data_nohd
# 
_entry.id   nohd 
# 
_audit_conform.dict_name      mmcif_pdbx.dic 
_audit_conform.dict_version   5.362 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
P 
# 
loop_
_atom_site.id 
_atom_site.group_PDB 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
1    ATOM   N N   .  MET A 1 1   ?  -43.367 51.259  -40.406 1.00 36.50 ?  1   MET A N   1 
2    ATOM   C CA  .  MET A 1 1   ?  -44.489 50.273  -40.469 1.00 36.50 ?  1   MET A CA  1 
3    ATOM   C C   .  MET A 1 1   ?  -44.475 49.331  -39.269 1.00 36.50 ?  1   MET A C   1 
4    ATOM   C CB  .  MET A 1 1   ?  -44.388 49.442  -41.752 1.00 36.50 ?  1   MET A CB  1 
5    ATOM   O O   .  MET A 1 1   ?  -43.468 48.674  -39.013 1.00 36.50 ?  1   MET A O   1 
6    ATOM   C CG  .  MET A 1 1   ?  -45.484 49.748  -42.762 1.00 36.50 ?  1   MET A CG  1 
7    ATOM   S SD  .  MET A 1 1   ?  -45.293 48.82   -44.299 1.00 36.50 ?  1   MET A SD  1 
8    ATOM   C CE  .  MET A 1 1   ?  -45.943 47.198  -43.876 1.00 36.50 ?  1   MET A CE  1 
9    ATOM   N N   .  LYS A 1 2   ?  -45.589 49.284  -38.543 1.00 35.81 ?  2   LYS A N   1 
10   ATOM   C CA  .  LYS A 1 2   ?  -45.763 48.399  -37.39  1.00 35.81 ?  2   LYS A CA  1 
11   ATOM   C C   .  LYS A 1 2   ?  -44.685 48.513  -36.314 1.00 35.81 ?  2   LYS A C   1 
12   ATOM   C CB  .  LYS A 1 2   ?  -45.847 46.933  -37.828 1.00 35.81 ?  2   LYS A CB  1 
13   ATOM   O O   .  LYS A 1 2   ?  -43.68  47.805  -36.338 1.00 35.81 ?  2   LYS A O   1 
14   ATOM   C CG  .  LYS A 1 2   ?  -47.119 46.58   -38.585 1.00 35.81 ?  2   LYS A CG  1 
15   ATOM   C CD  .  LYS A 1 2   ?  -47.243 45.075  -38.769 1.00 35.81 ?  2   LYS A CD  1 
16   ATOM   C CE  .  LYS A 1 2   ?  -48.516 44.721  -39.52  1.00 35.81 ?  2   LYS A CE  1 
17   ATOM   N NZ  .  LYS A 1 2   ?  -48.629 43.23   -39.63  1.00 35.81 ?  2   LYS A NZ  1 
18   ATOM   N N   .  LYS A 1 3   ?  -44.941 49.359  -35.323 1.00 39.53 ?  3   LYS A N   1 
19   ATOM   C CA  .  LYS A 1 3   ?  -44.266 49.25   -34.031 1.00 39.53 ?  3   LYS A CA  1 
20   ATOM   C C   .  LYS A 1 3   ?  -44.606 47.879  -33.455 1.00 39.53 ?  3   LYS A C   1 
21   ATOM   C CB  .  LYS A 1 3   ?  -44.769 50.315  -33.052 1.00 39.53 ?  3   LYS A CB  1 
22   ATOM   O O   .  LYS A 1 3   ?  -45.639 47.307  -33.8   1.00 39.53 ?  3   LYS A O   1 
23   ATOM   C CG  .  LYS A 1 3   ?  -44.483 51.756  -33.446 1.00 39.53 ?  3   LYS A CG  1 
24   ATOM   C CD  .  LYS A 1 3   ?  -45.008 52.696  -32.369 1.00 39.53 ?  3   LYS A CD  1 
25   ATOM   C CE  .  LYS A 1 3   ?  -44.813 54.154  -32.749 1.00 39.53 ?  3   LYS A CE  1 
26   ATOM   N NZ  .  LYS A 1 3   ?  -45.345 55.014  -31.642 1.00 39.53 ?  3   LYS A NZ  1 
27   ATOM   N N   .  ASN A 1 4   ?  -43.774 47.387  -32.545 1.00 31.73 ?  4   ASN A N   1 
28   ATOM   C CA  .  ASN A 1 4   ?  -44.251 46.94   -31.24  1.00 31.73 ?  4   ASN A CA  1 
29   ATOM   C C   .  ASN A 1 4   ?  -43.132 46.819  -30.21  1.00 31.73 ?  4   ASN A C   1 
30   ATOM   C CB  .  ASN A 1 4   ?  -44.975 45.596  -31.363 1.00 31.73 ?  4   ASN A CB  1 
31   ATOM   O O   .  ASN A 1 4   ?  -41.968 46.608  -30.551 1.00 31.73 ?  4   ASN A O   1 
32   ATOM   C CG  .  ASN A 1 4   ?  -46.477 45.755  -31.444 1.00 31.73 ?  4   ASN A CG  1 
33   ATOM   N ND2 .  ASN A 1 4   ?  -47.129 44.878  -32.19  1.00 31.73 ?  4   ASN A ND2 1 
34   ATOM   O OD1 .  ASN A 1 4   ?  -47.048 46.655  -30.831 1.00 31.73 ?  4   ASN A OD1 1 
35   ATOM   N N   .  LYS A 1 5   ?  -43.519 46.919  -28.942 1.00 40.91 ?  5   LYS A N   1 
36   ATOM   C CA  .  LYS A 1 5   ?  -42.699 46.479  -27.817 1.00 40.91 ?  5   LYS A CA  1 
37   ATOM   C C   .  LYS A 1 5   ?  -43.429 45.289  -27.207 1.00 40.91 ?  5   LYS A C   1 
38   ATOM   C CB  .  LYS A 1 5   ?  -42.586 47.554  -26.731 1.00 40.91 ?  5   LYS A CB  1 
39   ATOM   O O   .  LYS A 1 5   ?  -44.643 45.165  -27.364 1.00 40.91 ?  5   LYS A O   1 
40   ATOM   C CG  .  LYS A 1 5   ?  -41.817 48.814  -27.1   1.00 40.91 ?  5   LYS A CG  1 
41   ATOM   C CD  .  LYS A 1 5   ?  -41.724 49.722  -25.879 1.00 40.91 ?  5   LYS A CD  1 
42   ATOM   C CE  .  LYS A 1 5   ?  -40.991 51.02   -26.176 1.00 40.91 ?  5   LYS A CE  1 
43   ATOM   N NZ  .  LYS A 1 5   ?  -40.949 51.844  -24.923 1.00 40.91 ?  5   LYS A NZ  1 
44   ATOM   N N   .  PHE A 1 6   ?  -42.709 44.458  -26.463 1.00 30.42 ?  6   PHE A N   1 
45   ATOM   C CA  .  PHE A 1 6   ?  -43.346 43.516  -25.549 1.00 30.42 ?  6   PHE A CA  1 
46   ATOM   C C   .  PHE A 1 6   ?  -42.467 43.351  -24.313 1.00 30.42 ?  6   PHE A C   1 
47   ATOM   C CB  .  PHE A 1 6   ?  -43.627 42.174  -26.229 1.00 30.42 ?  6   PHE A CB  1 
48   ATOM   O O   .  PHE A 1 6   ?  -41.269 43.63   -24.355 1.00 30.42 ?  6   PHE A O   1 
49   ATOM   C CG  .  PHE A 1 6   ?  -45.06  41.737  -26.096 1.00 30.42 ?  6   PHE A CG  1 
50   ATOM   C CD1 .  PHE A 1 6   ?  -45.462 40.947  -25.024 1.00 30.42 ?  6   PHE A CD1 1 
51   ATOM   C CD2 .  PHE A 1 6   ?  -46.014 42.162  -27.014 1.00 30.42 ?  6   PHE A CD2 1 
52   ATOM   C CE1 .  PHE A 1 6   ?  -46.805 40.622  -24.844 1.00 30.42 ?  6   PHE A CE1 1 
53   ATOM   C CE2 .  PHE A 1 6   ?  -47.359 41.844  -26.844 1.00 30.42 ?  6   PHE A CE2 1 
54   ATOM   C CZ  .  PHE A 1 6   ?  -47.757 41.081  -25.75  1.00 30.42 ?  6   PHE A CZ  1 
55   ATOM   N N   .  TYR A 1 7   ?  -43.08  42.942  -23.208 1.00 31.92 ?  7   TYR A N   1 
56   ATOM   C CA  .  TYR A 1 7   ?  -42.445 43.009  -21.896 1.00 31.92 ?  7   TYR A CA  1 
57   ATOM   C C   .  TYR A 1 7   ?  -42.021 41.642  -21.37  1.00 31.92 ?  7   TYR A C   1 
58   ATOM   C CB  .  TYR A 1 7   ?  -43.404 43.654  -20.891 1.00 31.92 ?  7   TYR A CB  1 
59   ATOM   O O   .  TYR A 1 7   ?  -42.632 40.618  -21.678 1.00 31.92 ?  7   TYR A O   1 
60   ATOM   C CG  .  TYR A 1 7   ?  -43.585 45.141  -21.108 1.00 31.92 ?  7   TYR A CG  1 
61   ATOM   C CD1 .  TYR A 1 7   ?  -42.769 46.057  -20.442 1.00 31.92 ?  7   TYR A CD1 1 
62   ATOM   C CD2 .  TYR A 1 7   ?  -44.558 45.631  -21.98  1.00 31.92 ?  7   TYR A CD2 1 
63   ATOM   C CE1 .  TYR A 1 7   ?  -42.914 47.427  -20.648 1.00 31.92 ?  7   TYR A CE1 1 
64   ATOM   C CE2 .  TYR A 1 7   ?  -44.699 47      -22.198 1.00 31.92 ?  7   TYR A CE2 1 
65   ATOM   O OH  .  TYR A 1 7   ?  -44.031 49.245  -21.715 1.00 31.92 ?  7   TYR A OH  1 
66   ATOM   C CZ  .  TYR A 1 7   ?  -43.881 47.891  -21.523 1.00 31.92 ?  7   TYR A CZ  1 
67   ATOM   N N   .  LEU A 1 8   ?  -40.972 41.649  -20.554 1.00 30.92 ?  8   LEU A N   1 
68   ATOM   C CA  .  LEU A 1 8   ?  -40.499 40.441  -19.887 1.00 30.92 ?  8   LEU A CA  1 
69   ATOM   C C   .  LEU A 1 8   ?  -41.576 39.96   -18.919 1.00 30.92 ?  8   LEU A C   1 
70   ATOM   C CB  .  LEU A 1 8   ?  -39.22  40.72   -19.09  1.00 30.92 ?  8   LEU A CB  1 
71   ATOM   O O   .  LEU A 1 8   ?  -42.138 40.749  -18.16  1.00 30.92 ?  8   LEU A O   1 
72   ATOM   C CG  .  LEU A 1 8   ?  -37.869 40.812  -19.807 1.00 30.92 ?  8   LEU A CG  1 
73   ATOM   C CD1 .  LEU A 1 8   ?  -37.748 42.027  -20.719 1.00 30.92 ?  8   LEU A CD1 1 
74   ATOM   C CD2 .  LEU A 1 8   ?  -36.774 40.859  -18.748 1.00 30.92 ?  8   LEU A CD2 1 
75   ATOM   N N   .  PHE A 1 9   ?  -41.84  38.659  -18.936 1.00 28.33 ?  9   PHE A N   1 
76   ATOM   C CA  .  PHE A 1 9   ?  -42.756 38.045  -17.98  1.00 28.33 ?  9   PHE A CA  1 
77   ATOM   C C   .  PHE A 1 9   ?  -42.064 36.883  -17.275 1.00 28.33 ?  9   PHE A C   1 
78   ATOM   C CB  .  PHE A 1 9   ?  -44.02  37.554  -18.689 1.00 28.33 ?  9   PHE A CB  1 
79   ATOM   O O   .  PHE A 1 9   ?  -41.719 35.881  -17.902 1.00 28.33 ?  9   PHE A O   1 
80   ATOM   C CG  .  PHE A 1 9   ?  -45.251 38.329  -18.311 1.00 28.33 ?  9   PHE A CG  1 
81   ATOM   C CD1 .  PHE A 1 9   ?  -46.031 37.93   -17.231 1.00 28.33 ?  9   PHE A CD1 1 
82   ATOM   C CD2 .  PHE A 1 9   ?  -45.612 39.471  -19.02  1.00 28.33 ?  9   PHE A CD2 1 
83   ATOM   C CE1 .  PHE A 1 9   ?  -47.158 38.66   -16.859 1.00 28.33 ?  9   PHE A CE1 1 
84   ATOM   C CE2 .  PHE A 1 9   ?  -46.738 40.206  -18.657 1.00 28.33 ?  9   PHE A CE2 1 
85   ATOM   C CZ  .  PHE A 1 9   ?  -47.512 39.801  -17.573 1.00 28.33 ?  9   PHE A CZ  1 
86   ATOM   N N   .  LEU A 1 10  ?  -41.851 37.024  -15.972 1.00 32.47 ?  10  LEU A N   1 
87   ATOM   C CA  .  LEU A 1 10  ?  -41.252 35.957  -15.177 1.00 32.47 ?  10  LEU A CA  1 
88   ATOM   C C   .  LEU A 1 10  ?  -42.389 35.115  -14.607 1.00 32.47 ?  10  LEU A C   1 
89   ATOM   C CB  .  LEU A 1 10  ?  -40.38  36.514  -14.047 1.00 32.47 ?  10  LEU A CB  1 
90   ATOM   O O   .  LEU A 1 10  ?  -43.194 35.6    -13.813 1.00 32.47 ?  10  LEU A O   1 
91   ATOM   C CG  .  LEU A 1 10  ?  -39.089 37.249  -14.425 1.00 32.47 ?  10  LEU A CG  1 
92   ATOM   C CD1 .  LEU A 1 10  ?  -39.316 38.722  -14.749 1.00 32.47 ?  10  LEU A CD1 1 
93   ATOM   C CD2 .  LEU A 1 10  ?  -38.096 37.136  -13.274 1.00 32.47 ?  10  LEU A CD2 1 
94   ATOM   N N   .  GLY A 1 11  ?  -42.461 33.858  -15.033 1.00 27.95 ?  11  GLY A N   1 
95   ATOM   C CA  .  GLY A 1 11  ?  -43.543 32.98   -14.625 1.00 27.95 ?  11  GLY A CA  1 
96   ATOM   C C   .  GLY A 1 11  ?  -43.082 31.547  -14.451 1.00 27.95 ?  11  GLY A C   1 
97   ATOM   O O   .  GLY A 1 11  ?  -43.028 30.793  -15.421 1.00 27.95 ?  11  GLY A O   1 
98   ATOM   N N   .  ALA A 1 12  ?  -42.763 31.191  -13.21  1.00 26.72 ?  12  ALA A N   1 
99   ATOM   C CA  .  ALA A 1 12  ?  -42.28  29.861  -12.843 1.00 26.72 ?  12  ALA A CA  1 
100  ATOM   C C   .  ALA A 1 12  ?  -40.908 29.562  -13.454 1.00 26.72 ?  12  ALA A C   1 
101  ATOM   C CB  .  ALA A 1 12  ?  -43.31  28.802  -13.236 1.00 26.72 ?  12  ALA A CB  1 
102  ATOM   O O   .  ALA A 1 12  ?  -40.468 30.29   -14.342 1.00 26.72 ?  12  ALA A O   1 
103  ATOM   N N   .  ALA A 1 13  ?  -40.17  28.547  -13.009 1.00 26.86 ?  13  ALA A N   1 
104  ATOM   C CA  .  ALA A 1 13  ?  -40.417 27.732  -11.821 1.00 26.86 ?  13  ALA A CA  1 
105  ATOM   C C   .  ALA A 1 13  ?  -39.162 27.766  -10.954 1.00 26.86 ?  13  ALA A C   1 
106  ATOM   C CB  .  ALA A 1 13  ?  -40.727 26.295  -12.227 1.00 26.86 ?  13  ALA A CB  1 
107  ATOM   O O   .  ALA A 1 13  ?  -38.056 27.888  -11.481 1.00 26.86 ?  13  ALA A O   1 
108  ATOM   N N   .  PRO A 1 14  ?  -39.307 27.67   -9.622  1.00 27.89 ?  14  PRO A N   1 
109  ATOM   C CA  .  PRO A 1 14  ?  -38.037 27.589  -8.893  1.00 27.89 ?  14  PRO A CA  1 
110  ATOM   C C   .  PRO A 1 14  ?  -37.33  26.27   -9.187  1.00 27.89 ?  14  PRO A C   1 
111  ATOM   C CB  .  PRO A 1 14  ?  -38.468 27.685  -7.428  1.00 27.89 ?  14  PRO A CB  1 
112  ATOM   O O   .  PRO A 1 14  ?  -37.957 25.211  -9.235  1.00 27.89 ?  14  PRO A O   1 
113  ATOM   C CG  .  PRO A 1 14  ?  -39.844 27.11   -7.42   1.00 27.89 ?  14  PRO A CG  1 
114  ATOM   C CD  .  PRO A 1 14  ?  -40.461 27.575  -8.711  1.00 27.89 ?  14  PRO A CD  1 
115  ATOM   N N   .  VAL A 1 15  ?  -36.02  26.332  -9.396  1.00 29.30 ?  15  VAL A N   1 
116  ATOM   C CA  .  VAL A 1 15  ?  -35.242 25.124  -9.656  1.00 29.30 ?  15  VAL A CA  1 
117  ATOM   C C   .  VAL A 1 15  ?  -34.882 24.535  -8.299  1.00 29.30 ?  15  VAL A C   1 
118  ATOM   C CB  .  VAL A 1 15  ?  -33.958 25.384  -10.475 1.00 29.30 ?  15  VAL A CB  1 
119  ATOM   O O   .  VAL A 1 15  ?  -33.984 25.025  -7.615  1.00 29.30 ?  15  VAL A O   1 
120  ATOM   C CG1 .  VAL A 1 15  ?  -33.193 24.083  -10.702 1.00 29.30 ?  15  VAL A CG1 1 
121  ATOM   C CG2 .  VAL A 1 15  ?  -34.303 26.02   -11.82  1.00 29.30 ?  15  VAL A CG2 1 
122  ATOM   N N   .  LEU A 1 16  ?  -35.607 23.496  -7.901  1.00 26.48 ?  16  LEU A N   1 
123  ATOM   C CA  .  LEU A 1 16  ?  -35.281 22.789  -6.669  1.00 26.48 ?  16  LEU A CA  1 
124  ATOM   C C   .  LEU A 1 16  ?  -33.942 22.096  -6.891  1.00 26.48 ?  16  LEU A C   1 
125  ATOM   C CB  .  LEU A 1 16  ?  -36.357 21.762  -6.303  1.00 26.48 ?  16  LEU A CB  1 
126  ATOM   O O   .  LEU A 1 16  ?  -33.82  21.193  -7.719  1.00 26.48 ?  16  LEU A O   1 
127  ATOM   C CG  .  LEU A 1 16  ?  -37.546 22.261  -5.475  1.00 26.48 ?  16  LEU A CG  1 
128  ATOM   C CD1 .  LEU A 1 16  ?  -38.623 21.186  -5.432  1.00 26.48 ?  16  LEU A CD1 1 
129  ATOM   C CD2 .  LEU A 1 16  ?  -37.121 22.617  -4.054  1.00 26.48 ?  16  LEU A CD2 1 
130  ATOM   N N   .  SER A 1 17  ?  -32.936 22.544  -6.148  1.00 25.14 ?  17  SER A N   1 
131  ATOM   C CA  .  SER A 1 17  ?  -31.601 21.965  -6.225  1.00 25.14 ?  17  SER A CA  1 
132  ATOM   C C   .  SER A 1 17  ?  -31.553 20.74   -5.319  1.00 25.14 ?  17  SER A C   1 
133  ATOM   C CB  .  SER A 1 17  ?  -30.54  22.996  -5.83   1.00 25.14 ?  17  SER A CB  1 
134  ATOM   O O   .  SER A 1 17  ?  -30.909 20.737  -4.27   1.00 25.14 ?  17  SER A O   1 
135  ATOM   O OG  .  SER A 1 17  ?  -30.873 23.639  -4.611  1.00 25.14 ?  17  SER A OG  1 
136  ATOM   N N   .  VAL A 1 18  ?  -32.245 19.691  -5.75   1.00 25.16 ?  18  VAL A N   1 
137  ATOM   C CA  .  VAL A 1 18  ?  -32.179 18.402  -5.067  1.00 25.16 ?  18  VAL A CA  1 
138  ATOM   C C   .  VAL A 1 18  ?  -30.708 18.01   -5.139  1.00 25.16 ?  18  VAL A C   1 
139  ATOM   C CB  .  VAL A 1 18  ?  -33.048 17.318  -5.743  1.00 25.16 ?  18  VAL A CB  1 
140  ATOM   O O   .  VAL A 1 18  ?  -30.13  18.002  -6.227  1.00 25.16 ?  18  VAL A O   1 
141  ATOM   C CG1 .  VAL A 1 18  ?  -32.878 15.971  -5.045  1.00 25.16 ?  18  VAL A CG1 1 
142  ATOM   C CG2 .  VAL A 1 18  ?  -34.52  17.727  -5.728  1.00 25.16 ?  18  VAL A CG2 1 
143  ATOM   N N   .  PRO A 1 19  ?  -30.069 17.731  -3.992  1.00 26.36 ?  19  PRO A N   1 
144  ATOM   C CA  .  PRO A 1 19  ?  -28.627 17.516  -4.142  1.00 26.36 ?  19  PRO A CA  1 
145  ATOM   C C   .  PRO A 1 19  ?  -28.323 16.241  -4.92   1.00 26.36 ?  19  PRO A C   1 
146  ATOM   C CB  .  PRO A 1 19  ?  -28.138 17.421  -2.695  1.00 26.36 ?  19  PRO A CB  1 
147  ATOM   O O   .  PRO A 1 19  ?  -29.047 15.25   -4.821  1.00 26.36 ?  19  PRO A O   1 
148  ATOM   C CG  .  PRO A 1 19  ?  -29.321 16.909  -1.948  1.00 26.36 ?  19  PRO A CG  1 
149  ATOM   C CD  .  PRO A 1 19  ?  -30.484 17.622  -2.582  1.00 26.36 ?  19  PRO A CD  1 
150  ATOM   N N   .  LEU A 1 20  ?  -27.251 16.276  -5.702  1.00 23.11 ?  20  LEU A N   1 
151  ATOM   C CA  .  LEU A 1 20  ?  -26.834 15.095  -6.447  1.00 23.11 ?  20  LEU A CA  1 
152  ATOM   C C   .  LEU A 1 20  ?  -26.163 14.143  -5.464  1.00 23.11 ?  20  LEU A C   1 
153  ATOM   C CB  .  LEU A 1 20  ?  -25.898 15.464  -7.604  1.00 23.11 ?  20  LEU A CB  1 
154  ATOM   O O   .  LEU A 1 20  ?  -24.957 14.211  -5.224  1.00 23.11 ?  20  LEU A O   1 
155  ATOM   C CG  .  LEU A 1 20  ?  -26.408 15.118  -9.006  1.00 23.11 ?  20  LEU A CG  1 
156  ATOM   C CD1 .  LEU A 1 20  ?  -27.586 15.995  -9.411  1.00 23.11 ?  20  LEU A CD1 1 
157  ATOM   C CD2 .  LEU A 1 20  ?  -25.276 15.28   -10.012 1.00 23.11 ?  20  LEU A CD2 1 
158  ATOM   N N   .  VAL A 1 21  ?  -26.964 13.256  -4.886  1.00 27.45 ?  21  VAL A N   1 
159  ATOM   C CA  .  VAL A 1 21  ?  -26.426 12.17   -4.074  1.00 27.45 ?  21  VAL A CA  1 
160  ATOM   C C   .  VAL A 1 21  ?  -25.718 11.29   -5.095  1.00 27.45 ?  21  VAL A C   1 
161  ATOM   C CB  .  VAL A 1 21  ?  -27.508 11.374  -3.312  1.00 27.45 ?  21  VAL A CB  1 
162  ATOM   O O   .  VAL A 1 21  ?  -26.343 10.775  -6.022  1.00 27.45 ?  21  VAL A O   1 
163  ATOM   C CG1 .  VAL A 1 21  ?  -26.882 10.202  -2.561  1.00 27.45 ?  21  VAL A CG1 1 
164  ATOM   C CG2 .  VAL A 1 21  ?  -28.247 12.283  -2.332  1.00 27.45 ?  21  VAL A CG2 1 
165  ATOM   N N   .  ALA A 1 22  ?  -24.402 11.178  -4.963  1.00 27.48 ?  22  ALA A N   1 
166  ATOM   C CA  .  ALA A 1 22  ?  -23.605 10.504  -5.98   1.00 27.48 ?  22  ALA A CA  1 
167  ATOM   C C   .  ALA A 1 22  ?  -24.092 9.067   -6.137  1.00 27.48 ?  22  ALA A C   1 
168  ATOM   C CB  .  ALA A 1 22  ?  -22.13  10.531  -5.601  1.00 27.48 ?  22  ALA A CB  1 
169  ATOM   O O   .  ALA A 1 22  ?  -24.43  8.406   -5.155  1.00 27.48 ?  22  ALA A O   1 
170  ATOM   N N   .  ALA A 1 23  ?  -24.114 8.587   -7.376  1.00 26.47 ?  23  ALA A N   1 
171  ATOM   C CA  .  ALA A 1 23  ?  -24.427 7.19    -7.653  1.00 26.47 ?  23  ALA A CA  1 
172  ATOM   C C   .  ALA A 1 23  ?  -23.201 6.357   -7.29   1.00 26.47 ?  23  ALA A C   1 
173  ATOM   C CB  .  ALA A 1 23  ?  -24.802 7.008   -9.119  1.00 26.47 ?  23  ALA A CB  1 
174  ATOM   O O   .  ALA A 1 23  ?  -22.485 5.854   -8.156  1.00 26.47 ?  23  ALA A O   1 
175  ATOM   N N   .  SER A 1 24  ?  -22.943 6.256   -5.99   1.00 27.78 ?  24  SER A N   1 
176  ATOM   C CA  .  SER A 1 24  ?  -21.776 5.544   -5.483  1.00 27.78 ?  24  SER A CA  1 
177  ATOM   C C   .  SER A 1 24  ?  -21.8   4.117   -6.017  1.00 27.78 ?  24  SER A C   1 
178  ATOM   C CB  .  SER A 1 24  ?  -21.775 5.526   -3.953  1.00 27.78 ?  24  SER A CB  1 
179  ATOM   O O   .  SER A 1 24  ?  -22.812 3.423   -5.921  1.00 27.78 ?  24  SER A O   1 
180  ATOM   O OG  .  SER A 1 24  ?  -20.63  4.851   -3.462  1.00 27.78 ?  24  SER A OG  1 
181  ATOM   N N   .  CYS A 1 25  ?  -20.683 3.688   -6.592  1.00 28.86 ?  25  CYS A N   1 
182  ATOM   C CA  .  CYS A 1 25  ?  -20.588 2.336   -7.128  1.00 28.86 ?  25  CYS A CA  1 
183  ATOM   C C   .  CYS A 1 25  ?  -20.448 1.356   -5.967  1.00 28.86 ?  25  CYS A C   1 
184  ATOM   C CB  .  CYS A 1 25  ?  -19.387 2.244   -8.071  1.00 28.86 ?  25  CYS A CB  1 
185  ATOM   O O   .  CYS A 1 25  ?  -19.375 1.24    -5.376  1.00 28.86 ?  25  CYS A O   1 
186  ATOM   S SG  .  CYS A 1 25  ?  -19.533 3.36    -9.489  1.00 28.86 ?  25  CYS A SG  1 
187  ATOM   N N   .  GLY A 1 26  ?  -21.537 0.666   -5.644  1.00 38.03 ?  26  GLY A N   1 
188  ATOM   C CA  .  GLY A 1 26  ?  -21.499 -0.34   -4.598  1.00 38.03 ?  26  GLY A CA  1 
189  ATOM   C C   .  GLY A 1 26  ?  -20.411 -1.345  -4.922  1.00 38.03 ?  26  GLY A C   1 
190  ATOM   O O   .  GLY A 1 26  ?  -20.097 -1.561  -6.092  1.00 38.03 ?  26  GLY A O   1 
191  ATOM   N N   .  ASP A 1 27  ?  -19.804 -1.931  -3.896  1.00 52.94 ?  27  ASP A N   1 
192  ATOM   C CA  .  ASP A 1 27  ?  -18.601 -2.731  -4.094  1.00 52.94 ?  27  ASP A CA  1 
193  ATOM   C C   .  ASP A 1 27  ?  -18.861 -3.954  -4.97   1.00 52.94 ?  27  ASP A C   1 
194  ATOM   C CB  .  ASP A 1 27  ?  -18.017 -3.161  -2.749  1.00 52.94 ?  27  ASP A CB  1 
195  ATOM   O O   .  ASP A 1 27  ?  -19.475 -4.935  -4.55   1.00 52.94 ?  27  ASP A O   1 
196  ATOM   C CG  .  ASP A 1 27  ?  -17.382 -2.011  -1.993  1.00 52.94 ?  27  ASP A CG  1 
197  ATOM   O OD1 .  ASP A 1 27  ?  -16.43  -1.403  -2.528  1.00 52.94 ?  27  ASP A OD1 1 
198  ATOM   O OD2 .  ASP A 1 27  ?  -17.821 -1.72   -0.861  1.00 52.94 ?  27  ASP A OD2 1 
199  ATOM   N N   .  LYS A 1 28  ?  -18.386 -3.87   -6.209  1.00 54.56 ?  28  LYS A N   1 
200  ATOM   C CA  .  LYS A 1 28  ?  -18.585 -4.905  -7.221  1.00 54.56 ?  28  LYS A CA  1 
201  ATOM   C C   .  LYS A 1 28  ?  -17.668 -6.108  -7.027  1.00 54.56 ?  28  LYS A C   1 
202  ATOM   C CB  .  LYS A 1 28  ?  -18.333 -4.309  -8.61   1.00 54.56 ?  28  LYS A CB  1 
203  ATOM   O O   .  LYS A 1 28  ?  -17.744 -7.086  -7.77   1.00 54.56 ?  28  LYS A O   1 
204  ATOM   C CG  .  LYS A 1 28  ?  -19.194 -3.094  -8.935  1.00 54.56 ?  28  LYS A CG  1 
205  ATOM   C CD  .  LYS A 1 28  ?  -18.898 -2.529  -10.316 1.00 54.56 ?  28  LYS A CD  1 
206  ATOM   C CE  .  LYS A 1 28  ?  -19.653 -1.225  -10.524 1.00 54.56 ?  28  LYS A CE  1 
207  ATOM   N NZ  .  LYS A 1 28  ?  -19.288 -0.619  -11.847 1.00 54.56 ?  28  LYS A NZ  1 
208  ATOM   N N   .  TYR A 1 29  ?  -16.781 -6.004  -6.045  1.00 55.84 ?  29  TYR A N   1 
209  ATOM   C CA  .  TYR A 1 29  ?  -15.689 -6.957  -5.869  1.00 55.84 ?  29  TYR A CA  1 
210  ATOM   C C   .  TYR A 1 29  ?  -15.993 -8.083  -4.886  1.00 55.84 ?  29  TYR A C   1 
211  ATOM   C CB  .  TYR A 1 29  ?  -14.434 -6.215  -5.4    1.00 55.84 ?  29  TYR A CB  1 
212  ATOM   O O   .  TYR A 1 29  ?  -15.272 -9.079  -4.858  1.00 55.84 ?  29  TYR A O   1 
213  ATOM   C CG  .  TYR A 1 29  ?  -13.998 -5.105  -6.333  1.00 55.84 ?  29  TYR A CG  1 
214  ATOM   C CD1 .  TYR A 1 29  ?  -13.205 -5.378  -7.448  1.00 55.84 ?  29  TYR A CD1 1 
215  ATOM   C CD2 .  TYR A 1 29  ?  -14.39  -3.784  -6.105  1.00 55.84 ?  29  TYR A CD2 1 
216  ATOM   C CE1 .  TYR A 1 29  ?  -12.836 -4.363  -8.33   1.00 55.84 ?  29  TYR A CE1 1 
217  ATOM   C CE2 .  TYR A 1 29  ?  -14.032 -2.769  -6.99   1.00 55.84 ?  29  TYR A CE2 1 
218  ATOM   O OH  .  TYR A 1 29  ?  -12.928 -2.064  -8.986  1.00 55.84 ?  29  TYR A OH  1 
219  ATOM   C CZ  .  TYR A 1 29  ?  -13.263 -3.065  -8.103  1.00 55.84 ?  29  TYR A CZ  1 
220  ATOM   N N   .  PHE A 1 30  ?  -17.036 -7.929  -4.076  1.00 69.88 ?  30  PHE A N   1 
221  ATOM   C CA  .  PHE A 1 30  ?  -17.366 -8.913  -3.048  1.00 69.88 ?  30  PHE A CA  1 
222  ATOM   C C   .  PHE A 1 30  ?  -18.543 -9.794  -3.455  1.00 69.88 ?  30  PHE A C   1 
223  ATOM   C CB  .  PHE A 1 30  ?  -17.709 -8.223  -1.725  1.00 69.88 ?  30  PHE A CB  1 
224  ATOM   O O   .  PHE A 1 30  ?  -19.703 -9.402  -3.325  1.00 69.88 ?  30  PHE A O   1 
225  ATOM   C CG  .  PHE A 1 30  ?  -16.608 -7.349  -1.193  1.00 69.88 ?  30  PHE A CG  1 
226  ATOM   C CD1 .  PHE A 1 30  ?  -15.413 -7.898  -0.74   1.00 69.88 ?  30  PHE A CD1 1 
227  ATOM   C CD2 .  PHE A 1 30  ?  -16.778 -5.972  -1.139  1.00 69.88 ?  30  PHE A CD2 1 
228  ATOM   C CE1 .  PHE A 1 30  ?  -14.395 -7.08   -0.256  1.00 69.88 ?  30  PHE A CE1 1 
229  ATOM   C CE2 .  PHE A 1 30  ?  -15.753 -5.143  -0.696  1.00 69.88 ?  30  PHE A CE2 1 
230  ATOM   C CZ  .  PHE A 1 30  ?  -14.56  -5.698  -0.251  1.00 69.88 ?  30  PHE A CZ  1 
231  ATOM   N N   .  LYS A 1 31  ?  -18.235 -10.996 -3.929  1.00 78.12 ?  31  LYS A N   1 
232  ATOM   C CA  .  LYS A 1 31  ?  -19.244 -12.011 -4.225  1.00 78.12 ?  31  LYS A CA  1 
233  ATOM   C C   .  LYS A 1 31  ?  -19.002 -13.199 -3.302  1.00 78.12 ?  31  LYS A C   1 
234  ATOM   C CB  .  LYS A 1 31  ?  -19.141 -12.443 -5.691  1.00 78.12 ?  31  LYS A CB  1 
235  ATOM   O O   .  LYS A 1 31  ?  -17.862 -13.463 -2.923  1.00 78.12 ?  31  LYS A O   1 
236  ATOM   C CG  .  LYS A 1 31  ?  -19.433 -11.32  -6.678  1.00 78.12 ?  31  LYS A CG  1 
237  ATOM   C CD  .  LYS A 1 31  ?  -19.316 -11.791 -8.121  1.00 78.12 ?  31  LYS A CD  1 
238  ATOM   C CE  .  LYS A 1 31  ?  -19.52  -10.632 -9.084  1.00 78.12 ?  31  LYS A CE  1 
239  ATOM   N NZ  .  LYS A 1 31  ?  -19.361 -11.116 -10.496 1.00 78.12 ?  31  LYS A NZ  1 
240  ATOM   N N   .  GLU A 1 32  ?  -20.063 -13.899 -2.917  1.00 84.94 ?  32  GLU A N   1 
241  ATOM   C CA  .  GLU A 1 32  ?  -19.928 -15.051 -2.03   1.00 84.94 ?  32  GLU A CA  1 
242  ATOM   C C   .  GLU A 1 32  ?  -19.199 -16.19  -2.739  1.00 84.94 ?  32  GLU A C   1 
243  ATOM   C CB  .  GLU A 1 32  ?  -21.297 -15.548 -1.557  1.00 84.94 ?  32  GLU A CB  1 
244  ATOM   O O   .  GLU A 1 32  ?  -19.509 -16.533 -3.88   1.00 84.94 ?  32  GLU A O   1 
245  ATOM   C CG  .  GLU A 1 32  ?  -22.062 -14.547 -0.704  1.00 84.94 ?  32  GLU A CG  1 
246  ATOM   C CD  .  GLU A 1 32  ?  -23.339 -15.137 -0.134  1.00 84.94 ?  32  GLU A CD  1 
247  ATOM   O OE1 .  GLU A 1 32  ?  -23.522 -15.087 1.101   1.00 84.94 ?  32  GLU A OE1 1 
248  ATOM   O OE2 .  GLU A 1 32  ?  -24.164 -15.662 -0.912  1.00 84.94 ?  32  GLU A OE2 1 
249  ATOM   N N   .  THR A 1 33  ?  -18.217 -16.769 -2.056  1.00 87.56 ?  33  THR A N   1 
250  ATOM   C CA  .  THR A 1 33  ?  -17.431 -17.878 -2.589  1.00 87.56 ?  33  THR A CA  1 
251  ATOM   C C   .  THR A 1 33  ?  -16.992 -18.765 -1.427  1.00 87.56 ?  33  THR A C   1 
252  ATOM   C CB  .  THR A 1 33  ?  -16.206 -17.362 -3.374  1.00 87.56 ?  33  THR A CB  1 
253  ATOM   O O   .  THR A 1 33  ?  -17.062 -18.354 -0.27   1.00 87.56 ?  33  THR A O   1 
254  ATOM   C CG2 .  THR A 1 33  ?  -15.154 -16.739 -2.463  1.00 87.56 ?  33  THR A CG2 1 
255  ATOM   O OG1 .  THR A 1 33  ?  -15.608 -18.445 -4.097  1.00 87.56 ?  33  THR A OG1 1 
256  ATOM   N N   .  GLU A 1 34  ?  -16.547 -19.984 -1.712  1.00 89.25 ?  34  GLU A N   1 
257  ATOM   C CA  .  GLU A 1 34  ?  -16.056 -20.876 -0.666  1.00 89.25 ?  34  GLU A CA  1 
258  ATOM   C C   .  GLU A 1 34  ?  -14.628 -21.32  -0.973  1.00 89.25 ?  34  GLU A C   1 
259  ATOM   C CB  .  GLU A 1 34  ?  -16.988 -22.08  -0.509  1.00 89.25 ?  34  GLU A CB  1 
260  ATOM   O O   .  GLU A 1 34  ?  -14.342 -21.833 -2.054  1.00 89.25 ?  34  GLU A O   1 
261  ATOM   C CG  .  GLU A 1 34  ?  -16.679 -22.94  0.706   1.00 89.25 ?  34  GLU A CG  1 
262  ATOM   C CD  .  GLU A 1 34  ?  -17.662 -24.085 0.858   1.00 89.25 ?  34  GLU A CD  1 
263  ATOM   O OE1 .  GLU A 1 34  ?  -17.226 -25.256 0.84    1.00 89.25 ?  34  GLU A OE1 1 
264  ATOM   O OE2 .  GLU A 1 34  ?  -18.874 -23.817 1.006   1.00 89.25 ?  34  GLU A OE2 1 
265  ATOM   N N   .  VAL A 1 35  ?  -13.73  -21.091 -0.021  1.00 87.56 ?  35  VAL A N   1 
266  ATOM   C CA  .  VAL A 1 35  ?  -12.309 -21.379 -0.2    1.00 87.56 ?  35  VAL A CA  1 
267  ATOM   C C   .  VAL A 1 35  ?  -11.845 -22.336 0.892   1.00 87.56 ?  35  VAL A C   1 
268  ATOM   C CB  .  VAL A 1 35  ?  -11.447 -20.098 -0.145  1.00 87.56 ?  35  VAL A CB  1 
269  ATOM   O O   .  VAL A 1 35  ?  -11.865 -21.995 2.074   1.00 87.56 ?  35  VAL A O   1 
270  ATOM   C CG1 .  VAL A 1 35  ?  -9.969  -20.431 -0.332  1.00 87.56 ?  35  VAL A CG1 1 
271  ATOM   C CG2 .  VAL A 1 35  ?  -11.884 -19.108 -1.224  1.00 87.56 ?  35  VAL A CG2 1 
272  ATOM   N N   .  ASP A 1 36  ?  -11.454 -23.539 0.482   1.00 87.50 ?  36  ASP A N   1 
273  ATOM   C CA  .  ASP A 1 36  ?  -10.968 -24.575 1.392   1.00 87.50 ?  36  ASP A CA  1 
274  ATOM   C C   .  ASP A 1 36  ?  -11.982 -24.91  2.485   1.00 87.50 ?  36  ASP A C   1 
275  ATOM   C CB  .  ASP A 1 36  ?  -9.628  -24.168 2.012   1.00 87.50 ?  36  ASP A CB  1 
276  ATOM   O O   .  ASP A 1 36  ?  -11.621 -25.239 3.615   1.00 87.50 ?  36  ASP A O   1 
277  ATOM   C CG  .  ASP A 1 36  ?  -8.555  -23.923 0.968   1.00 87.50 ?  36  ASP A CG  1 
278  ATOM   O OD1 .  ASP A 1 36  ?  -8.428  -24.743 0.034   1.00 87.50 ?  36  ASP A OD1 1 
279  ATOM   O OD2 .  ASP A 1 36  ?  -7.826  -22.915 1.082   1.00 87.50 ?  36  ASP A OD2 1 
280  ATOM   N N   .  GLY A 1 37  ?  -13.262 -24.838 2.133   1.00 88.38 ?  37  GLY A N   1 
281  ATOM   C CA  .  GLY A 1 37  ?  -14.329 -25.14  3.071   1.00 88.38 ?  37  GLY A CA  1 
282  ATOM   C C   .  GLY A 1 37  ?  -14.768 -23.962 3.918   1.00 88.38 ?  37  GLY A C   1 
283  ATOM   O O   .  GLY A 1 37  ?  -15.564 -24.124 4.843   1.00 88.38 ?  37  GLY A O   1 
284  ATOM   N N   .  VAL A 1 38  ?  -14.267 -22.77  3.609   1.00 90.44 ?  38  VAL A N   1 
285  ATOM   C CA  .  VAL A 1 38  ?  -14.634 -21.558 4.338   1.00 90.44 ?  38  VAL A CA  1 
286  ATOM   C C   .  VAL A 1 38  ?  -15.417 -20.626 3.422   1.00 90.44 ?  38  VAL A C   1 
287  ATOM   C CB  .  VAL A 1 38  ?  -13.407 -20.785 4.872   1.00 90.44 ?  38  VAL A CB  1 
288  ATOM   O O   .  VAL A 1 38  ?  -14.892 -20.139 2.421   1.00 90.44 ?  38  VAL A O   1 
289  ATOM   C CG1 .  VAL A 1 38  ?  -13.852 -19.558 5.665   1.00 90.44 ?  38  VAL A CG1 1 
290  ATOM   C CG2 .  VAL A 1 38  ?  -12.552 -21.683 5.76    1.00 90.44 ?  38  VAL A CG2 1 
291  ATOM   N N   .  LYS A 1 39  ?  -16.673 -20.368 3.772   1.00 90.38 ?  39  LYS A N   1 
292  ATOM   C CA  .  LYS A 1 39  ?  -17.484 -19.409 3.027   1.00 90.38 ?  39  LYS A CA  1 
293  ATOM   C C   .  LYS A 1 39  ?  -16.92  -18.022 3.309   1.00 90.38 ?  39  LYS A C   1 
294  ATOM   C CB  .  LYS A 1 39  ?  -18.96  -19.494 3.425   1.00 90.38 ?  39  LYS A CB  1 
295  ATOM   O O   .  LYS A 1 39  ?  -16.75  -17.63  4.461   1.00 90.38 ?  39  LYS A O   1 
296  ATOM   C CG  .  LYS A 1 39  ?  -19.606 -20.823 3.058   1.00 90.38 ?  39  LYS A CG  1 
297  ATOM   C CD  .  LYS A 1 39  ?  -21.087 -20.843 3.403   1.00 90.38 ?  39  LYS A CD  1 
298  ATOM   C CE  .  LYS A 1 39  ?  -21.694 -22.201 3.091   1.00 90.38 ?  39  LYS A CE  1 
299  ATOM   N NZ  .  LYS A 1 39  ?  -23.156 -22.176 3.426   1.00 90.38 ?  39  LYS A NZ  1 
300  ATOM   N N   .  THR A 1 40  ?  -16.604 -17.304 2.239   1.00 91.00 ?  40  THR A N   1 
301  ATOM   C CA  .  THR A 1 40  ?  -15.933 -16.01  2.32    1.00 91.00 ?  40  THR A CA  1 
302  ATOM   C C   .  THR A 1 40  ?  -16.413 -15.156 1.149   1.00 91.00 ?  40  THR A C   1 
303  ATOM   C CB  .  THR A 1 40  ?  -14.397 -16.181 2.321   1.00 91.00 ?  40  THR A CB  1 
304  ATOM   O O   .  THR A 1 40  ?  -17.263 -15.589 0.37    1.00 91.00 ?  40  THR A O   1 
305  ATOM   C CG2 .  THR A 1 40  ?  -13.862 -16.664 0.978   1.00 91.00 ?  40  THR A CG2 1 
306  ATOM   O OG1 .  THR A 1 40  ?  -13.781 -14.929 2.643   1.00 91.00 ?  40  THR A OG1 1 
307  ATOM   N N   .  VAL A 1 41  ?  -15.886 -13.944 1.022   1.00 87.88 ?  41  VAL A N   1 
308  ATOM   C CA  .  VAL A 1 41  ?  -16.207 -13.079 -0.111  1.00 87.88 ?  41  VAL A CA  1 
309  ATOM   C C   .  VAL A 1 41  ?  -14.967 -12.908 -0.98   1.00 87.88 ?  41  VAL A C   1 
310  ATOM   C CB  .  VAL A 1 41  ?  -16.742 -11.693 0.314   1.00 87.88 ?  41  VAL A CB  1 
311  ATOM   O O   .  VAL A 1 41  ?  -13.84  -12.916 -0.484  1.00 87.88 ?  41  VAL A O   1 
312  ATOM   C CG1 .  VAL A 1 41  ?  -18.107 -11.831 0.978   1.00 87.88 ?  41  VAL A CG1 1 
313  ATOM   C CG2 .  VAL A 1 41  ?  -15.773 -10.98  1.256   1.00 87.88 ?  41  VAL A CG2 1 
314  ATOM   N N   .  THR A 1 42  ?  -15.18  -12.777 -2.284  1.00 86.31 ?  42  THR A N   1 
315  ATOM   C CA  .  THR A 1 42  ?  -14.081 -12.596 -3.228  1.00 86.31 ?  42  THR A CA  1 
316  ATOM   C C   .  THR A 1 42  ?  -13.365 -11.276 -2.962  1.00 86.31 ?  42  THR A C   1 
317  ATOM   C CB  .  THR A 1 42  ?  -14.568 -12.6   -4.692  1.00 86.31 ?  42  THR A CB  1 
318  ATOM   O O   .  THR A 1 42  ?  -13.983 -10.278 -2.594  1.00 86.31 ?  42  THR A O   1 
319  ATOM   C CG2 .  THR A 1 42  ?  -15.089 -13.971 -5.101  1.00 86.31 ?  42  THR A CG2 1 
320  ATOM   O OG1 .  THR A 1 42  ?  -15.628 -11.649 -4.848  1.00 86.31 ?  42  THR A OG1 1 
321  ATOM   N N   .  THR A 1 43  ?  -12.047 -11.289 -3.131  1.00 87.62 ?  43  THR A N   1 
322  ATOM   C CA  .  THR A 1 43  ?  -11.209 -10.117 -2.89   1.00 87.62 ?  43  THR A CA  1 
323  ATOM   C C   .  THR A 1 43  ?  -10.165 -10.002 -3.998  1.00 87.62 ?  43  THR A C   1 
324  ATOM   C CB  .  THR A 1 43  ?  -10.47  -10.226 -1.539  1.00 87.62 ?  43  THR A CB  1 
325  ATOM   O O   .  THR A 1 43  ?  -9.674  -11.013 -4.499  1.00 87.62 ?  43  THR A O   1 
326  ATOM   C CG2 .  THR A 1 43  ?  -11.446 -10.175 -0.369  1.00 87.62 ?  43  THR A CG2 1 
327  ATOM   O OG1 .  THR A 1 43  ?  -9.765  -11.471 -1.48   1.00 87.62 ?  43  THR A OG1 1 
328  ATOM   N N   .  LEU A 1 44  ?  -9.833  -8.776  -4.39   1.00 85.94 ?  44  LEU A N   1 
329  ATOM   C CA  .  LEU A 1 44  ?  -8.782  -8.541  -5.377  1.00 85.94 ?  44  LEU A CA  1 
330  ATOM   C C   .  LEU A 1 44  ?  -7.409  -8.896  -4.81   1.00 85.94 ?  44  LEU A C   1 
331  ATOM   C CB  .  LEU A 1 44  ?  -8.793  -7.071  -5.807  1.00 85.94 ?  44  LEU A CB  1 
332  ATOM   O O   .  LEU A 1 44  ?  -6.573  -9.478  -5.5    1.00 85.94 ?  44  LEU A O   1 
333  ATOM   C CG  .  LEU A 1 44  ?  -7.769  -6.644  -6.865  1.00 85.94 ?  44  LEU A CG  1 
334  ATOM   C CD1 .  LEU A 1 44  ?  -8.023  -7.317  -8.209  1.00 85.94 ?  44  LEU A CD1 1 
335  ATOM   C CD2 .  LEU A 1 44  ?  -7.823  -5.13   -7.02   1.00 85.94 ?  44  LEU A CD2 1 
336  ATOM   N N   .  SER A 1 45  ?  -7.18   -8.527  -3.555  1.00 85.62 ?  45  SER A N   1 
337  ATOM   C CA  .  SER A 1 45  ?  -5.925  -8.825  -2.873  1.00 85.62 ?  45  SER A CA  1 
338  ATOM   C C   .  SER A 1 45  ?  -5.962  -10.23  -2.281  1.00 85.62 ?  45  SER A C   1 
339  ATOM   C CB  .  SER A 1 45  ?  -5.691  -7.812  -1.751  1.00 85.62 ?  45  SER A CB  1 
340  ATOM   O O   .  SER A 1 45  ?  -7.001  -10.684 -1.804  1.00 85.62 ?  45  SER A O   1 
341  ATOM   O OG  .  SER A 1 45  ?  -5.633  -6.501  -2.286  1.00 85.62 ?  45  SER A OG  1 
342  ATOM   N N   .  HIS A 1 46  ?  -4.826  -10.918 -2.3    1.00 87.56 ?  46  HIS A N   1 
343  ATOM   C CA  .  HIS A 1 46  ?  -4.754  -12.272 -1.763  1.00 87.56 ?  46  HIS A CA  1 
344  ATOM   C C   .  HIS A 1 46  ?  -4.824  -12.244 -0.238  1.00 87.56 ?  46  HIS A C   1 
345  ATOM   C CB  .  HIS A 1 46  ?  -3.459  -12.944 -2.228  1.00 87.56 ?  46  HIS A CB  1 
346  ATOM   O O   .  HIS A 1 46  ?  -3.916  -11.74  0.423   1.00 87.56 ?  46  HIS A O   1 
347  ATOM   C CG  .  HIS A 1 46  ?  -3.336  -14.374 -1.802  1.00 87.56 ?  46  HIS A CG  1 
348  ATOM   C CD2 .  HIS A 1 46  ?  -2.48   -14.962 -0.927  1.00 87.56 ?  46  HIS A CD2 1 
349  ATOM   N ND1 .  HIS A 1 46  ?  -4.119  -15.401 -2.281  1.00 87.56 ?  46  HIS A ND1 1 
350  ATOM   C CE1 .  HIS A 1 46  ?  -3.712  -16.536 -1.693  1.00 87.56 ?  46  HIS A CE1 1 
351  ATOM   N NE2 .  HIS A 1 46  ?  -2.698  -16.317 -0.879  1.00 87.56 ?  46  HIS A NE2 1 
352  ATOM   N N   .  ILE A 1 47  ?  -5.918  -12.762 0.311   1.00 91.88 ?  47  ILE A N   1 
353  ATOM   C CA  .  ILE A 1 47  ?  -6.1    -12.859 1.758   1.00 91.88 ?  47  ILE A CA  1 
354  ATOM   C C   .  ILE A 1 47  ?  -6.583  -14.27  2.084   1.00 91.88 ?  47  ILE A C   1 
355  ATOM   C CB  .  ILE A 1 47  ?  -7.132  -11.838 2.292   1.00 91.88 ?  47  ILE A CB  1 
356  ATOM   O O   .  ILE A 1 47  ?  -7.586  -14.733 1.542   1.00 91.88 ?  47  ILE A O   1 
357  ATOM   C CG1 .  ILE A 1 47  ?  -6.746  -10.406 1.903   1.00 91.88 ?  47  ILE A CG1 1 
358  ATOM   C CG2 .  ILE A 1 47  ?  -7.245  -11.957 3.813   1.00 91.88 ?  47  ILE A CG2 1 
359  ATOM   C CD1 .  ILE A 1 47  ?  -7.838  -9.374  2.12    1.00 91.88 ?  47  ILE A CD1 1 
360  ATOM   N N   .  VAL A 1 48  ?  -5.853  -14.958 2.955   1.00 92.50 ?  48  VAL A N   1 
361  ATOM   C CA  .  VAL A 1 48  ?  -6.153  -16.339 3.328   1.00 92.50 ?  48  VAL A CA  1 
362  ATOM   C C   .  VAL A 1 48  ?  -7.135  -16.37  4.495   1.00 92.50 ?  48  VAL A C   1 
363  ATOM   C CB  .  VAL A 1 48  ?  -4.872  -17.106 3.733   1.00 92.50 ?  48  VAL A CB  1 
364  ATOM   O O   .  VAL A 1 48  ?  -6.91   -15.737 5.527   1.00 92.50 ?  48  VAL A O   1 
365  ATOM   C CG1 .  VAL A 1 48  ?  -5.196  -18.543 4.132   1.00 92.50 ?  48  VAL A CG1 1 
366  ATOM   C CG2 .  VAL A 1 48  ?  -3.861  -17.109 2.589   1.00 92.50 ?  48  VAL A CG2 1 
367  ATOM   N N   .  SER A 1 49  ?  -8.23   -17.102 4.321   1.00 93.44 ?  49  SER A N   1 
368  ATOM   C CA  .  SER A 1 49  ?  -9.245  -17.257 5.359   1.00 93.44 ?  49  SER A CA  1 
369  ATOM   C C   .  SER A 1 49  ?  -8.831  -18.258 6.436   1.00 93.44 ?  49  SER A C   1 
370  ATOM   C CB  .  SER A 1 49  ?  -10.551 -17.748 4.728   1.00 93.44 ?  49  SER A CB  1 
371  ATOM   O O   .  SER A 1 49  ?  -8.09   -19.203 6.168   1.00 93.44 ?  49  SER A O   1 
372  ATOM   O OG  .  SER A 1 49  ?  -11.026 -16.832 3.757   1.00 93.44 ?  49  SER A OG  1 
373  ATOM   N N   .  ARG A 1 50  ?  -9.336  -18.076 7.653   1.00 91.62 ?  50  ARG A N   1 
374  ATOM   C CA  .  ARG A 1 50  ?  -9.107  -19.034 8.733   1.00 91.62 ?  50  ARG A CA  1 
375  ATOM   C C   .  ARG A 1 50  ?  -10.264 -20.021 8.837   1.00 91.62 ?  50  ARG A C   1 
376  ATOM   C CB  .  ARG A 1 50  ?  -8.947  -18.326 10.08   1.00 91.62 ?  50  ARG A CB  1 
377  ATOM   O O   .  ARG A 1 50  ?  -11.429 -19.628 8.876   1.00 91.62 ?  50  ARG A O   1 
378  ATOM   C CG  .  ARG A 1 50  ?  -7.661  -17.525 10.222  1.00 91.62 ?  50  ARG A CG  1 
379  ATOM   C CD  .  ARG A 1 50  ?  -7.56   -16.902 11.605  1.00 91.62 ?  50  ARG A CD  1 
380  ATOM   N NE  .  ARG A 1 50  ?  -6.353  -16.086 11.74   1.00 91.62 ?  50  ARG A NE  1 
381  ATOM   N NH1 .  ARG A 1 50  ?  -6.648  -15.55  13.977  1.00 91.62 ?  50  ARG A NH1 1 
382  ATOM   N NH2 .  ARG A 1 50  ?  -4.866  -14.752 12.832  1.00 91.62 ?  50  ARG A NH2 1 
383  ATOM   C CZ  .  ARG A 1 50  ?  -5.97   -15.469 12.85   1.00 91.62 ?  50  ARG A CZ  1 
384  ATOM   N N   .  LYS A 1 51  ?  -9.928  -21.306 8.896   1.00 91.81 ?  51  LYS A N   1 
385  ATOM   C CA  .  LYS A 1 51  ?  -10.917 -22.364 9.089   1.00 91.81 ?  51  LYS A CA  1 
386  ATOM   C C   .  LYS A 1 51  ?  -11.396 -22.362 10.537  1.00 91.81 ?  51  LYS A C   1 
387  ATOM   C CB  .  LYS A 1 51  ?  -10.313 -23.732 8.756   1.00 91.81 ?  51  LYS A CB  1 
388  ATOM   O O   .  LYS A 1 51  ?  -10.599 -22.185 11.456  1.00 91.81 ?  51  LYS A O   1 
389  ATOM   C CG  .  LYS A 1 51  ?  -9.936  -23.91  7.291   1.00 91.81 ?  51  LYS A CG  1 
390  ATOM   C CD  .  LYS A 1 51  ?  -9.357  -25.292 7.026   1.00 91.81 ?  51  LYS A CD  1 
391  ATOM   C CE  .  LYS A 1 51  ?  -8.967  -25.444 5.564   1.00 91.81 ?  51  LYS A CE  1 
392  ATOM   N NZ  .  LYS A 1 51  ?  -8.371  -26.803 5.342   1.00 91.81 ?  51  LYS A NZ  1 
393  ATOM   N N   .  GLY A 1 52  ?  -12.694 -22.569 10.731  1.00 89.88 ?  52  GLY A N   1 
394  ATOM   C CA  .  GLY A 1 52  ?  -13.254 -22.646 12.07   1.00 89.88 ?  52  GLY A CA  1 
395  ATOM   C C   .  GLY A 1 52  ?  -13.276 -21.331 12.826  1.00 89.88 ?  52  GLY A C   1 
396  ATOM   O O   .  GLY A 1 52  ?  -13.253 -21.323 14.056  1.00 89.88 ?  52  GLY A O   1 
397  ATOM   N N   .  LEU A 1 53  ?  -13.308 -20.219 12.1    1.00 92.81 ?  53  LEU A N   1 
398  ATOM   C CA  .  LEU A 1 53  ?  -13.311 -18.896 12.716  1.00 92.81 ?  53  LEU A CA  1 
399  ATOM   C C   .  LEU A 1 53  ?  -14.674 -18.581 13.329  1.00 92.81 ?  53  LEU A C   1 
400  ATOM   C CB  .  LEU A 1 53  ?  -12.967 -17.847 11.655  1.00 92.81 ?  53  LEU A CB  1 
401  ATOM   O O   .  LEU A 1 53  ?  -15.69  -18.597 12.634  1.00 92.81 ?  53  LEU A O   1 
402  ATOM   C CG  .  LEU A 1 53  ?  -12.81  -16.407 12.15   1.00 92.81 ?  53  LEU A CG  1 
403  ATOM   C CD1 .  LEU A 1 53  ?  -11.524 -16.222 12.947  1.00 92.81 ?  53  LEU A CD1 1 
404  ATOM   C CD2 .  LEU A 1 53  ?  -12.825 -15.46  10.96   1.00 92.81 ?  53  LEU A CD2 1 
405  ATOM   N N   .  LYS A 1 54  ?  -14.696 -18.306 14.629  1.00 93.81 ?  54  LYS A N   1 
406  ATOM   C CA  .  LYS A 1 54  ?  -15.929 -17.99  15.349  1.00 93.81 ?  54  LYS A CA  1 
407  ATOM   C C   .  LYS A 1 54  ?  -15.705 -16.824 16.304  1.00 93.81 ?  54  LYS A C   1 
408  ATOM   C CB  .  LYS A 1 54  ?  -16.392 -19.206 16.157  1.00 93.81 ?  54  LYS A CB  1 
409  ATOM   O O   .  LYS A 1 54  ?  -14.576 -16.575 16.721  1.00 93.81 ?  54  LYS A O   1 
410  ATOM   C CG  .  LYS A 1 54  ?  -16.763 -20.415 15.31   1.00 93.81 ?  54  LYS A CG  1 
411  ATOM   C CD  .  LYS A 1 54  ?  -17.272 -21.559 16.174  1.00 93.81 ?  54  LYS A CD  1 
412  ATOM   C CE  .  LYS A 1 54  ?  -17.584 -22.78  15.324  1.00 93.81 ?  54  LYS A CE  1 
413  ATOM   N NZ  .  LYS A 1 54  ?  -18.11  -23.876 16.202  1.00 93.81 ?  54  LYS A NZ  1 
414  ATOM   N N   .  LEU A 1 55  ?  -16.779 -16.131 16.664  1.00 95.31 ?  55  LEU A N   1 
415  ATOM   C CA  .  LEU A 1 55  ?  -16.705 -15.081 17.677  1.00 95.31 ?  55  LEU A CA  1 
416  ATOM   C C   .  LEU A 1 55  ?  -16.33  -15.692 19.024  1.00 95.31 ?  55  LEU A C   1 
417  ATOM   C CB  .  LEU A 1 55  ?  -18.049 -14.359 17.81   1.00 95.31 ?  55  LEU A CB  1 
418  ATOM   O O   .  LEU A 1 55  ?  -16.836 -16.75  19.399  1.00 95.31 ?  55  LEU A O   1 
419  ATOM   C CG  .  LEU A 1 55  ?  -18.51  -13.466 16.654  1.00 95.31 ?  55  LEU A CG  1 
420  ATOM   C CD1 .  LEU A 1 55  ?  -19.958 -13.053 16.881  1.00 95.31 ?  55  LEU A CD1 1 
421  ATOM   C CD2 .  LEU A 1 55  ?  -17.628 -12.229 16.522  1.00 95.31 ?  55  LEU A CD2 1 
422  ATOM   N N   .  ARG A 1 56  ?  -15.45  -15.009 19.749  1.00 93.81 ?  56  ARG A N   1 
423  ATOM   C CA  .  ARG A 1 56  ?  -15.058 -15.417 21.096  1.00 93.81 ?  56  ARG A CA  1 
424  ATOM   C C   .  ARG A 1 56  ?  -16.225 -15.276 22.067  1.00 93.81 ?  56  ARG A C   1 
425  ATOM   C CB  .  ARG A 1 56  ?  -13.874 -14.578 21.584  1.00 93.81 ?  56  ARG A CB  1 
426  ATOM   O O   .  ARG A 1 56  ?  -17.173 -14.532 21.82   1.00 93.81 ?  56  ARG A O   1 
427  ATOM   C CG  .  ARG A 1 56  ?  -14.177 -13.097 21.754  1.00 93.81 ?  56  ARG A CG  1 
428  ATOM   C CD  .  ARG A 1 56  ?  -12.933 -12.342 22.193  1.00 93.81 ?  56  ARG A CD  1 
429  ATOM   N NE  .  ARG A 1 56  ?  -13.134 -10.893 22.189  1.00 93.81 ?  56  ARG A NE  1 
430  ATOM   N NH1 .  ARG A 1 56  ?  -14.145 -10.713 24.276  1.00 93.81 ?  56  ARG A NH1 1 
431  ATOM   N NH2 .  ARG A 1 56  ?  -13.771 -8.873  23.013  1.00 93.81 ?  56  ARG A NH2 1 
432  ATOM   C CZ  .  ARG A 1 56  ?  -13.683 -10.179 23.163  1.00 93.81 ?  56  ARG A CZ  1 
433  ATOM   N N   .  ASP A 1 57  ?  -16.127 -15.987 23.185  1.00 91.50 ?  57  ASP A N   1 
434  ATOM   C CA  .  ASP A 1 57  ?  -17.171 -15.953 24.204  1.00 91.50 ?  57  ASP A CA  1 
435  ATOM   C C   .  ASP A 1 57  ?  -17.436 -14.518 24.653  1.00 91.50 ?  57  ASP A C   1 
436  ATOM   C CB  .  ASP A 1 57  ?  -16.771 -16.799 25.416  1.00 91.50 ?  57  ASP A CB  1 
437  ATOM   O O   .  ASP A 1 57  ?  -16.516 -13.714 24.8    1.00 91.50 ?  57  ASP A O   1 
438  ATOM   C CG  .  ASP A 1 57  ?  -16.728 -18.283 25.108  1.00 91.50 ?  57  ASP A CG  1 
439  ATOM   O OD1 .  ASP A 1 57  ?  -17.505 -18.75  24.247  1.00 91.50 ?  57  ASP A OD1 1 
440  ATOM   O OD2 .  ASP A 1 57  ?  -15.918 -18.995 25.739  1.00 91.50 ?  57  ASP A OD2 1 
441  ATOM   N N   .  GLY A 1 58  ?  -18.712 -14.204 24.857  1.00 91.19 ?  58  GLY A N   1 
442  ATOM   C CA  .  GLY A 1 58  ?  -19.116 -12.864 25.244  1.00 91.19 ?  58  GLY A CA  1 
443  ATOM   C C   .  GLY A 1 58  ?  -19.52  -11.979 24.081  1.00 91.19 ?  58  GLY A C   1 
444  ATOM   O O   .  GLY A 1 58  ?  -20.127 -10.929 24.294  1.00 91.19 ?  58  GLY A O   1 
445  ATOM   N N   .  LEU A 1 59  ?  -19.203 -12.392 22.858  1.00 94.06 ?  59  LEU A N   1 
446  ATOM   C CA  .  LEU A 1 59  ?  -19.58  -11.641 21.665  1.00 94.06 ?  59  LEU A CA  1 
447  ATOM   C C   .  LEU A 1 59  ?  -20.658 -12.355 20.855  1.00 94.06 ?  59  LEU A C   1 
448  ATOM   C CB  .  LEU A 1 59  ?  -18.371 -11.397 20.756  1.00 94.06 ?  59  LEU A CB  1 
449  ATOM   O O   .  LEU A 1 59  ?  -20.588 -13.556 20.596  1.00 94.06 ?  59  LEU A O   1 
450  ATOM   C CG  .  LEU A 1 59  ?  -17.17  -10.607 21.285  1.00 94.06 ?  59  LEU A CG  1 
451  ATOM   C CD1 .  LEU A 1 59  ?  -16.221 -10.354 20.119  1.00 94.06 ?  59  LEU A CD1 1 
452  ATOM   C CD2 .  LEU A 1 59  ?  -17.569 -9.278  21.917  1.00 94.06 ?  59  LEU A CD2 1 
453  ATOM   N N   .  THR A 1 60  ?  -21.647 -11.577 20.435  1.00 94.44 ?  60  THR A N   1 
454  ATOM   C CA  .  THR A 1 60  ?  -22.714 -12.03  19.548  1.00 94.44 ?  60  THR A CA  1 
455  ATOM   C C   .  THR A 1 60  ?  -22.736 -11.057 18.374  1.00 94.44 ?  60  THR A C   1 
456  ATOM   C CB  .  THR A 1 60  ?  -24.092 -12.007 20.242  1.00 94.44 ?  60  THR A CB  1 
457  ATOM   O O   .  THR A 1 60  ?  -22.068 -10.025 18.413  1.00 94.44 ?  60  THR A O   1 
458  ATOM   C CG2 .  THR A 1 60  ?  -24.119 -12.922 21.461  1.00 94.44 ?  60  THR A CG2 1 
459  ATOM   O OG1 .  THR A 1 60  ?  -24.401 -10.67  20.654  1.00 94.44 ?  60  THR A OG1 1 
460  ATOM   N N   .  VAL A 1 61  ?  -23.501 -11.363 17.332  1.00 91.00 ?  61  VAL A N   1 
461  ATOM   C CA  .  VAL A 1 61  ?  -23.582 -10.476 16.173  1.00 91.00 ?  61  VAL A CA  1 
462  ATOM   C C   .  VAL A 1 61  ?  -24.081 -9.091  16.577  1.00 91.00 ?  61  VAL A C   1 
463  ATOM   C CB  .  VAL A 1 61  ?  -24.5   -11.053 15.071  1.00 91.00 ?  61  VAL A CB  1 
464  ATOM   O O   .  VAL A 1 61  ?  -23.634 -8.079  16.038  1.00 91.00 ?  61  VAL A O   1 
465  ATOM   C CG1 .  VAL A 1 61  ?  -24.614 -10.094 13.89   1.00 91.00 ?  61  VAL A CG1 1 
466  ATOM   C CG2 .  VAL A 1 61  ?  -23.972 -12.406 14.597  1.00 91.00 ?  61  VAL A CG2 1 
467  ATOM   N N   .  ASP A 1 62  ?  -25.001 -9.048  17.534  1.00 90.56 ?  62  ASP A N   1 
468  ATOM   C CA  .  ASP A 1 62  ?  -25.638 -7.802  17.952  1.00 90.56 ?  62  ASP A CA  1 
469  ATOM   C C   .  ASP A 1 62  ?  -24.742 -6.861  18.756  1.00 90.56 ?  62  ASP A C   1 
470  ATOM   C CB  .  ASP A 1 62  ?  -26.876 -8.128  18.79   1.00 90.56 ?  62  ASP A CB  1 
471  ATOM   O O   .  ASP A 1 62  ?  -24.942 -5.647  18.715  1.00 90.56 ?  62  ASP A O   1 
472  ATOM   C CG  .  ASP A 1 62  ?  -27.966 -8.8    17.978  1.00 90.56 ?  62  ASP A CG  1 
473  ATOM   O OD1 .  ASP A 1 62  ?  -28.362 -8.255  16.926  1.00 90.56 ?  62  ASP A OD1 1 
474  ATOM   O OD2 .  ASP A 1 62  ?  -28.435 -9.882  18.392  1.00 90.56 ?  62  ASP A OD2 1 
475  ATOM   N N   .  ASN A 1 63  ?  -23.776 -7.397  19.496  1.00 93.88 ?  63  ASN A N   1 
476  ATOM   C CA  .  ASN A 1 63  ?  -22.944 -6.578  20.375  1.00 93.88 ?  63  ASN A CA  1 
477  ATOM   C C   .  ASN A 1 63  ?  -21.448 -6.649  20.079  1.00 93.88 ?  63  ASN A C   1 
478  ATOM   C CB  .  ASN A 1 63  ?  -23.19  -6.963  21.837  1.00 93.88 ?  63  ASN A CB  1 
479  ATOM   O O   .  ASN A 1 63  ?  -20.635 -6.144  20.854  1.00 93.88 ?  63  ASN A O   1 
480  ATOM   C CG  .  ASN A 1 63  ?  -22.451 -8.22   22.244  1.00 93.88 ?  63  ASN A CG  1 
481  ATOM   N ND2 .  ASN A 1 63  ?  -21.999 -8.259  23.487  1.00 93.88 ?  63  ASN A ND2 1 
482  ATOM   O OD1 .  ASN A 1 63  ?  -22.292 -9.152  21.46   1.00 93.88 ?  63  ASN A OD1 1 
483  ATOM   N N   .  ALA A 1 64  ?  -21.078 -7.28   18.97   1.00 95.06 ?  64  ALA A N   1 
484  ATOM   C CA  .  ALA A 1 64  ?  -19.678 -7.369  18.572  1.00 95.06 ?  64  ALA A CA  1 
485  ATOM   C C   .  ALA A 1 64  ?  -19.118 -5.974  18.299  1.00 95.06 ?  64  ALA A C   1 
