Ticket #14661: 1cbs_final.cif

File 1cbs_final.cif, 253.0 KB (added by r.xie@…, 20 months ago)

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Line 
1data_1CBS
2#
3_entry.id 1CBS
4#
5_audit_conform.dict_name mmcif_pdbx.dic
6_audit_conform.dict_version 5.362
7#
8_pdbx_refine_tls_group.id 1
9_pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION'
10_pdbx_refine_tls_group.refine_tls_id 1
11_pdbx_refine_tls_group.beg_auth_asym_id A
12_pdbx_refine_tls_group.beg_auth_seq_id 1
13_pdbx_refine_tls_group.end_auth_asym_id A
14_pdbx_refine_tls_group.end_auth_seq_id 137
15_pdbx_refine_tls_group.beg_label_asym_id ?
16_pdbx_refine_tls_group.end_label_asym_id ?
17#
18_pdbx_refine_tls.id 1
19_pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION'
20_pdbx_refine_tls.method refined
21_pdbx_refine_tls.origin_x 17.7520
22_pdbx_refine_tls.origin_y 20.9130
23_pdbx_refine_tls.origin_z 27.2690
24_pdbx_refine_tls.T[1][1] 0.0287
25_pdbx_refine_tls.T[2][2] 0.0302
26_pdbx_refine_tls.T[3][3] 0.0137
27_pdbx_refine_tls.T[1][2] 0.0136
28_pdbx_refine_tls.T[1][3] 0.0046
29_pdbx_refine_tls.T[2][3] 0.0139
30_pdbx_refine_tls.L[1][1] 1.5637
31_pdbx_refine_tls.L[2][2] 1.5898
32_pdbx_refine_tls.L[3][3] 1.1883
33_pdbx_refine_tls.L[1][2] -0.1032
34_pdbx_refine_tls.L[1][3] -0.1833
35_pdbx_refine_tls.L[2][3] -0.1312
36_pdbx_refine_tls.S[1][1] 0.0785
37_pdbx_refine_tls.S[1][2] 0.0322
38_pdbx_refine_tls.S[1][3] 0.0090
39_pdbx_refine_tls.S[2][1] -0.0445
40_pdbx_refine_tls.S[2][2] 0.0034
41_pdbx_refine_tls.S[2][3] 0.0691
42_pdbx_refine_tls.S[3][1] -0.1258
43_pdbx_refine_tls.S[3][2] -0.0695
44_pdbx_refine_tls.S[3][3] -0.0819
45#
46loop_
47_refine_ls_restr.type
48_refine_ls_restr.pdbx_refine_id
49_refine_ls_restr.number
50_refine_ls_restr.dev_ideal
51_refine_ls_restr.dev_ideal_target
52r_bond_refined_d 'X-RAY DIFFRACTION' 1129 0.008 0.017
53r_bond_other_d 'X-RAY DIFFRACTION' 1097 0.001 0.016
54r_angle_refined_deg 'X-RAY DIFFRACTION' 1523 1.217 1.840
55r_angle_other_deg 'X-RAY DIFFRACTION' 2534 0.394 1.567
56r_dihedral_angle_1_deg 'X-RAY DIFFRACTION' 143 6.808 5.245
57r_dihedral_angle_2_deg 'X-RAY DIFFRACTION' 10 13.961 5.000
58r_dihedral_angle_3_deg 'X-RAY DIFFRACTION' 215 12.737 10.000
59r_chiral_restr 'X-RAY DIFFRACTION' 174 0.060 0.200
60r_gen_planes_refined 'X-RAY DIFFRACTION' 1303 0.004 0.020
61r_gen_planes_other 'X-RAY DIFFRACTION' 245 0.001 0.020
62r_mcbond_it 'X-RAY DIFFRACTION' 547 1.559 0.867
63r_mcbond_other 'X-RAY DIFFRACTION' 547 1.554 0.867
64r_mcangle_it 'X-RAY DIFFRACTION' 682 2.143 1.545
65r_mcangle_other 'X-RAY DIFFRACTION' 683 2.143 1.546
66r_scbond_it 'X-RAY DIFFRACTION' 582 4.989 1.535
67r_scbond_other 'X-RAY DIFFRACTION' 583 4.985 1.536
68r_scangle_other 'X-RAY DIFFRACTION' 842 7.585 2.474
69r_long_range_B_refined 'X-RAY DIFFRACTION' 1141 8.616 10.390
70r_long_range_B_other 'X-RAY DIFFRACTION' 1128 8.580 9.990
71#
72_refine_ls_shell.d_res_high 1.800
73_refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION'
74_refine_ls_shell.pdbx_total_number_of_bins_used 20
75_refine_ls_shell.d_res_low 1.846
76_refine_ls_shell.number_reflns_R_work 945
77_refine_ls_shell.percent_reflns_obs 89.39
78_refine_ls_shell.R_factor_R_work 0.191
79_refine_ls_shell.number_reflns_R_free 100
80_refine_ls_shell.R_factor_R_free 0.215
81#
82_refine.entry_id 1CBS
83_refine.pdbx_refine_id 'X-RAY DIFFRACTION'
84_refine.pdbx_diffrn_id 1
85_refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD'
86_refine.ls_d_res_high 1.80
87_refine.ls_d_res_low 14.94
88_refine.ls_percent_reflns_obs 90.34
89_refine.ls_number_reflns_obs 13182
90_refine.pdbx_ls_cross_valid_method THROUGHOUT
91_refine.pdbx_R_Free_selection_details RANDOM
92_refine.ls_R_factor_obs 0.15900
93_refine.ls_R_factor_R_work 0.15571
94_refine.ls_R_factor_R_free 0.18842
95_refine.ls_percent_reflns_R_free 10.2
96_refine.ls_number_reflns_R_free 1496
97_refine.B_iso_mean 20.395
98_refine.aniso_B[1][1] 0.33
99_refine.aniso_B[2][2] 0.35
100_refine.aniso_B[3][3] -0.67
101_refine.aniso_B[1][2] 0.00
102_refine.aniso_B[1][3] 0.00
103_refine.aniso_B[2][3] -0.00
104_refine.pdbx_overall_ESU_R 0.114
105_refine.pdbx_overall_ESU_R_Free 0.110
106_refine.overall_SU_ML 0.061
107_refine.overall_SU_B 3.913
108_refine.correlation_coeff_Fo_to_Fc 0.964
109_refine.correlation_coeff_Fo_to_Fc_free 0.948
110_refine.solvent_model_details MASK
111_refine.pdbx_solvent_vdw_probe_radii 1.00
112_refine.pdbx_solvent_ion_probe_radii 0.80
113_refine.pdbx_solvent_shrinkage_radii 0.80
114_refine.details
115;
116U VALUES : WITH TLS ADDED
117HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
118U VALUES : RESIDUAL ONLY
119;
