770    -89    761       N
ATOM   1686  NH2 ARG A 235      -7.879  45.178   5.776  1.00 69.60           N
ANISOU 1686  NH2 ARG A 235    10188   8326   7930    991   -192    820       N
ATOM   1687  N   ALA A 236      -4.973  38.582  11.389  1.00 37.49           N
ANISOU 1687  N   ALA A 236     5172   4439   4633    444   -181    379       N
ATOM   1688  CA  ALA A 236      -4.903  37.155  11.680  1.00 40.11           C
ANISOU 1688  CA  ALA A 236     5369   4836   5033    424   -176    312       C
ATOM   1689  C   ALA A 236      -5.200  36.897  13.156  1.00 41.27           C
ANISOU 1689  C   ALA A 236     5497   4943   5239    419   -229    282       C
ATOM   1690  O   ALA A 236      -6.025  36.037  13.491  1.00 41.72           O
ANISOU 1690  O   ALA A 236     5498   5055   5297    454   -247    224       O
ATOM   1691  CB  ALA A 236      -3.531  36.603  11.293  1.00 36.55           C
ANISOU 1691  CB  ALA A 236     4841   4397   4649    338   -124    321       C
ATOM   1692  N   ALA A 237      -4.558  37.662  14.052  1.00 43.14           N
ANISOU 1692  N   ALA A 237     5787   5087   5515    365   -253    320       N
ATOM   1693  CA  ALA A 237      -4.802  37.485  15.490  1.00 35.31           C
ANISOU 1693  CA  ALA A 237     4787   4063   4568    359   -305    295       C
ATOM   1694  C   ALA A 237      -6.243  37.816  15.848  1.00 45.94           C
ANISOU 1694  C   ALA A 237     6182   5432   5843    455   -340    263       C
ATOM   1695  O   ALA A 237      -6.869  37.092  16.629  1.00 46.15           O
ANISOU 1695  O   ALA A 237     6155   5499   5882    469   -363    218       O
ATOM   1696  CB  ALA A 237      -3.835  38.336  16.321  1.00 37.70           C
ANISOU 1696  CB  ALA A 237     5141   4269   4913    280   -327    334       C
ATOM   1697  N   LYS A 238      -6.803  38.889  15.269  1.00 42.18           N
ANISOU 1697  N   LYS A 238     5805   4937   5284    527   -344    288       N
ATOM   1698  CA  LYS A 238      -8.183  39.249  15.596  1.00 46.16           C
ANISOU 1698  CA  LYS A 238     6344   5481   5714    640   -380    252       C
ATOM   1699  C   LYS A 238      -9.169  38.202  15.095  1.00 49.49           C
ANISOU 1699  C   LYS A 238     6660   6043   6100    689   -371    191       C
ATOM   1700  O   LYS A 238     -10.114  37.845  15.807  1.00 43.95           O
ANISOU 1700  O   LYS A 238     5914   5406   5380    725   -395    138       O
ATOM   1701  CB  LYS A 238      -8.540  40.627  15.037  1.00 58.86           C
ANISOU 1701  CB  LYS A 238     8095   7032   7238    727   -391    295       C
ATOM   1702  CG  LYS A 238      -9.890  41.124  15.538  1.00 62.43           C
ANISOU 1702  CG  LYS A 238     8584   7522   7615    863   -435    253       C
ATOM   1703  CD  LYS A 238      -9.855  42.607  15.882  1.00 75.07           C
ANISOU 1703  CD  LYS A 238    10358   8985   9179    919   -463    292       C
ATOM   1704  CE  LYS A 238     -10.765  43.392  14.940  1.00 82.01           C
ANISOU 1704  CE  LYS A 238    11327   9889   9946   1078   -477    311       C
ATOM   1705  NZ  LYS A 238     -10.740  44.864  15.204  1.00 86.81           N
ANISOU 1705  NZ  LYS A 238    12134  10336  10513   1145   -503    352       N
ATOM   1706  N   VAL A 239      -8.956  37.681  13.884  1.00 45.82           N
ANISOU 1706  N   VAL A 239     6152   5637   5622    679   -333    193       N
ATOM   1707  CA  VAL A 239      -9.837  36.647  13.345  1.00 45.77           C
ANISOU 1707  CA  VAL A 239     6047   5764   5581    706   -323    125       C
ATOM   1708  C   VAL A 239      -9.816  35.403  14.220  1.00 44.86           C
ANISOU 1708  C   VAL A 239     5841   5664   5542    630   -321     75       C
ATOM   1709  O   VAL A 239     -10.842  34.736  14.408  1.00 44.37           O
ANISOU 1709  O   VAL A 239     5715   5695   5449    645   -329     11       O
ATOM   1710  CB  VAL A 239      -9.426  36.315  11.898  1.00 51.65           C
ANISOU 1710  CB  VAL A 239     6771   6556   6298    698   -279    133       C
ATOM   1711  CG1 VAL A 239     -10.069  35.030  11.452  1.00 54.46           C
ANISOU 1711  CG1 VAL A 239     7019   7030   6643    688   -265     51       C
ATOM   1712  CG2 VAL A 239      -9.807  37.457  10.990  1.00 52.48           C
ANISOU 1712  CG2 VAL A 239     6969   6674   6297    793   -287    179       C
ATOM   1713  N   MET A 240      -8.636  35.024  14.703  1.00 37.20           N
ANISOU 1713  N   MET A 240     4862   4608   4666    546   -309    103       N
ATOM   1714  CA  MET A 240      -8.538  33.903  15.630  1.00 42.05           C
ANISOU 1714  CA  MET A 240     5414   5213   5349    484   -313     72       C
ATOM   1715  C   MET A 240      -9.104  34.244  16.999  1.00 40.38           C
ANISOU 1715  C   MET A 240     5227   4985   5130    491   -354     68       C
ATOM   1716  O   MET A 240      -9.328  33.329  17.805  1.00 42.85           O
ANISOU 1716  O   MET A 240     5499   5308   5475    446   -359     41       O
ATOM   1717  CB  MET A 240      -7.079  33.478  15.770  1.00 40.45           C
ANISOU 1717  CB  MET A 240     5194   4935   5242    415   -297    107       C
ATOM   1718  CG  MET A 240      -6.488  32.925  14.482  1.00 56.56           C
ANISOU 1718  CG  MET A 240     7193   7005   7292    406   -248     97       C
ATOM   1719  SD  MET A 240      -7.182  31.323  14.046  1.00 59.30           S
ANISOU 1719  SD  MET A 240     7471   7419   7642    398   -224     13       S
ATOM   1720  CE  MET A 240      -8.199  31.770  12.652  1.00 67.38           C
ANISOU 1720  CE  MET A 240     8498   8556   8548    461   -208    -21       C
ATOM   1721  N   GLY A 241      -9.354  35.526  17.274  1.00 41.45           N
ANISOU 1721  N   GLY A 241     5439   5092   5218    547   -381     92       N
ATOM   1722  CA  GLY A 241      -9.838  35.924  18.584  1.00 39.66           C
ANISOU 1722  CA  GLY A 241     5241   4851   4978    561   -417     81       C
ATOM   1723  C   GLY A 241      -8.788  35.891  19.675  1.00 38.99           C
ANISOU 1723  C   GLY A 241     5175   4671   4967    485   -437    114       C
ATOM   1724  O   GLY A 241      -9.137  35.767  20.848  1.00 44.53           O
ANISOU 1724  O   GLY A 241     5877   5378   5664    474   -462     97       O
ATOM   1725  N   LEU A 242      -7.511  35.994  19.324  1.00 38.41           N
ANISOU 1725  N   LEU A 242     5112   4528   4955    431   -427    159       N
ATOM   1726  CA  LEU A 242      -6.424  35.979  20.289  1.00 40.20           C
ANISOU 1726  CA  LEU A 242     5340   4684   5248    359   -452    188       C
ATOM   1727  C   LEU A 242      -6.004  37.402  20.655  1.00 50.15           C
ANISOU 1727  C   LEU A 242     6698   5864   6493    352   -479    216       C
ATOM   1728  O   LEU A 242      -5.873  38.261  19.781  1.00 51.99           O
ANISOU 1728  O   LEU A 242     6993   6064   6699    370   -461    240       O
ATOM   1729  CB  LEU A 242      -5.228  35.226  19.707  1.00 37.62           C
ANISOU 1729  CB  LEU A 242     4948   4348   4996    302   -425    210       C
ATOM   1730  CG  LEU A 242      -5.442  33.731  19.504  1.00 40.41           C
ANISOU 1730  CG  LEU A 242     5223   4749   5380    300   -403    180       C
ATOM   1731  CD1 LEU A 242      -4.375  33.126  18.595  1.00 39.68           C
ANISOU 1731  CD1 LEU A 242     5073   4657   5345    277   -366    190       C
ATOM   1732  CD2 LEU A 242      -5.435  33.075  20.881  1.00 33.58           C
ANISOU 1732  CD2 LEU A 242     4348   3866   4545    273   -439    180       C
ATOM   1733  N   SER A 243      -5.781  37.649  21.955  1.00 48.39           N
ANISOU 1733  N   SER A 243     6501   5604   6283    321   -521    212       N
ATOM   1734  CA  SER A 243      -5.177  38.922  22.350  1.00 44.68           C
ANISOU 1734  CA  SER A 243     6125   5043   5808    288   -548    231       C
ATOM   1735  C   SER A 243      -3.663  38.900  22.230  1.00 39.94           C
ANISOU 1735  C   SER A 243     5489   4407   5281    184   -546    268       C
ATOM   1736  O   SER A 243      -3.047  39.958  22.065  1.00 43.99           O
ANISOU 1736  O   SER A 243     6075   4847   5791    133   -548    290       O
ATOM   1737  CB  SER A 243      -5.557  39.309  23.789  1.00 40.06           C
ANISOU 1737  CB  SER A 243     5588   4440   5194    296   -597    201       C
ATOM   1738  OG  SER A 243      -6.953  39.536  23.887  1.00 42.68           O
ANISOU 1738  OG  SER A 243     5952   4815   5449    399   -595    161       O
ATOM   1739  N   VAL A 244      -3.048  37.724  22.319  1.00 36.42           N
ANISOU 1739  N   VAL A 244     4932   4011   4894    151   -542    272       N
ATOM   1740  CA  VAL A 244      -1.600  37.586  22.223  1.00 41.86           C
ANISOU 1740  CA  VAL A 244     5557   4697   5650     67   -541    299       C
ATOM   1741  C   VAL A 244      -1.306  36.464  21.248  1.00 43.26           C
ANISOU 1741  C   VAL A 244     5636   4934   5866     85   -494    302       C
ATOM   1742  O   VAL A 244      -1.811  35.349  21.416  1.00 40.51           O
ANISOU 1742  O   VAL A 244     5243   4621   5528    130   -494    283       O
ATOM   1743  CB  VAL A 244      -0.948  37.289  23.587  1.00 48.81           C
ANISOU 1743  CB  VAL A 244     6400   5581   6564     22   -602    295       C
ATOM   1744  CG1 VAL A 244       0.544  37.102  23.421  1.00 51.99           C
ANISOU 1744  CG1 VAL A 244     6712   6011   7033    -53   -603    316       C
ATOM   1745  CG2 VAL A 244      -1.239  38.417  24.588  1.00 42.05           C
ANISOU 1745  CG2 VAL A 244     5648   4668   5662      1   -649    279       C