486  ATOM   C CB  .  ALA A 1 64  ?  -19.533 -8.247  17.334  1.00 95.06 ?  64  ALA A CB  1 
487  ATOM   O O   .  ALA A 1 64  ?  -19.853 -5.078  17.879  1.00 95.06 ?  64  ALA A O   1 
488  ATOM   N N   .  PRO A 1 65  ?  -17.815 -5.755  18.54   1.00 94.75 ?  65  PRO A N   1 
489  ATOM   C CA  .  PRO A 1 65  ?  -17.305 -4.423  18.197  1.00 94.75 ?  65  PRO A CA  1 
490  ATOM   C C   .  PRO A 1 65  ?  -17.434 -4.079  16.716  1.00 94.75 ?  65  PRO A C   1 
491  ATOM   C CB  .  PRO A 1 65  ?  -15.826 -4.504  18.585  1.00 94.75 ?  65  PRO A CB  1 
492  ATOM   O O   .  PRO A 1 65  ?  -17.341 -4.949  15.85   1.00 94.75 ?  65  PRO A O   1 
493  ATOM   C CG  .  PRO A 1 65  ?  -15.743 -5.617  19.573  1.00 94.75 ?  65  PRO A CG  1 
494  ATOM   C CD  .  PRO A 1 65  ?  -16.751 -6.615  19.088  1.00 94.75 ?  65  PRO A CD  1 
495  ATOM   N N   .  ARG A 1 66  ?  -17.63  -2.798  16.422  1.00 95.88 ?  66  ARG A N   1 
496  ATOM   C CA  .  ARG A 1 66  ?  -17.693 -2.322  15.042  1.00 95.88 ?  66  ARG A CA  1 
497  ATOM   C C   .  ARG A 1 66  ?  -16.322 -1.811  14.614  1.00 95.88 ?  66  ARG A C   1 
498  ATOM   C CB  .  ARG A 1 66  ?  -18.73  -1.204  14.899  1.00 95.88 ?  66  ARG A CB  1 
499  ATOM   O O   .  ARG A 1 66  ?  -15.588 -1.245  15.424  1.00 95.88 ?  66  ARG A O   1 
500  ATOM   C CG  .  ARG A 1 66  ?  -20.162 -1.613  15.219  1.00 95.88 ?  66  ARG A CG  1 
501  ATOM   C CD  .  ARG A 1 66  ?  -21.104 -0.42   15.121  1.00 95.88 ?  66  ARG A CD  1 
502  ATOM   N NE  .  ARG A 1 66  ?  -21.245 0.058   13.745  1.00 95.88 ?  66  ARG A NE  1 
503  ATOM   N NH1 .  ARG A 1 66  ?  -22.556 1.908   14.237  1.00 95.88 ?  66  ARG A NH1 1 
504  ATOM   N NH2 .  ARG A 1 66  ?  -21.985 1.45    12.098  1.00 95.88 ?  66  ARG A NH2 1 
505  ATOM   C CZ  .  ARG A 1 66  ?  -21.924 1.137   13.376  1.00 95.88 ?  66  ARG A CZ  1 
506  ATOM   N N   .  ALA A 1 67  ?  -15.991 -2.006  13.342  1.00 97.25 ?  67  ALA A N   1 
507  ATOM   C CA  .  ALA A 1 67  ?  -14.705 -1.586  12.795  1.00 97.25 ?  67  ALA A CA  1 
508  ATOM   C C   .  ALA A 1 67  ?  -14.871 -0.518  11.716  1.00 97.25 ?  67  ALA A C   1 
509  ATOM   C CB  .  ALA A 1 67  ?  -13.966 -2.792  12.228  1.00 97.25 ?  67  ALA A CB  1 
510  ATOM   O O   .  ALA A 1 67  ?  -15.87  -0.492  10.998  1.00 97.25 ?  67  ALA A O   1 
511  ATOM   N N   .  ALA A 1 68  ?  -13.88  0.358   11.588  1.00 97.94 ?  68  ALA A N   1 
512  ATOM   C CA  .  ALA A 1 68  ?  -13.876 1.394   10.56   1.00 97.94 ?  68  ALA A CA  1 
513  ATOM   C C   .  ALA A 1 68  ?  -12.522 1.442   9.86    1.00 97.94 ?  68  ALA A C   1 
514  ATOM   C CB  .  ALA A 1 68  ?  -14.191 2.753   11.17   1.00 97.94 ?  68  ALA A CB  1 
515  ATOM   O O   .  ALA A 1 68  ?  -11.507 1.031   10.42   1.00 97.94 ?  68  ALA A O   1 
516  ATOM   N N   .  PHE A 1 69  ?  -12.521 1.937   8.627   1.00 98.00 ?  69  PHE A N   1 
517  ATOM   C CA  .  PHE A 1 69  ?  -11.305 2.065   7.831   1.00 98.00 ?  69  PHE A CA  1 
518  ATOM   C C   .  PHE A 1 69  ?  -11.169 3.507   7.352   1.00 98.00 ?  69  PHE A C   1 
519  ATOM   C CB  .  PHE A 1 69  ?  -11.394 1.121   6.63    1.00 98.00 ?  69  PHE A CB  1 
520  ATOM   O O   .  PHE A 1 69  ?  -12.123 4.073   6.818   1.00 98.00 ?  69  PHE A O   1 
521  ATOM   C CG  .  PHE A 1 69  ?  -10.103 0.96    5.878   1.00 98.00 ?  69  PHE A CG  1 
522  ATOM   C CD1 .  PHE A 1 69  ?  -9.789  1.794   4.81    1.00 98.00 ?  69  PHE A CD1 1 
523  ATOM   C CD2 .  PHE A 1 69  ?  -9.214  -0.052  6.225   1.00 98.00 ?  69  PHE A CD2 1 
524  ATOM   C CE1 .  PHE A 1 69  ?  -8.617  1.606   4.083   1.00 98.00 ?  69  PHE A CE1 1 
525  ATOM   C CE2 .  PHE A 1 69  ?  -8.025  -0.227  5.523   1.00 98.00 ?  69  PHE A CE2 1 
526  ATOM   C CZ  .  PHE A 1 69  ?  -7.737  0.589   4.434   1.00 98.00 ?  69  PHE A CZ  1 
527  ATOM   N N   .  ILE A 1 70  ?  -10     4.106   7.549   1.00 97.88 ?  70  ILE A N   1 
528  ATOM   C CA  .  ILE A 1 70  ?  -9.76   5.48    7.116   1.00 97.88 ?  70  ILE A CA  1 
529  ATOM   C C   .  ILE A 1 70  ?  -8.488  5.486   6.274   1.00 97.88 ?  70  ILE A C   1 
530  ATOM   C CB  .  ILE A 1 70  ?  -9.598  6.455   8.308   1.00 97.88 ?  70  ILE A CB  1 
531  ATOM   O O   .  ILE A 1 70  ?  -7.442  5.029   6.734   1.00 97.88 ?  70  ILE A O   1 
532  ATOM   C CG1 .  ILE A 1 70  ?  -10.773 6.324   9.286   1.00 97.88 ?  70  ILE A CG1 1 
533  ATOM   C CG2 .  ILE A 1 70  ?  -9.495  7.892   7.796   1.00 97.88 ?  70  ILE A CG2 1 
534  ATOM   C CD1 .  ILE A 1 70  ?  -10.659 7.151   10.554  1.00 97.88 ?  70  ILE A CD1 1 
535  ATOM   N N   .  THR A 1 71  ?  -8.576  5.982   5.045   1.00 95.00 ?  71  THR A N   1 
536  ATOM   C CA  .  THR A 1 71  ?  -7.402  6.104   4.183   1.00 95.00 ?  71  THR A CA  1 
537  ATOM   C C   .  THR A 1 71  ?  -6.582  7.317   4.608   1.00 95.00 ?  71  THR A C   1 
538  ATOM   C CB  .  THR A 1 71  ?  -7.782  6.311   2.701   1.00 95.00 ?  71  THR A CB  1 
539  ATOM   O O   .  THR A 1 71  ?  -7.139  8.303   5.092   1.00 95.00 ?  71  THR A O   1 
540  ATOM   C CG2 .  THR A 1 71  ?  -8.583  5.133   2.16    1.00 95.00 ?  71  THR A CG2 1 
541  ATOM   O OG1 .  THR A 1 71  ?  -8.579  7.494   2.572   1.00 95.00 ?  71  THR A OG1 1 
542  ATOM   N N   .  ASP A 1 72  ?  -5.268  7.263   4.424   1.00 87.69 ?  72  ASP A N   1 
543  ATOM   C CA  .  ASP A 1 72  ?  -4.43   8.426   4.701   1.00 87.69 ?  72  ASP A CA  1 
544  ATOM   C C   .  ASP A 1 72  ?  -4.526  9.429   3.554   1.00 87.69 ?  72  ASP A C   1 
545  ATOM   C CB  .  ASP A 1 72  ?  -2.985  8.009   4.994   1.00 87.69 ?  72  ASP A CB  1 
546  ATOM   O O   .  ASP A 1 72  ?  -4.702  10.626  3.778   1.00 87.69 ?  72  ASP A O   1 
547  ATOM   C CG  .  ASP A 1 72  ?  -2.185  7.678   3.747   1.00 87.69 ?  72  ASP A CG  1 
548  ATOM   O OD1 .  ASP A 1 72  ?  -2.614  6.84    2.926   1.00 87.69 ?  72  ASP A OD1 1 
549  ATOM   O OD2 .  ASP A 1 72  ?  -1.075  8.233   3.599   1.00 87.69 ?  72  ASP A OD2 1 
550  ATOM   N N   .  GLU A 1 73  ?  -4.448  8.918   2.33    1.00 83.00 ?  73  GLU A N   1 
551  ATOM   C CA  .  GLU A 1 73  ?  -4.723  9.665   1.106   1.00 83.00 ?  73  GLU A CA  1 
552  ATOM   C C   .  GLU A 1 73  ?  -5.146  8.647   0.048   1.00 83.00 ?  73  GLU A C   1 
553  ATOM   C CB  .  GLU A 1 73  ?  -3.487  10.412  0.593   1.00 83.00 ?  73  GLU A CB  1 
554  ATOM   O O   .  GLU A 1 73  ?  -4.676  7.508   0.057   1.00 83.00 ?  73  GLU A O   1 
555  ATOM   C CG  .  GLU A 1 73  ?  -3.021  11.576  1.457   1.00 83.00 ?  73  GLU A CG  1 
556  ATOM   C CD  .  GLU A 1 73  ?  -1.915  12.388  0.809   1.00 83.00 ?  73  GLU A CD  1 
557  ATOM   O OE1 .  GLU A 1 73  ?  -1.199  13.102  1.544   1.00 83.00 ?  73  GLU A OE1 1 
558  ATOM   O OE2 .  GLU A 1 73  ?  -1.756  12.345  -0.429  1.00 83.00 ?  73  GLU A OE2 1 
559  ATOM   N N   .  GLY A 1 74  ?  -6.013  9.047   -0.876  1.00 82.50 ?  74  GLY A N   1 
560  ATOM   C CA  .  GLY A 1 74  ?  -6.405  8.168   -1.964  1.00 82.50 ?  74  GLY A CA  1 
561  ATOM   C C   .  GLY A 1 74  ?  -7.79   7.568   -1.819  1.00 82.50 ?  74  GLY A C   1 
562  ATOM   O O   .  GLY A 1 74  ?  -8.708  8.211   -1.311  1.00 82.50 ?  74  GLY A O   1 
563  ATOM   N N   .  SER A 1 75  ?  -7.952  6.336   -2.29   1.00 85.69 ?  75  SER A N   1 
564  ATOM   C CA  .  SER A 1 75  ?  -9.252  5.671   -2.307  1.00 85.69 ?  75  SER A CA  1 
565  ATOM   C C   .  SER A 1 75  ?  -9.101  4.163   -2.126  1.00 85.69 ?  75  SER A C   1 
566  ATOM   C CB  .  SER A 1 75  ?  -9.949  5.957   -3.64   1.00 85.69 ?  75  SER A CB  1 
567  ATOM   O O   .  SER A 1 75  ?  -8.059  3.597   -2.455  1.00 85.69 ?  75  SER A O   1 
568  ATOM   O OG  .  SER A 1 75  ?  -11.198 5.293   -3.728  1.00 85.69 ?  75  SER A OG  1 
569  ATOM   N N   .  VAL A 1 76  ?  -10.15  3.512   -1.634  1.00 88.81 ?  76  VAL A N   1 
570  ATOM   C CA  .  VAL A 1 76  ?  -10.175 2.059   -1.467  1.00 88.81 ?  76  VAL A CA  1 
571  ATOM   C C   .  VAL A 1 76  ?  -10.538 1.34    -2.764  1.00 88.81 ?  76  VAL A C   1 
572  ATOM   C CB  .  VAL A 1 76  ?  -11.156 1.596   -0.365  1.00 88.81 ?  76  VAL A CB  1 
573  ATOM   O O   .  VAL A 1 76  ?  -10.815 0.141   -2.768  1.00 88.81 ?  76  VAL A O   1 
574  ATOM   C CG1 .  VAL A 1 76  ?  -10.711 2.123   0.994   1.00 88.81 ?  76  VAL A CG1 1 
575  ATOM   C CG2 .  VAL A 1 76  ?  -12.588 2.033   -0.664  1.00 88.81 ?  76  VAL A CG2 1 
576  ATOM   N N   .  HIS A 1 77  ?  -10.497 2.075   -3.869  1.00 86.19 ?  77  HIS A N   1 
577  ATOM   C CA  .  HIS A 1 77  ?  -10.638 1.513   -5.209  1.00 86.19 ?  77  HIS A CA  1 
578  ATOM   C C   .  HIS A 1 77  ?  -9.357  1.749   -6.008  1.00 86.19 ?  77  HIS A C   1 
579  ATOM   C CB  .  HIS A 1 77  ?  -11.825 2.16    -5.929  1.00 86.19 ?  77  HIS A CB  1 
580  ATOM   O O   .  HIS A 1 77  ?  -9.375  1.791   -7.237  1.00 86.19 ?  77  HIS A O   1 
581  ATOM   C CG  .  HIS A 1 77  ?  -13.094 2.146   -5.134  1.00 86.19 ?  77  HIS A CG  1 
582  ATOM   C CD2 .  HIS A 1 77  ?  -13.755 3.156   -4.512  1.00 86.19 ?  77  HIS A CD2 1 
583  ATOM   N ND1 .  HIS A 1 77  ?  -13.851 1.022   -4.891  1.00 86.19 ?  77  HIS A ND1 1 
584  ATOM   C CE1 .  HIS A 1 77  ?  -14.912 1.392   -4.16   1.00 86.19 ?  77  HIS A CE1 1 
585  ATOM   N NE2 .  HIS A 1 77  ?  -14.895 2.686   -3.909  1.00 86.19 ?  77  HIS A NE2 1 
586  ATOM   N N   .  ASP A 1 78  ?  -8.247  1.918   -5.298  1.00 82.56 ?  78  ASP A N   1 
587  ATOM   C CA  .  ASP A 1 78  ?  -6.948  2.164   -5.921  1.00 82.56 ?  78  ASP A CA  1 
588  ATOM   C C   .  ASP A 1 78  ?  -6.201  0.886   -6.296  1.00 82.56 ?  78  ASP A C   1 
589  ATOM   C CB  .  ASP A 1 78  ?  -6.059  3.003   -4.998  1.00 82.56 ?  78  ASP A CB  1 
590  ATOM   O O   .  ASP A 1 78  ?  -5.024  0.938   -6.651  1.00 82.56 ?  78  ASP A O   1 
591  ATOM   C CG  .  ASP A 1 78  ?  -5.484  2.202   -3.842  1.00 82.56 ?  78  ASP A CG  1 
592  ATOM   O OD1 .  ASP A 1 78  ?  -6.102  1.224   -3.369  1.00 82.56 ?  78  ASP A OD1 1 
593  ATOM   O OD2 .  ASP A 1 78  ?  -4.383  2.561   -3.372  1.00 82.56 ?  78  ASP A OD2 1 
594  ATOM   N N   .  GLU A 1 79  ?  -6.892  -0.246  -6.203  1.00 84.56 ?  79  GLU A N   1 
595  ATOM   C CA  .  GLU A 1 79  ?  -6.432  -1.535  -6.719  1.00 84.56 ?  79  GLU A CA  1 
596  ATOM   C C   .  GLU A 1 79  ?  -5.155  -2.062  -6.067  1.00 84.56 ?  79  GLU A C   1 
597  ATOM   C CB  .  GLU A 1 79  ?  -6.25   -1.467  -8.239  1.00 84.56 ?  79  GLU A CB  1 
598  ATOM   O O   .  GLU A 1 79  ?  -4.546  -3.016  -6.553  1.00 84.56 ?  79  GLU A O   1 
599  ATOM   C CG  .  GLU A 1 79  ?  -7.523  -1.097  -8.987  1.00 84.56 ?  79  GLU A CG  1 
600  ATOM   C CD  .  GLU A 1 79  ?  -7.37   -1.208  -10.491 1.00 84.56 ?  79  GLU A CD  1 
601  ATOM   O OE1 .  GLU A 1 79  ?  -8.159  -1.952  -11.111 1.00 84.56 ?  79  GLU A OE1 1 
602  ATOM   O OE2 .  GLU A 1 79  ?  -6.475  -0.551  -11.065 1.00 84.56 ?  79  GLU A OE2 1 
603  ATOM   N N   .  SER A 1 80  ?  -4.747  -1.449  -4.96   1.00 85.25 ?  80  SER A N   1 
604  ATOM   C CA  .  SER A 1 80  ?  -3.499  -1.808  -4.296  1.00 85.25 ?  80  SER A CA  1 
605  ATOM   C C   .  SER A 1 80  ?  -3.48   -1.512  -2.797  1.00 85.25 ?  80  SER A C   1 
606  ATOM   C CB  .  SER A 1 80  ?  -2.346  -1.098  -5.012  1.00 85.25 ?  80  SER A CB  1 
607  ATOM   O O   .  SER A 1 80  ?  -3.836  -2.368  -1.988  1.00 85.25 ?  80  SER A O   1 
608  ATOM   O OG  .  SER A 1 80  ?  -2.597  0.293   -5.137  1.00 85.25 ?  80  SER A OG  1 
609  ATOM   N N   .  PHE A 1 81  ?  -3.039  -0.318  -2.415  1.00 88.12 ?  81  PHE A N   1 
610  ATOM   C CA  .  PHE A 1 81  ?  -2.681  -0.034  -1.029  1.00 88.12 ?  81  PHE A CA  1 
611  ATOM   C C   .  PHE A 1 81  ?  -3.881  0.026   -0.087  1.00 88.12 ?  81  PHE A C   1 
612  ATOM   C CB  .  PHE A 1 81  ?  -1.892  1.278   -0.975  1.00 88.12 ?  81  PHE A CB  1 
613  ATOM   O O   .  PHE A 1 81  ?  -3.92   -0.679  0.921   1.00 88.12 ?  81  PHE A O   1 
614  ATOM   C CG  .  PHE A 1 81  ?  -1.356  1.611   0.389   1.00 88.12 ?  81  PHE A CG  1 
615  ATOM   C CD1 .  PHE A 1 81  ?  -2.043  2.486   1.224   1.00 88.12 ?  81  PHE A CD1 1 
616  ATOM   C CD2 .  PHE A 1 81  ?  -0.155  1.066   0.828   1.00 88.12 ?  81  PHE A CD2 1 
617  ATOM   C CE1 .  PHE A 1 81  ?  -1.547  2.803   2.486   1.00 88.12 ?  81  PHE A CE1 1 
618  ATOM   C CE2 .  PHE A 1 81  ?  0.345   1.369   2.092   1.00 88.12 ?  81  PHE A CE2 1 
619  ATOM   C CZ  .  PHE A 1 81  ?  -0.357  2.233   2.927   1.00 88.12 ?  81  PHE A CZ  1 
620  ATOM   N N   .  ASN A 1 82  ?  -4.856  0.874   -0.397  1.00 91.19 ?  82  ASN A N   1 
621  ATOM   C CA  .  ASN A 1 82  ?  -6.005  1.057   0.484   1.00 91.19 ?  82  ASN A CA  1 
622  ATOM   C C   .  ASN A 1 82  ?  -7.082  0.001   0.252   1.00 91.19 ?  82  ASN A C   1 
623  ATOM   C CB  .  ASN A 1 82  ?  -6.602  2.451   0.283   1.00 91.19 ?  82  ASN A CB  1 
624  ATOM   O O   .  ASN A 1 82  ?  -7.808  -0.362  1.177   1.00 91.19 ?  82  ASN A O   1 
625  ATOM   C CG  .  ASN A 1 82  ?  -5.732  3.546   0.859   1.00 91.19 ?  82  ASN A CG  1 
626  ATOM   N ND2 .  ASN A 1 82  ?  -5.473  4.572   0.063   1.00 91.19 ?  82  ASN A ND2 1 
627  ATOM   O OD1 .  ASN A 1 82  ?  -5.313  3.48    2.011   1.00 91.19 ?  82  ASN A OD1 1 
628  ATOM   N N   .  GLN A 1 83  ?  -7.202  -0.487  -0.979  1.00 90.88 ?  83  GLN A N   1 
629  ATOM   C CA  .  GLN A 1 83  ?  -8.194  -1.513  -1.281  1.00 90.88 ?  83  GLN A CA  1 
630  ATOM   C C   .  GLN A 1 83  ?  -7.883  -2.812  -0.544  1.00 90.88 ?  83  GLN A C   1 
631  ATOM   C CB  .  GLN A 1 83  ?  -8.291  -1.775  -2.787  1.00 90.88 ?  83  GLN A CB  1 
632  ATOM   O O   .  GLN A 1 83  ?  -8.795  -3.487  -0.069  1.00 90.88 ?  83  GLN A O   1 
633  ATOM   C CG  .  GLN A 1 83  ?  -9.451  -2.701  -3.136  1.00 90.88 ?  83  GLN A CG  1 
634  ATOM   C CD  .  GLN A 1 83  ?  -9.778  -2.751  -4.615  1.00 90.88 ?  83  GLN A CD  1 
635  ATOM   N NE2 .  GLN A 1 83  ?  -10.48  -3.797  -5.024  1.00 90.88 ?  83  GLN A NE2 1 
636  ATOM   O OE1 .  GLN A 1 83  ?  -9.427  -1.858  -5.382  1.00 90.88 ?  83  GLN A OE1 1 
637  ATOM   N N   .  SER A 1 84  ?  -6.607  -3.168  -0.439  1.00 91.88 ?  84  SER A N   1 
638  ATOM   C CA  .  SER A 1 84  ?  -6.221  -4.413  0.218   1.00 91.88 ?  84  SER A CA  1 
639  ATOM   C C   .  SER A 1 84  ?  -6.639  -4.45   1.685   1.00 91.88 ?  84  SER A C   1 
640  ATOM   C CB  .  SER A 1 84  ?  -4.712  -4.637  0.1     1.00 91.88 ?  84  SER A CB  1 
641  ATOM   O O   .  SER A 1 84  ?  -7.009  -5.507  2.196   1.00 91.88 ?  84  SER A O   1 
642  ATOM   O OG  .  SER A 1 84  ?  -3.984  -3.63   0.78    1.00 91.88 ?  84  SER A OG  1 
643  ATOM   N N   .  GLY A 1 85  ?  -6.589  -3.306  2.36    1.00 94.69 ?  85  GLY A N   1 
644  ATOM   C CA  .  GLY A 1 85  ?  -6.974  -3.247  3.76    1.00 94.69 ?  85  GLY A CA  1 
645  ATOM   C C   .  GLY A 1 85  ?  -8.474  -3.191  3.975   1.00 94.69 ?  85  GLY A C   1 
646  ATOM   O O   .  GLY A 1 85  ?  -8.981  -3.738  4.953   1.00 94.69 ?  85  GLY A O   1 
647  ATOM   N N   .  TRP A 1 86  ?  -9.192  -2.524  3.078   1.00 93.94 ?  86  TRP A N   1 
648  ATOM   C CA  .  TRP A 1 86  ?  -10.646 -2.43   3.169   1.00 93.94 ?  86  TRP A CA  1 
649  ATOM   C C   .  TRP A 1 86  ?  -11.31  -3.784  2.938   1.00 93.94 ?  86  TRP A C   1 
650  ATOM   C CB  .  TRP A 1 86  ?  -11.156 -1.409  2.149   1.00 93.94 ?  86  TRP A CB  1 
651  ATOM   O O   .  TRP A 1 86  ?  -12.304 -4.126  3.578   1.00 93.94 ?  86  TRP A O   1 
652  ATOM   C CG  .  TRP A 1 86  ?  -12.65  -1.236  2.109   1.00 93.94 ?  86  TRP A CG  1 
653  ATOM   C CD1 .  TRP A 1 86  ?  -13.449 -1.315  1.007   1.00 93.94 ?  86  TRP A CD1 1 
654  ATOM   C CD2 .  TRP A 1 86  ?  -13.536 -0.923  3.196   1.00 93.94 ?  86  TRP A CD2 1 
655  ATOM   C CE2 .  TRP A 1 86  ?  -14.828 -0.738  2.651   1.00 93.94 ?  86  TRP A CE2 1 
656  ATOM   C CE3 .  TRP A 1 86  ?  -13.372 -0.789  4.581   1.00 93.94 ?  86  TRP A CE3 1 
657  ATOM   N NE1 .  TRP A 1 86  ?  -14.752 -1.02   1.314   1.00 93.94 ?  86  TRP A NE1 1 
658  ATOM   C CH2 .  TRP A 1 86  ?  -15.733 -0.231  4.791   1.00 93.94 ?  86  TRP A CH2 1 
659  ATOM   C CZ2 .  TRP A 1 86  ?  -15.921 -0.36   3.438   1.00 93.94 ?  86  TRP A CZ2 1 
660  ATOM   C CZ3 .  TRP A 1 86  ?  -14.47  -0.453  5.371   1.00 93.94 ?  86  TRP A CZ3 1 
661  ATOM   N N   .  GLU A 1 87  ?  -10.74  -4.564  2.027   1.00 92.69 ?  87  GLU A N   1 
662  ATOM   C CA  .  GLU A 1 87  ?  -11.238 -5.903  1.728   1.00 92.69 ?  87  GLU A CA  1 
663  ATOM   C C   .  GLU A 1 87  ?  -11.115 -6.825  2.937   1.00 92.69 ?  87  GLU A C   1 
664  ATOM   C CB  .  GLU A 1 87  ?  -10.474 -6.483  0.536   1.00 92.69 ?  87  GLU A CB  1 
665  ATOM   O O   .  GLU A 1 87  ?  -11.961 -7.693  3.149   1.00 92.69 ?  87  GLU A O   1 
666  ATOM   C CG  .  GLU A 1 87  ?  -10.857 -5.833  -0.786  1.00 92.69 ?  87  GLU A CG  1 
667  ATOM   C CD  .  GLU A 1 87  ?  -10.053 -6.354  -1.96   1.00 92.69 ?  87  GLU A CD  1 
668  ATOM   O OE1 .  GLU A 1 87  ?  -10.572 -6.286  -3.094  1.00 92.69 ?  87  GLU A OE1 1 
669  ATOM   O OE2 .  GLU A 1 87  ?  -8.908  -6.823  -1.784  1.00 92.69 ?  87  GLU A OE2 1 
670  ATOM   N N   .  ALA A 1 88  ?  -10.08  -6.621  3.744   1.00 95.44 ?  88  ALA A N   1 
671  ATOM   C CA  .  ALA A 1 88  ?  -9.884  -7.399  4.963   1.00 95.44 ?  88  ALA A CA  1 
672  ATOM   C C   .  ALA A 1 88  ?  -10.991 -7.142  5.981   1.00 95.44 ?  88  ALA A C   1 
673  ATOM   C CB  .  ALA A 1 88  ?  -8.535  -7.062  5.575   1.00 95.44 ?  88  ALA A CB  1 
674  ATOM   O O   .  ALA A 1 88  ?  -11.432 -8.057  6.676   1.00 95.44 ?  88  ALA A O   1 
675  ATOM   N N   .  VAL A 1 89  ?  -11.431 -5.891  6.07    1.00 95.31 ?  89  VAL A N   1 
676  ATOM   C CA  .  VAL A 1 89  ?  -12.472 -5.484  7.012   1.00 95.31 ?  89  VAL A CA  1 
677  ATOM   C C   .  VAL A 1 89  ?  -13.787 -6.183  6.678   1.00 95.31 ?  89  VAL A C   1 
678  ATOM   C CB  .  VAL A 1 89  ?  -12.684 -3.951  7.003   1.00 95.31 ?  89  VAL A CB  1 
679  ATOM   O O   .  VAL A 1 89  ?  -14.529 -6.592  7.572   1.00 95.31 ?  89  VAL A O   1 
680  ATOM   C CG1 .  VAL A 1 89  ?  -13.833 -3.547  7.922   1.00 95.31 ?  89  VAL A CG1 1 
681  ATOM   C CG2 .  VAL A 1 89  ?  -11.412 -3.231  7.445   1.00 95.31 ?  89  VAL A CG2 1 
682  ATOM   N N   .  HIS A 1 90  ?  -14.08  -6.336  5.392   1.00 90.25 ?  90  HIS A N   1 
683  ATOM   C CA  .  HIS A 1 90  ?  -15.277 -7.053  4.961   1.00 90.25 ?  90  HIS A CA  1 
684  ATOM   C C   .  HIS A 1 90  ?  -15.117 -8.567  5.04    1.00 90.25 ?  90  HIS A C   1 
685  ATOM   C CB  .  HIS A 1 90  ?  -15.639 -6.669  3.525   1.00 90.25 ?  90  HIS A CB  1 
686  ATOM   O O   .  HIS A 1 90  ?  -16.05  -9.267  5.437   1.00 90.25 ?  90  HIS A O   1 
687  ATOM   C CG  .  HIS A 1 90  ?  -16.216 -5.293  3.394   1.00 90.25 ?  90  HIS A CG  1 
688  ATOM   C CD2 .  HIS A 1 90  ?  -16.719 -4.652  2.309   1.00 90.25 ?  90  HIS A CD2 1 
689  ATOM   N ND1 .  HIS A 1 90  ?  -16.408 -4.421  4.443   1.00 90.25 ?  90  HIS A ND1 1 
690  ATOM   C CE1 .  HIS A 1 90  ?  -17.048 -3.344  3.969   1.00 90.25 ?  90  HIS A CE1 1 
691  ATOM   N NE2 .  HIS A 1 90  ?  -17.241 -3.435  2.668   1.00 90.25 ?  90  HIS A NE2 1 
692  ATOM   N N   .  LYS A 1 91  ?  -13.952 -9.074  4.654   1.00 92.38 ?  91  LYS A N   1 
693  ATOM   C CA  .  LYS A 1 91  ?  -13.716 -10.515 4.63    1.00 92.38 ?  91  LYS A CA  1 
694  ATOM   C C   .  LYS A 1 91  ?  -13.79  -11.121 6.026   1.00 92.38 ?  91  LYS A C   1 
695  ATOM   C CB  .  LYS A 1 91  ?  -12.361 -10.818 3.984   1.00 92.38 ?  91  LYS A CB  1 
696  ATOM   O O   .  LYS A 1 91  ?  -14.309 -12.221 6.201   1.00 92.38 ?  91  LYS A O   1 
697  ATOM   C CG  .  LYS A 1 91  ?  -12.205 -12.267 3.55    1.00 92.38 ?  91  LYS A CG  1 
698  ATOM   C CD  .  LYS A 1 91  ?  -10.789 -12.54  3.067   1.00 92.38 ?  91  LYS A CD  1 
699  ATOM   C CE  .  LYS A 1 91  ?  -10.655 -13.927 2.46    1.00 92.38 ?  91  LYS A CE  1 
700  ATOM   N NZ  .  LYS A 1 91  ?  -11.303 -13.953 1.106   1.00 92.38 ?  91  LYS A NZ  1 
701  ATOM   N N   .  ILE A 1 92  ?  -13.281 -10.401 7.02    1.00 95.00 ?  92  ILE A N   1 
702  ATOM   C CA  .  ILE A 1 92  ?  -13.327 -10.884 8.398   1.00 95.00 ?  92  ILE A CA  1 
703  ATOM   C C   .  ILE A 1 92  ?  -14.74  -10.815 8.971   1.00 95.00 ?  92  ILE A C   1 
704  ATOM   C CB  .  ILE A 1 92  ?  -12.318 -10.139 9.308   1.00 95.00 ?  92  ILE A CB  1 
705  ATOM   O O   .  ILE A 1 92  ?  -15.114 -11.641 9.801   1.00 95.00 ?  92  ILE A O   1 
706  ATOM   C CG1 .  ILE A 1 92  ?  -12.094 -10.896 10.621  1.00 95.00 ?  92  ILE A CG1 1 
707  ATOM   C CG2 .  ILE A 1 92  ?  -12.774 -8.719  9.633   1.00 95.00 ?  92  ILE A CG2 1 
708  ATOM   C CD1 .  ILE A 1 92  ?  -11.313 -12.181 10.466  1.00 95.00 ?  92  ILE A CD1 1 
709  ATOM   N N   .  SER A 1 93  ?  -15.536 -9.847  8.528   1.00 92.81 ?  93  SER A N   1 
710  ATOM   C CA  .  SER A 1 93  ?  -16.874 -9.657  9.081   1.00 92.81 ?  93  SER A CA  1 
711  ATOM   C C   .  SER A 1 93  ?  -17.889 -10.654 8.532   1.00 92.81 ?  93  SER A C   1 
712  ATOM   C CB  .  SER A 1 93  ?  -17.356 -8.233  8.808   1.00 92.81 ?  93  SER A CB  1 
713  ATOM   O O   .  SER A 1 93  ?  -18.768 -11.105 9.263   1.00 92.81 ?  93  SER A O   1 
714  ATOM   O OG  .  SER A 1 93  ?  -16.465 -7.298  9.392   1.00 92.81 ?  93  SER A OG  1 
715  ATOM   N N   .  TYR A 1 94  ?  -17.778 -10.99  7.252   1.00 91.38 ?  94  TYR A N   1 
716  ATOM   C CA  .  TYR A 1 94  ?  -18.68  -11.961 6.639   1.00 91.38 ?  94  TYR A CA  1 
717  ATOM   C C   .  TYR A 1 94  ?  -18.491 -13.355 7.231   1.00 91.38 ?  94  TYR A C   1 
718  ATOM   C CB  .  TYR A 1 94  ?  -18.447 -12.011 5.128   1.00 91.38 ?  94  TYR A CB  1 
719  ATOM   O O   .  TYR A 1 94  ?  -19.462 -14.051 7.524   1.00 91.38 ?  94  TYR A O   1 
720  ATOM   C CG  .  TYR A 1 94  ?  -19.262 -13.086 4.442   1.00 91.38 ?  94  TYR A CG  1 
721  ATOM   C CD1 .  TYR A 1 94  ?  -18.693 -14.324 4.143   1.00 91.38 ?  94  TYR A CD1 1 
722  ATOM   C CD2 .  TYR A 1 94  ?  -20.604 -12.879 4.122   1.00 91.38 ?  94  TYR A CD2 1 
723  ATOM   C CE1 .  TYR A 1 94  ?  -19.433 -15.318 3.508   1.00 91.38 ?  94  TYR A CE1 1 
724  ATOM   C CE2 .  TYR A 1 94  ?  -21.354 -13.879 3.504   1.00 91.38 ?  94  TYR A CE2 1 
725  ATOM   O OH  .  TYR A 1 94  ?  -21.486 -16.082 2.576   1.00 91.38 ?  94  TYR A OH  1 
726  ATOM   C CZ  .  TYR A 1 94  ?  -20.76  -15.09  3.192   1.00 91.38 ?  94  TYR A CZ  1 
727  ATOM   N N   .  GLU A 1 95  ?  -17.239 -13.767 7.398   1.00 93.56 ?  95  GLU A N   1 
728  ATOM   C CA  .  GLU A 1 95  ?  -16.92  -15.1   7.905   1.00 93.56 ?  95  GLU A CA  1 
729  ATOM   C C   .  GLU A 1 95  ?  -17.375 -15.295 9.349   1.00 93.56 ?  95  GLU A C   1 
730  ATOM   C CB  .  GLU A 1 95  ?  -15.411 -15.337 7.818   1.00 93.56 ?  95  GLU A CB  1 
731  ATOM   O O   .  GLU A 1 95  ?  -17.622 -16.419 9.783   1.00 93.56 ?  95  GLU A O   1 
732  ATOM   C CG  .  GLU A 1 95  ?  -14.877 -15.403 6.395   1.00 93.56 ?  95  GLU A CG  1 
733  ATOM   C CD  .  GLU A 1 95  ?  -13.37  -15.562 6.354   1.00 93.56 ?  95  GLU A CD  1 
734  ATOM   O OE1 .  GLU A 1 95  ?  -12.78  -15.474 5.256   1.00 93.56 ?  95  GLU A OE1 1 
735  ATOM   O OE2 .  GLU A 1 95  ?  -12.744 -15.786 7.411   1.00 93.56 ?  95  GLU A OE2 1 
736  ATOM   N N   .  LEU A 1 96  ?  -17.494 -14.195 10.085  1.00 93.81 ?  96  LEU A N   1 
737  ATOM   C CA  .  LEU A 1 96  ?  -17.979 -14.216 11.463  1.00 93.81 ?  96  LEU A CA  1 
738  ATOM   C C   .  LEU A 1 96  ?  -19.494 -14.048 11.551  1.00 93.81 ?  96  LEU A C   1 
739  ATOM   C CB  .  LEU A 1 96  ?  -17.305 -13.087 12.247  1.00 93.81 ?  96  LEU A CB  1 
740  ATOM   O O   .  LEU A 1 96  ?  -20.063 -14.077 12.643  1.00 93.81 ?  96  LEU A O   1 
741  ATOM   C CG  .  LEU A 1 96  ?  -15.81  -13.235 12.546  1.00 93.81 ?  96  LEU A CG  1 
742  ATOM   C CD1 .  LEU A 1 96  ?  -15.268 -11.898 13.027  1.00 93.81 ?  96  LEU A CD1 1 
743  ATOM   C CD2 .  LEU A 1 96  ?  -15.565 -14.296 13.612  1.00 93.81 ?  96  LEU A CD2 1 
744  ATOM   N N   .  GLY A 1 97  ?  -20.142 -13.859 10.406  1.00 91.00 ?  97  GLY A N   1 
745  ATOM   C CA  .  GLY A 1 97  ?  -21.578 -13.642 10.364  1.00 91.00 ?  97  GLY A CA  1 
746  ATOM   C C   .  GLY A 1 97  ?  -22.01  -12.27  10.844  1.00 91.00 ?  97  GLY A C   1 
747  ATOM   O O   .  GLY A 1 97  ?  -23.149 -12.086 11.274  1.00 91.00 ?  97  GLY A O   1 
748  ATOM   N N   .  LEU A 1 98  ?  -21.096 -11.306 10.784  1.00 91.50 ?  98  LEU A N   1 
749  ATOM   C CA  .  LEU A 1 98  ?  -21.362 -9.94   11.227  1.00 91.50 ?  98  LEU A CA  1 
750  ATOM   C C   .  LEU A 1 98  ?  -21.881 -9.069  10.085  1.00 91.50 ?  98  LEU A C   1 
751  ATOM   C CB  .  LEU A 1 98  ?  -20.09  -9.316  11.807  1.00 91.50 ?  98  LEU A CB  1 
752  ATOM   O O   .  LEU A 1 98  ?  -22.59  -8.09   10.312  1.00 91.50 ?  98  LEU A O   1 
753  ATOM   C CG  .  LEU A 1 98  ?  -19.419 -10     13.001  1.00 91.50 ?  98  LEU A CG  1 
754  ATOM   C CD1 .  LEU A 1 98  ?  -18.136 -9.254  13.347  1.00 91.50 ?  98  LEU A CD1 1 
755  ATOM   C CD2 .  LEU A 1 98  ?  -20.338 -10.039 14.213  1.00 91.50 ?  98  LEU A CD2 1 
756  ATOM   N N   .  ASP A 1 99  ?  -21.517 -9.422  8.857   1.00 86.94 ?  99  ASP A N   1 
757  ATOM   C CA  .  ASP A 1 99  ?  -22.058 -8.783  7.662   1.00 86.94 ?  99  ASP A CA  1 
758  ATOM   C C   .  ASP A 1 99  ?  -22.662 -9.832  6.733   1.00 86.94 ?  99  ASP A C   1 
759  ATOM   C CB  .  ASP A 1 99  ?  -20.969 -8.02   6.904   1.00 86.94 ?  99  ASP A CB  1 
760  ATOM   O O   .  ASP A 1 99  ?  -22.046 -10.861 6.454   1.00 86.94 ?  99  ASP A O   1 
761  ATOM   C CG  .  ASP A 1 99  ?  -20.777 -6.608  7.422   1.00 86.94 ?  99  ASP A CG  1 
762  ATOM   O OD1 .  ASP A 1 99  ?  -21.776 -5.864  7.518   1.00 86.94 ?  99  ASP A OD1 1 
763  ATOM   O OD2 .  ASP A 1 99  ?  -19.627 -6.216  7.715   1.00 86.94 ?  99  ASP A OD2 1 
764  ATOM   N N   .  LYS A 1 100 ?  -23.864 -9.559  6.236   1.00 74.12 ?  100 LYS A N   1 
765  ATOM   C CA  .  LYS A 1 100 ?  -24.513 -10.439 5.268   1.00 74.12 ?  100 LYS A CA  1 
766  ATOM   C C   .  LYS A 1 100 ?  -24.207 -9.943  3.859   1.00 74.12 ?  100 LYS A C   1 
767  ATOM   C CB  .  LYS A 1 100 ?  -26.029 -10.485 5.483   1.00 74.12 ?  100 LYS A CB  1 
768  ATOM   O O   .  LYS A 1 100 ?  -24.736 -8.922  3.422   1.00 74.12 ?  100 LYS A O   1 
769  ATOM   C CG  .  LYS A 1 100 ?  -26.452 -11.102 6.81    1.00 74.12 ?  100 LYS A CG  1 
770  ATOM   C CD  .  LYS A 1 100 ?  -27.967 -11.219 6.906   1.00 74.12 ?  100 LYS A CD  1 
771  ATOM   C CE  .  LYS A 1 100 ?  -28.39  -11.804 8.244   1.00 74.12 ?  100 LYS A CE  1 
772  ATOM   N NZ  .  LYS A 1 100 ?  -29.884 -11.938 8.284   1.00 74.12 ?  100 LYS A NZ  1 
773  ATOM   N N   .  ALA A 1 101 ?  -23.343 -10.665 3.156   1.00 62.78 ?  101 ALA A N   1 
774  ATOM   C CA  .  ALA A 1 101 ?  -23.024 -10.327 1.773   1.00 62.78 ?  101 ALA A CA  1 
775  ATOM   C C   .  ALA A 1 101 ?  -24.291 -10.44  0.931   1.00 62.78 ?  101 ALA A C   1 
776  ATOM   C CB  .  ALA A 1 101 ?  -21.943 -11.25  1.23    1.00 62.78 ?  101 ALA A CB  1 
777  ATOM   O O   .  ALA A 1 101 ?  -25.208 -11.193 1.26    1.00 62.78 ?  101 ALA A O   1 
778  ATOM   N N   .  GLN A 1 102 ?  -24.341 -9.678  -0.155  1.00 62.91 ?  102 GLN A N   1 
779  ATOM   C CA  .  GLN A 1 102 ?  -25.491 -9.673  -1.053  1.00 62.91 ?  102 GLN A CA  1 
780  ATOM   C C   .  GLN A 1 102 ?  -24.987 -9.955  -2.465  1.00 62.91 ?  102 GLN A C   1 
781  ATOM   C CB  .  GLN A 1 102 ?  -26.213 -8.325  -0.989  1.00 62.91 ?  102 GLN A CB  1 
782  ATOM   O O   .  GLN A 1 102 ?  -23.784 -9.897  -2.717  1.00 62.91 ?  102 GLN A O   1 
783  ATOM   C CG  .  GLN A 1 102 ?  -26.776 -7.994  0.387   1.00 62.91 ?  102 GLN A CG  1 
784  ATOM   C CD  .  GLN A 1 102 ?  -27.655 -6.759  0.371   1.00 62.91 ?  102 GLN A CD  1 
785  ATOM   N NE2 .  GLN A 1 102 ?  -28.794 -6.835  1.042   1.00 62.91 ?  102 GLN A NE2 1 
786  ATOM   O OE1 .  GLN A 1 102 ?  -27.324 -5.75   -0.246  1.00 62.91 ?  102 GLN A OE1 1 
787  ATOM   N N   .  VAL A 1 103 ?  -25.901 -10.27  -3.377  1.00 51.81 ?  103 VAL A N   1 
788  ATOM   C CA  .  VAL A 1 103 ?  -25.535 -10.617 -4.75   1.00 51.81 ?  103 VAL A CA  1 
789  ATOM   C C   .  VAL A 1 103 ?  -24.629 -9.557  -5.37   1.00 51.81 ?  103 VAL A C   1 
790  ATOM   C CB  .  VAL A 1 103 ?  -26.777 -10.82  -5.649  1.00 51.81 ?  103 VAL A CB  1 
791  ATOM   O O   .  VAL A 1 103 ?  -23.678 -9.892  -6.077  1.00 51.81 ?  103 VAL A O   1 
792  ATOM   C CG1 .  VAL A 1 103 ?  -26.373 -11.19  -7.073  1.00 51.81 ?  103 VAL A CG1 1 
793  ATOM   C CG2 .  VAL A 1 103 ?  -27.681 -11.91  -5.073  1.00 51.81 ?  103 VAL A CG2 1 
794  ATOM   N N   .  SER A 1 104 ?  -24.903 -8.286  -5.095  1.00 54.16 ?  104 SER A N   1 
795  ATOM   C CA  .  SER A 1 104 ?  -24.074 -7.197  -5.602  1.00 54.16 ?  104 SER A CA  1 
796  ATOM   C C   .  SER A 1 104 ?  -24.066 -5.982  -4.679  1.00 54.16 ?  104 SER A C   1 
797  ATOM   C CB  .  SER A 1 104 ?  -24.583 -6.771  -6.981  1.00 54.16 ?  104 SER A CB  1 
798  ATOM   O O   .  SER A 1 104 ?  -25.095 -5.333  -4.488  1.00 54.16 ?  104 SER A O   1 
799  ATOM   O OG  .  SER A 1 104 ?  -25.923 -6.315  -6.9    1.00 54.16 ?  104 SER A OG  1 
800  ATOM   N N   .  GLY A 1 105 ?  -22.897 -5.659  -4.136  1.00 58.34 ?  105 GLY A N   1 
801  ATOM   C CA  .  GLY A 1 105 ?  -22.687 -4.373  -3.494  1.00 58.34 ?  105 GLY A CA  1 
802  ATOM   C C   .  GLY A 1 105 ?  -23.57  -4.049  -2.304  1.00 58.34 ?  105 GLY A C   1 
803  ATOM   O O   .  GLY A 1 105 ?  -24.346 -3.096  -2.363  1.00 58.34 ?  105 GLY A O   1 
804  ATOM   N N   .  ASN A 1 106 ?  -23.445 -4.805  -1.217  1.00 62.78 ?  106 ASN A N   1 
805  ATOM   C CA  .  ASN A 1 106 ?  -24.223 -4.53   -0.013  1.00 62.78 ?  106 ASN A CA  1 
806  ATOM   C C   .  ASN A 1 106 ?  -24.003 -3.097  0.467   1.00 62.78 ?  106 ASN A C   1 
807  ATOM   C CB  .  ASN A 1 106 ?  -23.848 -5.496  1.114   1.00 62.78 ?  106 ASN A CB  1 
808  ATOM   O O   .  ASN A 1 106 ?  -22.868 -2.64   0.6     1.00 62.78 ?  106 ASN A O   1 
809  ATOM   C CG  .  ASN A 1 106 ?  -24.7   -5.298  2.351   1.00 62.78 ?  106 ASN A CG  1 
810  ATOM   N ND2 .  ASN A 1 106 ?  -24.123 -5.564  3.511   1.00 62.78 ?  106 ASN A ND2 1 
811  ATOM   O OD1 .  ASN A 1 106 ?  -25.86  -4.898  2.271   1.00 62.78 ?  106 ASN A OD1 1 
812  ATOM   N N   .  LYS A 1 107 ?  -25.103 -2.402  0.735   1.00 64.62 ?  107 LYS A N   1 
813  ATOM   C CA  .  LYS A 1 107 ?  -25.069 -1.004  1.16    1.00 64.62 ?  107 LYS A CA  1 
814  ATOM   C C   .  LYS A 1 107 ?  -25.247 -0.833  2.665   1.00 64.62 ?  107 LYS A C   1 
815  ATOM   C CB  .  LYS A 1 107 ?  -26.166 -0.216  0.437   1.00 64.62 ?  107 LYS A CB  1 
816  ATOM   O O   .  LYS A 1 107 ?  -24.932 0.219   3.218   1.00 64.62 ?  107 LYS A O   1 
817  ATOM   C CG  .  LYS A 1 107 ?  -26.039 -0.218  -1.082  1.00 64.62 ?  107 LYS A CG  1 
818  ATOM   C CD  .  LYS A 1 107 ?  -27.156 0.583   -1.735  1.00 64.62 ?  107 LYS A CD  1 
819  ATOM   C CE  .  LYS A 1 107 ?  -27.085 0.479   -3.25   1.00 64.62 ?  107 LYS A CE  1 
820  ATOM   N NZ  .  LYS A 1 107 ?  -28.238 1.221   -3.857  1.00 64.62 ?  107 LYS A NZ  1 
821  ATOM   N N   .  ASN A 1 108 ?  -25.758 -1.87   3.32    1.00 74.31 ?  108 ASN A N   1 
822  ATOM   C CA  .  ASN A 1 108 ?  -26.053 -1.829  4.75    1.00 74.31 ?  108 ASN A CA  1 
823  ATOM   C C   .  ASN A 1 108 ?  -24.933 -2.504  5.537   1.00 74.31 ?  108 ASN A C   1 
824  ATOM   C CB  .  ASN A 1 108 ?  -27.398 -2.51   5.015   1.00 74.31 ?  108 ASN A CB  1 
825  ATOM   O O   .  ASN A 1 108 ?  -25.151 -3.449  6.295   1.00 74.31 ?  108 ASN A O   1 
826  ATOM   C CG  .  ASN A 1 108 ?  -28.56  -1.74   4.427   1.00 74.31 ?  108 ASN A CG  1 
827  ATOM   N ND2 .  ASN A 1 108 ?  -29.386 -2.42   3.647   1.00 74.31 ?  108 ASN A ND2 1 
828  ATOM   O OD1 .  ASN A 1 108 ?  -28.712 -0.545  4.664   1.00 74.31 ?  108 ASN A OD1 1 
829  ATOM   N N   .  LEU A 1 109 ?  -23.719 -2.006  5.33    1.00 81.31 ?  109 LEU A N   1 
830  ATOM   C CA  .  LEU A 1 109 ?  -22.526 -2.55   5.972   1.00 81.31 ?  109 LEU A CA  1 
831  ATOM   C C   .  LEU A 1 109 ?  -22.333 -1.921  7.348   1.00 81.31 ?  109 LEU A C   1 
832  ATOM   C CB  .  LEU A 1 109 ?  -21.307 -2.253  5.094   1.00 81.31 ?  109 LEU A CB  1 
833  ATOM   O O   .  LEU A 1 109 ?  -22.31  -0.698  7.48    1.00 81.31 ?  109 LEU A O   1 
834  ATOM   C CG  .  LEU A 1 109 ?  -21.27  -2.945  3.728   1.00 81.31 ?  109 LEU A CG  1 
835  ATOM   C CD1 .  LEU A 1 109 ?  -20.389 -2.144  2.782   1.00 81.31 ?  109 LEU A CD1 1 
836  ATOM   C CD2 .  LEU A 1 109 ?  -20.769 -4.379  3.866   1.00 81.31 ?  109 LEU A CD2 1 
837  ATOM   N N   .  ARG A 1 110 ?  -22.183 -2.753  8.373   1.00 89.25 ?  110 ARG A N   1 
838  ATOM   C CA  .  ARG A 1 110 ?  -21.932 -2.265  9.729   1.00 89.25 ?  110 ARG A CA  1 
839  ATOM   C C   .  ARG A 1 110 ?  -20.627 -1.482  9.824   1.00 89.25 ?  110 ARG A C   1 
840  ATOM   C CB  .  ARG A 1 110 ?  -21.928 -3.422  10.734  1.00 89.25 ?  110 ARG A CB  1 
841  ATOM   O O   .  ARG A 1 110 ?  -20.512 -0.55   10.617  1.00 89.25 ?  110 ARG A O   1 
842  ATOM   C CG  .  ARG A 1 110 ?  -20.801 -4.43   10.54   1.00 89.25 ?  110 ARG A CG  1 
843  ATOM   C CD  .  ARG A 1 110 ?  -20.952 -5.638  11.446  1.00 89.25 ?  110 ARG A CD  1 
844  ATOM   N NE  .  ARG A 1 110 ?  -20.633 -5.324  12.839  1.00 89.25 ?  110 ARG A NE  1 
845  ATOM   N NH1 .  ARG A 1 110 ?  -22.18  -6.762  13.806  1.00 89.25 ?  110 ARG A NH1 1 
846  ATOM   N NH2 .  ARG A 1 110 ?  -20.801 -5.511  15.096  1.00 89.25 ?  110 ARG A NH2 1 
847  ATOM   C CZ  .  ARG A 1 110 ?  -21.21  -5.874  13.9    1.00 89.25 ?  110 ARG A CZ  1 
848  ATOM   N N   .  ASN A 1 111 ?  -19.647 -1.875  9.019   1.00 92.81 ?  111 ASN A N   1 
849  ATOM   C CA  .  ASN A 1 111 ?  -18.333 -1.242  9.028   1.00 92.81 ?  111 ASN A CA  1 
850  ATOM   C C   .  ASN A 1 111 ?  -18.276 -0.229  7.888   1.00 92.81 ?  111 ASN A C   1 
851  ATOM   C CB  .  ASN A 1 111 ?  -17.242 -2.303  8.868   1.00 92.81 ?  111 ASN A CB  1 
852  ATOM   O O   .  ASN A 1 111 ?  -18.68  -0.534  6.765   1.00 92.81 ?  111 ASN A O   1 
853  ATOM   C CG  .  ASN A 1 111 ?  -17.201 -3.271  10.031  1.00 92.81 ?  111 ASN A CG  1 
854  ATOM   N ND2 .  ASN A 1 111 ?  -16.793 -4.497  9.753   1.00 92.81 ?  111 ASN A ND2 1 
855  ATOM   O OD1 .  ASN A 1 111 ?  -17.539 -2.933  11.163  1.00 92.81 ?  111 ASN A OD1 1 
856  ATOM   N N   .  LYS A 1 112 ?  -17.785 0.97    8.183   1.00 93.31 ?  112 LYS A N   1 
857  ATOM   C CA  .  LYS A 1 112 ?  -17.783 2.065   7.215   1.00 93.31 ?  112 LYS A CA  1 
858  ATOM   C C   .  LYS A 1 112 ?  -16.366 2.504   6.866   1.00 93.31 ?  112 LYS A C   1 
859  ATOM   C CB  .  LYS A 1 112 ?  -18.572 3.262   7.758   1.00 93.31 ?  112 LYS A CB  1 
860  ATOM   O O   .  LYS A 1 112 ?  -15.421 2.272   7.62    1.00 93.31 ?  112 LYS A O   1 
861  ATOM   C CG  .  LYS A 1 112 ?  -20.033 2.99    8.109   1.00 93.31 ?  112 LYS A CG  1 
862  ATOM   C CD  .  LYS A 1 112 ?  -20.874 2.557   6.916   1.00 93.31 ?  112 LYS A CD  1 
863  ATOM   C CE  .  LYS A 1 112 ?  -22.35  2.531   7.279   1.00 93.31 ?  112 LYS A CE  1 
864  ATOM   N NZ  .  LYS A 1 112 ?  -23.14  1.997   6.123   1.00 93.31 ?  112 LYS A NZ  1 
865  ATOM   N N   .  VAL A 1 113 ?  -16.249 3.151   5.712   1.00 94.38 ?  113 VAL A N   1 
866  ATOM   C CA  .  VAL A 1 113 ?  -14.977 3.665   5.21    1.00 94.38 ?  113 VAL A CA  1 
867  ATOM   C C   .  VAL A 1 113 ?  -15.049 5.186   5.159   1.00 94.38 ?  113 VAL A C   1 
868  ATOM   C CB  .  VAL A 1 113 ?  -14.622 3.097   3.814   1.00 94.38 ?  113 VAL A CB  1 
869  ATOM   O O   .  VAL A 1 113 ?  -16.079 5.761   4.808   1.00 94.38 ?  113 VAL A O   1 
870  ATOM   C CG1 .  VAL A 1 113 ?  -15.677 3.442   2.766   1.00 94.38 ?  113 VAL A CG1 1 
871  ATOM   C CG2 .  VAL A 1 113 ?  -13.246 3.568   3.356   1.00 94.38 ?  113 VAL A CG2 1 
872  ATOM   N N   .  TYR A 1 114 ?  -13.948 5.832   5.525   1.00 95.38 ?  114 TYR A N   1 
873  ATOM   C CA  .  TYR A 1 114 ?  -13.813 7.277   5.386   1.00 95.38 ?  114 TYR A CA  1 
874  ATOM   C C   .  TYR A 1 114 ?  -12.653 7.533   4.428   1.00 95.38 ?  114 TYR A C   1 
875  ATOM   C CB  .  TYR A 1 114 ?  -13.536 7.938   6.738   1.00 95.38 ?  114 TYR A CB  1 
876  ATOM   O O   .  TYR A 1 114 ?  -11.571 6.966   4.582   1.00 95.38 ?  114 TYR A O   1 
877  ATOM   C CG  .  TYR A 1 114 ?  -14.621 7.725   7.774   1.00 95.38 ?  114 TYR A CG  1 
878  ATOM   C CD1 .  TYR A 1 114 ?  -15.659 8.646   7.919   1.00 95.38 ?  114 TYR A CD1 1 
879  ATOM   C CD2 .  TYR A 1 114 ?  -14.604 6.61    8.615   1.00 95.38 ?  114 TYR A CD2 1 
880  ATOM   C CE1 .  TYR A 1 114 ?  -16.646 8.467   8.888   1.00 95.38 ?  114 TYR A CE1 1 
881  ATOM   C CE2 .  TYR A 1 114 ?  -15.586 6.43    9.587   1.00 95.38 ?  114 TYR A CE2 1 
882  ATOM   O OH  .  TYR A 1 114 ?  -17.546 7.198   10.707  1.00 95.38 ?  114 TYR A OH  1 
883  ATOM   C CZ  .  TYR A 1 114 ?  -16.594 7.368   9.729   1.00 95.38 ?  114 TYR A CZ  1 
884  ATOM   N N   .  GLU A 1 115 ?  -12.892 8.375   3.43    1.00 93.75 ?  115 GLU A N   1 
885  ATOM   C CA  .  GLU A 1 115 ?  -11.883 8.715   2.43    1.00 93.75 ?  115 GLU A CA  1 
886  ATOM   C C   .  GLU A 1 115 ?  -11.65  10.223  2.494   1.00 93.75 ?  115 GLU A C   1 
887  ATOM   C CB  .  GLU A 1 115 ?  -12.349 8.303   1.03    1.00 93.75 ?  115 GLU A CB  1 
888  ATOM   O O   .  GLU A 1 115 ?  -12.205 10.982  1.698   1.00 93.75 ?  115 GLU A O   1 
889  ATOM   C CG  .  GLU A 1 115 ?  -12.569 6.805   0.864   1.00 93.75 ?  115 GLU A CG  1 
890  ATOM   C CD  .  GLU A 1 115 ?  -12.932 6.44    -0.562  1.00 93.75 ?  115 GLU A CD  1 
891  ATOM   O OE1 .  GLU A 1 115 ?  -12.243 5.578   -1.149  1.00 93.75 ?  115 GLU A OE1 1 
892  ATOM   O OE2 .  GLU A 1 115 ?  -13.895 7.013   -1.114  1.00 93.75 ?  115 GLU A OE2 1 
893  ATOM   N N   .  PRO A 1 116 ?  -10.86  10.686  3.476   1.00 91.50 ?  116 PRO A N   1 
894  ATOM   C CA  .  PRO A 1 116 ?  -10.743 12.143  3.598   1.00 91.50 ?  116 PRO A CA  1 
895  ATOM   C C   .  PRO A 1 116 ?  -9.957  12.815  2.477   1.00 91.50 ?  116 PRO A C   1 
896  ATOM   C CB  .  PRO A 1 116 ?  -10.023 12.318  4.937   1.00 91.50 ?  116 PRO A CB  1 
897  ATOM   O O   .  PRO A 1 116 ?  -8.941  12.307  2       1.00 91.50 ?  116 PRO A O   1 
898  ATOM   C CG  .  PRO A 1 116 ?  -9.21   11.079  5.078   1.00 91.50 ?  116 PRO A CG  1 
899  ATOM   C CD  .  PRO A 1 116 ?  -10.081 9.991   4.516   1.00 91.50 ?  116 PRO A CD  1 
900  ATOM   N N   .  LYS A 1 117 ?  -10.427 13.993  2.081   1.00 87.06 ?  117 LYS A N   1 
901  ATOM   C CA  .  LYS A 1 117 ?  -9.654  14.875  1.212   1.00 87.06 ?  117 LYS A CA  1 
902  ATOM   C C   .  LYS A 1 117 ?  -8.502  15.424  2.049   1.00 87.06 ?  117 LYS A C   1 
903  ATOM   C CB  .  LYS A 1 117 ?  -10.534 16.007  0.673   1.00 87.06 ?  117 LYS A CB  1 
904  ATOM   O O   .  LYS A 1 117 ?  -8.541  15.368  3.278   1.00 87.06 ?  117 LYS A O   1 
905  ATOM   C CG  .  LYS A 1 117 ?  -11.715 15.518  -0.158  1.00 87.06 ?  117 LYS A CG  1 
906  ATOM   C CD  .  LYS A 1 117 ?  -12.552 16.671  -0.693  1.00 87.06 ?  117 LYS A CD  1 
907  ATOM   C CE  .  LYS A 1 117 ?  -13.763 16.148  -1.449  1.00 87.06 ?  117 LYS A CE  1 
908  ATOM   N NZ  .  LYS A 1 117 ?  -14.549 17.299  -2.005  1.00 87.06 ?  117 LYS A NZ  1 
909  ATOM   N N   .  LYS A 1 118 ?  -7.479  15.966  1.397   1.00 82.56 ?  118 LYS A N   1 
910  ATOM   C CA  .  LYS A 1 118 ?  -6.335  16.52   2.118   1.00 82.56 ?  118 LYS A CA  1 
911  ATOM   C C   .  LYS A 1 118 ?  -6.833  17.536  3.142   1.00 82.56 ?  118 LYS A C   1 
912  ATOM   C CB  .  LYS A 1 118 ?  -5.357  17.176  1.138   1.00 82.56 ?  118 LYS A CB  1 
913  ATOM   O O   .  LYS A 1 118 ?  -7.561  18.464  2.796   1.00 82.56 ?  118 LYS A O   1 
914  ATOM   C CG  .  LYS A 1 118 ?  -4.053  17.632  1.776   1.00 82.56 ?  118 LYS A CG  1 
915  ATOM   C CD  .  LYS A 1 118 ?  -3.163  18.337  0.763   1.00 82.56 ?  118 LYS A CD  1 
916  ATOM   C CE  .  LYS A 1 118 ?  -1.839  18.742  1.39    1.00 82.56 ?  118 LYS A CE  1 
917  ATOM   N NZ  .  LYS A 1 118 ?  -1.028  19.488  0.373   1.00 82.56 ?  118 LYS A NZ  1 
918  ATOM   N N   .  GLY A 1 119 ?  -6.446  17.342  4.398   1.00 86.94 ?  119 GLY A N   1 
919  ATOM   C CA  .  GLY A 1 119 ?  -6.875  18.22   5.474   1.00 86.94 ?  119 GLY A CA  1 
920  ATOM   C C   .  GLY A 1 119 ?  -8.084  17.748  6.261   1.00 86.94 ?  119 GLY A C   1 
921  ATOM   O O   .  GLY A 1 119 ?  -8.302  18.203  7.382   1.00 86.94 ?  119 GLY A O   1 
922  ATOM   N N   .  GLU A 1 120 ?  -8.87   16.833  5.703   1.00 93.62 ?  120 GLU A N   1 
923  ATOM   C CA  .  GLU A 1 120 ?  -10.089 16.351  6.35    1.00 93.62 ?  120 GLU A CA  1 
924  ATOM   C C   .  GLU A 1 120 ?  -9.828  15.126  7.225   1.00 93.62 ?  120 GLU A C   1 
925  ATOM   C CB  .  GLU A 1 120 ?  -11.144 15.997  5.299   1.00 93.62 ?  120 GLU A CB  1 
926  ATOM   O O   .  GLU A 1 120 ?  -10.754 14.511  7.752   1.00 93.62 ?  120 GLU A O   1 
927  ATOM   C CG  .  GLU A 1 120 ?  -11.616 17.177  4.461   1.00 93.62 ?  120 GLU A CG  1 
928  ATOM   C CD  .  GLU A 1 120 ?  -12.668 16.777  3.443   1.00 93.62 ?  120 GLU A CD  1 
929  ATOM   O OE1 .  GLU A 1 120 ?  -13.238 17.675  2.788   1.00 93.62 ?  120 GLU A OE1 1 
930  ATOM   O OE2 .  GLU A 1 120 ?  -12.92  15.565  3.266   1.00 93.62 ?  120 GLU A OE2 1 
931  ATOM   N N   .  LEU A 1 121 ?  -8.555  14.784  7.388   1.00 95.69 ?  121 LEU A N   1 
932  ATOM   C CA  .  LEU A 1 121 ?  -8.145  13.63   8.183   1.00 95.69 ?  121 LEU A CA  1 
933  ATOM   C C   .  LEU A 1 121 ?  -8.653  13.729  9.618   1.00 95.69 ?  121 LEU A C   1 
934  ATOM   C CB  .  LEU A 1 121 ?  -6.617  13.534  8.192   1.00 95.69 ?  121 LEU A CB  1 
935  ATOM   O O   .  LEU A 1 121 ?  -9.096  12.736  10.194  1.00 95.69 ?  121 LEU A O   1 
936  ATOM   C CG  .  LEU A 1 121 ?  -5.945  12.872  6.985   1.00 95.69 ?  121 LEU A CG  1 
937  ATOM   C CD1 .  LEU A 1 121 ?  -4.483  13.292  6.915   1.00 95.69 ?  121 LEU A CD1 1 
938  ATOM   C CD2 .  LEU A 1 121 ?  -6.041  11.359  7.11    1.00 95.69 ?  121 LEU A CD2 1 
939  ATOM   N N   .  ALA A 1 122 ?  -8.596  14.929  10.184  1.00 95.56 ?  122 ALA A N   1 
940  ATOM   C CA  .  ALA A 1 122 ?  -9.031  15.154  11.559  1.00 95.56 ?  122 ALA A CA  1 
941  ATOM   C C   .  ALA A 1 122 ?  -10.52  14.858  11.731  1.00 95.56 ?  122 ALA A C   1 
942  ATOM   C CB  .  ALA A 1 122 ?  -8.728  16.587  11.975  1.00 95.56 ?  122 ALA A CB  1 
943  ATOM   O O   .  ALA A 1 122 ?  -10.94  14.329  12.76   1.00 95.56 ?  122 ALA A O   1 
944  ATOM   N N   .  SER A 1 123 ?  -11.316 15.188  10.719  1.00 96.38 ?  123 SER A N   1 
945  ATOM   C CA  .  SER A 1 123 ?  -12.763 15.003  10.782  1.00 96.38 ?  123 SER A CA  1 
946  ATOM   C C   .  SER A 1 123 ?  -13.15  13.529  10.712  1.00 96.38 ?  123 SER A C   1 
947  ATOM   C CB  .  SER A 1 123 ?  -13.442 15.756  9.637   1.00 96.38 ?  123 SER A CB  1 
948  ATOM   O O   .  SER A 1 123 ?  -14.135 13.111  11.319  1.00 96.38 ?  123 SER A O   1 
949  ATOM   O OG  .  SER A 1 123 ?  -13.173 17.145  9.726   1.00 96.38 ?  123 SER A OG  1 
950  ATOM   N N   .  SER A 1 124 ?  -12.372 12.737  9.983   1.00 97.44 ?  124 SER A N   1 
951  ATOM   C CA  .  SER A 1 124 ?  -12.649 11.311  9.847   1.00 97.44 ?  124 SER A CA  1 
952  ATOM   C C   .  SER A 1 124 ?  -12.458 10.576  11.17   1.00 97.44 ?  124 SER A C   1 
953  ATOM   C CB  .  SER A 1 124 ?  -11.754 10.689  8.774   1.00 97.44 ?  124 SER A CB  1 
954  ATOM   O O   .  SER A 1 124 ?  -13.22  9.662   11.483  1.00 97.44 ?  124 SER A O   1 
955  ATOM   O OG  .  SER A 1 124 ?  -12.041 11.252  7.506   1.00 97.44 ?  124 SER A OG  1 
956  ATOM   N N   .  TYR A 1 125 ?  -11.461 10.973  11.954  1.00 97.81 ?  125 TYR A N   1 
957  ATOM   C CA  .  TYR A 1 125 ?  -11.256 10.366  13.265  1.00 97.81 ?  125 TYR A CA  1 
958  ATOM   C C   .  TYR A 1 125 ?  -12.449 10.686  14.16   1.00 97.81 ?  125 TYR A C   1 
959  ATOM   C CB  .  TYR A 1 125 ?  -9.986  10.876  13.953  1.00 97.81 ?  125 TYR A CB  1 
960  ATOM   O O   .  TYR A 1 125 ?  -12.985 9.807   14.834  1.00 97.81 ?  125 TYR A O   1 
961  ATOM   C CG  .  TYR A 1 125 ?  -8.728  10.875  13.111  1.00 97.81 ?  125 TYR A CG  1 
962  ATOM   C CD1 .  TYR A 1 125 ?  -8.372  9.778   12.324  1.00 97.81 ?  125 TYR A CD1 1 
963  ATOM   C CD2 .  TYR A 1 125 ?  -7.882  11.983  13.122  1.00 97.81 ?  125 TYR A CD2 1 
964  ATOM   C CE1 .  TYR A 1 125 ?  -7.23   9.813   11.526  1.00 97.81 ?  125 TYR A CE1 1 
965  ATOM   C CE2 .  TYR A 1 125 ?  -6.737  12.019  12.332  1.00 97.81 ?  125 TYR A CE2 1 
966  ATOM   O OH  .  TYR A 1 125 ?  -5.277  10.975  10.768  1.00 97.81 ?  125 TYR A OH  1 
967  ATOM   C CZ  .  TYR A 1 125 ?  -6.416  10.934  11.537  1.00 97.81 ?  125 TYR A CZ  1 
968  ATOM   N N   .  LYS A 1 126 ?  -12.852 11.952  14.171  1.00 97.94 ?  126 LYS A N   1 
969  ATOM   C CA  .  LYS A 1 126 ?  -13.946 12.416  15.021  1.00 97.94 ?  126 LYS A CA  1 
970  ATOM   C C   .  LYS A 1 126 ?  -15.247 11.696  14.691  1.00 97.94 ?  126 LYS A C   1 
971  ATOM   C CB  .  LYS A 1 126 ?  -14.137 13.928  14.866  1.00 97.94 ?  126 LYS A CB  1 
972  ATOM   O O   .  LYS A 1 126 ?  -15.965 11.269  15.593  1.00 97.94 ?  126 LYS A O   1 
973  ATOM   C CG  .  LYS A 1 126 ?  -12.964 14.75   15.384  1.00 97.94 ?  126 LYS A CG  1 