120#
121loop_
122_software.pdbx_ordinal
123_software.name
124_software.classification
125_software.version
126_software.date
1271 REFMAC refinement ? ?
1282 dssp 'model annotation' 4.4.3 2023-10-02T08:50:04Z
129#
130loop_
131_atom_type.symbol
132C
133N
134O
135S
136#
137loop_
138_pdbx_entity_nonpoly.entity_id
139_pdbx_entity_nonpoly.name
140_pdbx_entity_nonpoly.comp_id
1412 RETINOICACID REA
1423 water HOH
143#
144_entity_poly.entity_id 1
145_entity_poly.pdbx_seq_one_letter_code
146;PNFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRP
147CKSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE
148;
149_entity_poly.pdbx_seq_one_letter_code_can
150;PNFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRP
151CKSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE
152;
153_entity_poly.nstd_monomer no
154_entity_poly.pdbx_strand_id A
155_entity_poly.nstd_linkage no
156_entity_poly.type polypeptide(L)
157#
158loop_
159_atom_site_anisotrop.id
160_atom_site_anisotrop.type_symbol
161_atom_site_anisotrop.pdbx_label_atom_id
162_atom_site_anisotrop.pdbx_label_alt_id
163_atom_site_anisotrop.pdbx_label_comp_id
164_atom_site_anisotrop.pdbx_label_asym_id
165_atom_site_anisotrop.pdbx_label_seq_id
166_atom_site_anisotrop.U[1][1]
167_atom_site_anisotrop.U[2][2]
168_atom_site_anisotrop.U[3][3]
169_atom_site_anisotrop.U[1][2]
170_atom_site_anisotrop.U[1][3]
171_atom_site_anisotrop.U[2][3]