ATOM   1746  N   ALA A 245      -0.495  36.747  20.233  1.00 41.56           N
ANISOU 1746  N   ALA A 245     5394   4727   5669     44   -451    324       N
ATOM   1747  CA  ALA A 245      -0.204  35.720  19.237  1.00 38.25           C
ANISOU 1747  CA  ALA A 245     4884   4368   5279     69   -401    317       C
ATOM   1748  C   ALA A 245       1.130  36.006  18.573  1.00 40.26           C
ANISOU 1748  C   ALA A 245     5079   4649   5569     -3   -366    340       C
ATOM   1749  O   ALA A 245       1.530  37.154  18.395  1.00 46.30           O
ANISOU 1749  O   ALA A 245     5900   5380   6312    -73   -357    367       O
ATOM   1750  CB  ALA A 245      -1.322  35.653  18.179  1.00 38.66           C
ANISOU 1750  CB  ALA A 245     4978   4440   5272    136   -359    302       C
ATOM   1751  N   GLY A 246       1.832  34.918  18.203  1.00 40.96           N
ANISOU 1751  N   GLY A 246     5053   4801   5710     14   -342    325       N
ATOM   1752  CA  GLY A 246       2.886  35.005  17.217  1.00 42.33           C
ANISOU 1752  CA  GLY A 246     5151   5032   5899    -31   -284    335       C
ATOM   1753  C   GLY A 246       2.296  34.627  15.867  1.00 45.68           C
ANISOU 1753  C   GLY A 246     5586   5488   6282     24   -217    320       C
ATOM   1754  O   GLY A 246       1.655  33.586  15.738  1.00 47.85           O
ANISOU 1754  O   GLY A 246     5844   5774   6562    100   -215    283       O
ATOM   1755  N   VAL A 247       2.479  35.498  14.890  1.00 42.08           N
ANISOU 1755  N   VAL A 247     5168   5042   5776    -23   -164    349       N
ATOM   1756  CA  VAL A 247       1.936  35.290  13.548  1.00 44.63           C
ANISOU 1756  CA  VAL A 247     5510   5406   6041     25   -103    340       C
ATOM   1757  C   VAL A 247       3.110  35.160  12.582  1.00 47.48           C
ANISOU 1757  C   VAL A 247     5779   5852   6411    -23    -30    344       C
ATOM   1758  O   VAL A 247       3.920  36.088  12.456  1.00 47.43           O
ANISOU 1758  O   VAL A 247     5777   5848   6396   -123     -5    387       O
ATOM   1759  CB  VAL A 247       1.005  36.441  13.134  1.00 39.97           C
ANISOU 1759  CB  VAL A 247     5063   4763   5362     31   -101    377       C
ATOM   1760  CG1 VAL A 247       0.483  36.208  11.716  1.00 42.89           C
ANISOU 1760  CG1 VAL A 247     5444   5193   5657     85    -43    369       C
ATOM   1761  CG2 VAL A 247      -0.158  36.603  14.144  1.00 40.93           C
ANISOU 1761  CG2 VAL A 247     5263   4821   5470     88   -171    364       C
ATOM   1762  N   ASP A 248       3.203  34.016  11.903  1.00 43.83           N
ANISOU 1762  N   ASP A 248     5233   5458   5962     41      9    295       N
ATOM   1763  CA  ASP A 248       4.273  33.765  10.937  1.00 52.17           C
ANISOU 1763  CA  ASP A 248     6188   6615   7020     15     86    284       C
ATOM   1764  C   ASP A 248       3.803  34.157   9.535  1.00 52.13           C
ANISOU 1764  C   ASP A 248     6244   6648   6915     19    154    297       C
ATOM   1765  O   ASP A 248       2.796  33.639   9.043  1.00 48.68           O
ANISOU 1765  O   ASP A 248     5848   6212   6435     99    154    262       O
ATOM   1766  CB  ASP A 248       4.688  32.292  10.963  1.00 48.77           C
ANISOU 1766  CB  ASP A 248     5641   6234   6655     98     90    215       C
ATOM   1767  CG  ASP A 248       5.510  31.938  12.194  1.00 57.59           C
ANISOU 1767  CG  ASP A 248     6677   7343   7863     95     32    213       C
ATOM   1768  OD1 ASP A 248       5.832  32.850  12.971  1.00 56.50           O
ANISOU 1768  OD1 ASP A 248     6556   7176   7734     13     -8    258       O
ATOM   1769  OD2 ASP A 248       5.830  30.750  12.384  1.00 65.43           O
ANISOU 1769  OD2 ASP A 248     7594   8354   8911    177     22    164       O
ATOM   1770  N   ILE A 249       4.545  35.041   8.885  1.00 51.89           N
ANISOU 1770  N   ILE A 249     6216   6658   6841    -73    214    347       N
ATOM   1771  CA  ILE A 249       4.157  35.599   7.596  1.00 52.01           C
ANISOU 1771  CA  ILE A 249     6310   6704   6746    -81    278    380       C
ATOM   1772  C   ILE A 249       5.255  35.298   6.590  1.00 54.92           C
ANISOU 1772  C   ILE A 249     6566   7203   7097   -122    374    366       C
ATOM   1773  O   ILE A 249       6.442  35.486   6.881  1.00 52.60           O
ANISOU 1773  O   ILE A 249     6177   6958   6852   -211    399    377       O
ATOM   1774  CB  ILE A 249       3.892  37.112   7.697  1.00 45.97           C
ANISOU 1774  CB  ILE A 249     5698   5847   5922   -159    266    470       C
ATOM   1775  CG1 ILE A 249       2.481  37.346   8.255  1.00 49.01           C
ANISOU 1775  CG1 ILE A 249     6205   6133   6282    -71    187    471       C
ATOM   1776  CG2 ILE A 249       4.081  37.809   6.347  1.00 48.15           C
ANISOU 1776  CG2 ILE A 249     6036   6170   6087   -209    351    527       C
ATOM   1777  CD1 ILE A 249       2.196  38.782   8.598  1.00 50.94           C
ANISOU 1777  CD1 ILE A 249     6610   6262   6483   -123    159    547       C
ATOM   1778  N   LEU A 250       4.861  34.805   5.424  1.00 56.04           N
ANISOU 1778  N   LEU A 250     6710   7418   7166    -59    427    334       N
ATOM   1779  CA  LEU A 250       5.769  34.622   4.300  1.00 50.10           C
ANISOU 1779  CA  LEU A 250     5868   6800   6366    -93    531    321       C
ATOM   1780  C   LEU A 250       5.637  35.823   3.366  1.00 54.01           C
ANISOU 1780  C   LEU A 250     6485   7302   6735   -172    587    412       C
ATOM   1781  O   LEU A 250       4.529  36.145   2.917  1.00 50.31           O
ANISOU 1781  O   LEU A 250     6146   6788   6180   -115    565    437       O
ATOM   1782  CB  LEU A 250       5.439  33.330   3.559  1.00 51.50           C
ANISOU 1782  CB  LEU A 250     5985   7054   6529     25    557    222       C
ATOM   1783  CG  LEU A 250       6.086  33.276   2.180  1.00 60.36           C
ANISOU 1783  CG  LEU A 250     7052   8322   7562      2    670    210       C
ATOM   1784  CD1 LEU A 250       7.595  33.145   2.333  1.00 62.75           C
ANISOU 1784  CD1 LEU A 250     7195   8722   7927    -62    727    197       C
ATOM   1785  CD2 LEU A 250       5.519  32.148   1.375  1.00 56.09           C
ANISOU 1785  CD2 LEU A 250     6492   7839   6982    118    689    111       C
ATOM   1786  N   ARG A 251       6.756  36.487   3.088  1.00 53.60           N
ANISOU 1786  N   ARG A 251     6390   7308   6667   -305    659    462       N
ATOM   1787  CA  ARG A 251       6.796  37.607   2.147  1.00 61.37           C
ANISOU 1787  CA  ARG A 251     7494   8298   7526   -399    728    558       C
ATOM   1788  C   ARG A 251       6.826  37.068   0.721  1.00 66.36           C
ANISOU 1788  C   ARG A 251     8086   9074   8053   -351    819    527       C
ATOM   1789  O   ARG A 251       7.897  36.770   0.189  1.00 69.12           O
ANISOU 1789  O   ARG A 251     8302   9564   8396   -410    910    501       O
ATOM   1790  CB  ARG A 251       8.019  38.478   2.400  1.00 62.01           C
ANISOU 1790  CB  ARG A 251     7539   8393   7626   -585    780    620       C
ATOM   1791  CG  ARG A 251       8.030  39.213   3.719  1.00 69.54           C
ANISOU 1791  CG  ARG A 251     8557   9204   8662   -657    696    657       C
ATOM   1792  CD  ARG A 251       9.436  39.733   4.016  1.00 68.90           C
ANISOU 1792  CD  ARG A 251     8374   9185   8621   -845    748    679       C
ATOM   1793  NE  ARG A 251       9.485  40.656   5.148  1.00 71.21           N
ANISOU 1793  NE  ARG A 251     8755   9334   8966   -947    678    721       N
ATOM   1794  CZ  ARG A 251       9.542  41.976   5.021  1.00 72.51           C
ANISOU 1794  CZ  ARG A 251     9088   9394   9070  -1094    703    816       C
ATOM   1795  NH1 ARG A 251       9.547  42.517   3.806  1.00 78.53           N
ANISOU 1795  NH1 ARG A 251     9946  10180   9710  -1152    796    889       N
ATOM   1796  NH2 ARG A 251       9.586  42.751   6.098  1.00 67.36           N
ANISOU 1796  NH2 ARG A 251     8517   8607   8469  -1181    635    837       N
ATOM   1797  N   SER A 252       5.659  36.963   0.077  1.00 63.03           N
ANISOU 1797  N   SER A 252     7774   8635   7539   -245    795    524       N
ATOM   1798  CA  SER A 252       5.567  36.431  -1.278  1.00 62.97           C
ANISOU 1798  CA  SER A 252     7741   8767   7419   -191    871    485       C
ATOM   1799  C   SER A 252       5.484  37.558  -2.310  1.00 65.15           C
ANISOU 1799  C   SER A 252     8162   9059   7534   -262    934    601       C
ATOM   1800  O   SER A 252       5.517  38.744  -1.979  1.00 67.63           O
ANISOU 1800  O   SER A 252     8605   9262   7829   -355    921    712       O
ATOM   1801  CB  SER A 252       4.364  35.492  -1.399  1.00 59.44           C
ANISOU 1801  CB  SER A 252     7307   8317   6963    -34    805    395       C
ATOM   1802  OG  SER A 252       3.170  36.199  -1.712  1.00 59.34           O
ANISOU 1802  OG  SER A 252     7460   8242   6844     16    755    457       O
ATOM   1803  N   ASN A 253       5.398  37.174  -3.588  1.00 64.46           N
ANISOU 1803  N   ASN A 253     8062   9108   7322   -219   1004    575       N
ATOM   1804  CA  ASN A 253       5.046  38.121  -4.642  1.00 67.21           C
ANISOU 1804  CA  ASN A 253     8572   9471   7492   -248   1049    684       C
ATOM   1805  C   ASN A 253       3.549  38.404  -4.697  1.00 72.32           C