974  ATOM   C CD  .  LYS A 1 126 ?  -13.196 16.24   15.179  1.00 97.94 ?  126 LYS A CD  1 
975  ATOM   C CE  .  LYS A 1 126 ?  -11.99  17.036  15.648  1.00 97.94 ?  126 LYS A CE  1 
976  ATOM   N NZ  .  LYS A 1 126 ?  -12.242 18.505  15.473  1.00 97.94 ?  126 LYS A NZ  1 
977  ATOM   N N   .  ASN A 1 127 ?  -15.539 11.556  13.403  1.00 97.94 ?  127 ASN A N   1 
978  ATOM   C CA  .  ASN A 1 127 ?  -16.75  10.871  12.964  1.00 97.94 ?  127 ASN A CA  1 
979  ATOM   C C   .  ASN A 1 127 ?  -16.725 9.392   13.341  1.00 97.94 ?  127 ASN A C   1 
980  ATOM   C CB  .  ASN A 1 127 ?  -16.921 11.015  11.45   1.00 97.94 ?  127 ASN A CB  1 
981  ATOM   O O   .  ASN A 1 127 ?  -17.761 8.82    13.675  1.00 97.94 ?  127 ASN A O   1 
982  ATOM   C CG  .  ASN A 1 127 ?  -17.317 12.416  11.037  1.00 97.94 ?  127 ASN A CG  1 
983  ATOM   N ND2 .  ASN A 1 127 ?  -16.845 12.844  9.876   1.00 97.94 ?  127 ASN A ND2 1 
984  ATOM   O OD1 .  ASN A 1 127 ?  -18.055 13.101  11.741  1.00 97.94 ?  127 ASN A OD1 1 
985  ATOM   N N   .  ALA A 1 128 ?  -15.554 8.766   13.278  1.00 98.06 ?  128 ALA A N   1 
986  ATOM   C CA  .  ALA A 1 128 ?  -15.415 7.359   13.643  1.00 98.06 ?  128 ALA A CA  1 
987  ATOM   C C   .  ALA A 1 128 ?  -15.553 7.141   15.149  1.00 98.06 ?  128 ALA A C   1 
988  ATOM   C CB  .  ALA A 1 128 ?  -14.074 6.825   13.157  1.00 98.06 ?  128 ALA A CB  1 
989  ATOM   O O   .  ALA A 1 128 ?  -16.111 6.138   15.594  1.00 98.06 ?  128 ALA A O   1 
990  ATOM   N N   .  ILE A 1 129 ?  -15.032 8.079   15.932  1.00 98.25 ?  129 ILE A N   1 
991  ATOM   C CA  .  ILE A 1 129 ?  -15.112 8.026   17.39   1.00 98.25 ?  129 ILE A CA  1 
992  ATOM   C C   .  ILE A 1 129 ?  -16.543 8.285   17.856  1.00 98.25 ?  129 ILE A C   1 
993  ATOM   C CB  .  ILE A 1 129 ?  -14.156 9.058   18.035  1.00 98.25 ?  129 ILE A CB  1 
994  ATOM   O O   .  ILE A 1 129 ?  -17.034 7.612   18.762  1.00 98.25 ?  129 ILE A O   1 
995  ATOM   C CG1 .  ILE A 1 129 ?  -12.696 8.686   17.747  1.00 98.25 ?  129 ILE A CG1 1 
996  ATOM   C CG2 .  ILE A 1 129 ?  -14.378 9.145   19.543  1.00 98.25 ?  129 ILE A CG2 1 
997  ATOM   C CD1 .  ILE A 1 129 ?  -11.716 9.833   17.904  1.00 98.25 ?  129 ILE A CD1 1 
998  ATOM   N N   .  ASP A 1 130 ?  -17.217 9.246   17.234  1.00 98.00 ?  130 ASP A N   1 
999  ATOM   C CA  .  ASP A 1 130 ?  -18.597 9.574   17.583  1.00 98.00 ?  130 ASP A CA  1 
1000 ATOM   C C   .  ASP A 1 130 ?  -19.575 8.48    17.161  1.00 98.00 ?  130 ASP A C   1 
1001 ATOM   C CB  .  ASP A 1 130 ?  -19.004 10.899  16.932  1.00 98.00 ?  130 ASP A CB  1 
1002 ATOM   O O   .  ASP A 1 130 ?  -20.612 8.288   17.796  1.00 98.00 ?  130 ASP A O   1 
1003 ATOM   C CG  .  ASP A 1 130 ?  -18.298 12.092  17.547  1.00 98.00 ?  130 ASP A CG  1 
1004 ATOM   O OD1 .  ASP A 1 130 ?  -18.045 12.086  18.771  1.00 98.00 ?  130 ASP A OD1 1 
1005 ATOM   O OD2 .  ASP A 1 130 ?  -18.003 13.059  16.813  1.00 98.00 ?  130 ASP A OD2 1 
1006 ATOM   N N   .  SER A 1 131 ?  -19.236 7.747   16.106  1.00 96.50 ?  131 SER A N   1 
1007 ATOM   C CA  .  SER A 1 131 ?  -20.04  6.619   15.643  1.00 96.50 ?  131 SER A CA  1 
1008 ATOM   C C   .  SER A 1 131 ?  -19.733 5.346   16.428  1.00 96.50 ?  131 SER A C   1 
1009 ATOM   C CB  .  SER A 1 131 ?  -19.781 6.367   14.157  1.00 96.50 ?  131 SER A CB  1 
1010 ATOM   O O   .  SER A 1 131 ?  -20.261 4.275   16.128  1.00 96.50 ?  131 SER A O   1 
1011 ATOM   O OG  .  SER A 1 131 ?  -20.107 7.508   13.382  1.00 96.50 ?  131 SER A OG  1 
1012 ATOM   N N   .  SER A 1 132 ?  -18.885 5.488   17.442  1.00 93.94 ?  132 SER A N   1 
1013 ATOM   C CA  .  SER A 1 132 ?  -18.501 4.408   18.346  1.00 93.94 ?  132 SER A CA  1 
1014 ATOM   C C   .  SER A 1 132 ?  -17.972 3.165   17.634  1.00 93.94 ?  132 SER A C   1 
1015 ATOM   C CB  .  SER A 1 132 ?  -19.685 4.041   19.243  1.00 93.94 ?  132 SER A CB  1 
1016 ATOM   O O   .  SER A 1 132 ?  -18.37  2.038   17.933  1.00 93.94 ?  132 SER A O   1 
1017 ATOM   O OG  .  SER A 1 132 ?  -20.182 5.196   19.896  1.00 93.94 ?  132 SER A OG  1 
1018 ATOM   N N   .  PHE A 1 133 ?  -17.035 3.368   16.714  1.00 97.75 ?  133 PHE A N   1 
1019 ATOM   C CA  .  PHE A 1 133 ?  -16.246 2.257   16.192  1.00 97.75 ?  133 PHE A CA  1 
1020 ATOM   C C   .  PHE A 1 133 ?  -15.12  1.984   17.184  1.00 97.75 ?  133 PHE A C   1 
1021 ATOM   C CB  .  PHE A 1 133 ?  -15.673 2.578   14.809  1.00 97.75 ?  133 PHE A CB  1 
1022 ATOM   O O   .  PHE A 1 133 ?  -14.38  2.893   17.559  1.00 97.75 ?  133 PHE A O   1 
1023 ATOM   C CG  .  PHE A 1 133 ?  -16.714 2.665   13.728  1.00 97.75 ?  133 PHE A CG  1 
1024 ATOM   C CD1 .  PHE A 1 133 ?  -17.237 1.508   13.165  1.00 97.75 ?  133 PHE A CD1 1 
1025 ATOM   C CD2 .  PHE A 1 133 ?  -17.157 3.896   13.258  1.00 97.75 ?  133 PHE A CD2 1 
1026 ATOM   C CE1 .  PHE A 1 133 ?  -18.203 1.571   12.166  1.00 97.75 ?  133 PHE A CE1 1 
1027 ATOM   C CE2 .  PHE A 1 133 ?  -18.103 3.973   12.239  1.00 97.75 ?  133 PHE A CE2 1 
1028 ATOM   C CZ  .  PHE A 1 133 ?  -18.641 2.807   11.704  1.00 97.75 ?  133 PHE A CZ  1 
1029 ATOM   N N   .  ARG A 1 134 ?  -14.997 0.737   17.629  1.00 96.12 ?  134 ARG A N   1 
1030 ATOM   C CA  .  ARG A 1 134 ?  -13.971 0.387   18.609  1.00 96.12 ?  134 ARG A CA  1 
1031 ATOM   C C   .  ARG A 1 134 ?  -12.634 0.124   17.931  1.00 96.12 ?  134 ARG A C   1 
1032 ATOM   C CB  .  ARG A 1 134 ?  -14.377 -0.829  19.446  1.00 96.12 ?  134 ARG A CB  1 
1033 ATOM   O O   .  ARG A 1 134 ?  -11.588 0.489   18.461  1.00 96.12 ?  134 ARG A O   1 
1034 ATOM   C CG  .  ARG A 1 134 ?  -13.467 -1.055  20.648  1.00 96.12 ?  134 ARG A CG  1 
1035 ATOM   C CD  .  ARG A 1 134 ?  -13.876 -2.274  21.462  1.00 96.12 ?  134 ARG A CD  1 
1036 ATOM   N NE  .  ARG A 1 134 ?  -13.044 -2.409  22.658  1.00 96.12 ?  134 ARG A NE  1 
1037 ATOM   N NH1 .  ARG A 1 134 ?  -14.004 -4.368  23.442  1.00 96.12 ?  134 ARG A NH1 1 
1038 ATOM   N NH2 .  ARG A 1 134 ?  -12.34  -3.37   24.603  1.00 96.12 ?  134 ARG A NH2 1 
1039 ATOM   C CZ  .  ARG A 1 134 ?  -13.14  -3.379  23.558  1.00 96.12 ?  134 ARG A CZ  1 
1040 ATOM   N N   .  TYR A 1 135 ?  -12.664 -0.521  16.771  1.00 97.31 ?  135 TYR A N   1 
1041 ATOM   C CA  .  TYR A 1 135 ?  -11.439 -0.788  16.025  1.00 97.31 ?  135 TYR A CA  1 
1042 ATOM   C C   .  TYR A 1 135 ?  -11.381 0.139   14.815  1.00 97.31 ?  135 TYR A C   1 
1043 ATOM   C CB  .  TYR A 1 135 ?  -11.379 -2.254  15.586  1.00 97.31 ?  135 TYR A CB  1 
1044 ATOM   O O   .  TYR A 1 135 ?  -12.249 0.083   13.944  1.00 97.31 ?  135 TYR A O   1 
1045 ATOM   C CG  .  TYR A 1 135 ?  -11.53  -3.251  16.718  1.00 97.31 ?  135 TYR A CG  1 
1046 ATOM   C CD1 .  TYR A 1 135 ?  -10.89  -3.062  17.945  1.00 97.31 ?  135 TYR A CD1 1 
1047 ATOM   C CD2 .  TYR A 1 135 ?  -12.328 -4.386  16.559  1.00 97.31 ?  135 TYR A CD2 1 
1048 ATOM   C CE1 .  TYR A 1 135 ?  -11.079 -3.954  18.999  1.00 97.31 ?  135 TYR A CE1 1 
1049 ATOM   C CE2 .  TYR A 1 135 ?  -12.489 -5.3    17.599  1.00 97.31 ?  135 TYR A CE2 1 
1050 ATOM   O OH  .  TYR A 1 135 ?  -12.058 -5.955  19.857  1.00 97.31 ?  135 TYR A OH  1 
1051 ATOM   C CZ  .  TYR A 1 135 ?  -11.879 -5.069  18.82   1.00 97.31 ?  135 TYR A CZ  1 
1052 ATOM   N N   .  ILE A 1 136 ?  -10.372 1.001   14.76   1.00 98.50 ?  136 ILE A N   1 
1053 ATOM   C CA  .  ILE A 1 136 ?  -10.22  1.923   13.639  1.00 98.50 ?  136 ILE A CA  1 
1054 ATOM   C C   .  ILE A 1 136 ?  -8.91   1.604   12.928  1.00 98.50 ?  136 ILE A C   1 
1055 ATOM   C CB  .  ILE A 1 136 ?  -10.245 3.405   14.078  1.00 98.50 ?  136 ILE A CB  1 
1056 ATOM   O O   .  ILE A 1 136 ?  -7.828  1.73    13.501  1.00 98.50 ?  136 ILE A O   1 
1057 ATOM   C CG1 .  ILE A 1 136 ?  -11.577 3.735   14.765  1.00 98.50 ?  136 ILE A CG1 1 
1058 ATOM   C CG2 .  ILE A 1 136 ?  -10.03  4.312   12.866  1.00 98.50 ?  136 ILE A CG2 1 
1059 ATOM   C CD1 .  ILE A 1 136 ?  -11.639 5.104   15.416  1.00 98.50 ?  136 ILE A CD1 1 
1060 ATOM   N N   .  VAL A 1 137 ?  -9.019  1.169   11.678  1.00 98.56 ?  137 VAL A N   1 
1061 ATOM   C CA  .  VAL A 1 137 ?  -7.851  0.855   10.861  1.00 98.56 ?  137 VAL A CA  1 
1062 ATOM   C C   .  VAL A 1 137 ?  -7.423  2.125   10.135  1.00 98.56 ?  137 VAL A C   1 
1063 ATOM   C CB  .  VAL A 1 137 ?  -8.127  -0.247  9.814   1.00 98.56 ?  137 VAL A CB  1 
1064 ATOM   O O   .  VAL A 1 137 ?  -8.175  2.682   9.335   1.00 98.56 ?  137 VAL A O   1 
1065 ATOM   C CG1 .  VAL A 1 137 ?  -6.869  -0.546  9.003   1.00 98.56 ?  137 VAL A CG1 1 
1066 ATOM   C CG2 .  VAL A 1 137 ?  -8.616  -1.525  10.491  1.00 98.56 ?  137 VAL A CG2 1 
1067 ATOM   N N   .  LEU A 1 138 ?  -6.211  2.573   10.438  1.00 97.88 ?  138 LEU A N   1 
1068 ATOM   C CA  .  LEU A 1 138 ?  -5.612  3.734   9.792   1.00 97.88 ?  138 LEU A CA  1 
1069 ATOM   C C   .  LEU A 1 138 ?  -4.577  3.201   8.808   1.00 97.88 ?  138 LEU A C   1 
1070 ATOM   C CB  .  LEU A 1 138 ?  -4.95   4.635   10.839  1.00 97.88 ?  138 LEU A CB  1 
1071 ATOM   O O   .  LEU A 1 138 ?  -3.734  2.384   9.179   1.00 97.88 ?  138 LEU A O   1 
1072 ATOM   C CG  .  LEU A 1 138 ?  -5.848  5.25    11.916  1.00 97.88 ?  138 LEU A CG  1 
1073 ATOM   C CD1 .  LEU A 1 138 ?  -5.005  6.143   12.818  1.00 97.88 ?  138 LEU A CD1 1 
1074 ATOM   C CD2 .  LEU A 1 138 ?  -6.983  6.068   11.313  1.00 97.88 ?  138 LEU A CD2 1 
1075 ATOM   N N   .  CYS A 1 139 ?  -4.656  3.635   7.556   1.00 95.25 ?  139 CYS A N   1 
1076 ATOM   C CA  .  CYS A 1 139 ?  -3.873  3.033   6.484   1.00 95.25 ?  139 CYS A CA  1 
1077 ATOM   C C   .  CYS A 1 139 ?  -3.002  4.063   5.772   1.00 95.25 ?  139 CYS A C   1 
1078 ATOM   C CB  .  CYS A 1 139 ?  -4.808  2.319   5.505   1.00 95.25 ?  139 CYS A CB  1 
1079 ATOM   O O   .  CYS A 1 139 ?  -3.445  4.74    4.844   1.00 95.25 ?  139 CYS A O   1 
1080 ATOM   S SG  .  CYS A 1 139 ?  -3.975  1.079   4.48    1.00 95.25 ?  139 CYS A SG  1 
1081 ATOM   N N   .  GLY A 1 140 ?  -1.753  4.159   6.216   1.00 93.12 ?  140 GLY A N   1 
1082 ATOM   C CA  .  GLY A 1 140 ?  -0.794  5.078   5.629   1.00 93.12 ?  140 GLY A CA  1 
1083 ATOM   C C   .  GLY A 1 140 ?  -0.244  6.085   6.621   1.00 93.12 ?  140 GLY A C   1 
1084 ATOM   O O   .  GLY A 1 140 ?  -0.836  6.374   7.66    1.00 93.12 ?  140 GLY A O   1 
1085 ATOM   N N   .  PHE A 1 141 ?  0.935   6.611   6.309   1.00 90.00 ?  141 PHE A N   1 
1086 ATOM   C CA  .  PHE A 1 141 ?  1.722   7.378   7.269   1.00 90.00 ?  141 PHE A CA  1 
1087 ATOM   C C   .  PHE A 1 141 ?  1.338   8.848   7.433   1.00 90.00 ?  141 PHE A C   1 
1088 ATOM   C CB  .  PHE A 1 141 ?  3.199   7.28    6.878   1.00 90.00 ?  141 PHE A CB  1 
1089 ATOM   O O   .  PHE A 1 141 ?  1.77    9.483   8.395   1.00 90.00 ?  141 PHE A O   1 
1090 ATOM   C CG  .  PHE A 1 141 ?  3.51    7.887   5.538   1.00 90.00 ?  141 PHE A CG  1 
1091 ATOM   C CD1 .  PHE A 1 141 ?  3.446   7.114   4.383   1.00 90.00 ?  141 PHE A CD1 1 
1092 ATOM   C CD2 .  PHE A 1 141 ?  3.848   9.232   5.431   1.00 90.00 ?  141 PHE A CD2 1 
1093 ATOM   C CE1 .  PHE A 1 141 ?  3.665   7.684   3.133   1.00 90.00 ?  141 PHE A CE1 1 
1094 ATOM   C CE2 .  PHE A 1 141 ?  4.084   9.808   4.186   1.00 90.00 ?  141 PHE A CE2 1 
1095 ATOM   C CZ  .  PHE A 1 141 ?  3.982   9.033   3.035   1.00 90.00 ?  141 PHE A CZ  1 
1096 ATOM   N N   .  THR A 1 142 ?  0.535   9.406   6.533   1.00 91.44 ?  142 THR A N   1 
1097 ATOM   C CA  .  THR A 1 142 ?  0.193   10.826  6.617   1.00 91.44 ?  142 THR A CA  1 
1098 ATOM   C C   .  THR A 1 142 ?  -0.843  11.103  7.703   1.00 91.44 ?  142 THR A C   1 
1099 ATOM   C CB  .  THR A 1 142 ?  -0.326  11.413  5.287   1.00 91.44 ?  142 THR A CB  1 
1100 ATOM   O O   .  THR A 1 142 ?  -1.107  12.259  8.031   1.00 91.44 ?  142 THR A O   1 
1101 ATOM   C CG2 .  THR A 1 142 ?  0.684   11.226  4.161   1.00 91.44 ?  142 THR A CG2 1 
1102 ATOM   O OG1 .  THR A 1 142 ?  -1.557  10.778  4.924   1.00 91.44 ?  142 THR A OG1 1 
1103 ATOM   N N   .  HIS A 1 143 ?  -1.393  10.051  8.301   1.00 95.62 ?  143 HIS A N   1 
1104 ATOM   C CA  .  HIS A 1 143 ?  -2.307  10.198  9.43    1.00 95.62 ?  143 HIS A CA  1 
1105 ATOM   C C   .  HIS A 1 143 ?  -1.657  10.899  10.62   1.00 95.62 ?  143 HIS A C   1 
1106 ATOM   C CB  .  HIS A 1 143 ?  -2.785  8.832   9.931   1.00 95.62 ?  143 HIS A CB  1 
1107 ATOM   O O   .  HIS A 1 143 ?  -2.349  11.561  11.394  1.00 95.62 ?  143 HIS A O   1 
1108 ATOM   C CG  .  HIS A 1 143 ?  -3.739  8.135   9.012   1.00 95.62 ?  143 HIS A CG  1 
1109 ATOM   C CD2 .  HIS A 1 143 ?  -3.618  6.958   8.345   1.00 95.62 ?  143 HIS A CD2 1 
1110 ATOM   N ND1 .  HIS A 1 143 ?  -5.032  8.546   8.775   1.00 95.62 ?  143 HIS A ND1 1 
1111 ATOM   C CE1 .  HIS A 1 143 ?  -5.625  7.622   8.008   1.00 95.62 ?  143 HIS A CE1 1 
1112 ATOM   N NE2 .  HIS A 1 143 ?  -4.814  6.611   7.769   1.00 95.62 ?  143 HIS A NE2 1 
1113 ATOM   N N   .  LYS A 1 144 ?  -0.348  10.735  10.787  1.00 93.38 ?  144 LYS A N   1 
1114 ATOM   C CA  .  LYS A 1 144 ?  0.339   11.134  12.015  1.00 93.38 ?  144 LYS A CA  1 
1115 ATOM   C C   .  LYS A 1 144 ?  0.033   12.557  12.469  1.00 93.38 ?  144 LYS A C   1 
1116 ATOM   C CB  .  LYS A 1 144 ?  1.856   10.996  11.854  1.00 93.38 ?  144 LYS A CB  1 
1117 ATOM   O O   .  LYS A 1 144 ?  -0.401  12.765  13.599  1.00 93.38 ?  144 LYS A O   1 
1118 ATOM   C CG  .  LYS A 1 144 ?  2.361   9.57    11.703  1.00 93.38 ?  144 LYS A CG  1 
1119 ATOM   C CD  .  LYS A 1 144 ?  3.876   9.563   11.568  1.00 93.38 ?  144 LYS A CD  1 
1120 ATOM   C CE  .  LYS A 1 144 ?  4.378   8.155   11.316  1.00 93.38 ?  144 LYS A CE  1 
1121 ATOM   N NZ  .  LYS A 1 144 ?  5.872   8.14    11.241  1.00 93.38 ?  144 LYS A NZ  1 
1122 ATOM   N N   .  ALA A 1 145 ?  0.287   13.534  11.606  1.00 92.94 ?  145 ALA A N   1 
1123 ATOM   C CA  .  ALA A 1 145 ?  0.209   14.935  12.007  1.00 92.94 ?  145 ALA A CA  1 
1124 ATOM   C C   .  ALA A 1 145 ?  -1.202  15.339  12.426  1.00 92.94 ?  145 ALA A C   1 
1125 ATOM   C CB  .  ALA A 1 145 ?  0.701   15.829  10.876  1.00 92.94 ?  145 ALA A CB  1 
1126 ATOM   O O   .  ALA A 1 145 ?  -1.375  16.11   13.368  1.00 92.94 ?  145 ALA A O   1 
1127 ATOM   N N   .  ALA A 1 146 ?  -2.208  14.831  11.724  1.00 95.56 ?  146 ALA A N   1 
1128 ATOM   C CA  .  ALA A 1 146 ?  -3.596  15.148  12.045  1.00 95.56 ?  146 ALA A CA  1 
1129 ATOM   C C   .  ALA A 1 146 ?  -4.061  14.419  13.304  1.00 95.56 ?  146 ALA A C   1 
1130 ATOM   C CB  .  ALA A 1 146 ?  -4.493  14.79   10.868  1.00 95.56 ?  146 ALA A CB  1 
1131 ATOM   O O   .  ALA A 1 146 ?  -4.833  14.961  14.093  1.00 95.56 ?  146 ALA A O   1 
1132 ATOM   N N   .  LEU A 1 147 ?  -3.601  13.185  13.479  1.00 95.31 ?  147 LEU A N   1 
1133 ATOM   C CA  .  LEU A 1 147 ?  -3.971  12.372  14.634  1.00 95.31 ?  147 LEU A CA  1 
1134 ATOM   C C   .  LEU A 1 147 ?  -3.419  12.951  15.934  1.00 95.31 ?  147 LEU A C   1 
1135 ATOM   C CB  .  LEU A 1 147 ?  -3.455  10.944  14.441  1.00 95.31 ?  147 LEU A CB  1 
1136 ATOM   O O   .  LEU A 1 147 ?  -4.071  12.883  16.974  1.00 95.31 ?  147 LEU A O   1 
1137 ATOM   C CG  .  LEU A 1 147 ?  -3.968  9.895   15.433  1.00 95.31 ?  147 LEU A CG  1 
1138 ATOM   C CD1 .  LEU A 1 147 ?  -5.443  9.578   15.215  1.00 95.31 ?  147 LEU A CD1 1 
1139 ATOM   C CD2 .  LEU A 1 147 ?  -3.147  8.625   15.269  1.00 95.31 ?  147 LEU A CD2 1 
1140 ATOM   N N   .  TYR A 1 148 ?  -2.225  13.533  15.87   1.00 95.38 ?  148 TYR A N   1 
1141 ATOM   C CA  .  TYR A 1 148 ?  -1.587  14.112  17.05   1.00 95.38 ?  148 TYR A CA  1 
1142 ATOM   C C   .  TYR A 1 148 ?  -2.298  15.379  17.519  1.00 95.38 ?  148 TYR A C   1 
1143 ATOM   C CB  .  TYR A 1 148 ?  -0.118  14.455  16.778  1.00 95.38 ?  148 TYR A CB  1 
1144 ATOM   O O   .  TYR A 1 148 ?  -2.076  15.839  18.639  1.00 95.38 ?  148 TYR A O   1 
1145 ATOM   C CG  .  TYR A 1 148 ?  0.792   13.315  16.364  1.00 95.38 ?  148 TYR A CG  1 
1146 ATOM   C CD1 .  TYR A 1 148 ?  0.507   11.984  16.678  1.00 95.38 ?  148 TYR A CD1 1 
1147 ATOM   C CD2 .  TYR A 1 148 ?  1.964   13.586  15.655  1.00 95.38 ?  148 TYR A CD2 1 
1148 ATOM   C CE1 .  TYR A 1 148 ?  1.354   10.956  16.275  1.00 95.38 ?  148 TYR A CE1 1 
1149 ATOM   C CE2 .  TYR A 1 148 ?  2.83    12.562  15.277  1.00 95.38 ?  148 TYR A CE2 1 
1150 ATOM   O OH  .  TYR A 1 148 ?  3.358   10.237  15.186  1.00 95.38 ?  148 TYR A OH  1 
1151 ATOM   C CZ  .  TYR A 1 148 ?  2.516   11.25   15.583  1.00 95.38 ?  148 TYR A CZ  1 
1152 ATOM   N N   .  GLY A 1 149 ?  -3.149  15.935  16.663  1.00 94.44 ?  149 GLY A N   1 
1153 ATOM   C CA  .  GLY A 1 149 ?  -3.898  17.135  16.995  1.00 94.44 ?  149 GLY A CA  1 
1154 ATOM   C C   .  GLY A 1 149 ?  -5.283  16.873  17.553  1.00 94.44 ?  149 GLY A C   1 
1155 ATOM   O O   .  GLY A 1 149 ?  -6.094  17.794  17.64   1.00 94.44 ?  149 GLY A O   1 
1156 ATOM   N N   .  LEU A 1 150 ?  -5.568  15.628  17.923  1.00 95.75 ?  150 LEU A N   1 
1157 ATOM   C CA  .  LEU A 1 150 ?  -6.863  15.283  18.5    1.00 95.75 ?  150 LEU A CA  1 
1158 ATOM   C C   .  LEU A 1 150 ?  -7.074  16.009  19.825  1.00 95.75 ?  150 LEU A C   1 
1159 ATOM   C CB  .  LEU A 1 150 ?  -6.982  13.773  18.725  1.00 95.75 ?  150 LEU A CB  1 
1160 ATOM   O O   .  LEU A 1 150 ?  -6.175  16.103  20.661  1.00 95.75 ?  150 LEU A O   1 
1161 ATOM   C CG  .  LEU A 1 150 ?  -7.398  12.906  17.531  1.00 95.75 ?  150 LEU A CG  1 
1162 ATOM   C CD1 .  LEU A 1 150 ?  -7.308  11.439  17.929  1.00 95.75 ?  150 LEU A CD1 1 
1163 ATOM   C CD2 .  LEU A 1 150 ?  -8.82   13.218  17.076  1.00 95.75 ?  150 LEU A CD2 1 
1164 ATOM   N N   .  GLU A 1 151 ?  -8.28   16.536  19.998  1.00 96.12 ?  151 GLU A N   1 
1165 ATOM   C CA  .  GLU A 1 151 ?  -8.614  17.32   21.183  1.00 96.12 ?  151 GLU A CA  1 
1166 ATOM   C C   .  GLU A 1 151 ?  -8.737  16.417  22.41   1.00 96.12 ?  151 GLU A C   1 
1167 ATOM   C CB  .  GLU A 1 151 ?  -9.927  18.08   20.971  1.00 96.12 ?  151 GLU A CB  1 
1168 ATOM   O O   .  GLU A 1 151 ?  -9.039  15.23   22.28   1.00 96.12 ?  151 GLU A O   1 
1169 ATOM   C CG  .  GLU A 1 151 ?  -9.886  19.139  19.876  1.00 96.12 ?  151 GLU A CG  1 
1170 ATOM   C CD  .  GLU A 1 151 ?  -10.052 18.578  18.474  1.00 96.12 ?  151 GLU A CD  1 
1171 ATOM   O OE1 .  GLU A 1 151 ?  -9.885  19.347  17.503  1.00 96.12 ?  151 GLU A OE1 1 
1172 ATOM   O OE2 .  GLU A 1 151 ?  -10.366 17.379  18.311  1.00 96.12 ?  151 GLU A OE2 1 
1173 ATOM   N N   .  PRO A 1 152 ?  -8.52   16.96   23.619  1.00 97.19 ?  152 PRO A N   1 
1174 ATOM   C CA  .  PRO A 1 152 ?  -8.626  16.081  24.79   1.00 97.19 ?  152 PRO A CA  1 
1175 ATOM   C C   .  PRO A 1 152 ?  -9.987  15.416  24.975  1.00 97.19 ?  152 PRO A C   1 
1176 ATOM   C CB  .  PRO A 1 152 ?  -8.336  17.019  25.964  1.00 97.19 ?  152 PRO A CB  1 
1177 ATOM   O O   .  PRO A 1 152 ?  -10.082 14.361  25.6    1.00 97.19 ?  152 PRO A O   1 
1178 ATOM   C CG  .  PRO A 1 152 ?  -7.564  18.146  25.375  1.00 97.19 ?  152 PRO A CG  1 
1179 ATOM   C CD  .  PRO A 1 152 ?  -8.165  18.335  24.014  1.00 97.19 ?  152 PRO A CD  1 
1180 ATOM   N N   .  GLU A 1 153 ?  -11.043 16.027  24.449  1.00 97.94 ?  153 GLU A N   1 
1181 ATOM   C CA  .  GLU A 1 153 ?  -12.38  15.449  24.55   1.00 97.94 ?  153 GLU A CA  1 
1182 ATOM   C C   .  GLU A 1 153 ?  -12.503 14.173  23.72   1.00 97.94 ?  153 GLU A C   1 
1183 ATOM   C CB  .  GLU A 1 153 ?  -13.458 16.465  24.157  1.00 97.94 ?  153 GLU A CB  1 
1184 ATOM   O O   .  GLU A 1 153 ?  -13.228 13.256  24.1    1.00 97.94 ?  153 GLU A O   1 
1185 ATOM   C CG  .  GLU A 1 153 ?  -13.495 16.844  22.682  1.00 97.94 ?  153 GLU A CG  1 
1186 ATOM   C CD  .  GLU A 1 153 ?  -14.553 17.885  22.366  1.00 97.94 ?  153 GLU A CD  1 
1187 ATOM   O OE1 .  GLU A 1 153 ?  -14.712 18.226  21.174  1.00 97.94 ?  153 GLU A OE1 1 
1188 ATOM   O OE2 .  GLU A 1 153 ?  -15.241 18.363  23.293  1.00 97.94 ?  153 GLU A OE2 1 
1189 ATOM   N N   .  TYR A 1 154 ?  -11.787 14.092  22.603  1.00 98.19 ?  154 TYR A N   1 
1190 ATOM   C CA  .  TYR A 1 154 ?  -11.814 12.896  21.767  1.00 98.19 ?  154 TYR A CA  1 
1191 ATOM   C C   .  TYR A 1 154 ?  -10.84  11.852  22.301  1.00 98.19 ?  154 TYR A C   1 
1192 ATOM   C CB  .  TYR A 1 154 ?  -11.501 13.225  20.305  1.00 98.19 ?  154 TYR A CB  1 
1193 ATOM   O O   .  TYR A 1 154 ?  -11.089 10.654  22.178  1.00 98.19 ?  154 TYR A O   1 
1194 ATOM   C CG  .  TYR A 1 154 ?  -12.665 13.886  19.601  1.00 98.19 ?  154 TYR A CG  1 
1195 ATOM   C CD1 .  TYR A 1 154 ?  -13.714 13.121  19.087  1.00 98.19 ?  154 TYR A CD1 1 
1196 ATOM   C CD2 .  TYR A 1 154 ?  -12.739 15.273  19.482  1.00 98.19 ?  154 TYR A CD2 1 
1197 ATOM   C CE1 .  TYR A 1 154 ?  -14.832 13.729  18.521  1.00 98.19 ?  154 TYR A CE1 1 
1198 ATOM   C CE2 .  TYR A 1 154 ?  -13.856 15.886  18.919  1.00 98.19 ?  154 TYR A CE2 1 
1199 ATOM   O OH  .  TYR A 1 154 ?  -16.017 15.718  17.921  1.00 98.19 ?  154 TYR A OH  1 
1200 ATOM   C CZ  .  TYR A 1 154 ?  -14.905 15.111  18.456  1.00 98.19 ?  154 TYR A CZ  1 
1201 ATOM   N N   .  ILE A 1 155 ?  -9.755  12.3    22.924  1.00 98.00 ?  155 ILE A N   1 
1202 ATOM   C CA  .  ILE A 1 155 ?  -8.858  11.397  23.641  1.00 98.00 ?  155 ILE A CA  1 
1203 ATOM   C C   .  ILE A 1 155 ?  -9.639  10.733  24.772  1.00 98.00 ?  155 ILE A C   1 
1204 ATOM   C CB  .  ILE A 1 155 ?  -7.62   12.131  24.204  1.00 98.00 ?  155 ILE A CB  1 
1205 ATOM   O O   .  ILE A 1 155 ?  -9.513  9.529   24.999  1.00 98.00 ?  155 ILE A O   1 
1206 ATOM   C CG1 .  ILE A 1 155 ?  -6.768  12.747  23.085  1.00 98.00 ?  155 ILE A CG1 1 
1207 ATOM   C CG2 .  ILE A 1 155 ?  -6.784  11.194  25.072  1.00 98.00 ?  155 ILE A CG2 1 
1208 ATOM   C CD1 .  ILE A 1 155 ?  -6.151  11.779  22.087  1.00 98.00 ?  155 ILE A CD1 1 
1209 ATOM   N N   .  LYS A 1 156 ?  -10.468 11.505  25.467  1.00 97.81 ?  156 LYS A N   1 
1210 ATOM   C CA  .  LYS A 1 156 ?  -11.309 10.97   26.535  1.00 97.81 ?  156 LYS A CA  1 
1211 ATOM   C C   .  LYS A 1 156 ?  -12.296 9.935   26.004  1.00 97.81 ?  156 LYS A C   1 
1212 ATOM   C CB  .  LYS A 1 156 ?  -12.051 12.111  27.237  1.00 97.81 ?  156 LYS A CB  1 
1213 ATOM   O O   .  LYS A 1 156 ?  -12.492 8.891   26.623  1.00 97.81 ?  156 LYS A O   1 
1214 ATOM   C CG  .  LYS A 1 156 ?  -12.774 11.683  28.505  1.00 97.81 ?  156 LYS A CG  1 
1215 ATOM   C CD  .  LYS A 1 156 ?  -13.477 12.861  29.165  1.00 97.81 ?  156 LYS A CD  1 
1216 ATOM   C CE  .  LYS A 1 156 ?  -14.086 12.483  30.508  1.00 97.81 ?  156 LYS A CE  1 
1217 ATOM   N NZ  .  LYS A 1 156 ?  -15.214 11.513  30.321  1.00 97.81 ?  156 LYS A NZ  1 
1218 ATOM   N N   .  LYS A 1 157 ?  -12.905 10.214  24.855  1.00 98.12 ?  157 LYS A N   1 
1219 ATOM   C CA  .  LYS A 1 157 ?  -13.825 9.278   24.21   1.00 98.12 ?  157 LYS A CA  1 
1220 ATOM   C C   .  LYS A 1 157 ?  -13.109 8.009   23.757  1.00 98.12 ?  157 LYS A C   1 
1221 ATOM   C CB  .  LYS A 1 157 ?  -14.504 9.935   23.005  1.00 98.12 ?  157 LYS A CB  1 
1222 ATOM   O O   .  LYS A 1 157 ?  -13.678 6.921   23.818  1.00 98.12 ?  157 LYS A O   1 
1223 ATOM   C CG  .  LYS A 1 157 ?  -15.499 11.032  23.356  1.00 98.12 ?  157 LYS A CG  1 
1224 ATOM   C CD  .  LYS A 1 157 ?  -15.974 11.77   22.112  1.00 98.12 ?  157 LYS A CD  1 
1225 ATOM   C CE  .  LYS A 1 157 ?  -16.885 12.932  22.473  1.00 98.12 ?  157 LYS A CE  1 
1226 ATOM   N NZ  .  LYS A 1 157 ?  -17.271 13.661  21.221  1.00 98.12 ?  157 LYS A NZ  1 
1227 ATOM   N N   .  ILE A 1 158 ?  -11.868 8.149   23.305  1.00 98.00 ?  158 ILE A N   1 
1228 ATOM   C CA  .  ILE A 1 158 ?  -11.05  7.004   22.912  1.00 98.00 ?  158 ILE A CA  1 
1229 ATOM   C C   .  ILE A 1 158 ?  -10.786 6.104   24.115  1.00 98.00 ?  158 ILE A C   1 
1230 ATOM   C CB  .  ILE A 1 158 ?  -9.715  7.449   22.27   1.00 98.00 ?  158 ILE A CB  1 
1231 ATOM   O O   .  ILE A 1 158 ?  -10.912 4.885   24.009  1.00 98.00 ?  158 ILE A O   1 
1232 ATOM   C CG1 .  ILE A 1 158 ?  -9.97   8.015   20.868  1.00 98.00 ?  158 ILE A CG1 1 
1233 ATOM   C CG2 .  ILE A 1 158 ?  -8.72   6.292   22.193  1.00 98.00 ?  158 ILE A CG2 1 
1234 ATOM   C CD1 .  ILE A 1 158 ?  -8.89   8.957   20.37   1.00 98.00 ?  158 ILE A CD1 1 
1235 ATOM   N N   .  LYS A 1 159 ?  -10.432 6.691   25.254  1.00 96.94 ?  159 LYS A N   1 
1236 ATOM   C CA  .  LYS A 1 159 ?  -10.165 5.906   26.458  1.00 96.94 ?  159 LYS A CA  1 
1237 ATOM   C C   .  LYS A 1 159 ?  -11.425 5.268   27.031  1.00 96.94 ?  159 LYS A C   1 
1238 ATOM   C CB  .  LYS A 1 159 ?  -9.512  6.769   27.541  1.00 96.94 ?  159 LYS A CB  1 
1239 ATOM   O O   .  LYS A 1 159 ?  -11.401 4.111   27.446  1.00 96.94 ?  159 LYS A O   1 
1240 ATOM   C CG  .  LYS A 1 159 ?  -8.094  7.211   27.216  1.00 96.94 ?  159 LYS A CG  1 
1241 ATOM   C CD  .  LYS A 1 159 ?  -7.513  8.014   28.369  1.00 96.94 ?  159 LYS A CD  1 
1242 ATOM   C CE  .  LYS A 1 159 ?  -6.103  8.476   28.05   1.00 96.94 ?  159 LYS A CE  1 
1243 ATOM   N NZ  .  LYS A 1 159 ?  -5.559  9.263   29.205  1.00 96.94 ?  159 LYS A NZ  1 
1244 ATOM   N N   .  ASP A 1 160 ?  -12.509 6.033   27.068  1.00 96.38 ?  160 ASP A N   1 
1245 ATOM   C CA  .  ASP A 1 160 ?  -13.757 5.582   27.677  1.00 96.38 ?  160 ASP A CA  1 
1246 ATOM   C C   .  ASP A 1 160 ?  -14.398 4.43    26.908  1.00 96.38 ?  160 ASP A C   1 
1247 ATOM   C CB  .  ASP A 1 160 ?  -14.759 6.738   27.754  1.00 96.38 ?  160 ASP A CB  1 
1248 ATOM   O O   .  ASP A 1 160 ?  -15.03  3.557   27.501  1.00 96.38 ?  160 ASP A O   1 
1249 ATOM   C CG  .  ASP A 1 160 ?  -14.36  7.8     28.762  1.00 96.38 ?  160 ASP A CG  1 
1250 ATOM   O OD1 .  ASP A 1 160 ?  -13.494 7.549   29.627  1.00 96.38 ?  160 ASP A OD1 1 
1251 ATOM   O OD2 .  ASP A 1 160 ?  -14.931 8.91    28.704  1.00 96.38 ?  160 ASP A OD2 1 
1252 ATOM   N N   .  ASN A 1 161 ?  -14.244 4.433   25.589  1.00 95.94 ?  161 ASN A N   1 
1253 ATOM   C CA  .  ASN A 1 161 ?  -14.82  3.393   24.742  1.00 95.94 ?  161 ASN A CA  1 
1254 ATOM   C C   .  ASN A 1 161 ?  -13.786 2.35    24.324  1.00 95.94 ?  161 ASN A C   1 
1255 ATOM   C CB  .  ASN A 1 161 ?  -15.451 4.039   23.506  1.00 95.94 ?  161 ASN A CB  1 
1256 ATOM   O O   .  ASN A 1 161 ?  -14.087 1.459   23.529  1.00 95.94 ?  161 ASN A O   1 
1257 ATOM   C CG  .  ASN A 1 161 ?  -16.666 4.873   23.844  1.00 95.94 ?  161 ASN A CG  1 
1258 ATOM   N ND2 .  ASN A 1 161 ?  -16.505 6.187   23.826  1.00 95.94 ?  161 ASN A ND2 1 
1259 ATOM   O OD1 .  ASN A 1 161 ?  -17.743 4.344   24.109  1.00 95.94 ?  161 ASN A OD1 1 
1260 ATOM   N N   .  ASN A 1 162 ?  -12.573 2.474   24.854  1.00 95.19 ?  162 ASN A N   1 
1261 ATOM   C CA  .  ASN A 1 162 ?  -11.477 1.552   24.567  1.00 95.19 ?  162 ASN A CA  1 
1262 ATOM   C C   .  ASN A 1 162 ?  -11.258 1.396   23.064  1.00 95.19 ?  162 ASN A C   1 
1263 ATOM   C CB  .  ASN A 1 162 ?  -11.759 0.199   25.227  1.00 95.19 ?  162 ASN A CB  1 
1264 ATOM   O O   .  ASN A 1 162 ?  -11.113 0.289   22.544  1.00 95.19 ?  162 ASN A O   1 
1265 ATOM   C CG  .  ASN A 1 162 ?  -11.66  0.265   26.733  1.00 95.19 ?  162 ASN A CG  1 
1266 ATOM   N ND2 .  ASN A 1 162 ?  -12.751 -0.044  27.415  1.00 95.19 ?  162 ASN A ND2 1 
1267 ATOM   O OD1 .  ASN A 1 162 ?  -10.605 0.58    27.28   1.00 95.19 ?  162 ASN A OD1 1 
1268 ATOM   N N   .  ILE A 1 163 ?  -11.223 2.527   22.368  1.00 97.69 ?  163 ILE A N   1 
1269 ATOM   C CA  .  ILE A 1 163 ?  -11.03  2.543   20.921  1.00 97.69 ?  163 ILE A CA  1 
1270 ATOM   C C   .  ILE A 1 163 ?  -9.558  2.277   20.621  1.00 97.69 ?  163 ILE A C   1 
1271 ATOM   C CB  .  ILE A 1 163 ?  -11.485 3.878   20.286  1.00 97.69 ?  163 ILE A CB  1 
1272 ATOM   O O   .  ILE A 1 163 ?  -8.667  2.929   21.166  1.00 97.69 ?  163 ILE A O   1 
1273 ATOM   C CG1 .  ILE A 1 163 ?  -12.984 4.085   20.536  1.00 97.69 ?  163 ILE A CG1 1 
1274 ATOM   C CG2 .  ILE A 1 163 ?  -11.182 3.899   18.788  1.00 97.69 ?  163 ILE A CG2 1 
1275 ATOM   C CD1 .  ILE A 1 163 ?  -13.532 5.435   20.113  1.00 97.69 ?  163 ILE A CD1 1 
1276 ATOM   N N   .  VAL A 1 164 ?  -9.316  1.303   19.751  1.00 96.81 ?  164 VAL A N   1 
1277 ATOM   C CA  .  VAL A 1 164 ?  -7.966  0.883   19.387  1.00 96.81 ?  164 VAL A CA  1 
1278 ATOM   C C   .  VAL A 1 164 ?  -7.706  1.238   17.928  1.00 96.81 ?  164 VAL A C   1 
1279 ATOM   C CB  .  VAL A 1 164 ?  -7.77   -0.641  19.552  1.00 96.81 ?  164 VAL A CB  1 
1280 ATOM   O O   .  VAL A 1 164 ?  -8.474  0.863   17.04   1.00 96.81 ?  164 VAL A O   1 
1281 ATOM   C CG1 .  VAL A 1 164 ?  -6.351  -1.054  19.176  1.00 96.81 ?  164 VAL A CG1 1 
1282 ATOM   C CG2 .  VAL A 1 164 ?  -8.069  -1.074  20.985  1.00 96.81 ?  164 VAL A CG2 1 
1283 ATOM   N N   .  PHE A 1 165 ?  -6.614  1.953   17.684  1.00 97.88 ?  165 PHE A N   1 
1284 ATOM   C CA  .  PHE A 1 165 ?  -6.203  2.285   16.325  1.00 97.88 ?  165 PHE A CA  1 
1285 ATOM   C C   .  PHE A 1 165 ?  -5.195  1.252   15.835  1.00 97.88 ?  165 PHE A C   1 
1286 ATOM   C CB  .  PHE A 1 165 ?  -5.579  3.681   16.26   1.00 97.88 ?  165 PHE A CB  1 
1287 ATOM   O O   .  PHE A 1 165 ?  -4.151  1.041   16.452  1.00 97.88 ?  165 PHE A O   1 
1288 ATOM   C CG  .  PHE A 1 165 ?  -6.533  4.788   16.614  1.00 97.88 ?  165 PHE A CG  1 
1289 ATOM   C CD1 .  PHE A 1 165 ?  -7.321  5.381   15.632  1.00 97.88 ?  165 PHE A CD1 1 
1290 ATOM   C CD2 .  PHE A 1 165 ?  -6.649  5.231   17.927  1.00 97.88 ?  165 PHE A CD2 1 
1291 ATOM   C CE1 .  PHE A 1 165 ?  -8.203  6.409   15.951  1.00 97.88 ?  165 PHE A CE1 1 
1292 ATOM   C CE2 .  PHE A 1 165 ?  -7.547  6.24    18.26   1.00 97.88 ?  165 PHE A CE2 1 
1293 ATOM   C CZ  .  PHE A 1 165 ?  -8.323  6.835   17.27   1.00 97.88 ?  165 PHE A CZ  1 
1294 ATOM   N N   .  ILE A 1 166 ?  -5.513  0.62    14.71   1.00 97.38 ?  166 ILE A N   1 
1295 ATOM   C CA  .  ILE A 1 166 ?  -4.582  -0.282  14.04   1.00 97.38 ?  166 ILE A CA  1 
1296 ATOM   C C   .  ILE A 1 166 ?  -3.884  0.601   13.014  1.00 97.38 ?  166 ILE A C   1 
1297 ATOM   C CB  .  ILE A 1 166 ?  -5.286  -1.477  13.359  1.00 97.38 ?  166 ILE A CB  1 
1298 ATOM   O O   .  ILE A 1 166 ?  -4.515  1.096   12.08   1.00 97.38 ?  166 ILE A O   1 
1299 ATOM   C CG1 .  ILE A 1 166 ?  -6.03   -2.318  14.404  1.00 97.38 ?  166 ILE A CG1 1 
1300 ATOM   C CG2 .  ILE A 1 166 ?  -4.267  -2.332  12.606  1.00 97.38 ?  166 ILE A CG2 1 
1301 ATOM   C CD1 .  ILE A 1 166 ?  -7.063  -3.272  13.836  1.00 97.38 ?  166 ILE A CD1 1 
1302 ATOM   N N   .  THR A 1 167 ?  -2.596  0.844   13.228  1.00 96.50 ?  167 THR A N   1 
1303 ATOM   C CA  .  THR A 1 167 ?  -1.851  1.81    12.427  1.00 96.50 ?  167 THR A CA  1 
1304 ATOM   C C   .  THR A 1 167 ?  -0.992  1.07    11.408  1.00 96.50 ?  167 THR A C   1 
1305 ATOM   C CB  .  THR A 1 167 ?  -0.969  2.726   13.3    1.00 96.50 ?  167 THR A CB  1 
1306 ATOM   O O   .  THR A 1 167 ?  0.038   0.482   11.738  1.00 96.50 ?  167 THR A O   1 
1307 ATOM   C CG2 .  THR A 1 167 ?  -1.816  3.561   14.253  1.00 96.50 ?  167 THR A CG2 1 
1308 ATOM   O OG1 .  THR A 1 167 ?  -0.065  1.938   14.083  1.00 96.50 ?  167 THR A OG1 1 
1309 ATOM   N N   .  VAL A 1 168 ?  -1.457  1.068   10.164  1.00 95.31 ?  168 VAL A N   1 
1310 ATOM   C CA  .  VAL A 1 168 ?  -0.787  0.345   9.088   1.00 95.31 ?  168 VAL A CA  1 
1311 ATOM   C C   .  VAL A 1 168 ?  0.247   1.246   8.425   1.00 95.31 ?  168 VAL A C   1 
1312 ATOM   C CB  .  VAL A 1 168 ?  -1.776  -0.166  8.017   1.00 95.31 ?  168 VAL A CB  1 
1313 ATOM   O O   .  VAL A 1 168 ?  -0.063  2.348   7.971   1.00 95.31 ?  168 VAL A O   1 
1314 ATOM   C CG1 .  VAL A 1 168 ?  -1.038  -0.901  6.903   1.00 95.31 ?  168 VAL A CG1 1 
1315 ATOM   C CG2 .  VAL A 1 168 ?  -2.817  -1.093  8.641   1.00 95.31 ?  168 VAL A CG2 1 
1316 ATOM   N N   .  ASP A 1 169 ?  1.472   0.733   8.38    1.00 92.50 ?  169 ASP A N   1 
1317 ATOM   C CA  .  ASP A 1 169 ?  2.616   1.383   7.747   1.00 92.50 ?  169 ASP A CA  1 
1318 ATOM   C C   .  ASP A 1 169 ?  3.098   2.624   8.494   1.00 92.50 ?  169 ASP A C   1 
1319 ATOM   C CB  .  ASP A 1 169 ?  2.308   1.703   6.279   1.00 92.50 ?  169 ASP A CB  1 
1320 ATOM   O O   .  ASP A 1 169 ?  3.833   3.446   7.945   1.00 92.50 ?  169 ASP A O   1 
1321 ATOM   C CG  .  ASP A 1 169 ?  3.272   1.043   5.311   1.00 92.50 ?  169 ASP A CG  1 
1322 ATOM   O OD1 .  ASP A 1 169 ?  4.2     0.316   5.727   1.00 92.50 ?  169 ASP A OD1 1 
1323 ATOM   O OD2 .  ASP A 1 169 ?  3.089   1.247   4.093   1.00 92.50 ?  169 ASP A OD2 1 
1324 ATOM   N N   .  PHE A 1 170 ?  2.725   2.734   9.765   1.00 93.44 ?  170 PHE A N   1 
1325 ATOM   C CA  .  PHE A 1 170 ?  3.371   3.668   10.681  1.00 93.44 ?  170 PHE A CA  1 
1326 ATOM   C C   .  PHE A 1 170 ?  3.23    3.266   12.147  1.00 93.44 ?  170 PHE A C   1 
1327 ATOM   C CB  .  PHE A 1 170 ?  2.849   5.091   10.465  1.00 93.44 ?  170 PHE A CB  1 
1328 ATOM   O O   .  PHE A 1 170 ?  2.253   2.629   12.541  1.00 93.44 ?  170 PHE A O   1 
1329 ATOM   C CG  .  PHE A 1 170 ?  1.446   5.33    10.955  1.00 93.44 ?  170 PHE A CG  1 
1330 ATOM   C CD1 .  PHE A 1 170 ?  0.351   4.965   10.18   1.00 93.44 ?  170 PHE A CD1 1 
1331 ATOM   C CD2 .  PHE A 1 170 ?  1.224   5.988   12.161  1.00 93.44 ?  170 PHE A CD2 1 
1332 ATOM   C CE1 .  PHE A 1 170 ?  -0.945  5.282   10.58   1.00 93.44 ?  170 PHE A CE1 1 
1333 ATOM   C CE2 .  PHE A 1 170 ?  -0.066  6.334   12.558  1.00 93.44 ?  170 PHE A CE2 1 
1334 ATOM   C CZ  .  PHE A 1 170 ?  -1.152  5.987   11.761  1.00 93.44 ?  170 PHE A CZ  1 
1335 ATOM   N N   .  ASP A 1 171 ?  4.22    3.632   12.954  1.00 93.31 ?  171 ASP A N   1 
1336 ATOM   C CA  .  ASP A 1 171 ?  4.203   3.356   14.388  1.00 93.31 ?  171 ASP A CA  1 
1337 ATOM   C C   .  ASP A 1 171 ?  4.53    4.627   15.166  1.00 93.31 ?  171 ASP A C   1 
1338 ATOM   C CB  .  ASP A 1 171 ?  5.215   2.27    14.76   1.00 93.31 ?  171 ASP A CB  1 
1339 ATOM   O O   .  ASP A 1 171 ?  5.645   5.144   15.112  1.00 93.31 ?  171 ASP A O   1 
1340 ATOM   C CG  .  ASP A 1 171 ?  5.196   1.946   16.242  1.00 93.31 ?  171 ASP A CG  1 
1341 ATOM   O OD1 .  ASP A 1 171 ?  4.169   2.192   16.911  1.00 93.31 ?  171 ASP A OD1 1 
1342 ATOM   O OD2 .  ASP A 1 171 ?  6.217   1.45    16.763  1.00 93.31 ?  171 ASP A OD2 1 
1343 ATOM   N N   .  ILE A 1 172 ?  3.542   5.119   15.903  1.00 94.12 ?  172 ILE A N   1 
1344 ATOM   C CA  .  ILE A 1 172 ?  3.686   6.346   16.682  1.00 94.12 ?  172 ILE A CA  1 
1345 ATOM   C C   .  ILE A 1 172 ?  4.707   6.156   17.8    1.00 94.12 ?  172 ILE A C   1 
1346 ATOM   C CB  .  ILE A 1 172 ?  2.334   6.771   17.3    1.00 94.12 ?  172 ILE A CB  1 
1347 ATOM   O O   .  ILE A 1 172 ?  5.446   7.073   18.152  1.00 94.12 ?  172 ILE A O   1 
1348 ATOM   C CG1 .  ILE A 1 172 ?  1.28    6.948   16.2    1.00 94.12 ?  172 ILE A CG1 1 
1349 ATOM   C CG2 .  ILE A 1 172 ?  2.502   8.057   18.105  1.00 94.12 ?  172 ILE A CG2 1 
1350 ATOM   C CD1 .  ILE A 1 172 ?  -0.14   7.058   16.712  1.00 94.12 ?  172 ILE A CD1 1 
1351 ATOM   N N   .  GLN A 1 173 ?  4.754   4.949   18.353  1.00 92.69 ?  173 GLN A N   1 
1352 ATOM   C CA  .  GLN A 1 173 ?  5.641   4.649   19.473  1.00 92.69 ?  173 GLN A CA  1 
1353 ATOM   C C   .  GLN A 1 173 ?  7.113   4.637   19.068  1.00 92.69 ?  173 GLN A C   1 
1354 ATOM   C CB  .  GLN A 1 173 ?  5.272   3.292   20.074  1.00 92.69 ?  173 GLN A CB  1 
1355 ATOM   O O   .  GLN A 1 173 ?  7.98    4.936   19.888  1.00 92.69 ?  173 GLN A O   1 
1356 ATOM   C CG  .  GLN A 1 173 ?  3.843   3.22    20.593  1.00 92.69 ?  173 GLN A CG  1 
1357 ATOM   C CD  .  GLN A 1 173 ?  3.54    1.875   21.216  1.00 92.69 ?  173 GLN A CD  1 
1358 ATOM   N NE2 .  GLN A 1 173 ?  3.376   0.861   20.381  1.00 92.69 ?  173 GLN A NE2 1 
1359 ATOM   O OE1 .  GLN A 1 173 ?  3.465   1.748   22.436  1.00 92.69 ?  173 GLN A OE1 1 
1360 ATOM   N N   .  GLN A 1 174 ?  7.395   4.306   17.813  1.00 91.38 ?  174 GLN A N   1 
1361 ATOM   C CA  .  GLN A 1 174 ?  8.761   4.351   17.302  1.00 91.38 ?  174 GLN A CA  1 
1362 ATOM   C C   .  GLN A 1 174 ?  9.212   5.802   17.162  1.00 91.38 ?  174 GLN A C   1 
1363 ATOM   C CB  .  GLN A 1 174 ?  8.85    3.638   15.95   1.00 91.38 ?  174 GLN A CB  1 
1364 ATOM   O O   .  GLN A 1 174 ?  10.365  6.13    17.432  1.00 91.38 ?  174 GLN A O   1 
1365 ATOM   C CG  .  GLN A 1 174 ?  10.27   3.516   15.415  1.00 91.38 ?  174 GLN A CG  1 
1366 ATOM   C CD  .  GLN A 1 174 ?  10.345  2.676   14.156  1.00 91.38 ?  174 GLN A CD  1 
1367 ATOM   N NE2 .  GLN A 1 174 ?  11.347  1.813   14.08   1.00 91.38 ?  174 GLN A NE2 1 
1368 ATOM   O OE1 .  GLN A 1 174 ?  9.512   2.792   13.26   1.00 91.38 ?  174 GLN A OE1 1 
1369 ATOM   N N   .  ASP A 1 175 ?  8.299   6.676   16.751  1.00 91.62 ?  175 ASP A N   1 
1370 ATOM   C CA  .  ASP A 1 175 ?  8.607   8.098   16.644  1.00 91.62 ?  175 ASP A CA  1 
1371 ATOM   C C   .  ASP A 1 175 ?  8.868   8.677   18.033  1.00 91.62 ?  175 ASP A C   1 
1372 ATOM   C CB  .  ASP A 1 175 ?  7.446   8.849   15.989  1.00 91.62 ?  175 ASP A CB  1 
1373 ATOM   O O   .  ASP A 1 175 ?  9.769   9.493   18.224  1.00 91.62 ?  175 ASP A O   1 
1374 ATOM   C CG  .  ASP A 1 175 ?  7.192   8.413   14.56   1.00 91.62 ?  175 ASP A CG  1 
1375 ATOM   O OD1 .  ASP A 1 175 ?  8.151   8.311   13.766  1.00 91.62 ?  175 ASP A OD1 1 
1376 ATOM   O OD2 .  ASP A 1 175 ?  6.011   8.193   14.219  1.00 91.62 ?  175 ASP A OD2 1 
1377 ATOM   N N   .  ALA A 1 176 ?  8.078   8.24    19.008  1.00 92.75 ?  176 ALA A N   1 
1378 ATOM   C CA  .  ALA A 1 176 ?  8.208   8.706   20.385  1.00 92.75 ?  176 ALA A CA  1 
1379 ATOM   C C   .  ALA A 1 176 ?  9.519   8.254   21.024  1.00 92.75 ?  176 ALA A C   1 
1380 ATOM   C CB  .  ALA A 1 176 ?  7.029   8.206   21.208  1.00 92.75 ?  176 ALA A CB  1 
1381 ATOM   O O   .  ALA A 1 176 ?  10.1    8.976   21.835  1.00 92.75 ?  176 ALA A O   1 
1382 ATOM   N N   .  SER A 1 177 ?  9.979   7.058   20.672  1.00 91.44 ?  177 SER A N   1 
1383 ATOM   C CA  .  SER A 1 177 ?  11.216  6.507   21.221  1.00 91.44 ?  177 SER A CA  1 
1384 ATOM   C C   .  SER A 1 177 ?  12.458  7.022   20.499  1.00 91.44 ?  177 SER A C   1 
1385 ATOM   C CB  .  SER A 1 177 ?  11.182  4.978   21.161  1.00 91.44 ?  177 SER A CB  1 
1386 ATOM   O O   .  SER A 1 177 ?  13.572  6.892   21.006  1.00 91.44 ?  177 SER A O   1 
1387 ATOM   O OG  .  SER A 1 177 ?  11.166  4.514   19.822  1.00 91.44 ?  177 SER A OG  1 
1388 ATOM   N N   .  THR A 1 178 ?  12.264  7.623   19.33   1.00 87.69 ?  178 THR A N   1 
1389 ATOM   C CA  .  THR A 1 178 ?  13.342  8.279   18.592  1.00 87.69 ?  178 THR A CA  1 
1390 ATOM   C C   .  THR A 1 178 ?  13.341  9.788   18.825  1.00 87.69 ?  178 THR A C   1 
1391 ATOM   C CB  .  THR A 1 178 ?  13.267  7.997   17.077  1.00 87.69 ?  178 THR A CB  1 
1392 ATOM   O O   .  THR A 1 178 ?  14.201  10.501  18.308  1.00 87.69 ?  178 THR A O   1 
1393 ATOM   C CG2 .  THR A 1 178 ?  13.538  6.527   16.775  1.00 87.69 ?  178 THR A CG2 1 
1394 ATOM   O OG1 .  THR A 1 178 ?  11.969  8.343   16.58   1.00 87.69 ?  178 THR A OG1 1 
1395 ATOM   N N   .  GLY A 1 179 ?  12.412  10.261  19.65   1.00 85.38 ?  179 GLY A N   1 
1396 ATOM   C CA  .  GLY A 1 179 ?  12.447  11.627  20.142  1.00 85.38 ?  179 GLY A CA  1 
1397 ATOM   C C   .  GLY A 1 179 ?  11.552  12.644  19.46   1.00 85.38 ?  179 GLY A C   1 
1398 ATOM   O O   .  GLY A 1 179 ?  11.78   13.844  19.606  1.00 85.38 ?  179 GLY A O   1 
1399 ATOM   N N   .  GLU A 1 180 ?  10.528  12.2    18.74   1.00 92.31 ?  180 GLU A N   1 
1400 ATOM   C CA  .  GLU A 1 180 ?  9.56    13.122  18.153  1.00 92.31 ?  180 GLU A CA  1 
1401 ATOM   C C   .  GLU A 1 180 ?  8.653   13.68   19.25   1.00 92.31 ?  180 GLU A C   1 
1402 ATOM   C CB  .  GLU A 1 180 ?  8.725   12.417  17.08   1.00 92.31 ?  180 GLU A CB  1 
1403 ATOM   O O   .  GLU A 1 180 ?  7.895   12.929  19.868  1.00 92.31 ?  180 GLU A O   1 
1404 ATOM   C CG  .  GLU A 1 180 ?  7.664   13.293  16.43   1.00 92.31 ?  180 GLU A CG  1 
1405 ATOM   C CD  .  GLU A 1 180 ?  8.254   14.458  15.66   1.00 92.31 ?  180 GLU A CD  1 
1406 ATOM   O OE1 .  GLU A 1 180 ?  7.881   15.611  15.966  1.00 92.31 ?  180 GLU A OE1 1 
1407 ATOM   O OE2 .  GLU A 1 180 ?  9.092   14.238  14.76   1.00 92.31 ?  180 GLU A OE2 1 
1408 ATOM   N N   .  PRO A 1 181 ?  8.722   14.992  19.53   1.00 94.81 ?  181 PRO A N   1 
1409 ATOM   C CA  .  PRO A 1 181 ?  7.903   15.466  20.652  1.00 94.81 ?  181 PRO A CA  1 
1410 ATOM   C C   .  PRO A 1 181 ?  6.397   15.307  20.464  1.00 94.81 ?  181 PRO A C   1 
1411 ATOM   C CB  .  PRO A 1 181 ?  8.267   16.95   20.756  1.00 94.81 ?  181 PRO A CB  1 
1412 ATOM   O O   .  PRO A 1 181 ?  5.671   15.053  21.423  1.00 94.81 ?  181 PRO A O   1 
1413 ATOM   C CG  .  PRO A 1 181 ?  9.599   17.064  20.099  1.00 94.81 ?  181 PRO A CG  1 
1414 ATOM   C CD  .  PRO A 1 181 ?  9.525   16.09   18.961  1.00 94.81 ?  181 PRO A CD  1 
1415 ATOM   N N   .  ALA A 1 182 ?  5.925   15.472  19.233  1.00 95.75 ?  182 ALA A N   1 
1416 ATOM   C CA  .  ALA A 1 182 ?  4.497   15.381  18.94   1.00 95.75 ?  182 ALA A CA  1 
1417 ATOM   C C   .  ALA A 1 182 ?  3.983   13.958  19.136  1.00 95.75 ?  182 ALA A C   1 
1418 ATOM   C CB  .  ALA A 1 182 ?  4.225   15.847  17.516  1.00 95.75 ?  182 ALA A CB  1 
1419 ATOM   O O   .  ALA A 1 182 ?  2.863   13.749  19.601  1.00 95.75 ?  182 ALA A O   1 
1420 ATOM   N N   .  ALA A 1 183 ?  4.807   12.976  18.788  1.00 96.06 ?  183 ALA A N   1 
1421 ATOM   C CA  .  ALA A 1 183 ?  4.438   11.574  18.949  1.00 96.06 ?  183 ALA A CA  1 
1422 ATOM   C C   .  ALA A 1 183 ?  4.491   11.172  20.42   1.00 96.06 ?  183 ALA A C   1 
1423 ATOM   C CB  .  ALA A 1 183 ?  5.364   10.69   18.133  1.00 96.06 ?  183 ALA A CB  1 
1424 ATOM   O O   .  ALA A 1 183 ?  3.607   10.465  20.902  1.00 96.06 ?  183 ALA A O   1 
1425 ATOM   N N   .  LYS A 1 184 ?  5.515   11.626  21.136  1.00 96.06 ?  184 LYS A N   1 
1426 ATOM   C CA  .  LYS A 1 184 ?  5.628   11.349  22.566  1.00 96.06 ?  184 LYS A CA  1 
1427 ATOM   C C   .  LYS A 1 184 ?  4.452   11.955  23.322  1.00 96.06 ?  184 LYS A C   1 
1428 ATOM   C CB  .  LYS A 1 184 ?  6.952   11.886  23.117  1.00 96.06 ?  184 LYS A CB  1 
1429 ATOM   O O   .  LYS A 1 184 ?  3.886   11.317  24.208  1.00 96.06 ?  184 LYS A O   1 
1430 ATOM   C CG  .  LYS A 1 184 ?  7.185   11.526  24.579  1.00 96.06 ?  184 LYS A CG  1 
1431 ATOM   C CD  .  LYS A 1 184 ?  8.498   12.095  25.099  1.00 96.06 ?  184 LYS A CD  1 
1432 ATOM   C CE  .  LYS A 1 184 ?  8.695   11.801  26.58   1.00 96.06 ?  184 LYS A CE  1 
1433 ATOM   N NZ  .  LYS A 1 184 ?  8.874   10.329  26.807  1.00 96.06 ?  184 LYS A NZ  1 
1434 ATOM   N N   .  ALA A 1 185 ?  4.081   13.177  22.959  1.00 96.75 ?  185 ALA A N   1 
1435 ATOM   C CA  .  ALA A 1 185 ?  2.941   13.845  23.578  1.00 96.75 ?  185 ALA A CA  1 
1436 ATOM   C C   .  ALA A 1 185 ?  1.652   13.071  23.318  1.00 96.75 ?  185 ALA A C   1 
1437 ATOM   C CB  .  ALA A 1 185 ?  2.815   15.269  23.053  1.00 96.75 ?  185 ALA A CB  1 
1438 ATOM   O O   .  ALA A 1 185 ?  0.79    12.993  24.19   1.00 96.75 ?  185 ALA A O   1 
1439 ATOM   N N   .  PHE A 1 186 ?  1.509   12.497  22.127  1.00 97.06 ?  186 PHE A N   1 
1440 ATOM   C CA  .  PHE A 1 186 ?  0.313   11.728  21.799  1.00 97.06 ?  186 PHE A CA  1 
1441 ATOM   C C   .  PHE A 1 186 ?  0.252   10.389  22.528  1.00 97.06 ?  186 PHE A C   1 
1442 ATOM   C CB  .  PHE A 1 186 ?  0.217   11.491  20.291  1.00 97.06 ?  186 PHE A CB  1 
1443 ATOM   O O   .  PHE A 1 186 ?  -0.813  9.999   23.001  1.00 97.06 ?  186 PHE A O   1 
1444 ATOM   C CG  .  PHE A 1 186 ?  -1.064  10.819  19.879  1.00 97.06 ?  186 PHE A CG  1 
1445 ATOM   C CD1 .  PHE A 1 186 ?  -1.104  9.448   19.648  1.00 97.06 ?  186 PHE A CD1 1 
1446 ATOM   C CD2 .  PHE A 1 186 ?  -2.236  11.557  19.757  1.00 97.06 ?  186 PHE A CD2 1 
1447 ATOM   C CE1 .  PHE A 1 186 ?  -2.291  8.825   19.272  1.00 97.06 ?  186 PHE A CE1 1 
1448 ATOM   C CE2 .  PHE A 1 186 ?  -3.43   10.941  19.396  1.00 97.06 ?  186 PHE A CE2 1 
1449 ATOM   C CZ  .  PHE A 1 186 ?  -3.456  9.574   19.141  1.00 97.06 ?  186 PHE A CZ  1 
1450 ATOM   N N   .  VAL A 1 187 ?  1.374   9.68    22.615  1.00 96.38 ?  187 VAL A N   1 
1451 ATOM   C CA  .  VAL A 1 187 ?  1.42    8.412   23.343  1.00 96.38 ?  187 VAL A CA  1 
1452 ATOM   C C   .  VAL A 1 187 ?  1.099   8.657   24.813  1.00 96.38 ?  187 VAL A C   1 
1453 ATOM   C CB  .  VAL A 1 187 ?  2.787   7.699   23.226  1.00 96.38 ?  187 VAL A CB  1 
1454 ATOM   O O   .  VAL A 1 187 ?  0.381   7.877   25.436  1.00 96.38 ?  187 VAL A O   1 
1455 ATOM   C CG1 .  VAL A 1 187 ?  2.836   6.453   24.108  1.00 96.38 ?  187 VAL A CG1 1 
1456 ATOM   C CG2 .  VAL A 1 187 ?  3.052   7.287   21.779  1.00 96.38 ?  187 VAL A CG2 1 
1457 ATOM   N N   .  ASP A 1 188 ?  1.614   9.75    25.366  1.00 95.69 ?  188 ASP A N   1 
1458 ATOM   C CA  .  ASP A 1 188 ?  1.347   10.102  26.758  1.00 95.69 ?  188 ASP A CA  1 
1459 ATOM   C C   .  ASP A 1 188 ?  -0.126  10.435  26.98   1.00 95.69 ?  188 ASP A C   1 
1460 ATOM   C CB  .  ASP A 1 188 ?  2.205   11.3    27.175  1.00 95.69 ?  188 ASP A CB  1 
1461 ATOM   O O   .  ASP A 1 188 ?  -0.686  10.126  28.032  1.00 95.69 ?  188 ASP A O   1 