172_atom_site_anisotrop.pdbx_auth_seq_id
173_atom_site_anisotrop.pdbx_auth_comp_id
174_atom_site_anisotrop.pdbx_auth_asym_id
175_atom_site_anisotrop.pdbx_auth_atom_id
176_atom_site_anisotrop.pdbx_auth_alt_id
177_atom_site_anisotrop.pdbx_PDB_ins_code
178_atom_site_anisotrop.pdbx_PDB_model_num
1791 N N . PRO A 1 0.4700 0.5002 0.3882 -0.0014 0.0174 0.0706 1 PRO A N ? ? ?
1802 C CA . PRO A 1 0.5067 0.5353 0.4322 -0.0017 0.0084 0.0639 1 PRO A CA ? ? ?
1813 C CB . PRO A 1 0.4657 0.4936 0.4118 -0.0018 0.0103 0.0609 1 PRO A CB ? ? ?
1824 C CG . PRO A 1 0.4502 0.4801 0.3958 -0.0011 0.0201 0.0609 1 PRO A CG ? ? ?
1835 C CD . PRO A 1 0.4627 0.4944 0.3961 -0.0014 0.0250 0.0698 1 PRO A CD ? ? ?
1846 C C . PRO A 1 0.4558 0.4832 0.3676 -0.0019 0.0065 0.0534 1 PRO A C ? ? ?
1857 O O . PRO A 1 0.4375 0.4635 0.3409 -0.0011 0.0136 0.0481 1 PRO A O ? ? ?
1868 N N . ASN A 2 0.3542 0.3821 0.2656 -0.0028 -0.0026 0.0502 2 ASN A N ? ? ?
1879 C CA . ASN A 2 0.3302 0.3564 0.2333 -0.0043 -0.0052 0.0396 2 ASN A CA ? ? ?
18810 C CB . ASN A 2 0.4115 0.4405 0.2989 -0.0059 -0.0130 0.0392 2 ASN A CB ? ? ?
18911 C CG . ASN A 2 0.4967 0.5229 0.3758 -0.0086 -0.0151 0.0272 2 ASN A CG ? ? ?
19012 O OD1 . ASN A 2 0.3543 0.3748 0.2344 -0.0085 -0.0084 0.0200 2 ASN A OD1 ? ? ?
19113 N ND2 . ASN A 2 0.6593 0.6894 0.5310 -0.0111 -0.0246 0.0251 2 ASN A ND2 ? ? ?
19214 C C . ASN A 2 0.2447 0.2701 0.1646 -0.0050 -0.0087 0.0342 2 ASN A C ? ? ?
19315 O O . ASN A 2 0.2539 0.2825 0.1823 -0.0056 -0.0160 0.0356 2 ASN A O ? ? ?
19416 N N . PHE A 3 0.1997 0.2210 0.1240 -0.0045 -0.0029 0.0284 3 PHE A N ? ? ?
19517 C CA . PHE A 3 0.1791 0.1989 0.1165 -0.0050 -0.0047 0.0238 3 PHE A CA ? ? ?
19618 C CB . PHE A 3 0.1733 0.1900 0.1179 -0.0028 0.0021 0.0222 3 PHE A CB ? ? ?
19719 C CG . PHE A 3 0.1732 0.1927 0.1297 -0.0012 0.0039 0.0287 3 PHE A CG ? ? ?
19820 C CD1 . PHE A 3 0.1907 0.2125 0.1443 -0.0004 0.0084 0.0345 3 PHE A CD1 ? ? ?
19921 C CD2 . PHE A 3 0.1988 0.2184 0.1691 -0.0008 0.0016 0.0286 3 PHE A CD2 ? ? ?
20022 C CE1 . PHE A 3 0.1749 0.1993 0.1416 -0.0001 0.0099 0.0401 3 PHE A CE1 ? ? ?
20123 C CE2 . PHE A 3 0.1976 0.2191 0.1790 -0.0001 0.0025 0.0332 3 PHE A CE2 ? ? ?
20224 C CZ . PHE A 3 0.1742 0.1981 0.1549 -0.0002 0.0064 0.0389 3 PHE A CZ ? ? ?
20325 C C . PHE A 3 0.1776 0.1951 0.1098 -0.0079 -0.0079 0.0156 3 PHE A C ? ? ?
20426 O O . PHE A 3 0.1742 0.1906 0.1166 -0.0087 -0.0090 0.0124 3 PHE A O ? ? ?
20527 N N . SER A 4 0.1841 0.2004 0.1001 -0.0097 -0.0090 0.0121 4 SER A N ? ? ?
20628 C CA . SER A 4 0.2101 0.2229 0.1208 -0.0135 -0.0117 0.0032 4 SER A CA ? ? ?
20729 C CB . SER A 4 0.2603 0.2711 0.1498 -0.0152 -0.0125 -0.0011 4 SER A CB ? ? ?
20830 O OG . SER A 4 0.2947 0.2992 0.1740 -0.0121 -0.0029 -0.0027 4 SER A OG ? ? ?
20931 C C . SER A 4 0.2182 0.2371 0.1405 -0.0166 -0.0200 0.0029 4 SER A C ? ? ?
21032 O O . SER A 4 0.1877 0.2145 0.1140 -0.0160 -0.0263 0.0088 4 SER A O ? ? ?
21133 N N . GLY A 5 0.2114 0.2266 0.1401 -0.0196 -0.0196 -0.0036 5 GLY A N ? ? ?
21234 C CA . GLY A 5 0.2465 0.2685 0.1863 -0.0235 -0.0266 -0.0052 5 GLY A CA ? ? ?
21335 C C . GLY A 5 0.2041 0.2220 0.1561 -0.0254 -0.0228 -0.0087 5 GLY A C ? ? ?
21436 O O . GLY A 5 0.1736 0.1826 0.1241 -0.0234 -0.0154 -0.0099 5 GLY A O ? ? ?
21537 N N . ASN A 6 0.1682 0.1936 0.1325 -0.0291 -0.0279 -0.0098 6 ASN A N ? ? ?
21638 C CA . ASN A 6 0.1640 0.1883 0.1421 -0.0309 -0.0242 -0.0112 6 ASN A CA ? ? ?
21739 C CB . ASN A 6 0.1999 0.2276 0.1842 -0.0385 -0.0285 -0.0170 6 ASN A CB ? ? ?
21840 C CG . ASN A 6 0.3358 0.3524 0.3059 -0.0429 -0.0276 -0.0247 6 ASN A CG ? ? ?
21941 O OD1 . ASN A 6 0.3133 0.3168 0.2781 -0.0420 -0.0198 -0.0268 6 ASN A OD1 ? ? ?
22042 N ND2 . ASN A 6 0.4133 0.4341 0.3761 -0.0473 -0.0356 -0.0291 6 ASN A ND2 ? ? ?
22143 C C . ASN A 6 0.1417 0.1743 0.1337 -0.0267 -0.0246 -0.0049 6 ASN A C ? ? ?
22244 O O . ASN A 6 0.1693 0.2129 0.1693 -0.0264 -0.0312 -0.0022 6 ASN A O ? ? ?
22345 N N . TRP A 7 0.1258 0.1530 0.1203 -0.0230 -0.0179 -0.0029 7 TRP A N ? ? ?