ANISOU 1805  C   ASN A 253     9377  10032   8069   -119    949    709       C
ATOM   1806  O   ASN A 253       3.136  39.356  -5.371  1.00 84.03           O
ANISOU 1806  O   ASN A 253    11028  11489   9409   -125    959    820       O
ATOM   1807  CB  ASN A 253       5.502  37.607  -6.012  1.00 81.06           C
ANISOU 1807  CB  ASN A 253    10254  11422   9123   -246   1161    644       C
ATOM   1808  CG  ASN A 253       6.943  37.137  -6.014  1.00 87.66           C
ANISOU 1808  CG  ASN A 253    10899  12382  10026   -342   1262    591       C
ATOM   1809  OD1 ASN A 253       7.275  36.133  -6.646  1.00 92.97           O
ANISOU 1809  OD1 ASN A 253    11439  13206  10681   -282   1320    481       O
ATOM   1810  ND2 ASN A 253       7.809  37.861  -5.311  1.00 84.02           N
ANISOU 1810  ND2 ASN A 253    10419  11865   9641   -489   1283    660       N
ATOM   1811  N   HIS A 254       2.732  37.590  -4.033  1.00 61.38           N
ANISOU 1811  N   HIS A 254     7941   8611   6769     -2    855    610       N
ATOM   1812  CA  HIS A 254       1.312  37.858  -3.882  1.00 64.97           C
ANISOU 1812  CA  HIS A 254     8517   8994   7175    116    752    624       C
ATOM   1813  C   HIS A 254       1.015  38.710  -2.659  1.00 58.31           C
ANISOU 1813  C   HIS A 254     7769   7971   6416     97    672    691       C
ATOM   1814  O   HIS A 254      -0.159  38.933  -2.352  1.00 65.87           O
ANISOU 1814  O   HIS A 254     8812   8868   7348    203    582    694       O
ATOM   1815  CB  HIS A 254       0.498  36.555  -3.768  1.00 76.41           C
ANISOU 1815  CB  HIS A 254     9864  10502   8666    236    694    478       C
ATOM   1816  CG  HIS A 254       1.150  35.358  -4.388  1.00 93.30           C
ANISOU 1816  CG  HIS A 254    11853  12778  10818    235    768    363       C
ATOM   1817  ND1 HIS A 254       1.459  35.287  -5.729  1.00101.34           N
ANISOU 1817  ND1 HIS A 254    12868  13941  11695    229    856    360       N
ATOM   1818  CD2 HIS A 254       1.532  34.175  -3.850  1.00 96.43           C
ANISOU 1818  CD2 HIS A 254    12108  13186  11346    252    767    243       C
ATOM   1819  CE1 HIS A 254       2.016  34.117  -5.989  1.00102.37           C
ANISOU 1819  CE1 HIS A 254    12856  14168  11874    244    907    236       C
ATOM   1820  NE2 HIS A 254       2.073  33.423  -4.866  1.00 99.76           N
ANISOU 1820  NE2 HIS A 254    12444  13751  11710    262    853    165       N
ATOM   1821  N   GLY A 255       2.038  39.178  -1.951  1.00 58.42           N
ANISOU 1821  N   GLY A 255     7762   7910   6523    -33    702    737       N
ATOM   1822  CA  GLY A 255       1.831  39.891  -0.713  1.00 54.71           C
ANISOU 1822  CA  GLY A 255     7372   7273   6141    -57    625    781       C
ATOM   1823  C   GLY A 255       2.074  38.991   0.479  1.00 50.74           C
ANISOU 1823  C   GLY A 255     6720   6752   5807    -51    577    682       C
ATOM   1824  O   GLY A 255       2.519  37.848   0.339  1.00 46.12           O
ANISOU 1824  O   GLY A 255     5975   6272   5276    -35    609    588       O
ATOM   1825  N   PRO A 256       1.764  39.481   1.678  1.00 50.36           N
ANISOU 1825  N   PRO A 256     6731   6567   5838    -54    499    702       N
ATOM   1826  CA  PRO A 256       2.038  38.697   2.892  1.00 47.81           C
ANISOU 1826  CA  PRO A 256     6279   6220   5666    -56    450    622       C
ATOM   1827  C   PRO A 256       1.081  37.521   3.005  1.00 47.91           C
ANISOU 1827  C   PRO A 256     6223   6280   5702     78    398    519       C
ATOM   1828  O   PRO A 256      -0.137  37.692   2.958  1.00 46.51           O
ANISOU 1828  O   PRO A 256     6131   6077   5464    174    341    518       O
ATOM   1829  CB  PRO A 256       1.810  39.706   4.029  1.00 48.99           C
ANISOU 1829  CB  PRO A 256     6544   6210   5859    -91    380    679       C
ATOM   1830  CG  PRO A 256       1.464  41.022   3.371  1.00 53.71           C
ANISOU 1830  CG  PRO A 256     7339   6734   6333   -107    397    788       C
ATOM   1831  CD  PRO A 256       1.016  40.707   1.981  1.00 48.32           C
ANISOU 1831  CD  PRO A 256     6668   6168   5524    -31    442    789       C
ATOM   1832  N   LEU A 257       1.630  36.321   3.173  1.00 47.06           N
ANISOU 1832  N   LEU A 257     5961   6241   5680     84    416    431       N
ATOM   1833  CA  LEU A 257       0.807  35.137   3.377  1.00 41.42           C
ANISOU 1833  CA  LEU A 257     5188   5549   4998    186    370    330       C
ATOM   1834  C   LEU A 257       0.996  34.641   4.804  1.00 46.73           C
ANISOU 1834  C   LEU A 257     5800   6145   5809    180    310    296       C
ATOM   1835  O   LEU A 257       2.129  34.521   5.280  1.00 50.27           O
ANISOU 1835  O   LEU A 257     6166   6593   6340    116    330    299       O
ATOM   1836  CB  LEU A 257       1.155  34.040   2.374  1.00 38.48           C
ANISOU 1836  CB  LEU A 257     4715   5302   4604    218    437    246       C
ATOM   1837  CG  LEU A 257       1.219  34.461   0.905  1.00 42.91           C
ANISOU 1837  CG  LEU A 257     5318   5965   5021    212    512    278       C
ATOM   1838  CD1 LEU A 257       1.703  33.295   0.092  1.00 46.16           C
ANISOU 1838  CD1 LEU A 257     5615   6497   5428    242    578    178       C
ATOM   1839  CD2 LEU A 257      -0.133  34.952   0.380  1.00 44.94           C
ANISOU 1839  CD2 LEU A 257     5697   6224   5155    286    467    303       C
ATOM   1840  N   VAL A 258      -0.108  34.372   5.483  1.00 43.18           N
ANISOU 1840  N   VAL A 258     5388   5643   5376    245    236    264       N
ATOM   1841  CA  VAL A 258      -0.048  33.896   6.862  1.00 40.93           C
ANISOU 1841  CA  VAL A 258     5061   5285   5205    241    176    238       C
ATOM   1842  C   VAL A 258       0.264  32.404   6.832  1.00 43.41           C
ANISOU 1842  C   VAL A 258     5264   5641   5587    276    192    147       C
ATOM   1843  O   VAL A 258      -0.432  31.632   6.163  1.00 43.75           O
ANISOU 1843  O   VAL A 258     5301   5733   5588    332    203     79       O
ATOM   1844  CB  VAL A 258      -1.361  34.180   7.604  1.00 41.69           C
ANISOU 1844  CB  VAL A 258     5238   5320   5283    291     99    238       C
ATOM   1845  CG1 VAL A 258      -1.378  33.468   8.978  1.00 43.77           C
ANISOU 1845  CG1 VAL A 258     5454   5524   5653    291     44    202       C
ATOM   1846  CG2 VAL A 258      -1.537  35.671   7.786  1.00 41.12           C
ANISOU 1846  CG2 VAL A 258     5284   5181   5157    269     78    325       C
ATOM   1847  N   MET A 259       1.346  32.010   7.502  1.00 46.01           N
ANISOU 1847  N   MET A 259     5512   5956   6016    246    194    142       N
ATOM   1848  CA  MET A 259       1.779  30.614   7.538  1.00 51.44           C
ANISOU 1848  CA  MET A 259     6105   6665   6773    295    207     62       C
ATOM   1849  C   MET A 259       1.467  29.936   8.857  1.00 51.24           C
ANISOU 1849  C   MET A 259     6082   6553   6835    320    134     42       C
ATOM   1850  O   MET A 259       1.291  28.716   8.886  1.00 54.66           O
ANISOU 1850  O   MET A 259     6490   6973   7307    374    132    -27       O
ATOM   1851  CB  MET A 259       3.286  30.496   7.285  1.00 45.11           C
ANISOU 1851  CB  MET A 259     5194   5931   6015    268    263     62       C
ATOM   1852  CG  MET A 259       3.775  31.067   5.954  1.00 54.69           C
ANISOU 1852  CG  MET A 259     6391   7248   7139    230    351     81       C
ATOM   1853  SD  MET A 259       2.909  30.439   4.495  1.00 63.16           S
ANISOU 1853  SD  MET A 259     7498   8393   8106    299    402      9       S
ATOM   1854  CE  MET A 259       3.160  28.666   4.668  1.00 71.65           C
ANISOU 1854  CE  MET A 259     8489   9463   9272    391    401   -113       C
ATOM   1855  N   GLU A 260       1.379  30.692   9.946  1.00 46.47           N
ANISOU 1855  N   GLU A 260     5516   5884   6255    281     77    101       N
ATOM   1856  CA  GLU A 260       1.047  30.093  11.231  1.00 51.10           C
ANISOU 1856  CA  GLU A 260     6111   6394   6908    301      9     90       C
ATOM   1857  C   GLU A 260       0.519  31.179  12.147  1.00 51.56           C
ANISOU 1857  C   GLU A 260     6246   6396   6948    261    -48    148       C
ATOM   1858  O   GLU A 260       0.991  32.323  12.086  1.00 46.67           O
ANISOU 1858  O   GLU A 260     5649   5778   6306    205    -40    203       O
ATOM   1859  CB  GLU A 260       2.277  29.418  11.859  1.00 61.28           C
ANISOU 1859  CB  GLU A 260     7309   7681   8292    312     -2     83       C
ATOM   1860  CG  GLU A 260       1.943  28.475  13.003  1.00 78.90           C
ANISOU 1860  CG  GLU A 260     9558   9836  10585    352    -63     66       C
ATOM   1861  CD  GLU A 260       0.881  27.466  12.621  1.00 94.48           C
ANISOU 1861  CD  GLU A 260    11579  11781  12537    394    -52      3       C
ATOM   1862  OE1 GLU A 260       1.258  26.409  12.069  1.00101.23           O
ANISOU 1862  OE1 GLU A 260    12399  12643  13422    445    -18    -54       O
ATOM   1863  OE2 GLU A 260      -0.322  27.732  12.858  1.00 94.43           O
ANISOU 1863  OE2 GLU A 260    11643  11752  12484    374    -77      5       O
ATOM   1864  N   VAL A 261      -0.459  30.825  12.985  1.00 45.65           N
ANISOU 1864  N   VAL A 261     5543   5598   6204    284    -99    132       N
ATOM   1865  CA  VAL A 261      -0.871  31.666  14.105  1.00 45.09           C