1462 ATOM   C CG  .  ASP A 1 188 ?  3.686   10.972  27.24   1.00 95.69 ?  188 ASP A CG  1 
1463 ATOM   O OD1 .  ASP A 1 188 ?  4.051   9.782   27.354  1.00 95.69 ?  188 ASP A OD1 1 
1464 ATOM   O OD2 .  ASP A 1 188 ?  4.504   11.915  27.193  1.00 95.69 ?  188 ASP A OD2 1 
1465 ATOM   N N   .  LYS A 1 189 ?  -0.751  11.075  25.997  1.00 96.12 ?  189 LYS A N   1 
1466 ATOM   C CA  .  LYS A 1 189 ?  -2.159  11.455  26.086  1.00 96.12 ?  189 LYS A CA  1 
1467 ATOM   C C   .  LYS A 1 189 ?  -3.12   10.296  25.847  1.00 96.12 ?  189 LYS A C   1 
1468 ATOM   C CB  .  LYS A 1 189 ?  -2.476  12.576  25.093  1.00 96.12 ?  189 LYS A CB  1 
1469 ATOM   O O   .  LYS A 1 189 ?  -4.139  10.203  26.527  1.00 96.12 ?  189 LYS A O   1 
1470 ATOM   C CG  .  LYS A 1 189 ?  -1.927  13.935  25.502  1.00 96.12 ?  189 LYS A CG  1 
1471 ATOM   C CD  .  LYS A 1 189 ?  -2.183  14.977  24.423  1.00 96.12 ?  189 LYS A CD  1 
1472 ATOM   C CE  .  LYS A 1 189 ?  -1.58   16.318  24.808  1.00 96.12 ?  189 LYS A CE  1 
1473 ATOM   N NZ  .  LYS A 1 189 ?  -1.882  17.314  23.728  1.00 96.12 ?  189 LYS A NZ  1 
1474 ATOM   N N   .  ILE A 1 190 ?  -2.832  9.441   24.872  1.00 96.56 ?  190 ILE A N   1 
1475 ATOM   C CA  .  ILE A 1 190 ?  -3.73   8.337   24.537  1.00 96.56 ?  190 ILE A CA  1 
1476 ATOM   C C   .  ILE A 1 190 ?  -3.573  7.163   25.502  1.00 96.56 ?  190 ILE A C   1 
1477 ATOM   C CB  .  ILE A 1 190 ?  -3.556  7.869   23.072  1.00 96.56 ?  190 ILE A CB  1 
1478 ATOM   O O   .  ILE A 1 190 ?  -4.501  6.375   25.684  1.00 96.56 ?  190 ILE A O   1 
1479 ATOM   C CG1 .  ILE A 1 190 ?  -4.785  7.061   22.637  1.00 96.56 ?  190 ILE A CG1 1 
1480 ATOM   C CG2 .  ILE A 1 190 ?  -2.277  7.052   22.889  1.00 96.56 ?  190 ILE A CG2 1 
1481 ATOM   C CD1 .  ILE A 1 190 ?  -4.88   6.795   21.147  1.00 96.56 ?  190 ILE A CD1 1 
1482 ATOM   N N   .  GLY A 1 191 ?  -2.409  7.054   26.134  1.00 95.56 ?  191 GLY A N   1 
1483 ATOM   C CA  .  GLY A 1 191 ?  -2.158  5.978   27.075  1.00 95.56 ?  191 GLY A CA  1 
1484 ATOM   C C   .  GLY A 1 191 ?  -1.783  4.664   26.416  1.00 95.56 ?  191 GLY A C   1 
1485 ATOM   O O   .  GLY A 1 191 ?  -1.441  4.599   25.234  1.00 95.56 ?  191 GLY A O   1 
1486 ATOM   N N   .  GLN A 1 192 ?  -1.839  3.595   27.202  1.00 95.75 ?  192 GLN A N   1 
1487 ATOM   C CA  .  GLN A 1 192 ?  -1.484  2.26    26.732  1.00 95.75 ?  192 GLN A CA  1 
1488 ATOM   C C   .  GLN A 1 192 ?  -2.71   1.423   26.375  1.00 95.75 ?  192 GLN A C   1 
1489 ATOM   C CB  .  GLN A 1 192 ?  -0.685  1.53    27.814  1.00 95.75 ?  192 GLN A CB  1 
1490 ATOM   O O   .  GLN A 1 192 ?  -3.778  1.573   26.967  1.00 95.75 ?  192 GLN A O   1 
1491 ATOM   C CG  .  GLN A 1 192 ?  0.738   2.035   28.007  1.00 95.75 ?  192 GLN A CG  1 
1492 ATOM   C CD  .  GLN A 1 192 ?  1.606   1.789   26.789  1.00 95.75 ?  192 GLN A CD  1 
1493 ATOM   N NE2 .  GLN A 1 192 ?  2.396   2.781   26.406  1.00 95.75 ?  192 GLN A NE2 1 
1494 ATOM   O OE1 .  GLN A 1 192 ?  1.56    0.717   26.188  1.00 95.75 ?  192 GLN A OE1 1 
1495 ATOM   N N   .  GLY A 1 193 ?  -2.537  0.526   25.41   1.00 95.38 ?  193 GLY A N   1 
1496 ATOM   C CA  .  GLY A 1 193 ?  -3.586  -0.401  25.024  1.00 95.38 ?  193 GLY A CA  1 
1497 ATOM   C C   .  GLY A 1 193 ?  -4.575  0.115   23.997  1.00 95.38 ?  193 GLY A C   1 
1498 ATOM   O O   .  GLY A 1 193 ?  -5.672  -0.427  23.869  1.00 95.38 ?  193 GLY A O   1 
1499 ATOM   N N   .  ARG A 1 194 ?  -4.198  1.158   23.264  1.00 96.19 ?  194 ARG A N   1 
1500 ATOM   C CA  .  ARG A 1 194 ?  -5.052  1.733   22.226  1.00 96.19 ?  194 ARG A CA  1 
1501 ATOM   C C   .  ARG A 1 194 ?  -4.377  1.827   20.86   1.00 96.19 ?  194 ARG A C   1 
1502 ATOM   C CB  .  ARG A 1 194 ?  -5.548  3.117   22.659  1.00 96.19 ?  194 ARG A CB  1 
1503 ATOM   O O   .  ARG A 1 194 ?  -4.948  2.387   19.926  1.00 96.19 ?  194 ARG A O   1 
1504 ATOM   C CG  .  ARG A 1 194 ?  -6.667  3.091   23.697  1.00 96.19 ?  194 ARG A CG  1 
1505 ATOM   C CD  .  ARG A 1 194 ?  -6.168  3.248   25.126  1.00 96.19 ?  194 ARG A CD  1 
1506 ATOM   N NE  .  ARG A 1 194 ?  -7.279  3.227   26.078  1.00 96.19 ?  194 ARG A NE  1 
1507 ATOM   N NH1 .  ARG A 1 194 ?  -5.993  3.456   27.996  1.00 96.19 ?  194 ARG A NH1 1 
1508 ATOM   N NH2 .  ARG A 1 194 ?  -8.241  3.295   28.146  1.00 96.19 ?  194 ARG A NH2 1 
1509 ATOM   C CZ  .  ARG A 1 194 ?  -7.159  3.324   27.396  1.00 96.19 ?  194 ARG A CZ  1 
1510 ATOM   N N   .  LEU A 1 195 ?  -3.172  1.28    20.74   1.00 96.19 ?  195 LEU A N   1 
1511 ATOM   C CA  .  LEU A 1 195 ?  -2.422  1.311   19.486  1.00 96.19 ?  195 LEU A CA  1 
1512 ATOM   C C   .  LEU A 1 195 ?  -1.881  -0.061  19.095  1.00 96.19 ?  195 LEU A C   1 
1513 ATOM   C CB  .  LEU A 1 195 ?  -1.241  2.281   19.604  1.00 96.19 ?  195 LEU A CB  1 
1514 ATOM   O O   .  LEU A 1 195 ?  -1.289  -0.761  19.917  1.00 96.19 ?  195 LEU A O   1 
1515 ATOM   C CG  .  LEU A 1 195 ?  -1.536  3.76    19.871  1.00 96.19 ?  195 LEU A CG  1 
1516 ATOM   C CD1 .  LEU A 1 195 ?  -0.224  4.5     20.107  1.00 96.19 ?  195 LEU A CD1 1 
1517 ATOM   C CD2 .  LEU A 1 195 ?  -2.284  4.396   18.705  1.00 96.19 ?  195 LEU A CD2 1 
1518 ATOM   N N   .  ILE A 1 196 ?  -2.071  -0.419  17.829  1.00 95.44 ?  196 ILE A N   1 
1519 ATOM   C CA  .  ILE A 1 196 ?  -1.486  -1.625  17.245  1.00 95.44 ?  196 ILE A CA  1 
1520 ATOM   C C   .  ILE A 1 196 ?  -0.721  -1.261  15.972  1.00 95.44 ?  196 ILE A C   1 
1521 ATOM   C CB  .  ILE A 1 196 ?  -2.559  -2.672  16.869  1.00 95.44 ?  196 ILE A CB  1 
1522 ATOM   O O   .  ILE A 1 196 ?  -1.339  -0.941  14.957  1.00 95.44 ?  196 ILE A O   1 
1523 ATOM   C CG1 .  ILE A 1 196 ?  -3.27   -3.187  18.127  1.00 95.44 ?  196 ILE A CG1 1 
1524 ATOM   C CG2 .  ILE A 1 196 ?  -1.913  -3.822  16.098  1.00 95.44 ?  196 ILE A CG2 1 
1525 ATOM   C CD1 .  ILE A 1 196 ?  -4.541  -3.97   17.853  1.00 95.44 ?  196 ILE A CD1 1 
1526 ATOM   N N   .  PRO A 1 197 ?  0.622   -1.288  16.001  1.00 94.50 ?  197 PRO A N   1 
1527 ATOM   C CA  .  PRO A 1 197 ?  1.357   -1.025  14.758  1.00 94.50 ?  197 PRO A CA  1 
1528 ATOM   C C   .  PRO A 1 197 ?  1.458   -2.213  13.803  1.00 94.50 ?  197 PRO A C   1 
1529 ATOM   C CB  .  PRO A 1 197 ?  2.749   -0.652  15.27   1.00 94.50 ?  197 PRO A CB  1 
1530 ATOM   O O   .  PRO A 1 197 ?  1.586   -3.361  14.228  1.00 94.50 ?  197 PRO A O   1 
1531 ATOM   C CG  .  PRO A 1 197 ?  2.905   -1.49   16.491  1.00 94.50 ?  197 PRO A CG  1 
1532 ATOM   C CD  .  PRO A 1 197 ?  1.543   -1.526  17.127  1.00 94.50 ?  197 PRO A CD  1 
1533 ATOM   N N   .  VAL A 1 198 ?  1.415   -1.933  12.505  1.00 93.62 ?  198 VAL A N   1 
1534 ATOM   C CA  .  VAL A 1 198 ?  1.617   -2.949  11.473  1.00 93.62 ?  198 VAL A CA  1 
1535 ATOM   C C   .  VAL A 1 198 ?  2.647   -2.441  10.468  1.00 93.62 ?  198 VAL A C   1 
1536 ATOM   C CB  .  VAL A 1 198 ?  0.305   -3.291  10.731  1.00 93.62 ?  198 VAL A CB  1 
1537 ATOM   O O   .  VAL A 1 198 ?  2.319   -1.676  9.561   1.00 93.62 ?  198 VAL A O   1 
1538 ATOM   C CG1 .  VAL A 1 198 ?  0.552   -4.368  9.679   1.00 93.62 ?  198 VAL A CG1 1 
1539 ATOM   C CG2 .  VAL A 1 198 ?  -0.77   -3.768  11.705  1.00 93.62 ?  198 VAL A CG2 1 
1540 ATOM   N N   .  ILE A 1 199 ?  3.9     -2.847  10.648  1.00 92.25 ?  199 ILE A N   1 
1541 ATOM   C CA  .  ILE A 1 199 ?  5.018   -2.337  9.856   1.00 92.25 ?  199 ILE A CA  1 
1542 ATOM   C C   .  ILE A 1 199 ?  5.587   -3.44   8.967   1.00 92.25 ?  199 ILE A C   1 
1543 ATOM   C CB  .  ILE A 1 199 ?  6.146   -1.809  10.777  1.00 92.25 ?  199 ILE A CB  1 
1544 ATOM   O O   .  ILE A 1 199 ?  5.777   -4.563  9.43    1.00 92.25 ?  199 ILE A O   1 
1545 ATOM   C CG1 .  ILE A 1 199 ?  5.612   -0.809  11.811  1.00 92.25 ?  199 ILE A CG1 1 
1546 ATOM   C CG2 .  ILE A 1 199 ?  7.272   -1.172  9.963   1.00 92.25 ?  199 ILE A CG2 1 
1547 ATOM   C CD1 .  ILE A 1 199 ?  4.952   0.439   11.253  1.00 92.25 ?  199 ILE A CD1 1 
1548 ATOM   N N   .  PHE A 1 200 ?  5.87    -3.132  7.705   1.00 92.94 ?  200 PHE A N   1 
1549 ATOM   C CA  .  PHE A 1 200 ?  6.401   -4.11   6.759   1.00 92.94 ?  200 PHE A CA  1 
1550 ATOM   C C   .  PHE A 1 200 ?  7.829   -3.759  6.347   1.00 92.94 ?  200 PHE A C   1 
1551 ATOM   C CB  .  PHE A 1 200 ?  5.532   -4.15   5.498   1.00 92.94 ?  200 PHE A CB  1 
1552 ATOM   O O   .  PHE A 1 200 ?  8.216   -2.591  6.376   1.00 92.94 ?  200 PHE A O   1 
1553 ATOM   C CG  .  PHE A 1 200 ?  4.088   -4.477  5.763   1.00 92.94 ?  200 PHE A CG  1 
1554 ATOM   C CD1 .  PHE A 1 200 ?  3.666   -5.799  5.858   1.00 92.94 ?  200 PHE A CD1 1 
1555 ATOM   C CD2 .  PHE A 1 200 ?  3.151   -3.459  5.902   1.00 92.94 ?  200 PHE A CD2 1 
1556 ATOM   C CE1 .  PHE A 1 200 ?  2.331   -6.102  6.114   1.00 92.94 ?  200 PHE A CE1 1 
1557 ATOM   C CE2 .  PHE A 1 200 ?  1.813   -3.752  6.145   1.00 92.94 ?  200 PHE A CE2 1 
1558 ATOM   C CZ  .  PHE A 1 200 ?  1.404   -5.076  6.261   1.00 92.94 ?  200 PHE A CZ  1 
1559 ATOM   N N   .  ASP A 1 201 ?  8.6     -4.759  5.934   1.00 93.06 ?  201 ASP A N   1 
1560 ATOM   C CA  .  ASP A 1 201 ?  9.943   -4.534  5.403   1.00 93.06 ?  201 ASP A CA  1 
1561 ATOM   C C   .  ASP A 1 201 ?  10.057  -5.064  3.975   1.00 93.06 ?  201 ASP A C   1 
1562 ATOM   C CB  .  ASP A 1 201 ?  11.001  -5.202  6.284   1.00 93.06 ?  201 ASP A CB  1 
1563 ATOM   O O   .  ASP A 1 201 ?  10.522  -6.18   3.738   1.00 93.06 ?  201 ASP A O   1 
1564 ATOM   C CG  .  ASP A 1 201 ?  12.415  -4.892  5.831   1.00 93.06 ?  201 ASP A CG  1 
1565 ATOM   O OD1 .  ASP A 1 201 ?  12.593  -4.09   4.892   1.00 93.06 ?  201 ASP A OD1 1 
1566 ATOM   O OD2 .  ASP A 1 201 ?  13.367  -5.46   6.407   1.00 93.06 ?  201 ASP A OD2 1 
1567 ATOM   N N   .  THR A 1 202 ?  9.638   -4.246  3.016   1.00 96.06 ?  202 THR A N   1 
1568 ATOM   C CA  .  THR A 1 202 ?  9.612   -4.645  1.611   1.00 96.06 ?  202 THR A CA  1 
1569 ATOM   C C   .  THR A 1 202 ?  10.984  -4.616  0.943   1.00 96.06 ?  202 THR A C   1 
1570 ATOM   C CB  .  THR A 1 202 ?  8.663   -3.755  0.783   1.00 96.06 ?  202 THR A CB  1 
1571 ATOM   O O   .  THR A 1 202 ?  11.117  -5.046  -0.203  1.00 96.06 ?  202 THR A O   1 
1572 ATOM   C CG2 .  THR A 1 202 ?  7.219   -3.904  1.246   1.00 96.06 ?  202 THR A CG2 1 
1573 ATOM   O OG1 .  THR A 1 202 ?  9.053   -2.384  0.924   1.00 96.06 ?  202 THR A OG1 1 
1574 ATOM   N N   .  LYS A 1 203 ?  12.012  -4.173  1.661   1.00 96.31 ?  203 LYS A N   1 
1575 ATOM   C CA  .  LYS A 1 203 ?  13.383  -4.214  1.15    1.00 96.31 ?  203 LYS A CA  1 
1576 ATOM   C C   .  LYS A 1 203 ?  13.733  -5.644  0.757   1.00 96.31 ?  203 LYS A C   1 
1577 ATOM   C CB  .  LYS A 1 203 ?  14.403  -3.755  2.199   1.00 96.31 ?  203 LYS A CB  1 
1578 ATOM   O O   .  LYS A 1 203 ?  14.423  -5.9    -0.228  1.00 96.31 ?  203 LYS A O   1 
1579 ATOM   C CG  .  LYS A 1 203 ?  14.233  -2.358  2.779   1.00 96.31 ?  203 LYS A CG  1 
1580 ATOM   C CD  .  LYS A 1 203 ?  15.42   -2.01   3.668   1.00 96.31 ?  203 LYS A CD  1 
1581 ATOM   C CE  .  LYS A 1 203 ?  15.197  -0.736  4.466   1.00 96.31 ?  203 LYS A CE  1 
1582 ATOM   N NZ  .  LYS A 1 203 ?  14.285  -1.029  5.622   1.00 96.31 ?  203 LYS A NZ  1 
1583 ATOM   N N   .  GLN A 1 204 ?  13.253  -6.576  1.574   1.00 96.19 ?  204 GLN A N   1 
1584 ATOM   C CA  .  GLN A 1 204 ?  13.583  -7.991  1.447   1.00 96.19 ?  204 GLN A CA  1 
1585 ATOM   C C   .  GLN A 1 204 ?  12.938  -8.631  0.221   1.00 96.19 ?  204 GLN A C   1 
1586 ATOM   C CB  .  GLN A 1 204 ?  13.123  -8.719  2.713   1.00 96.19 ?  204 GLN A CB  1 
1587 ATOM   O O   .  GLN A 1 204 ?  13.571  -9.411  -0.49   1.00 96.19 ?  204 GLN A O   1 
1588 ATOM   C CG  .  GLN A 1 204 ?  13.798  -8.228  3.988   1.00 96.19 ?  204 GLN A CG  1 
1589 ATOM   C CD  .  GLN A 1 204 ?  13.362  -9.012  5.208   1.00 96.19 ?  204 GLN A CD  1 
1590 ATOM   N NE2 .  GLN A 1 204 ?  13.342  -8.364  6.362   1.00 96.19 ?  204 GLN A NE2 1 
1591 ATOM   O OE1 .  GLN A 1 204 ?  13.055  -10.198 5.12    1.00 96.19 ?  204 GLN A OE1 1 
1592 ATOM   N N   .  ALA A 1 205 ?  11.673  -8.309  -0.021  1.00 97.69 ?  205 ALA A N   1 
1593 ATOM   C CA  .  ALA A 1 205 ?  10.939  -8.881  -1.145  1.00 97.69 ?  205 ALA A CA  1 
1594 ATOM   C C   .  ALA A 1 205 ?  11.356  -8.241  -2.467  1.00 97.69 ?  205 ALA A C   1 
1595 ATOM   C CB  .  ALA A 1 205 ?  9.446   -8.697  -0.93   1.00 97.69 ?  205 ALA A CB  1 
1596 ATOM   O O   .  ALA A 1 205 ?  11.409  -8.903  -3.503  1.00 97.69 ?  205 ALA A O   1 
1597 ATOM   N N   .  ALA A 1 206 ?  11.642  -6.944  -2.429  1.00 98.69 ?  206 ALA A N   1 
1598 ATOM   C CA  .  ALA A 1 206 ?  12.024  -6.205  -3.628  1.00 98.69 ?  206 ALA A CA  1 
1599 ATOM   C C   .  ALA A 1 206 ?  13.406  -6.609  -4.138  1.00 98.69 ?  206 ALA A C   1 
1600 ATOM   C CB  .  ALA A 1 206 ?  11.979  -4.716  -3.338  1.00 98.69 ?  206 ALA A CB  1 
1601 ATOM   O O   .  ALA A 1 206 ?  13.69   -6.505  -5.331  1.00 98.69 ?  206 ALA A O   1 
1602 ATOM   N N   .  TYR A 1 207 ?  14.255  -7.104  -3.243  1.00 98.81 ?  207 TYR A N   1 
1603 ATOM   C CA  .  TYR A 1 207 ?  15.556  -7.646  -3.624  1.00 98.81 ?  207 TYR A CA  1 
1604 ATOM   C C   .  TYR A 1 207 ?  15.398  -8.809  -4.6    1.00 98.81 ?  207 TYR A C   1 
1605 ATOM   C CB  .  TYR A 1 207 ?  16.307  -8.113  -2.376  1.00 98.81 ?  207 TYR A CB  1 
1606 ATOM   O O   .  TYR A 1 207 ?  16.168  -8.946  -5.552  1.00 98.81 ?  207 TYR A O   1 
1607 ATOM   C CG  .  TYR A 1 207 ?  17.749  -8.486  -2.645  1.00 98.81 ?  207 TYR A CG  1 
1608 ATOM   C CD1 .  TYR A 1 207 ?  18.099  -9.801  -2.952  1.00 98.81 ?  207 TYR A CD1 1 
1609 ATOM   C CD2 .  TYR A 1 207 ?  18.761  -7.527  -2.581  1.00 98.81 ?  207 TYR A CD2 1 
1610 ATOM   C CE1 .  TYR A 1 207 ?  19.43   -10.156 -3.156  1.00 98.81 ?  207 TYR A CE1 1 
1611 ATOM   C CE2 .  TYR A 1 207 ?  20.093  -7.88   -2.786  1.00 98.81 ?  207 TYR A CE2 1 
1612 ATOM   O OH  .  TYR A 1 207 ?  21.735  -9.553  -3.26   1.00 98.81 ?  207 TYR A OH  1 
1613 ATOM   C CZ  .  TYR A 1 207 ?  20.421  -9.194  -3.068  1.00 98.81 ?  207 TYR A CZ  1 
1614 ATOM   N N   .  ILE A 1 208 ?  14.384  -9.635  -4.363  1.00 98.75 ?  208 ILE A N   1 
1615 ATOM   C CA  .  ILE A 1 208 ?  14.088  -10.774 -5.228  1.00 98.75 ?  208 ILE A CA  1 
1616 ATOM   C C   .  ILE A 1 208 ?  13.654  -10.261 -6.598  1.00 98.75 ?  208 ILE A C   1 
1617 ATOM   C CB  .  ILE A 1 208 ?  12.979  -11.672 -4.631  1.00 98.75 ?  208 ILE A CB  1 
1618 ATOM   O O   .  ILE A 1 208 ?  14.114  -10.753 -7.627  1.00 98.75 ?  208 ILE A O   1 
1619 ATOM   C CG1 .  ILE A 1 208 ?  13.423  -12.236 -3.275  1.00 98.75 ?  208 ILE A CG1 1 
1620 ATOM   C CG2 .  ILE A 1 208 ?  12.627  -12.802 -5.596  1.00 98.75 ?  208 ILE A CG2 1 
1621 ATOM   C CD1 .  ILE A 1 208 ?  12.306  -12.841 -2.446  1.00 98.75 ?  208 ILE A CD1 1 
1622 ATOM   N N   .  ALA A 1 209 ?  12.784  -9.257  -6.611  1.00 98.88 ?  209 ALA A N   1 
1623 ATOM   C CA  .  ALA A 1 209 ?  12.304  -8.677  -7.861  1.00 98.88 ?  209 ALA A CA  1 
1624 ATOM   C C   .  ALA A 1 209 ?  13.445  -8.042  -8.654  1.00 98.88 ?  209 ALA A C   1 
1625 ATOM   C CB  .  ALA A 1 209 ?  11.222  -7.644  -7.579  1.00 98.88 ?  209 ALA A CB  1 
1626 ATOM   O O   .  ALA A 1 209 ?  13.497  -8.164  -9.877  1.00 98.88 ?  209 ALA A O   1 
1627 ATOM   N N   .  GLY A 1 210 ?  14.357  -7.365  -7.964  1.00 98.88 ?  210 GLY A N   1 
1628 ATOM   C CA  .  GLY A 1 210 ?  15.486  -6.737  -8.628  1.00 98.88 ?  210 GLY A CA  1 
1629 ATOM   C C   .  GLY A 1 210 ?  16.412  -7.718  -9.319  1.00 98.88 ?  210 GLY A C   1 
1630 ATOM   O O   .  GLY A 1 210 ?  16.768  -7.524  -10.481 1.00 98.88 ?  210 GLY A O   1 
1631 ATOM   N N   .  ARG A 1 211 ?  16.8    -8.783  -8.624  1.00 98.81 ?  211 ARG A N   1 
1632 ATOM   C CA  .  ARG A 1 211 ?  17.667  -9.796  -9.224  1.00 98.81 ?  211 ARG A CA  1 
1633 ATOM   C C   .  ARG A 1 211 ?  16.953  -10.514 -10.362 1.00 98.81 ?  211 ARG A C   1 
1634 ATOM   C CB  .  ARG A 1 211 ?  18.108  -10.842 -8.198  1.00 98.81 ?  211 ARG A CB  1 
1635 ATOM   O O   .  ARG A 1 211 ?  17.555  -10.803 -11.394 1.00 98.81 ?  211 ARG A O   1 
1636 ATOM   C CG  .  ARG A 1 211 ?  19.195  -10.375 -7.242  1.00 98.81 ?  211 ARG A CG  1 
1637 ATOM   C CD  .  ARG A 1 211 ?  19.724  -11.53  -6.403  1.00 98.81 ?  211 ARG A CD  1 
1638 ATOM   N NE  .  ARG A 1 211 ?  20.388  -12.548 -7.218  1.00 98.81 ?  211 ARG A NE  1 
1639 ATOM   N NH1 .  ARG A 1 211 ?  22.47   -11.519 -7.334  1.00 98.81 ?  211 ARG A NH1 1 
1640 ATOM   N NH2 .  ARG A 1 211 ?  22.107  -13.5   -8.363  1.00 98.81 ?  211 ARG A NH2 1 
1641 ATOM   C CZ  .  ARG A 1 211 ?  21.654  -12.515 -7.617  1.00 98.81 ?  211 ARG A CZ  1 
1642 ATOM   N N   .  ALA A 1 212 ?  15.675  -10.811 -10.157 1.00 98.94 ?  212 ALA A N   1 
1643 ATOM   C CA  .  ALA A 1 212 ?  14.879  -11.512 -11.158 1.00 98.94 ?  212 ALA A CA  1 
1644 ATOM   C C   .  ALA A 1 212 ?  14.771  -10.695 -12.441 1.00 98.94 ?  212 ALA A C   1 
1645 ATOM   C CB  .  ALA A 1 212 ?  13.492  -11.798 -10.608 1.00 98.94 ?  212 ALA A CB  1 
1646 ATOM   O O   .  ALA A 1 212 ?  14.83   -11.244 -13.54  1.00 98.94 ?  212 ALA A O   1 
1647 ATOM   N N   .  LEU A 1 213 ?  14.602  -9.385  -12.305 1.00 98.94 ?  213 LEU A N   1 
1648 ATOM   C CA  .  LEU A 1 213 ?  14.496  -8.503  -13.461 1.00 98.94 ?  213 LEU A CA  1 
1649 ATOM   C C   .  LEU A 1 213 ?  15.774  -8.502  -14.294 1.00 98.94 ?  213 LEU A C   1 
1650 ATOM   C CB  .  LEU A 1 213 ?  14.203  -7.075  -12.996 1.00 98.94 ?  213 LEU A CB  1 
1651 ATOM   O O   .  LEU A 1 213 ?  15.722  -8.55   -15.522 1.00 98.94 ?  213 LEU A O   1 
1652 ATOM   C CG  .  LEU A 1 213 ?  13.978  -6.078  -14.136 1.00 98.94 ?  213 LEU A CG  1 
1653 ATOM   C CD1 .  LEU A 1 213 ?  12.642  -6.315  -14.826 1.00 98.94 ?  213 LEU A CD1 1 
1654 ATOM   C CD2 .  LEU A 1 213 ?  14.048  -4.665  -13.584 1.00 98.94 ?  213 LEU A CD2 1 
1655 ATOM   N N   .  ALA A 1 214 ?  16.917  -8.424  -13.621 1.00 98.88 ?  214 ALA A N   1 
1656 ATOM   C CA  .  ALA A 1 214 ?  18.204  -8.402  -14.307 1.00 98.88 ?  214 ALA A CA  1 
1657 ATOM   C C   .  ALA A 1 214 ?  18.486  -9.745  -14.976 1.00 98.88 ?  214 ALA A C   1 
1658 ATOM   C CB  .  ALA A 1 214 ?  19.311  -8.043  -13.325 1.00 98.88 ?  214 ALA A CB  1 
1659 ATOM   O O   .  ALA A 1 214 ?  18.976  -9.796  -16.104 1.00 98.88 ?  214 ALA A O   1 
1660 ATOM   N N   .  ASP A 1 215 ?  18.154  -10.832 -14.286 1.00 98.88 ?  215 ASP A N   1 
1661 ATOM   C CA  .  ASP A 1 215 ?  18.296  -12.177 -14.835 1.00 98.88 ?  215 ASP A CA  1 
1662 ATOM   C C   .  ASP A 1 215 ?  17.374  -12.384 -16.033 1.00 98.88 ?  215 ASP A C   1 
1663 ATOM   C CB  .  ASP A 1 215 ?  17.962  -13.208 -13.755 1.00 98.88 ?  215 ASP A CB  1 
1664 ATOM   O O   .  ASP A 1 215 ?  17.744  -13.023 -17.017 1.00 98.88 ?  215 ASP A O   1 
1665 ATOM   C CG  .  ASP A 1 215 ?  18.234  -14.63  -14.203 1.00 98.88 ?  215 ASP A CG  1 
1666 ATOM   O OD1 .  ASP A 1 215 ?  19.3    -14.884 -14.803 1.00 98.88 ?  215 ASP A OD1 1 
1667 ATOM   O OD2 .  ASP A 1 215 ?  17.379  -15.503 -13.943 1.00 98.88 ?  215 ASP A OD2 1 
1668 ATOM   N N   .  TYR A 1 216 ?  16.167  -11.836 -15.954 1.00 98.81 ?  216 TYR A N   1 
1669 ATOM   C CA  .  TYR A 1 216 ?  15.201  -11.915 -17.044 1.00 98.81 ?  216 TYR A CA  1 
1670 ATOM   C C   .  TYR A 1 216 ?  15.677  -11.127 -18.26  1.00 98.81 ?  216 TYR A C   1 
1671 ATOM   C CB  .  TYR A 1 216 ?  13.85   -11.381 -16.562 1.00 98.81 ?  216 TYR A CB  1 
1672 ATOM   O O   .  TYR A 1 216 ?  15.635  -11.627 -19.385 1.00 98.81 ?  216 TYR A O   1 
1673 ATOM   C CG  .  TYR A 1 216 ?  12.809  -11.27  -17.653 1.00 98.81 ?  216 TYR A CG  1 
1674 ATOM   C CD1 .  TYR A 1 216 ?  12.441  -10.023 -18.159 1.00 98.81 ?  216 TYR A CD1 1 
1675 ATOM   C CD2 .  TYR A 1 216 ?  12.184  -12.408 -18.165 1.00 98.81 ?  216 TYR A CD2 1 
1676 ATOM   C CE1 .  TYR A 1 216 ?  11.468  -9.915  -19.149 1.00 98.81 ?  216 TYR A CE1 1 
1677 ATOM   C CE2 .  TYR A 1 216 ?  11.229  -12.305 -19.173 1.00 98.81 ?  216 TYR A CE2 1 
1678 ATOM   O OH  .  TYR A 1 216 ?  9.965   -10.951 -20.683 1.00 98.81 ?  216 TYR A OH  1 
1679 ATOM   C CZ  .  TYR A 1 216 ?  10.883  -11.059 -19.664 1.00 98.81 ?  216 TYR A CZ  1 
1680 ATOM   N N   .  PHE A 1 217 ?  16.143  -9.901  -18.043 1.00 98.75 ?  217 PHE A N   1 
1681 ATOM   C CA  .  PHE A 1 217 ?  16.605  -9.064  -19.145 1.00 98.75 ?  217 PHE A CA  1 
1682 ATOM   C C   .  PHE A 1 217 ?  17.835  -9.653  -19.826 1.00 98.75 ?  217 PHE A C   1 
1683 ATOM   C CB  .  PHE A 1 217 ?  16.978  -7.659  -18.664 1.00 98.75 ?  217 PHE A CB  1 
1684 ATOM   O O   .  PHE A 1 217 ?  17.991  -9.522  -21.038 1.00 98.75 ?  217 PHE A O   1 
1685 ATOM   C CG  .  PHE A 1 217 ?  15.82   -6.72   -18.457 1.00 98.75 ?  217 PHE A CG  1 
1686 ATOM   C CD1 .  PHE A 1 217 ?  14.75   -6.656  -19.347 1.00 98.75 ?  217 PHE A CD1 1 
1687 ATOM   C CD2 .  PHE A 1 217 ?  15.877  -5.792  -17.424 1.00 98.75 ?  217 PHE A CD2 1 
1688 ATOM   C CE1 .  PHE A 1 217 ?  13.829  -5.614  -19.279 1.00 98.75 ?  217 PHE A CE1 1 
1689 ATOM   C CE2 .  PHE A 1 217 ?  14.974  -4.735  -17.359 1.00 98.75 ?  217 PHE A CE2 1 
1690 ATOM   C CZ  .  PHE A 1 217 ?  13.963  -4.631  -18.307 1.00 98.75 ?  217 PHE A CZ  1 
1691 ATOM   N N   .  SER A 1 218 ?  18.721  -10.283 -19.062 1.00 98.38 ?  218 SER A N   1 
1692 ATOM   C CA  .  SER A 1 218 ?  19.923  -10.877 -19.638 1.00 98.38 ?  218 SER A CA  1 
1693 ATOM   C C   .  SER A 1 218 ?  19.585  -12.043 -20.563 1.00 98.38 ?  218 SER A C   1 
1694 ATOM   C CB  .  SER A 1 218 ?  20.857  -11.359 -18.528 1.00 98.38 ?  218 SER A CB  1 
1695 ATOM   O O   .  SER A 1 218 ?  20.285  -12.291 -21.545 1.00 98.38 ?  218 SER A O   1 
1696 ATOM   O OG  .  SER A 1 218 ?  20.294  -12.447 -17.815 1.00 98.38 ?  218 SER A OG  1 
1697 ATOM   N N   .  LYS A 1 219 ?  18.516  -12.762 -20.237 1.00 97.88 ?  219 LYS A N   1 
1698 ATOM   C CA  .  LYS A 1 219 ?  18.102  -13.936 -20.999 1.00 97.88 ?  219 LYS A CA  1 
1699 ATOM   C C   .  LYS A 1 219 ?  17.322  -13.596 -22.264 1.00 97.88 ?  219 LYS A C   1 
1700 ATOM   C CB  .  LYS A 1 219 ?  17.273  -14.869 -20.112 1.00 97.88 ?  219 LYS A CB  1 
1701 ATOM   O O   .  LYS A 1 219 ?  17.466  -14.295 -23.266 1.00 97.88 ?  219 LYS A O   1 
1702 ATOM   C CG  .  LYS A 1 219 ?  18.091  -15.551 -19.022 1.00 97.88 ?  219 LYS A CG  1 
1703 ATOM   C CD  .  LYS A 1 219 ?  17.216  -16.352 -18.071 1.00 97.88 ?  219 LYS A CD  1 
1704 ATOM   C CE  .  LYS A 1 219 ?  18.056  -17.014 -16.99  1.00 97.88 ?  219 LYS A CE  1 
1705 ATOM   N NZ  .  LYS A 1 219 ?  17.168  -17.792 -16.064 1.00 97.88 ?  219 LYS A NZ  1 
1706 ATOM   N N   .  ILE A 1 220 ?  16.496  -12.556 -22.228 1.00 97.12 ?  220 ILE A N   1 
1707 ATOM   C CA  .  ILE A 1 220 ?  15.686  -12.196 -23.392 1.00 97.12 ?  220 ILE A CA  1 
1708 ATOM   C C   .  ILE A 1 220 ?  16.272  -11.067 -24.238 1.00 97.12 ?  220 ILE A C   1 
1709 ATOM   C CB  .  ILE A 1 220 ?  14.22   -11.854 -23.036 1.00 97.12 ?  220 ILE A CB  1 
1710 ATOM   O O   .  ILE A 1 220 ?  15.9    -10.914 -25.4   1.00 97.12 ?  220 ILE A O   1 
1711 ATOM   C CG1 .  ILE A 1 220 ?  14.104  -10.555 -22.232 1.00 97.12 ?  220 ILE A CG1 1 
1712 ATOM   C CG2 .  ILE A 1 220 ?  13.57   -13.012 -22.279 1.00 97.12 ?  220 ILE A CG2 1 
1713 ATOM   C CD1 .  ILE A 1 220 ?  12.773  -9.857  -22.423 1.00 97.12 ?  220 ILE A CD1 1 
1714 ATOM   N N   .  TYR A 1 221 ?  17.191  -10.289 -23.675 1.00 97.38 ?  221 TYR A N   1 
1715 ATOM   C CA  .  TYR A 1 221 ?  17.844  -9.201  -24.398 1.00 97.38 ?  221 TYR A CA  1 
1716 ATOM   C C   .  TYR A 1 221 ?  19.361  -9.351  -24.341 1.00 97.38 ?  221 TYR A C   1 
1717 ATOM   C CB  .  TYR A 1 221 ?  17.444  -7.838  -23.825 1.00 97.38 ?  221 TYR A CB  1 
1718 ATOM   O O   .  TYR A 1 221 ?  20.091  -8.404  -24.045 1.00 97.38 ?  221 TYR A O   1 
1719 ATOM   C CG  .  TYR A 1 221 ?  15.977  -7.485  -23.947 1.00 97.38 ?  221 TYR A CG  1 
1720 ATOM   C CD1 .  TYR A 1 221 ?  15.276  -7.669  -25.14  1.00 97.38 ?  221 TYR A CD1 1 
1721 ATOM   C CD2 .  TYR A 1 221 ?  15.3    -6.926  -22.863 1.00 97.38 ?  221 TYR A CD2 1 
1722 ATOM   C CE1 .  TYR A 1 221 ?  13.929  -7.323  -25.24  1.00 97.38 ?  221 TYR A CE1 1 
1723 ATOM   C CE2 .  TYR A 1 221 ?  13.954  -6.584  -22.958 1.00 97.38 ?  221 TYR A CE2 1 
1724 ATOM   O OH  .  TYR A 1 221 ?  11.941  -6.455  -24.237 1.00 97.38 ?  221 TYR A OH  1 
1725 ATOM   C CZ  .  TYR A 1 221 ?  13.274  -6.785  -24.147 1.00 97.38 ?  221 TYR A CZ  1 
1726 ATOM   N N   .  LYS A 1 222 ?  19.83   -10.555 -24.652 1.00 95.38 ?  222 LYS A N   1 
1727 ATOM   C CA  .  LYS A 1 222 ?  21.261  -10.826 -24.763 1.00 95.38 ?  222 LYS A CA  1 
1728 ATOM   C C   .  LYS A 1 222 ?  21.91   -9.939  -25.821 1.00 95.38 ?  222 LYS A C   1 
1729 ATOM   C CB  .  LYS A 1 222 ?  21.479  -12.301 -25.112 1.00 95.38 ?  222 LYS A CB  1 
1730 ATOM   O O   .  LYS A 1 222 ?  23.033  -9.468  -25.648 1.00 95.38 ?  222 LYS A O   1 
1731 ATOM   C CG  .  LYS A 1 222 ?  22.941  -12.722 -25.126 1.00 95.38 ?  222 LYS A CG  1 
1732 ATOM   C CD  .  LYS A 1 222 ?  23.089  -14.171 -25.565 1.00 95.38 ?  222 LYS A CD  1 
1733 ATOM   C CE  .  LYS A 1 222 ?  24.547  -14.602 -25.543 1.00 95.38 ?  222 LYS A CE  1 
1734 ATOM   N NZ  .  LYS A 1 222 ?  24.649  -16.016 -26.031 1.00 95.38 ?  222 LYS A NZ  1 
1735 ATOM   N N   .  ASP A 1 223 ?  21.192  -9.73   -26.918 1.00 96.56 ?  223 ASP A N   1 
1736 ATOM   C CA  .  ASP A 1 223 ?  21.691  -8.945  -28.044 1.00 96.56 ?  223 ASP A CA  1 
1737 ATOM   C C   .  ASP A 1 223 ?  21.149  -7.516  -28.06  1.00 96.56 ?  223 ASP A C   1 
1738 ATOM   C CB  .  ASP A 1 223 ?  21.308  -9.647  -29.35  1.00 96.56 ?  223 ASP A CB  1 
1739 ATOM   O O   .  ASP A 1 223 ?  21.445  -6.744  -28.971 1.00 96.56 ?  223 ASP A O   1 
1740 ATOM   C CG  .  ASP A 1 223 ?  21.963  -11.008 -29.491 1.00 96.56 ?  223 ASP A CG  1 
1741 ATOM   O OD1 .  ASP A 1 223 ?  23.198  -11.103 -29.328 1.00 96.56 ?  223 ASP A OD1 1 
1742 ATOM   O OD2 .  ASP A 1 223 ?  21.243  -11.994 -29.757 1.00 96.56 ?  223 ASP A OD2 1 
1743 ATOM   N N   .  ASN A 1 224 ?  20.361  -7.16   -27.051 1.00 97.12 ?  224 ASN A N   1 
1744 ATOM   C CA  .  ASN A 1 224 ?  19.746  -5.838  -26.972 1.00 97.12 ?  224 ASN A CA  1 
1745 ATOM   C C   .  ASN A 1 224 ?  20.028  -5.164  -25.629 1.00 97.12 ?  224 ASN A C   1 
1746 ATOM   C CB  .  ASN A 1 224 ?  18.234  -5.957  -27.184 1.00 97.12 ?  224 ASN A CB  1 
1747 ATOM   O O   .  ASN A 1 224 ?  19.129  -5.025  -24.798 1.00 97.12 ?  224 ASN A O   1 
1748 ATOM   C CG  .  ASN A 1 224 ?  17.867  -6.537  -28.532 1.00 97.12 ?  224 ASN A CG  1 
1749 ATOM   N ND2 .  ASN A 1 224 ?  18.243  -5.851  -29.6   1.00 97.12 ?  224 ASN A ND2 1 
1750 ATOM   O OD1 .  ASN A 1 224 ?  17.225  -7.581  -28.611 1.00 97.12 ?  224 ASN A OD1 1 
1751 ATOM   N N   .  PRO A 1 225 ?  21.274  -4.721  -25.394 1.00 96.12 ?  225 PRO A N   1 
1752 ATOM   C CA  .  PRO A 1 225 ?  21.568  -4.172  -24.065 1.00 96.12 ?  225 PRO A CA  1 
1753 ATOM   C C   .  PRO A 1 225 ?  20.843  -2.868  -23.742 1.00 96.12 ?  225 PRO A C   1 
1754 ATOM   C CB  .  PRO A 1 225 ?  23.085  -3.974  -24.106 1.00 96.12 ?  225 PRO A CB  1 
1755 ATOM   O O   .  PRO A 1 225 ?  20.626  -2.54   -22.577 1.00 96.12 ?  225 PRO A O   1 
1756 ATOM   C CG  .  PRO A 1 225 ?  23.388  -3.751  -25.547 1.00 96.12 ?  225 PRO A CG  1 
1757 ATOM   C CD  .  PRO A 1 225 ?  22.469  -4.706  -26.257 1.00 96.12 ?  225 PRO A CD  1 
1758 ATOM   N N   .  GLU A 1 226 ?  20.452  -2.129  -24.774 1.00 96.19 ?  226 GLU A N   1 
1759 ATOM   C CA  .  GLU A 1 226 ?  19.716  -0.879  -24.602 1.00 96.19 ?  226 GLU A CA  1 
1760 ATOM   C C   .  GLU A 1 226 ?  18.289  -1.088  -24.098 1.00 96.19 ?  226 GLU A C   1 
1761 ATOM   C CB  .  GLU A 1 226 ?  19.707  -0.073  -25.906 1.00 96.19 ?  226 GLU A CB  1 
1762 ATOM   O O   .  GLU A 1 226 ?  17.655  -0.149  -23.619 1.00 96.19 ?  226 GLU A O   1 
1763 ATOM   C CG  .  GLU A 1 226 ?  18.841  -0.622  -27.036 1.00 96.19 ?  226 GLU A CG  1 
1764 ATOM   C CD  .  GLU A 1 226 ?  19.354  -1.928  -27.617 1.00 96.19 ?  226 GLU A CD  1 
1765 ATOM   O OE1 .  GLU A 1 226 ?  18.523  -2.769  -28.022 1.00 96.19 ?  226 GLU A OE1 1 
1766 ATOM   O OE2 .  GLU A 1 226 ?  20.584  -2.134  -27.69  1.00 96.19 ?  226 GLU A OE2 1 
1767 ATOM   N N   .  LYS A 1 227 ?  17.786  -2.315  -24.184 1.00 97.75 ?  227 LYS A N   1 
1768 ATOM   C CA  .  LYS A 1 227 ?  16.439  -2.633  -23.714 1.00 97.75 ?  227 LYS A CA  1 
1769 ATOM   C C   .  LYS A 1 227 ?  16.419  -3.109  -22.265 1.00 97.75 ?  227 LYS A C   1 
1770 ATOM   C CB  .  LYS A 1 227 ?  15.792  -3.698  -24.604 1.00 97.75 ?  227 LYS A CB  1 
1771 ATOM   O O   .  LYS A 1 227 ?  15.351  -3.297  -21.685 1.00 97.75 ?  227 LYS A O   1 
1772 ATOM   C CG  .  LYS A 1 227 ?  15.549  -3.243  -26.037 1.00 97.75 ?  227 LYS A CG  1 
1773 ATOM   C CD  .  LYS A 1 227 ?  14.782  -4.294  -26.824 1.00 97.75 ?  227 LYS A CD  1 
1774 ATOM   C CE  .  LYS A 1 227 ?  14.601  -3.879  -28.275 1.00 97.75 ?  227 LYS A CE  1 
1775 ATOM   N NZ  .  LYS A 1 227 ?  13.798  -4.931  -28.981 1.00 97.75 ?  227 LYS A NZ  1 
1776 ATOM   N N   .  ARG A 1 228 ?  17.595  -3.293  -21.673 1.00 98.62 ?  228 ARG A N   1 
1777 ATOM   C CA  .  ARG A 1 228 ?  17.72   -3.765  -20.294 1.00 98.62 ?  228 ARG A CA  1 
1778 ATOM   C C   .  ARG A 1 228 ?  17.656  -2.597  -19.314 1.00 98.62 ?  228 ARG A C   1 
1779 ATOM   C CB  .  ARG A 1 228 ?  19.034  -4.536  -20.127 1.00 98.62 ?  228 ARG A CB  1 
1780 ATOM   O O   .  ARG A 1 228 ?  18.59   -2.357  -18.549 1.00 98.62 ?  228 ARG A O   1 
1781 ATOM   C CG  .  ARG A 1 228 ?  19.215  -5.678  -21.121 1.00 98.62 ?  228 ARG A CG  1 
1782 ATOM   C CD  .  ARG A 1 228 ?  20.29   -6.665  -20.684 1.00 98.62 ?  228 ARG A CD  1 
1783 ATOM   N NE  .  ARG A 1 228 ?  21.601  -6.026  -20.559 1.00 98.62 ?  228 ARG A NE  1 
1784 ATOM   N NH1 .  ARG A 1 228 ?  22.715  -7.264  -22.187 1.00 98.62 ?  228 ARG A NH1 1 
1785 ATOM   N NH2 .  ARG A 1 228 ?  23.798  -5.672  -21.003 1.00 98.62 ?  228 ARG A NH2 1 
1786 ATOM   C CZ  .  ARG A 1 228 ?  22.686  -6.329  -21.259 1.00 98.62 ?  228 ARG A CZ  1 
1787 ATOM   N N   .  THR A 1 229 ?  16.552  -1.859  -19.36  1.00 98.75 ?  229 THR A N   1 
1788 ATOM   C CA  .  THR A 1 229 ?  16.398  -0.628  -18.586 1.00 98.75 ?  229 THR A CA  1 
1789 ATOM   C C   .  THR A 1 229 ?  15.137  -0.591  -17.728 1.00 98.75 ?  229 THR A C   1 
1790 ATOM   C CB  .  THR A 1 229 ?  16.347  0.612   -19.504 1.00 98.75 ?  229 THR A CB  1 
1791 ATOM   O O   .  THR A 1 229 ?  14.112  -1.177  -18.079 1.00 98.75 ?  229 THR A O   1 
1792 ATOM   C CG2 .  THR A 1 229 ?  17.652  0.79    -20.271 1.00 98.75 ?  229 THR A CG2 1 
1793 ATOM   O OG1 .  THR A 1 229 ?  15.273  0.467   -20.443 1.00 98.75 ?  229 THR A OG1 1 
1794 ATOM   N N   .  ILE A 1 230 ?  15.224  0.116   -16.606 1.00 98.88 ?  230 ILE A N   1 
1795 ATOM   C CA  .  ILE A 1 230 ?  14.097  0.324   -15.698 1.00 98.88 ?  230 ILE A CA  1 
1796 ATOM   C C   .  ILE A 1 230 ?  14.029  1.778   -15.232 1.00 98.88 ?  230 ILE A C   1 
1797 ATOM   C CB  .  ILE A 1 230 ?  14.171  -0.614  -14.467 1.00 98.88 ?  230 ILE A CB  1 
1798 ATOM   O O   .  ILE A 1 230 ?  15.059  2.405   -14.981 1.00 98.88 ?  230 ILE A O   1 
1799 ATOM   C CG1 .  ILE A 1 230 ?  12.902  -0.469  -13.619 1.00 98.88 ?  230 ILE A CG1 1 
1800 ATOM   C CG2 .  ILE A 1 230 ?  15.422  -0.339  -13.629 1.00 98.88 ?  230 ILE A CG2 1 
1801 ATOM   C CD1 .  ILE A 1 230 ?  12.649  -1.587  -12.632 1.00 98.88 ?  230 ILE A CD1 1 
1802 ATOM   N N   .  GLY A 1 231 ?  12.82   2.315   -15.107 1.00 98.69 ?  231 GLY A N   1 
1803 ATOM   C CA  .  GLY A 1 231 ?  12.63   3.616   -14.489 1.00 98.69 ?  231 GLY A CA  1 
1804 ATOM   C C   .  GLY A 1 231 ?  11.263  3.772   -13.851 1.00 98.69 ?  231 GLY A C   1 
1805 ATOM   O O   .  GLY A 1 231 ?  10.314  3.084   -14.229 1.00 98.69 ?  231 GLY A O   1 
1806 ATOM   N N   .  ALA A 1 232 ?  11.147  4.678   -12.886 1.00 98.62 ?  232 ALA A N   1 
1807 ATOM   C CA  .  ALA A 1 232 ?  9.879   4.923   -12.206 1.00 98.62 ?  232 ALA A CA  1 
1808 ATOM   C C   .  ALA A 1 232 ?  9.79    6.309   -11.57  1.00 98.62 ?  232 ALA A C   1 
1809 ATOM   C CB  .  ALA A 1 232 ?  9.635   3.852   -11.159 1.00 98.62 ?  232 ALA A CB  1 
1810 ATOM   O O   .  ALA A 1 232 ?  10.679  7.146   -11.727 1.00 98.62 ?  232 ALA A O   1 
1811 ATOM   N N   .  PHE A 1 233 ?  8.692   6.538   -10.858 1.00 98.56 ?  233 PHE A N   1 
1812 ATOM   C CA  .  PHE A 1 233 ?  8.372   7.827   -10.255 1.00 98.56 ?  233 PHE A CA  1 
1813 ATOM   C C   .  PHE A 1 233 ?  7.676   7.587   -8.92   1.00 98.56 ?  233 PHE A C   1 
1814 ATOM   C CB  .  PHE A 1 233 ?  7.437   8.616   -11.175 1.00 98.56 ?  233 PHE A CB  1 
1815 ATOM   O O   .  PHE A 1 233 ?  7.22    6.476   -8.646  1.00 98.56 ?  233 PHE A O   1 
1816 ATOM   C CG  .  PHE A 1 233 ?  6.156   7.894   -11.495 1.00 98.56 ?  233 PHE A CG  1 
1817 ATOM   C CD1 .  PHE A 1 233 ?  6.03    7.192   -12.688 1.00 98.56 ?  233 PHE A CD1 1 
1818 ATOM   C CD2 .  PHE A 1 233 ?  5.096   7.883   -10.595 1.00 98.56 ?  233 PHE A CD2 1 
1819 ATOM   C CE1 .  PHE A 1 233 ?  4.894   6.432   -12.953 1.00 98.56 ?  233 PHE A CE1 1 
1820 ATOM   C CE2 .  PHE A 1 233 ?  3.963   7.112   -10.841 1.00 98.56 ?  233 PHE A CE2 1 
1821 ATOM   C CZ  .  PHE A 1 233 ?  3.858   6.391   -12.025 1.00 98.56 ?  233 PHE A CZ  1 
1822 ATOM   N N   .  GLY A 1 234 ?  7.612   8.63    -8.099  1.00 96.69 ?  234 GLY A N   1 
1823 ATOM   C CA  .  GLY A 1 234 ?  7.074   8.509   -6.757  1.00 96.69 ?  234 GLY A CA  1 
1824 ATOM   C C   .  GLY A 1 234 ?  6.069   9.52    -6.247  1.00 96.69 ?  234 GLY A C   1 
1825 ATOM   O O   .  GLY A 1 234 ?  5.896   10.595  -6.817  1.00 96.69 ?  234 GLY A O   1 
1826 ATOM   N N   .  GLY A 1 235 ?  5.427   9.161   -5.141  1.00 93.00 ?  235 GLY A N   1 
1827 ATOM   C CA  .  GLY A 1 235 ?  4.375   9.965   -4.544  1.00 93.00 ?  235 GLY A CA  1 
1828 ATOM   C C   .  GLY A 1 235 ?  4.84    10.899  -3.442  1.00 93.00 ?  235 GLY A C   1 
1829 ATOM   O O   .  GLY A 1 235 ?  4.717   12.116  -3.582  1.00 93.00 ?  235 GLY A O   1 
1830 ATOM   N N   .  ILE A 1 236 ?  5.328   10.34   -2.339  1.00 91.44 ?  236 ILE A N   1 
1831 ATOM   C CA  .  ILE A 1 236 ?  5.807   11.111  -1.191  1.00 91.44 ?  236 ILE A CA  1 
1832 ATOM   C C   .  ILE A 1 236 ?  6.954   10.364  -0.505  1.00 91.44 ?  236 ILE A C   1 
1833 ATOM   C CB  .  ILE A 1 236 ?  4.7     11.31   -0.126  1.00 91.44 ?  236 ILE A CB  1 
1834 ATOM   O O   .  ILE A 1 236 ?  6.794   9.185   -0.184  1.00 91.44 ?  236 ILE A O   1 
1835 ATOM   C CG1 .  ILE A 1 236 ?  3.486   12.05   -0.703  1.00 91.44 ?  236 ILE A CG1 1 
1836 ATOM   C CG2 .  ILE A 1 236 ?  5.241   12.079  1.081   1.00 91.44 ?  236 ILE A CG2 1 
1837 ATOM   C CD1 .  ILE A 1 236 ?  2.293   12.142  0.233   1.00 91.44 ?  236 ILE A CD1 1 
1838 ATOM   N N   .  PRO A 1 237 ?  8.101   11.015  -0.242  1.00 90.50 ?  237 PRO A N   1 
1839 ATOM   C CA  .  PRO A 1 237 ?  9.189   10.285  0.422   1.00 90.50 ?  237 PRO A CA  1 
1840 ATOM   C C   .  PRO A 1 237 ?  8.998   9.955   1.902   1.00 90.50 ?  237 PRO A C   1 
1841 ATOM   C CB  .  PRO A 1 237 ?  10.39   11.214  0.227   1.00 90.50 ?  237 PRO A CB  1 
1842 ATOM   O O   .  PRO A 1 237 ?  9.003   10.84   2.76    1.00 90.50 ?  237 PRO A O   1 
1843 ATOM   C CG  .  PRO A 1 237 ?  9.788   12.573  0.217   1.00 90.50 ?  237 PRO A CG  1 
1844 ATOM   C CD  .  PRO A 1 237 ?  8.503   12.4    -0.546  1.00 90.50 ?  237 PRO A CD  1 
1845 ATOM   N N   .  TRP A 1 238 ?  8.861   8.668   2.205   1.00 89.31 ?  238 TRP A N   1 
1846 ATOM   C CA  .  TRP A 1 238 ?  8.806   8.186   3.583   1.00 89.31 ?  238 TRP A CA  1 
1847 ATOM   C C   .  TRP A 1 238 ?  9.278   6.733   3.649   1.00 89.31 ?  238 TRP A C   1 
1848 ATOM   C CB  .  TRP A 1 238 ?  7.369   8.299   4.101   1.00 89.31 ?  238 TRP A CB  1 
1849 ATOM   O O   .  TRP A 1 238 ?  8.99    5.969   2.731   1.00 89.31 ?  238 TRP A O   1 
1850 ATOM   C CG  .  TRP A 1 238 ?  7.265   8.127   5.588   1.00 89.31 ?  238 TRP A CG  1 
1851 ATOM   C CD1 .  TRP A 1 238 ?  6.78    7.049   6.263   1.00 89.31 ?  238 TRP A CD1 1 
1852 ATOM   C CD2 .  TRP A 1 238 ?  7.725   9.035   6.601   1.00 89.31 ?  238 TRP A CD2 1 
1853 ATOM   C CE2 .  TRP A 1 238 ?  7.605   8.373   7.846   1.00 89.31 ?  238 TRP A CE2 1 
1854 ATOM   C CE3 .  TRP A 1 238 ?  8.336   10.296  6.571   1.00 89.31 ?  238 TRP A CE3 1 
1855 ATOM   N NE1 .  TRP A 1 238 ?  6.971   7.181   7.613   1.00 89.31 ?  238 TRP A NE1 1 
1856 ATOM   C CH2 .  TRP A 1 238 ?  8.74    10.134  8.969   1.00 89.31 ?  238 TRP A CH2 1 
1857 ATOM   C CZ2 .  TRP A 1 238 ?  8.15    8.896   9.022   1.00 89.31 ?  238 TRP A CZ2 1 
1858 ATOM   C CZ3 .  TRP A 1 238 ?  8.829   10.842  7.755   1.00 89.31 ?  238 TRP A CZ3 1 
1859 ATOM   N N   .  PRO A 1 239 ?  9.989   6.31    4.71    1.00 89.12 ?  239 PRO A N   1 
1860 ATOM   C CA  .  PRO A 1 239 ?  10.417  4.904   4.753   1.00 89.12 ?  239 PRO A CA  1 
1861 ATOM   C C   .  PRO A 1 239 ?  9.339   3.833   4.612   1.00 89.12 ?  239 PRO A C   1 
1862 ATOM   C CB  .  PRO A 1 239 ?  11.083  4.777   6.124   1.00 89.12 ?  239 PRO A CB  1 
1863 ATOM   O O   .  PRO A 1 239 ?  9.645   2.692   4.27    1.00 89.12 ?  239 PRO A O   1 
1864 ATOM   C CG  .  PRO A 1 239 ?  11.535  6.15    6.445   1.00 89.12 ?  239 PRO A CG  1 
1865 ATOM   C CD  .  PRO A 1 239 ?  10.455  7.036   5.905   1.00 89.12 ?  239 PRO A CD  1 
1866 ATOM   N N   .  SER A 1 240 ?  8.082   4.189   4.85    1.00 88.75 ?  240 SER A N   1 
1867 ATOM   C CA  .  SER A 1 240 ?  6.978   3.255   4.646   1.00 88.75 ?  240 SER A CA  1 
1868 ATOM   C C   .  SER A 1 240 ?  6.769   2.935   3.168   1.00 88.75 ?  240 SER A C   1 
1869 ATOM   C CB  .  SER A 1 240 ?  5.688   3.84    5.224   1.00 88.75 ?  240 SER A CB  1 
1870 ATOM   O O   .  SER A 1 240 ?  6.063   1.987   2.826   1.00 88.75 ?  240 SER A O   1 
1871 ATOM   O OG  .  SER A 1 240 ?  5.87    4.198   6.584   1.00 88.75 ?  240 SER A OG  1 
1872 ATOM   N N   .  VAL A 1 241 ?  7.371   3.737   2.297   1.00 93.44 ?  241 VAL A N   1 
1873 ATOM   C CA  .  VAL A 1 241 ?  7.234   3.587   0.85    1.00 93.44 ?  241 VAL A CA  1 
1874 ATOM   C C   .  VAL A 1 241 ?  8.593   3.577   0.152   1.00 93.44 ?  241 VAL A C   1 
1875 ATOM   C CB  .  VAL A 1 241 ?  6.35    4.705   0.241   1.00 93.44 ?  241 VAL A CB  1 
1876 ATOM   O O   .  VAL A 1 241 ?  8.666   3.218   -1.019  1.00 93.44 ?  241 VAL A O   1 
1877 ATOM   C CG1 .  VAL A 1 241 ?  5.945   4.392   -1.199  1.00 93.44 ?  241 VAL A CG1 1 
1878 ATOM   C CG2 .  VAL A 1 241 ?  5.077   4.898   1.064   1.00 93.44 ?  241 VAL A CG2 1 
1879 ATOM   N N   .  SER A 1 242 ?  9.667   3.948   0.844   1.00 94.12 ?  242 SER A N   1 
1880 ATOM   C CA  .  SER A 1 242 ?  10.994  4.048   0.238   1.00 94.12 ?  242 SER A CA  1 
1881 ATOM   C C   .  SER A 1 242 ?  11.882  2.816   0.413   1.00 94.12 ?  242 SER A C   1 
1882 ATOM   C CB  .  SER A 1 242 ?  11.738  5.28    0.759   1.00 94.12 ?  242 SER A CB  1 
1883 ATOM   O O   .  SER A 1 242 ?  13.094  2.871   0.203   1.00 94.12 ?  242 SER A O   1 
1884 ATOM   O OG  .  SER A 1 242 ?  12.204  5.092   2.083   1.00 94.12 ?  242 SER A OG  1 
1885 ATOM   N N   .  ASP A 1 243 ?  11.282  1.7     0.81    1.00 95.75 ?  243 ASP A N   1 
1886 ATOM   C CA  .  ASP A 1 243 ?  12.018  0.465   1.072   1.00 95.75 ?  243 ASP A CA  1 
1887 ATOM   C C   .  ASP A 1 243 ?  12.347  -0.374  -0.162  1.00 95.75 ?  243 ASP A C   1 
1888 ATOM   C CB  .  ASP A 1 243 ?  11.202  -0.411  2.027   1.00 95.75 ?  243 ASP A CB  1 
1889 ATOM   O O   .  ASP A 1 243 ?  13.205  -1.255  -0.115  1.00 95.75 ?  243 ASP A O   1 
1890 ATOM   C CG  .  ASP A 1 243 ?  11.373  -0.023  3.484   1.00 95.75 ?  243 ASP A CG  1 
1891 ATOM   O OD1 .  ASP A 1 243 ?  12.206  0.849   3.811   1.00 95.75 ?  243 ASP A OD1 1 
1892 ATOM   O OD2 .  ASP A 1 243 ?  10.687  -0.636  4.329   1.00 95.75 ?  243 ASP A OD2 1 
1893 ATOM   N N   .  PHE A 1 244 ?  11.651  -0.162  -1.271  1.00 98.19 ?  244 PHE A N   1 
1894 ATOM   C CA  .  PHE A 1 244 ?  11.703  -1.122  -2.369  1.00 98.19 ?  244 PHE A CA  1 
1895 ATOM   C C   .  PHE A 1 244 ?  12.964  -1.059  -3.231  1.00 98.19 ?  244 PHE A C   1 
1896 ATOM   C CB  .  PHE A 1 244 ?  10.482  -0.957  -3.276  1.00 98.19 ?  244 PHE A CB  1 
1897 ATOM   O O   .  PHE A 1 244 ?  13.382  -2.094  -3.743  1.00 98.19 ?  244 PHE A O   1 
1898 ATOM   C CG  .  PHE A 1 244 ?  9.157   -1.232  -2.61   1.00 98.19 ?  244 PHE A CG  1 
1899 ATOM   C CD1 .  PHE A 1 244 ?  8.492   -2.429  -2.855  1.00 98.19 ?  244 PHE A CD1 1 
1900 ATOM   C CD2 .  PHE A 1 244 ?  8.531   -0.276  -1.814  1.00 98.19 ?  244 PHE A CD2 1 
1901 ATOM   C CE1 .  PHE A 1 244 ?  7.203   -2.644  -2.369  1.00 98.19 ?  244 PHE A CE1 1 
1902 ATOM   C CE2 .  PHE A 1 244 ?  7.253   -0.489  -1.305  1.00 98.19 ?  244 PHE A CE2 1 
1903 ATOM   C CZ  .  PHE A 1 244 ?  6.578   -1.668  -1.602  1.00 98.19 ?  244 PHE A CZ  1 
1904 ATOM   N N   .  ILE A 1 245 ?  13.587  0.099   -3.428  1.00 98.50 ?  245 ILE A N   1 
1905 ATOM   C CA  .  ILE A 1 245 ?  14.79   0.197   -4.257  1.00 98.50 ?  245 ILE A CA  1 
1906 ATOM   C C   .  ILE A 1 245 ?  15.997  -0.23   -3.431  1.00 98.50 ?  245 ILE A C   1 
1907 ATOM   C CB  .  ILE A 1 245 ?  15.03   1.597   -4.881  1.00 98.50 ?  245 ILE A CB  1 
1908 ATOM   O O   .  ILE A 1 245 ?  16.983  -0.735  -3.969  1.00 98.50 ?  245 ILE A O   1 
1909 ATOM   C CG1 .  ILE A 1 245 ?  14.828  1.538   -6.396  1.00 98.50 ?  245 ILE A CG1 1 
1910 ATOM   C CG2 .  ILE A 1 245 ?  16.396  2.179   -4.511  1.00 98.50 ?  245 ILE A CG2 1 
1911 ATOM   C CD1 .  ILE A 1 245 ?  14.717  2.912   -7.022  1.00 98.50 ?  245 ILE A CD1 1 
1912 ATOM   N N   .  ALA A 1 246 ?  15.886  -0.068  -2.116  1.00 98.31 ?  246 ALA A N   1 
1913 ATOM   C CA  .  ALA A 1 246 ?  16.887  -0.595  -1.198  1.00 98.31 ?  246 ALA A CA  1 
1914 ATOM   C C   .  ALA A 1 246 ?  17.072  -2.071  -1.542  1.00 98.31 ?  246 ALA A C   1 
1915 ATOM   C CB  .  ALA A 1 246 ?  16.44   -0.399  0.245   1.00 98.31 ?  246 ALA A CB  1 
1916 ATOM   O O   .  ALA A 1 246 ?  18.195  -2.57   -1.574  1.00 98.31 ?  246 ALA A O   1 
1917 ATOM   N N   .  GLY A 1 247 ?  15.977  -2.75   -1.869  1.00 98.50 ?  247 GLY A N   1 
1918 ATOM   C CA  .  GLY A 1 247 ?  16.062  -4.085  -2.433  1.00 98.50 ?  247 GLY A CA  1 
1919 ATOM   C C   .  GLY A 1 247 ?  16.263  -4.146  -3.935  1.00 98.50 ?  247 GLY A C   1 
1920 ATOM   O O   .  GLY A 1 247 ?  17.159  -4.846  -4.404  1.00 98.50 ?  247 GLY A O   1 
1921 ATOM   N N   .  THR A 1 248 ?  15.425  -3.46   -4.705  1.00 98.88 ?  248 THR A N   1 
1922 ATOM   C CA  .  THR A 1 248 ?  15.396  -3.62   -6.158  1.00 98.88 ?  248 THR A CA  1 
1923 ATOM   C C   .  THR A 1 248 ?  16.71   -3.243  -6.833  1.00 98.88 ?  248 THR A C   1 
1924 ATOM   C CB  .  THR A 1 248 ?  14.265  -2.803  -6.819  1.00 98.88 ?  248 THR A CB  1 
1925 ATOM   O O   .  THR A 1 248 ?  17.215  -4.012  -7.651  1.00 98.88 ?  248 THR A O   1 
1926 ATOM   C CG2 .  THR A 1 248 ?  14.117  -3.133  -8.298  1.00 98.88 ?  248 THR A CG2 1 
1927 ATOM   O OG1 .  THR A 1 248 ?  13.022  -3.1    -6.171  1.00 98.88 ?  248 THR A OG1 1 
1928 ATOM   N N   .  PHE A 1 249 ?  17.277  -2.084  -6.516  1.00 98.81 ?  249 PHE A N   1 
1929 ATOM   C CA  .  PHE A 1 249 ?  18.543  -1.702  -7.136  1.00 98.81 ?  249 PHE A CA  1 
1930 ATOM   C C   .  PHE A 1 249 ?  19.694  -2.478  -6.511  1.00 98.81 ?  249 PHE A C   1 
1931 ATOM   C CB  .  PHE A 1 249 ?  18.844  -0.202  -7.042  1.00 98.81 ?  249 PHE A CB  1 
1932 ATOM   O O   .  PHE A 1 249 ?  20.617  -2.848  -7.23   1.00 98.81 ?  249 PHE A O   1 
1933 ATOM   C CG  .  PHE A 1 249 ?  18.139  0.663   -8.057  1.00 98.81 ?  249 PHE A CG  1 
1934 ATOM   C CD1 .  PHE A 1 249 ?  17.678  0.179   -9.281  1.00 98.81 ?  249 PHE A CD1 1 
1935 ATOM   C CD2 .  PHE A 1 249 ?  18.012  2.024   -7.8    1.00 98.81 ?  249 PHE A CD2 1 
1936 ATOM   C CE1 .  PHE A 1 249 ?  17.118  1.034   -10.225 1.00 98.81 ?  249 PHE A CE1 1 
1937 ATOM   C CE2 .  PHE A 1 249 ?  17.466  2.887   -8.743  1.00 98.81 ?  249 PHE A CE2 1 
1938 ATOM   C CZ  .  PHE A 1 249 ?  17.035  2.395   -9.967  1.00 98.81 ?  249 PHE A CZ  1 
1939 ATOM   N N   .  GLN A 1 250 ?  19.669  -2.753  -5.212  1.00 98.81 ?  250 GLN A N   1 
1940 ATOM   C CA  .  GLN A 1 250 ?  20.756  -3.521  -4.611  1.00 98.81 ?  250 GLN A CA  1 
1941 ATOM   C C   .  GLN A 1 250 ?  20.801  -4.922  -5.211  1.00 98.81 ?  250 GLN A C   1 
1942 ATOM   C CB  .  GLN A 1 250 ?  20.604  -3.592  -3.09   1.00 98.81 ?  250 GLN A CB  1 
1943 ATOM   O O   .  GLN A 1 250 ?  21.878  -5.477  -5.425  1.00 98.81 ?  250 GLN A O   1 
1944 ATOM   C CG  .  GLN A 1 250 ?  21.843  -4.083  -2.352  1.00 98.81 ?  250 GLN A CG  1 
1945 ATOM   C CD  .  GLN A 1 250 ?  23.034  -3.16   -2.521  1.00 98.81 ?  250 GLN A CD  1 
1946 ATOM   N NE2 .  GLN A 1 250 ?  24.186  -3.731  -2.837  1.00 98.81 ?  250 GLN A NE2 1 
1947 ATOM   O OE1 .  GLN A 1 250 ?  22.925  -1.944  -2.38   1.00 98.81 ?  250 GLN A OE1 1 
1948 ATOM   N N   .  GLY A 1 251 ?  19.631  -5.482  -5.501  1.00 98.81 ?  251 GLY A N   1 
1949 ATOM   C CA  .  GLY A 1 251 ?  19.551  -6.765  -6.177  1.00 98.81 ?  251 GLY A CA  1 