22446 C CA . TRP A 7 0.1221 0.1543 0.1266 -0.0184 -0.0173 0.0017 7 TRP A CA ? ? ?
22547 C CB . TRP A 7 0.1323 0.1581 0.1298 -0.0137 -0.0137 0.0046 7 TRP A CB ? ? ?
22648 C CG . TRP A 7 0.1379 0.1630 0.1253 -0.0126 -0.0160 0.0069 7 TRP A CG ? ? ?
22749 C CD1 . TRP A 7 0.1544 0.1738 0.1288 -0.0137 -0.0139 0.0046 7 TRP A CD1 ? ? ?
22850 N NE1 . TRP A 7 0.1785 0.1998 0.1459 -0.0119 -0.0156 0.0085 7 TRP A NE1 ? ? ?
22951 C CE2 . TRP A 7 0.1473 0.1746 0.1238 -0.0098 -0.0193 0.0140 7 TRP A CE2 ? ? ?
23052 C CZ2 . TRP A 7 0.1442 0.1743 0.1187 -0.0077 -0.0217 0.0206 7 TRP A CZ2 ? ? ?
23153 C CH2 . TRP A 7 0.1303 0.1643 0.1168 -0.0054 -0.0250 0.0253 7 TRP A CH2 ? ? ?
23254 C CZ3 . TRP A 7 0.1232 0.1595 0.1230 -0.0049 -0.0255 0.0228 7 TRP A CZ3 ? ? ?
23355 C CE3 . TRP A 7 0.1296 0.1644 0.1305 -0.0072 -0.0226 0.0166 7 TRP A CE3 ? ? ?
23456 C CD2 . TRP A 7 0.1307 0.1604 0.1201 -0.0099 -0.0196 0.0125 7 TRP A CD2 ? ? ?
23557 C C . TRP A 7 0.1474 0.1812 0.1635 -0.0190 -0.0131 0.0007 7 TRP A C ? ? ?
23658 O O . TRP A 7 0.1427 0.1695 0.1560 -0.0211 -0.0078 -0.0017 7 TRP A O ? ? ?
23759 N N . LYS A 8 0.1205 0.1632 0.1494 -0.0167 -0.0149 0.0029 8 LYS A N ? ? ?
23860 C CA . LYS A 8 0.1539 0.1993 0.1934 -0.0164 -0.0097 0.0022 8 LYS A CA ? ? ?
23961 C CB . LYS A 8 0.2372 0.2950 0.2923 -0.0197 -0.0127 0.0015 8 LYS A CB ? ? ?
24062 C CG . LYS A 8 0.2955 0.3638 0.3608 -0.0160 -0.0194 0.0046 8 LYS A CG ? ? ?
24163 C CD . LYS A 8 0.4530 0.5363 0.5358 -0.0194 -0.0239 0.0041 8 LYS A CD ? ? ?
24264 C CE . LYS A 8 0.5265 0.6153 0.6239 -0.0209 -0.0165 0.0025 8 LYS A CE ? ? ?
24365 N NZ . LYS A 8 0.6055 0.6943 0.7087 -0.0137 -0.0105 0.0041 8 LYS A NZ ? ? ?
24466 C C . LYS A 8 0.1355 0.1802 0.1776 -0.0102 -0.0075 0.0043 8 LYS A C ? ? ?
24567 O O . LYS A 8 0.1282 0.1746 0.1717 -0.0068 -0.0118 0.0070 8 LYS A O ? ? ?
24668 N N . ILE A 9 0.1034 0.1442 0.1448 -0.0088 -0.0007 0.0032 9 ILE A N ? ? ?
24769 C CA . ILE A 9 0.0926 0.1307 0.1335 -0.0034 0.0013 0.0035 9 ILE A CA ? ? ?
24870 C CB . ILE A 9 0.1117 0.1428 0.1438 -0.0027 0.0080 0.0021 9 ILE A CB ? ? ?
24971 C CG1 . ILE A 9 0.1472 0.1733 0.1737 0.0020 0.0080 0.0015 9 ILE A CG1 ? ? ?
25072 C CG2 . ILE A 9 0.1509 0.1863 0.1895 -0.0039 0.0144 0.0011 9 ILE A CG2 ? ? ?
25173 C CD1 . ILE A 9 0.1774 0.1964 0.1916 0.0026 0.0118 0.0011 9 ILE A CD1 ? ? ?
25274 C C . ILE A 9 0.0930 0.1394 0.1483 -0.0002 0.0011 0.0035 9 ILE A C ? ? ?
25375 O O . ILE A 9 0.0977 0.1524 0.1641 -0.0019 0.0030 0.0029 9 ILE A O ? ? ?
25476 N N . ILE A 10 0.0886 0.1325 0.1453 0.0045 -0.0008 0.0041 10 ILE A N ? ? ?
25577 C CA . ILE A 10 0.1078 0.1568 0.1778 0.0091 0.0000 0.0035 10 ILE A CA ? ? ?
25678 C CB . ILE A 10 0.1491 0.2024 0.2282 0.0111 -0.0074 0.0077 10 ILE A CB ? ? ?
25779 C CG1 . ILE A 10 0.1758 0.2203 0.2458 0.0118 -0.0112 0.0103 10 ILE A CG1 ? ? ?
25880 C CG2 . ILE A 10 0.1732 0.2361 0.2569 0.0071 -0.0123 0.0101 10 ILE A CG2 ? ? ?
25981 C CD1 . ILE A 10 0.2008 0.2476 0.2800 0.0152 -0.0173 0.0158 10 ILE A CD1 ? ? ?
26082 C C . ILE A 10 0.1173 0.1591 0.1836 0.0134 0.0044 0.0000 10 ILE A C ? ? ?
26183 O O . ILE A 10 0.1208 0.1655 0.1968 0.0176 0.0076 -0.0021 10 ILE A O ? ? ?
26284 N N . ARG A 11 0.1044 0.1373 0.1569 0.0126 0.0045 -0.0011 11 ARG A N ? ? ?
26385 C CA . ARG A 11 0.1164 0.1423 0.1627 0.0157 0.0074 -0.0054 11 ARG A CA ? ? ?
26486 C CB . ARG A 11 0.1460 0.1667 0.1970 0.0183 0.0029 -0.0056 11 ARG A CB ? ? ?
26587 C CG . ARG A 11 0.1871 0.1997 0.2315 0.0205 0.0044 -0.0115 11 ARG A CG ? ? ?
26688 C CD . ARG A 11 0.1931 0.1991 0.2438 0.0217 -0.0002 -0.0114 11 ARG A CD ? ? ?
26789 N NE . ARG A 11 0.2138 0.2209 0.2788 0.0258 0.0000 -0.0105 11 ARG A NE ? ? ?
26890 C CZ . ARG A 11 0.2776 0.2810 0.3476 0.0305 0.0038 -0.0162 11 ARG A CZ ? ? ?
26991 N NH1 . ARG A 11 0.2610 0.2606 0.3209 0.0315 0.0083 -0.0238 11 ARG A NH1 ? ? ?
27092 N NH2 . ARG A 11 0.2671 0.2705 0.3520 0.0349 0.0031 -0.0143 11 ARG A NH2 ? ? ?
27193 C C . ARG A 11 0.1134 0.1336 0.1444 0.0136 0.0081 -0.0061 11 ARG A C ? ? ?