ANISOU 1865  CA  VAL A 261     5532   5472   6126    258   -158    174       C
ATOM   1866  C   VAL A 261      -0.689  30.857  15.383  1.00 52.56           C
ANISOU 1866  C   VAL A 261     6455   6372   7142    263   -208    167       C
ATOM   1867  O   VAL A 261      -1.266  29.772  15.524  1.00 49.73           O
ANISOU 1867  O   VAL A 261     6096   6001   6797    295   -212    126       O
ATOM   1868  CB  VAL A 261      -2.315  32.158  13.967  1.00 43.42           C
ANISOU 1868  CB  VAL A 261     5400   5265   5834    287   -172    165       C
ATOM   1869  CG1 VAL A 261      -2.680  33.055  15.161  1.00 40.82           C
ANISOU 1869  CG1 VAL A 261     5134   4879   5496    271   -230    200       C
ATOM   1870  CG2 VAL A 261      -2.506  32.910  12.643  1.00 41.24           C
ANISOU 1870  CG2 VAL A 261     5156   5035   5476    299   -128    179       C
ATOM   1871  N   ASN A 262       0.117  31.378  16.306  1.00 46.20           N
ANISOU 1871  N   ASN A 262     5637   5541   6376    225   -247    207       N
ATOM   1872  CA  ASN A 262       0.519  30.663  17.515  1.00 43.60           C
ANISOU 1872  CA  ASN A 262     5280   5179   6107    234   -300    212       C
ATOM   1873  C   ASN A 262       0.002  31.427  18.722  1.00 41.64           C
ANISOU 1873  C   ASN A 262     5099   4890   5834    204   -359    239       C
ATOM   1874  O   ASN A 262       0.397  32.579  18.947  1.00 43.67           O
ANISOU 1874  O   ASN A 262     5376   5139   6076    155   -375    268       O
ATOM   1875  CB  ASN A 262       2.044  30.517  17.585  1.00 42.89           C
ANISOU 1875  CB  ASN A 262     5094   5123   6079    223   -301    225       C
ATOM   1876  CG  ASN A 262       2.501  29.573  18.706  1.00 64.11           C
ANISOU 1876  CG  ASN A 262     7749   7785   8824    261   -358    230       C
ATOM   1877  OD1 ASN A 262       1.728  29.221  19.613  1.00 68.85           O
ANISOU 1877  OD1 ASN A 262     8414   8333   9415    273   -401    236       O
ATOM   1878  ND2 ASN A 262       3.767  29.163  18.646  1.00 64.76           N
ANISOU 1878  ND2 ASN A 262     7732   7915   8961    285   -359    228       N
ATOM   1879  N   SER A 263      -0.850  30.774  19.514  1.00 41.78           N
ANISOU 1879  N   SER A 263     5153   4879   5844    227   -389    227       N
ATOM   1880  CA  SER A 263      -1.459  31.417  20.675  1.00 43.86           C
ANISOU 1880  CA  SER A 263     5479   5117   6071    207   -440    244       C
ATOM   1881  C   SER A 263      -0.526  31.495  21.872  1.00 45.19           C
ANISOU 1881  C   SER A 263     5626   5267   6276    181   -499    275       C
ATOM   1882  O   SER A 263      -0.815  32.238  22.815  1.00 51.87           O
ANISOU 1882  O   SER A 263     6524   6097   7089    156   -542    286       O
ATOM   1883  CB  SER A 263      -2.709  30.654  21.093  1.00 52.94           C
ANISOU 1883  CB  SER A 263     6665   6261   7188    227   -442    219       C
ATOM   1884  OG  SER A 263      -2.337  29.332  21.449  1.00 60.62           O
ANISOU 1884  OG  SER A 263     7612   7208   8211    240   -449    220       O
ATOM   1885  N   SER A 264       0.561  30.729  21.880  1.00 47.56           N
ANISOU 1885  N   SER A 264     5853   5580   6640    196   -507    283       N
ATOM   1886  CA  SER A 264       1.506  30.733  22.996  1.00 52.60           C
ANISOU 1886  CA  SER A 264     6455   6223   7307    183   -573    311       C
ATOM   1887  C   SER A 264       2.927  30.858  22.468  1.00 48.30           C
ANISOU 1887  C   SER A 264     5806   5732   6813    171   -563    314       C
ATOM   1888  O   SER A 264       3.755  29.955  22.652  1.00 49.27           O
ANISOU 1888  O   SER A 264     5855   5879   6985    221   -583    317       O
ATOM   1889  CB  SER A 264       1.343  29.472  23.844  1.00 60.32           C
ANISOU 1889  CB  SER A 264     7447   7171   8302    233   -608    324       C
ATOM   1890  OG  SER A 264       2.268  29.488  24.922  1.00 72.61           O
ANISOU 1890  OG  SER A 264     8967   8744   9875    233   -680    354       O
ATOM   1891  N   PRO A 265       3.251  31.972  21.804  1.00 48.57           N
ANISOU 1891  N   PRO A 265     5831   5790   6832    107   -532    314       N
ATOM   1892  CA  PRO A 265       4.584  32.101  21.206  1.00 44.84           C
ANISOU 1892  CA  PRO A 265     5246   5389   6400     78   -508    313       C
ATOM   1893  C   PRO A 265       5.650  32.147  22.281  1.00 50.05           C
ANISOU 1893  C   PRO A 265     5831   6095   7091     54   -581    325       C
ATOM   1894  O   PRO A 265       5.440  32.714  23.356  1.00 49.56           O
ANISOU 1894  O   PRO A 265     5823   6003   7003     13   -643    337       O
ATOM   1895  CB  PRO A 265       4.508  33.433  20.458  1.00 45.96           C
ANISOU 1895  CB  PRO A 265     5433   5526   6502     -9   -463    321       C
ATOM   1896  CG  PRO A 265       3.514  34.221  21.258  1.00 47.02           C
ANISOU 1896  CG  PRO A 265     5694   5586   6586    -31   -504    329       C
ATOM   1897  CD  PRO A 265       2.485  33.229  21.697  1.00 45.92           C
ANISOU 1897  CD  PRO A 265     5593   5416   6438     54   -521    317       C
ATOM   1898  N   GLY A 266       6.804  31.554  21.980  1.00 49.95           N
ANISOU 1898  N   GLY A 266     5686   6165   7127     85   -576    315       N
ATOM   1899  CA  GLY A 266       7.941  31.662  22.880  1.00 50.83           C
ANISOU 1899  CA  GLY A 266     5697   6352   7263     61   -647    321       C
ATOM   1900  C   GLY A 266       8.452  33.087  22.979  1.00 53.38           C
ANISOU 1900  C   GLY A 266     6009   6709   7564    -86   -651    322       C
ATOM   1901  O   GLY A 266       8.356  33.874  22.037  1.00 49.52           O
ANISOU 1901  O   GLY A 266     5549   6211   7057   -163   -581    321       O
ATOM   1902  N   LEU A 267       9.002  33.423  24.147  1.00 49.13           N
ANISOU 1902  N   LEU A 267     5439   6207   7023   -131   -737    324       N
ATOM   1903  CA  LEU A 267       9.481  34.776  24.404  1.00 52.24           C
ANISOU 1903  CA  LEU A 267     5836   6619   7393   -287   -752    316       C
ATOM   1904  C   LEU A 267      10.982  34.945  24.211  1.00 50.17           C
ANISOU 1904  C   LEU A 267     5392   6506   7162   -360   -754    297       C
ATOM   1905  O   LEU A 267      11.438  36.083  24.049  1.00 48.62           O
ANISOU 1905  O   LEU A 267     5195   6328   6951   -518   -735    288       O
ATOM   1906  CB  LEU A 267       9.130  35.208  25.839  1.00 48.73           C
ANISOU 1906  CB  LEU A 267     5474   6129   6911   -315   -845    316       C
ATOM   1907  CG  LEU A 267       7.650  35.369  26.205  1.00 51.54           C
ANISOU 1907  CG  LEU A 267     6008   6353   7220   -276   -846    326       C
ATOM   1908  CD1 LEU A 267       7.459  36.266  27.420  1.00 49.55           C
ANISOU 1908  CD1 LEU A 267     5841   6066   6920   -349   -919    312       C
ATOM   1909  CD2 LEU A 267       6.902  35.930  25.033  1.00 53.25           C
ANISOU 1909  CD2 LEU A 267     6315   6496   7420   -297   -756    329       C
ATOM   1910  N   GLU A 268      11.759  33.858  24.222  1.00 52.52           N
ANISOU 1910  N   GLU A 268     5540   6914   7502   -253   -774    288       N
ATOM   1911  CA  GLU A 268      13.216  34.002  24.291  1.00 55.14           C
ANISOU 1911  CA  GLU A 268     5675   7420   7857   -313   -797    262       C
ATOM   1912  C   GLU A 268      13.782  34.631  23.024  1.00 50.11           C
ANISOU 1912  C   GLU A 268     4965   6852   7225   -429   -691    248       C
ATOM   1913  O   GLU A 268      14.593  35.563  23.092  1.00 56.36           O
ANISOU 1913  O   GLU A 268     5682   7728   8006   -594   -692    231       O
ATOM   1914  CB  GLU A 268      13.889  32.649  24.557  1.00 46.59           C
ANISOU 1914  CB  GLU A 268     4448   6440   6812   -138   -845    254       C
ATOM   1915  CG  GLU A 268      15.407  32.779  24.624  1.00 54.27           C
ANISOU 1915  CG  GLU A 268     5191   7625   7804   -185   -872    219       C
ATOM   1916  CD  GLU A 268      16.092  31.615  25.330  1.00 60.47           C
ANISOU 1916  CD  GLU A 268     5848   8514   8613     -5   -962    215       C
ATOM   1917  OE1 GLU A 268      15.413  30.605  25.601  1.00 62.92           O
ANISOU 1917  OE1 GLU A 268     6259   8716   8931    160   -987    244       O
ATOM   1918  OE2 GLU A 268      17.308  31.722  25.609  1.00 66.49           O
ANISOU 1918  OE2 GLU A 268     6412   9468   9381    -30  -1009    183       O
ATOM   1919  N   GLY A 269      13.360  34.144  21.857  1.00 54.50           N
ANISOU 1919  N   GLY A 269     5545   7375   7788   -356   -598    253       N
ATOM   1920  CA  GLY A 269      13.929  34.648  20.618  1.00 58.58           C
ANISOU 1920  CA  GLY A 269     5988   7972   8298   -457   -492    244       C
ATOM   1921  C   GLY A 269      13.588  36.104  20.363  1.00 61.57           C
ANISOU 1921  C   GLY A 269     6500   8264   8631   -648   -452    268       C
ATOM   1922  O   GLY A 269      14.441  36.886  19.935  1.00 56.08           O
ANISOU 1922  O   GLY A 269     5725   7658   7924   -809   -405    262       O
ATOM   1923  N   ILE A 270      12.339  36.494  20.628  1.00 61.26           N
ANISOU 1923  N   ILE A 270     6666   8049   8560   -634   -469    295       N
ATOM   1924  CA  ILE A 270      11.940  37.870  20.353  1.00 48.96           C
ANISOU 1924  CA  ILE A 270     5262   6387   6956   -788   -432    319       C
ATOM   1925  C   ILE A 270      12.588  38.828  21.347  1.00 60.81           C