1950 ATOM   C C   .  GLY A 1 251 ?  20.061  -6.709  -7.603  1.00 98.81 ?  251 GLY A C   1 
1951 ATOM   O O   .  GLY A 1 251 ?  20.754  -7.625  -8.042  1.00 98.81 ?  251 GLY A O   1 
1952 ATOM   N N   .  ILE A 1 252 ?  19.738  -5.643  -8.328  1.00 98.94 ?  252 ILE A N   1 
1953 ATOM   C CA  .  ILE A 1 252 ?  20.234  -5.458  -9.691  1.00 98.94 ?  252 ILE A CA  1 
1954 ATOM   C C   .  ILE A 1 252 ?  21.737  -5.188  -9.677  1.00 98.94 ?  252 ILE A C   1 
1955 ATOM   C CB  .  ILE A 1 252 ?  19.506  -4.307  -10.427 1.00 98.94 ?  252 ILE A CB  1 
1956 ATOM   O O   .  ILE A 1 252 ?  22.468  -5.732  -10.501 1.00 98.94 ?  252 ILE A O   1 
1957 ATOM   C CG1 .  ILE A 1 252 ?  18.04   -4.683  -10.672 1.00 98.94 ?  252 ILE A CG1 1 
1958 ATOM   C CG2 .  ILE A 1 252 ?  20.189  -4.004  -11.759 1.00 98.94 ?  252 ILE A CG2 1 
1959 ATOM   C CD1 .  ILE A 1 252 ?  17.127  -3.525  -11.023 1.00 98.94 ?  252 ILE A CD1 1 
1960 ATOM   N N   .  ILE A 1 253 ?  22.205  -4.354  -8.754  1.00 98.75 ?  253 ILE A N   1 
1961 ATOM   C CA  .  ILE A 1 253 ?  23.626  -4.034  -8.631  1.00 98.75 ?  253 ILE A CA  1 
1962 ATOM   C C   .  ILE A 1 253 ?  24.42   -5.279  -8.247  1.00 98.75 ?  253 ILE A C   1 
1963 ATOM   C CB  .  ILE A 1 253 ?  23.874  -2.921  -7.584  1.00 98.75 ?  253 ILE A CB  1 
1964 ATOM   O O   .  ILE A 1 253 ?  25.489  -5.526  -8.802  1.00 98.75 ?  253 ILE A O   1 
1965 ATOM   C CG1 .  ILE A 1 253 ?  23.268  -1.592  -8.052  1.00 98.75 ?  253 ILE A CG1 1 
1966 ATOM   C CG2 .  ILE A 1 253 ?  25.371  -2.727  -7.34   1.00 98.75 ?  253 ILE A CG2 1 
1967 ATOM   C CD1 .  ILE A 1 253 ?  22.986  -0.611  -6.929  1.00 98.75 ?  253 ILE A CD1 1 
1968 ATOM   N N   .  ASP A 1 254 ?  23.911  -6.073  -7.311  1.00 98.56 ?  254 ASP A N   1 
1969 ATOM   C CA  .  ASP A 1 254 ?  24.593  -7.297  -6.9    1.00 98.56 ?  254 ASP A CA  1 
1970 ATOM   C C   .  ASP A 1 254 ?  24.596  -8.325  -8.029  1.00 98.56 ?  254 ASP A C   1 
1971 ATOM   C CB  .  ASP A 1 254 ?  23.934  -7.893  -5.653  1.00 98.56 ?  254 ASP A CB  1 
1972 ATOM   O O   .  ASP A 1 254 ?  25.539  -9.103  -8.166  1.00 98.56 ?  254 ASP A O   1 
1973 ATOM   C CG  .  ASP A 1 254 ?  24.197  -7.07   -4.405  1.00 98.56 ?  254 ASP A CG  1 
1974 ATOM   O OD1 .  ASP A 1 254 ?  25.187  -6.308  -4.365  1.00 98.56 ?  254 ASP A OD1 1 
1975 ATOM   O OD2 .  ASP A 1 254 ?  23.422  -7.19   -3.433  1.00 98.56 ?  254 ASP A OD2 1 
1976 ATOM   N N   .  TRP A 1 255 ?  23.552  -8.316  -8.85   1.00 98.69 ?  255 TRP A N   1 
1977 ATOM   C CA  .  TRP A 1 255 ?  23.489  -9.183  -10.022 1.00 98.69 ?  255 TRP A CA  1 
1978 ATOM   C C   .  TRP A 1 255 ?  24.437  -8.68   -11.109 1.00 98.69 ?  255 TRP A C   1 
1979 ATOM   C CB  .  TRP A 1 255 ?  22.052  -9.258  -10.544 1.00 98.69 ?  255 TRP A CB  1 
1980 ATOM   O O   .  TRP A 1 255 ?  25.088  -9.475  -11.786 1.00 98.69 ?  255 TRP A O   1 
1981 ATOM   C CG  .  TRP A 1 255 ?  21.813  -10.43  -11.446 1.00 98.69 ?  255 TRP A CG  1 
1982 ATOM   C CD1 .  TRP A 1 255 ?  21.355  -11.663 -11.092 1.00 98.69 ?  255 TRP A CD1 1 
1983 ATOM   C CD2 .  TRP A 1 255 ?  22.038  -10.5   -12.863 1.00 98.69 ?  255 TRP A CD2 1 
1984 ATOM   C CE2 .  TRP A 1 255 ?  21.755  -11.824 -13.273 1.00 98.69 ?  255 TRP A CE2 1 
1985 ATOM   C CE3 .  TRP A 1 255 ?  22.495  -9.585  -13.821 1.00 98.69 ?  255 TRP A CE3 1 
1986 ATOM   N NE1 .  TRP A 1 255 ?  21.313  -12.507 -12.171 1.00 98.69 ?  255 TRP A NE1 1 
1987 ATOM   C CH2 .  TRP A 1 255 ?  22.463  -11.357 -15.491 1.00 98.69 ?  255 TRP A CH2 1 
1988 ATOM   C CZ2 .  TRP A 1 255 ?  21.979  -12.263 -14.581 1.00 98.69 ?  255 TRP A CZ2 1 
1989 ATOM   C CZ3 .  TRP A 1 255 ?  22.69   -10.016 -15.131 1.00 98.69 ?  255 TRP A CZ3 1 
1990 ATOM   N N   .  ASN A 1 256 ?  24.523  -7.362  -11.259 1.00 98.62 ?  256 ASN A N   1 
1991 ATOM   C CA  .  ASN A 1 256 ?  25.404  -6.718  -12.229 1.00 98.62 ?  256 ASN A CA  1 
1992 ATOM   C C   .  ASN A 1 256 ?  26.882  -6.906  -11.896 1.00 98.62 ?  256 ASN A C   1 
1993 ATOM   C CB  .  ASN A 1 256 ?  25.13   -5.21   -12.258 1.00 98.62 ?  256 ASN A CB  1 
1994 ATOM   O O   .  ASN A 1 256 ?  27.724  -6.94   -12.793 1.00 98.62 ?  256 ASN A O   1 
1995 ATOM   C CG  .  ASN A 1 256 ?  23.848  -4.843  -12.975 1.00 98.62 ?  256 ASN A CG  1 
1996 ATOM   N ND2 .  ASN A 1 256 ?  23.55   -3.553  -12.98  1.00 98.62 ?  256 ASN A ND2 1 
1997 ATOM   O OD1 .  ASN A 1 256 ?  23.148  -5.681  -13.542 1.00 98.62 ?  256 ASN A OD1 1 
1998 ATOM   N N   .  LYS A 1 257 ?  27.207  -6.984  -10.61  1.00 98.00 ?  257 LYS A N   1 
1999 ATOM   C CA  .  LYS A 1 257 ?  28.58   -7.222  -10.166 1.00 98.00 ?  257 LYS A CA  1 
2000 ATOM   C C   .  LYS A 1 257 ?  29.026  -8.632  -10.531 1.00 98.00 ?  257 LYS A C   1 
2001 ATOM   C CB  .  LYS A 1 257 ?  28.688  -7.029  -8.651  1.00 98.00 ?  257 LYS A CB  1 
2002 ATOM   O O   .  LYS A 1 257 ?  30.172  -8.851  -10.92  1.00 98.00 ?  257 LYS A O   1 
2003 ATOM   C CG  .  LYS A 1 257 ?  28.72   -5.572  -8.212  1.00 98.00 ?  257 LYS A CG  1 
2004 ATOM   C CD  .  LYS A 1 257 ?  28.674  -5.453  -6.696  1.00 98.00 ?  257 LYS A CD  1 
2005 ATOM   C CE  .  LYS A 1 257 ?  28.732  -3.999  -6.256  1.00 98.00 ?  257 LYS A CE  1 
2006 ATOM   N NZ  .  LYS A 1 257 ?  28.647  -3.936  -4.76   1.00 98.00 ?  257 LYS A NZ  1 
2007 ATOM   N N   .  GLU A 1 258 ?  28.108  -9.579  -10.383 1.00 97.88 ?  258 GLU A N   1 
2008 ATOM   C CA  .  GLU A 1 258 ?  28.357  -10.976 -10.731 1.00 97.88 ?  258 GLU A CA  1 
2009 ATOM   C C   .  GLU A 1 258 ?  28.381  -11.173 -12.244 1.00 97.88 ?  258 GLU A C   1 
2010 ATOM   C CB  .  GLU A 1 258 ?  27.262  -11.855 -10.121 1.00 97.88 ?  258 GLU A CB  1 
2011 ATOM   O O   .  GLU A 1 258 ?  29.111  -12.023 -12.754 1.00 97.88 ?  258 GLU A O   1 
2012 ATOM   C CG  .  GLU A 1 258 ?  27.294  -11.923 -8.601  1.00 97.88 ?  258 GLU A CG  1 
2013 ATOM   C CD  .  GLU A 1 258 ?  26.109  -12.679 -8.028  1.00 97.88 ?  258 GLU A CD  1 
2014 ATOM   O OE1 .  GLU A 1 258 ?  26.199  -13.146 -6.873  1.00 97.88 ?  258 GLU A OE1 1 
2015 ATOM   O OE2 .  GLU A 1 258 ?  25.067  -12.812 -8.707  1.00 97.88 ?  258 GLU A OE2 1 
2016 ATOM   N N   .  HIS A 1 259 ?  27.574  -10.393 -12.955 1.00 97.88 ?  259 HIS A N   1 
2017 ATOM   C CA  .  HIS A 1 259 ?  27.429  -10.507 -14.403 1.00 97.88 ?  259 HIS A CA  1 
2018 ATOM   C C   .  HIS A 1 259 ?  27.723  -9.166  -15.076 1.00 97.88 ?  259 HIS A C   1 
2019 ATOM   C CB  .  HIS A 1 259 ?  26.007  -10.962 -14.74  1.00 97.88 ?  259 HIS A CB  1 
2020 ATOM   O O   .  HIS A 1 259 ?  26.807  -8.464  -15.508 1.00 97.88 ?  259 HIS A O   1 
2021 ATOM   C CG  .  HIS A 1 259 ?  25.601  -12.232 -14.059 1.00 97.88 ?  259 HIS A CG  1 
2022 ATOM   C CD2 .  HIS A 1 259 ?  25.645  -13.522 -14.479 1.00 97.88 ?  259 HIS A CD2 1 
2023 ATOM   N ND1 .  HIS A 1 259 ?  25.062  -12.288 -12.794 1.00 97.88 ?  259 HIS A ND1 1 
2024 ATOM   C CE1 .  HIS A 1 259 ?  24.823  -13.574 -12.505 1.00 97.88 ?  259 HIS A CE1 1 
2025 ATOM   N NE2 .  HIS A 1 259 ?  25.153  -14.363 -13.509 1.00 97.88 ?  259 HIS A NE2 1 
2026 ATOM   N N   .  PRO A 1 260 ?  29.006  -8.779  -15.165 1.00 96.75 ?  260 PRO A N   1 
2027 ATOM   C CA  .  PRO A 1 260 ?  29.297  -7.42   -15.635 1.00 96.75 ?  260 PRO A CA  1 
2028 ATOM   C C   .  PRO A 1 260 ?  29.092  -7.18   -17.129 1.00 96.75 ?  260 PRO A C   1 
2029 ATOM   C CB  .  PRO A 1 260 ?  30.765  -7.239  -15.248 1.00 96.75 ?  260 PRO A CB  1 
2030 ATOM   O O   .  PRO A 1 260 ?  29.116  -6.04   -17.591 1.00 96.75 ?  260 PRO A O   1 
2031 ATOM   C CG  .  PRO A 1 260 ?  31.328  -8.614  -15.344 1.00 96.75 ?  260 PRO A CG  1 
2032 ATOM   C CD  .  PRO A 1 260 ?  30.24   -9.49   -14.786 1.00 96.75 ?  260 PRO A CD  1 
2033 ATOM   N N   .  GLU A 1 261 ?  28.896  -8.254  -17.884 1.00 95.81 ?  261 GLU A N   1 
2034 ATOM   C CA  .  GLU A 1 261 ?  28.654  -8.164  -19.322 1.00 95.81 ?  261 GLU A CA  1 
2035 ATOM   C C   .  GLU A 1 261 ?  27.175  -8.034  -19.68  1.00 95.81 ?  261 GLU A C   1 
2036 ATOM   C CB  .  GLU A 1 261 ?  29.254  -9.378  -20.04  1.00 95.81 ?  261 GLU A CB  1 
2037 ATOM   O O   .  GLU A 1 261 ?  26.837  -7.747  -20.829 1.00 95.81 ?  261 GLU A O   1 
2038 ATOM   C CG  .  GLU A 1 261 ?  28.53   -10.702 -19.827 1.00 95.81 ?  261 GLU A CG  1 
2039 ATOM   C CD  .  GLU A 1 261 ?  28.584  -11.182 -18.388 1.00 95.81 ?  261 GLU A CD  1 
2040 ATOM   O OE1 .  GLU A 1 261 ?  27.515  -11.477 -17.812 1.00 95.81 ?  261 GLU A OE1 1 
2041 ATOM   O OE2 .  GLU A 1 261 ?  29.691  -11.26  -17.816 1.00 95.81 ?  261 GLU A OE2 1 
2042 ATOM   N N   .  ALA A 1 262 ?  26.292  -8.252  -18.711 1.00 97.44 ?  262 ALA A N   1 
2043 ATOM   C CA  .  ALA A 1 262 ?  24.854  -8.277  -18.962 1.00 97.44 ?  262 ALA A CA  1 
2044 ATOM   C C   .  ALA A 1 262 ?  24.081  -7.346  -18.029 1.00 97.44 ?  262 ALA A C   1 
2045 ATOM   C CB  .  ALA A 1 262 ?  24.34   -9.705  -18.837 1.00 97.44 ?  262 ALA A CB  1 
2046 ATOM   O O   .  ALA A 1 262 ?  22.948  -7.63   -17.64  1.00 97.44 ?  262 ALA A O   1 
2047 ATOM   N N   .  LYS A 1 263 ?  24.706  -6.233  -17.658 1.00 98.31 ?  263 LYS A N   1 
2048 ATOM   C CA  .  LYS A 1 263 ?  24.147  -5.33   -16.655 1.00 98.31 ?  263 LYS A CA  1 
2049 ATOM   C C   .  LYS A 1 263 ?  22.829  -4.677  -17.059 1.00 98.31 ?  263 LYS A C   1 
2050 ATOM   C CB  .  LYS A 1 263 ?  25.146  -4.223  -16.308 1.00 98.31 ?  263 LYS A CB  1 
2051 ATOM   O O   .  LYS A 1 263 ?  22.663  -4.207  -18.184 1.00 98.31 ?  263 LYS A O   1 
2052 ATOM   C CG  .  LYS A 1 263 ?  26.475  -4.722  -15.76  1.00 98.31 ?  263 LYS A CG  1 
2053 ATOM   C CD  .  LYS A 1 263 ?  27.307  -3.567  -15.222 1.00 98.31 ?  263 LYS A CD  1 
2054 ATOM   C CE  .  LYS A 1 263 ?  28.667  -4.038  -14.735 1.00 98.31 ?  263 LYS A CE  1 
2055 ATOM   N NZ  .  LYS A 1 263 ?  29.395  -2.889  -14.103 1.00 98.31 ?  263 LYS A NZ  1 
2056 ATOM   N N   .  THR A 1 264 ?  21.913  -4.616  -16.099 1.00 98.75 ?  264 THR A N   1 
2057 ATOM   C CA  .  THR A 1 264 ?  20.657  -3.883  -16.234 1.00 98.75 ?  264 THR A CA  1 
2058 ATOM   C C   .  THR A 1 264 ?  20.854  -2.499  -15.623 1.00 98.75 ?  264 THR A C   1 
2059 ATOM   C CB  .  THR A 1 264 ?  19.521  -4.616  -15.493 1.00 98.75 ?  264 THR A CB  1 
2060 ATOM   O O   .  THR A 1 264 ?  21.384  -2.381  -14.519 1.00 98.75 ?  264 THR A O   1 
2061 ATOM   C CG2 .  THR A 1 264 ?  18.216  -3.829  -15.507 1.00 98.75 ?  264 THR A CG2 1 
2062 ATOM   O OG1 .  THR A 1 264 ?  19.304  -5.882  -16.128 1.00 98.75 ?  264 THR A OG1 1 
2063 ATOM   N N   .  LYS A 1 265 ?  20.454  -1.453  -16.34  1.00 98.62 ?  265 LYS A N   1 
2064 ATOM   C CA  .  LYS A 1 265 ?  20.723  -0.079  -15.921 1.00 98.62 ?  265 LYS A CA  1 
2065 ATOM   C C   .  LYS A 1 265 ?  19.453  0.716   -15.638 1.00 98.62 ?  265 LYS A C   1 
2066 ATOM   C CB  .  LYS A 1 265 ?  21.541  0.631   -17.004 1.00 98.62 ?  265 LYS A CB  1 
2067 ATOM   O O   .  LYS A 1 265 ?  18.399  0.452   -16.215 1.00 98.62 ?  265 LYS A O   1 
2068 ATOM   C CG  .  LYS A 1 265 ?  22.921  0.021   -17.219 1.00 98.62 ?  265 LYS A CG  1 
2069 ATOM   C CD  .  LYS A 1 265 ?  23.714  0.783   -18.269 1.00 98.62 ?  265 LYS A CD  1 
2070 ATOM   C CE  .  LYS A 1 265 ?  25.079  0.146   -18.473 1.00 98.62 ?  265 LYS A CE  1 
2071 ATOM   N NZ  .  LYS A 1 265 ?  25.834  0.91    -19.519 1.00 98.62 ?  265 LYS A NZ  1 
2072 ATOM   N N   .  SER A 1 266 ?  19.561  1.706   -14.759 1.00 98.56 ?  266 SER A N   1 
2073 ATOM   C CA  .  SER A 1 266 ?  18.45   2.613   -14.485 1.00 98.56 ?  266 SER A CA  1 
2074 ATOM   C C   .  SER A 1 266 ?  18.33   3.621   -15.624 1.00 98.56 ?  266 SER A C   1 
2075 ATOM   C CB  .  SER A 1 266 ?  18.671  3.367   -13.171 1.00 98.56 ?  266 SER A CB  1 
2076 ATOM   O O   .  SER A 1 266 ?  19.336  4.124   -16.122 1.00 98.56 ?  266 SER A O   1 
2077 ATOM   O OG  .  SER A 1 266 ?  17.59   4.245   -12.908 1.00 98.56 ?  266 SER A OG  1 
2078 ATOM   N N   .  LEU A 1 267 ?  17.103  3.926   -16.033 1.00 98.00 ?  267 LEU A N   1 
2079 ATOM   C CA  .  LEU A 1 267 ?  16.86   4.947   -17.048 1.00 98.00 ?  267 LEU A CA  1 
2080 ATOM   C C   .  LEU A 1 267 ?  17.293  6.326   -16.559 1.00 98.00 ?  267 LEU A C   1 
2081 ATOM   C CB  .  LEU A 1 267 ?  15.368  4.987   -17.396 1.00 98.00 ?  267 LEU A CB  1 
2082 ATOM   O O   .  LEU A 1 267 ?  17.843  7.122   -17.319 1.00 98.00 ?  267 LEU A O   1 
2083 ATOM   C CG  .  LEU A 1 267 ?  14.97   5.967   -18.505 1.00 98.00 ?  267 LEU A CG  1 
2084 ATOM   C CD1 .  LEU A 1 267 ?  15.506  5.527   -19.863 1.00 98.00 ?  267 LEU A CD1 1 
2085 ATOM   C CD2 .  LEU A 1 267 ?  13.456  6.104   -18.571 1.00 98.00 ?  267 LEU A CD2 1 
2086 ATOM   N N   .  ASN A 1 268 ?  17.022  6.612   -15.29  1.00 96.94 ?  268 ASN A N   1 
2087 ATOM   C CA  .  ASN A 1 268 ?  17.168  7.956   -14.743 1.00 96.94 ?  268 ASN A CA  1 
2088 ATOM   C C   .  ASN A 1 268 ?  18.111  7.972   -13.543 1.00 96.94 ?  268 ASN A C   1 
2089 ATOM   C CB  .  ASN A 1 268 ?  15.787  8.467   -14.32  1.00 96.94 ?  268 ASN A CB  1 
2090 ATOM   O O   .  ASN A 1 268 ?  18.138  7.023   -12.759 1.00 96.94 ?  268 ASN A O   1 
2091 ATOM   C CG  .  ASN A 1 268 ?  14.79   8.475   -15.459 1.00 96.94 ?  268 ASN A CG  1 
2092 ATOM   N ND2 .  ASN A 1 268 ?  14.968  9.387   -16.402 1.00 96.94 ?  268 ASN A ND2 1 
2093 ATOM   O OD1 .  ASN A 1 268 ?  13.861  7.671   -15.487 1.00 96.94 ?  268 ASN A OD1 1 
2094 ATOM   N N   .  ASN A 1 269 ?  18.869  9.054   -13.396 1.00 93.88 ?  269 ASN A N   1 
2095 ATOM   C CA  .  ASN A 1 269 ?  19.728  9.249   -12.23  1.00 93.88 ?  269 ASN A CA  1 
2096 ATOM   C C   .  ASN A 1 269 ?  19.13   10.248  -11.242 1.00 93.88 ?  269 ASN A C   1 
2097 ATOM   C CB  .  ASN A 1 269 ?  21.102  9.754   -12.677 1.00 93.88 ?  269 ASN A CB  1 
2098 ATOM   O O   .  ASN A 1 269 ?  19.686  10.485  -10.169 1.00 93.88 ?  269 ASN A O   1 
2099 ATOM   C CG  .  ASN A 1 269 ?  21.892  8.703   -13.423 1.00 93.88 ?  269 ASN A CG  1 
2100 ATOM   N ND2 .  ASN A 1 269 ?  22.451  9.081   -14.56  1.00 93.88 ?  269 ASN A ND2 1 
2101 ATOM   O OD1 .  ASN A 1 269 ?  22.007  7.565   -12.975 1.00 93.88 ?  269 ASN A OD1 1 
2102 ATOM   N N   .  THR A 1 270 ?  18.004  10.842  -11.619 1.00 95.75 ?  270 THR A N   1 
2103 ATOM   C CA  .  THR A 1 270 ?  17.25   11.738  -10.748 1.00 95.75 ?  270 THR A CA  1 
2104 ATOM   C C   .  THR A 1 270 ?  15.796  11.283  -10.8   1.00 95.75 ?  270 THR A C   1 
2105 ATOM   C CB  .  THR A 1 270 ?  17.347  13.209  -11.199 1.00 95.75 ?  270 THR A CB  1 
2106 ATOM   O O   .  THR A 1 270 ?  15.222  11.159  -11.882 1.00 95.75 ?  270 THR A O   1 
2107 ATOM   C CG2 .  THR A 1 270 ?  16.664  14.14   -10.204 1.00 95.75 ?  270 THR A CG2 1 
2108 ATOM   O OG1 .  THR A 1 270 ?  18.728  13.577  -11.293 1.00 95.75 ?  270 THR A OG1 1 
2109 ATOM   N N   .  ILE A 1 271 ?  15.227  10.994  -9.636  1.00 97.44 ?  271 ILE A N   1 
2110 ATOM   C CA  .  ILE A 1 271 ?  13.893  10.406  -9.543  1.00 97.44 ?  271 ILE A CA  1 
2111 ATOM   C C   .  ILE A 1 271 ?  12.904  11.415  -8.969  1.00 97.44 ?  271 ILE A C   1 
2112 ATOM   C CB  .  ILE A 1 271 ?  13.901  9.15    -8.64   1.00 97.44 ?  271 ILE A CB  1 
2113 ATOM   O O   .  ILE A 1 271 ?  13.144  12.001  -7.913  1.00 97.44 ?  271 ILE A O   1 
2114 ATOM   C CG1 .  ILE A 1 271 ?  14.98   8.146   -9.067  1.00 97.44 ?  271 ILE A CG1 1 
2115 ATOM   C CG2 .  ILE A 1 271 ?  12.522  8.497   -8.616  1.00 97.44 ?  271 ILE A CG2 1 
2116 ATOM   C CD1 .  ILE A 1 271 ?  14.957  7.691   -10.516 1.00 97.44 ?  271 ILE A CD1 1 
2117 ATOM   N N   .  GLU A 1 272 ?  11.784  11.608  -9.658  1.00 96.94 ?  272 GLU A N   1 
2118 ATOM   C CA  .  GLU A 1 272 ?  10.696  12.426  -9.132  1.00 96.94 ?  272 GLU A CA  1 
2119 ATOM   C C   .  GLU A 1 272 ?  9.999   11.636  -8.028  1.00 96.94 ?  272 GLU A C   1 
2120 ATOM   C CB  .  GLU A 1 272 ?  9.692   12.768  -10.236 1.00 96.94 ?  272 GLU A CB  1 
2121 ATOM   O O   .  GLU A 1 272 ?  9.559   10.512  -8.26   1.00 96.94 ?  272 GLU A O   1 
2122 ATOM   C CG  .  GLU A 1 272 ?  8.522   13.619  -9.762  1.00 96.94 ?  272 GLU A CG  1 
2123 ATOM   C CD  .  GLU A 1 272 ?  8.964   15.008  -9.341  1.00 96.94 ?  272 GLU A CD  1 
2124 ATOM   O OE1 .  GLU A 1 272 ?  8.857   15.33   -8.139  1.00 96.94 ?  272 GLU A OE1 1 
2125 ATOM   O OE2 .  GLU A 1 272 ?  9.437   15.779  -10.203 1.00 96.94 ?  272 GLU A OE2 1 
2126 ATOM   N N   .  LEU A 1 273 ?  9.916   12.21   -6.832  1.00 95.56 ?  273 LEU A N   1 
2127 ATOM   C CA  .  LEU A 1 273 ?  9.36    11.517  -5.672  1.00 95.56 ?  273 LEU A CA  1 
2128 ATOM   C C   .  LEU A 1 273 ?  8.159   12.248  -5.077  1.00 95.56 ?  273 LEU A C   1 
2129 ATOM   C CB  .  LEU A 1 273 ?  10.438  11.398  -4.59   1.00 95.56 ?  273 LEU A CB  1 
2130 ATOM   O O   .  LEU A 1 273 ?  7.8     12.028  -3.92   1.00 95.56 ?  273 LEU A O   1 
2131 ATOM   C CG  .  LEU A 1 273 ?  11.748  10.686  -4.942  1.00 95.56 ?  273 LEU A CG  1 
2132 ATOM   C CD1 .  LEU A 1 273 ?  12.753  10.919  -3.823  1.00 95.56 ?  273 LEU A CD1 1 
2133 ATOM   C CD2 .  LEU A 1 273 ?  11.576  9.192   -5.16   1.00 95.56 ?  273 LEU A CD2 1 
2134 ATOM   N N   .  LYS A 1 274 ?  7.573   13.164  -5.843  1.00 94.62 ?  274 LYS A N   1 
2135 ATOM   C CA  .  LYS A 1 274 ?  6.557   14.075  -5.317  1.00 94.62 ?  274 LYS A CA  1 
2136 ATOM   C C   .  LYS A 1 274 ?  5.341   14.229  -6.228  1.00 94.62 ?  274 LYS A C   1 
2137 ATOM   C CB  .  LYS A 1 274 ?  7.193   15.439  -5.032  1.00 94.62 ?  274 LYS A CB  1 
2138 ATOM   O O   .  LYS A 1 274 ?  4.914   15.342  -6.529  1.00 94.62 ?  274 LYS A O   1 
2139 ATOM   C CG  .  LYS A 1 274 ?  8.345   15.367  -4.035  1.00 94.62 ?  274 LYS A CG  1 
2140 ATOM   C CD  .  LYS A 1 274 ?  8.931   16.734  -3.715  1.00 94.62 ?  274 LYS A CD  1 
2141 ATOM   C CE  .  LYS A 1 274 ?  10.129  16.585  -2.789  1.00 94.62 ?  274 LYS A CE  1 
2142 ATOM   N NZ  .  LYS A 1 274 ?  10.68   17.936  -2.44   1.00 94.62 ?  274 LYS A NZ  1 
2143 ATOM   N N   .  THR A 1 275 ?  4.78    13.104  -6.658  1.00 94.31 ?  275 THR A N   1 
2144 ATOM   C CA  .  THR A 1 275 ?  3.605   13.099  -7.528  1.00 94.31 ?  275 THR A CA  1 
2145 ATOM   C C   .  THR A 1 275 ?  2.28    12.922  -6.791  1.00 94.31 ?  275 THR A C   1 
2146 ATOM   C CB  .  THR A 1 275 ?  3.666   11.978  -8.588  1.00 94.31 ?  275 THR A CB  1 
2147 ATOM   O O   .  THR A 1 275 ?  1.22    12.998  -7.413  1.00 94.31 ?  275 THR A O   1 
2148 ATOM   C CG2 .  THR A 1 275 ?  4.9     12.102  -9.476  1.00 94.31 ?  275 THR A CG2 1 
2149 ATOM   O OG1 .  THR A 1 275 ?  3.68    10.699  -7.943  1.00 94.31 ?  275 THR A OG1 1 
2150 ATOM   N N   .  SER A 1 276 ?  2.341   12.697  -5.482  1.00 89.75 ?  276 SER A N   1 
2151 ATOM   C CA  .  SER A 1 276 ?  1.166   12.382  -4.673  1.00 89.75 ?  276 SER A CA  1 
2152 ATOM   C C   .  SER A 1 276 ?  0.51    11.084  -5.144  1.00 89.75 ?  276 SER A C   1 
2153 ATOM   C CB  .  SER A 1 276 ?  0.162   13.539  -4.705  1.00 89.75 ?  276 SER A CB  1 
2154 ATOM   O O   .  SER A 1 276 ?  0.986   10.435  -6.075  1.00 89.75 ?  276 SER A O   1 
2155 ATOM   O OG  .  SER A 1 276 ?  -0.775  13.429  -3.647  1.00 89.75 ?  276 SER A OG  1 
2156 ATOM   N N   .  PHE A 1 277 ?  -0.587  10.698  -4.502  1.00 88.19 ?  277 PHE A N   1 
2157 ATOM   C CA  .  PHE A 1 277 ?  -1.3    9.468   -4.84   1.00 88.19 ?  277 PHE A CA  1 
2158 ATOM   C C   .  PHE A 1 277 ?  -2.509  9.77    -5.724  1.00 88.19 ?  277 PHE A C   1 
2159 ATOM   C CB  .  PHE A 1 277 ?  -1.761  8.759   -3.562  1.00 88.19 ?  277 PHE A CB  1 
2160 ATOM   O O   .  PHE A 1 277 ?  -3.547  9.115   -5.626  1.00 88.19 ?  277 PHE A O   1 
2161 ATOM   C CG  .  PHE A 1 277 ?  -0.649  8.443   -2.599  1.00 88.19 ?  277 PHE A CG  1 
2162 ATOM   C CD1 .  PHE A 1 277 ?  0.174   7.34    -2.802  1.00 88.19 ?  277 PHE A CD1 1 
2163 ATOM   C CD2 .  PHE A 1 277 ?  -0.444  9.233   -1.473  1.00 88.19 ?  277 PHE A CD2 1 
2164 ATOM   C CE1 .  PHE A 1 277 ?  1.199   7.039   -1.908  1.00 88.19 ?  277 PHE A CE1 1 
2165 ATOM   C CE2 .  PHE A 1 277 ?  0.556   8.922   -0.555  1.00 88.19 ?  277 PHE A CE2 1 
2166 ATOM   C CZ  .  PHE A 1 277 ?  1.389   7.831   -0.78   1.00 88.19 ?  277 PHE A CZ  1 
2167 ATOM   N N   .  THR A 1 278 ?  -2.378  10.781  -6.576  1.00 87.44 ?  278 THR A N   1 
2168 ATOM   C CA  .  THR A 1 278 ?  -3.519  11.365  -7.276  1.00 87.44 ?  278 THR A CA  1 
2169 ATOM   C C   .  THR A 1 278 ?  -3.373  11.298  -8.793  1.00 87.44 ?  278 THR A C   1 
2170 ATOM   C CB  .  THR A 1 278 ?  -3.693  12.841  -6.865  1.00 87.44 ?  278 THR A CB  1 
2171 ATOM   O O   .  THR A 1 278 ?  -2.358  11.71   -9.354  1.00 87.44 ?  278 THR A O   1 
2172 ATOM   C CG2 .  THR A 1 278 ?  -4.992  13.429  -7.4    1.00 87.44 ?  278 THR A CG2 1 
2173 ATOM   O OG1 .  THR A 1 278 ?  -3.71   12.929  -5.435  1.00 87.44 ?  278 THR A OG1 1 
2174 ATOM   N N   .  SER A 1 279 ?  -4.406  10.784  -9.452  1.00 90.56 ?  279 SER A N   1 
2175 ATOM   C CA  .  SER A 1 279 ?  -4.429  10.69   -10.909 1.00 90.56 ?  279 SER A CA  1 
2176 ATOM   C C   .  SER A 1 279 ?  -4.633  12.056  -11.556 1.00 90.56 ?  279 SER A C   1 
2177 ATOM   C CB  .  SER A 1 279 ?  -5.56   9.758   -11.35  1.00 90.56 ?  279 SER A CB  1 
2178 ATOM   O O   .  SER A 1 279 ?  -5.488  12.833  -11.13  1.00 90.56 ?  279 SER A O   1 
2179 ATOM   O OG  .  SER A 1 279 ?  -5.593  9.628   -12.76  1.00 90.56 ?  279 SER A OG  1 
2180 ATOM   N N   .  GLY A 1 280 ?  -3.861  12.331  -12.603 1.00 92.31 ?  280 GLY A N   1 
2181 ATOM   C CA  .  GLY A 1 280 ?  -4.084  13.511  -13.42  1.00 92.31 ?  280 GLY A CA  1 
2182 ATOM   C C   .  GLY A 1 280 ?  -3.272  14.747  -13.085 1.00 92.31 ?  280 GLY A C   1 
2183 ATOM   O O   .  GLY A 1 280 ?  -3.382  15.752  -13.786 1.00 92.31 ?  280 GLY A O   1 
2184 ATOM   N N   .  GLU A 1 281 ?  -2.453  14.702  -12.04  1.00 93.88 ?  281 GLU A N   1 
2185 ATOM   C CA  .  GLU A 1 281 ?  -1.622  15.854  -11.696 1.00 93.88 ?  281 GLU A CA  1 
2186 ATOM   C C   .  GLU A 1 281 ?  -0.558  16.072  -12.77  1.00 93.88 ?  281 GLU A C   1 
2187 ATOM   C CB  .  GLU A 1 281 ?  -0.932  15.676  -10.341 1.00 93.88 ?  281 GLU A CB  1 
2188 ATOM   O O   .  GLU A 1 281 ?  0.017   15.107  -13.273 1.00 93.88 ?  281 GLU A O   1 
2189 ATOM   C CG  .  GLU A 1 281 ?  -1.879  15.63   -9.151  1.00 93.88 ?  281 GLU A CG  1 
2190 ATOM   C CD  .  GLU A 1 281 ?  -1.147  15.681  -7.82   1.00 93.88 ?  281 GLU A CD  1 
2191 ATOM   O OE1 .  GLU A 1 281 ?  -1.814  15.575  -6.769  1.00 93.88 ?  281 GLU A OE1 1 
2192 ATOM   O OE2 .  GLU A 1 281 ?  0.09    15.851  -7.802  1.00 93.88 ?  281 GLU A OE2 1 
2193 ATOM   N N   .  PRO A 1 282 ?  -0.262  17.331  -13.137 1.00 97.25 ?  282 PRO A N   1 
2194 ATOM   C CA  .  PRO A 1 282 ?  0.769   17.486  -14.171 1.00 97.25 ?  282 PRO A CA  1 
2195 ATOM   C C   .  PRO A 1 282 ?  2.131   16.905  -13.8   1.00 97.25 ?  282 PRO A C   1 
2196 ATOM   C CB  .  PRO A 1 282 ?  0.871   19.004  -14.344 1.00 97.25 ?  282 PRO A CB  1 
2197 ATOM   O O   .  PRO A 1 282 ?  2.874   16.442  -14.665 1.00 97.25 ?  282 PRO A O   1 
2198 ATOM   C CG  .  PRO A 1 282 ?  -0.435  19.532  -13.86  1.00 97.25 ?  282 PRO A CG  1 
2199 ATOM   C CD  .  PRO A 1 282 ?  -0.797  18.636  -12.711 1.00 97.25 ?  282 PRO A CD  1 
2200 ATOM   N N   .  VAL A 1 283 ?  2.464   16.939  -12.513 1.00 96.94 ?  283 VAL A N   1 
2201 ATOM   C CA  .  VAL A 1 283 ?  3.706   16.348  -12.019 1.00 96.94 ?  283 VAL A CA  1 
2202 ATOM   C C   .  VAL A 1 283 ?  3.677   14.828  -12.159 1.00 96.94 ?  283 VAL A C   1 
2203 ATOM   C CB  .  VAL A 1 283 ?  4.015   16.782  -10.566 1.00 96.94 ?  283 VAL A CB  1 
2204 ATOM   O O   .  VAL A 1 283 ?  4.712   14.208  -12.396 1.00 96.94 ?  283 VAL A O   1 
2205 ATOM   C CG1 .  VAL A 1 283 ?  2.943   16.31   -9.587  1.00 96.94 ?  283 VAL A CG1 1 
2206 ATOM   C CG2 .  VAL A 1 283 ?  5.399   16.308  -10.131 1.00 96.94 ?  283 VAL A CG2 1 
2207 ATOM   N N   .  ALA A 1 284 ?  2.499   14.223  -12.051 1.00 97.19 ?  284 ALA A N   1 
2208 ATOM   C CA  .  ALA A 1 284 ?  2.357   12.779  -12.205 1.00 97.19 ?  284 ALA A CA  1 
2209 ATOM   C C   .  ALA A 1 284 ?  2.426   12.396  -13.68  1.00 97.19 ?  284 ALA A C   1 
2210 ATOM   C CB  .  ALA A 1 284 ?  1.039   12.309  -11.603 1.00 97.19 ?  284 ALA A CB  1 
2211 ATOM   O O   .  ALA A 1 284 ?  3.104   11.439  -14.05  1.00 97.19 ?  284 ALA A O   1 
2212 ATOM   N N   .  VAL A 1 285 ?  1.722   13.144  -14.522 1.00 98.25 ?  285 VAL A N   1 
2213 ATOM   C CA  .  VAL A 1 285 ?  1.667   12.857  -15.954 1.00 98.25 ?  285 VAL A CA  1 
2214 ATOM   C C   .  VAL A 1 285 ?  3.05    13.004  -16.58  1.00 98.25 ?  285 VAL A C   1 
2215 ATOM   C CB  .  VAL A 1 285 ?  0.652   13.767  -16.682 1.00 98.25 ?  285 VAL A CB  1 
2216 ATOM   O O   .  VAL A 1 285 ?  3.459   12.176  -17.392 1.00 98.25 ?  285 VAL A O   1 
2217 ATOM   C CG1 .  VAL A 1 285 ?  0.691   13.537  -18.19  1.00 98.25 ?  285 VAL A CG1 1 
2218 ATOM   C CG2 .  VAL A 1 285 ?  -0.763  13.507  -16.166 1.00 98.25 ?  285 VAL A CG2 1 
2219 ATOM   N N   .  ALA A 1 286 ?  3.786   14.041  -16.192 1.00 98.38 ?  286 ALA A N   1 
2220 ATOM   C CA  .  ALA A 1 286 ?  5.134   14.252  -16.711 1.00 98.38 ?  286 ALA A CA  1 
2221 ATOM   C C   .  ALA A 1 286 ?  6.081   13.145  -16.255 1.00 98.38 ?  286 ALA A C   1 
2222 ATOM   C CB  .  ALA A 1 286 ?  5.66    15.611  -16.268 1.00 98.38 ?  286 ALA A CB  1 
2223 ATOM   O O   .  ALA A 1 286 ?  6.953   12.713  -17.009 1.00 98.38 ?  286 ALA A O   1 
2224 ATOM   N N   .  ALA A 1 287 ?  5.912   12.685  -15.02  1.00 98.50 ?  287 ALA A N   1 
2225 ATOM   C CA  .  ALA A 1 287 ?  6.755   11.629  -14.469 1.00 98.50 ?  287 ALA A CA  1 
2226 ATOM   C C   .  ALA A 1 287 ?  6.454   10.269  -15.094 1.00 98.50 ?  287 ALA A C   1 
2227 ATOM   C CB  .  ALA A 1 287 ?  6.588   11.574  -12.958 1.00 98.50 ?  287 ALA A CB  1 
2228 ATOM   O O   .  ALA A 1 287 ?  7.364   9.473   -15.324 1.00 98.50 ?  287 ALA A O   1 
2229 ATOM   N N   .  ILE A 1 288 ?  5.185   10.004  -15.389 1.00 98.69 ?  288 ILE A N   1 
2230 ATOM   C CA  .  ILE A 1 288 ?  4.791   8.779   -16.082 1.00 98.69 ?  288 ILE A CA  1 
2231 ATOM   C C   .  ILE A 1 288 ?  5.398   8.767   -17.483 1.00 98.69 ?  288 ILE A C   1 
2232 ATOM   C CB  .  ILE A 1 288 ?  3.253   8.631   -16.18  1.00 98.69 ?  288 ILE A CB  1 
2233 ATOM   O O   .  ILE A 1 288 ?  5.968   7.762   -17.905 1.00 98.69 ?  288 ILE A O   1 
2234 ATOM   C CG1 .  ILE A 1 288 ?  2.642   8.418   -14.789 1.00 98.69 ?  288 ILE A CG1 1 
2235 ATOM   C CG2 .  ILE A 1 288 ?  2.879   7.452   -17.077 1.00 98.69 ?  288 ILE A CG2 1 
2236 ATOM   C CD1 .  ILE A 1 288 ?  1.166   8.75    -14.687 1.00 98.69 ?  288 ILE A CD1 1 
2237 ATOM   N N   .  ASN A 1 289 ?  5.3     9.882   -18.2   1.00 98.44 ?  289 ASN A N   1 
2238 ATOM   C CA  .  ASN A 1 289 ?  5.807   9.953   -19.567 1.00 98.44 ?  289 ASN A CA  1 
2239 ATOM   C C   .  ASN A 1 289 ?  7.324   9.788   -19.625 1.00 98.44 ?  289 ASN A C   1 
2240 ATOM   C CB  .  ASN A 1 289 ?  5.401   11.28   -20.213 1.00 98.44 ?  289 ASN A CB  1 
2241 ATOM   O O   .  ASN A 1 289 ?  7.864   9.305   -20.62  1.00 98.44 ?  289 ASN A O   1 
2242 ATOM   C CG  .  ASN A 1 289 ?  3.93    11.328  -20.565 1.00 98.44 ?  289 ASN A CG  1 
2243 ATOM   N ND2 .  ASN A 1 289 ?  3.34    12.509  -20.468 1.00 98.44 ?  289 ASN A ND2 1 
2244 ATOM   O OD1 .  ASN A 1 289 ?  3.331   10.323  -20.94  1.00 98.44 ?  289 ASN A OD1 1 
2245 ATOM   N N   .  SER A 1 290 ?  8.008   10.179  -18.555 1.00 98.44 ?  290 SER A N   1 
2246 ATOM   C CA  .  SER A 1 290 ?  9.455   10.013  -18.452 1.00 98.44 ?  290 SER A CA  1 
2247 ATOM   C C   .  SER A 1 290 ?  9.885   8.549   -18.435 1.00 98.44 ?  290 SER A C   1 
2248 ATOM   C CB  .  SER A 1 290 ?  9.962   10.689  -17.176 1.00 98.44 ?  290 SER A CB  1 
2249 ATOM   O O   .  SER A 1 290 ?  10.964  8.218   -18.926 1.00 98.44 ?  290 SER A O   1 
2250 ATOM   O OG  .  SER A 1 290 ?  11.371  10.573  -17.067 1.00 98.44 ?  290 SER A OG  1 
2251 ATOM   N N   .  VAL A 1 291 ?  9.072   7.678   -17.846 1.00 98.38 ?  291 VAL A N   1 
2252 ATOM   C CA  .  VAL A 1 291 ?  9.514   6.325   -17.508 1.00 98.38 ?  291 VAL A CA  1 
2253 ATOM   C C   .  VAL A 1 291 ?  8.856   5.201   -18.301 1.00 98.38 ?  291 VAL A C   1 
2254 ATOM   C CB  .  VAL A 1 291 ?  9.328   6.022   -16.007 1.00 98.38 ?  291 VAL A CB  1 
2255 ATOM   O O   .  VAL A 1 291 ?  9.301   4.056   -18.233 1.00 98.38 ?  291 VAL A O   1 
2256 ATOM   C CG1 .  VAL A 1 291 ?  10.036  7.086   -15.172 1.00 98.38 ?  291 VAL A CG1 1 
2257 ATOM   C CG2 .  VAL A 1 291 ?  7.85    5.936   -15.638 1.00 98.38 ?  291 VAL A CG2 1 
2258 ATOM   N N   .  ILE A 1 292 ?  7.831   5.522   -19.083 1.00 98.44 ?  292 ILE A N   1 
2259 ATOM   C CA  .  ILE A 1 292 ?  7.312   4.595   -20.089 1.00 98.44 ?  292 ILE A CA  1 
2260 ATOM   C C   .  ILE A 1 292 ?  8.302   4.449   -21.242 1.00 98.44 ?  292 ILE A C   1 
2261 ATOM   C CB  .  ILE A 1 292 ?  5.942   5.033   -20.658 1.00 98.44 ?  292 ILE A CB  1 
2262 ATOM   O O   .  ILE A 1 292 ?  8.088   3.659   -22.16  1.00 98.44 ?  292 ILE A O   1 
2263 ATOM   C CG1 .  ILE A 1 292 ?  6.041   6.42    -21.304 1.00 98.44 ?  292 ILE A CG1 1 
2264 ATOM   C CG2 .  ILE A 1 292 ?  4.883   4.985   -19.56  1.00 98.44 ?  292 ILE A CG2 1 
2265 ATOM   C CD1 .  ILE A 1 292 ?  4.797   6.869   -22.048 1.00 98.44 ?  292 ILE A CD1 1 
2266 ATOM   N N   .  LYS A 1 293 ?  9.39    5.21    -21.178 1.00 98.19 ?  293 LYS A N   1 
2267 ATOM   C CA  .  LYS A 1 293 ?  10.494  5.116   -22.129 1.00 98.19 ?  293 LYS A CA  1 
2268 ATOM   C C   .  LYS A 1 293 ?  11.368  3.899   -21.841 1.00 98.19 ?  293 LYS A C   1 
2269 ATOM   C CB  .  LYS A 1 293 ?  11.34   6.391   -22.053 1.00 98.19 ?  293 LYS A CB  1 
2270 ATOM   O O   .  LYS A 1 293 ?  12.028  3.375   -22.737 1.00 98.19 ?  293 LYS A O   1 
2271 ATOM   C CG  .  LYS A 1 293 ?  10.555  7.665   -22.338 1.00 98.19 ?  293 LYS A CG  1 
2272 ATOM   C CD  .  LYS A 1 293 ?  11.423  8.905   -22.192 1.00 98.19 ?  293 LYS A CD  1 
2273 ATOM   C CE  .  LYS A 1 293 ?  10.579  10.162  -22.33  1.00 98.19 ?  293 LYS A CE  1 
2274 ATOM   N NZ  .  LYS A 1 293 ?  11.442  11.372  -22.125 1.00 98.19 ?  293 LYS A NZ  1 
2275 ATOM   N N   .  ALA A 1 294 ?  11.374  3.465   -20.585 1.00 98.56 ?  294 ALA A N   1 
2276 ATOM   C CA  .  ALA A 1 294 ?  12.112  2.276   -20.17  1.00 98.56 ?  294 ALA A CA  1 
2277 ATOM   C C   .  ALA A 1 294 ?  11.33   1.032   -20.579 1.00 98.56 ?  294 ALA A C   1 
2278 ATOM   C CB  .  ALA A 1 294 ?  12.317  2.278   -18.661 1.00 98.56 ?  294 ALA A CB  1 
2279 ATOM   O O   .  ALA A 1 294 ?  10.114  1.086   -20.768 1.00 98.56 ?  294 ALA A O   1 
2280 ATOM   N N   .  THR A 1 295 ?  12.018  -0.097  -20.706 1.00 98.69 ?  295 THR A N   1 
2281 ATOM   C CA  .  THR A 1 295 ?  11.336  -1.354  -21.002 1.00 98.69 ?  295 THR A CA  1 
2282 ATOM   C C   .  THR A 1 295 ?  10.533  -1.815  -19.788 1.00 98.69 ?  295 THR A C   1 
2283 ATOM   C CB  .  THR A 1 295 ?  12.326  -2.458  -21.415 1.00 98.69 ?  295 THR A CB  1 
2284 ATOM   O O   .  THR A 1 295 ?  9.394   -2.262  -19.921 1.00 98.69 ?  295 THR A O   1 
2285 ATOM   C CG2 .  THR A 1 295 ?  11.588  -3.685  -21.929 1.00 98.69 ?  295 THR A CG2 1 
2286 ATOM   O OG1 .  THR A 1 295 ?  13.168  -1.966  -22.465 1.00 98.69 ?  295 THR A OG1 1 
2287 ATOM   N N   .  ALA A 1 296 ?  11.122  -1.685  -18.604 1.00 98.88 ?  296 ALA A N   1 
2288 ATOM   C CA  .  ALA A 1 296 ?  10.423  -1.967  -17.355 1.00 98.88 ?  296 ALA A CA  1 
2289 ATOM   C C   .  ALA A 1 296 ?  10.04   -0.659  -16.671 1.00 98.88 ?  296 ALA A C   1 
2290 ATOM   C CB  .  ALA A 1 296 ?  11.307  -2.786  -16.424 1.00 98.88 ?  296 ALA A CB  1 
2291 ATOM   O O   .  ALA A 1 296 ?  10.882  0.216   -16.47  1.00 98.88 ?  296 ALA A O   1 
2292 ATOM   N N   .  SER A 1 297 ?  8.775   -0.536  -16.285 1.00 98.88 ?  297 SER A N   1 
2293 ATOM   C CA  .  SER A 1 297 ?  8.343   0.575   -15.443 1.00 98.88 ?  297 SER A CA  1 
2294 ATOM   C C   .  SER A 1 297 ?  7.984   0.015   -14.071 1.00 98.88 ?  297 SER A C   1 
2295 ATOM   C CB  .  SER A 1 297 ?  7.138   1.283   -16.068 1.00 98.88 ?  297 SER A CB  1 
2296 ATOM   O O   .  SER A 1 297 ?  7.484   -1.106  -13.973 1.00 98.88 ?  297 SER A O   1 
2297 ATOM   O OG  .  SER A 1 297 ?  7.445   1.773   -17.362 1.00 98.88 ?  297 SER A OG  1 
2298 ATOM   N N   .  TYR A 1 298 ?  8.223   0.789   -13.018 1.00 98.81 ?  298 TYR A N   1 
2299 ATOM   C CA  .  TYR A 1 298 ?  7.829   0.401   -11.665 1.00 98.81 ?  298 TYR A CA  1 
2300 ATOM   C C   .  TYR A 1 298 ?  6.843   1.424   -11.097 1.00 98.81 ?  298 TYR A C   1 
2301 ATOM   C CB  .  TYR A 1 298 ?  9.088   0.287   -10.799 1.00 98.81 ?  298 TYR A CB  1 
2302 ATOM   O O   .  TYR A 1 298 ?  7.111   2.066   -10.082 1.00 98.81 ?  298 TYR A O   1 
2303 ATOM   C CG  .  TYR A 1 298 ?  9.003   -0.582  -9.561  1.00 98.81 ?  298 TYR A CG  1 
2304 ATOM   C CD1 .  TYR A 1 298 ?  10.175  -1.072  -8.983  1.00 98.81 ?  298 TYR A CD1 1 
2305 ATOM   C CD2 .  TYR A 1 298 ?  7.787   -0.884  -8.945  1.00 98.81 ?  298 TYR A CD2 1 
2306 ATOM   C CE1 .  TYR A 1 298 ?  10.143  -1.802  -7.799  1.00 98.81 ?  298 TYR A CE1 1 
2307 ATOM   C CE2 .  TYR A 1 298 ?  7.751   -1.643  -7.779  1.00 98.81 ?  298 TYR A CE2 1 
2308 ATOM   O OH  .  TYR A 1 298 ?  8.895   -2.779  -6.016  1.00 98.81 ?  298 TYR A OH  1 
2309 ATOM   C CZ  .  TYR A 1 298 ?  8.929   -2.078  -7.198  1.00 98.81 ?  298 TYR A CZ  1 
2310 ATOM   N N   .  PRO A 1 299 ?  5.695   1.629   -11.765 1.00 98.12 ?  299 PRO A N   1 
2311 ATOM   C CA  .  PRO A 1 299 ?  4.888   2.818   -11.473 1.00 98.12 ?  299 PRO A CA  1 
2312 ATOM   C C   .  PRO A 1 299 ?  4.049   2.69    -10.207 1.00 98.12 ?  299 PRO A C   1 
2313 ATOM   C CB  .  PRO A 1 299 ?  3.97    2.901   -12.693 1.00 98.12 ?  299 PRO A CB  1 
2314 ATOM   O O   .  PRO A 1 299 ?  3.093   1.916   -10.165 1.00 98.12 ?  299 PRO A O   1 
2315 ATOM   C CG  .  PRO A 1 299 ?  3.749   1.479   -13.072 1.00 98.12 ?  299 PRO A CG  1 
2316 ATOM   C CD  .  PRO A 1 299 ?  5.06    0.798   -12.804 1.00 98.12 ?  299 PRO A CD  1 
2317 ATOM   N N   .  VAL A 1 300 ?  4.397   3.437   -9.165  1.00 97.31 ?  300 VAL A N   1 
2318 ATOM   C CA  .  VAL A 1 300 ?  3.646   3.364   -7.914  1.00 97.31 ?  300 VAL A CA  1 
2319 ATOM   C C   .  VAL A 1 300 ?  3.314   4.741   -7.351  1.00 97.31 ?  300 VAL A C   1 
2320 ATOM   C CB  .  VAL A 1 300 ?  4.425   2.604   -6.822  1.00 97.31 ?  300 VAL A CB  1 
2321 ATOM   O O   .  VAL A 1 300 ?  4.201   5.514   -6.993  1.00 97.31 ?  300 VAL A O   1 
2322 ATOM   C CG1 .  VAL A 1 300 ?  3.591   2.482   -5.551  1.00 97.31 ?  300 VAL A CG1 1 
2323 ATOM   C CG2 .  VAL A 1 300 ?  4.836   1.216   -7.303  1.00 97.31 ?  300 VAL A CG2 1 
2324 ATOM   N N   .  ALA A 1 301 ?  2.02    5.023   -7.248  1.00 94.19 ?  301 ALA A N   1 
2325 ATOM   C CA  .  ALA A 1 301 ?  1.49    5.899   -6.206  1.00 94.19 ?  301 ALA A CA  1 
2326 ATOM   C C   .  ALA A 1 301 ?  0.034   5.504   -5.972  1.00 94.19 ?  301 ALA A C   1 
2327 ATOM   C CB  .  ALA A 1 301 ?  1.608   7.362   -6.603  1.00 94.19 ?  301 ALA A CB  1 
2328 ATOM   O O   .  ALA A 1 301 ?  -0.878  6.333   -5.978  1.00 94.19 ?  301 ALA A O   1 
2329 ATOM   N N   .  GLY A 1 302 ?  -0.174  4.202   -5.804  1.00 89.12 ?  302 GLY A N   1 
2330 ATOM   C CA  .  GLY A 1 302 ?  -1.513  3.65    -5.697  1.00 89.12 ?  302 GLY A CA  1 
2331 ATOM   C C   .  GLY A 1 302 ?  -2.16   3.53    -7.063  1.00 89.12 ?  302 GLY A C   1 
2332 ATOM   O O   .  GLY A 1 302 ?  -1.916  2.572   -7.796  1.00 89.12 ?  302 GLY A O   1 
2333 ATOM   N N   .  SER A 1 303 ?  -2.973  4.519   -7.42   1.00 88.12 ?  303 SER A N   1 
2334 ATOM   C CA  .  SER A 1 303 ?  -3.726  4.488   -8.671  1.00 88.12 ?  303 SER A CA  1 
2335 ATOM   C C   .  SER A 1 303 ?  -2.91   4.864   -9.907  1.00 88.12 ?  303 SER A C   1 
2336 ATOM   C CB  .  SER A 1 303 ?  -4.936  5.419   -8.566  1.00 88.12 ?  303 SER A CB  1 
2337 ATOM   O O   .  SER A 1 303 ?  -3.342  4.611   -11.031 1.00 88.12 ?  303 SER A O   1 
2338 ATOM   O OG  .  SER A 1 303 ?  -4.532  6.773   -8.452  1.00 88.12 ?  303 SER A OG  1 
2339 ATOM   N N   .  LEU A 1 304 ?  -1.732  5.451   -9.72   1.00 95.38 ?  304 LEU A N   1 
2340 ATOM   C CA  .  LEU A 1 304 ?  -0.884  5.815   -10.854 1.00 95.38 ?  304 LEU A CA  1 
2341 ATOM   C C   .  LEU A 1 304 ?  -0.253  4.594   -11.52  1.00 95.38 ?  304 LEU A C   1 
2342 ATOM   C CB  .  LEU A 1 304 ?  0.213   6.805   -10.451 1.00 95.38 ?  304 LEU A CB  1 
2343 ATOM   O O   .  LEU A 1 304 ?  0.249   4.684   -12.641 1.00 95.38 ?  304 LEU A O   1 
2344 ATOM   C CG  .  LEU A 1 304 ?  -0.188  8.21    -9.988  1.00 95.38 ?  304 LEU A CG  1 
2345 ATOM   C CD1 .  LEU A 1 304 ?  1.061   9.065   -9.817  1.00 95.38 ?  304 LEU A CD1 1 
2346 ATOM   C CD2 .  LEU A 1 304 ?  -1.116  8.887   -10.988 1.00 95.38 ?  304 LEU A CD2 1 
2347 ATOM   N N   .  SER A 1 305 ?  -0.314  3.444   -10.857 1.00 95.81 ?  305 SER A N   1 
2348 ATOM   C CA  .  SER A 1 305 ?  0.102   2.189   -11.475 1.00 95.81 ?  305 SER A CA  1 
2349 ATOM   C C   .  SER A 1 305 ?  -0.764  1.889   -12.695 1.00 95.81 ?  305 SER A C   1 
2350 ATOM   C CB  .  SER A 1 305 ?  -0.019  1.039   -10.472 1.00 95.81 ?  305 SER A CB  1 
2351 ATOM   O O   .  SER A 1 305 ?  -0.291  1.339   -13.69  1.00 95.81 ?  305 SER A O   1 
2352 ATOM   O OG  .  SER A 1 305 ?  0.766   1.293   -9.321  1.00 95.81 ?  305 SER A OG  1 
2353 ATOM   N N   .  SER A 1 306 ?  -2.037  2.257   -12.597 1.00 95.06 ?  306 SER A N   1 
2354 ATOM   C CA  .  SER A 1 306 ?  -3.021  2.002   -13.644 1.00 95.06 ?  306 SER A CA  1 
2355 ATOM   C C   .  SER A 1 306 ?  -2.985  3.05    -14.751 1.00 95.06 ?  306 SER A C   1 
2356 ATOM   C CB  .  SER A 1 306 ?  -4.421  1.963   -13.027 1.00 95.06 ?  306 SER A CB  1 
2357 ATOM   O O   .  SER A 1 306 ?  -3.316  2.759   -15.899 1.00 95.06 ?  306 SER A O   1 
2358 ATOM   O OG  .  SER A 1 306 ?  -4.456  1.044   -11.949 1.00 95.06 ?  306 SER A OG  1 
2359 ATOM   N N   .  ASP A 1 307 ?  -2.572  4.268   -14.419 1.00 97.19 ?  307 ASP A N   1 
2360 ATOM   C CA  .  ASP A 1 307 ?  -2.448  5.322   -15.422 1.00 97.19 ?  307 ASP A CA  1 
2361 ATOM   C C   .  ASP A 1 307 ?  -1.259  5.042   -16.337 1.00 97.19 ?  307 ASP A C   1 
2362 ATOM   C CB  .  ASP A 1 307 ?  -2.278  6.693   -14.763 1.00 97.19 ?  307 ASP A CB  1 
2363 ATOM   O O   .  ASP A 1 307 ?  -1.319  5.283   -17.541 1.00 97.19 ?  307 ASP A O   1 
2364 ATOM   C CG  .  ASP A 1 307 ?  -3.558  7.2     -14.127 1.00 97.19 ?  307 ASP A CG  1 
2365 ATOM   O OD1 .  ASP A 1 307 ?  -4.657  6.721   -14.482 1.00 97.19 ?  307 ASP A OD1 1 
2366 ATOM   O OD2 .  ASP A 1 307 ?  -3.466  8.104   -13.271 1.00 97.19 ?  307 ASP A OD2 1 
2367 ATOM   N N   .  THR A 1 308 ?  -0.183  4.513   -15.765 1.00 98.44 ?  308 THR A N   1 
2368 ATOM   C CA  .  THR A 1 308 ?  0.984   4.114   -16.547 1.00 98.44 ?  308 THR A CA  1 
2369 ATOM   C C   .  THR A 1 308 ?  0.637   2.935   -17.45  1.00 98.44 ?  308 THR A C   1 
2370 ATOM   C CB  .  THR A 1 308 ?  2.152   3.711   -15.628 1.00 98.44 ?  308 THR A CB  1 
2371 ATOM   O O   .  THR A 1 308 ?  1.113   2.837   -18.581 1.00 98.44 ?  308 THR A O   1 
2372 ATOM   C CG2 .  THR A 1 308 ?  3.417   3.428   -16.427 1.00 98.44 ?  308 THR A CG2 1 
2373 ATOM   O OG1 .  THR A 1 308 ?  2.416   4.779   -14.71  1.00 98.44 ?  308 THR A OG1 1 
2374 ATOM   N N   .  ALA A 1 309 ?  -0.209  2.039   -16.953 1.00 97.94 ?  309 ALA A N   1 
2375 ATOM   C CA  .  ALA A 1 309 ?  -0.664  0.895   -17.735 1.00 97.94 ?  309 ALA A CA  1 
2376 ATOM   C C   .  ALA A 1 309 ?  -1.379  1.367   -18.999 1.00 97.94 ?  309 ALA A C   1 
2377 ATOM   C CB  .  ALA A 1 309 ?  -1.574  0.016   -16.887 1.00 97.94 ?  309 ALA A CB  1 
2378 ATOM   O O   .  ALA A 1 309 ?  -1.196  0.798   -20.076 1.00 97.94 ?  309 ALA A O   1 
2379 ATOM   N N   .  LYS A 1 310 ?  -2.18   2.42    -18.863 1.00 97.69 ?  310 LYS A N   1 
2380 ATOM   C CA  .  LYS A 1 310 ?  -2.885  3.031   -19.988 1.00 97.69 ?  310 LYS A CA  1 
2381 ATOM   C C   .  LYS A 1 310 ?  -1.923  3.687   -20.972 1.00 97.69 ?  310 LYS A C   1 
2382 ATOM   C CB  .  LYS A 1 310 ?  -3.88   4.076   -19.474 1.00 97.69 ?  310 LYS A CB  1 
2383 ATOM   O O   .  LYS A 1 310 ?  -2.1    3.565   -22.181 1.00 97.69 ?  310 LYS A O   1 
2384 ATOM   C CG  .  LYS A 1 310 ?  -5.015  3.489   -18.646 1.00 97.69 ?  310 LYS A CG  1 
2385 ATOM   C CD  .  LYS A 1 310 ?  -5.829  4.575   -17.959 1.00 97.69 ?  310 LYS A CD  1 
2386 ATOM   C CE  .  LYS A 1 310 ?  -6.84   3.965   -17.001 1.00 97.69 ?  310 LYS A CE  1 
2387 ATOM   N NZ  .  LYS A 1 310 ?  -7.589  5.059   -16.3   1.00 97.69 ?  310 LYS A NZ  1 
2388 ATOM   N N   .  GLU A 1 311 ?  -0.917  4.391   -20.465 1.00 98.31 ?  311 GLU A N   1 
2389 ATOM   C CA  .  GLU A 1 311 ?  0.048   5.068   -21.328 1.00 98.31 ?  311 GLU A CA  1 
2390 ATOM   C C   .  GLU A 1 311 ?  0.906   4.092   -22.127 1.00 98.31 ?  311 GLU A C   1 
2391 ATOM   C CB  .  GLU A 1 311 ?  0.955   6.003   -20.521 1.00 98.31 ?  311 GLU A CB  1 
2392 ATOM   O O   .  GLU A 1 311 ?  1.175   4.327   -23.304 1.00 98.31 ?  311 GLU A O   1 
2393 ATOM   C CG  .  GLU A 1 311 ?  0.25    7.228   -19.956 1.00 98.31 ?  311 GLU A CG  1 
2394 ATOM   C CD  .  GLU A 1 311 ?  -0.456  8.037   -21.029 1.00 98.31 ?  311 GLU A CD  1 
2395 ATOM   O OE1 .  GLU A 1 311 ?  -1.642  8.382   -20.84  1.00 98.31 ?  311 GLU A OE1 1 
2396 ATOM   O OE2 .  GLU A 1 311 ?  0.154   8.319   -22.082 1.00 98.31 ?  311 GLU A OE2 1 
2397 ATOM   N N   .  ILE A 1 312 ?  1.322   2.988   -21.516 1.00 98.31 ?  312 ILE A N   1 
2398 ATOM   C CA  .  ILE A 1 312 ?  2.084   1.969   -22.236 1.00 98.31 ?  312 ILE A CA  1 
2399 ATOM   C C   .  ILE A 1 312 ?  1.196   1.347   -23.311 1.00 98.31 ?  312 ILE A C   1 
2400 ATOM   C CB  .  ILE A 1 312 ?  2.639   0.873   -21.297 1.00 98.31 ?  312 ILE A CB  1 
2401 ATOM   O O   .  ILE A 1 312 ?  1.654   1.052   -24.414 1.00 98.31 ?  312 ILE A O   1 
2402 ATOM   C CG1 .  ILE A 1 312 ?  3.656   1.48    -20.324 1.00 98.31 ?  312 ILE A CG1 1 
2403 ATOM   C CG2 .  ILE A 1 312 ?  3.295   -0.246  -22.108 1.00 98.31 ?  312 ILE A CG2 1 
2404 ATOM   C CD1 .  ILE A 1 312 ?  4.073   0.564   -19.19  1.00 98.31 ?  312 ILE A CD1 1 
2405 ATOM   N N   .  LYS A 1 313 ?  -0.084  1.17    -23.001 1.00 97.25 ?  313 LYS A N   1 
2406 ATOM   C CA  .  LYS A 1 313 ?  -1.046  0.637   -23.964 1.00 97.25 ?  313 LYS A CA  1 
2407 ATOM   C C   .  LYS A 1 313 ?  -1.183  1.549   -25.181 1.00 97.25 ?  313 LYS A C   1 
2408 ATOM   C CB  .  LYS A 1 313 ?  -2.402  0.437   -23.283 1.00 97.25 ?  313 LYS A CB  1 
2409 ATOM   O O   .  LYS A 1 313 ?  -1.356  1.065   -26.298 1.00 97.25 ?  313 LYS A O   1 
2410 ATOM   C CG  .  LYS A 1 313 ?  -3.406  -0.355  -24.107 1.00 97.25 ?  313 LYS A CG  1 
2411 ATOM   C CD  .  LYS A 1 313 ?  -4.704  -0.542  -23.336 1.00 97.25 ?  313 LYS A CD  1 
2412 ATOM   C CE  .  LYS A 1 313 ?  -5.689  -1.405  -24.105 1.00 97.25 ?  313 LYS A CE  1 
2413 ATOM   N NZ  .  LYS A 1 313 ?  -6.924  -1.555  -23.269 1.00 97.25 ?  313 LYS A NZ  1 
2414 ATOM   N N   .  LYS A 1 314 ?  -1.09   2.857   -24.964 1.00 97.56 ?  314 LYS A N   1 
2415 ATOM   C CA  .  LYS A 1 314 ?  -1.14   3.84    -26.046 1.00 97.56 ?  314 LYS A CA  1 
2416 ATOM   C C   .  LYS A 1 314 ?  0.091   3.778   -26.945 1.00 97.56 ?  314 LYS A C   1 
2417 ATOM   C CB  .  LYS A 1 314 ?  -1.269  5.261   -25.49  1.00 97.56 ?  314 LYS A CB  1 
2418 ATOM   O O   .  LYS A 1 314 ?  -0.008  4.062   -28.137 1.00 97.56 ?  314 LYS A O   1 
2419 ATOM   C CG  .  LYS A 1 314 ?  -2.608  5.564   -24.832 1.00 97.56 ?  314 LYS A CG  1 
2420 ATOM   C CD  .  LYS A 1 314 ?  -2.624  6.965   -24.239 1.00 97.56 ?  314 LYS A CD  1 
2421 ATOM   C CE  .  LYS A 1 314 ?  -3.934  7.237   -23.518 1.00 97.56 ?  314 LYS A CE  1 
2422 ATOM   N NZ  .  LYS A 1 314 ?  -3.882  8.608   -22.914 1.00 97.56 ?  314 LYS A NZ  1 
2423 ATOM   N N   .  LEU A 1 315 ?  1.24    3.424   -26.381 1.00 96.44 ?  315 LEU A N   1 
2424 ATOM   C CA  .  LEU A 1 315 ?  2.46    3.273   -27.171 1.00 96.44 ?  315 LEU A CA  1 
2425 ATOM   C C   .  LEU A 1 315 ?  2.354   2.078   -28.115 1.00 96.44 ?  315 LEU A C   1 
2426 ATOM   C CB  .  LEU A 1 315 ?  3.684   3.071   -26.273 1.00 96.44 ?  315 LEU A CB  1 
2427 ATOM   O O   .  LEU A 1 315 ?  2.863   2.114   -29.234 1.00 96.44 ?  315 LEU A O   1 
2428 ATOM   C CG  .  LEU A 1 315 ?  4.128   4.196   -25.333 1.00 96.44 ?  315 LEU A CG  1 
2429 ATOM   C CD1 .  LEU A 1 315 ?  5.295   3.686   -24.496 1.00 96.44 ?  315 LEU A CD1 1 
2430 ATOM   C CD2 .  LEU A 1 315 ?  4.548   5.444   -26.099 1.00 96.44 ?  315 LEU A CD2 1 
2431 ATOM   N N   .  GLY A 1 316 ?  1.714   1.013   -27.642 1.00 93.62 ?  316 GLY A N   1 
2432 ATOM   C CA  .  GLY A 1 316 ?  1.581   -0.202  -28.427 1.00 93.62 ?  316 GLY A CA  1 
2433 ATOM   C C   .  GLY A 1 316 ?  2.831   -1.061  -28.439 1.00 93.62 ?  316 GLY A C   1 
2434 ATOM   O O   .  GLY A 1 316 ?  2.913   -2.042  -29.179 1.00 93.62 ?  316 GLY A O   1 
2435 ATOM   N N   .  ASP A 1 317 ?  3.818   -0.693  -27.63  1.00 94.00 ?  317 ASP A N   1 
2436 ATOM   C CA  .  ASP A 1 317 ?  5.098   -1.392  -27.6   1.00 94.00 ?  317 ASP A CA  1 
2437 ATOM   C C   .  ASP A 1 317 ?  5.02    -2.641  -26.725 1.00 94.00 ?  317 ASP A C   1 