27294 O O . ARG A 11 0.1072 0.1260 0.1339 0.0110 0.0046 -0.0030 11 ARG A O ? ? ?
27395 N N . SER A 12 0.1223 0.1396 0.1449 0.0153 0.0129 -0.0098 12 SER A N ? ? ?
27496 C CA . SER A 12 0.1259 0.1378 0.1339 0.0147 0.0123 -0.0103 12 SER A CA ? ? ?
27597 C CB . SER A 12 0.1375 0.1501 0.1379 0.0129 0.0174 -0.0078 12 SER A CB ? ? ?
27698 O OG . SER A 12 0.1387 0.1462 0.1255 0.0133 0.0161 -0.0069 12 SER A OG ? ? ?
27799 C C . SER A 12 0.1397 0.1470 0.1404 0.0179 0.0130 -0.0162 12 SER A C ? ? ?
278100 O O . SER A 12 0.1606 0.1686 0.1610 0.0204 0.0186 -0.0198 12 SER A O ? ? ?
279101 N N . GLU A 13 0.1184 0.1213 0.1136 0.0176 0.0073 -0.0175 13 GLU A N ? ? ?
280102 C CA . GLU A 13 0.1518 0.1499 0.1385 0.0196 0.0062 -0.0242 13 GLU A CA ? ? ?
281103 C CB . GLU A 13 0.1557 0.1498 0.1521 0.0195 0.0010 -0.0277 13 GLU A CB ? ? ?
282104 C CG . GLU A 13 0.1947 0.1890 0.2055 0.0213 0.0033 -0.0277 13 GLU A CG ? ? ?
283105 C CD . GLU A 13 0.2543 0.2461 0.2651 0.0256 0.0089 -0.0346 13 GLU A CD ? ? ?
284106 O OE1 . GLU A 13 0.2754 0.2635 0.2726 0.0270 0.0108 -0.0410 13 GLU A OE1 ? ? ?
285107 O OE2 . GLU A 13 0.3092 0.3032 0.3335 0.0281 0.0115 -0.0335 13 GLU A OE2 ? ? ?
286108 C C . GLU A 13 0.1438 0.1408 0.1173 0.0188 0.0024 -0.0234 13 GLU A C ? ? ?
287109 O O . GLU A 13 0.1221 0.1206 0.0989 0.0167 -0.0022 -0.0191 13 GLU A O ? ? ?
288110 N N . ASN A 14 0.1566 0.1514 0.1151 0.0210 0.0045 -0.0273 14 ASN A N ? ? ?
289111 C CA . ASN A 14 0.1711 0.1651 0.1165 0.0211 -0.0009 -0.0278 14 ASN A CA ? ? ?
290112 C CB . ASN A 14 0.1578 0.1512 0.1111 0.0189 -0.0101 -0.0309 14 ASN A CB ? ? ?
291113 C CG . ASN A 14 0.1889 0.1795 0.1305 0.0195 -0.0156 -0.0389 14 ASN A CG ? ? ?
292114 O OD1 . ASN A 14 0.2005 0.1878 0.1280 0.0221 -0.0119 -0.0445 14 ASN A OD1 ? ? ?
293115 N ND2 . ASN A 14 0.1774 0.1697 0.1243 0.0168 -0.0245 -0.0400 14 ASN A ND2 ? ? ?
294116 C C . ASN A 14 0.1628 0.1591 0.1026 0.0210 -0.0004 -0.0196 14 ASN A C ? ? ?
295117 O O . ASN A 14 0.1584 0.1557 0.0923 0.0214 -0.0064 -0.0180 14 ASN A O ? ? ?
296118 N N . PHE A 15 0.1524 0.1495 0.0949 0.0205 0.0065 -0.0146 15 PHE A N ? ? ?
297119 C CA . PHE A 15 0.1557 0.1525 0.0938 0.0203 0.0077 -0.0073 15 PHE A CA ? ? ?
298120 C CB . PHE A 15 0.1652 0.1624 0.1108 0.0181 0.0146 -0.0034 15 PHE A CB ? ? ?
299121 C CG . PHE A 15 0.1711 0.1655 0.1140 0.0175 0.0161 0.0033 15 PHE A CG ? ? ?
300122 C CD1 . PHE A 15 0.2366 0.2310 0.1842 0.0172 0.0110 0.0057 15 PHE A CD1 ? ? ?
301123 C CD2 . PHE A 15 0.2013 0.1923 0.1372 0.0172 0.0234 0.0074 15 PHE A CD2 ? ? ?
302124 C CE1 . PHE A 15 0.2499 0.2403 0.1953 0.0174 0.0131 0.0111 15 PHE A CE1 ? ? ?
303125 C CE2 . PHE A 15 0.2191 0.2053 0.1533 0.0166 0.0250 0.0134 15 PHE A CE2 ? ? ?
304126 C CZ . PHE A 15 0.2304 0.2158 0.1690 0.0171 0.0198 0.0148 15 PHE A CZ ? ? ?
305127 C C . PHE A 15 0.1759 0.1702 0.0952 0.0232 0.0087 -0.0054 15 PHE A C ? ? ?
306128 O O . PHE A 15 0.1830 0.1770 0.0970 0.0246 0.0045 -0.0009 15 PHE A O ? ? ?
307129 N N . GLU A 16 0.1967 0.1896 0.1055 0.0248 0.0145 -0.0084 16 GLU A N ? ? ?
308130 C CA . GLU A 16 0.2365 0.2269 0.1245 0.0278 0.0158 -0.0060 16 GLU A CA ? ? ?
309131 C CB . GLU A 16 0.2932 0.2825 0.1702 0.0292 0.0250 -0.0093 16 GLU A CB ? ? ?
310132 C CG . GLU A 16 0.3492 0.3355 0.2014 0.0326 0.0261 -0.0059 16 GLU A CG ? ? ?
311133 C CD . GLU A 16 0.4037 0.3885 0.2432 0.0339 0.0385 -0.0042 16 GLU A CD ? ? ?
312134 O OE1 . GLU A 16 0.4230 0.4101 0.2737 0.0326 0.0468 -0.0077 16 GLU A OE1 ? ? ?
313135 O OE2 . GLU A 16 0.4517 0.4334 0.2702 0.0365 0.0403 0.0014 16 GLU A OE2 ? ? ?
314136 C C . GLU A 16 0.2293 0.2206 0.1080 0.0296 0.0051 -0.0091 16 GLU A C ? ? ?
315137 O O . GLU A 16 0.2285 0.2194 0.0951 0.0321 0.0017 -0.0036 16 GLU A O ? ? ?
316138 N N . GLU A 17 0.2134 0.2061 0.0988 0.0284 -0.0006 -0.0177 17 GLU A N ? ? ?
317139 C CA . GLU A 17 0.2396 0.2341 0.1196 0.0288 -0.0116 -0.0220 17 GLU A CA ? ? ?
318140 C CB . GLU A 17 0.2742 0.2674 0.1633 0.0265 -0.0152 -0.0326 17 GLU A CB ? ? ?