ANISOU 1925  C   ILE A 270     6755   7901   8451   -949   -499    304       C
ATOM   1926  O   ILE A 270      12.980  39.942  20.976  1.00 68.35           O
ANISOU 1926  O   ILE A 270     7751   8839   9381  -1129   -454    313       O
ATOM   1927  CB  ILE A 270      10.398  37.972  20.332  1.00 54.78           C
ANISOU 1927  CB  ILE A 270     6207   6949   7656   -701   -433    344       C
ATOM   1928  CG1 ILE A 270       9.948  39.355  19.852  1.00 61.77           C
ANISOU 1928  CG1 ILE A 270     7264   7718   8487   -826   -387    374       C
ATOM   1929  CG2 ILE A 270       9.791  37.597  21.680  1.00 50.69           C
ANISOU 1929  CG2 ILE A 270     5744   6373   7143   -616   -536    332       C
ATOM   1930  CD1 ILE A 270      10.224  39.601  18.368  1.00 68.54           C
ANISOU 1930  CD1 ILE A 270     8110   8613   9321   -879   -274    401       C
ATOM   1931  N   GLU A 271      12.762  38.406  22.607  1.00 55.72           N
ANISOU 1931  N   GLU A 271     6058   7291   7825   -897   -605    280       N
ATOM   1932  CA  GLU A 271      13.409  39.262  23.597  1.00 58.23           C
ANISOU 1932  CA  GLU A 271     6357   7638   8131  -1050   -677    253       C
ATOM   1933  C   GLU A 271      14.912  39.361  23.367  1.00 60.31           C
ANISOU 1933  C   GLU A 271     6399   8100   8417  -1174   -663    224       C
ATOM   1934  O   GLU A 271      15.491  40.445  23.501  1.00 61.09           O
ANISOU 1934  O   GLU A 271     6501   8212   8496  -1382   -660    206       O
ATOM   1935  CB  GLU A 271      13.128  38.750  25.012  1.00 57.80           C
ANISOU 1935  CB  GLU A 271     6311   7575   8074   -950   -797    238       C
ATOM   1936  CG  GLU A 271      11.676  38.958  25.447  1.00 57.97           C
ANISOU 1936  CG  GLU A 271     6556   7412   8058   -878   -816    256       C
ATOM   1937  CD  GLU A 271      11.483  38.869  26.953  1.00 55.13           C
ANISOU 1937  CD  GLU A 271     6229   7043   7675   -846   -931    237       C
ATOM   1938  OE1 GLU A 271      12.262  38.165  27.624  1.00 52.63           O
ANISOU 1938  OE1 GLU A 271     5763   6858   7375   -800  -1003    224       O
ATOM   1939  OE2 GLU A 271      10.546  39.511  27.465  1.00 54.72           O
ANISOU 1939  OE2 GLU A 271     6354   6859   7579   -858   -950    233       O
ATOM   1940  N   THR A 272      15.562  38.244  23.043  1.00 56.22           N
ANISOU 1940  N   THR A 272     5685   7739   7937  -1051   -654    211       N
ATOM   1941  CA  THR A 272      16.996  38.284  22.771  1.00 55.95           C
ANISOU 1941  CA  THR A 272     5413   7925   7920  -1153   -635    176       C
ATOM   1942  C   THR A 272      17.296  39.125  21.535  1.00 59.14           C
ANISOU 1942  C   THR A 272     5828   8340   8304  -1329   -506    190       C
ATOM   1943  O   THR A 272      18.228  39.931  21.539  1.00 64.66           O
ANISOU 1943  O   THR A 272     6433   9144   8992  -1538   -491    166       O
ATOM   1944  CB  THR A 272      17.532  36.863  22.610  1.00 64.63           C
ANISOU 1944  CB  THR A 272     6317   9180   9061   -947   -647    158       C
ATOM   1945  OG1 THR A 272      17.247  36.112  23.799  1.00 66.68           O
ANISOU 1945  OG1 THR A 272     6591   9414   9330   -791   -768    158       O
ATOM   1946  CG2 THR A 272      19.044  36.877  22.372  1.00 68.80           C
ANISOU 1946  CG2 THR A 272     6570   9967   9602  -1034   -631    111       C
ATOM   1947  N   THR A 273      16.486  38.983  20.480  1.00 65.04           N
ANISOU 1947  N   THR A 273     6697   8977   9037  -1258   -414    229       N
ATOM   1948  CA  THR A 273      16.710  39.745  19.253  1.00 68.76           C
ANISOU 1948  CA  THR A 273     7198   9454   9475  -1413   -289    255       C
ATOM   1949  C   THR A 273      16.452  41.234  19.456  1.00 70.61           C
ANISOU 1949  C   THR A 273     7625   9537   9667  -1631   -283    280       C
ATOM   1950  O   THR A 273      17.298  42.069  19.125  1.00 76.80           O
ANISOU 1950  O   THR A 273     8356  10392  10432  -1852   -230    277       O
ATOM   1951  CB  THR A 273      15.812  39.224  18.131  1.00 70.74           C
ANISOU 1951  CB  THR A 273     7549   9620   9709  -1271   -205    290       C
ATOM   1952  OG1 THR A 273      16.055  37.826  17.922  1.00 72.40           O
ANISOU 1952  OG1 THR A 273     7599   9952   9959  -1070   -206    259       O
ATOM   1953  CG2 THR A 273      16.092  39.989  16.832  1.00 74.83           C
ANISOU 1953  CG2 THR A 273     8097  10157  10179  -1427    -73    324       C
ATOM   1954  N   THR A 274      15.276  41.589  19.970  1.00 64.68           N
ANISOU 1954  N   THR A 274     7103   8576   8898  -1572   -333    303       N
ATOM   1955  CA  THR A 274      14.849  42.984  19.996  1.00 67.78           C
ANISOU 1955  CA  THR A 274     7720   8787   9244  -1740   -317    331       C
ATOM   1956  C   THR A 274      15.305  43.737  21.238  1.00 73.55           C
ANISOU 1956  C   THR A 274     8465   9503   9977  -1891   -409    287       C
ATOM   1957  O   THR A 274      15.289  44.972  21.232  1.00 76.84           O
ANISOU 1957  O   THR A 274     9042   9794  10360  -2078   -389    298       O
ATOM   1958  CB  THR A 274      13.316  43.078  19.897  1.00 68.33           C
ANISOU 1958  CB  THR A 274     8034   8644   9284  -1593   -322    369       C
ATOM   1959  OG1 THR A 274      12.719  42.612  21.113  1.00 72.33           O
ANISOU 1959  OG1 THR A 274     8569   9106   9809  -1461   -432    339       O
ATOM   1960  CG2 THR A 274      12.788  42.246  18.742  1.00 62.43           C
ANISOU 1960  CG2 THR A 274     7271   7920   8531  -1434   -245    401       C
ATOM   1961  N   GLY A 275      15.708  43.037  22.299  1.00 71.29           N
ANISOU 1961  N   GLY A 275     8028   9336   9724  -1815   -512    238       N
ATOM   1962  CA  GLY A 275      15.932  43.671  23.582  1.00 63.40           C
ANISOU 1962  CA  GLY A 275     7063   8311   8714  -1925   -615    191       C
ATOM   1963  C   GLY A 275      14.673  44.101  24.309  1.00 65.77           C
ANISOU 1963  C   GLY A 275     7615   8389   8984  -1849   -672    197       C
ATOM   1964  O   GLY A 275      14.758  44.486  25.484  1.00 66.99           O
ANISOU 1964  O   GLY A 275     7802   8526   9125  -1905   -767    151       O
ATOM   1965  N   LYS A 276      13.510  44.041  23.663  1.00 59.35           N
ANISOU 1965  N   LYS A 276     6973   7424   8155  -1720   -619    246       N
ATOM   1966  CA  LYS A 276      12.272  44.525  24.262  1.00 68.27           C
ANISOU 1966  CA  LYS A 276     8339   8354   9248  -1645   -662    248       C
ATOM   1967  C   LYS A 276      11.845  43.658  25.454  1.00 72.07           C
ANISOU 1967  C   LYS A 276     8773   8873   9735  -1482   -765    219       C
ATOM   1968  O   LYS A 276      12.197  42.478  25.567  1.00 69.02           O
ANISOU 1968  O   LYS A 276     8208   8631   9384  -1365   -790    218       O
ATOM   1969  CB  LYS A 276      11.151  44.558  23.217  1.00 60.57           C
ANISOU 1969  CB  LYS A 276     7521   7244   8247  -1528   -581    306       C
ATOM   1970  CG  LYS A 276      11.346  45.594  22.109  1.00 66.58           C
ANISOU 1970  CG  LYS A 276     8397   7920   8979  -1682   -483    349       C
ATOM   1971  CD  LYS A 276      10.089  45.739  21.254  1.00 60.20           C
ANISOU 1971  CD  LYS A 276     7777   6968   8131  -1546   -428    403       C
ATOM   1972  CE  LYS A 276      10.330  46.595  20.020  1.00 61.32           C
ANISOU 1972  CE  LYS A 276     8021   7044   8235  -1677   -325    462       C
ATOM   1973  NZ  LYS A 276      11.001  47.858  20.373  1.00 70.86           N
ANISOU 1973  NZ  LYS A 276     9332   8164   9427  -1915   -328    452       N
ATOM   1974  N   ASN A 277      11.075  44.272  26.358  1.00 67.55           N
ANISOU 1974  N   ASN A 277     8376   8165   9124  -1471   -824    194       N
ATOM   1975  CA  ASN A 277      10.514  43.576  27.517  1.00 59.31           C
ANISOU 1975  CA  ASN A 277     7326   7139   8068  -1326   -915    172       C
ATOM   1976  C   ASN A 277       9.121  43.088  27.135  1.00 58.71           C
ANISOU 1976  C   ASN A 277     7366   6964   7977  -1137   -878    208       C
ATOM   1977  O   ASN A 277       8.098  43.682  27.479  1.00 59.08           O
ANISOU 1977  O   ASN A 277     7596   6874   7979  -1095   -888    198       O
ATOM   1978  CB  ASN A 277      10.481  44.487  28.739  1.00 55.36           C
ANISOU 1978  CB  ASN A 277     6938   6572   7525  -1423   -997    114       C
ATOM   1979  CG  ASN A 277      10.022  43.764  29.986  1.00 58.93           C
ANISOU 1979  CG  ASN A 277     7372   7069   7952  -1289  -1090     92       C
ATOM   1980  OD1 ASN A 277       9.644  42.595  29.935  1.00 54.63           O
ANISOU 1980  OD1 ASN A 277     6750   6583   7423  -1124  -1090    127       O
ATOM   1981  ND2 ASN A 277      10.052  44.456  31.120  1.00 65.20           N
ANISOU 1981  ND2 ASN A 277     8245   7830   8700  -1365  -1167     34       N
ATOM   1982  N   VAL A 278       9.087  41.969  26.415  1.00 51.18           N
ANISOU 1982  N   VAL A 278     6297   6092   7059  -1018   -836    243       N
ATOM   1983  CA  VAL A 278       7.811  41.468  25.926  1.00 49.81           C
ANISOU 1983  CA  VAL A 278     6214   5841   6869   -858   -795    272       C
ATOM   1984  C   VAL A 278       6.968  40.916  27.072  1.00 45.63           C
ANISOU 1984  C   VAL A 278     5729   5296   6314   -737   -866    256       C
ATOM   1985  O   VAL A 278       5.744  41.091  27.095  1.00 48.29           O