2438 ATOM   C CB  .  ASP A 1 317 ?  6.207   -0.463  -27.101 1.00 94.00 ?  317 ASP A CB  1 
2439 ATOM   O O   .  ASP A 1 317 ?  5.175   -2.581  -25.504 1.00 94.00 ?  317 ASP A O   1 
2440 ATOM   C CG  .  ASP A 1 317 ?  7.589   -1.068  -27.269 1.00 94.00 ?  317 ASP A CG  1 
2441 ATOM   O OD1 .  ASP A 1 317 ?  7.704   -2.251  -27.655 1.00 94.00 ?  317 ASP A OD1 1 
2442 ATOM   O OD2 .  ASP A 1 317 ?  8.586   -0.357  -27.024 1.00 94.00 ?  317 ASP A OD2 1 
2443 ATOM   N N   .  LYS A 1 318 ?  4.789   -3.78   -27.369 1.00 92.31 ?  318 LYS A N   1 
2444 ATOM   C CA  .  LYS A 1 318 ?  4.591   -5.054  -26.679 1.00 92.31 ?  318 LYS A CA  1 
2445 ATOM   C C   .  LYS A 1 318 ?  5.777   -5.504  -25.833 1.00 92.31 ?  318 LYS A C   1 
2446 ATOM   C CB  .  LYS A 1 318 ?  4.251   -6.152  -27.691 1.00 92.31 ?  318 LYS A CB  1 
2447 ATOM   O O   .  LYS A 1 318 ?  5.615   -6.351  -24.958 1.00 92.31 ?  318 LYS A O   1 
2448 ATOM   C CG  .  LYS A 1 318 ?  2.974   -5.901  -28.485 1.00 92.31 ?  318 LYS A CG  1 
2449 ATOM   C CD  .  LYS A 1 318 ?  2.662   -7.059  -29.423 1.00 92.31 ?  318 LYS A CD  1 
2450 ATOM   C CE  .  LYS A 1 318 ?  1.429   -6.764  -30.263 1.00 92.31 ?  318 LYS A CE  1 
2451 ATOM   N NZ  .  LYS A 1 318 ?  1.138   -7.931  -31.159 1.00 92.31 ?  318 LYS A NZ  1 
2452 ATOM   N N   .  ASN A 1 319 ?  6.955   -4.942  -26.076 1.00 94.06 ?  319 ASN A N   1 
2453 ATOM   C CA  .  ASN A 1 319 ?  8.146   -5.277  -25.299 1.00 94.06 ?  319 ASN A CA  1 
2454 ATOM   C C   .  ASN A 1 319 ?  8.116   -4.74   -23.868 1.00 94.06 ?  319 ASN A C   1 
2455 ATOM   C CB  .  ASN A 1 319 ?  9.39    -4.72   -25.996 1.00 94.06 ?  319 ASN A CB  1 
2456 ATOM   O O   .  ASN A 1 319 ?  8.907   -5.179  -23.033 1.00 94.06 ?  319 ASN A O   1 
2457 ATOM   C CG  .  ASN A 1 319 ?  9.687   -5.422  -27.302 1.00 94.06 ?  319 ASN A CG  1 
2458 ATOM   N ND2 .  ASN A 1 319 ?  9.803   -4.653  -28.373 1.00 94.06 ?  319 ASN A ND2 1 
2459 ATOM   O OD1 .  ASN A 1 319 ?  9.823   -6.642  -27.348 1.00 94.06 ?  319 ASN A OD1 1 
2460 ATOM   N N   .  LYS A 1 320 ?  7.24    -3.78   -23.589 1.00 98.12 ?  320 LYS A N   1 
2461 ATOM   C CA  .  LYS A 1 320 ?  7.236   -3.078  -22.306 1.00 98.12 ?  320 LYS A CA  1 
2462 ATOM   C C   .  LYS A 1 320 ?  6.296   -3.696  -21.277 1.00 98.12 ?  320 LYS A C   1 
2463 ATOM   C CB  .  LYS A 1 320 ?  6.87    -1.607  -22.525 1.00 98.12 ?  320 LYS A CB  1 
2464 ATOM   O O   .  LYS A 1 320 ?  5.291   -4.314  -21.627 1.00 98.12 ?  320 LYS A O   1 
2465 ATOM   C CG  .  LYS A 1 320 ?  7.867   -0.864  -23.401 1.00 98.12 ?  320 LYS A CG  1 
2466 ATOM   C CD  .  LYS A 1 320 ?  7.643   0.64    -23.341 1.00 98.12 ?  320 LYS A CD  1 
2467 ATOM   C CE  .  LYS A 1 320 ?  8.629   1.408   -24.211 1.00 98.12 ?  320 LYS A CE  1 
2468 ATOM   N NZ  .  LYS A 1 320 ?  10.02   1.198   -23.691 1.00 98.12 ?  320 LYS A NZ  1 
2469 ATOM   N N   .  PHE A 1 321 ?  6.641   -3.533  -20.004 1.00 98.56 ?  321 PHE A N   1 
2470 ATOM   C CA  .  PHE A 1 321 ?  5.893   -4.147  -18.91  1.00 98.56 ?  321 PHE A CA  1 
2471 ATOM   C C   .  PHE A 1 321 ?  6.011   -3.39   -17.587 1.00 98.56 ?  321 PHE A C   1 
2472 ATOM   C CB  .  PHE A 1 321 ?  6.36    -5.594  -18.73  1.00 98.56 ?  321 PHE A CB  1 
2473 ATOM   O O   .  PHE A 1 321 ?  6.85    -2.504  -17.425 1.00 98.56 ?  321 PHE A O   1 
2474 ATOM   C CG  .  PHE A 1 321 ?  7.829   -5.732  -18.44  1.00 98.56 ?  321 PHE A CG  1 
2475 ATOM   C CD1 .  PHE A 1 321 ?  8.722   -6.048  -19.458 1.00 98.56 ?  321 PHE A CD1 1 
2476 ATOM   C CD2 .  PHE A 1 321 ?  8.313   -5.577  -17.146 1.00 98.56 ?  321 PHE A CD2 1 
2477 ATOM   C CE1 .  PHE A 1 321 ?  10.067  -6.276  -19.181 1.00 98.56 ?  321 PHE A CE1 1 
2478 ATOM   C CE2 .  PHE A 1 321 ?  9.655   -5.802  -16.858 1.00 98.56 ?  321 PHE A CE2 1 
2479 ATOM   C CZ  .  PHE A 1 321 ?  10.53   -6.174  -17.874 1.00 98.56 ?  321 PHE A CZ  1 
2480 ATOM   N N   .  ILE A 1 322 ?  5.143   -3.751  -16.648 1.00 98.81 ?  322 ILE A N   1 
2481 ATOM   C CA  .  ILE A 1 322 ?  5.033   -3.096  -15.346 1.00 98.81 ?  322 ILE A CA  1 
2482 ATOM   C C   .  ILE A 1 322 ?  5.415   -4.035  -14.204 1.00 98.81 ?  322 ILE A C   1 
2483 ATOM   C CB  .  ILE A 1 322 ?  3.587   -2.576  -15.164 1.00 98.81 ?  322 ILE A CB  1 
2484 ATOM   O O   .  ILE A 1 322 ?  5.049   -5.21   -14.195 1.00 98.81 ?  322 ILE A O   1 
2485 ATOM   C CG1 .  ILE A 1 322 ?  3.453   -1.236  -15.893 1.00 98.81 ?  322 ILE A CG1 1 
2486 ATOM   C CG2 .  ILE A 1 322 ?  3.182   -2.464  -13.693 1.00 98.81 ?  322 ILE A CG2 1 
2487 ATOM   C CD1 .  ILE A 1 322 ?  2.03    -0.755  -16.076 1.00 98.81 ?  322 ILE A CD1 1 
2488 ATOM   N N   .  ILE A 1 323 ?  6.148   -3.498  -13.234 1.00 98.81 ?  323 ILE A N   1 
2489 ATOM   C CA  .  ILE A 1 323 ?  6.304   -4.117  -11.919 1.00 98.81 ?  323 ILE A CA  1 
2490 ATOM   C C   .  ILE A 1 323 ?  5.315   -3.451  -10.964 1.00 98.81 ?  323 ILE A C   1 
2491 ATOM   C CB  .  ILE A 1 323 ?  7.742   -3.946  -11.378 1.00 98.81 ?  323 ILE A CB  1 
2492 ATOM   O O   .  ILE A 1 323 ?  5.288   -2.226  -10.856 1.00 98.81 ?  323 ILE A O   1 
2493 ATOM   C CG1 .  ILE A 1 323 ?  8.743   -4.606  -12.334 1.00 98.81 ?  323 ILE A CG1 1 
2494 ATOM   C CG2 .  ILE A 1 323 ?  7.857   -4.542  -9.976  1.00 98.81 ?  323 ILE A CG2 1 
2495 ATOM   C CD1 .  ILE A 1 323 ?  10.193  -4.277  -12.048 1.00 98.81 ?  323 ILE A CD1 1 
2496 ATOM   N N   .  GLY A 1 324 ?  4.495   -4.255  -10.294 1.00 97.75 ?  324 GLY A N   1 
2497 ATOM   C CA  .  GLY A 1 324 ?  3.475   -3.741  -9.393  1.00 97.75 ?  324 GLY A CA  1 
2498 ATOM   C C   .  GLY A 1 324 ?  3.77    -3.881  -7.91   1.00 97.75 ?  324 GLY A C   1 
2499 ATOM   O O   .  GLY A 1 324 ?  4.826   -4.387  -7.53   1.00 97.75 ?  324 GLY A O   1 
2500 ATOM   N N   .  VAL A 1 325 ?  2.842   -3.444  -7.064  1.00 96.19 ?  325 VAL A N   1 
2501 ATOM   C CA  .  VAL A 1 325 ?  2.997   -3.517  -5.61   1.00 96.19 ?  325 VAL A CA  1 
2502 ATOM   C C   .  VAL A 1 325 ?  1.718   -3.858  -4.852  1.00 96.19 ?  325 VAL A C   1 
2503 ATOM   C CB  .  VAL A 1 325 ?  3.459   -2.177  -4.994  1.00 96.19 ?  325 VAL A CB  1 
2504 ATOM   O O   .  VAL A 1 325 ?  0.614   -3.709  -5.376  1.00 96.19 ?  325 VAL A O   1 
2505 ATOM   C CG1 .  VAL A 1 325 ?  4.872   -1.837  -5.441  1.00 96.19 ?  325 VAL A CG1 1 
2506 ATOM   C CG2 .  VAL A 1 325 ?  2.488   -1.048  -5.335  1.00 96.19 ?  325 VAL A CG2 1 
2507 ATOM   N N   .  ASP A 1 326 ?  1.912   -4.262  -3.599  1.00 93.50 ?  326 ASP A N   1 
2508 ATOM   C CA  .  ASP A 1 326 ?  0.869   -4.467  -2.594  1.00 93.50 ?  326 ASP A CA  1 
2509 ATOM   C C   .  ASP A 1 326 ?  0.01    -5.702  -2.85   1.00 93.50 ?  326 ASP A C   1 
2510 ATOM   C CB  .  ASP A 1 326 ?  -0.019  -3.228  -2.431  1.00 93.50 ?  326 ASP A CB  1 
2511 ATOM   O O   .  ASP A 1 326 ?  -0.005  -6.636  -2.048  1.00 93.50 ?  326 ASP A O   1 
2512 ATOM   C CG  .  ASP A 1 326 ?  0.762   -1.994  -2.021  1.00 93.50 ?  326 ASP A CG  1 
2513 ATOM   O OD1 .  ASP A 1 326 ?  1.698   -2.11   -1.202  1.00 93.50 ?  326 ASP A OD1 1 
2514 ATOM   O OD2 .  ASP A 1 326 ?  0.437   -0.89   -2.505  1.00 93.50 ?  326 ASP A OD2 1 
2515 ATOM   N N   .  ALA A 1 327 ?  -0.681  -5.697  -3.984  1.00 91.88 ?  327 ALA A N   1 
2516 ATOM   C CA  .  ALA A 1 327 ?  -1.544  -6.79   -4.415  1.00 91.88 ?  327 ALA A CA  1 
2517 ATOM   C C   .  ALA A 1 327 ?  -0.978  -7.326  -5.727  1.00 91.88 ?  327 ALA A C   1 
2518 ATOM   C CB  .  ALA A 1 327 ?  -2.97   -6.287  -4.609  1.00 91.88 ?  327 ALA A CB  1 
2519 ATOM   O O   .  ALA A 1 327 ?  -0.109  -6.702  -6.334  1.00 91.88 ?  327 ALA A O   1 
2520 ATOM   N N   .  ASP A 1 328 ?  -1.466  -8.475  -6.183  1.00 94.69 ?  328 ASP A N   1 
2521 ATOM   C CA  .  ASP A 1 328 ?  -0.991  -9.031  -7.445  1.00 94.69 ?  328 ASP A CA  1 
2522 ATOM   C C   .  ASP A 1 328 ?  -1.69   -8.299  -8.588  1.00 94.69 ?  328 ASP A C   1 
2523 ATOM   C CB  .  ASP A 1 328 ?  -1.254  -10.537 -7.51   1.00 94.69 ?  328 ASP A CB  1 
2524 ATOM   O O   .  ASP A 1 328 ?  -2.775  -8.683  -9.027  1.00 94.69 ?  328 ASP A O   1 
2525 ATOM   C CG  .  ASP A 1 328 ?  -0.607  -11.183 -8.721  1.00 94.69 ?  328 ASP A CG  1 
2526 ATOM   O OD1 .  ASP A 1 328 ?  0.123   -10.491 -9.462  1.00 94.69 ?  328 ASP A OD1 1 
2527 ATOM   O OD2 .  ASP A 1 328 ?  -0.823  -12.395 -8.928  1.00 94.69 ?  328 ASP A OD2 1 
2528 ATOM   N N   .  GLN A 1 329 ?  -1.076  -7.213  -9.043  1.00 94.81 ?  329 GLN A N   1 
2529 ATOM   C CA  .  GLN A 1 329 ?  -1.746  -6.251  -9.914  1.00 94.81 ?  329 GLN A CA  1 
2530 ATOM   C C   .  GLN A 1 329 ?  -2.043  -6.761  -11.321 1.00 94.81 ?  329 GLN A C   1 
2531 ATOM   C CB  .  GLN A 1 329 ?  -0.941  -4.952  -10.005 1.00 94.81 ?  329 GLN A CB  1 
2532 ATOM   O O   .  GLN A 1 329 ?  -2.721  -6.075  -12.081 1.00 94.81 ?  329 GLN A O   1 
2533 ATOM   C CG  .  GLN A 1 329 ?  -0.818  -4.201  -8.686  1.00 94.81 ?  329 GLN A CG  1 
2534 ATOM   C CD  .  GLN A 1 329 ?  -0.324  -2.782  -8.882  1.00 94.81 ?  329 GLN A CD  1 
2535 ATOM   N NE2 .  GLN A 1 329 ?  -1.087  -1.814  -8.399  1.00 94.81 ?  329 GLN A NE2 1 
2536 ATOM   O OE1 .  GLN A 1 329 ?  0.729   -2.554  -9.473  1.00 94.81 ?  329 GLN A OE1 1 
2537 ATOM   N N   .  LYS A 1 330 ?  -1.593  -7.961  -11.674 1.00 95.06 ?  330 LYS A N   1 
2538 ATOM   C CA  .  LYS A 1 330 ?  -2      -8.571  -12.939 1.00 95.06 ?  330 LYS A CA  1 
2539 ATOM   C C   .  LYS A 1 330 ?  -3.476  -8.953  -12.926 1.00 95.06 ?  330 LYS A C   1 
2540 ATOM   C CB  .  LYS A 1 330 ?  -1.127  -9.784  -13.277 1.00 95.06 ?  330 LYS A CB  1 
2541 ATOM   O O   .  LYS A 1 330 ?  -4.101  -9.083  -13.977 1.00 95.06 ?  330 LYS A O   1 
2542 ATOM   C CG  .  LYS A 1 330 ?  -1.391  -11.032 -12.447 1.00 95.06 ?  330 LYS A CG  1 
2543 ATOM   C CD  .  LYS A 1 330 ?  -0.359  -12.105 -12.758 1.00 95.06 ?  330 LYS A CD  1 
2544 ATOM   C CE  .  LYS A 1 330 ?  -0.66   -13.408 -12.04  1.00 95.06 ?  330 LYS A CE  1 
2545 ATOM   N NZ  .  LYS A 1 330 ?  0.481   -14.339 -12.315 1.00 95.06 ?  330 LYS A NZ  1 
2546 ATOM   N N   .  ASN A 1 331 ?  -4.029  -9.118  -11.729 1.00 91.62 ?  331 ASN A N   1 
2547 ATOM   C CA  .  ASN A 1 331 ?  -5.453  -9.391  -11.564 1.00 91.62 ?  331 ASN A CA  1 
2548 ATOM   C C   .  ASN A 1 331 ?  -6.276  -8.124  -11.784 1.00 91.62 ?  331 ASN A C   1 
2549 ATOM   C CB  .  ASN A 1 331 ?  -5.714  -9.944  -10.16  1.00 91.62 ?  331 ASN A CB  1 
2550 ATOM   O O   .  ASN A 1 331 ?  -7.434  -8.189  -12.194 1.00 91.62 ?  331 ASN A O   1 
2551 ATOM   C CG  .  ASN A 1 331 ?  -5.092  -11.307 -9.947  1.00 91.62 ?  331 ASN A CG  1 
2552 ATOM   N ND2 .  ASN A 1 331 ?  -4.714  -11.594 -8.712  1.00 91.62 ?  331 ASN A ND2 1 
2553 ATOM   O OD1 .  ASN A 1 331 ?  -4.96   -12.099 -10.877 1.00 91.62 ?  331 ASN A OD1 1 
2554 ATOM   N N   .  ALA A 1 332 ?  -5.675  -6.974  -11.497 1.00 89.25 ?  332 ALA A N   1 
2555 ATOM   C CA  .  ALA A 1 332 ?  -6.33   -5.681  -11.67  1.00 89.25 ?  332 ALA A CA  1 
2556 ATOM   C C   .  ALA A 1 332 ?  -6.092  -5.115  -13.068 1.00 89.25 ?  332 ALA A C   1 
2557 ATOM   C CB  .  ALA A 1 332 ?  -5.815  -4.703  -10.622 1.00 89.25 ?  332 ALA A CB  1 
2558 ATOM   O O   .  ALA A 1 332 ?  -7.01   -4.615  -13.716 1.00 89.25 ?  332 ALA A O   1 
2559 ATOM   N N   .  LEU A 1 333 ?  -4.847  -5.188  -13.526 1.00 93.12 ?  333 LEU A N   1 
2560 ATOM   C CA  .  LEU A 1 333 ?  -4.439  -4.633  -14.812 1.00 93.12 ?  333 LEU A CA  1 
2561 ATOM   C C   .  LEU A 1 333 ?  -4.461  -5.73   -15.873 1.00 93.12 ?  333 LEU A C   1 
2562 ATOM   C CB  .  LEU A 1 333 ?  -3.041  -4.015  -14.698 1.00 93.12 ?  333 LEU A CB  1 
2563 ATOM   O O   .  LEU A 1 333 ?  -3.435  -6.096  -16.447 1.00 93.12 ?  333 LEU A O   1 
2564 ATOM   C CG  .  LEU A 1 333 ?  -2.837  -2.909  -13.657 1.00 93.12 ?  333 LEU A CG  1 
2565 ATOM   C CD1 .  LEU A 1 333 ?  -1.368  -2.504  -13.623 1.00 93.12 ?  333 LEU A CD1 1 
2566 ATOM   C CD2 .  LEU A 1 333 ?  -3.701  -1.694  -13.96  1.00 93.12 ?  333 LEU A CD2 1 
2567 ATOM   N N   .  LYS A 1 334 ?  -5.654  -6.262  -16.116 1.00 91.44 ?  334 LYS A N   1 
2568 ATOM   C CA  .  LYS A 1 334 ?  -5.846  -7.311  -17.112 1.00 91.44 ?  334 LYS A CA  1 
2569 ATOM   C C   .  LYS A 1 334 ?  -5.651  -6.709  -18.5   1.00 91.44 ?  334 LYS A C   1 
2570 ATOM   C CB  .  LYS A 1 334 ?  -7.245  -7.922  -16.982 1.00 91.44 ?  334 LYS A CB  1 
2571 ATOM   O O   .  LYS A 1 334 ?  -6.114  -5.604  -18.778 1.00 91.44 ?  334 LYS A O   1 
2572 ATOM   C CG  .  LYS A 1 334 ?  -7.487  -8.623  -15.65  1.00 91.44 ?  334 LYS A CG  1 
2573 ATOM   C CD  .  LYS A 1 334 ?  -8.869  -9.259  -15.597 1.00 91.44 ?  334 LYS A CD  1 
2574 ATOM   C CE  .  LYS A 1 334 ?  -9.125  -9.904  -14.244 1.00 91.44 ?  334 LYS A CE  1 
2575 ATOM   N NZ  .  LYS A 1 334 ?  -10.477 -10.556 -14.243 1.00 91.44 ?  334 LYS A NZ  1 
2576 ATOM   N N   .  GLY A 1 335 ?  -4.95   -7.436  -19.363 1.00 93.88 ?  335 GLY A N   1 
2577 ATOM   C CA  .  GLY A 1 335 ?  -4.626  -6.926  -20.685 1.00 93.88 ?  335 GLY A CA  1 
2578 ATOM   C C   .  GLY A 1 335 ?  -3.363  -6.087  -20.715 1.00 93.88 ?  335 GLY A C   1 
2579 ATOM   O O   .  GLY A 1 335 ?  -3.054  -5.454  -21.725 1.00 93.88 ?  335 GLY A O   1 
2580 ATOM   N N   .  HIS A 1 336 ?  -2.619  -6.095  -19.614 1.00 97.00 ?  336 HIS A N   1 
2581 ATOM   C CA  .  HIS A 1 336 ?  -1.345  -5.39   -19.513 1.00 97.00 ?  336 HIS A CA  1 
2582 ATOM   C C   .  HIS A 1 336 ?  -0.269  -6.381  -19.073 1.00 97.00 ?  336 HIS A C   1 
2583 ATOM   C CB  .  HIS A 1 336 ?  -1.46   -4.246  -18.502 1.00 97.00 ?  336 HIS A CB  1 
2584 ATOM   O O   .  HIS A 1 336 ?  -0.569  -7.372  -18.407 1.00 97.00 ?  336 HIS A O   1 
2585 ATOM   C CG  .  HIS A 1 336 ?  -2.502  -3.23   -18.856 1.00 97.00 ?  336 HIS A CG  1 
2586 ATOM   C CD2 .  HIS A 1 336 ?  -3.781  -3.086  -18.423 1.00 97.00 ?  336 HIS A CD2 1 
2587 ATOM   N ND1 .  HIS A 1 336 ?  -2.301  -2.182  -19.726 1.00 97.00 ?  336 HIS A ND1 1 
2588 ATOM   C CE1 .  HIS A 1 336 ?  -3.42   -1.444  -19.745 1.00 97.00 ?  336 HIS A CE1 1 
2589 ATOM   N NE2 .  HIS A 1 336 ?  -4.353  -1.965  -18.974 1.00 97.00 ?  336 HIS A NE2 1 
2590 ATOM   N N   .  ARG A 1 337 ?  0.98    -6.129  -19.452 1.00 98.25 ?  337 ARG A N   1 
2591 ATOM   C CA  .  ARG A 1 337 ?  2.074   -7.052  -19.153 1.00 98.25 ?  337 ARG A CA  1 
2592 ATOM   C C   .  ARG A 1 337 ?  2.705   -6.727  -17.805 1.00 98.25 ?  337 ARG A C   1 
2593 ATOM   C CB  .  ARG A 1 337 ?  3.148   -6.987  -20.244 1.00 98.25 ?  337 ARG A CB  1 
2594 ATOM   O O   .  ARG A 1 337 ?  3.157   -5.605  -17.581 1.00 98.25 ?  337 ARG A O   1 
2595 ATOM   C CG  .  ARG A 1 337 ?  2.658   -7.353  -21.639 1.00 98.25 ?  337 ARG A CG  1 
2596 ATOM   C CD  .  ARG A 1 337 ?  3.797   -7.35   -22.648 1.00 98.25 ?  337 ARG A CD  1 
2597 ATOM   N NE  .  ARG A 1 337 ?  4.72    -8.465  -22.435 1.00 98.25 ?  337 ARG A NE  1 
2598 ATOM   N NH1 .  ARG A 1 337 ?  6.681   -7.22   -22.302 1.00 98.25 ?  337 ARG A NH1 1 
2599 ATOM   N NH2 .  ARG A 1 337 ?  6.739   -9.472  -22.146 1.00 98.25 ?  337 ARG A NH2 1 
2600 ATOM   C CZ  .  ARG A 1 337 ?  6.037   -8.37   -22.306 1.00 98.25 ?  337 ARG A CZ  1 
2601 ATOM   N N   .  ILE A 1 338 ?  2.725   -7.712  -16.914 1.00 98.50 ?  338 ILE A N   1 
2602 ATOM   C CA  .  ILE A 1 338 ?  3.244   -7.54   -15.559 1.00 98.50 ?  338 ILE A CA  1 
2603 ATOM   C C   .  ILE A 1 338 ?  4.388   -8.521  -15.323 1.00 98.50 ?  338 ILE A C   1 
2604 ATOM   C CB  .  ILE A 1 338 ?  2.145   -7.797  -14.5   1.00 98.50 ?  338 ILE A CB  1 
2605 ATOM   O O   .  ILE A 1 338 ?  4.21    -9.728  -15.478 1.00 98.50 ?  338 ILE A O   1 
2606 ATOM   C CG1 .  ILE A 1 338 ?  0.9     -6.934  -14.745 1.00 98.50 ?  338 ILE A CG1 1 
2607 ATOM   C CG2 .  ILE A 1 338 ?  2.684   -7.589  -13.085 1.00 98.50 ?  338 ILE A CG2 1 
2608 ATOM   C CD1 .  ILE A 1 338 ?  1.086   -5.43   -14.698 1.00 98.50 ?  338 ILE A CD1 1 
2609 ATOM   N N   .  PHE A 1 339 ?  5.566   -8.026  -14.96  1.00 98.75 ?  339 PHE A N   1 
2610 ATOM   C CA  .  PHE A 1 339 ?  6.695   -8.908  -14.673 1.00 98.75 ?  339 PHE A CA  1 
2611 ATOM   C C   .  PHE A 1 339 ?  6.538   -9.587  -13.317 1.00 98.75 ?  339 PHE A C   1 
2612 ATOM   C CB  .  PHE A 1 339 ?  8.009   -8.124  -14.717 1.00 98.75 ?  339 PHE A CB  1 
2613 ATOM   O O   .  PHE A 1 339 ?  6.713   -10.798 -13.195 1.00 98.75 ?  339 PHE A O   1 
2614 ATOM   C CG  .  PHE A 1 339 ?  9.215   -8.944  -14.352 1.00 98.75 ?  339 PHE A CG  1 
2615 ATOM   C CD1 .  PHE A 1 339 ?  9.849   -8.76   -13.127 1.00 98.75 ?  339 PHE A CD1 1 
2616 ATOM   C CD2 .  PHE A 1 339 ?  9.703   -9.913  -15.221 1.00 98.75 ?  339 PHE A CD2 1 
2617 ATOM   C CE1 .  PHE A 1 339 ?  10.908  -9.578  -12.742 1.00 98.75 ?  339 PHE A CE1 1 
2618 ATOM   C CE2 .  PHE A 1 339 ?  10.756  -10.739 -14.842 1.00 98.75 ?  339 PHE A CE2 1 
2619 ATOM   C CZ  .  PHE A 1 339 ?  11.352  -10.581 -13.596 1.00 98.75 ?  339 PHE A CZ  1 
2620 ATOM   N N   .  THR A 1 340 ?  6.221   -8.798  -12.297 1.00 98.75 ?  340 THR A N   1 
2621 ATOM   C CA  .  THR A 1 340 ?  6.007   -9.295  -10.941 1.00 98.75 ?  340 THR A CA  1 
2622 ATOM   C C   .  THR A 1 340 ?  5.248   -8.209  -10.187 1.00 98.75 ?  340 THR A C   1 
2623 ATOM   C CB  .  THR A 1 340 ?  7.341   -9.603  -10.222 1.00 98.75 ?  340 THR A CB  1 
2624 ATOM   O O   .  THR A 1 340 ?  5.207   -7.063  -10.633 1.00 98.75 ?  340 THR A O   1 
2625 ATOM   C CG2 .  THR A 1 340 ?  8.124   -8.341  -9.882  1.00 98.75 ?  340 THR A CG2 1 
2626 ATOM   O OG1 .  THR A 1 340 ?  7.079   -10.3   -8.998  1.00 98.75 ?  340 THR A OG1 1 
2627 ATOM   N N   .  SER A 1 341 ?  4.676   -8.551  -9.038  1.00 98.38 ?  341 SER A N   1 
2628 ATOM   C CA  .  SER A 1 341 ?  4.271   -7.543  -8.063  1.00 98.38 ?  341 SER A CA  1 
2629 ATOM   C C   .  SER A 1 341 ?  5.044   -7.792  -6.773  1.00 98.38 ?  341 SER A C   1 
2630 ATOM   C CB  .  SER A 1 341 ?  2.765   -7.6    -7.796  1.00 98.38 ?  341 SER A CB  1 
2631 ATOM   O O   .  SER A 1 341 ?  5.215   -8.942  -6.368  1.00 98.38 ?  341 SER A O   1 
2632 ATOM   O OG  .  SER A 1 341 ?  2.038   -7.347  -8.986  1.00 98.38 ?  341 SER A OG  1 
2633 ATOM   N N   .  VAL A 1 342 ?  5.529   -6.729  -6.141  1.00 98.19 ?  342 VAL A N   1 
2634 ATOM   C CA  .  VAL A 1 342 ?  6.196   -6.856  -4.848  1.00 98.19 ?  342 VAL A CA  1 
2635 ATOM   C C   .  VAL A 1 342 ?  5.123   -6.692  -3.78   1.00 98.19 ?  342 VAL A C   1 
2636 ATOM   C CB  .  VAL A 1 342 ?  7.34    -5.845  -4.624  1.00 98.19 ?  342 VAL A CB  1 
2637 ATOM   O O   .  VAL A 1 342 ?  4.621   -5.597  -3.524  1.00 98.19 ?  342 VAL A O   1 
2638 ATOM   C CG1 .  VAL A 1 342 ?  8.006   -6.111  -3.277  1.00 98.19 ?  342 VAL A CG1 1 
2639 ATOM   C CG2 .  VAL A 1 342 ?  8.378   -5.964  -5.737  1.00 98.19 ?  342 VAL A CG2 1 
2640 ATOM   N N   .  MET A 1 343 ?  4.74    -7.824  -3.201  1.00 95.88 ?  343 MET A N   1 
2641 ATOM   C CA  .  MET A 1 343 ?  3.555   -7.908  -2.355  1.00 95.88 ?  343 MET A CA  1 
2642 ATOM   C C   .  MET A 1 343 ?  3.787   -7.234  -1.007  1.00 95.88 ?  343 MET A C   1 
2643 ATOM   C CB  .  MET A 1 343 ?  3.18    -9.375  -2.125  1.00 95.88 ?  343 MET A CB  1 
2644 ATOM   O O   .  MET A 1 343 ?  4.869   -7.327  -0.426  1.00 95.88 ?  343 MET A O   1 
2645 ATOM   C CG  .  MET A 1 343 ?  2.922   -10.174 -3.397  1.00 95.88 ?  343 MET A CG  1 
2646 ATOM   S SD  .  MET A 1 343 ?  1.518   -9.568  -4.357  1.00 95.88 ?  343 MET A SD  1 
2647 ATOM   C CE  .  MET A 1 343 ?  0.128   -10.089 -3.351  1.00 95.88 ?  343 MET A CE  1 
2648 ATOM   N N   .  LYS A 1 344 ?  2.741   -6.584  -0.509  1.00 94.75 ?  344 LYS A N   1 
2649 ATOM   C CA  .  LYS A 1 344 ?  2.697   -6.04   0.846   1.00 94.75 ?  344 LYS A CA  1 
2650 ATOM   C C   .  LYS A 1 344 ?  1.296   -6.355  1.354   1.00 94.75 ?  344 LYS A C   1 
2651 ATOM   C CB  .  LYS A 1 344 ?  2.953   -4.53   0.857   1.00 94.75 ?  344 LYS A CB  1 
2652 ATOM   O O   .  LYS A 1 344 ?  0.343   -5.633  1.063   1.00 94.75 ?  344 LYS A O   1 
2653 ATOM   C CG  .  LYS A 1 344 ?  2.972   -3.924  2.256   1.00 94.75 ?  344 LYS A CG  1 
2654 ATOM   C CD  .  LYS A 1 344 ?  2.896   -2.402  2.235   1.00 94.75 ?  344 LYS A CD  1 
2655 ATOM   C CE  .  LYS A 1 344 ?  4.178   -1.758  1.734   1.00 94.75 ?  344 LYS A CE  1 
2656 ATOM   N NZ  .  LYS A 1 344 ?  4.038   -0.267  1.791   1.00 94.75 ?  344 LYS A NZ  1 
2657 ATOM   N N   .  LEU A 1 345 ?  1.175   -7.467  2.069   1.00 94.12 ?  345 LEU A N   1 
2658 ATOM   C CA  .  LEU A 1 345 ?  -0.131  -8.01   2.429   1.00 94.12 ?  345 LEU A CA  1 
2659 ATOM   C C   .  LEU A 1 345 ?  -0.739  -7.29   3.629   1.00 94.12 ?  345 LEU A C   1 
2660 ATOM   C CB  .  LEU A 1 345 ?  -0.035  -9.517  2.689   1.00 94.12 ?  345 LEU A CB  1 
2661 ATOM   O O   .  LEU A 1 345 ?  -0.883  -7.849  4.716   1.00 94.12 ?  345 LEU A O   1 
2662 ATOM   C CG  .  LEU A 1 345 ?  0.435   -10.418 1.542   1.00 94.12 ?  345 LEU A CG  1 
2663 ATOM   C CD1 .  LEU A 1 345 ?  0.495   -11.858 2.03    1.00 94.12 ?  345 LEU A CD1 1 
2664 ATOM   C CD2 .  LEU A 1 345 ?  -0.495  -10.327 0.337   1.00 94.12 ?  345 LEU A CD2 1 
2665 ATOM   N N   .  ILE A 1 346 ?  -1.137  -6.046  3.386   1.00 94.31 ?  346 ILE A N   1 
2666 ATOM   C CA  .  ILE A 1 346 ?  -1.916  -5.263  4.341   1.00 94.31 ?  346 ILE A CA  1 
2667 ATOM   C C   .  ILE A 1 346 ?  -3.211  -6.015  4.622   1.00 94.31 ?  346 ILE A C   1 
2668 ATOM   C CB  .  ILE A 1 346 ?  -2.249  -3.857  3.79    1.00 94.31 ?  346 ILE A CB  1 
2669 ATOM   O O   .  ILE A 1 346 ?  -3.632  -6.137  5.772   1.00 94.31 ?  346 ILE A O   1 
2670 ATOM   C CG1 .  ILE A 1 346 ?  -0.96   -3.058  3.568   1.00 94.31 ?  346 ILE A CG1 1 
2671 ATOM   C CG2 .  ILE A 1 346 ?  -3.2    -3.128  4.738   1.00 94.31 ?  346 ILE A CG2 1 
2672 ATOM   C CD1 .  ILE A 1 346 ?  -1.119  -1.851  2.667   1.00 94.31 ?  346 ILE A CD1 1 
2673 ATOM   N N   .  GLY A 1 347 ?  -3.822  -6.543  3.567   1.00 94.62 ?  347 GLY A N   1 
2674 ATOM   C CA  .  GLY A 1 347 ?  -5.055  -7.293  3.721   1.00 94.62 ?  347 GLY A CA  1 
2675 ATOM   C C   .  GLY A 1 347 ?  -4.923  -8.478  4.657   1.00 94.62 ?  347 GLY A C   1 
2676 ATOM   O O   .  GLY A 1 347 ?  -5.83   -8.748  5.44    1.00 94.62 ?  347 GLY A O   1 
2677 ATOM   N N   .  GLN A 1 348 ?  -3.802  -9.19   4.603   1.00 94.44 ?  348 GLN A N   1 
2678 ATOM   C CA  .  GLN A 1 348 ?  -3.603  -10.341 5.478   1.00 94.44 ?  348 GLN A CA  1 
2679 ATOM   C C   .  GLN A 1 348 ?  -3.33   -9.903  6.915   1.00 94.44 ?  348 GLN A C   1 
2680 ATOM   C CB  .  GLN A 1 348 ?  -2.447  -11.207 4.972   1.00 94.44 ?  348 GLN A CB  1 
2681 ATOM   O O   .  GLN A 1 348 ?  -3.798  -10.535 7.862   1.00 94.44 ?  348 GLN A O   1 
2682 ATOM   C CG  .  GLN A 1 348 ?  -2.375  -12.579 5.627   1.00 94.44 ?  348 GLN A CG  1 
2683 ATOM   C CD  .  GLN A 1 348 ?  -3.535  -13.462 5.217   1.00 94.44 ?  348 GLN A CD  1 
2684 ATOM   N NE2 .  GLN A 1 348 ?  -4.343  -13.887 6.177   1.00 94.44 ?  348 GLN A NE2 1 
2685 ATOM   O OE1 .  GLN A 1 348 ?  -3.711  -13.746 4.035   1.00 94.44 ?  348 GLN A OE1 1 
2686 ATOM   N N   .  ALA A 1 349 ?  -2.562  -8.832  7.084   1.00 94.38 ?  349 ALA A N   1 
2687 ATOM   C CA  .  ALA A 1 349 ?  -2.221  -8.342  8.415   1.00 94.38 ?  349 ALA A CA  1 
2688 ATOM   C C   .  ALA A 1 349 ?  -3.427  -7.739  9.133   1.00 94.38 ?  349 ALA A C   1 
2689 ATOM   C CB  .  ALA A 1 349 ?  -1.094  -7.324  8.325   1.00 94.38 ?  349 ALA A CB  1 
2690 ATOM   O O   .  ALA A 1 349 ?  -3.65   -8.018  10.309  1.00 94.38 ?  349 ALA A O   1 
2691 ATOM   N N   .  VAL A 1 350 ?  -4.213  -6.924  8.436   1.00 95.94 ?  350 VAL A N   1 
2692 ATOM   C CA  .  VAL A 1 350 ?  -5.415  -6.328  9.019   1.00 95.94 ?  350 VAL A CA  1 
2693 ATOM   C C   .  VAL A 1 350 ?  -6.413  -7.435  9.344   1.00 95.94 ?  350 VAL A C   1 
2694 ATOM   C CB  .  VAL A 1 350 ?  -6.073  -5.289  8.081   1.00 95.94 ?  350 VAL A CB  1 
2695 ATOM   O O   .  VAL A 1 350 ?  -7.039  -7.424  10.403  1.00 95.94 ?  350 VAL A O   1 
2696 ATOM   C CG1 .  VAL A 1 350 ?  -7.411  -4.811  8.639   1.00 95.94 ?  350 VAL A CG1 1 
2697 ATOM   C CG2 .  VAL A 1 350 ?  -5.151  -4.087  7.889   1.00 95.94 ?  350 VAL A CG2 1 
2698 ATOM   N N   .  TYR A 1 351 ?  -6.536  -8.402  8.441   1.00 96.12 ?  351 TYR A N   1 
2699 ATOM   C CA  .  TYR A 1 351 ?  -7.426  -9.541  8.639   1.00 96.12 ?  351 TYR A CA  1 
2700 ATOM   C C   .  TYR A 1 351 ?  -7.039  -10.333 9.886   1.00 96.12 ?  351 TYR A C   1 
2701 ATOM   C CB  .  TYR A 1 351 ?  -7.381  -10.436 7.398   1.00 96.12 ?  351 TYR A CB  1 
2702 ATOM   O O   .  TYR A 1 351 ?  -7.903  -10.669 10.693  1.00 96.12 ?  351 TYR A O   1 
2703 ATOM   C CG  .  TYR A 1 351 ?  -8.178  -11.715 7.51    1.00 96.12 ?  351 TYR A CG  1 
2704 ATOM   C CD1 .  TYR A 1 351 ?  -7.57   -12.882 7.973   1.00 96.12 ?  351 TYR A CD1 1 
2705 ATOM   C CD2 .  TYR A 1 351 ?  -9.521  -11.768 7.132   1.00 96.12 ?  351 TYR A CD2 1 
2706 ATOM   C CE1 .  TYR A 1 351 ?  -8.291  -14.062 8.094   1.00 96.12 ?  351 TYR A CE1 1 
2707 ATOM   C CE2 .  TYR A 1 351 ?  -10.247 -12.953 7.245   1.00 96.12 ?  351 TYR A CE2 1 
2708 ATOM   O OH  .  TYR A 1 351 ?  -10.331 -15.253 7.945   1.00 96.12 ?  351 TYR A OH  1 
2709 ATOM   C CZ  .  TYR A 1 351 ?  -9.631  -14.085 7.754   1.00 96.12 ?  351 TYR A CZ  1 
2710 ATOM   N N   .  ASN A 1 352 ?  -5.756  -10.639 10.048  1.00 94.31 ?  352 ASN A N   1 
2711 ATOM   C CA  .  ASN A 1 352 ?  -5.298  -11.434 11.184  1.00 94.31 ?  352 ASN A CA  1 
2712 ATOM   C C   .  ASN A 1 352 ?  -5.398  -10.7   12.52   1.00 94.31 ?  352 ASN A C   1 
2713 ATOM   C CB  .  ASN A 1 352 ?  -3.845  -11.866 10.973  1.00 94.31 ?  352 ASN A CB  1 
2714 ATOM   O O   .  ASN A 1 352 ?  -5.67   -11.319 13.549  1.00 94.31 ?  352 ASN A O   1 
2715 ATOM   C CG  .  ASN A 1 352 ?  -3.706  -13.01  9.991   1.00 94.31 ?  352 ASN A CG  1 
2716 ATOM   N ND2 .  ASN A 1 352 ?  -2.6    -13.021 9.265   1.00 94.31 ?  352 ASN A ND2 1 
2717 ATOM   O OD1 .  ASN A 1 352 ?  -4.558  -13.89  9.903   1.00 94.31 ?  352 ASN A OD1 1 
2718 ATOM   N N   .  VAL A 1 353 ?  -5.156  -9.393  12.519  1.00 94.62 ?  353 VAL A N   1 
2719 ATOM   C CA  .  VAL A 1 353 ?  -5.25   -8.598  13.742  1.00 94.62 ?  353 VAL A CA  1 
2720 ATOM   C C   .  VAL A 1 353 ?  -6.707  -8.501  14.183  1.00 94.62 ?  353 VAL A C   1 
2721 ATOM   C CB  .  VAL A 1 353 ?  -4.659  -7.179  13.577  1.00 94.62 ?  353 VAL A CB  1 
2722 ATOM   O O   .  VAL A 1 353 ?  -7.005  -8.636  15.369  1.00 94.62 ?  353 VAL A O   1 
2723 ATOM   C CG1 .  VAL A 1 353 ?  -4.975  -6.301  14.786  1.00 94.62 ?  353 VAL A CG1 1 
2724 ATOM   C CG2 .  VAL A 1 353 ?  -3.143  -7.25   13.401  1.00 94.62 ?  353 VAL A CG2 1 
2725 ATOM   N N   .  LEU A 1 354 ?  -7.617  -8.282  13.239  1.00 95.69 ?  354 LEU A N   1 
2726 ATOM   C CA  .  LEU A 1 354 ?  -9.04   -8.236  13.56   1.00 95.69 ?  354 LEU A CA  1 
2727 ATOM   C C   .  LEU A 1 354 ?  -9.551  -9.624  13.936  1.00 95.69 ?  354 LEU A C   1 
2728 ATOM   C CB  .  LEU A 1 354 ?  -9.845  -7.673  12.384  1.00 95.69 ?  354 LEU A CB  1 
2729 ATOM   O O   .  LEU A 1 354 ?  -10.392 -9.753  14.824  1.00 95.69 ?  354 LEU A O   1 
2730 ATOM   C CG  .  LEU A 1 354 ?  -9.672  -6.183  12.07   1.00 95.69 ?  354 LEU A CG  1 
2731 ATOM   C CD1 .  LEU A 1 354 ?  -10.391 -5.842  10.77   1.00 95.69 ?  354 LEU A CD1 1 
2732 ATOM   C CD2 .  LEU A 1 354 ?  -10.217 -5.301  13.189  1.00 95.69 ?  354 LEU A CD2 1 
2733 ATOM   N N   .  ALA A 1 355 ?  -9.042  -10.659 13.277  1.00 95.19 ?  355 ALA A N   1 
2734 ATOM   C CA  .  ALA A 1 355 ?  -9.443  -12.029 13.579  1.00 95.19 ?  355 ALA A CA  1 
2735 ATOM   C C   .  ALA A 1 355 ?  -9.197  -12.363 15.046  1.00 95.19 ?  355 ALA A C   1 
2736 ATOM   C CB  .  ALA A 1 355 ?  -8.689  -13.018 12.697  1.00 95.19 ?  355 ALA A CB  1 
2737 ATOM   O O   .  ALA A 1 355 ?  -10.05  -12.953 15.703  1.00 95.19 ?  355 ALA A O   1 
2738 ATOM   N N   .  ASP A 1 356 ?  -8.026  -11.995 15.553  1.00 94.00 ?  356 ASP A N   1 
2739 ATOM   C CA  .  ASP A 1 356 ?  -7.658  -12.287 16.935  1.00 94.00 ?  356 ASP A CA  1 
2740 ATOM   C C   .  ASP A 1 356 ?  -8.564  -11.555 17.921  1.00 94.00 ?  356 ASP A C   1 
2741 ATOM   C CB  .  ASP A 1 356 ?  -6.212  -11.852 17.18   1.00 94.00 ?  356 ASP A CB  1 
2742 ATOM   O O   .  ASP A 1 356 ?  -8.941  -12.096 18.96   1.00 94.00 ?  356 ASP A O   1 
2743 ATOM   C CG  .  ASP A 1 356 ?  -5.209  -12.651 16.37   1.00 94.00 ?  356 ASP A CG  1 
2744 ATOM   O OD1 .  ASP A 1 356 ?  -5.504  -13.795 15.965  1.00 94.00 ?  356 ASP A OD1 1 
2745 ATOM   O OD2 .  ASP A 1 356 ?  -4.094  -12.137 16.141  1.00 94.00 ?  356 ASP A OD2 1 
2746 ATOM   N N   .  LEU A 1 357 ?  -8.898  -10.314 17.585  1.00 94.12 ?  357 LEU A N   1 
2747 ATOM   C CA  .  LEU A 1 357 ?  -9.71   -9.46   18.445  1.00 94.12 ?  357 LEU A CA  1 
2748 ATOM   C C   .  LEU A 1 357 ?  -11.148 -9.964  18.54   1.00 94.12 ?  357 LEU A C   1 
2749 ATOM   C CB  .  LEU A 1 357 ?  -9.691  -8.029  17.897  1.00 94.12 ?  357 LEU A CB  1 
2750 ATOM   O O   .  LEU A 1 357 ?  -11.779 -9.865  19.592  1.00 94.12 ?  357 LEU A O   1 
2751 ATOM   C CG  .  LEU A 1 357 ?  -8.39   -7.24   18.078  1.00 94.12 ?  357 LEU A CG  1 
2752 ATOM   C CD1 .  LEU A 1 357 ?  -8.364  -6.03   17.152  1.00 94.12 ?  357 LEU A CD1 1 
2753 ATOM   C CD2 .  LEU A 1 357 ?  -8.233  -6.773  19.521  1.00 94.12 ?  357 LEU A CD2 1 
2754 ATOM   N N   .  TYR A 1 358 ?  -11.668 -10.491 17.436  1.00 94.75 ?  358 TYR A N   1 
2755 ATOM   C CA  .  TYR A 1 358 ?  -13.017 -11.046 17.405  1.00 94.75 ?  358 TYR A CA  1 
2756 ATOM   C C   .  TYR A 1 358 ?  -13.11  -12.491 17.889  1.00 94.75 ?  358 TYR A C   1 
2757 ATOM   C CB  .  TYR A 1 358 ?  -13.577 -11.001 15.98   1.00 94.75 ?  358 TYR A CB  1 
2758 ATOM   O O   .  TYR A 1 358 ?  -14.158 -12.898 18.389  1.00 94.75 ?  358 TYR A O   1 
2759 ATOM   C CG  .  TYR A 1 358 ?  -13.979 -9.626  15.49   1.00 94.75 ?  358 TYR A CG  1 
2760 ATOM   C CD1 .  TYR A 1 358 ?  -15.026 -8.929  16.095  1.00 94.75 ?  358 TYR A CD1 1 
2761 ATOM   C CD2 .  TYR A 1 358 ?  -13.356 -9.049  14.382  1.00 94.75 ?  358 TYR A CD2 1 
2762 ATOM   C CE1 .  TYR A 1 358 ?  -15.434 -7.688  15.611  1.00 94.75 ?  358 TYR A CE1 1 
2763 ATOM   C CE2 .  TYR A 1 358 ?  -13.749 -7.8    13.905  1.00 94.75 ?  358 TYR A CE2 1 
2764 ATOM   O OH  .  TYR A 1 358 ?  -15.178 -5.895  14.048  1.00 94.75 ?  358 TYR A OH  1 
2765 ATOM   C CZ  .  TYR A 1 358 ?  -14.787 -7.125  14.524  1.00 94.75 ?  358 TYR A CZ  1 
2766 ATOM   N N   .  SER A 1 359 ?  -12.059 -13.284 17.702  1.00 93.25 ?  359 SER A N   1 
2767 ATOM   C CA  .  SER A 1 359 ?  -12.141 -14.728 17.916  1.00 93.25 ?  359 SER A CA  1 
2768 ATOM   C C   .  SER A 1 359 ?  -11.317 -15.305 19.064  1.00 93.25 ?  359 SER A C   1 
2769 ATOM   C CB  .  SER A 1 359 ?  -11.739 -15.474 16.642  1.00 93.25 ?  359 SER A CB  1 
2770 ATOM   O O   .  SER A 1 359 ?  -11.596 -16.42  19.504  1.00 93.25 ?  359 SER A O   1 
2771 ATOM   O OG  .  SER A 1 359 ?  -10.355 -15.338 16.372  1.00 93.25 ?  359 SER A OG  1 
2772 ATOM   N N   .  GLN A 1 360 ?  -10.308 -14.585 19.544  1.00 85.50 ?  360 GLN A N   1 
2773 ATOM   C CA  .  GLN A 1 360 ?  -9.437  -15.113 20.591  1.00 85.50 ?  360 GLN A CA  1 
2774 ATOM   C C   .  GLN A 1 360 ?  -9.425  -14.263 21.857  1.00 85.50 ?  360 GLN A C   1 
2775 ATOM   C CB  .  GLN A 1 360 ?  -8.009  -15.292 20.068  1.00 85.50 ?  360 GLN A CB  1 
2776 ATOM   O O   .  GLN A 1 360 ?  -9.511  -14.807 22.958  1.00 85.50 ?  360 GLN A O   1 
2777 ATOM   C CG  .  GLN A 1 360 ?  -7.897  -16.312 18.943  1.00 85.50 ?  360 GLN A CG  1 
2778 ATOM   C CD  .  GLN A 1 360 ?  -6.46   -16.607 18.565  1.00 85.50 ?  360 GLN A CD  1 
2779 ATOM   N NE2 .  GLN A 1 360 ?  -6.136  -16.429 17.294  1.00 85.50 ?  360 GLN A NE2 1 
2780 ATOM   O OE1 .  GLN A 1 360 ?  -5.65   -17.007 19.397  1.00 85.50 ?  360 GLN A OE1 1 
2781 ATOM   N N   .  GLY A 1 361 ?  -9.331  -12.945 21.725  1.00 71.81 ?  361 GLY A N   1 
2782 ATOM   C CA  .  GLY A 1 361 ?  -9.355  -12.089 22.898  1.00 71.81 ?  361 GLY A CA  1 
2783 ATOM   C C   .  GLY A 1 361 ?  -8.8    -10.692 22.709  1.00 71.81 ?  361 GLY A C   1 
2784 ATOM   O O   .  GLY A 1 361 ?  -8.28   -10.329 21.655  1.00 71.81 ?  361 GLY A O   1 
2785 ATOM   N N   .  GLU A 1 362 ?  -8.899  -9.906  23.775  1.00 70.50 ?  362 GLU A N   1 
2786 ATOM   C CA  .  GLU A 1 362 ?  -8.365  -8.546  23.8    1.00 70.50 ?  362 GLU A CA  1 
2787 ATOM   C C   .  GLU A 1 362 ?  -6.9    -8.567  24.232  1.00 70.50 ?  362 GLU A C   1 
2788 ATOM   C CB  .  GLU A 1 362 ?  -9.18   -7.691  24.773  1.00 70.50 ?  362 GLU A CB  1 
2789 ATOM   O O   .  GLU A 1 362 ?  -6.241  -7.53   24.312  1.00 70.50 ?  362 GLU A O   1 
2790 ATOM   C CG  .  GLU A 1 362 ?  -10.654 -7.583  24.406  1.00 70.50 ?  362 GLU A CG  1 
2791 ATOM   C CD  .  GLU A 1 362 ?  -11.417 -6.619  25.297  1.00 70.50 ?  362 GLU A CD  1 
2792 ATOM   O OE1 .  GLU A 1 362 ?  -12.655 -6.532  25.153  1.00 70.50 ?  362 GLU A OE1 1 
2793 ATOM   O OE2 .  GLU A 1 362 ?  -10.801 -5.931  26.138  1.00 70.50 ?  362 GLU A OE2 1 
2794 ATOM   N N   .  ASN A 1 363 ?  -6.417  -9.771  24.521  1.00 75.31 ?  363 ASN A N   1 
2795 ATOM   C CA  .  ASN A 1 363 ?  -5.06   -10.018 24.995  1.00 75.31 ?  363 ASN A CA  1 
2796 ATOM   C C   .  ASN A 1 363 ?  -4.41   -11.218 24.309  1.00 75.31 ?  363 ASN A C   1 
2797 ATOM   C CB  .  ASN A 1 363 ?  -5.119  -10.295 26.5    1.00 75.31 ?  363 ASN A CB  1 
2798 ATOM   O O   .  ASN A 1 363 ?  -3.44   -11.779 24.818  1.00 75.31 ?  363 ASN A O   1 
2799 ATOM   C CG  .  ASN A 1 363 ?  -5.763  -11.629 26.817  1.00 75.31 ?  363 ASN A CG  1 
2800 ATOM   N ND2 .  ASN A 1 363 ?  -5.091  -12.424 27.635  1.00 75.31 ?  363 ASN A ND2 1 
2801 ATOM   O OD1 .  ASN A 1 363 ?  -6.854  -11.945 26.345  1.00 75.31 ?  363 ASN A OD1 1 
2802 ATOM   N N   .  SER A 1 364 ?  -4.968  -11.64  23.179  1.00 80.56 ?  364 SER A N   1 
2803 ATOM   C CA  .  SER A 1 364 ?  -4.555  -12.877 22.52   1.00 80.56 ?  364 SER A CA  1 
2804 ATOM   C C   .  SER A 1 364 ?  -4.291  -12.689 21.029  1.00 80.56 ?  364 SER A C   1 
2805 ATOM   C CB  .  SER A 1 364 ?  -5.633  -13.943 22.727  1.00 80.56 ?  364 SER A CB  1 
2806 ATOM   O O   .  SER A 1 364 ?  -4.868  -13.376 20.186  1.00 80.56 ?  364 SER A O   1 
2807 ATOM   O OG  .  SER A 1 364 ?  -5.869  -14.15  24.11   1.00 80.56 ?  364 SER A OG  1 
2808 ATOM   N N   .  LEU A 1 365 ?  -3.413  -11.746 20.704  1.00 84.88 ?  365 LEU A N   1 
2809 ATOM   C CA  .  LEU A 1 365 ?  -3.085  -11.453 19.313  1.00 84.88 ?  365 LEU A CA  1 
2810 ATOM   C C   .  LEU A 1 365 ?  -1.809  -12.184 18.902  1.00 84.88 ?  365 LEU A C   1 
2811 ATOM   C CB  .  LEU A 1 365 ?  -2.946  -9.943  19.098  1.00 84.88 ?  365 LEU A CB  1 
2812 ATOM   O O   .  LEU A 1 365 ?  -0.789  -12.118 19.588  1.00 84.88 ?  365 LEU A O   1 
2813 ATOM   C CG  .  LEU A 1 365 ?  -4.23   -9.12   18.94   1.00 84.88 ?  365 LEU A CG  1 
2814 ATOM   C CD1 .  LEU A 1 365 ?  -5.103  -9.103  20.189  1.00 84.88 ?  365 LEU A CD1 1 
2815 ATOM   C CD2 .  LEU A 1 365 ?  -3.861  -7.695  18.552  1.00 84.88 ?  365 LEU A CD2 1 
2816 ATOM   N N   .  SER A 1 366 ?  -1.876  -12.897 17.783  1.00 84.19 ?  366 SER A N   1 
2817 ATOM   C CA  .  SER A 1 366 ?  -0.769  -13.733 17.327  1.00 84.19 ?  366 SER A CA  1 
2818 ATOM   C C   .  SER A 1 366 ?  0.324   -12.943 16.614  1.00 84.19 ?  366 SER A C   1 
2819 ATOM   C CB  .  SER A 1 366 ?  -1.296  -14.823 16.391  1.00 84.19 ?  366 SER A CB  1 
2820 ATOM   O O   .  SER A 1 366 ?  1.474   -13.378 16.558  1.00 84.19 ?  366 SER A O   1 
2821 ATOM   O OG  .  SER A 1 366 ?  -1.848  -14.257 15.214  1.00 84.19 ?  366 SER A OG  1 
2822 ATOM   N N   .  LEU A 1 367 ?  -0.028  -11.781 16.075  1.00 82.88 ?  367 LEU A N   1 
2823 ATOM   C CA  .  LEU A 1 367 ?  0.95    -10.905 15.434  1.00 82.88 ?  367 LEU A CA  1 
2824 ATOM   C C   .  LEU A 1 367 ?  1.39    -9.79   16.377  1.00 82.88 ?  367 LEU A C   1 
2825 ATOM   C CB  .  LEU A 1 367 ?  0.374   -10.289 14.155  1.00 82.88 ?  367 LEU A CB  1 
2826 ATOM   O O   .  LEU A 1 367 ?  2.3     -9.026  16.06   1.00 82.88 ?  367 LEU A O   1 
2827 ATOM   C CG  .  LEU A 1 367 ?  -0.052  -11.235 13.029  1.00 82.88 ?  367 LEU A CG  1 
2828 ATOM   C CD1 .  LEU A 1 367 ?  -0.592  -10.418 11.862  1.00 82.88 ?  367 LEU A CD1 1 
2829 ATOM   C CD2 .  LEU A 1 367 ?  1.107   -12.1   12.547  1.00 82.88 ?  367 LEU A CD2 1 
2830 ATOM   N N   .  GLN A 1 368 ?  0.728   -9.7    17.525  1.00 83.00 ?  368 GLN A N   1 
2831 ATOM   C CA  .  GLN A 1 368 ?  1.009   -8.68   18.532  1.00 83.00 ?  368 GLN A CA  1 
2832 ATOM   C C   .  GLN A 1 368 ?  0.92    -9.289  19.93   1.00 83.00 ?  368 GLN A C   1 
2833 ATOM   C CB  .  GLN A 1 368 ?  -0.006  -7.541  18.41   1.00 83.00 ?  368 GLN A CB  1 
2834 ATOM   O O   .  GLN A 1 368 ?  0.047   -8.917  20.716  1.00 83.00 ?  368 GLN A O   1 
2835 ATOM   C CG  .  GLN A 1 368 ?  0.014   -6.802  17.08   1.00 83.00 ?  368 GLN A CG  1 
2836 ATOM   C CD  .  GLN A 1 368 ?  1.198   -5.864  16.952  1.00 83.00 ?  368 GLN A CD  1 
2837 ATOM   N NE2 .  GLN A 1 368 ?  2.019   -6.069  15.935  1.00 83.00 ?  368 GLN A NE2 1 
2838 ATOM   O OE1 .  GLN A 1 368 ?  1.364   -4.954  17.76   1.00 83.00 ?  368 GLN A OE1 1 
2839 ATOM   N N   .  PRO A 1 369 ?  1.803   -10.245 20.26   1.00 82.25 ?  369 PRO A N   1 
2840 ATOM   C CA  .  PRO A 1 369 ?  1.668   -10.793 21.614  1.00 82.25 ?  369 PRO A CA  1 
2841 ATOM   C C   .  PRO A 1 369 ?  2.001   -9.755  22.681  1.00 82.25 ?  369 PRO A C   1 
2842 ATOM   C CB  .  PRO A 1 369 ?  2.666   -11.953 21.621  1.00 82.25 ?  369 PRO A CB  1 
2843 ATOM   O O   .  PRO A 1 369 ?  2.881   -8.914  22.498  1.00 82.25 ?  369 PRO A O   1 
2844 ATOM   C CG  .  PRO A 1 369 ?  3.703   -11.543 20.633  1.00 82.25 ?  369 PRO A CG  1 
2845 ATOM   C CD  .  PRO A 1 369 ?  2.922   -10.873 19.536  1.00 82.25 ?  369 PRO A CD  1 
2846 ATOM   N N   .  GLY A 1 370 ?  1.273   -9.806  23.791  1.00 84.62 ?  370 GLY A N   1 
2847 ATOM   C CA  .  GLY A 1 370 ?  1.446   -8.832  24.854  1.00 84.62 ?  370 GLY A CA  1 
2848 ATOM   C C   .  GLY A 1 370 ?  0.573   -7.6    24.713  1.00 84.62 ?  370 GLY A C   1 
2849 ATOM   O O   .  GLY A 1 370 ?  0.467   -6.82   25.658  1.00 84.62 ?  370 GLY A O   1 
2850 ATOM   N N   .  PHE A 1 371 ?  -0.07   -7.416  23.564  1.00 92.31 ?  371 PHE A N   1 
2851 ATOM   C CA  .  PHE A 1 371 ?  -1.046  -6.342  23.418  1.00 92.31 ?  371 PHE A CA  1 
2852 ATOM   C C   .  PHE A 1 371 ?  -2.228  -6.627  24.339  1.00 92.31 ?  371 PHE A C   1 
2853 ATOM   C CB  .  PHE A 1 371 ?  -1.556  -6.233  21.979  1.00 92.31 ?  371 PHE A CB  1 
2854 ATOM   O O   .  PHE A 1 371 ?  -2.734  -7.747  24.381  1.00 92.31 ?  371 PHE A O   1 
2855 ATOM   C CG  .  PHE A 1 371 ?  -2.68   -5.245  21.82   1.00 92.31 ?  371 PHE A CG  1 
2856 ATOM   C CD1 .  PHE A 1 371 ?  -3.994  -5.683  21.692  1.00 92.31 ?  371 PHE A CD1 1 
2857 ATOM   C CD2 .  PHE A 1 371 ?  -2.433  -3.878  21.861  1.00 92.31 ?  371 PHE A CD2 1 
2858 ATOM   C CE1 .  PHE A 1 371 ?  -5.041  -4.772  21.595  1.00 92.31 ?  371 PHE A CE1 1 
2859 ATOM   C CE2 .  PHE A 1 371 ?  -3.473  -2.957  21.78   1.00 92.31 ?  371 PHE A CE2 1 
2860 ATOM   C CZ  .  PHE A 1 371 ?  -4.782  -3.406  21.657  1.00 92.31 ?  371 PHE A CZ  1 
2861 ATOM   N N   .  GLU A 1 372 ?  -2.67   -5.606  25.064  1.00 92.88 ?  372 GLU A N   1 
2862 ATOM   C CA  .  GLU A 1 372 ?  -3.835  -5.72   25.936  1.00 92.88 ?  372 GLU A CA  1 
2863 ATOM   C C   .  GLU A 1 372 ?  -4.612  -4.409  25.868  1.00 92.88 ?  372 GLU A C   1 
2864 ATOM   C CB  .  GLU A 1 372 ?  -3.408  -5.98   27.382  1.00 92.88 ?  372 GLU A CB  1 
2865 ATOM   O O   .  GLU A 1 372 ?  -4.054  -3.34   26.126  1.00 92.88 ?  372 GLU A O   1 
2866 ATOM   C CG  .  GLU A 1 372 ?  -2.742  -7.325  27.628  1.00 92.88 ?  372 GLU A CG  1 
2867 ATOM   C CD  .  GLU A 1 372 ?  -2.467  -7.554  29.102  1.00 92.88 ?  372 GLU A CD  1 
2868 ATOM   O OE1 .  GLU A 1 372 ?  -1.286  -7.552  29.507  1.00 92.88 ?  372 GLU A OE1 1 
2869 ATOM   O OE2 .  GLU A 1 372 ?  -3.437  -7.727  29.87   1.00 92.88 ?  372 GLU A OE2 1 
2870 ATOM   N N   .  ILE A 1 373 ?  -5.891  -4.476  25.511  1.00 92.31 ?  373 ILE A N   1 
2871 ATOM   C CA  .  ILE A 1 373 ?  -6.69   -3.261  25.37   1.00 92.31 ?  373 ILE A CA  1 
2872 ATOM   C C   .  ILE A 1 373 ?  -6.8    -2.57   26.726  1.00 92.31 ?  373 ILE A C   1 
2873 ATOM   C CB  .  ILE A 1 373 ?  -8.103  -3.514  24.795  1.00 92.31 ?  373 ILE A CB  1 
2874 ATOM   O O   .  ILE A 1 373 ?  -7.172  -3.181  27.728  1.00 92.31 ?  373 ILE A O   1 
2875 ATOM   C CG1 .  ILE A 1 373 ?  -8      -4.189  23.422  1.00 92.31 ?  373 ILE A CG1 1 
2876 ATOM   C CG2 .  ILE A 1 373 ?  -8.853  -2.188  24.674  1.00 92.31 ?  373 ILE A CG2 1 
2877 ATOM   C CD1 .  ILE A 1 373 ?  -9.323  -4.538  22.764  1.00 92.31 ?  373 ILE A CD1 1 
2878 ATOM   N N   .  GLY A 1 374 ?  -6.447  -1.289  26.747  1.00 93.00 ?  374 GLY A N   1 
2879 ATOM   C CA  .  GLY A 1 374 ?  -6.465  -0.506  27.97   1.00 93.00 ?  374 GLY A CA  1 
2880 ATOM   C C   .  GLY A 1 374 ?  -5.25   -0.668  28.865  1.00 93.00 ?  374 GLY A C   1 
2881 ATOM   O O   .  GLY A 1 374 ?  -5.153  0.022   29.88   1.00 93.00 ?  374 GLY A O   1 
2882 ATOM   N N   .  LYS A 1 375 ?  -4.336  -1.573  28.526  1.00 93.94 ?  375 LYS A N   1 
2883 ATOM   C CA  .  LYS A 1 375 ?  -3.182  -1.858  29.378  1.00 93.94 ?  375 LYS A CA  1 
2884 ATOM   C C   .  LYS A 1 375 ?  -1.816  -1.793  28.701  1.00 93.94 ?  375 LYS A C   1 
2885 ATOM   C CB  .  LYS A 1 375 ?  -3.343  -3.233  30.032  1.00 93.94 ?  375 LYS A CB  1 
2886 ATOM   O O   .  LYS A 1 375 ?  -0.869  -1.292  29.305  1.00 93.94 ?  375 LYS A O   1 
2887 ATOM   C CG  .  LYS A 1 375 ?  -4.572  -3.373  30.92   1.00 93.94 ?  375 LYS A CG  1 
2888 ATOM   C CD  .  LYS A 1 375 ?  -4.626  -4.747  31.571  1.00 93.94 ?  375 LYS A CD  1 
2889 ATOM   C CE  .  LYS A 1 375 ?  -5.899  -4.914  32.384  1.00 93.94 ?  375 LYS A CE  1 
2890 ATOM   N NZ  .  LYS A 1 375 ?  -5.888  -6.26   33.046  1.00 93.94 ?  375 LYS A NZ  1 
2891 ATOM   N N   .  LYS A 1 376 ?  -1.688  -2.305  27.48   1.00 94.81 ?  376 LYS A N   1 
2892 ATOM   C CA  .  LYS A 1 376 ?  -0.407  -2.309  26.774  1.00 94.81 ?  376 LYS A CA  1 
2893 ATOM   C C   .  LYS A 1 376 ?  -0.566  -2.205  25.261  1.00 94.81 ?  376 LYS A C   1 
2894 ATOM   C CB  .  LYS A 1 376 ?  0.379   -3.579  27.115  1.00 94.81 ?  376 LYS A CB  1 
2895 ATOM   O O   .  LYS A 1 376 ?  -1.314  -2.97   24.656  1.00 94.81 ?  376 LYS A O   1 
2896 ATOM   C CG  .  LYS A 1 376 ?  1.806   -3.559  26.582  1.00 94.81 ?  376 LYS A CG  1 
2897 ATOM   C CD  .  LYS A 1 376 ?  2.637   -4.732  27.078  1.00 94.81 ?  376 LYS A CD  1 
2898 ATOM   C CE  .  LYS A 1 376 ?  4.022   -4.697  26.451  1.00 94.81 ?  376 LYS A CE  1 
2899 ATOM   N NZ  .  LYS A 1 376 ?  4.837   -5.861  26.931  1.00 94.81 ?  376 LYS A NZ  1 
2900 ATOM   N N   .  ASN A 1 377 ?  0.134   -1.247  24.662  1.00 95.12 ?  377 ASN A N   1 
2901 ATOM   C CA  .  ASN A 1 377 ?  0.145   -1.076  23.212  1.00 95.12 ?  377 ASN A CA  1 
2902 ATOM   C C   .  ASN A 1 377 ?  0.945   -2.195  22.55   1.00 95.12 ?  377 ASN A C   1 
2903 ATOM   C CB  .  ASN A 1 377 ?  0.791   0.261   22.841  1.00 95.12 ?  377 ASN A CB  1 
2904 ATOM   O O   .  ASN A 1 377 ?  1.801   -2.818  23.177  1.00 95.12 ?  377 ASN A O   1 
2905 ATOM   C CG  .  ASN A 1 377 ?  -0.086  1.451   23.156  1.00 95.12 ?  377 ASN A CG  1 
2906 ATOM   N ND2 .  ASN A 1 377 ?  0.53    2.546   23.57   1.00 95.12 ?  377 ASN A ND2 1 
2907 ATOM   O OD1 .  ASN A 1 377 ?  -1.306  1.395   23.017  1.00 95.12 ?  377 ASN A OD1 1 
2908 ATOM   N N   .  GLY A 1 378 ?  0.671   -2.437  21.273  1.00 90.88 ?  378 GLY A N   1 
2909 ATOM   C CA  .  GLY A 1 378 ?  1.361   -3.489  20.548  1.00 90.88 ?  378 GLY A CA  1 
2910 ATOM   C C   .  GLY A 1 378 ?  2.8     -3.134  20.231  1.00 90.88 ?  378 GLY A C   1 
2911 ATOM   O O   .  GLY A 1 378 ?  3.125   -1.973  19.98   1.00 90.88 ?  378 GLY A O   1 
2912 ATOM   N N   .  GLU A 1 379 ?  3.673   -4.135  20.231  1.00 85.50 ?  379 GLU A N   1 
2913 ATOM   C CA  .  GLU A 1 379 ?  5.075   -3.934  19.882  1.00 85.50 ?  379 GLU A CA  1 
2914 ATOM   C C   .  GLU A 1 379 ?  5.241   -4.045  18.37   1.00 85.50 ?  379 GLU A C   1 
2915 ATOM   C CB  .  GLU A 1 379 ?  5.967   -4.968  20.575  1.00 85.50 ?  379 GLU A CB  1 
2916 ATOM   O O   .  GLU A 1 379 ?  4.646   -4.914  17.731  1.00 85.50 ?  379 GLU A O   1 
2917 ATOM   C CG  .  GLU A 1 379 ?  5.979   -4.853  22.094  1.00 85.50 ?  379 GLU A CG  1 
2918 ATOM   C CD  .  GLU A 1 379 ?  6.936   -5.833  22.749  1.00 85.50 ?  379 GLU A CD  1 
2919 ATOM   O OE1 .  GLU A 1 379 ?  6.975   -5.879  23.997  1.00 85.50 ?  379 GLU A OE1 1 
2920 ATOM   O OE2 .  GLU A 1 379 ?  7.664   -6.554  22.033  1.00 85.50 ?  379 GLU A OE2 1 
2921 ATOM   N N   .  ALA A 1 380 ?  6.041   -3.159  17.787  1.00 74.69 ?  380 ALA A N   1 
2922 ATOM   C CA  .  ALA A 1 380 ?  6.228   -3.141  16.339  1.00 74.69 ?  380 ALA A CA  1 
2923 ATOM   C C   .  ALA A 1 380 ?  7.113   -4.286  15.853  1.00 74.69 ?  380 ALA A C   1 
2924 ATOM   C CB  .  ALA A 1 380 ?  6.798   -1.799  15.899  1.00 74.69 ?  380 ALA A CB  1 
2925 ATOM   O O   .  ALA A 1 380 ?  8.293   -4.101  15.554  1.00 74.69 ?  380 ALA A O   1 