319141 C CG . GLU A 17 0.3467 0.3351 0.2249 0.0283 -0.0086 -0.0408 17 GLU A CG ? ? ?
320142 C CD . GLU A 17 0.4263 0.4136 0.3120 0.0290 0.0034 -0.0396 17 GLU A CD ? ? ?
321143 O OE1 . GLU A 17 0.3113 0.3012 0.2109 0.0275 0.0068 -0.0323 17 GLU A OE1 ? ? ?
322144 O OE2 . GLU A 17 0.5838 0.5680 0.4612 0.0313 0.0094 -0.0466 17 GLU A OE2 ? ? ?
323145 C C . GLU A 17 0.2077 0.2067 0.0971 0.0283 -0.0191 -0.0156 17 GLU A C ? ? ?
324146 O O . GLU A 17 0.2168 0.2190 0.0980 0.0300 -0.0272 -0.0145 17 GLU A O ? ? ?
325147 N N . LEU A 18 0.1828 0.1828 0.0895 0.0263 -0.0163 -0.0112 18 LEU A N ? ? ?
326148 C CA . LEU A 18 0.1764 0.1802 0.0923 0.0265 -0.0206 -0.0048 18 LEU A CA ? ? ?
327149 C CB . LEU A 18 0.1759 0.1795 0.1080 0.0240 -0.0159 -0.0022 18 LEU A CB ? ? ?
328150 C CG . LEU A 18 0.2003 0.2071 0.1424 0.0245 -0.0180 0.0037 18 LEU A CG ? ? ?
329151 C CD1 . LEU A 18 0.2242 0.2375 0.1781 0.0228 -0.0256 0.0011 18 LEU A CD1 ? ? ?
330152 C CD2 . LEU A 18 0.2176 0.2218 0.1684 0.0226 -0.0114 0.0064 18 LEU A CD2 ? ? ?
331153 C C . LEU A 18 0.1898 0.1923 0.0932 0.0306 -0.0194 0.0032 18 LEU A C ? ? ?
332154 O O . LEU A 18 0.1884 0.1953 0.0915 0.0331 -0.0266 0.0065 18 LEU A O ? ? ?
333155 N N . LEU A 19 0.2086 0.2052 0.1029 0.0314 -0.0103 0.0068 19 LEU A N ? ? ?
334156 C CA . LEU A 19 0.2244 0.2173 0.1064 0.0352 -0.0078 0.0155 19 LEU A CA ? ? ?
335157 C CB . LEU A 19 0.2397 0.2258 0.1176 0.0339 0.0041 0.0189 19 LEU A CB ? ? ?
336158 C CG . LEU A 19 0.2425 0.2271 0.1377 0.0299 0.0095 0.0192 19 LEU A CG ? ? ?
337159 C CD1 . LEU A 19 0.2834 0.2625 0.1753 0.0279 0.0204 0.0227 19 LEU A CD1 ? ? ?
338160 C CD2 . LEU A 19 0.2477 0.2319 0.1527 0.0308 0.0062 0.0236 19 LEU A CD2 ? ? ?
339161 C C . LEU A 19 0.2454 0.2397 0.1080 0.0391 -0.0140 0.0159 19 LEU A C ? ? ?
340162 O O . LEU A 19 0.2468 0.2410 0.1026 0.0433 -0.0174 0.0236 19 LEU A O ? ? ?
341163 N N . LYS A 20 0.2550 0.2505 0.1082 0.0382 -0.0157 0.0075 20 LYS A N ? ? ?
342164 C CA . LYS A 20 0.3030 0.3003 0.1356 0.0413 -0.0227 0.0058 20 LYS A CA ? ? ?
343165 C CB . LYS A 20 0.3697 0.3657 0.1931 0.0396 -0.0216 -0.0059 20 LYS A CB ? ? ?
344166 C CG . LYS A 20 0.5036 0.4979 0.2980 0.0431 -0.0229 -0.0071 20 LYS A CG ? ? ?
345167 C CD . LYS A 20 0.6083 0.6009 0.3929 0.0417 -0.0233 -0.0211 20 LYS A CD ? ? ?
346168 C CE . LYS A 20 0.7528 0.7413 0.5473 0.0397 -0.0111 -0.0261 20 LYS A CE ? ? ?
347169 N NZ . LYS A 20 0.7659 0.7512 0.5531 0.0415 0.0028 -0.0177 20 LYS A NZ ? ? ?
348170 C C . LYS A 20 0.2829 0.2882 0.1220 0.0425 -0.0364 0.0063 20 LYS A C ? ? ?
349171 O O . LYS A 20 0.2827 0.2903 0.1090 0.0470 -0.0424 0.0123 20 LYS A O ? ? ?
350172 N N . VAL A 21 0.2590 0.2693 0.1190 0.0387 -0.0414 0.0007 21 VAL A N ? ? ?
351173 C CA . VAL A 21 0.2656 0.2855 0.1371 0.0389 -0.0534 0.0013 21 VAL A CA ? ? ?
352174 C CB . VAL A 21 0.3233 0.3468 0.2177 0.0332 -0.0558 -0.0055 21 VAL A CB ? ? ?
353175 C CG1 . VAL A 21 0.3879 0.4226 0.2999 0.0330 -0.0655 -0.0028 21 VAL A CG1 ? ? ?
354176 C CG2 . VAL A 21 0.3544 0.3751 0.2432 0.0295 -0.0584 -0.0175 21 VAL A CG2 ? ? ?
355177 C C . VAL A 21 0.2464 0.2686 0.1237 0.0435 -0.0535 0.0130 21 VAL A C ? ? ?
356178 O O . VAL A 21 0.2204 0.2507 0.0985 0.0468 -0.0633 0.0166 21 VAL A O ? ? ?
357179 N N . LEU A 22 0.2410 0.2562 0.1231 0.0439 -0.0426 0.0187 22 LEU A N ? ? ?
358180 C CA . LEU A 22 0.2564 0.2708 0.1445 0.0484 -0.0409 0.0289 22 LEU A CA ? ? ?
359181 C CB . LEU A 22 0.2364 0.2441 0.1365 0.0458 -0.0303 0.0302 22 LEU A CB ? ? ?
360182 C CG . LEU A 22 0.2559 0.2691 0.1765 0.0411 -0.0312 0.0244 22 LEU A CG ? ? ?
361183 C CD1 . LEU A 22 0.2693 0.2756 0.1974 0.0384 -0.0213 0.0251 22 LEU A CD1 ? ? ?
362184 C CD2 . LEU A 22 0.2816 0.3049 0.2168 0.0434 -0.0387 0.0267 22 LEU A CD2 ? ? ?
363185 C C . LEU A 22 0.2826 0.2917 0.1504 0.0543 -0.0399 0.0378 22 LEU A C ? ? ?
364186 O O . LEU A 22 0.2883 0.2952 0.1594 0.0592 -0.0388 0.0470 22 LEU A O ? ? ?
365187 N N . GLY A 23 0.2885 0.2945 0.1348 0.0542 -0.0393 0.0352 23 GLY A N ? ? ?