ANISOU 1985  O   VAL A 278     6201   5536   6610   -653   -852    257       O
ATOM   1986  CB  VAL A 278       8.048  40.426  24.822  1.00 50.63           C
ANISOU 1986  CB  VAL A 278     6190   6034   7015   -779   -728    303       C
ATOM   1987  CG1 VAL A 278       6.732  39.808  24.404  1.00 43.93           C
ANISOU 1987  CG1 VAL A 278     5422   5123   6148   -622   -696    321       C
ATOM   1988  CG2 VAL A 278       8.717  41.097  23.630  1.00 53.91           C
ANISOU 1988  CG2 VAL A 278     6588   6459   7436   -902   -644    322       C
ATOM   1989  N   ALA A 279       7.596  40.228  28.031  1.00 44.45           N
ANISOU 1989  N   ALA A 279     5461   5249   6179   -723   -941    242       N
ATOM   1990  CA  ALA A 279       6.843  39.778  29.198  1.00 44.09           C
ANISOU 1990  CA  ALA A 279     5469   5189   6094   -628  -1007    232       C
ATOM   1991  C   ALA A 279       6.160  40.958  29.881  1.00 42.23           C
ANISOU 1991  C   ALA A 279     5406   4845   5795   -678  -1033    194       C
ATOM   1992  O   ALA A 279       4.972  40.888  30.218  1.00 44.95           O
ANISOU 1992  O   ALA A 279     5858   5126   6095   -583  -1030    190       O
ATOM   1993  CB  ALA A 279       7.764  39.053  30.174  1.00 43.07           C
ANISOU 1993  CB  ALA A 279     5201   5187   5976   -621  -1094    226       C
ATOM   1994  N   GLY A 280       6.889  42.063  30.053  1.00 42.31           N
ANISOU 1994  N   GLY A 280     5447   4831   5799   -831  -1053    160       N
ATOM   1995  CA  GLY A 280       6.309  43.234  30.695  1.00 43.59           C
ANISOU 1995  CA  GLY A 280     5787   4873   5901   -879  -1078    114       C
ATOM   1996  C   GLY A 280       5.169  43.830  29.892  1.00 46.66           C
ANISOU 1996  C   GLY A 280     6342   5121   6266   -815  -1006    129       C
ATOM   1997  O   GLY A 280       4.155  44.259  30.452  1.00 46.21           O
ANISOU 1997  O   GLY A 280     6423   4983   6152   -745  -1021     99       O
ATOM   1998  N   ILE A 281       5.317  43.867  28.567  1.00 40.56           N
ANISOU 1998  N   ILE A 281     5554   4329   5528   -830   -927    172       N
ATOM   1999  CA  ILE A 281       4.239  44.386  27.728  1.00 42.17           C
ANISOU 1999  CA  ILE A 281     5908   4413   5701   -753   -864    193       C
ATOM   2000  C   ILE A 281       2.990  43.532  27.906  1.00 42.74           C
ANISOU 2000  C   ILE A 281     5983   4510   5748   -573   -863    197       C
ATOM   2001  O   ILE A 281       1.859  44.044  27.967  1.00 46.61           O
ANISOU 2001  O   ILE A 281     6610   4916   6184   -485   -854    180       O
ATOM   2002  CB  ILE A 281       4.696  44.440  26.256  1.00 47.08           C
ANISOU 2002  CB  ILE A 281     6496   5036   6356   -801   -781    245       C
ATOM   2003  CG1 ILE A 281       5.771  45.532  26.085  1.00 51.42           C
ANISOU 2003  CG1 ILE A 281     7085   5537   6914  -1003   -771    240       C
ATOM   2004  CG2 ILE A 281       3.495  44.666  25.323  1.00 42.13           C
ANISOU 2004  CG2 ILE A 281     5996   4322   5691   -680   -722    275       C
ATOM   2005  CD1 ILE A 281       6.537  45.493  24.773  1.00 52.48           C
ANISOU 2005  CD1 ILE A 281     7144   5717   7081  -1088   -690    290       C
ATOM   2006  N   ILE A 282       3.182  42.217  28.022  1.00 39.33           N
ANISOU 2006  N   ILE A 282     5398   4196   5349   -515   -872    215       N
ATOM   2007  CA  ILE A 282       2.060  41.300  28.205  1.00 39.33           C
ANISOU 2007  CA  ILE A 282     5391   4225   5327   -371   -867    220       C
ATOM   2008  C   ILE A 282       1.391  41.526  29.556  1.00 42.05           C
ANISOU 2008  C   ILE A 282     5812   4556   5610   -336   -926    178       C
ATOM   2009  O   ILE A 282       0.158  41.552  29.656  1.00 40.57           O
ANISOU 2009  O   ILE A 282     5700   4342   5371   -237   -909    163       O
ATOM   2010  CB  ILE A 282       2.548  39.850  28.040  1.00 41.76           C
ANISOU 2010  CB  ILE A 282     5537   4641   5687   -333   -865    250       C
ATOM   2011  CG1 ILE A 282       2.865  39.542  26.564  1.00 40.56           C
ANISOU 2011  CG1 ILE A 282     5324   4507   5582   -331   -790    283       C
ATOM   2012  CG2 ILE A 282       1.532  38.843  28.642  1.00 36.46           C
ANISOU 2012  CG2 ILE A 282     4864   4000   4987   -219   -877    251       C
ATOM   2013  CD1 ILE A 282       3.555  38.170  26.375  1.00 38.48           C
ANISOU 2013  CD1 ILE A 282     4902   4343   5376   -294   -788    303       C
ATOM   2014  N   ILE A 283       2.186  41.693  30.620  1.00 43.89           N
ANISOU 2014  N   ILE A 283     6018   4820   5838   -415   -996    153       N
ATOM   2015  CA  ILE A 283       1.608  41.985  31.929  1.00 40.34           C
ANISOU 2015  CA  ILE A 283     5647   4363   5318   -389  -1051    106       C
ATOM   2016  C   ILE A 283       0.800  43.272  31.864  1.00 45.06           C
ANISOU 2016  C   ILE A 283     6420   4840   5862   -374  -1032     62       C
ATOM   2017  O   ILE A 283      -0.329  43.345  32.364  1.00 41.67           O
ANISOU 2017  O   ILE A 283     6065   4400   5369   -276  -1031     32       O
ATOM   2018  CB  ILE A 283       2.704  42.081  33.003  1.00 44.23           C
ANISOU 2018  CB  ILE A 283     6085   4914   5807   -489  -1135     81       C
ATOM   2019  CG1 ILE A 283       3.483  40.767  33.100  1.00 42.36           C
ANISOU 2019  CG1 ILE A 283     5678   4800   5617   -473  -1161    128       C
ATOM   2020  CG2 ILE A 283       2.082  42.521  34.350  1.00 41.38           C
ANISOU 2020  CG2 ILE A 283     5824   4541   5357   -467  -1189     24       C
ATOM   2021  CD1 ILE A 283       2.609  39.541  33.448  1.00 40.35           C
ANISOU 2021  CD1 ILE A 283     5402   4590   5339   -345  -1155    162       C
ATOM   2022  N   GLU A 284       1.376  44.307  31.242  1.00 43.30           N
ANISOU 2022  N   GLU A 284     6267   4524   5660   -469  -1015     57       N
ATOM   2023  CA  GLU A 284       0.690  45.591  31.118  1.00 49.76           C
ANISOU 2023  CA  GLU A 284     7276   5200   6429   -449   -999     20       C
ATOM   2024  C   GLU A 284      -0.638  45.440  30.383  1.00 51.27           C
ANISOU 2024  C   GLU A 284     7518   5370   6591   -290   -943     38       C
ATOM   2025  O   GLU A 284      -1.631  46.084  30.740  1.00 44.61           O
ANISOU 2025  O   GLU A 284     6801   4465   5682   -197   -946     -6       O
ATOM   2026  CB  GLU A 284       1.589  46.589  30.393  1.00 51.38           C
ANISOU 2026  CB  GLU A 284     7550   5304   6668   -590   -978     31       C
ATOM   2027  CG  GLU A 284       0.920  47.916  30.071  1.00 63.99           C
ANISOU 2027  CG  GLU A 284     9371   6725   8219   -562   -954      9       C
ATOM   2028  CD  GLU A 284       1.834  48.853  29.303  1.00 75.08           C
ANISOU 2028  CD  GLU A 284    10855   8018   9653   -722   -925     33       C
ATOM   2029  OE1 GLU A 284       2.082  48.580  28.108  1.00 72.34           O
ANISOU 2029  OE1 GLU A 284    10455   7688   9341   -735   -864    102       O
ATOM   2030  OE2 GLU A 284       2.304  49.853  29.895  1.00 80.33           O
ANISOU 2030  OE2 GLU A 284    11641   8581  10301   -842   -959    -18       O
ATOM   2031  N   HIS A 285      -0.675  44.595  29.350  1.00 47.15           N
ANISOU 2031  N   HIS A 285     6893   4909   6112   -252   -892     96       N
ATOM   2032  CA  HIS A 285      -1.939  44.315  28.672  1.00 43.75           C
ANISOU 2032  CA  HIS A 285     6483   4489   5649   -106   -846    107       C
ATOM   2033  C   HIS A 285      -2.976  43.779  29.652  1.00 44.01           C
ANISOU 2033  C   HIS A 285     6499   4597   5626     -4   -868     67       C
ATOM   2034  O   HIS A 285      -4.127  44.229  29.672  1.00 41.58           O
ANISOU 2034  O   HIS A 285     6275   4269   5256    109   -855     33       O
ATOM   2035  CB  HIS A 285      -1.719  43.311  27.541  1.00 42.43           C
ANISOU 2035  CB  HIS A 285     6190   4396   5535    -97   -796    165       C
ATOM   2036  CG  HIS A 285      -2.988  42.890  26.879  1.00 47.91           C
ANISOU 2036  CG  HIS A 285     6882   5127   6193     40   -754    168       C
ATOM   2037  ND1 HIS A 285      -3.580  43.630  25.875  1.00 44.81           N
ANISOU 2037  ND1 HIS A 285     6587   4671   5766    106   -717    180       N
ATOM   2038  CD2 HIS A 285      -3.794  41.822  27.091  1.00 45.33           C
ANISOU 2038  CD2 HIS A 285     6471   4901   5853    118   -747    159       C
ATOM   2039  CE1 HIS A 285      -4.693  43.029  25.490  1.00 48.02           C
ANISOU 2039  CE1 HIS A 285     6952   5154   6139    223   -693    172       C
ATOM   2040  NE2 HIS A 285      -4.846  41.929  26.212  1.00 50.62           N
ANISOU 2040  NE2 HIS A 285     7170   5580   6481    223   -706    157       N
ATOM   2041  N   LEU A 286      -2.570  42.821  30.484  1.00 38.90           N
ANISOU 2041  N   LEU A 286     5741   4042   4995    -41   -901     71       N
ATOM   2042  CA  LEU A 286      -3.448  42.266  31.507  1.00 49.13           C
ANISOU 2042  CA  LEU A 286     7021   5415   6231     30   -919     40       C
ATOM   2043  C   LEU A 286      -3.927  43.326  32.493  1.00 49.44           C
ANISOU 2043  C   LEU A 286     7187   5404   6192     55   -953    -31       C
ATOM   2044  O   LEU A 286      -5.084  43.295  32.929  1.00 50.68           O
ANISOU 2044  O   LEU A 286     7372   5606   6279    155   -941    -69       O
ATOM   2045  CB  LEU A 286      -2.718  41.160  32.267  1.00 44.58           C