2926 ATOM   N N   .  LYS A 1 381 ?  6.522   -5.471  15.741  1.00 74.50 ?  381 LYS A N   1 
2927 ATOM   C CA  .  LYS A 1 381 ?  7.075   -6.508  14.876  1.00 74.50 ?  381 LYS A CA  1 
2928 ATOM   C C   .  LYS A 1 381 ?  7.063   -5.947  13.46   1.00 74.50 ?  381 LYS A C   1 
2929 ATOM   C CB  .  LYS A 1 381 ?  6.257   -7.801  14.929  1.00 74.50 ?  381 LYS A CB  1 
2930 ATOM   O O   .  LYS A 1 381 ?  6.084   -5.337  13.03   1.00 74.50 ?  381 LYS A O   1 
2931 ATOM   C CG  .  LYS A 1 381 ?  6.401   -8.576  16.231  1.00 74.50 ?  381 LYS A CG  1 
2932 ATOM   C CD  .  LYS A 1 381 ?  5.729   -9.938  16.133  1.00 74.50 ?  381 LYS A CD  1 
2933 ATOM   C CE  .  LYS A 1 381 ?  5.914   -10.733 17.416  1.00 74.50 ?  381 LYS A CE  1 
2934 ATOM   N NZ  .  LYS A 1 381 ?  5.325   -12.103 17.244  1.00 74.50 ?  381 LYS A NZ  1 
2935 ATOM   N N   .  VAL A 1 382 ?  8.165   -6.147  12.747  1.00 81.50 ?  382 VAL A N   1 
2936 ATOM   C CA  .  VAL A 1 382 ?  8.287   -5.669  11.374  1.00 81.50 ?  382 VAL A CA  1 
2937 ATOM   C C   .  VAL A 1 382 ?  8.189   -6.888  10.466  1.00 81.50 ?  382 VAL A C   1 
2938 ATOM   C CB  .  VAL A 1 382 ?  9.606   -4.909  11.124  1.00 81.50 ?  382 VAL A CB  1 
2939 ATOM   O O   .  VAL A 1 382 ?  8.99    -7.818  10.564  1.00 81.50 ?  382 VAL A O   1 
2940 ATOM   C CG1 .  VAL A 1 382 ?  9.674   -4.438  9.678   1.00 81.50 ?  382 VAL A CG1 1 
2941 ATOM   C CG2 .  VAL A 1 382 ?  9.724   -3.713  12.067  1.00 81.50 ?  382 VAL A CG2 1 
2942 ATOM   N N   .  PHE A 1 383 ?  7.166   -6.897  9.62    1.00 82.75 ?  383 PHE A N   1 
2943 ATOM   C CA  .  PHE A 1 383 ?  6.817   -8.074  8.833   1.00 82.75 ?  383 PHE A CA  1 
2944 ATOM   C C   .  PHE A 1 383 ?  7.561   -8.089  7.5     1.00 82.75 ?  383 PHE A C   1 
2945 ATOM   C CB  .  PHE A 1 383 ?  5.3     -8.122  8.629   1.00 82.75 ?  383 PHE A CB  1 
2946 ATOM   O O   .  PHE A 1 383 ?  7.158   -7.448  6.528   1.00 82.75 ?  383 PHE A O   1 
2947 ATOM   C CG  .  PHE A 1 383 ?  4.518   -8.105  9.915   1.00 82.75 ?  383 PHE A CG  1 
2948 ATOM   C CD1 .  PHE A 1 383 ?  4.509   -9.217  10.751  1.00 82.75 ?  383 PHE A CD1 1 
2949 ATOM   C CD2 .  PHE A 1 383 ?  3.813   -6.969  10.301  1.00 82.75 ?  383 PHE A CD2 1 
2950 ATOM   C CE1 .  PHE A 1 383 ?  3.854   -9.179  11.98   1.00 82.75 ?  383 PHE A CE1 1 
2951 ATOM   C CE2 .  PHE A 1 383 ?  3.155   -6.921  11.528  1.00 82.75 ?  383 PHE A CE2 1 
2952 ATOM   C CZ  .  PHE A 1 383 ?  3.185   -8.024  12.375  1.00 82.75 ?  383 PHE A CZ  1 
2953 ATOM   N N   .  GLY A 1 384 ?  8.673   -8.817  7.484   1.00 83.06 ?  384 GLY A N   1 
2954 ATOM   C CA  .  GLY A 1 384 ?  9.482   -8.972  6.289   1.00 83.06 ?  384 GLY A CA  1 
2955 ATOM   C C   .  GLY A 1 384 ?  9.171   -10.244 5.525   1.00 83.06 ?  384 GLY A C   1 
2956 ATOM   O O   .  GLY A 1 384 ?  8.073   -10.794 5.619   1.00 83.06 ?  384 GLY A O   1 
2957 ATOM   N N   .  TYR A 1 385 ?  10.146  -10.72  4.759   1.00 81.00 ?  385 TYR A N   1 
2958 ATOM   C CA  .  TYR A 1 385 ?  9.986   -11.952 3.995   1.00 81.00 ?  385 TYR A CA  1 
2959 ATOM   C C   .  TYR A 1 385 ?  10.079  -13.12  4.973   1.00 81.00 ?  385 TYR A C   1 
2960 ATOM   C CB  .  TYR A 1 385 ?  11.07   -12.053 2.919   1.00 81.00 ?  385 TYR A CB  1 
2961 ATOM   O O   .  TYR A 1 385 ?  11.021  -13.202 5.762   1.00 81.00 ?  385 TYR A O   1 
2962 ATOM   C CG  .  TYR A 1 385 ?  10.819  -13.157 1.916   1.00 81.00 ?  385 TYR A CG  1 
2963 ATOM   C CD1 .  TYR A 1 385 ?  11.344  -14.435 2.109   1.00 81.00 ?  385 TYR A CD1 1 
2964 ATOM   C CD2 .  TYR A 1 385 ?  10.045  -12.922 0.779   1.00 81.00 ?  385 TYR A CD2 1 
2965 ATOM   C CE1 .  TYR A 1 385 ?  11.104  -15.453 1.189   1.00 81.00 ?  385 TYR A CE1 1 
2966 ATOM   C CE2 .  TYR A 1 385 ?  9.797   -13.938 -0.141  1.00 81.00 ?  385 TYR A CE2 1 
2967 ATOM   O OH  .  TYR A 1 385 ?  10.063  -16.211 -0.822  1.00 81.00 ?  385 TYR A OH  1 
2968 ATOM   C CZ  .  TYR A 1 385 ?  10.325  -15.201 0.073   1.00 81.00 ?  385 TYR A CZ  1 
2969 ATOM   N N   .  GLY A 1 386 ?  9.085   -14.001 4.949   1.00 75.31 ?  386 GLY A N   1 
2970 ATOM   C CA  .  GLY A 1 386 ?  9.013   -15.074 5.924   1.00 75.31 ?  386 GLY A CA  1 
2971 ATOM   C C   .  GLY A 1 386 ?  9.569   -16.397 5.44    1.00 75.31 ?  386 GLY A C   1 
2972 ATOM   O O   .  GLY A 1 386 ?  9.746   -16.623 4.243   1.00 75.31 ?  386 GLY A O   1 
2973 ATOM   N N   .  GLU A 1 387 ?  9.834   -17.285 6.392   1.00 72.81 ?  387 GLU A N   1 
2974 ATOM   C CA  .  GLU A 1 387 ?  10.318  -18.631 6.094   1.00 72.81 ?  387 GLU A CA  1 
2975 ATOM   C C   .  GLU A 1 387 ?  9.162   -19.52  5.639   1.00 72.81 ?  387 GLU A C   1 
2976 ATOM   C CB  .  GLU A 1 387 ?  10.958  -19.243 7.343   1.00 72.81 ?  387 GLU A CB  1 
2977 ATOM   O O   .  GLU A 1 387 ?  9.361   -20.546 4.99    1.00 72.81 ?  387 GLU A O   1 
2978 ATOM   C CG  .  GLU A 1 387 ?  12.197  -18.504 7.832   1.00 72.81 ?  387 GLU A CG  1 
2979 ATOM   C CD  .  GLU A 1 387 ?  12.807  -19.136 9.07    1.00 72.81 ?  387 GLU A CD  1 
2980 ATOM   O OE1 .  GLU A 1 387 ?  13.847  -18.628 9.54    1.00 72.81 ?  387 GLU A OE1 1 
2981 ATOM   O OE2 .  GLU A 1 387 ?  12.256  -20.131 9.589   1.00 72.81 ?  387 GLU A OE2 1 
2982 ATOM   N N   .  ASN A 1 388 ?  7.95    -19.114 6       1.00 75.81 ?  388 ASN A N   1 
2983 ATOM   C CA  .  ASN A 1 388 ?  6.728   -19.831 5.656   1.00 75.81 ?  388 ASN A CA  1 
2984 ATOM   C C   .  ASN A 1 388 ?  5.606   -18.815 5.456   1.00 75.81 ?  388 ASN A C   1 
2985 ATOM   C CB  .  ASN A 1 388 ?  6.391   -20.826 6.768   1.00 75.81 ?  388 ASN A CB  1 
2986 ATOM   O O   .  ASN A 1 388 ?  5.745   -17.651 5.828   1.00 75.81 ?  388 ASN A O   1 
2987 ATOM   C CG  .  ASN A 1 388 ?  6.129   -20.151 8.096   1.00 75.81 ?  388 ASN A CG  1 
2988 ATOM   N ND2 .  ASN A 1 388 ?  6.922   -20.494 9.098   1.00 75.81 ?  388 ASN A ND2 1 
2989 ATOM   O OD1 .  ASN A 1 388 ?  5.219   -19.337 8.23    1.00 75.81 ?  388 ASN A OD1 1 
2990 ATOM   N N   .  GLU A 1 389 ?  4.502   -19.244 4.854   1.00 71.44 ?  389 GLU A N   1 
2991 ATOM   C CA  .  GLU A 1 389 ?  3.425   -18.333 4.472   1.00 71.44 ?  389 GLU A CA  1 
2992 ATOM   C C   .  GLU A 1 389 ?  2.738   -17.628 5.639   1.00 71.44 ?  389 GLU A C   1 
2993 ATOM   C CB  .  GLU A 1 389 ?  2.372   -19.078 3.646   1.00 71.44 ?  389 GLU A CB  1 
2994 ATOM   O O   .  GLU A 1 389 ?  2.243   -16.514 5.479   1.00 71.44 ?  389 GLU A O   1 
2995 ATOM   C CG  .  GLU A 1 389 ?  2.907   -19.696 2.361   1.00 71.44 ?  389 GLU A CG  1 
2996 ATOM   C CD  .  GLU A 1 389 ?  3.583   -18.676 1.461   1.00 71.44 ?  389 GLU A CD  1 
2997 ATOM   O OE1 .  GLU A 1 389 ?  4.726   -18.927 1.024   1.00 71.44 ?  389 GLU A OE1 1 
2998 ATOM   O OE2 .  GLU A 1 389 ?  2.987   -17.613 1.19    1.00 71.44 ?  389 GLU A OE2 1 
2999 ATOM   N N   .  ALA A 1 390 ?  2.716   -18.247 6.814   1.00 72.19 ?  390 ALA A N   1 
3000 ATOM   C CA  .  ALA A 1 390 ?  2.109   -17.625 7.988   1.00 72.19 ?  390 ALA A CA  1 
3001 ATOM   C C   .  ALA A 1 390 ?  2.915   -16.417 8.461   1.00 72.19 ?  390 ALA A C   1 
3002 ATOM   C CB  .  ALA A 1 390 ?  1.978   -18.645 9.112   1.00 72.19 ?  390 ALA A CB  1 
3003 ATOM   O O   .  ALA A 1 390 ?  2.363   -15.473 9.027   1.00 72.19 ?  390 ALA A O   1 
3004 ATOM   N N   .  SER A 1 391 ?  4.225   -16.457 8.238   1.00 76.19 ?  391 SER A N   1 
3005 ATOM   C CA  .  SER A 1 391 ?  5.131   -15.376 8.62    1.00 76.19 ?  391 SER A CA  1 
3006 ATOM   C C   .  SER A 1 391 ?  5.465   -14.421 7.476   1.00 76.19 ?  391 SER A C   1 
3007 ATOM   C CB  .  SER A 1 391 ?  6.433   -15.983 9.148   1.00 76.19 ?  391 SER A CB  1 
3008 ATOM   O O   .  SER A 1 391 ?  6.067   -13.37  7.699   1.00 76.19 ?  391 SER A O   1 
3009 ATOM   O OG  .  SER A 1 391 ?  7.105   -16.706 8.131   1.00 76.19 ?  391 SER A OG  1 
3010 ATOM   N N   .  LYS A 1 392 ?  5.101   -14.794 6.254   1.00 85.12 ?  392 LYS A N   1 
3011 ATOM   C CA  .  LYS A 1 392 ?  5.459   -14.039 5.055   1.00 85.12 ?  392 LYS A CA  1 
3012 ATOM   C C   .  LYS A 1 392 ?  4.366   -13.054 4.659   1.00 85.12 ?  392 LYS A C   1 
3013 ATOM   C CB  .  LYS A 1 392 ?  5.717   -15.02  3.907   1.00 85.12 ?  392 LYS A CB  1 
3014 ATOM   O O   .  LYS A 1 392 ?  3.324   -13.443 4.134   1.00 85.12 ?  392 LYS A O   1 
3015 ATOM   C CG  .  LYS A 1 392 ?  6.284   -14.392 2.64    1.00 85.12 ?  392 LYS A CG  1 
3016 ATOM   C CD  .  LYS A 1 392 ?  6.365   -15.397 1.498   1.00 85.12 ?  392 LYS A CD  1 
3017 ATOM   C CE  .  LYS A 1 392 ?  7.367   -16.509 1.772   1.00 85.12 ?  392 LYS A CE  1 
3018 ATOM   N NZ  .  LYS A 1 392 ?  7.412   -17.43  0.589   1.00 85.12 ?  392 LYS A NZ  1 
3019 ATOM   N N   .  TYR A 1 393 ?  4.621   -11.772 4.894   1.00 91.56 ?  393 TYR A N   1 
3020 ATOM   C CA  .  TYR A 1 393 ?  3.664   -10.724 4.544   1.00 91.56 ?  393 TYR A CA  1 
3021 ATOM   C C   .  TYR A 1 393 ?  4.133   -9.86   3.378   1.00 91.56 ?  393 TYR A C   1 
3022 ATOM   C CB  .  TYR A 1 393 ?  3.369   -9.845  5.76    1.00 91.56 ?  393 TYR A CB  1 
3023 ATOM   O O   .  TYR A 1 393 ?  3.365   -9.054  2.85    1.00 91.56 ?  393 TYR A O   1 
3024 ATOM   C CG  .  TYR A 1 393 ?  2.614   -10.588 6.84    1.00 91.56 ?  393 TYR A CG  1 
3025 ATOM   C CD1 .  TYR A 1 393 ?  1.219   -10.564 6.873   1.00 91.56 ?  393 TYR A CD1 1 
3026 ATOM   C CD2 .  TYR A 1 393 ?  3.286   -11.359 7.789   1.00 91.56 ?  393 TYR A CD2 1 
3027 ATOM   C CE1 .  TYR A 1 393 ?  0.512   -11.37  7.761   1.00 91.56 ?  393 TYR A CE1 1 
3028 ATOM   C CE2 .  TYR A 1 393 ?  2.583   -12.172 8.675   1.00 91.56 ?  393 TYR A CE2 1 
3029 ATOM   O OH  .  TYR A 1 393 ?  0.509   -13.079 9.43    1.00 91.56 ?  393 TYR A OH  1 
3030 ATOM   C CZ  .  TYR A 1 393 ?  1.201   -12.204 8.625   1.00 91.56 ?  393 TYR A CZ  1 
3031 ATOM   N N   .  VAL A 1 394 ?  5.379   -10.044 2.957   1.00 94.25 ?  394 VAL A N   1 
3032 ATOM   C CA  .  VAL A 1 394 ?  5.887   -9.42   1.738   1.00 94.25 ?  394 VAL A CA  1 
3033 ATOM   C C   .  VAL A 1 394 ?  6.535   -10.506 0.886   1.00 94.25 ?  394 VAL A C   1 
3034 ATOM   C CB  .  VAL A 1 394 ?  6.886   -8.269  2.003   1.00 94.25 ?  394 VAL A CB  1 
3035 ATOM   O O   .  VAL A 1 394 ?  7.05    -11.491 1.414   1.00 94.25 ?  394 VAL A O   1 
3036 ATOM   C CG1 .  VAL A 1 394 ?  6.232   -7.155  2.817   1.00 94.25 ?  394 VAL A CG1 1 
3037 ATOM   C CG2 .  VAL A 1 394 ?  8.13    -8.763  2.729   1.00 94.25 ?  394 VAL A CG2 1 
3038 ATOM   N N   .  GLY A 1 395 ?  6.493   -10.345 -0.432  1.00 94.88 ?  395 GLY A N   1 
3039 ATOM   C CA  .  GLY A 1 395 ?  7.015   -11.358 -1.332  1.00 94.88 ?  395 GLY A CA  1 
3040 ATOM   C C   .  GLY A 1 395 ?  6.897   -10.929 -2.781  1.00 94.88 ?  395 GLY A C   1 
3041 ATOM   O O   .  GLY A 1 395 ?  6.704   -9.745  -3.056  1.00 94.88 ?  395 GLY A O   1 
3042 ATOM   N N   .  VAL A 1 396 ?  6.998   -11.872 -3.711  1.00 96.88 ?  396 VAL A N   1 
3043 ATOM   C CA  .  VAL A 1 396 ?  6.862   -11.569 -5.135  1.00 96.88 ?  396 VAL A CA  1 
3044 ATOM   C C   .  VAL A 1 396 ?  5.781   -12.436 -5.772  1.00 96.88 ?  396 VAL A C   1 
3045 ATOM   C CB  .  VAL A 1 396 ?  8.183   -11.74  -5.921  1.00 96.88 ?  396 VAL A CB  1 
3046 ATOM   O O   .  VAL A 1 396 ?  5.652   -13.62  -5.463  1.00 96.88 ?  396 VAL A O   1 
3047 ATOM   C CG1 .  VAL A 1 396 ?  9.203   -10.696 -5.475  1.00 96.88 ?  396 VAL A CG1 1 
3048 ATOM   C CG2 .  VAL A 1 396 ?  8.763   -13.144 -5.759  1.00 96.88 ?  396 VAL A CG2 1 
3049 ATOM   N N   .  ALA A 1 397 ?  4.984   -11.828 -6.645  1.00 96.75 ?  397 ALA A N   1 
3050 ATOM   C CA  .  ALA A 1 397 ?  3.932   -12.537 -7.367  1.00 96.75 ?  397 ALA A CA  1 
3051 ATOM   C C   .  ALA A 1 397 ?  4.448   -13.09  -8.693  1.00 96.75 ?  397 ALA A C   1 
3052 ATOM   C CB  .  ALA A 1 397 ?  2.757   -11.603 -7.62   1.00 96.75 ?  397 ALA A CB  1 
3053 ATOM   O O   .  ALA A 1 397 ?  5.374   -12.539 -9.288  1.00 96.75 ?  397 ALA A O   1 
3054 ATOM   N N   .  THR A 1 398 ?  3.837   -14.171 -9.166  1.00 97.44 ?  398 THR A N   1 
3055 ATOM   C CA  .  THR A 1 398 ?  4.223   -14.779 -10.437 1.00 97.44 ?  398 THR A CA  1 
3056 ATOM   C C   .  THR A 1 398 ?  3.882   -13.854 -11.601 1.00 97.44 ?  398 THR A C   1 
3057 ATOM   C CB  .  THR A 1 398 ?  3.52    -16.135 -10.655 1.00 97.44 ?  398 THR A CB  1 
3058 ATOM   O O   .  THR A 1 398 ?  2.988   -13.013 -11.51  1.00 97.44 ?  398 THR A O   1 
3059 ATOM   C CG2 .  THR A 1 398 ?  4.012   -17.175 -9.655  1.00 97.44 ?  398 THR A CG2 1 
3060 ATOM   O OG1 .  THR A 1 398 ?  2.107   -15.972 -10.488 1.00 97.44 ?  398 THR A OG1 1 
3061 ATOM   N N   .  SER A 1 399 ?  4.618   -14.006 -12.696 1.00 98.19 ?  399 SER A N   1 
3062 ATOM   C CA  .  SER A 1 399 ?  4.517   -13.103 -13.839 1.00 98.19 ?  399 SER A CA  1 
3063 ATOM   C C   .  SER A 1 399 ?  3.2     -13.189 -14.606 1.00 98.19 ?  399 SER A C   1 
3064 ATOM   C CB  .  SER A 1 399 ?  5.679   -13.372 -14.797 1.00 98.19 ?  399 SER A CB  1 
3065 ATOM   O O   .  SER A 1 399 ?  2.546   -14.23  -14.664 1.00 98.19 ?  399 SER A O   1 
3066 ATOM   O OG  .  SER A 1 399 ?  5.598   -14.68  -15.336 1.00 98.19 ?  399 SER A OG  1 
3067 ATOM   N N   .  GLY A 1 400 ?  2.835   -12.061 -15.206 1.00 97.31 ?  400 GLY A N   1 
3068 ATOM   C CA  .  GLY A 1 400 ?  1.649   -11.944 -16.037 1.00 97.31 ?  400 GLY A CA  1 
3069 ATOM   C C   .  GLY A 1 400 ?  1.976   -11.142 -17.281 1.00 97.31 ?  400 GLY A C   1 
3070 ATOM   O O   .  GLY A 1 400 ?  1.322   -10.146 -17.588 1.00 97.31 ?  400 GLY A O   1 
3071 ATOM   N N   .  LEU A 1 401 ?  3.018   -11.568 -17.986 1.00 97.06 ?  401 LEU A N   1 
3072 ATOM   C CA  .  LEU A 1 401 ?  3.516   -10.877 -19.173 1.00 97.06 ?  401 LEU A CA  1 
3073 ATOM   C C   .  LEU A 1 401 ?  2.724   -11.199 -20.437 1.00 97.06 ?  401 LEU A C   1 
3074 ATOM   C CB  .  LEU A 1 401 ?  4.989   -11.236 -19.389 1.00 97.06 ?  401 LEU A CB  1 
3075 ATOM   O O   .  LEU A 1 401 ?  3.054   -10.709 -21.515 1.00 97.06 ?  401 LEU A O   1 
3076 ATOM   C CG  .  LEU A 1 401 ?  5.978   -10.756 -18.322 1.00 97.06 ?  401 LEU A CG  1 
3077 ATOM   C CD1 .  LEU A 1 401 ?  7.333   -11.41  -18.54  1.00 97.06 ?  401 LEU A CD1 1 
3078 ATOM   C CD2 .  LEU A 1 401 ?  6.138   -9.24   -18.36  1.00 97.06 ?  401 LEU A CD2 1 
3079 ATOM   N N   .  LEU A 1 402 ?  1.677   -12.004 -20.289 1.00 93.56 ?  402 LEU A N   1 
3080 ATOM   C CA  .  LEU A 1 402 ?  0.754   -12.349 -21.37  1.00 93.56 ?  402 LEU A CA  1 
3081 ATOM   C C   .  LEU A 1 402 ?  1.434   -13.108 -22.508 1.00 93.56 ?  402 LEU A C   1 
3082 ATOM   C CB  .  LEU A 1 402 ?  0.072   -11.093 -21.925 1.00 93.56 ?  402 LEU A CB  1 
3083 ATOM   O O   .  LEU A 1 402 ?  0.953   -13.125 -23.64  1.00 93.56 ?  402 LEU A O   1 
3084 ATOM   C CG  .  LEU A 1 402 ?  -0.589  -10.113 -20.95  1.00 93.56 ?  402 LEU A CG  1 
3085 ATOM   C CD1 .  LEU A 1 402 ?  -1.091  -8.905  -21.732 1.00 93.56 ?  402 LEU A CD1 1 
3086 ATOM   C CD2 .  LEU A 1 402 ?  -1.745  -10.748 -20.186 1.00 93.56 ?  402 LEU A CD2 1 
3087 ATOM   N N   .  ASP A 1 403 ?  2.553   -13.749 -22.191 1.00 93.19 ?  403 ASP A N   1 
3088 ATOM   C CA  .  ASP A 1 403 ?  3.288   -14.583 -23.135 1.00 93.19 ?  403 ASP A CA  1 
3089 ATOM   C C   .  ASP A 1 403 ?  3.942   -15.725 -22.365 1.00 93.19 ?  403 ASP A C   1 
3090 ATOM   C CB  .  ASP A 1 403 ?  4.372   -13.778 -23.853 1.00 93.19 ?  403 ASP A CB  1 
3091 ATOM   O O   .  ASP A 1 403 ?  4.811   -15.496 -21.525 1.00 93.19 ?  403 ASP A O   1 
3092 ATOM   C CG  .  ASP A 1 403 ?  5.127   -14.617 -24.865 1.00 93.19 ?  403 ASP A CG  1 
3093 ATOM   O OD1 .  ASP A 1 403 ?  4.51    -15.074 -25.85  1.00 93.19 ?  403 ASP A OD1 1 
3094 ATOM   O OD2 .  ASP A 1 403 ?  6.34    -14.843 -24.669 1.00 93.19 ?  403 ASP A OD2 1 
3095 ATOM   N N   .  SER A 1 404 ?  3.518   -16.953 -22.643 1.00 93.50 ?  404 SER A N   1 
3096 ATOM   C CA  .  SER A 1 404 ?  3.953   -18.111 -21.866 1.00 93.50 ?  404 SER A CA  1 
3097 ATOM   C C   .  SER A 1 404 ?  5.464   -18.319 -21.861 1.00 93.50 ?  404 SER A C   1 
3098 ATOM   C CB  .  SER A 1 404 ?  3.271   -19.374 -22.395 1.00 93.50 ?  404 SER A CB  1 
3099 ATOM   O O   .  SER A 1 404 ?  6.017   -18.783 -20.865 1.00 93.50 ?  404 SER A O   1 
3100 ATOM   O OG  .  SER A 1 404 ?  3.643   -19.625 -23.739 1.00 93.50 ?  404 SER A OG  1 
3101 ATOM   N N   .  LYS A 1 405 ?  6.14    -17.991 -22.958 1.00 96.44 ?  405 LYS A N   1 
3102 ATOM   C CA  .  LYS A 1 405 ?  7.592   -18.145 -23.019 1.00 96.44 ?  405 LYS A CA  1 
3103 ATOM   C C   .  LYS A 1 405 ?  8.285   -17.154 -22.092 1.00 96.44 ?  405 LYS A C   1 
3104 ATOM   C CB  .  LYS A 1 405 ?  8.103   -17.973 -24.452 1.00 96.44 ?  405 LYS A CB  1 
3105 ATOM   O O   .  LYS A 1 405 ?  9.208   -17.519 -21.366 1.00 96.44 ?  405 LYS A O   1 
3106 ATOM   C CG  .  LYS A 1 405 ?  9.589   -18.272 -24.593 1.00 96.44 ?  405 LYS A CG  1 
3107 ATOM   C CD  .  LYS A 1 405 ?  10.08   -18.033 -26.012 1.00 96.44 ?  405 LYS A CD  1 
3108 ATOM   C CE  .  LYS A 1 405 ?  11.553  -18.389 -26.132 1.00 96.44 ?  405 LYS A CE  1 
3109 ATOM   N NZ  .  LYS A 1 405 ?  12.016  -18.111 -27.531 1.00 96.44 ?  405 LYS A NZ  1 
3110 ATOM   N N   .  ASN A 1 406 ?  7.851   -15.899 -22.128 1.00 96.88 ?  406 ASN A N   1 
3111 ATOM   C CA  .  ASN A 1 406 ?  8.425   -14.875 -21.263 1.00 96.88 ?  406 ASN A CA  1 
3112 ATOM   C C   .  ASN A 1 406 ?  8.061   -15.125 -19.802 1.00 96.88 ?  406 ASN A C   1 
3113 ATOM   C CB  .  ASN A 1 406 ?  7.936   -13.485 -21.677 1.00 96.88 ?  406 ASN A CB  1 
3114 ATOM   O O   .  ASN A 1 406 ?  8.861   -14.843 -18.912 1.00 96.88 ?  406 ASN A O   1 
3115 ATOM   C CG  .  ASN A 1 406 ?  8.65    -12.957 -22.902 1.00 96.88 ?  406 ASN A CG  1 
3116 ATOM   N ND2 .  ASN A 1 406 ?  7.908   -12.318 -23.792 1.00 96.88 ?  406 ASN A ND2 1 
3117 ATOM   O OD1 .  ASN A 1 406 ?  9.862   -13.102 -23.036 1.00 96.88 ?  406 ASN A OD1 1 
3118 ATOM   N N   .  ASP A 1 407 ?  6.861   -15.637 -19.555 1.00 97.31 ?  407 ASP A N   1 
3119 ATOM   C CA  .  ASP A 1 407 ?  6.422   -15.956 -18.199 1.00 97.31 ?  407 ASP A CA  1 
3120 ATOM   C C   .  ASP A 1 407 ?  7.239   -17.098 -17.602 1.00 97.31 ?  407 ASP A C   1 
3121 ATOM   C CB  .  ASP A 1 407 ?  4.94    -16.339 -18.185 1.00 97.31 ?  407 ASP A CB  1 
3122 ATOM   O O   .  ASP A 1 407 ?  7.578   -17.076 -16.421 1.00 97.31 ?  407 ASP A O   1 
3123 ATOM   C CG  .  ASP A 1 407 ?  4.027   -15.147 -18.402 1.00 97.31 ?  407 ASP A CG  1 
3124 ATOM   O OD1 .  ASP A 1 407 ?  4.292   -14.075 -17.818 1.00 97.31 ?  407 ASP A OD1 1 
3125 ATOM   O OD2 .  ASP A 1 407 ?  3.027   -15.27  -19.14  1.00 97.31 ?  407 ASP A OD2 1 
3126 ATOM   N N   .  GLU A 1 408 ?  7.557   -18.103 -18.412 1.00 98.38 ?  408 GLU A N   1 
3127 ATOM   C CA  .  GLU A 1 408 ?  8.362   -19.232 -17.956 1.00 98.38 ?  408 GLU A CA  1 
3128 ATOM   C C   .  GLU A 1 408 ?  9.75    -18.764 -17.527 1.00 98.38 ?  408 GLU A C   1 
3129 ATOM   C CB  .  GLU A 1 408 ?  8.472   -20.274 -19.073 1.00 98.38 ?  408 GLU A CB  1 
3130 ATOM   O O   .  GLU A 1 408 ?  10.29   -19.222 -16.519 1.00 98.38 ?  408 GLU A O   1 
3131 ATOM   C CG  .  GLU A 1 408 ?  9.103   -21.589 -18.642 1.00 98.38 ?  408 GLU A CG  1 
3132 ATOM   C CD  .  GLU A 1 408 ?  9.245   -22.566 -19.795 1.00 98.38 ?  408 GLU A CD  1 
3133 ATOM   O OE1 .  GLU A 1 408 ?  10.135  -23.441 -19.723 1.00 98.38 ?  408 GLU A OE1 1 
3134 ATOM   O OE2 .  GLU A 1 408 ?  8.472   -22.482 -20.773 1.00 98.38 ?  408 GLU A OE2 1 
3135 ATOM   N N   .  ILE A 1 409 ?  10.322  -17.84  -18.291 1.00 98.56 ?  409 ILE A N   1 
3136 ATOM   C CA  .  ILE A 1 409 ?  11.643  -17.292 -17.992 1.00 98.56 ?  409 ILE A CA  1 
3137 ATOM   C C   .  ILE A 1 409 ?  11.551  -16.371 -16.779 1.00 98.56 ?  409 ILE A C   1 
3138 ATOM   C CB  .  ILE A 1 409 ?  12.231  -16.515 -19.194 1.00 98.56 ?  409 ILE A CB  1 
3139 ATOM   O O   .  ILE A 1 409 ?  12.419  -16.396 -15.906 1.00 98.56 ?  409 ILE A O   1 
3140 ATOM   C CG1 .  ILE A 1 409 ?  12.371  -17.434 -20.415 1.00 98.56 ?  409 ILE A CG1 1 
3141 ATOM   C CG2 .  ILE A 1 409 ?  13.6    -15.934 -18.84  1.00 98.56 ?  409 ILE A CG2 1 
3142 ATOM   C CD1 .  ILE A 1 409 ?  12.567  -16.705 -21.731 1.00 98.56 ?  409 ILE A CD1 1 
3143 ATOM   N N   .  ALA A 1 410 ?  10.503  -15.557 -16.72  1.00 98.69 ?  410 ALA A N   1 
3144 ATOM   C CA  .  ALA A 1 410 ?  10.313  -14.602 -15.633 1.00 98.69 ?  410 ALA A CA  1 
3145 ATOM   C C   .  ALA A 1 410 ?  10.054  -15.299 -14.3   1.00 98.69 ?  410 ALA A C   1 
3146 ATOM   C CB  .  ALA A 1 410 ?  9.158   -13.666 -15.96  1.00 98.69 ?  410 ALA A CB  1 
3147 ATOM   O O   .  ALA A 1 410 ?  10.603  -14.906 -13.272 1.00 98.69 ?  410 ALA A O   1 
3148 ATOM   N N   .  ASN A 1 411 ?  9.213   -16.327 -14.305 1.00 98.69 ?  411 ASN A N   1 
3149 ATOM   C CA  .  ASN A 1 411 ?  8.924   -17.076 -13.087 1.00 98.69 ?  411 ASN A CA  1 
3150 ATOM   C C   .  ASN A 1 411 ?  10.15   -17.857 -12.623 1.00 98.69 ?  411 ASN A C   1 
3151 ATOM   C CB  .  ASN A 1 411 ?  7.736   -18.015 -13.308 1.00 98.69 ?  411 ASN A CB  1 
3152 ATOM   O O   .  ASN A 1 411 ?  10.378  -17.998 -11.422 1.00 98.69 ?  411 ASN A O   1 
3153 ATOM   C CG  .  ASN A 1 411 ?  6.418   -17.273 -13.361 1.00 98.69 ?  411 ASN A CG  1 
3154 ATOM   N ND2 .  ASN A 1 411 ?  5.568   -17.632 -14.309 1.00 98.69 ?  411 ASN A ND2 1 
3155 ATOM   O OD1 .  ASN A 1 411 ?  6.162   -16.388 -12.547 1.00 98.69 ?  411 ASN A OD1 1 
3156 ATOM   N N   .  LYS A 1 412 ?  10.945  -18.353 -13.566 1.00 98.75 ?  412 LYS A N   1 
3157 ATOM   C CA  .  LYS A 1 412 ?  12.204  -19.018 -13.237 1.00 98.75 ?  412 LYS A CA  1 
3158 ATOM   C C   .  LYS A 1 412 ?  13.205  -18.032 -12.644 1.00 98.75 ?  412 LYS A C   1 
3159 ATOM   C CB  .  LYS A 1 412 ?  12.789  -19.677 -14.489 1.00 98.75 ?  412 LYS A CB  1 
3160 ATOM   O O   .  LYS A 1 412 ?  13.927  -18.362 -11.706 1.00 98.75 ?  412 LYS A O   1 
3161 ATOM   C CG  .  LYS A 1 412 ?  14.004  -20.549 -14.21  1.00 98.75 ?  412 LYS A CG  1 
3162 ATOM   C CD  .  LYS A 1 412 ?  14.519  -21.187 -15.491 1.00 98.75 ?  412 LYS A CD  1 
3163 ATOM   C CE  .  LYS A 1 412 ?  15.682  -22.12  -15.199 1.00 98.75 ?  412 LYS A CE  1 
3164 ATOM   N NZ  .  LYS A 1 412 ?  16.165  -22.718 -16.486 1.00 98.75 ?  412 LYS A NZ  1 
3165 ATOM   N N   .  ALA A 1 413 ?  13.254  -16.827 -13.201 1.00 98.81 ?  413 ALA A N   1 
3166 ATOM   C CA  .  ALA A 1 413 ?  14.134  -15.778 -12.696 1.00 98.81 ?  413 ALA A CA  1 
3167 ATOM   C C   .  ALA A 1 413 ?  13.743  -15.381 -11.274 1.00 98.81 ?  413 ALA A C   1 
3168 ATOM   C CB  .  ALA A 1 413 ?  14.086  -14.567 -13.618 1.00 98.81 ?  413 ALA A CB  1 
3169 ATOM   O O   .  ALA A 1 413 ?  14.609  -15.168 -10.426 1.00 98.81 ?  413 ALA A O   1 
3170 ATOM   N N   .  LEU A 1 414 ?  12.443  -15.294 -11.015 1.00 98.75 ?  414 LEU A N   1 
3171 ATOM   C CA  .  LEU A 1 414 ?  11.927  -15.005 -9.679  1.00 98.75 ?  414 LEU A CA  1 
3172 ATOM   C C   .  LEU A 1 414 ?  12.258  -16.128 -8.699  1.00 98.75 ?  414 LEU A C   1 
3173 ATOM   C CB  .  LEU A 1 414 ?  10.412  -14.784 -9.736  1.00 98.75 ?  414 LEU A CB  1 
3174 ATOM   O O   .  LEU A 1 414 ?  12.606  -15.866 -7.549  1.00 98.75 ?  414 LEU A O   1 
3175 ATOM   C CG  .  LEU A 1 414 ?  9.914   -13.476 -10.362 1.00 98.75 ?  414 LEU A CG  1 
3176 ATOM   C CD1 .  LEU A 1 414 ?  8.431   -13.585 -10.695 1.00 98.75 ?  414 LEU A CD1 1 
3177 ATOM   C CD2 .  LEU A 1 414 ?  10.129  -12.286 -9.433  1.00 98.75 ?  414 LEU A CD2 1 
3178 ATOM   N N   .  GLU A 1 415 ?  12.141  -17.374 -9.143  1.00 98.50 ?  415 GLU A N   1 
3179 ATOM   C CA  .  GLU A 1 415 ?  12.454  -18.527 -8.303  1.00 98.50 ?  415 GLU A CA  1 
3180 ATOM   C C   .  GLU A 1 415 ?  13.936  -18.572 -7.936  1.00 98.50 ?  415 GLU A C   1 
3181 ATOM   C CB  .  GLU A 1 415 ?  12.063  -19.818 -9.029  1.00 98.50 ?  415 GLU A CB  1 
3182 ATOM   O O   .  GLU A 1 415 ?  14.294  -18.832 -6.788  1.00 98.50 ?  415 GLU A O   1 
3183 ATOM   C CG  .  GLU A 1 415 ?  12.198  -21.074 -8.181  1.00 98.50 ?  415 GLU A CG  1 
3184 ATOM   C CD  .  GLU A 1 415 ?  11.842  -22.339 -8.942  1.00 98.50 ?  415 GLU A CD  1 
3185 ATOM   O OE1 .  GLU A 1 415 ?  11.867  -23.424 -8.324  1.00 98.50 ?  415 GLU A OE1 1 
3186 ATOM   O OE2 .  GLU A 1 415 ?  11.546  -22.272 -10.155 1.00 98.50 ?  415 GLU A OE2 1 
3187 ATOM   N N   .  GLU A 1 416 ?  14.801  -18.329 -8.914  1.00 98.62 ?  416 GLU A N   1 
3188 ATOM   C CA  .  GLU A 1 416 ?  16.246  -18.34  -8.698  1.00 98.62 ?  416 GLU A CA  1 
3189 ATOM   C C   .  GLU A 1 416 ?  16.672  -17.186 -7.794  1.00 98.62 ?  416 GLU A C   1 
3190 ATOM   C CB  .  GLU A 1 416 ?  16.979  -18.247 -10.038 1.00 98.62 ?  416 GLU A CB  1 
3191 ATOM   O O   .  GLU A 1 416 ?  17.557  -17.336 -6.951  1.00 98.62 ?  416 GLU A O   1 
3192 ATOM   C CG  .  GLU A 1 416 ?  16.885  -19.516 -10.875 1.00 98.62 ?  416 GLU A CG  1 
3193 ATOM   C CD  .  GLU A 1 416 ?  17.515  -19.365 -12.248 1.00 98.62 ?  416 GLU A CD  1 
3194 ATOM   O OE1 .  GLU A 1 416 ?  17.437  -20.327 -13.042 1.00 98.62 ?  416 GLU A OE1 1 
3195 ATOM   O OE2 .  GLU A 1 416 ?  18.098  -18.304 -12.556 1.00 98.62 ?  416 GLU A OE2 1 
3196 ATOM   N N   .  ALA A 1 417 ?  16.031  -16.036 -7.965  1.00 98.75 ?  417 ALA A N   1 
3197 ATOM   C CA  .  ALA A 1 417 ?  16.294  -14.867 -7.133  1.00 98.75 ?  417 ALA A CA  1 
3198 ATOM   C C   .  ALA A 1 417 ?  15.798  -15.08  -5.705  1.00 98.75 ?  417 ALA A C   1 
3199 ATOM   C CB  .  ALA A 1 417 ?  15.634  -13.64  -7.744  1.00 98.75 ?  417 ALA A CB  1 
3200 ATOM   O O   .  ALA A 1 417 ?  16.396  -14.575 -4.755  1.00 98.75 ?  417 ALA A O   1 
3201 ATOM   N N   .  THR A 1 418 ?  14.715  -15.835 -5.551  1.00 97.62 ?  418 THR A N   1 
3202 ATOM   C CA  .  THR A 1 418 ?  14.192  -16.185 -4.233  1.00 97.62 ?  418 THR A CA  1 
3203 ATOM   C C   .  THR A 1 418 ?  15.157  -17.123 -3.518  1.00 97.62 ?  418 THR A C   1 
3204 ATOM   C CB  .  THR A 1 418 ?  12.813  -16.871 -4.325  1.00 97.62 ?  418 THR A CB  1 
3205 ATOM   O O   .  THR A 1 418 ?  15.435  -16.948 -2.332  1.00 97.62 ?  418 THR A O   1 
3206 ATOM   C CG2 .  THR A 1 418 ?  12.249  -17.16  -2.94   1.00 97.62 ?  418 THR A CG2 1 
3207 ATOM   O OG1 .  THR A 1 418 ?  11.897  -16.013 -5.016  1.00 97.62 ?  418 THR A OG1 1 
3208 ATOM   N N   .  LYS A 1 419 ?  15.677  -18.113 -4.236  1.00 97.69 ?  419 LYS A N   1 
3209 ATOM   C CA  .  LYS A 1 419 ?  16.642  -19.05  -3.665  1.00 97.69 ?  419 LYS A CA  1 
3210 ATOM   C C   .  LYS A 1 419 ?  17.933  -18.338 -3.278  1.00 97.69 ?  419 LYS A C   1 
3211 ATOM   C CB  .  LYS A 1 419 ?  16.923  -20.189 -4.649  1.00 97.69 ?  419 LYS A CB  1 
3212 ATOM   O O   .  LYS A 1 419 ?  18.513  -18.638 -2.236  1.00 97.69 ?  419 LYS A O   1 
3213 ATOM   C CG  .  LYS A 1 419 ?  15.737  -21.128 -4.827  1.00 97.69 ?  419 LYS A CG  1 
3214 ATOM   C CD  .  LYS A 1 419 ?  16.024  -22.228 -5.837  1.00 97.69 ?  419 LYS A CD  1 
3215 ATOM   C CE  .  LYS A 1 419 ?  14.786  -23.083 -6.053  1.00 97.69 ?  419 LYS A CE  1 
3216 ATOM   N NZ  .  LYS A 1 419 ?  15.096  -24.193 -7.013  1.00 97.69 ?  419 LYS A NZ  1 
3217 ATOM   N N   .  TYR A 1 420 ?  18.372  -17.396 -4.104  1.00 98.06 ?  420 TYR A N   1 
3218 ATOM   C CA  .  TYR A 1 420 ?  19.529  -16.566 -3.778  1.00 98.06 ?  420 TYR A CA  1 
3219 ATOM   C C   .  TYR A 1 420 ?  19.275  -15.737 -2.521  1.00 98.06 ?  420 TYR A C   1 
3220 ATOM   C CB  .  TYR A 1 420 ?  19.851  -15.627 -4.944  1.00 98.06 ?  420 TYR A CB  1 
3221 ATOM   O O   .  TYR A 1 420 ?  20.143  -15.625 -1.655  1.00 98.06 ?  420 TYR A O   1 
3222 ATOM   C CG  .  TYR A 1 420 ?  21.171  -14.902 -4.792  1.00 98.06 ?  420 TYR A CG  1 
3223 ATOM   C CD1 .  TYR A 1 420 ?  21.264  -13.739 -4.026  1.00 98.06 ?  420 TYR A CD1 1 
3224 ATOM   C CD2 .  TYR A 1 420 ?  22.321  -15.37  -5.428  1.00 98.06 ?  420 TYR A CD2 1 
3225 ATOM   C CE1 .  TYR A 1 420 ?  22.468  -13.046 -3.918  1.00 98.06 ?  420 TYR A CE1 1 
3226 ATOM   C CE2 .  TYR A 1 420 ?  23.524  -14.674 -5.334  1.00 98.06 ?  420 TYR A CE2 1 
3227 ATOM   O OH  .  TYR A 1 420 ?  24.764  -12.801 -4.521  1.00 98.06 ?  420 TYR A OH  1 
3228 ATOM   C CZ  .  TYR A 1 420 ?  23.587  -13.509 -4.588  1.00 98.06 ?  420 TYR A CZ  1 
3229 ATOM   N N   .  TYR A 1 421 ?  18.09   -15.144 -2.427  1.00 97.25 ?  421 TYR A N   1 
3230 ATOM   C CA  .  TYR A 1 421 ?  17.732  -14.336 -1.266  1.00 97.25 ?  421 TYR A CA  1 
3231 ATOM   C C   .  TYR A 1 421 ?  17.706  -15.169 0.012   1.00 97.25 ?  421 TYR A C   1 
3232 ATOM   C CB  .  TYR A 1 421 ?  16.375  -13.657 -1.468  1.00 97.25 ?  421 TYR A CB  1 
3233 ATOM   O O   .  TYR A 1 421 ?  18.244  -14.754 1.036   1.00 97.25 ?  421 TYR A O   1 
3234 ATOM   C CG  .  TYR A 1 421 ?  15.94   -12.883 -0.243  1.00 97.25 ?  421 TYR A CG  1 
3235 ATOM   C CD1 .  TYR A 1 421 ?  15.025  -13.432 0.656   1.00 97.25 ?  421 TYR A CD1 1 
3236 ATOM   C CD2 .  TYR A 1 421 ?  16.501  -11.64  0.057   1.00 97.25 ?  421 TYR A CD2 1 
3237 ATOM   C CE1 .  TYR A 1 421 ?  14.759  -12.809 1.872   1.00 97.25 ?  421 TYR A CE1 1 
3238 ATOM   C CE2 .  TYR A 1 421 ?  16.244  -11.018 1.276   1.00 97.25 ?  421 TYR A CE2 1 
3239 ATOM   O OH  .  TYR A 1 421 ?  15.245  -11.078 3.442   1.00 97.25 ?  421 TYR A OH  1 
3240 ATOM   C CZ  .  TYR A 1 421 ?  15.41   -11.632 2.194   1.00 97.25 ?  421 TYR A CZ  1 
3241 ATOM   N N   .  GLU A 1 422 ?  17.071  -16.334 -0.042  1.00 95.19 ?  422 GLU A N   1 
3242 ATOM   C CA  .  GLU A 1 422 ?  16.953  -17.206 1.123   1.00 95.19 ?  422 GLU A CA  1 
3243 ATOM   C C   .  GLU A 1 422 ?  18.297  -17.77  1.578   1.00 95.19 ?  422 GLU A C   1 
3244 ATOM   C CB  .  GLU A 1 422 ?  15.994  -18.359 0.812   1.00 95.19 ?  422 GLU A CB  1 
3245 ATOM   O O   .  GLU A 1 422 ?  18.546  -17.889 2.778   1.00 95.19 ?  422 GLU A O   1 
3246 ATOM   C CG  .  GLU A 1 422 ?  14.538  -17.928 0.687   1.00 95.19 ?  422 GLU A CG  1 
3247 ATOM   C CD  .  GLU A 1 422 ?  13.622  -19.065 0.273   1.00 95.19 ?  422 GLU A CD  1 
3248 ATOM   O OE1 .  GLU A 1 422 ?  12.397  -18.832 0.188   1.00 95.19 ?  422 GLU A OE1 1 
3249 ATOM   O OE2 .  GLU A 1 422 ?  14.105  -20.19  0.019   1.00 95.19 ?  422 GLU A OE2 1 
3250 ATOM   N N   .  SER A 1 423 ?  19.161  -18.128 0.635   1.00 96.88 ?  423 SER A N   1 
3251 ATOM   C CA  .  SER A 1 423 ?  20.446  -18.742 0.962   1.00 96.88 ?  423 SER A CA  1 
3252 ATOM   C C   .  SER A 1 423 ?  21.43   -17.777 1.619   1.00 96.88 ?  423 SER A C   1 
3253 ATOM   C CB  .  SER A 1 423 ?  21.083  -19.339 -0.295  1.00 96.88 ?  423 SER A CB  1 
3254 ATOM   O O   .  SER A 1 423 ?  22.281  -18.195 2.403   1.00 96.88 ?  423 SER A O   1 
3255 ATOM   O OG  .  SER A 1 423 ?  21.424  -18.33  -1.23   1.00 96.88 ?  423 SER A OG  1 
3256 ATOM   N N   .  LYS A 1 424 ?  21.31   -16.49  1.31    1.00 96.69 ?  424 LYS A N   1 
3257 ATOM   C CA  .  LYS A 1 424 ?  22.165  -15.457 1.893   1.00 96.69 ?  424 LYS A CA  1 
3258 ATOM   C C   .  LYS A 1 424 ?  21.331  -14.445 2.67    1.00 96.69 ?  424 LYS A C   1 
3259 ATOM   C CB  .  LYS A 1 424 ?  22.954  -14.739 0.795   1.00 96.69 ?  424 LYS A CB  1 
3260 ATOM   O O   .  LYS A 1 424 ?  21.655  -13.258 2.72    1.00 96.69 ?  424 LYS A O   1 
3261 ATOM   C CG  .  LYS A 1 424 ?  23.891  -15.637 0.002   1.00 96.69 ?  424 LYS A CG  1 
3262 ATOM   C CD  .  LYS A 1 424 ?  24.729  -14.816 -0.966  1.00 96.69 ?  424 LYS A CD  1 
3263 ATOM   C CE  .  LYS A 1 424 ?  25.619  -15.708 -1.815  1.00 96.69 ?  424 LYS A CE  1 
3264 ATOM   N NZ  .  LYS A 1 424 ?  26.508  -14.847 -2.662  1.00 96.69 ?  424 LYS A NZ  1 
3265 ATOM   N N   .  LYS A 1 425 ?  20.243  -14.918 3.269   1.00 93.31 ?  425 LYS A N   1 
3266 ATOM   C CA  .  LYS A 1 425 ?  19.248  -14.036 3.872   1.00 93.31 ?  425 LYS A CA  1 
3267 ATOM   C C   .  LYS A 1 425 ?  19.821  -13.076 4.908   1.00 93.31 ?  425 LYS A C   1 
3268 ATOM   C CB  .  LYS A 1 425 ?  18.105  -14.862 4.467   1.00 93.31 ?  425 LYS A CB  1 
3269 ATOM   O O   .  LYS A 1 425 ?  19.543  -11.88  4.854   1.00 93.31 ?  425 LYS A O   1 
3270 ATOM   C CG  .  LYS A 1 425 ?  16.888  -14.024 4.826   1.00 93.31 ?  425 LYS A CG  1 
3271 ATOM   C CD  .  LYS A 1 425 ?  15.752  -14.873 5.375   1.00 93.31 ?  425 LYS A CD  1 
3272 ATOM   C CE  .  LYS A 1 425 ?  14.525  -14.01  5.622   1.00 93.31 ?  425 LYS A CE  1 
3273 ATOM   N NZ  .  LYS A 1 425 ?  13.41   -14.843 6.179   1.00 93.31 ?  425 LYS A NZ  1 
3274 ATOM   N N   .  ALA A 1 426 ?  20.621  -13.585 5.837   1.00 94.06 ?  426 ALA A N   1 
3275 ATOM   C CA  .  ALA A 1 426 ?  21.182  -12.751 6.897   1.00 94.06 ?  426 ALA A CA  1 
3276 ATOM   C C   .  ALA A 1 426 ?  22.114  -11.674 6.345   1.00 94.06 ?  426 ALA A C   1 
3277 ATOM   C CB  .  ALA A 1 426 ?  21.923  -13.619 7.905   1.00 94.06 ?  426 ALA A CB  1 
3278 ATOM   O O   .  ALA A 1 426 ?  22.082  -10.528 6.792   1.00 94.06 ?  426 ALA A O   1 
3279 ATOM   N N   .  GLU A 1 427 ?  22.945  -12.04  5.376   1.00 96.75 ?  427 GLU A N   1 
3280 ATOM   C CA  .  GLU A 1 427 ?  23.878  -11.103 4.755   1.00 96.75 ?  427 GLU A CA  1 
3281 ATOM   C C   .  GLU A 1 427 ?  23.127  -9.994  4.024   1.00 96.75 ?  427 GLU A C   1 
3282 ATOM   C CB  .  GLU A 1 427 ?  24.773  -11.85  3.761   1.00 96.75 ?  427 GLU A CB  1 
3283 ATOM   O O   .  GLU A 1 427 ?  23.484  -8.819  4.107   1.00 96.75 ?  427 GLU A O   1 
3284 ATOM   C CG  .  GLU A 1 427 ?  25.874  -10.999 3.145   1.00 96.75 ?  427 GLU A CG  1 
3285 ATOM   C CD  .  GLU A 1 427 ?  26.684  -11.757 2.107   1.00 96.75 ?  427 GLU A CD  1 
3286 ATOM   O OE1 .  GLU A 1 427 ?  27.643  -11.175 1.559   1.00 96.75 ?  427 GLU A OE1 1 
3287 ATOM   O OE2 .  GLU A 1 427 ?  26.368  -12.932 1.82    1.00 96.75 ?  427 GLU A OE2 1 
3288 ATOM   N N   .  ILE A 1 428 ?  22.086  -10.381 3.295   1.00 97.19 ?  428 ILE A N   1 
3289 ATOM   C CA  .  ILE A 1 428 ?  21.3    -9.437  2.508   1.00 97.19 ?  428 ILE A CA  1 
3290 ATOM   C C   .  ILE A 1 428 ?  20.492  -8.539  3.439   1.00 97.19 ?  428 ILE A C   1 
3291 ATOM   C CB  .  ILE A 1 428 ?  20.383  -10.163 1.498   1.00 97.19 ?  428 ILE A CB  1 
3292 ATOM   O O   .  ILE A 1 428 ?  20.469  -7.325  3.25    1.00 97.19 ?  428 ILE A O   1 
3293 ATOM   C CG1 .  ILE A 1 428 ?  21.234  -10.923 0.473   1.00 97.19 ?  428 ILE A CG1 1 
3294 ATOM   C CG2 .  ILE A 1 428 ?  19.483  -9.159  0.782   1.00 97.19 ?  428 ILE A CG2 1 
3295 ATOM   C CD1 .  ILE A 1 428 ?  20.492  -12.009 -0.274  1.00 97.19 ?  428 ILE A CD1 1 
3296 ATOM   N N   .  GLN A 1 429 ?  19.85   -9.102  4.457   1.00 94.94 ?  429 GLN A N   1 
3297 ATOM   C CA  .  GLN A 1 429 ?  19.098  -8.296  5.416   1.00 94.94 ?  429 GLN A CA  1 
3298 ATOM   C C   .  GLN A 1 429 ?  19.996  -7.26   6.087   1.00 94.94 ?  429 GLN A C   1 
3299 ATOM   C CB  .  GLN A 1 429 ?  18.449  -9.183  6.482   1.00 94.94 ?  429 GLN A CB  1 
3300 ATOM   O O   .  GLN A 1 429 ?  19.573  -6.124  6.305   1.00 94.94 ?  429 GLN A O   1 
3301 ATOM   C CG  .  GLN A 1 429 ?  17.271  -10.009 5.98    1.00 94.94 ?  429 GLN A CG  1 
3302 ATOM   C CD  .  GLN A 1 429 ?  16.761  -10.971 7.034   1.00 94.94 ?  429 GLN A CD  1 
3303 ATOM   N NE2 .  GLN A 1 429 ?  15.461  -10.946 7.285   1.00 94.94 ?  429 GLN A NE2 1 
3304 ATOM   O OE1 .  GLN A 1 429 ?  17.525  -11.739 7.613   1.00 94.94 ?  429 GLN A OE1 1 
3305 ATOM   N N   .  LYS A 1 430 ?  21.231  -7.64   6.402   1.00 95.56 ?  430 LYS A N   1 
3306 ATOM   C CA  .  LYS A 1 430 ?  22.201  -6.711  6.975   1.00 95.56 ?  430 LYS A CA  1 
3307 ATOM   C C   .  LYS A 1 430 ?  22.542  -5.603  5.984   1.00 95.56 ?  430 LYS A C   1 
3308 ATOM   C CB  .  LYS A 1 430 ?  23.476  -7.458  7.378   1.00 95.56 ?  430 LYS A CB  1 
3309 ATOM   O O   .  LYS A 1 430 ?  22.584  -4.43   6.35    1.00 95.56 ?  430 LYS A O   1 
3310 ATOM   C CG  .  LYS A 1 430 ?  24.5    -6.584  8.089   1.00 95.56 ?  430 LYS A CG  1 
3311 ATOM   C CD  .  LYS A 1 430 ?  25.779  -7.354  8.38    1.00 95.56 ?  430 LYS A CD  1 
3312 ATOM   C CE  .  LYS A 1 430 ?  26.781  -6.479  9.116   1.00 95.56 ?  430 LYS A CE  1 
3313 ATOM   N NZ  .  LYS A 1 430 ?  28.056  -7.243  9.313   1.00 95.56 ?  430 LYS A NZ  1 
3314 ATOM   N N   .  THR A 1 431 ?  22.794  -5.984  4.737   1.00 95.81 ?  431 THR A N   1 
3315 ATOM   C CA  .  THR A 1 431 ?  23.142  -5.027  3.69    1.00 95.81 ?  431 THR A CA  1 
3316 ATOM   C C   .  THR A 1 431 ?  22.002  -4.04   3.458   1.00 95.81 ?  431 THR A C   1 
3317 ATOM   C CB  .  THR A 1 431 ?  23.462  -5.738  2.358   1.00 95.81 ?  431 THR A CB  1 
3318 ATOM   O O   .  THR A 1 431 ?  22.232  -2.84   3.325   1.00 95.81 ?  431 THR A O   1 
3319 ATOM   C CG2 .  THR A 1 431 ?  23.968  -4.753  1.311   1.00 95.81 ?  431 THR A CG2 1 
3320 ATOM   O OG1 .  THR A 1 431 ?  24.471  -6.731  2.579   1.00 95.81 ?  431 THR A OG1 1 
3321 ATOM   N N   .  LEU A 1 432 ?  20.775  -4.549  3.421   1.00 96.00 ?  432 LEU A N   1 
3322 ATOM   C CA  .  LEU A 1 432 ?  19.592  -3.736  3.15    1.00 96.00 ?  432 LEU A CA  1 
3323 ATOM   C C   .  LEU A 1 432 ?  19.325  -2.706  4.244   1.00 96.00 ?  432 LEU A C   1 
3324 ATOM   C CB  .  LEU A 1 432 ?  18.363  -4.641  3.019   1.00 96.00 ?  432 LEU A CB  1 
3325 ATOM   O O   .  LEU A 1 432 ?  18.836  -1.61   3.974   1.00 96.00 ?  432 LEU A O   1 
3326 ATOM   C CG  .  LEU A 1 432 ?  18.276  -5.596  1.824   1.00 96.00 ?  432 LEU A CG  1 
3327 ATOM   C CD1 .  LEU A 1 432 ?  17.093  -6.537  2.03    1.00 96.00 ?  432 LEU A CD1 1 
3328 ATOM   C CD2 .  LEU A 1 432 ?  18.124  -4.854  0.509   1.00 96.00 ?  432 LEU A CD2 1 
3329 ATOM   N N   .  SER A 1 433 ?  19.617  -3.07   5.488   1.00 93.31 ?  433 SER A N   1 
3330 ATOM   C CA  .  SER A 1 433 ?  19.329  -2.204  6.627   1.00 93.31 ?  433 SER A CA  1 
3331 ATOM   C C   .  SER A 1 433 ?  20.254  -0.995  6.732   1.00 93.31 ?  433 SER A C   1 
3332 ATOM   C CB  .  SER A 1 433 ?  19.418  -3.017  7.921   1.00 93.31 ?  433 SER A CB  1 
3333 ATOM   O O   .  SER A 1 433 ?  19.892  0.009   7.344   1.00 93.31 ?  433 SER A O   1 
3334 ATOM   O OG  .  SER A 1 433 ?  20.749  -3.436  8.168   1.00 93.31 ?  433 SER A OG  1 
3335 ATOM   N N   .  GLY A 1 434 ?  21.449  -1.091  6.156   1.00 94.44 ?  434 GLY A N   1 
3336 ATOM   C CA  .  GLY A 1 434 ?  22.46   -0.062  6.328   1.00 94.44 ?  434 GLY A CA  1 
3337 ATOM   C C   .  GLY A 1 434 ?  22.646  0.912   5.181   1.00 94.44 ?  434 GLY A C   1 
3338 ATOM   O O   .  GLY A 1 434 ?  23.562  1.732   5.218   1.00 94.44 ?  434 GLY A O   1 
3339 ATOM   N N   .  GLN A 1 435 ?  21.805  0.831   4.156   1.00 94.44 ?  435 GLN A N   1 
3340 ATOM   C CA  .  GLN A 1 435 ?  22      1.612   2.936   1.00 94.44 ?  435 GLN A CA  1 
3341 ATOM   C C   .  GLN A 1 435 ?  21.842  3.12    3.104   1.00 94.44 ?  435 GLN A C   1 
3342 ATOM   C CB  .  GLN A 1 435 ?  21.047  1.116   1.847   1.00 94.44 ?  435 GLN A CB  1 
3343 ATOM   O O   .  GLN A 1 435 ?  22.381  3.889   2.308   1.00 94.44 ?  435 GLN A O   1 
3344 ATOM   C CG  .  GLN A 1 435 ?  21.435  -0.253  1.312   1.00 94.44 ?  435 GLN A CG  1 
3345 ATOM   C CD  .  GLN A 1 435 ?  20.361  -0.847  0.429   1.00 94.44 ?  435 GLN A CD  1 
3346 ATOM   N NE2 .  GLN A 1 435 ?  20.626  -0.925  -0.864  1.00 94.44 ?  435 GLN A NE2 1 
3347 ATOM   O OE1 .  GLN A 1 435 ?  19.302  -1.242  0.907   1.00 94.44 ?  435 GLN A OE1 1 
3348 ATOM   N N   .  LEU A 1 436 ?  21.125  3.551   4.135   1.00 93.00 ?  436 LEU A N   1 
3349 ATOM   C CA  .  LEU A 1 436 ?  21.008  4.976   4.429   1.00 93.00 ?  436 LEU A CA  1 
3350 ATOM   C C   .  LEU A 1 436 ?  22.37   5.541   4.828   1.00 93.00 ?  436 LEU A C   1 
3351 ATOM   C CB  .  LEU A 1 436 ?  19.994  5.198   5.556   1.00 93.00 ?  436 LEU A CB  1 
3352 ATOM   O O   .  LEU A 1 436 ?  22.724  6.663   4.469   1.00 93.00 ?  436 LEU A O   1 
3353 ATOM   C CG  .  LEU A 1 436 ?  19.565  6.649   5.794   1.00 93.00 ?  436 LEU A CG  1 
3354 ATOM   C CD1 .  LEU A 1 436 ?  18.648  7.143   4.68    1.00 93.00 ?  436 LEU A CD1 1 
3355 ATOM   C CD2 .  LEU A 1 436 ?  18.842  6.757   7.13    1.00 93.00 ?  436 LEU A CD2 1 
3356 ATOM   N N   .  GLU A 1 437 ?  23.137  4.748   5.568   1.00 94.56 ?  437 GLU A N   1 
3357 ATOM   C CA  .  GLU A 1 437 ?  24.466  5.146   6.023   1.00 94.56 ?  437 GLU A CA  1 
3358 ATOM   C C   .  GLU A 1 437 ?  25.528  4.913   4.951   1.00 94.56 ?  437 GLU A C   1 
3359 ATOM   C CB  .  GLU A 1 437 ?  24.849  4.384   7.295   1.00 94.56 ?  437 GLU A CB  1 
3360 ATOM   O O   .  GLU A 1 437 ?  26.515  5.644   4.881   1.00 94.56 ?  437 GLU A O   1 
3361 ATOM   C CG  .  GLU A 1 437 ?  23.947  4.667   8.489   1.00 94.56 ?  437 GLU A CG  1 
3362 ATOM   C CD  .  GLU A 1 437 ?  23.898  6.143   8.839   1.00 94.56 ?  437 GLU A CD  1 
3363 ATOM   O OE1 .  GLU A 1 437 ?  22.786  6.693   8.992   1.00 94.56 ?  437 GLU A OE1 1 
3364 ATOM   O OE2 .  GLU A 1 437 ?  24.972  6.771   8.954   1.00 94.56 ?  437 GLU A OE2 1 
3365 ATOM   N N   .  GLU A 1 438 ?  25.329  3.908   4.106   1.00 95.62 ?  438 GLU A N   1 
3366 ATOM   C CA  .  GLU A 1 438 ?  26.212  3.679   2.965   1.00 95.62 ?  438 GLU A CA  1 
3367 ATOM   C C   .  GLU A 1 438 ?  26.096  4.839   1.981   1.00 95.62 ?  438 GLU A C   1 
3368 ATOM   C CB  .  GLU A 1 438 ?  25.871  2.367   2.252   1.00 95.62 ?  438 GLU A CB  1 
3369 ATOM   O O   .  GLU A 1 438 ?  27.101  5.317   1.455   1.00 95.62 ?  438 GLU A O   1 
3370 ATOM   C CG  .  GLU A 1 438 ?  26.181  1.118   3.067   1.00 95.62 ?  438 GLU A CG  1 
3371 ATOM   C CD  .  GLU A 1 438 ?  25.771  -0.161  2.36    1.00 95.62 ?  438 GLU A CD  1 
3372 ATOM   O OE1 .  GLU A 1 438 ?  26.012  -1.251  2.921   1.00 95.62 ?  438 GLU A OE1 1 
3373 ATOM   O OE2 .  GLU A 1 438 ?  25.217  -0.096  1.242   1.00 95.62 ?  438 GLU A OE2 1 
3374 ATOM   N N   .  ALA A 1 439 ?  24.873  5.305   1.747   1.00 96.00 ?  439 ALA A N   1 
3375 ATOM   C CA  .  ALA A 1 439 ?  24.64   6.459   0.885   1.00 96.00 ?  439 ALA A CA  1 
3376 ATOM   C C   .  ALA A 1 439 ?  25.239  7.714   1.514   1.00 96.00 ?  439 ALA A C   1 
3377 ATOM   C CB  .  ALA A 1 439 ?  23.148  6.649   0.65    1.00 96.00 ?  439 ALA A CB  1 
3378 ATOM   O O   .  ALA A 1 439 ?  25.808  8.555   0.819   1.00 96.00 ?  439 ALA A O   1 
3379 ATOM   N N   .  LYS A 1 440 ?  25.126  7.829   2.833   1.00 96.38 ?  440 LYS A N   1 
3380 ATOM   C CA  .  LYS A 1 440 ?  25.72   8.938   3.575   1.00 96.38 ?  440 LYS A CA  1 
3381 ATOM   C C   .  LYS A 1 440 ?  27.237  8.939   3.435   1.00 96.38 ?  440 LYS A C   1 
3382 ATOM   C CB  .  LYS A 1 440 ?  25.319  8.836   5.049   1.00 96.38 ?  440 LYS A CB  1 
3383 ATOM   O O   .  LYS A 1 440 ?  27.849  9.988   3.236   1.00 96.38 ?  440 LYS A O   1 
3384 ATOM   C CG  .  LYS A 1 440 ?  25.787  9.994   5.915   1.00 96.38 ?  440 LYS A CG  1 
3385 ATOM   C CD  .  LYS A 1 440 ?  25.252  9.844   7.331   1.00 96.38 ?  440 LYS A CD  1 
3386 ATOM   C CE  .  LYS A 1 440 ?  25.621  11.041  8.191   1.00 96.38 ?  440 LYS A CE  1 
3387 ATOM   N NZ  .  LYS A 1 440 ?  25.073  10.823  9.569   1.00 96.38 ?  440 LYS A NZ  1 
3388 ATOM   N N   .  LYS A 1 441 ?  27.839  7.76    3.546   1.00 96.81 ?  441 LYS A N   1 
3389 ATOM   C CA  .  LYS A 1 441 ?  29.286  7.604   3.424   1.00 96.81 ?  441 LYS A CA  1 
3390 ATOM   C C   .  LYS A 1 441 ?  29.767  7.906   2.01    1.00 96.81 ?  441 LYS A C   1 
3391 ATOM   C CB  .  LYS A 1 441 ?  29.677  6.177   3.82    1.00 96.81 ?  441 LYS A CB  1 
3392 ATOM   O O   .  LYS A 1 441 ?  30.795  8.555   1.826   1.00 96.81 ?  441 LYS A O   1 
3393 ATOM   C CG  .  LYS A 1 441 ?  31.177  5.946   3.912   1.00 96.81 ?  441 LYS A CG  1 
3394 ATOM   C CD  .  LYS A 1 441 ?  31.48   4.498   4.265   1.00 96.81 ?  441 LYS A CD  1 
3395 ATOM   C CE  .  LYS A 1 441 ?  32.974  4.277   4.425   1.00 96.81 ?  441 LYS A CE  1 
3396 ATOM   N NZ  .  LYS A 1 441 ?  33.219  2.831   4.738   1.00 96.81 ?  441 LYS A NZ  1 
3397 ATOM   N N   .  ALA A 1 442 ?  29.033  7.413   1.019   1.00 96.12 ?  442 ALA A N   1 
3398 ATOM   C CA  .  ALA A 1 442 ?  29.407  7.582   -0.382  1.00 96.12 ?  442 ALA A CA  1 
3399 ATOM   C C   .  ALA A 1 442 ?  29.19   9.002   -0.897  1.00 96.12 ?  442 ALA A C   1 
3400 ATOM   C CB  .  ALA A 1 442 ?  28.625  6.598   -1.239  1.00 96.12 ?  442 ALA A CB  1 
3401 ATOM   O O   .  ALA A 1 442 ?  29.972  9.495   -1.71   1.00 96.12 ?  442 ALA A O   1 
3402 ATOM   N N   .  LEU A 1 443 ?  28.125  9.658   -0.447  1.00 95.56 ?  443 LEU A N   1 
3403 ATOM   C CA  .  LEU A 1 443 ?  27.816  11.015  -0.887  1.00 95.56 ?  443 LEU A CA  1 
3404 ATOM   C C   .  LEU A 1 443 ?  28.585  12.069  -0.096  1.00 95.56 ?  443 LEU A C   1 
3405 ATOM   C CB  .  LEU A 1 443 ?  26.308  11.272  -0.793  1.00 95.56 ?  443 LEU A CB  1 
3406 ATOM   O O   .  LEU A 1 443 ?  28.881  13.143  -0.621  1.00 95.56 ?  443 LEU A O   1 
3407 ATOM   C CG  .  LEU A 1 443 ?  25.42   10.513  -1.785  1.00 95.56 ?  443 LEU A CG  1 
3408 ATOM   C CD1 .  LEU A 1 443 ?  23.955  10.712  -1.419  1.00 95.56 ?  443 LEU A CD1 1 
3409 ATOM   C CD2 .  LEU A 1 443 ?  25.648  10.987  -3.218  1.00 95.56 ?  443 LEU A CD2 1 
3410 ATOM   N N   .  GLY A 1 444 ?  28.923  11.771  1.154   1.00 96.12 ?  444 GLY A N   1 
3411 ATOM   C CA  .  GLY A 1 444 ?  29.771  12.664  1.924   1.00 96.12 ?  444 GLY A CA  1 
3412 ATOM   C C   .  GLY A 1 444 ?  29.099  13.989  2.228   1.00 96.12 ?  444 GLY A C   1 
3413 ATOM   O O   .  GLY A 1 444 ?  27.993  14.035  2.765   1.00 96.12 ?  444 GLY A O   1 