366188 C CA . GLY A 23 0.3252 0.3271 0.1486 0.0598 -0.0396 0.0437 23 GLY A CA ? ? ?
367189 C C . GLY A 23 0.3298 0.3190 0.1444 0.0605 -0.0257 0.0516 23 GLY A C ? ? ?
368190 O O . GLY A 23 0.3510 0.3348 0.1508 0.0657 -0.0245 0.0621 23 GLY A O ? ? ?
369191 N N . VAL A 24 0.2905 0.2749 0.1150 0.0549 -0.0155 0.0470 24 VAL A N ? ? ?
370192 C CA . VAL A 24 0.2910 0.2645 0.1099 0.0538 -0.0024 0.0531 24 VAL A CA ? ? ?
371193 C CB . VAL A 24 0.2723 0.2437 0.1109 0.0476 0.0054 0.0481 24 VAL A CB ? ? ?
372194 C CG1 . VAL A 24 0.2686 0.2297 0.1040 0.0454 0.0184 0.0543 24 VAL A CG1 ? ? ?
373195 C CG2 . VAL A 24 0.2582 0.2323 0.1173 0.0475 0.0008 0.0476 24 VAL A CG2 ? ? ?
374196 C C . VAL A 24 0.3217 0.2928 0.1173 0.0539 0.0028 0.0524 24 VAL A C ? ? ?
375197 O O . VAL A 24 0.3092 0.2851 0.1015 0.0515 0.0016 0.0422 24 VAL A O ? ? ?
376198 N N . ASN A 25 0.3216 0.2844 0.1014 0.0569 0.0098 0.0634 25 ASN A N ? ? ?
377199 C CA . ASN A 25 0.3785 0.3391 0.1331 0.0579 0.0155 0.0645 25 ASN A CA ? ? ?
378200 C CB . ASN A 25 0.4238 0.3756 0.1591 0.0631 0.0193 0.0799 25 ASN A CB ? ? ?
379201 C CG . ASN A 25 0.4848 0.4248 0.2283 0.0606 0.0327 0.0898 25 ASN A CG ? ? ?
380202 O OD1 . ASN A 25 0.4690 0.4072 0.2239 0.0543 0.0434 0.0857 25 ASN A OD1 ? ? ?
381203 N ND2 . ASN A 25 0.5159 0.4472 0.2539 0.0656 0.0324 0.1036 25 ASN A ND2 ? ? ?
382204 C C . ASN A 25 0.3640 0.3230 0.1238 0.0521 0.0286 0.0586 25 ASN A C ? ? ?
383205 O O . ASN A 25 0.3363 0.2944 0.1182 0.0474 0.0334 0.0564 25 ASN A O ? ? ?
384206 N N . VAL A 26 0.3978 0.3573 0.1368 0.0529 0.0342 0.0561 26 VAL A N ? ? ?
385207 C CA . VAL A 26 0.4036 0.3644 0.1475 0.0486 0.0459 0.0489 26 VAL A CA ? ? ?
386208 C CB . VAL A 26 0.4934 0.4542 0.2080 0.0516 0.0516 0.0473 26 VAL A CB ? ? ?
387209 C CG1 . VAL A 26 0.5340 0.4962 0.2545 0.0480 0.0666 0.0422 26 VAL A CG1 ? ? ?
388210 C CG2 . VAL A 26 0.5184 0.4844 0.2188 0.0547 0.0382 0.0369 26 VAL A CG2 ? ? ?
389211 C C . VAL A 26 0.3708 0.3267 0.1311 0.0438 0.0590 0.0553 26 VAL A C ? ? ?
390212 O O . VAL A 26 0.3528 0.3125 0.1339 0.0391 0.0628 0.0483 26 VAL A O ? ? ?
391213 N N . MET A 27 0.3762 0.3235 0.1274 0.0449 0.0654 0.0688 27 MET A N ? ? ?
392214 C CA . MET A 27 0.3798 0.3215 0.1457 0.0395 0.0781 0.0750 27 MET A CA ? ? ?
393215 C CB . MET A 27 0.4334 0.3639 0.1827 0.0414 0.0860 0.0908 27 MET A CB ? ? ?
394216 C CG . MET A 27 0.5444 0.4749 0.2729 0.0417 0.0992 0.0947 27 MET A CG ? ? ?
395217 S SD . MET A 27 0.7077 0.6381 0.3956 0.0507 0.0928 0.0986 27 MET A SD ? ? ?
396218 C CE . MET A 27 0.6607 0.5913 0.3297 0.0492 0.1127 0.1018 27 MET A CE ? ? ?
397219 C C . MET A 27 0.3643 0.3050 0.1578 0.0355 0.0735 0.0726 27 MET A C ? ? ?
398220 O O . MET A 27 0.3441 0.2863 0.1567 0.0293 0.0804 0.0693 27 MET A O ? ? ?
399221 N N . LEU A 28 0.3356 0.2750 0.1316 0.0392 0.0618 0.0737 28 LEU A N ? ? ?
400222 C CA . LEU A 28 0.3050 0.2437 0.1247 0.0360 0.0579 0.0706 28 LEU A CA ? ? ?
401223 C CB . LEU A 28 0.3082 0.2438 0.1274 0.0417 0.0476 0.0752 28 LEU A CB ? ? ?
402224 C CG . LEU A 28 0.3420 0.2645 0.1534 0.0450 0.0518 0.0889 28 LEU A CG ? ? ?
403225 C CD1 . LEU A 28 0.3525 0.2746 0.1639 0.0523 0.0408 0.0931 28 LEU A CD1 ? ? ?
404226 C CD2 . LEU A 28 0.3187 0.2311 0.1457 0.0388 0.0616 0.0913 28 LEU A CD2 ? ? ?
405227 C C . LEU A 28 0.2886 0.2378 0.1238 0.0326 0.0537 0.0576 28 LEU A C ? ? ?
406228 O O . LEU A 28 0.2680 0.2177 0.1226 0.0277 0.0554 0.0542 28 LEU A O ? ? ?
407229 N N . ARG A 29 0.2909 0.2479 0.1171 0.0351 0.0480 0.0504 29 ARG A N ? ? ?
408230 C CA . ARG A 29 0.2965 0.2618 0.1366 0.0323 0.0449 0.0388 29 ARG A CA ? ? ?
409231 C CB . ARG A 29 0.3475 0.3184 0.1748 0.0356 0.0383 0.0311 29 ARG A CB ? ? ?
410232 C CG . ARG A 29 0.3850 0.3594 0.2141 0.0380 0.0245 0.0286 29 ARG A CG ? ? ?
411233 C CD . ARG A 29 0.4831 0.4630 0.3077 0.0385 0.0182 0.0175 29 ARG A CD ? ? ?
412234 N NE . ARG A 29 0.6505 0.6312 0.4539 0.0428 0.0104 0.0181 29 ARG A NE ? ? ?