ANISOU 2045  CB  LEU A 286     6331   4926   5683    -27   -958     68       C
ATOM   2046  CG  LEU A 286      -2.720  39.755  31.702  1.00 48.45           C
ANISOU 2046  CG  LEU A 286     6701   5488   6222     -3   -925    123       C
ATOM   2047  CD1 LEU A 286      -2.112  38.838  32.756  1.00 43.54           C
ANISOU 2047  CD1 LEU A 286     6008   4933   5601    -37   -978    146       C
ATOM   2048  CD2 LEU A 286      -4.137  39.322  31.327  1.00 41.94           C
ANISOU 2048  CD2 LEU A 286     5880   4700   5354     95   -872    113       C
ATOM   2049  N   GLU A 287      -3.044  44.248  32.892  1.00 42.40           N
ANISOU 2049  N   GLU A 287     6371   4432   5308    -40   -996    -57       N
ATOM   2050  CA  GLU A 287      -3.461  45.314  33.796  1.00 44.77           C
ANISOU 2050  CA  GLU A 287     6810   4667   5532    -17  -1028   -136       C
ATOM   2051  C   GLU A 287      -4.554  46.170  33.164  1.00 50.99           C
ANISOU 2051  C   GLU A 287     7724   5371   6277    108   -987   -165       C
ATOM   2052  O   GLU A 287      -5.514  46.565  33.839  1.00 45.38           O
ANISOU 2052  O   GLU A 287     7085   4670   5486    211   -992   -230       O
ATOM   2053  CB  GLU A 287      -2.269  46.199  34.172  1.00 44.10           C
ANISOU 2053  CB  GLU A 287     6792   4494   5468   -162  -1078   -164       C
ATOM   2054  CG  GLU A 287      -1.258  45.535  35.086  1.00 44.80           C
ANISOU 2054  CG  GLU A 287     6768   4683   5573   -268  -1139   -159       C
ATOM   2055  CD  GLU A 287       0.051  46.276  35.095  1.00 50.35           C
ANISOU 2055  CD  GLU A 287     7492   5323   6315   -433  -1177   -175       C
ATOM   2056  OE1 GLU A 287       0.118  47.345  34.464  1.00 49.35           O
ANISOU 2056  OE1 GLU A 287     7492   5058   6199   -473  -1152   -190       O
ATOM   2057  OE2 GLU A 287       1.018  45.796  35.720  1.00 46.54           O
ANISOU 2057  OE2 GLU A 287     6902   4933   5849   -525  -1233   -171       O
ATOM   2058  N   LYS A 288      -4.407  46.487  31.874  1.00 44.94           N
ANISOU 2058  N   LYS A 288     6989   4529   5556    109   -947   -117       N
ATOM   2059  CA  LYS A 288      -5.342  47.398  31.214  1.00 54.72           C
ANISOU 2059  CA  LYS A 288     8365   5676   6751    236   -917   -135       C
ATOM   2060  C   LYS A 288      -6.696  46.744  30.968  1.00 56.54           C
ANISOU 2060  C   LYS A 288     8524   6025   6935    398   -883   -141       C
ATOM   2061  O   LYS A 288      -7.723  47.428  30.992  1.00 56.97           O
ANISOU 2061  O   LYS A 288     8674   6054   6920    540   -876   -190       O
ATOM   2062  CB  LYS A 288      -4.775  47.883  29.874  1.00 59.14           C
ANISOU 2062  CB  LYS A 288     8981   6128   7361    186   -884    -71       C
ATOM   2063  CG  LYS A 288      -3.494  48.704  29.957  1.00 72.14           C
ANISOU 2063  CG  LYS A 288    10716   7647   9048     12   -906    -67       C
ATOM   2064  CD  LYS A 288      -3.269  49.502  28.664  1.00 80.80           C
ANISOU 2064  CD  LYS A 288    11931   8608  10160     -8   -863    -10       C
ATOM   2065  CE  LYS A 288      -1.944  50.275  28.677  1.00 87.10           C
ANISOU 2065  CE  LYS A 288    12806   9289  10999   -215   -874     -2       C
ATOM   2066  NZ  LYS A 288      -1.882  51.336  29.734  1.00 89.74           N
ANISOU 2066  NZ  LYS A 288    13308   9497  11293   -256   -924    -85       N
ATOM   2067  N   ASN A 289      -6.730  45.437  30.717  1.00 50.39           N
ANISOU 2067  N   ASN A 289     7578   5378   6189    382   -861    -98       N
ATOM   2068  CA  ASN A 289      -7.966  44.806  30.272  1.00 53.26           C
ANISOU 2068  CA  ASN A 289     7867   5855   6514    509   -821   -102       C
ATOM   2069  C   ASN A 289      -8.565  43.829  31.270  1.00 55.04           C
ANISOU 2069  C   ASN A 289     7987   6227   6700    521   -823   -130       C
ATOM   2070  O   ASN A 289      -9.742  43.485  31.132  1.00 54.98           O
ANISOU 2070  O   ASN A 289     7928   6322   6638    624   -792   -156       O
ATOM   2071  CB  ASN A 289      -7.735  44.093  28.932  1.00 52.78           C
ANISOU 2071  CB  ASN A 289     7717   5822   6513    489   -781    -32       C
ATOM   2072  CG  ASN A 289      -7.221  45.045  27.864  1.00 59.59           C
ANISOU 2072  CG  ASN A 289     8689   6552   7400    477   -769      5       C
ATOM   2073  OD1 ASN A 289      -6.054  45.002  27.478  1.00 58.32           O
ANISOU 2073  OD1 ASN A 289     8514   6339   7306    353   -767     52       O
ATOM   2074  ND2 ASN A 289      -8.086  45.932  27.410  1.00 60.27           N
ANISOU 2074  ND2 ASN A 289     8888   6587   7425    608   -761    -16       N
ATOM   2075  N   GLY A 290      -7.811  43.386  32.270  1.00 51.01           N
ANISOU 2075  N   GLY A 290     7440   5735   6205    418   -858   -125       N
ATOM   2076  CA  GLY A 290      -8.319  42.362  33.160  1.00 56.11           C
ANISOU 2076  CA  GLY A 290     7994   6515   6811    417   -854   -133       C
ATOM   2077  C   GLY A 290      -8.265  42.709  34.632  1.00 68.60           C
ANISOU 2077  C   GLY A 290     9626   8113   8324    397   -897   -186       C
ATOM   2078  O   GLY A 290      -8.348  41.819  35.488  1.00 71.31           O
ANISOU 2078  O   GLY A 290     9902   8556   8638    361   -903   -174       O
ATOM   2079  N   GLY A 291      -8.129  43.993  34.949  1.00 66.80           N
ANISOU 2079  N   GLY A 291     9530   7786   8066    418   -926   -244       N
ATOM   2080  CA  GLY A 291      -8.126  44.417  36.329  1.00 76.26           C
ANISOU 2080  CA  GLY A 291    10787   9000   9188    406   -967   -309       C
ATOM   2081  C   GLY A 291      -9.527  44.439  36.911  1.00 88.90           C
ANISOU 2081  C   GLY A 291    12387  10711  10681    530   -935   -376       C
ATOM   2082  O   GLY A 291     -10.514  44.674  36.201  1.00 92.34           O
ANISOU 2082  O   GLY A 291    12823  11168  11095    650   -892   -397       O
ATOM   2083  N   PRO A 292      -9.644  44.178  38.228  1.00 89.60           N
ANISOU 2083  N   PRO A 292    12465  10888  10692    505   -955   -412       N
ATOM   2084  CA  PRO A 292     -10.896  44.260  39.000  1.00 92.34           C
ANISOU 2084  CA  PRO A 292    12809  11357  10917    609   -923   -488       C
ATOM   2085  C   PRO A 292     -11.729  45.526  38.737  1.00 93.68           C
ANISOU 2085  C   PRO A 292    13087  11472  11036    763   -909   -581       C
ATOM   2086  O   PRO A 292     -11.184  46.603  38.475  1.00 91.32           O
ANISOU 2086  O   PRO A 292    12921  11008  10767    770   -943   -608       O
ATOM   2087  CB  PRO A 292     -10.403  44.236  40.451  1.00 87.56           C
ANISOU 2087  CB  PRO A 292    12234  10791  10244    534   -970   -518       C
ATOM   2088  CG  PRO A 292      -9.177  43.390  40.397  1.00 82.58           C
ANISOU 2088  CG  PRO A 292    11541  10138   9697    394  -1009   -422       C
ATOM   2089  CD  PRO A 292      -8.537  43.639  39.041  1.00 82.89           C
ANISOU 2089  CD  PRO A 292    11585  10049   9859    372  -1008   -373       C
TER
HETATM 2090  O   HOH S   1     -11.636  13.391   0.702  1.00 57.66           O
ANISOU 2090  O   HOH S   1     7375   7404   7130   -258    269  -1918       O
HETATM 2091  O   HOH S   2      -2.921  18.313  42.537  1.00 50.87           O
ANISOU 2091  O   HOH S   2     7825   5450   6055    151  -1124   1435       O
HETATM 2092  O   HOH S   3     -13.221  30.687  25.933  1.00 41.49           O
ANISOU 2092  O   HOH S   3     5285   5336   5143    184   -406    -41       O
HETATM 2093  O   HOH S   4       9.967  29.390  26.885  1.00 54.15           O
ANISOU 2093  O   HOH S   4     5943   6912   7721    306   -977    379       O
HETATM 2094  O   HOH S   5       0.957  47.711  15.429  1.00 50.00           O
ANISOU 2094  O   HOH S   5     7687   4972   6338   -435   -228    717       O
HETATM 2095  O   HOH S   6      -8.341  35.605  23.433  1.00 35.48           O
ANISOU 2095  O   HOH S   6     4757   4155   4569    382   -523    118       O
HETATM 2096  O   HOH S   7      -0.955  42.519  43.538  1.00 45.71           O
ANISOU 2096  O   HOH S   7     6706   5477   5186   -289  -1507   -266       O
HETATM 2097  O   HOH S   8       4.693  23.832  36.740  1.00 53.78           O
ANISOU 2097  O   HOH S   8     6959   6329   7147    637  -1414    883       O
HETATM 2098  O   HOH S   9     -12.807  26.623  19.887  1.00 42.73           O
ANISOU 2098  O   HOH S   9     5307   5454   5475     54   -259   -189       O
HETATM 2099  O   HOH S  10      10.867  30.879  24.196  1.00 50.31           O
ANISOU 2099  O   HOH S  10     5293   6549   7272    124   -787    309       O
HETATM 2100  O   HOH S  11     -12.413  25.985  24.705  1.00 47.80           O
ANISOU 2100  O   HOH S  11     6104   5935   6124    -89   -311    -15       O
HETATM 2101  O   HOH S  12     -11.693  34.837  21.518  1.00 47.43           O
ANISOU 2101  O   HOH S  12     6146   5959   5915    524   -451    -11       O
HETATM 2102  O   HOH S  13       0.845  46.413  26.772  1.00 55.18           O
ANISOU 2102  O   HOH S  13     8055   5720   7190   -466   -789    186       O
HETATM 2103  O   HOH S  14       1.411  47.383  38.129  1.00 51.77           O
ANISOU 2103  O   HOH S  14     7751   5549   6370   -653  -1369   -352       O
HETATM 2104  O   HOH S  15      -8.482   7.860  -4.589  1.00 63.61           O
ANISOU 2104  O   HOH S  15     8605   7719   7846    -22    558  -2816       O
HETATM 2105  O   HOH S  16      -1.946  28.154  18.797  1.00 51.91           O