3414 ATOM   N N   .  THR A 1 445 ?  29.761  15.079  1.856   1.00 94.06 ?  445 THR A N   1 
3415 ATOM   C CA  .  THR A 1 445 ?  29.236  16.427  2.071   1.00 94.06 ?  445 THR A CA  1 
3416 ATOM   C C   .  THR A 1 445 ?  28.007  16.737  1.221   1.00 94.06 ?  445 THR A C   1 
3417 ATOM   C CB  .  THR A 1 445 ?  30.291  17.503  1.742   1.00 94.06 ?  445 THR A CB  1 
3418 ATOM   O O   .  THR A 1 445 ?  27.353  17.759  1.425   1.00 94.06 ?  445 THR A O   1 
3419 ATOM   C CG2 .  THR A 1 445 ?  31.51   17.386  2.651   1.00 94.06 ?  445 THR A CG2 1 
3420 ATOM   O OG1 .  THR A 1 445 ?  30.719  17.346  0.384   1.00 94.06 ?  445 THR A OG1 1 
3421 ATOM   N N   .  LYS A 1 446 ?  27.679  15.855  0.282   1.00 93.06 ?  446 LYS A N   1 
3422 ATOM   C CA  .  LYS A 1 446 ?  26.475  15.994  -0.535  1.00 93.06 ?  446 LYS A CA  1 
3423 ATOM   C C   .  LYS A 1 446 ?  25.245  15.434  0.175   1.00 93.06 ?  446 LYS A C   1 
3424 ATOM   C CB  .  LYS A 1 446 ?  26.669  15.29   -1.881  1.00 93.06 ?  446 LYS A CB  1 
3425 ATOM   O O   .  LYS A 1 446 ?  24.129  15.527  -0.336  1.00 93.06 ?  446 LYS A O   1 
3426 ATOM   C CG  .  LYS A 1 446 ?  27.826  15.835  -2.708  1.00 93.06 ?  446 LYS A CG  1 
3427 ATOM   C CD  .  LYS A 1 446 ?  27.991  15.063  -4.009  1.00 93.06 ?  446 LYS A CD  1 
3428 ATOM   C CE  .  LYS A 1 446 ?  29.193  15.566  -4.792  1.00 93.06 ?  446 LYS A CE  1 
3429 ATOM   N NZ  .  LYS A 1 446 ?  29.319  14.786  -6.067  1.00 93.06 ?  446 LYS A NZ  1 
3430 ATOM   N N   .  TRP A 1 447 ?  25.453  14.842  1.346   1.00 94.75 ?  447 TRP A N   1 
3431 ATOM   C CA  .  TRP A 1 447 ?  24.362  14.325  2.166   1.00 94.75 ?  447 TRP A CA  1 
3432 ATOM   C C   .  TRP A 1 447 ?  23.595  15.466  2.833   1.00 94.75 ?  447 TRP A C   1 
3433 ATOM   C CB  .  TRP A 1 447 ?  24.921  13.394  3.243   1.00 94.75 ?  447 TRP A CB  1 
3434 ATOM   O O   .  TRP A 1 447 ?  24.204  16.335  3.457   1.00 94.75 ?  447 TRP A O   1 
3435 ATOM   C CG  .  TRP A 1 447 ?  23.858  12.626  3.968   1.00 94.75 ?  447 TRP A CG  1 
3436 ATOM   C CD1 .  TRP A 1 447 ?  23.432  12.806  5.25    1.00 94.75 ?  447 TRP A CD1 1 
3437 ATOM   C CD2 .  TRP A 1 447 ?  23.075  11.537  3.458   1.00 94.75 ?  447 TRP A CD2 1 
3438 ATOM   C CE2 .  TRP A 1 447 ?  22.303  11.031  4.529   1.00 94.75 ?  447 TRP A CE2 1 
3439 ATOM   C CE3 .  TRP A 1 447 ?  22.941  10.946  2.195   1.00 94.75 ?  447 TRP A CE3 1 
3440 ATOM   N NE1 .  TRP A 1 447 ?  22.512  11.853  5.604   1.00 94.75 ?  447 TRP A NE1 1 
3441 ATOM   C CH2 .  TRP A 1 447 ?  21.367  9.347   3.138   1.00 94.75 ?  447 TRP A CH2 1 
3442 ATOM   C CZ2 .  TRP A 1 447 ?  21.467  9.92    4.381   1.00 94.75 ?  447 TRP A CZ2 1 
3443 ATOM   C CZ3 .  TRP A 1 447 ?  22.078  9.864   2.039   1.00 94.75 ?  447 TRP A CZ3 1 
3444 ATOM   N N   .  PRO A 1 448 ?  22.258  15.496  2.705   1.00 91.88 ?  448 PRO A N   1 
3445 ATOM   C CA  .  PRO A 1 448 ?  21.536  16.609  3.33    1.00 91.88 ?  448 PRO A CA  1 
3446 ATOM   C C   .  PRO A 1 448 ?  21.282  16.42   4.823   1.00 91.88 ?  448 PRO A C   1 
3447 ATOM   C CB  .  PRO A 1 448 ?  20.218  16.628  2.555   1.00 91.88 ?  448 PRO A CB  1 
3448 ATOM   O O   .  PRO A 1 448 ?  21.233  15.3    5.33    1.00 91.88 ?  448 PRO A O   1 
3449 ATOM   C CG  .  PRO A 1 448 ?  19.976  15.196  2.244   1.00 91.88 ?  448 PRO A CG  1 
3450 ATOM   C CD  .  PRO A 1 448 ?  21.332  14.586  2.007   1.00 91.88 ?  448 PRO A CD  1 
3451 ATOM   N N   .  ASP A 1 449 ?  21.106  17.531  5.529   1.00 87.44 ?  449 ASP A N   1 
3452 ATOM   C CA  .  ASP A 1 449 ?  20.814  17.497  6.96    1.00 87.44 ?  449 ASP A CA  1 
3453 ATOM   C C   .  ASP A 1 449 ?  19.347  17.179  7.246   1.00 87.44 ?  449 ASP A C   1 
3454 ATOM   C CB  .  ASP A 1 449 ?  21.164  18.849  7.585   1.00 87.44 ?  449 ASP A CB  1 
3455 ATOM   O O   .  ASP A 1 449 ?  18.987  16.818  8.366   1.00 87.44 ?  449 ASP A O   1 
3456 ATOM   C CG  .  ASP A 1 449 ?  22.658  19.114  7.594   1.00 87.44 ?  449 ASP A CG  1 
3457 ATOM   O OD1 .  ASP A 1 449 ?  23.42   18.252  8.081   1.00 87.44 ?  449 ASP A OD1 1 
3458 ATOM   O OD2 .  ASP A 1 449 ?  23.07   20.195  7.121   1.00 87.44 ?  449 ASP A OD2 1 
3459 ATOM   N N   .  GLN A 1 450 ?  18.5    17.325  6.233   1.00 83.25 ?  450 GLN A N   1 
3460 ATOM   C CA  .  GLN A 1 450 ?  17.06   17.141  6.386   1.00 83.25 ?  450 GLN A CA  1 
3461 ATOM   C C   .  GLN A 1 450 ?  16.657  15.699  6.084   1.00 83.25 ?  450 GLN A C   1 
3462 ATOM   C CB  .  GLN A 1 450 ?  16.307  18.084  5.443   1.00 83.25 ?  450 GLN A CB  1 
3463 ATOM   O O   .  GLN A 1 450 ?  16.837  15.243  4.955   1.00 83.25 ?  450 GLN A O   1 
3464 ATOM   C CG  .  GLN A 1 450 ?  16.582  19.561  5.695   1.00 83.25 ?  450 GLN A CG  1 
3465 ATOM   C CD  .  GLN A 1 450 ?  16.265  19.971  7.119   1.00 83.25 ?  450 GLN A CD  1 
3466 ATOM   N NE2 .  GLN A 1 450 ?  17.216  20.616  7.778   1.00 83.25 ?  450 GLN A NE2 1 
3467 ATOM   O OE1 .  GLN A 1 450 ?  15.179  19.704  7.629   1.00 83.25 ?  450 GLN A OE1 1 
3468 ATOM   N N   .  PRO A 1 451 ?  16.101  14.962  7.062   1.00 79.25 ?  451 PRO A N   1 
3469 ATOM   C CA  .  PRO A 1 451 ?  15.772  13.558  6.788   1.00 79.25 ?  451 PRO A CA  1 
3470 ATOM   C C   .  PRO A 1 451 ?  14.848  13.311  5.598   1.00 79.25 ?  451 PRO A C   1 
3471 ATOM   C CB  .  PRO A 1 451 ?  15.1    13.091  8.082   1.00 79.25 ?  451 PRO A CB  1 
3472 ATOM   O O   .  PRO A 1 451 ?  14.954  12.281  4.935   1.00 79.25 ?  451 PRO A O   1 
3473 ATOM   C CG  .  PRO A 1 451 ?  15.633  13.998  9.131   1.00 79.25 ?  451 PRO A CG  1 
3474 ATOM   C CD  .  PRO A 1 451 ?  15.763  15.328  8.45    1.00 79.25 ?  451 PRO A CD  1 
3475 ATOM   N N   .  ALA A 1 452 ?  13.951  14.25   5.317   1.00 74.00 ?  452 ALA A N   1 
3476 ATOM   C CA  .  ALA A 1 452 ?  13.035  14.124  4.186   1.00 74.00 ?  452 ALA A CA  1 
3477 ATOM   C C   .  ALA A 1 452 ?  13.776  14.034  2.854   1.00 74.00 ?  452 ALA A C   1 
3478 ATOM   C CB  .  ALA A 1 452 ?  12.073  15.305  4.17    1.00 74.00 ?  452 ALA A CB  1 
3479 ATOM   O O   .  ALA A 1 452 ?  13.296  13.411  1.907   1.00 74.00 ?  452 ALA A O   1 
3480 ATOM   N N   .  ASP A 1 453 ?  14.954  14.646  2.782   1.00 86.88 ?  453 ASP A N   1 
3481 ATOM   C CA  .  ASP A 1 453 ?  15.764  14.643  1.567   1.00 86.88 ?  453 ASP A CA  1 
3482 ATOM   C C   .  ASP A 1 453 ?  16.836  13.556  1.597   1.00 86.88 ?  453 ASP A C   1 
3483 ATOM   C CB  .  ASP A 1 453 ?  16.429  16.01   1.392   1.00 86.88 ?  453 ASP A CB  1 
3484 ATOM   O O   .  ASP A 1 453 ?  17.384  13.184  0.559   1.00 86.88 ?  453 ASP A O   1 
3485 ATOM   C CG  .  ASP A 1 453 ?  15.422  17.12   1.163   1.00 86.88 ?  453 ASP A CG  1 
3486 ATOM   O OD1 .  ASP A 1 453 ?  14.566  16.977  0.263   1.00 86.88 ?  453 ASP A OD1 1 
3487 ATOM   O OD2 .  ASP A 1 453 ?  15.492  18.144  1.875   1.00 86.88 ?  453 ASP A OD2 1 
3488 ATOM   N N   .  GLN A 1 454 ?  17.128  13.037  2.785   1.00 91.12 ?  454 GLN A N   1 
3489 ATOM   C CA  .  GLN A 1 454 ?  18.119  11.977  2.947   1.00 91.12 ?  454 GLN A CA  1 
3490 ATOM   C C   .  GLN A 1 454 ?  17.663  10.693  2.264   1.00 91.12 ?  454 GLN A C   1 
3491 ATOM   C CB  .  GLN A 1 454 ?  18.366  11.699  4.432   1.00 91.12 ?  454 GLN A CB  1 
3492 ATOM   O O   .  GLN A 1 454 ?  18.452  10.017  1.604   1.00 91.12 ?  454 GLN A O   1 
3493 ATOM   C CG  .  GLN A 1 454 ?  19.157  12.79   5.136   1.00 91.12 ?  454 GLN A CG  1 
3494 ATOM   C CD  .  GLN A 1 454 ?  19.394  12.494  6.603   1.00 91.12 ?  454 GLN A CD  1 
3495 ATOM   N NE2 .  GLN A 1 454 ?  19.921  13.474  7.319   1.00 91.12 ?  454 GLN A NE2 1 
3496 ATOM   O OE1 .  GLN A 1 454 ?  19.121  11.399  7.091   1.00 91.12 ?  454 GLN A OE1 1 
3497 ATOM   N N   .  PHE A 1 455 ?  16.385  10.361  2.412   1.00 90.94 ?  455 PHE A N   1 
3498 ATOM   C CA  .  PHE A 1 455 ?  15.838  9.179   1.755   1.00 90.94 ?  455 PHE A CA  1 
3499 ATOM   C C   .  PHE A 1 455 ?  15.867  9.376   0.243   1.00 90.94 ?  455 PHE A C   1 
3500 ATOM   C CB  .  PHE A 1 455 ?  14.407  8.898   2.222   1.00 90.94 ?  455 PHE A CB  1 
3501 ATOM   O O   .  PHE A 1 455 ?  16.179  8.45    -0.503  1.00 90.94 ?  455 PHE A O   1 
3502 ATOM   C CG  .  PHE A 1 455 ?  14.281  8.738   3.712   1.00 90.94 ?  455 PHE A CG  1 
3503 ATOM   C CD1 .  PHE A 1 455 ?  14.952  7.716   4.375   1.00 90.94 ?  455 PHE A CD1 1 
3504 ATOM   C CD2 .  PHE A 1 455 ?  13.515  9.631   4.453   1.00 90.94 ?  455 PHE A CD2 1 
3505 ATOM   C CE1 .  PHE A 1 455 ?  14.923  7.63    5.764   1.00 90.94 ?  455 PHE A CE1 1 
3506 ATOM   C CE2 .  PHE A 1 455 ?  13.465  9.544   5.843   1.00 90.94 ?  455 PHE A CE2 1 
3507 ATOM   C CZ  .  PHE A 1 455 ?  14.187  8.553   6.501   1.00 90.94 ?  455 PHE A CZ  1 
3508 ATOM   N N   .  GLY A 1 456 ?  15.56   10.587  -0.211  1.00 93.25 ?  456 GLY A N   1 
3509 ATOM   C CA  .  GLY A 1 456 ?  15.549  10.866  -1.636  1.00 93.25 ?  456 GLY A CA  1 
3510 ATOM   C C   .  GLY A 1 456 ?  16.927  10.776  -2.262  1.00 93.25 ?  456 GLY A C   1 
3511 ATOM   O O   .  GLY A 1 456 ?  17.083  10.252  -3.365  1.00 93.25 ?  456 GLY A O   1 
3512 ATOM   N N   .  LYS A 1 457 ?  17.941  11.273  -1.561  1.00 95.19 ?  457 LYS A N   1 
3513 ATOM   C CA  .  LYS A 1 457 ?  19.317  11.192  -2.046  1.00 95.19 ?  457 LYS A CA  1 
3514 ATOM   C C   .  LYS A 1 457 ?  19.84   9.76    -2.03   1.00 95.19 ?  457 LYS A C   1 
3515 ATOM   C CB  .  LYS A 1 457 ?  20.234  12.108  -1.231  1.00 95.19 ?  457 LYS A CB  1 
3516 ATOM   O O   .  LYS A 1 457 ?  20.666  9.408   -2.869  1.00 95.19 ?  457 LYS A O   1 
3517 ATOM   C CG  .  LYS A 1 457 ?  20.015  13.599  -1.467  1.00 95.19 ?  457 LYS A CG  1 
3518 ATOM   C CD  .  LYS A 1 457 ?  20.428  14.057  -2.86   1.00 95.19 ?  457 LYS A CD  1 
3519 ATOM   C CE  .  LYS A 1 457 ?  20.362  15.573  -2.965  1.00 95.19 ?  457 LYS A CE  1 
3520 ATOM   N NZ  .  LYS A 1 457 ?  20.734  16.003  -4.353  1.00 95.19 ?  457 LYS A NZ  1 
3521 ATOM   N N   .  MET A 1 458 ?  19.349  8.935   -1.112  1.00 96.38 ?  458 MET A N   1 
3522 ATOM   C CA  .  MET A 1 458 ?  19.661  7.508   -1.114  1.00 96.38 ?  458 MET A CA  1 
3523 ATOM   C C   .  MET A 1 458 ?  19.163  6.847   -2.399  1.00 96.38 ?  458 MET A C   1 
3524 ATOM   C CB  .  MET A 1 458 ?  19.028  6.823   0.101   1.00 96.38 ?  458 MET A CB  1 
3525 ATOM   O O   .  MET A 1 458 ?  19.859  6.014   -2.978  1.00 96.38 ?  458 MET A O   1 
3526 ATOM   C CG  .  MET A 1 458 ?  19.385  5.351   0.254   1.00 96.38 ?  458 MET A CG  1 
3527 ATOM   S SD  .  MET A 1 458 ?  18.458  4.573   1.594   1.00 96.38 ?  458 MET A SD  1 
3528 ATOM   C CE  .  MET A 1 458 ?  16.881  4.202   0.802   1.00 96.38 ?  458 MET A CE  1 
3529 ATOM   N N   .  ILE A 1 459 ?  17.971  7.222   -2.852  1.00 97.06 ?  459 ILE A N   1 
3530 ATOM   C CA  .  ILE A 1 459 ?  17.403  6.665   -4.079  1.00 97.06 ?  459 ILE A CA  1 
3531 ATOM   C C   .  ILE A 1 459 ?  18.212  7.127   -5.288  1.00 97.06 ?  459 ILE A C   1 
3532 ATOM   C CB  .  ILE A 1 459 ?  15.923  7.073   -4.295  1.00 97.06 ?  459 ILE A CB  1 
3533 ATOM   O O   .  ILE A 1 459 ?  18.572  6.323   -6.147  1.00 97.06 ?  459 ILE A O   1 
3534 ATOM   C CG1 .  ILE A 1 459 ?  15.035  6.676   -3.109  1.00 97.06 ?  459 ILE A CG1 1 
3535 ATOM   C CG2 .  ILE A 1 459 ?  15.377  6.469   -5.587  1.00 97.06 ?  459 ILE A CG2 1 
3536 ATOM   C CD1 .  ILE A 1 459 ?  15.051  5.213   -2.707  1.00 97.06 ?  459 ILE A CD1 1 
3537 ATOM   N N   .  ASN A 1 460 ?  18.508  8.421   -5.348  1.00 97.25 ?  460 ASN A N   1 
3538 ATOM   C CA  .  ASN A 1 460 ?  19.246  8.986   -6.473  1.00 97.25 ?  460 ASN A CA  1 
3539 ATOM   C C   .  ASN A 1 460 ?  20.684  8.475   -6.523  1.00 97.25 ?  460 ASN A C   1 
3540 ATOM   C CB  .  ASN A 1 460 ?  19.238  10.515  -6.388  1.00 97.25 ?  460 ASN A CB  1 
3541 ATOM   O O   .  ASN A 1 460 ?  21.282  8.398   -7.595  1.00 97.25 ?  460 ASN A O   1 
3542 ATOM   C CG  .  ASN A 1 460 ?  17.868  11.103  -6.648  1.00 97.25 ?  460 ASN A CG  1 
3543 ATOM   N ND2 .  ASN A 1 460 ?  17.463  12.057  -5.825  1.00 97.25 ?  460 ASN A ND2 1 
3544 ATOM   O OD1 .  ASN A 1 460 ?  17.183  10.719  -7.592  1.00 97.25 ?  460 ASN A OD1 1 
3545 ATOM   N N   .  TRP A 1 461 ?  21.24   8.112   -5.372  1.00 97.88 ?  461 TRP A N   1 
3546 ATOM   C CA  .  TRP A 1 461 ?  22.568  7.509   -5.313  1.00 97.88 ?  461 TRP A CA  1 
3547 ATOM   C C   .  TRP A 1 461 ?  22.556  6.092   -5.877  1.00 97.88 ?  461 TRP A C   1 
3548 ATOM   C CB  .  TRP A 1 461 ?  23.08   7.498   -3.87   1.00 97.88 ?  461 TRP A CB  1 
3549 ATOM   O O   .  TRP A 1 461 ?  23.385  5.754   -6.721  1.00 97.88 ?  461 TRP A O   1 
3550 ATOM   C CG  .  TRP A 1 461 ?  24.376  6.76    -3.716  1.00 97.88 ?  461 TRP A CG  1 
3551 ATOM   C CD1 .  TRP A 1 461 ?  25.587  7.094   -4.244  1.00 97.88 ?  461 TRP A CD1 1 
3552 ATOM   C CD2 .  TRP A 1 461 ?  24.591  5.52    -3.023  1.00 97.88 ?  461 TRP A CD2 1 
3553 ATOM   C CE2 .  TRP A 1 461 ?  25.951  5.168   -3.192  1.00 97.88 ?  461 TRP A CE2 1 
3554 ATOM   C CE3 .  TRP A 1 461 ?  23.775  4.686   -2.247  1.00 97.88 ?  461 TRP A CE3 1 
3555 ATOM   N NE1 .  TRP A 1 461 ?  26.535  6.15    -3.947  1.00 97.88 ?  461 TRP A NE1 1 
3556 ATOM   C CH2 .  TRP A 1 461 ?  25.684  3.224   -1.849  1.00 97.88 ?  461 TRP A CH2 1 
3557 ATOM   C CZ2 .  TRP A 1 461 ?  26.5    4.019   -2.614  1.00 97.88 ?  461 TRP A CZ2 1 
3558 ATOM   C CZ3 .  TRP A 1 461 ?  24.327  3.548   -1.659  1.00 97.88 ?  461 TRP A CZ3 1 
3559 ATOM   N N   .  LEU A 1 462 ?  21.61   5.273   -5.431  1.00 98.25 ?  462 LEU A N   1 
3560 ATOM   C CA  .  LEU A 1 462 ?  21.511  3.89    -5.89   1.00 98.25 ?  462 LEU A CA  1 
3561 ATOM   C C   .  LEU A 1 462 ?  21.171  3.827   -7.376  1.00 98.25 ?  462 LEU A C   1 
3562 ATOM   C CB  .  LEU A 1 462 ?  20.462  3.134   -5.068  1.00 98.25 ?  462 LEU A CB  1 
3563 ATOM   O O   .  LEU A 1 462 ?  21.585  2.9     -8.069  1.00 98.25 ?  462 LEU A O   1 
3564 ATOM   C CG  .  LEU A 1 462 ?  20.824  2.791   -3.619  1.00 98.25 ?  462 LEU A CG  1 
3565 ATOM   C CD1 .  LEU A 1 462 ?  19.588  2.334   -2.856  1.00 98.25 ?  462 LEU A CD1 1 
3566 ATOM   C CD2 .  LEU A 1 462 ?  21.887  1.699   -3.568  1.00 98.25 ?  462 LEU A CD2 1 
3567 ATOM   N N   .  ALA A 1 463 ?  20.44   4.818   -7.876  1.00 98.25 ?  463 ALA A N   1 
3568 ATOM   C CA  .  ALA A 1 463 ?  20.143  4.913   -9.303  1.00 98.25 ?  463 ALA A CA  1 
3569 ATOM   C C   .  ALA A 1 463 ?  21.41   5.041   -10.145 1.00 98.25 ?  463 ALA A C   1 
3570 ATOM   C CB  .  ALA A 1 463 ?  19.219  6.097   -9.564  1.00 98.25 ?  463 ALA A CB  1 
3571 ATOM   O O   .  ALA A 1 463 ?  21.512  4.454   -11.222 1.00 98.25 ?  463 ALA A O   1 
3572 ATOM   N N   .  LYS A 1 464 ?  22.374  5.803   -9.64   1.00 97.94 ?  464 LYS A N   1 
3573 ATOM   C CA  .  LYS A 1 464 ?  23.64   6.035   -10.331 1.00 97.94 ?  464 LYS A CA  1 
3574 ATOM   C C   .  LYS A 1 464 ?  24.558  4.821   -10.238 1.00 97.94 ?  464 LYS A C   1 
3575 ATOM   C CB  .  LYS A 1 464 ?  24.339  7.264   -9.745  1.00 97.94 ?  464 LYS A CB  1 
3576 ATOM   O O   .  LYS A 1 464 ?  25.306  4.53    -11.169 1.00 97.94 ?  464 LYS A O   1 
3577 ATOM   C CG  .  LYS A 1 464 ?  23.582  8.563   -9.983  1.00 97.94 ?  464 LYS A CG  1 
3578 ATOM   C CD  .  LYS A 1 464 ?  24.204  9.722   -9.219  1.00 97.94 ?  464 LYS A CD  1 
3579 ATOM   C CE  .  LYS A 1 464 ?  23.371  10.982  -9.385  1.00 97.94 ?  464 LYS A CE  1 
3580 ATOM   N NZ  .  LYS A 1 464 ?  24.012  12.111  -8.632  1.00 97.94 ?  464 LYS A NZ  1 
3581 ATOM   N N   .  GLU A 1 465 ?  24.489  4.11    -9.119  1.00 97.75 ?  465 GLU A N   1 
3582 ATOM   C CA  .  GLU A 1 465 ?  25.22   2.855   -8.959  1.00 97.75 ?  465 GLU A CA  1 
3583 ATOM   C C   .  GLU A 1 465 ?  24.678  1.799   -9.918  1.00 97.75 ?  465 GLU A C   1 
3584 ATOM   C CB  .  GLU A 1 465 ?  25.112  2.33    -7.524  1.00 97.75 ?  465 GLU A CB  1 
3585 ATOM   O O   .  GLU A 1 465 ?  25.429  0.969   -10.428 1.00 97.75 ?  465 GLU A O   1 
3586 ATOM   C CG  .  GLU A 1 465 ?  25.698  3.232   -6.445  1.00 97.75 ?  465 GLU A CG  1 
3587 ATOM   C CD  .  GLU A 1 465 ?  27.162  3.558   -6.675  1.00 97.75 ?  465 GLU A CD  1 
3588 ATOM   O OE1 .  GLU A 1 465 ?  27.548  4.736   -6.525  1.00 97.75 ?  465 GLU A OE1 1 
3589 ATOM   O OE2 .  GLU A 1 465 ?  27.944  2.646   -7.018  1.00 97.75 ?  465 GLU A OE2 1 
3590 ATOM   N N   .  THR A 1 466 ?  23.374  1.836   -10.169 1.00 97.38 ?  466 THR A N   1 
3591 ATOM   C CA  .  THR A 1 466 ?  22.721  0.896   -11.077 1.00 97.38 ?  466 THR A CA  1 
3592 ATOM   C C   .  THR A 1 466 ?  23.133  1.106   -12.532 1.00 97.38 ?  466 THR A C   1 
3593 ATOM   C CB  .  THR A 1 466 ?  21.187  1.006   -10.975 1.00 97.38 ?  466 THR A CB  1 
3594 ATOM   O O   .  THR A 1 466 ?  23.229  0.145   -13.293 1.00 97.38 ?  466 THR A O   1 
3595 ATOM   C CG2 .  THR A 1 466 ?  20.492  -0.103  -11.755 1.00 97.38 ?  466 THR A CG2 1 
3596 ATOM   O OG1 .  THR A 1 466 ?  20.801  0.885   -9.601  1.00 97.38 ?  466 THR A OG1 1 
3597 ATOM   N N   .  GLN A 1 467 ?  23.39   2.347   -12.932 1.00 93.06 ?  467 GLN A N   1 
3598 ATOM   C CA  .  GLN A 1 467 ?  23.84   2.613   -14.296 1.00 93.06 ?  467 GLN A CA  1 
3599 ATOM   C C   .  GLN A 1 467 ?  25.255  2.108   -14.567 1.00 93.06 ?  467 GLN A C   1 
3600 ATOM   C CB  .  GLN A 1 467 ?  23.796  4.106   -14.627 1.00 93.06 ?  467 GLN A CB  1 
3601 ATOM   O O   .  GLN A 1 467 ?  25.609  1.855   -15.719 1.00 93.06 ?  467 GLN A O   1 
3602 ATOM   C CG  .  GLN A 1 467 ?  22.402  4.709   -14.71  1.00 93.06 ?  467 GLN A CG  1 
3603 ATOM   C CD  .  GLN A 1 467 ?  22.377  5.945   -15.587 1.00 93.06 ?  467 GLN A CD  1 
3604 ATOM   N NE2 .  GLN A 1 467 ?  21.261  6.169   -16.264 1.00 93.06 ?  467 GLN A NE2 1 
3605 ATOM   O OE1 .  GLN A 1 467 ?  23.356  6.684   -15.677 1.00 93.06 ?  467 GLN A OE1 1 
3606 ATOM   N N   .  LYS A 1 468 ?  26.066  1.971   -13.524 1.00 89.69 ?  468 LYS A N   1 
3607 ATOM   C CA  .  LYS A 1 468 ?  27.45   1.525   -13.675 1.00 89.69 ?  468 LYS A CA  1 
3608 ATOM   C C   .  LYS A 1 468 ?  27.496  0.097   -14.209 1.00 89.69 ?  468 LYS A C   1 
3609 ATOM   C CB  .  LYS A 1 468 ?  28.19   1.608   -12.336 1.00 89.69 ?  468 LYS A CB  1 
3610 ATOM   O O   .  LYS A 1 468 ?  28.402  -0.185  -15.021 1.00 89.69 ?  468 LYS A O   1 
3611 ATOM   C CG  .  LYS A 1 468 ?  28.35   3.028   -11.81  1.00 89.69 ?  468 LYS A CG  1 
3612 ATOM   C CD  .  LYS A 1 468 ?  29.09   3.05    -10.482 1.00 89.69 ?  468 LYS A CD  1 
3613 ATOM   C CE  .  LYS A 1 468 ?  29.167  4.464   -9.927  1.00 89.69 ?  468 LYS A CE  1 
3614 ATOM   N NZ  .  LYS A 1 468 ?  29.905  4.449   -8.621  1.00 89.69 ?  468 LYS A NZ  1 
3615 ATOM   O OXT .  LYS A 1 468 ?  26.639  -0.716  -13.803 1.00 89.69 ?  468 LYS A OXT 1 
3616 HETATM O O3X ?  NAP B 2 .   ?  11.32   4.478   -3.215  1.00 30.98 ?  1   NAP B O3X 1 
3617 HETATM P P2B ?  NAP B 2 .   ?  11.604  3.028   -3.33   1.00 31.44 ?  1   NAP B P2B 1 
3618 HETATM O O1X ?  NAP B 2 .   ?  12.952  2.747   -2.788  1.00 35.73 ?  1   NAP B O1X 1 
3619 HETATM O O2X ?  NAP B 2 .   ?  10.605  2.255   -2.568  1.00 30.51 ?  1   NAP B O2X 1 
3620 HETATM O O2B ?  NAP B 2 .   ?  11.537  2.604   -4.884  1.00 34.49 ?  1   NAP B O2B 1 
3621 HETATM C C2B ?  NAP B 2 .   ?  10.402  3.043   -5.646  1.00 33.76 ?  1   NAP B C2B 1 
3622 HETATM C C1B ?  NAP B 2 .   ?  10.423  2.681   -7.132  1.00 35.26 ?  1   NAP B C1B 1 
3623 HETATM N N9A ?  NAP B 2 .   ?  11.317  3.445   -7.999  1.00 30.26 ?  1   NAP B N9A 1 
3624 HETATM C C4A ?  NAP B 2 .   ?  12.106  2.884   -8.954  1.00 30.05 ?  1   NAP B C4A 1 
3625 HETATM N N3A ?  NAP B 2 .   ?  12.319  1.592   -9.259  1.00 31.54 ?  1   NAP B N3A 1 
3626 HETATM C C2A ?  NAP B 2 .   ?  13.181  1.384   -10.269 1.00 34.01 ?  1   NAP B C2A 1 
3627 HETATM N N1A ?  NAP B 2 .   ?  13.833  2.316   -10.976 1.00 34.31 ?  1   NAP B N1A 1 
3628 HETATM C C6A ?  NAP B 2 .   ?  13.604  3.571   -10.626 1.00 29.78 ?  1   NAP B C6A 1 
3629 HETATM N N6A ?  NAP B 2 .   ?  14.296  4.486   -11.33  1.00 32.13 ?  1   NAP B N6A 1 
3630 HETATM C C5A ?  NAP B 2 .   ?  12.727  3.907   -9.592  1.00 34.21 ?  1   NAP B C5A 1 
3631 HETATM N N7A ?  NAP B 2 .   ?  12.394  5.139   -9.108  1.00 31.44 ?  1   NAP B N7A 1 
3632 HETATM C C8A ?  NAP B 2 .   ?  11.51   4.83    -8.136  1.00 30.66 ?  1   NAP B C8A 1 
3633 HETATM O O4B ?  NAP B 2 .   ?  9.03    2.862   -7.528  1.00 31.23 ?  1   NAP B O4B 1 
3634 HETATM C C3B ?  NAP B 2 .   ?  9.064   2.373   -5.237  1.00 34.38 ?  1   NAP B C3B 1 
3635 HETATM O O3B ?  NAP B 2 .   ?  9.11    0.945   -5.405  1.00 33.82 ?  1   NAP B O3B 1 
3636 HETATM C C4B ?  NAP B 2 .   ?  8.181   2.976   -6.344  1.00 35.50 ?  1   NAP B C4B 1 
3637 HETATM C C5B ?  NAP B 2 .   ?  7.845   4.483   -6.081  1.00 35.49 ?  1   NAP B C5B 1 
3638 HETATM O O5B ?  NAP B 2 .   ?  8.015   4.776   -4.671  1.00 36.72 ?  1   NAP B O5B 1 
3639 HETATM P PA  ?  NAP B 2 .   ?  8.209   6.289   -4.173  1.00 40.98 ?  1   NAP B PA  1 
3640 HETATM O O1A ?  NAP B 2 .   ?  9.197   6.999   -5.013  1.00 48.43 ?  1   NAP B O1A 1 
3641 HETATM O O2A ?  NAP B 2 .   ?  6.912   7       -4.104  1.00 42.58 ?  1   NAP B O2A 1 
3642 HETATM O O3  ?  NAP B 2 .   ?  8.766   6.005   -2.79   1.00 54.56 ?  1   NAP B O3  1 
3643 HETATM P PN  ?  NAP B 2 .   ?  9.334   7.137   -1.928  1.00 79.66 ?  1   NAP B PN  1 
3644 HETATM O O1N ?  NAP B 2 .   ?  10.813  7.157   -2.033  1.00 71.59 ?  1   NAP B O1N 1 
3645 HETATM O O2N ?  NAP B 2 .   ?  8.947   6.909   -0.513  1.00 68.51 ?  1   NAP B O2N 1 
3646 HETATM O O5D ?  NAP B 2 .   ?  8.794   8.444   -2.377  1.00 79.45 ?  1   NAP B O5D 1 
# 
_atom_sites.entry_id                    nohd 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
_database_PDB_matrix.entry_id          nohd 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_symmetry.entry_id               nohd 
_symmetry.space_group_name_H-M   'P 1' 
_symmetry.Int_Tables_number      1 
# 
_cell.entry_id      nohd 
_cell.length_a      1.000 
_cell.length_b      1.000 
_cell.length_c      1.000 
_cell.angle_alpha   90.00 
_cell.angle_beta    90.00 
_cell.angle_gamma   90.00 
_cell.Z_PDB         1 
# 
loop_
_chem_comp.id 
_chem_comp.name 
_chem_comp.formula 
_chem_comp.formula_weight 
_chem_comp.mon_nstd_flag 
_chem_comp.type 
ALA ALANINE                                            'C3 H7 N O2'        89.093002  y  'L-PEPTIDE LINKING' 
ARG ARGININE                                           'C6 H15 N4 O2'      175.209000 y  'L-PEPTIDE LINKING' 
ASN ASPARAGINE                                         'C4 H8 N2 O3'       132.117996 y  'L-PEPTIDE LINKING' 
ASP 'ASPARTIC ACID'                                    'C4 H7 N O4'        133.102997 y  'L-PEPTIDE LINKING' 
CYS CYSTEINE                                           'C3 H7 N O2 S'      121.157997 y  'L-PEPTIDE LINKING' 
GLN GLUTAMINE                                          'C5 H10 N2 O3'      146.143997 y  'L-PEPTIDE LINKING' 
GLU 'GLUTAMIC ACID'                                    'C5 H9 N O4'        147.128998 y  'L-PEPTIDE LINKING' 
GLY GLYCINE                                            'C2 H5 N O2'        75.067001  y  'PEPTIDE LINKING'   
HIS HISTIDINE                                          'C6 H10 N3 O2'      156.162003 y  'L-PEPTIDE LINKING' 
ILE ISOLEUCINE                                         'C6 H13 N O2'       131.173004 y  'L-PEPTIDE LINKING' 
LEU LEUCINE                                            'C6 H13 N O2'       131.173004 y  'L-PEPTIDE LINKING' 
LYS LYSINE                                             'C6 H15 N2 O2'      147.195007 y  'L-PEPTIDE LINKING' 
MET METHIONINE                                         'C5 H11 N O2 S'     149.210999 y  'L-PEPTIDE LINKING' 
PHE PHENYLALANINE                                      'C9 H11 N O2'       165.188995 y  'L-PEPTIDE LINKING' 
PRO PROLINE                                            'C5 H9 N O2'        115.129997 y  'L-PEPTIDE LINKING' 
SER SERINE                                             'C3 H7 N O3'        105.093002 y  'L-PEPTIDE LINKING' 
THR THREONINE                                          'C4 H9 N O3'        119.119003 y  'L-PEPTIDE LINKING' 
TRP TRYPTOPHAN                                         'C11 H12 N2 O2'     204.225006 y  'L-PEPTIDE LINKING' 
TYR TYROSINE                                           'C9 H11 N O3'       181.188995 y  'L-PEPTIDE LINKING' 
VAL VALINE                                             'C5 H11 N O2'       117.146004 y  'L-PEPTIDE LINKING' 
NAP 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 'C21 H28 N7 O17 P3' 743.405    ?  NON-POLYMER         
# 
_struct.entry_id                  nohd 
_struct.title                     'ALPHAFOLD MONOMER V2.0 PREDICTION FOR P48-LIKE PROTEIN (Q6E5B5)' 
_struct.pdbx_descriptor           'P48-LIKE PROTEIN' 
_struct.pdbx_model_type_details   ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.pdbx_seq_one_letter_code       
;MKKNKFYLFLGAAPVLSVPLVAASCGDKYFKETEVDGVKTVTTLSHIVSRKGLKLRDGLTVDNAPRAAFITDEGSVHDES
FNQSGWEAVHKISYELGLDKAQVSGNKNLRNKVYEPKKGELASSYKNAIDSSFRYIVLCGFTHKAALYGLEPEYIKKIKD
NNIVFITVDFDIQQDASTGEPAAKAFVDKIGQGRLIPVIFDTKQAAYIAGRALADYFSKIYKDNPEKRTIGAFGGIPWPS
VSDFIAGTFQGIIDWNKEHPEAKTKSLNNTIELKTSFTSGEPVAVAAINSVIKATASYPVAGSLSSDTAKEIKKLGDKNK
FIIGVDADQKNALKGHRIFTSVMKLIGQAVYNVLADLYSQGENSLSLQPGFEIGKKNGEAKVFGYGENEASKYVGVATSG
LLDSKNDEIANKALEEATKYYESKKAEIQKTLSGQLEEAKKALGTKWPDQPADQFGKMINWLAKETQK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKNKFYLFLGAAPVLSVPLVAASCGDKYFKETEVDGVKTVTTLSHIVSRKGLKLRDGLTVDNAPRAAFITDEGSVHDES
FNQSGWEAVHKISYELGLDKAQVSGNKNLRNKVYEPKKGELASSYKNAIDSSFRYIVLCGFTHKAALYGLEPEYIKKIKD
NNIVFITVDFDIQQDASTGEPAAKAFVDKIGQGRLIPVIFDTKQAAYIAGRALADYFSKIYKDNPEKRTIGAFGGIPWPS
VSDFIAGTFQGIIDWNKEHPEAKTKSLNNTIELKTSFTSGEPVAVAAINSVIKATASYPVAGSLSSDTAKEIKKLGDKNK
FIIGVDADQKNALKGHRIFTSVMKLIGQAVYNVLADLYSQGENSLSLQPGFEIGKKNGEAKVFGYGENEASKYVGVATSG
LLDSKNDEIANKALEEATKYYESKKAEIQKTLSGQLEEAKKALGTKWPDQPADQFGKMINWLAKETQK
;
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_strand_id                 A 
_entity_poly.nstd_linkage                   no 
_entity_poly.type                           polypeptide(L) 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LYS n 
1 4   ASN n 
1 5   LYS n 
1 6   PHE n 
1 7   TYR n 
1 8   LEU n 
1 9   PHE n 
1 10  LEU n 
1 11  GLY n 
1 12  ALA n 
1 13  ALA n 
1 14  PRO n 
1 15  VAL n 
1 16  LEU n 
1 17  SER n 
1 18  VAL n 
1 19  PRO n 
1 20  LEU n 
1 21  VAL n 
1 22  ALA n 
1 23  ALA n 
1 24  SER n 
1 25  CYS n 
1 26  GLY n 
1 27  ASP n 
1 28  LYS n 
1 29  TYR n 
1 30  PHE n 
1 31  LYS n 
1 32  GLU n 
1 33  THR n 
1 34  GLU n 
1 35  VAL n 
1 36  ASP n 
1 37  GLY n 
1 38  VAL n 
1 39  LYS n 
1 40  THR n 
1 41  VAL n 
1 42  THR n 
1 43  THR n 
1 44  LEU n 
1 45  SER n 
1 46  HIS n 
1 47  ILE n 
1 48  VAL n 
1 49  SER n 
1 50  ARG n 
1 51  LYS n 
1 52  GLY n 
1 53  LEU n 
1 54  LYS n 
1 55  LEU n 
1 56  ARG n 
1 57  ASP n 
1 58  GLY n 
1 59  LEU n 
1 60  THR n 
1 61  VAL n 
1 62  ASP n 
1 63  ASN n 
1 64  ALA n 
1 65  PRO n 
1 66  ARG n 
1 67  ALA n 
1 68  ALA n 
1 69  PHE n 
1 70  ILE n 
1 71  THR n 
1 72  ASP n 
1 73  GLU n 
1 74  GLY n 
1 75  SER n 
1 76  VAL n 
1 77  HIS n 
1 78  ASP n 
1 79  GLU n 
1 80  SER n 
1 81  PHE n 
1 82  ASN n 
1 83  GLN n 
1 84  SER n 
1 85  GLY n 
1 86  TRP n 
1 87  GLU n 
1 88  ALA n 
1 89  VAL n 
1 90  HIS n 
1 91  LYS n 
1 92  ILE n 
1 93  SER n 
1 94  TYR n 
1 95  GLU n 
1 96  LEU n 
1 97  GLY n 
1 98  LEU n 
1 99  ASP n 
1 100 LYS n 
1 101 ALA n 
1 102 GLN n 
1 103 VAL n 
1 104 SER n 
1 105 GLY n 
1 106 ASN n 
1 107 LYS n 
1 108 ASN n 
1 109 LEU n 
1 110 ARG n 
1 111 ASN n 
1 112 LYS n 
1 113 VAL n 
1 114 TYR n 
1 115 GLU n 
1 116 PRO n 
1 117 LYS n 
1 118 LYS n 
1 119 GLY n 
1 120 GLU n 
1 121 LEU n 
1 122 ALA n 
1 123 SER n 
1 124 SER n 
1 125 TYR n 
1 126 LYS n 
1 127 ASN n 
1 128 ALA n 
1 129 ILE n 
1 130 ASP n 
1 131 SER n 
1 132 SER n 
1 133 PHE n 
1 134 ARG n 
1 135 TYR n 
1 136 ILE n 
1 137 VAL n 
1 138 LEU n 
1 139 CYS n 
1 140 GLY n 
1 141 PHE n 
1 142 THR n 
1 143 HIS n 
1 144 LYS n 
1 145 ALA n 
1 146 ALA n 
1 147 LEU n 
1 148 TYR n 
1 149 GLY n 
1 150 LEU n 
1 151 GLU n 
1 152 PRO n 
1 153 GLU n 
1 154 TYR n 
1 155 ILE n 
1 156 LYS n 
1 157 LYS n 
1 158 ILE n 
1 159 LYS n 
1 160 ASP n 
1 161 ASN n 
1 162 ASN n 
1 163 ILE n 
1 164 VAL n 
1 165 PHE n 
1 166 ILE n 
1 167 THR n 
1 168 VAL n 
1 169 ASP n 
1 170 PHE n 
1 171 ASP n 
1 172 ILE n 
1 173 GLN n 
1 174 GLN n 
1 175 ASP n 
1 176 ALA n 
1 177 SER n 
1 178 THR n 
1 179 GLY n 
1 180 GLU n 
1 181 PRO n 
1 182 ALA n 
1 183 ALA n 
1 184 LYS n 
1 185 ALA n 
1 186 PHE n 
1 187 VAL n 
1 188 ASP n 
1 189 LYS n 
1 190 ILE n 
1 191 GLY n 
1 192 GLN n 
1 193 GLY n 
1 194 ARG n 
1 195 LEU n 
1 196 ILE n 
1 197 PRO n 
1 198 VAL n 
1 199 ILE n 
1 200 PHE n 
1 201 ASP n 
1 202 THR n 
1 203 LYS n 
1 204 GLN n 
1 205 ALA n 
1 206 ALA n 
1 207 TYR n 
1 208 ILE n 
1 209 ALA n 
1 210 GLY n 
1 211 ARG n 
1 212 ALA n 
1 213 LEU n 
1 214 ALA n 
1 215 ASP n 
1 216 TYR n 
1 217 PHE n 
1 218 SER n 
1 219 LYS n 
1 220 ILE n 
1 221 TYR n 
1 222 LYS n 
1 223 ASP n 
1 224 ASN n 
1 225 PRO n 
1 226 GLU n 
1 227 LYS n 
1 228 ARG n 
1 229 THR n 
1 230 ILE n 
1 231 GLY n 
1 232 ALA n 
1 233 PHE n 
1 234 GLY n 
1 235 GLY n 
1 236 ILE n 
1 237 PRO n 
1 238 TRP n 
1 239 PRO n 
1 240 SER n 
1 241 VAL n 
1 242 SER n 
1 243 ASP n 
1 244 PHE n 
1 245 ILE n 
1 246 ALA n 
1 247 GLY n 
1 248 THR n 
1 249 PHE n 
1 250 GLN n 
1 251 GLY n 
1 252 ILE n 
1 253 ILE n 
1 254 ASP n 
1 255 TRP n 
1 256 ASN n 
1 257 LYS n 
1 258 GLU n 
1 259 HIS n 
1 260 PRO n 
1 261 GLU n 
1 262 ALA n 
1 263 LYS n 
1 264 THR n 
1 265 LYS n 
1 266 SER n 
1 267 LEU n 
1 268 ASN n 
1 269 ASN n 
1 270 THR n 
1 271 ILE n 
1 272 GLU n 
1 273 LEU n 
1 274 LYS n 
1 275 THR n 
1 276 SER n 
1 277 PHE n 
1 278 THR n 
1 279 SER n 
1 280 GLY n 
1 281 GLU n 
1 282 PRO n 
1 283 VAL n 
1 284 ALA n 
1 285 VAL n 
1 286 ALA n 
1 287 ALA n 
1 288 ILE n 
1 289 ASN n 
1 290 SER n 
1 291 VAL n 
1 292 ILE n 
1 293 LYS n 
1 294 ALA n 
1 295 THR n 
1 296 ALA n 
1 297 SER n 
1 298 TYR n 
1 299 PRO n 
1 300 VAL n 
1 301 ALA n 
1 302 GLY n 
1 303 SER n 
1 304 LEU n 
1 305 SER n 
1 306 SER n 
1 307 ASP n 
1 308 THR n 
1 309 ALA n 
1 310 LYS n 
1 311 GLU n 
1 312 ILE n 
1 313 LYS n 
1 314 LYS n 
1 315 LEU n 
1 316 GLY n 
1 317 ASP n 
1 318 LYS n 
1 319 ASN n 
1 320 LYS n 
1 321 PHE n 
1 322 ILE n 
1 323 ILE n 
1 324 GLY n 
1 325 VAL n 
1 326 ASP n 
1 327 ALA n 
1 328 ASP n 
1 329 GLN n 
1 330 LYS n 
1 331 ASN n 
1 332 ALA n 
1 333 LEU n 
1 334 LYS n 
1 335 GLY n 
1 336 HIS n 
1 337 ARG n 
1 338 ILE n 
1 339 PHE n 
1 340 THR n 
1 341 SER n 
1 342 VAL n 
1 343 MET n 
1 344 LYS n 
1 345 LEU n 
1 346 ILE n 
1 347 GLY n 
1 348 GLN n 
1 349 ALA n 
1 350 VAL n 
1 351 TYR n 
1 352 ASN n 
1 353 VAL n 
1 354 LEU n 
1 355 ALA n 
1 356 ASP n 
1 357 LEU n 
1 358 TYR n 
1 359 SER n 
1 360 GLN n 
1 361 GLY n 
1 362 GLU n 
1 363 ASN n 
1 364 SER n 
1 365 LEU n 
1 366 SER n 
1 367 LEU n 
1 368 GLN n 
1 369 PRO n 
1 370 GLY n 
1 371 PHE n 
1 372 GLU n 
1 373 ILE n 
1 374 GLY n 
1 375 LYS n 
1 376 LYS n 
1 377 ASN n 
1 378 GLY n 
1 379 GLU n 
1 380 ALA n 
1 381 LYS n 
1 382 VAL n 
1 383 PHE n 
1 384 GLY n 
1 385 TYR n 
1 386 GLY n 
1 387 GLU n 
1 388 ASN n 
1 389 GLU n 
1 390 ALA n 
1 391 SER n 
1 392 LYS n 
1 393 TYR n 
1 394 VAL n 
1 395 GLY n 
1 396 VAL n 
1 397 ALA n 
1 398 THR n 
1 399 SER n 
1 400 GLY n 
1 401 LEU n 
1 402 LEU n 
1 403 ASP n 
1 404 SER n 
1 405 LYS n 
1 406 ASN n 
1 407 ASP n 
1 408 GLU n 
1 409 ILE n 
1 410 ALA n 
1 411 ASN n 
1 412 LYS n 
1 413 ALA n 
1 414 LEU n 
1 415 GLU n 
1 416 GLU n 
1 417 ALA n 
1 418 THR n 
1 419 LYS n 
1 420 TYR n 
1 421 TYR n 
1 422 GLU n 
1 423 SER n 
1 424 LYS n 
1 425 LYS n 
1 426 ALA n 
1 427 GLU n 
1 428 ILE n 
1 429 GLN n 
1 430 LYS n 
1 431 THR n 
1 432 LEU n 
1 433 SER n 
1 434 GLY n 
1 435 GLN n 
1 436 LEU n 
1 437 GLU n 
1 438 GLU n 
1 439 ALA n 
1 440 LYS n 
1 441 LYS n 
1 442 ALA n 
1 443 LEU n 
1 444 GLY n 
1 445 THR n 
1 446 LYS n 
1 447 TRP n 
1 448 PRO n 
1 449 ASP n 
1 450 GLN n 
1 451 PRO n 
1 452 ALA n 
1 453 ASP n 
1 454 GLN n 
1 455 PHE n 
1 456 GLY n 
1 457 LYS n 
1 458 MET n 
1 459 ILE n 
1 460 ASN n 
1 461 TRP n 
1 462 LEU n 
1 463 ALA n 
1 464 LYS n 
1 465 GLU n 
1 466 THR n 
1 467 GLN n 
1 468 LYS n 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              XXXX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 468 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q6E5B5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  468 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       468 
# 
_struct_ref.id                  1 
_struct_ref.entity_id           1 
_struct_ref.db_name             UNP 
_struct_ref.db_code             Q6E5B5_MYCBV 
_struct_ref.pdbx_db_accession   Q6E5B5 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.pdbx_number_of_molecules 
_entity.details 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.pdbx_ec 
_entity.pdbx_parent_entity_id 
_entity.formula_weight 
1 polymer     nat 'P48-LIKE PROTEIN'                                 1 ?  ?  ?  ?  ?  ?       
2 non-polymer ?   'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 1 ?  ?  ?  ?  ?  743.405 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.common_name                ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_organism_scientific   'MYCOPLASMA BOVIS' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      28903 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_organ                 ? 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.entity_id 
_struct_asym.pdbx_modified 
_struct_asym.details 
A N 1 ? ? 
B N 2 N ? 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  PRO 19  19  19  PRO PRO A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  CYS 25  25  25  CYS CYS A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  PHE 69  69  69  PHE PHE A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  TRP 86  86  86  TRP TRP A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 GLN 102 102 102 GLN GLN A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 ASN 106 106 106 ASN ASN A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 PRO 116 116 116 PRO PRO A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 LYS 144 144 144 LYS LYS A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 TYR 148 148 148 TYR TYR A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 GLN 173 173 173 GLN GLN A . n 
A 1 174 GLN 174 174 174 GLN GLN A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 PHE 186 186 186 PHE PHE A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 LYS 189 189 189 LYS LYS A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 GLY 191 191 191 GLY GLY A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 GLN 204 204 204 GLN GLN A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TYR 207 207 207 TYR TYR A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 TYR 216 216 216 TYR TYR A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 LYS 219 219 219 LYS LYS A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 ASN 224 224 224 ASN ASN A . n 
A 1 225 PRO 225 225 225 PRO PRO A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 PHE 233 233 233 PHE PHE A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 TRP 238 238 238 TRP TRP A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 SER 242 242 242 SER SER A . n 
A 1 243 ASP 243 243 243 ASP ASP A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 PHE 249 249 249 PHE PHE A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 TRP 255 255 255 TRP TRP A . n 
A 1 256 ASN 256 256 256 ASN ASN A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 HIS 259 259 259 HIS HIS A . n 
A 1 260 PRO 260 260 260 PRO PRO A . n 
A 1 261 GLU 261 261 261 GLU GLU A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 LYS 263 263 263 LYS LYS A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 ASN 268 268 268 ASN ASN A . n 
A 1 269 ASN 269 269 269 ASN ASN A . n 
A 1 270 THR 270 270 270 THR THR A . n 
A 1 271 ILE 271 271 271 ILE ILE A . n 
A 1 272 GLU 272 272 272 GLU GLU A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 THR 275 275 275 THR THR A . n 
A 1 276 SER 276 276 276 SER SER A . n 
A 1 277 PHE 277 277 277 PHE PHE A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 PRO 282 282 282 PRO PRO A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 ILE 288 288 288 ILE ILE A . n 
A 1 289 ASN 289 289 289 ASN ASN A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 VAL 291 291 291 VAL VAL A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 LYS 293 293 293 LYS LYS A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 ALA 296 296 296 ALA ALA A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 TYR 298 298 298 TYR TYR A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 SER 305 305 305 SER SER A . n 
A 1 306 SER 306 306 306 SER SER A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 THR 308 308 308 THR THR A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 LYS 314 314 314 LYS LYS A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 ASP 317 317 317 ASP ASP A . n 
A 1 318 LYS 318 318 318 LYS LYS A . n 
A 1 319 ASN 319 319 319 ASN ASN A . n 
A 1 320 LYS 320 320 320 LYS LYS A . n 
A 1 321 PHE 321 321 321 PHE PHE A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 ILE 323 323 323 ILE ILE A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 VAL 325 325 325 VAL VAL A . n 
A 1 326 ASP 326 326 326 ASP ASP A . n 
A 1 327 ALA 327 327 327 ALA ALA A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 GLN 329 329 329 GLN GLN A . n 
A 1 330 LYS 330 330 330 LYS LYS A . n 
A 1 331 ASN 331 331 331 ASN ASN A . n 
A 1 332 ALA 332 332 332 ALA ALA A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 LYS 334 334 334 LYS LYS A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 HIS 336 336 336 HIS HIS A . n 
A 1 337 ARG 337 337 337 ARG ARG A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 THR 340 340 340 THR THR A . n 
A 1 341 SER 341 341 341 SER SER A . n 
A 1 342 VAL 342 342 342 VAL VAL A . n 
A 1 343 MET 343 343 343 MET MET A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 ILE 346 346 346 ILE ILE A . n 
A 1 347 GLY 347 347 347 GLY GLY A . n 
A 1 348 GLN 348 348 348 GLN GLN A . n 
A 1 349 ALA 349 349 349 ALA ALA A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 TYR 351 351 351 TYR TYR A . n 
A 1 352 ASN 352 352 352 ASN ASN A . n 
A 1 353 VAL 353 353 353 VAL VAL A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 ALA 355 355 355 ALA ALA A . n 
A 1 356 ASP 356 356 356 ASP ASP A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 TYR 358 358 358 TYR TYR A . n 
A 1 359 SER 359 359 359 SER SER A . n 
A 1 360 GLN 360 360 360 GLN GLN A . n 
A 1 361 GLY 361 361 361 GLY GLY A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 SER 364 364 364 SER SER A . n 
A 1 365 LEU 365 365 365 LEU LEU A . n 
A 1 366 SER 366 366 366 SER SER A . n 
A 1 367 LEU 367 367 367 LEU LEU A . n 
A 1 368 GLN 368 368 368 GLN GLN A . n 
A 1 369 PRO 369 369 369 PRO PRO A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 PHE 371 371 371 PHE PHE A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 LYS 376 376 376 LYS LYS A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 GLY 378 378 378 GLY GLY A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 ALA 380 380 380 ALA ALA A . n 
A 1 381 LYS 381 381 381 LYS LYS A . n 
A 1 382 VAL 382 382 382 VAL VAL A . n 
A 1 383 PHE 383 383 383 PHE PHE A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 TYR 385 385 385 TYR TYR A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 ASN 388 388 388 ASN ASN A . n 
A 1 389 GLU 389 389 389 GLU GLU A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 SER 391 391 391 SER SER A . n 
A 1 392 LYS 392 392 392 LYS LYS A . n 
A 1 393 TYR 393 393 393 TYR TYR A . n 
A 1 394 VAL 394 394 394 VAL VAL A . n 
A 1 395 GLY 395 395 395 GLY GLY A . n 
A 1 396 VAL 396 396 396 VAL VAL A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 THR 398 398 398 THR THR A . n 
A 1 399 SER 399 399 399 SER SER A . n 
A 1 400 GLY 400 400 400 GLY GLY A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 ASP 403 403 403 ASP ASP A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 LYS 405 405 405 LYS LYS A . n 
A 1 406 ASN 406 406 406 ASN ASN A . n 
A 1 407 ASP 407 407 407 ASP ASP A . n 
A 1 408 GLU 408 408 408 GLU GLU A . n 
A 1 409 ILE 409 409 409 ILE ILE A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 ASN 411 411 411 ASN ASN A . n 
A 1 412 LYS 412 412 412 LYS LYS A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 GLU 416 416 416 GLU GLU A . n 
A 1 417 ALA 417 417 417 ALA ALA A . n 
A 1 418 THR 418 418 418 THR THR A . n 
A 1 419 LYS 419 419 419 LYS LYS A . n 
A 1 420 TYR 420 420 420 TYR TYR A . n 
A 1 421 TYR 421 421 421 TYR TYR A . n 
A 1 422 GLU 422 422 422 GLU GLU A . n 
A 1 423 SER 423 423 423 SER SER A . n 
A 1 424 LYS 424 424 424 LYS LYS A . n 
A 1 425 LYS 425 425 425 LYS LYS A . n 
A 1 426 ALA 426 426 426 ALA ALA A . n 
A 1 427 GLU 427 427 427 GLU GLU A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 GLN 429 429 429 GLN GLN A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 THR 431 431 431 THR THR A . n 
A 1 432 LEU 432 432 432 LEU LEU A . n 
A 1 433 SER 433 433 433 SER SER A . n 
A 1 434 GLY 434 434 434 GLY GLY A . n 
A 1 435 GLN 435 435 435 GLN GLN A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 GLU 437 437 437 GLU GLU A . n 
A 1 438 GLU 438 438 438 GLU GLU A . n 
A 1 439 ALA 439 439 439 ALA ALA A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 LYS 441 441 441 LYS LYS A . n 
A 1 442 ALA 442 442 442 ALA ALA A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 GLY 444 444 444 GLY GLY A . n 
A 1 445 THR 445 445 445 THR THR A . n 
A 1 446 LYS 446 446 446 LYS LYS A . n 
A 1 447 TRP 447 447 447 TRP TRP A . n 
A 1 448 PRO 448 448 448 PRO PRO A . n 
A 1 449 ASP 449 449 449 ASP ASP A . n 
A 1 450 GLN 450 450 450 GLN GLN A . n 
A 1 451 PRO 451 451 451 PRO PRO A . n 
A 1 452 ALA 452 452 452 ALA ALA A . n 
A 1 453 ASP 453 453 453 ASP ASP A . n 
A 1 454 GLN 454 454 454 GLN GLN A . n 
A 1 455 PHE 455 455 455 PHE PHE A . n 
A 1 456 GLY 456 456 456 GLY GLY A . n 
A 1 457 LYS 457 457 457 LYS LYS A . n 
A 1 458 MET 458 458 458 MET MET A . n 
A 1 459 ILE 459 459 459 ILE ILE A . n 
A 1 460 ASN 460 460 460 ASN ASN A . n 
A 1 461 TRP 461 461 461 TRP TRP A . n 
A 1 462 LEU 462 462 462 LEU LEU A . n 
A 1 463 ALA 463 463 463 ALA ALA A . n 
A 1 464 LYS 464 464 464 LYS LYS A . n 
A 1 465 GLU 465 465 465 GLU GLU A . n 
A 1 466 THR 466 466 466 THR THR A . n 
A 1 467 GLN 467 467 467 GLN GLN A . n 
A 1 468 LYS 468 468 468 LYS LYS A . n 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
1 'John Jumper'               1  
1 'Richard Evans'             2  
1 'Alexander Pritzel'         3  
1 'Tim Green'                 4  
1 'Michael Figurnov'          5  
1 'Olaf Ronneberger'          6  
1 'Kathryn Tunyasuvunakool'   7  
1 'Russ Bates'                8  
1 'Augustin Zidek'            9  
1 'Anna Potapenko'            10 
1 'Alex Bridgland'            11 
1 'Clemens Meyer'             12 
1 'Simon A A Kohl'            13 
1 'Andrew J Ballard'          14 
1 'Andrew Cowie'              15 
1 'Bernardino Romera-Paredes' 16 
1 'Stanislav Nikolov'         17 
1 'Rishub Jain'               18 
1 'Jonas Adler'               19 
1 'Trevor Back'               20 
1 'Stig Petersen'             21 
1 'David Reiman'              22 
1 'Ellen Clancy'              23 
1 'Michal Zielinski'          24 
1 'Martin Steinegger'         25 
1 'Michalina Pacholska'       26 
1 'Tamas Berghammer'          27 
1 'David Silver'              28 
1 'Oriol Vinyals'             29 
1 'Andrew W Senior'           30 
1 'Koray Kavukcuoglu'         31 
1 'Pushmeet Kohli'            32 
1 'Demis Hassabis'            33 
# 
_citation.id                        1 
_citation.title                     'HIGHLY ACCURATE PROTEIN STRUCTURE PREDICTION WITH ALPHAFOLD' 
_citation.journal_abbrev            NATURE 
_citation.journal_volume            596 
_citation.page_first                583 
_citation.year                      2021 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           0028-0836 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   34265844 
_citation.pdbx_database_id_DOI      10.1038/s41586-021-03819-2 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          NAP 
_pdbx_nonpoly_scheme.pdb_seq_num     1 
_pdbx_nonpoly_scheme.auth_seq_num    1 
_pdbx_nonpoly_scheme.pdb_mon_id      NAP 
_pdbx_nonpoly_scheme.auth_mon_id     NAP 
_pdbx_nonpoly_scheme.pdb_strand_id   B 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
_pdbx_entity_nonpoly.comp_id     NAP 
# 
_software.pdbx_ordinal     1 
_software.name             alphafill 
_software.version          2.0.0 
_software.date             2023-03-01T13:35:51Z 
_software.classification   'model annotation' 
# 