ANISOU 2105  O   HOH S  16     6433   6143   7146    291   -337    148       O
HETATM 2106  O   HOH S  17      -6.431  39.551  27.076  1.00 51.00           O
ANISOU 2106  O   HOH S  17     7031   5849   6497    309   -692    122       O
HETATM 2107  O   HOH S  18      -5.336  42.058  16.360  1.00 52.28           O
ANISOU 2107  O   HOH S  18     7404   5892   6568    423   -383    403       O
HETATM 2108  O   HOH S  19       2.212  22.898  28.819  1.00 60.42           O
ANISOU 2108  O   HOH S  19     7713   6885   8357    549   -858    559       O
HETATM 2109  O   HOH S  20     -11.056  21.014  11.726  1.00 56.02           O
ANISOU 2109  O   HOH S  20     6988   7021   7277    -30    -38   -636       O
HETATM 2110  O   HOH S  21     -10.448  21.146  26.112  1.00 49.59           O
ANISOU 2110  O   HOH S  21     6640   5663   6539   -285   -290    153       O
HETATM 2111  O   HOH S  22       4.207  36.287  43.426  1.00 51.22           O
ANISOU 2111  O   HOH S  22     6734   6589   6139   -239  -1780    234       O
HETATM 2112  O   HOH S  23       1.895  48.249  -0.778  1.00 51.00           O
ANISOU 2112  O   HOH S  23     8252   5846   5279   -446    644   1553       O
HETATM 2113  O   HOH S  24      -6.633  20.521  12.058  1.00 51.35           O
ANISOU 2113  O   HOH S  24     6471   6089   6950    208    -20   -481       O
HETATM 2114  O   HOH S  25      -2.806  46.105  25.177  1.00 55.59           O
ANISOU 2114  O   HOH S  25     8240   5775   7108      7   -708    206       O
HETATM 2115  O   HOH S  26     -12.097  37.394  27.789  1.00 53.51           O
ANISOU 2115  O   HOH S  26     7137   6655   6539    552   -586    -55       O
HETATM 2116  O   HOH S  27     -11.256  23.024  16.786  1.00 46.84           O
ANISOU 2116  O   HOH S  27     5876   5761   6162    -42   -157   -320       O
HETATM 2117  O   HOH S  28       4.198  43.902   2.426  1.00 51.82           O
ANISOU 2117  O   HOH S  28     7336   6368   5987   -585    602   1058       O
HETATM 2118  O   HOH S  29      -4.363  17.207  26.947  1.00 63.80           O
ANISOU 2118  O   HOH S  29     8785   6757   8698    151   -472    435       O
HETATM 2119  O   HOH S  30      -4.267  20.970  13.605  1.00 53.40           O
ANISOU 2119  O   HOH S  30     6719   6218   7354    332    -70   -313       O
HETATM 2120  O   HOH S  31     -11.529  27.215  43.174  1.00 51.08           O
ANISOU 2120  O   HOH S  31     7219   6664   5527   -366   -634    573       O
HETATM 2121  O   HOH S  32      -1.096  46.526  22.820  1.00 54.42           O
ANISOU 2121  O   HOH S  32     8093   5566   7020   -188   -607    333       O
HETATM 2122  O   HOH S  33      -2.393  41.160  45.327  1.00 66.81           O
ANISOU 2122  O   HOH S  33     9387   8348   7650   -179  -1492   -228       O
HETATM 2123  O   HOH S  34     -13.059  25.274  22.420  1.00 48.38           O
ANISOU 2123  O   HOH S  34     6103   6075   6205   -106   -255   -127       O
HETATM 2124  O   HOH S  35      11.605  31.861  21.343  1.00 55.90           O
ANISOU 2124  O   HOH S  35     5876   7374   7989    -18   -570    265       O
HETATM 2125  O   HOH S  36      10.429  34.438  20.476  1.00 55.70           O
ANISOU 2125  O   HOH S  36     6093   7200   7870   -298   -476    301       O
HETATM 2126  O   HOH S  37      -6.922   9.418   5.042  1.00 56.47           O
ANISOU 2126  O   HOH S  37     7833   5961   7662     62    333  -1663       O
HETATM 2127  O   HOH S  38       4.573  48.358   1.670  1.00 57.53           O
ANISOU 2127  O   HOH S  38     8820   6585   6453   -929    690   1453       O
HETATM 2128  O   HOH S  39      -9.317  37.766  27.296  1.00 50.51           O
ANISOU 2128  O   HOH S  39     6834   6036   6321    434   -631     51       O
HETATM 2129  O   HOH S  40       2.178  50.880   2.490  1.00 58.91           O
ANISOU 2129  O   HOH S  40     9657   6219   6506   -653    497   1602       O
HETATM 2130  O   HOH S  41      -4.120  17.374  24.221  1.00 67.17           O
ANISOU 2130  O   HOH S  41     9069   7241   9211    208   -391    258       O
HETATM 2131  O   HOH S  42      13.250  34.342  37.952  1.00 63.62           O
ANISOU 2131  O   HOH S  42     7052   8738   8382   -239  -1906    280       O
HETATM 2132  O   HOH S  43       7.922  43.839  33.934  1.00 54.58           O
ANISOU 2132  O   HOH S  43     7102   6429   7207  -1082  -1324    -21       O
HETATM 2133  O   HOH S  44      -3.494  28.792  13.924  1.00 50.96           O
ANISOU 2133  O   HOH S  44     6289   6229   6843    336   -156     15       O
HETATM 2134  O   HOH S  45      -5.270  40.824  18.868  1.00 43.71           O
ANISOU 2134  O   HOH S  45     6173   4847   5588    365   -453    315       O
HETATM 2135  O   HOH S  46      -6.481  44.382  16.084  1.00 58.69           O
ANISOU 2135  O   HOH S  46     8528   6536   7236    587   -420    448       O
HETATM 2136  O   HOH S  47       2.718  33.476  45.104  1.00 62.37           O
ANISOU 2136  O   HOH S  47     8277   8054   7365    -50  -1772    448       O
HETATM 2137  O   HOH S  48      -1.986  31.528  25.188  1.00 52.90           O
ANISOU 2137  O   HOH S  48     6732   6205   7164    164   -621    295       O
HETATM 2138  O   HOH S  49      -8.690  37.932  24.680  1.00 49.75           O
ANISOU 2138  O   HOH S  49     6725   5888   6290    454   -583     98       O
HETATM 2139  O   HOH S  50      -1.649  28.788  25.255  1.00 57.33           O
ANISOU 2139  O   HOH S  50     7254   6728   7800    216   -610    316       O
HETATM 2140  O   HOH S  51       4.404  24.862  39.331  1.00 64.37           O
ANISOU 2140  O   HOH S  51     8383   7806   8268    546  -1547    929       O
HETATM 2141  O   HOH S  52      -9.770  32.078  41.856  1.00 56.75           O
ANISOU 2141  O   HOH S  52     7808   7339   6417    -57   -822    273       O
HETATM 2142  O   HOH S  53       7.107  30.406  19.441  1.00 60.29           O
ANISOU 2142  O   HOH S  53     6896   7542   8469    182   -418    265       O
HETATM 2143  O   HOH S  54      -0.144  26.946   6.307  1.00 57.36           O
ANISOU 2143  O   HOH S  54     6855   7427   7511    464    226   -223       O
HETATM 2144  O   HOH S  55       4.760  40.907   2.371  1.00 60.11           O
ANISOU 2144  O   HOH S  55     7910   7748   7181   -455    625    821       O
HETATM 2145  O   HOH S  56     -13.644  35.181  32.897  1.00 57.42           O
ANISOU 2145  O   HOH S  56     7562   7436   6817    346   -562    -91       O
HETATM 2146  O   HOH S  57       5.438  40.340   0.278  1.00 64.02           O
ANISOU 2146  O   HOH S  57     8312   8486   7527   -476    787    820       O
HETATM 2147  O   HOH S  58       6.154  21.606  37.342  1.00 64.43           O
ANISOU 2147  O   HOH S  58     8357   7606   8517    917  -1537   1022       O
HETATM 2148  O   HOH S  59      -5.644  29.955  46.047  1.00 63.44           O
ANISOU 2148  O   HOH S  59     8859   8157   7089    -97  -1179    623       O
HETATM 2149  O   HOH S  60      -9.996  11.409  10.829  1.00 67.10           O
ANISOU 2149  O   HOH S  60     9136   7339   9021   -394    164  -1117       O
HETATM 2150  O   HOH S  61      -3.603  16.320 -11.044  1.00 62.35           O
ANISOU 2150  O   HOH S  61     7613   9255   6823    740    852  -2211       O
HETATM 2151  O   HOH S  62      -7.922  22.579  18.895  1.00 53.40           O
ANISOU 2151  O   HOH S  62     6831   6251   7206     66   -222   -108       O
HETATM 2152  O   HOH S  63       2.349  16.434   9.337  1.00 62.61           O
ANISOU 2152  O   HOH S  63     7739   7257   8791    981    162   -671       O
HETATM 2153  O   HOH S  64       0.833  33.467  46.239  1.00 64.14           O
ANISOU 2153  O   HOH S  64     8671   8291   7407    -55  -1697    442       O
HETATM 2154  O   HOH S  65     -15.644  27.096  19.342  1.00 36.87           O
ANISOU 2154  O   HOH S  65     4675   4797   4539   -105   -325   -188       O
HETATM 2155  O   HOH S  66      -1.602  47.336  27.027  1.00 59.61           O
ANISOU 2155  O   HOH S  66     8868   6155   7625   -187   -793    134       O
HETATM 2156  O   HOH S  67       3.996  24.379  29.969  1.00 62.01           O
ANISOU 2156  O   HOH S  67     7753   7264   8546    564   -994    586       O
HETATM 2157  O   HOH S  68      -6.970  42.442  23.177  1.00 55.73           O
ANISOU 2157  O   HOH S  68     7888   6264   7024    475   -609    180       O
HETATM 2158  O   HOH S  69      10.527  44.867  16.846  1.00 55.70           O
ANISOU 2158  O   HOH S  69     7069   6592   7503  -1514   -103    557       O
HETATM 2159  O   HOH S  70     -12.734  33.469  19.314  1.00 61.66           O
ANISOU 2159  O   HOH S  70     7821   7930   7678    527   -392    -82       O
HETATM 2160  O   HOH S  71     -12.889   6.940  -1.390  1.00 72.39           O
ANISOU 2160  O   HOH S  71     9825   8659   9023   -785    405  -2765       O
HETATM 2161  O   HOH S  72      -0.647  48.762   8.913  1.00 58.89           O
ANISOU 2161  O   HOH S  72     9212   6153   7009   -150     22   1069       O
HETATM 2162  O   HOH S  73       4.726  42.641  -1.289  1.00 70.39           O
ANISOU 2162  O   HOH S  73     9540   9160   8046   -546    848   1067       O
HETATM 2163  O   HOH S  74     -15.766  36.950  25.420  1.00 64.26           O
ANISOU 2163  O   HOH S  74     8276   8420   7720    766   -499   -203       O
HETATM 2164  O   HOH S  75       3.280  26.585   0.981  1.00 61.62           O
ANISOU 2164  O   HOH S  75     7142   8463   7806    532    606   -377       O
TER
END



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