413235 C CZ . ARG A 29 0.5286 0.5075 0.3083 0.0454 0.0142 0.0176 29 ARG A CZ ? ? ?
414236 N NH1 . ARG A 29 0.6127 0.5912 0.3877 0.0442 0.0226 0.0104 29 ARG A NH1 ? ? ?
415237 N NH2 . ARG A 29 0.4765 0.4542 0.2359 0.0498 0.0091 0.0246 29 ARG A NH2 ? ? ?
416238 C C . ARG A 29 0.3165 0.2837 0.1675 0.0273 0.0560 0.0363 29 ARG A C ? ? ?
417239 O O . ARG A 29 0.2701 0.2415 0.1405 0.0236 0.0549 0.0310 29 ARG A O ? ? ?
418240 N N . LYS A 30 0.3204 0.2854 0.1587 0.0275 0.0665 0.0407 30 LYS A N ? ? ?
419241 C CA . LYS A 30 0.3928 0.3612 0.2423 0.0230 0.0782 0.0395 30 LYS A CA ? ? ?
420242 C CB . LYS A 30 0.4642 0.4289 0.2951 0.0242 0.0903 0.0469 30 LYS A CB ? ? ?
421243 C CG . LYS A 30 0.5678 0.5392 0.4077 0.0208 0.1035 0.0446 30 LYS A CG ? ? ?
422244 C CD . LYS A 30 0.6462 0.6149 0.4629 0.0233 0.1154 0.0511 30 LYS A CD ? ? ?
423245 C CE . LYS A 30 0.7776 0.7545 0.6033 0.0209 0.1299 0.0485 30 LYS A CE ? ? ?
424246 N NZ . LYS A 30 0.8560 0.8341 0.7055 0.0132 0.1383 0.0545 30 LYS A NZ ? ? ?
425247 C C . LYS A 30 0.3534 0.3201 0.2252 0.0169 0.0800 0.0420 30 LYS A C ? ? ?
426248 O O . LYS A 30 0.3621 0.3359 0.2529 0.0131 0.0807 0.0360 30 LYS A O ? ? ?
427249 N N . ILE A 31 0.3337 0.2905 0.2025 0.0164 0.0799 0.0506 31 ILE A N ? ? ?
428250 C CA . ILE A 31 0.3088 0.2612 0.1956 0.0106 0.0813 0.0524 31 ILE A CA ? ? ?
429251 C CB . ILE A 31 0.3255 0.2637 0.2035 0.0121 0.0823 0.0628 31 ILE A CB ? ? ?
430252 C CG1 . ILE A 31 0.3486 0.2806 0.2119 0.0123 0.0937 0.0728 31 ILE A CG1 ? ? ?
431253 C CG2 . ILE A 31 0.3120 0.2434 0.2074 0.0066 0.0822 0.0628 31 ILE A CG2 ? ? ?
432254 C CD1 . ILE A 31 0.3824 0.2991 0.2333 0.0157 0.0946 0.0850 31 ILE A CD1 ? ? ?
433255 C C . ILE A 31 0.3108 0.2687 0.2133 0.0094 0.0715 0.0442 31 ILE A C ? ? ?
434256 O O . ILE A 31 0.2643 0.2263 0.1845 0.0038 0.0728 0.0402 31 ILE A O ? ? ?
435257 N N . ALA A 32 0.2521 0.2104 0.1480 0.0146 0.0616 0.0421 32 ALA A N ? ? ?
436258 C CA . ALA A 32 0.2368 0.1992 0.1454 0.0139 0.0529 0.0360 32 ALA A CA ? ? ?
437259 C CB . ALA A 32 0.2481 0.2105 0.1482 0.0198 0.0435 0.0362 32 ALA A CB ? ? ?
438260 C C . ALA A 32 0.2217 0.1945 0.1420 0.0116 0.0517 0.0277 32 ALA A C ? ? ?
439261 O O . ALA A 32 0.1976 0.1734 0.1327 0.0079 0.0493 0.0243 32 ALA A O ? ? ?
440262 N N . VAL A 33 0.2417 0.2195 0.1546 0.0141 0.0533 0.0245 33 VAL A N ? ? ?
441263 C CA . VAL A 33 0.2446 0.2311 0.1687 0.0134 0.0521 0.0167 33 VAL A CA ? ? ?
442264 C CB . VAL A 33 0.2729 0.2619 0.1846 0.0176 0.0537 0.0124 33 VAL A CB ? ? ?
443265 C CG1 . VAL A 33 0.3322 0.3287 0.2573 0.0173 0.0549 0.0049 33 VAL A CG1 ? ? ?
444266 C CG2 . VAL A 33 0.3073 0.2939 0.2058 0.0218 0.0443 0.0106 33 VAL A CG2 ? ? ?
445267 C C . VAL A 33 0.2310 0.2223 0.1718 0.0082 0.0588 0.0165 33 VAL A C ? ? ?
446268 O O . VAL A 33 0.2498 0.2471 0.2059 0.0062 0.0549 0.0123 33 VAL A O ? ? ?
447269 N N . ALA A 34 0.2336 0.2225 0.1720 0.0057 0.0685 0.0218 34 ALA A N ? ? ?
448270 C CA . ALA A 34 0.2413 0.2362 0.1976 -0.0001 0.0748 0.0219 34 ALA A CA ? ? ?
449271 C CB . ALA A 34 0.2693 0.2609 0.2205 -0.0025 0.0869 0.0286 34 ALA A CB ? ? ?
450272 C C . ALA A 34 0.2702 0.2637 0.2400 -0.0051 0.0690 0.0215 34 ALA A C ? ? ?
451273 O O . ALA A 34 0.2510 0.2532 0.2378 -0.0083 0.0666 0.0175 34 ALA A O ? ? ?
452274 N N . ALA A 35 0.2125 0.1952 0.1742 -0.0053 0.0663 0.0253 35 ALA A N ? ? ?
453275 C CA . ALA A 35 0.2065 0.1857 0.1781 -0.0100 0.0621 0.0243 35 ALA A CA ? ? ?
454276 C CB . ALA A 35 0.2301 0.1950 0.1915 -0.0093 0.0629 0.0296 35 ALA A CB ? ? ?
455277 C C . ALA A 35 0.1970 0.1817 0.1738 -0.0083 0.0522 0.0186 35 ALA A C ? ? ?
456278 O O . ALA A 35 0.1804 0.1683 0.1686 -0.0127 0.0488 0.0156 35 ALA A O ? ? ?
457279 N N . ALA A 36 0.1709 0.1566 0.1388 -0.0023 0.0475 0.0174 36 ALA A N ? ? ?
458280 C CA . ALA A 36 0.1892 0.1792 0.1618 -0.0008 0.0390 0.0132 36 ALA A CA ? ? ?
459281 C CB . ALA A 36 0.1901 0.1779 0.1515 0.0049 0.0344 0.0134 36 ALA A CB ? ? ?
460282 C C . ALA A 36 0.1759 0.1763 0.1610 -0.0017 0.0373 0.0089 36 ALA A C ? ? ?
461283 O O . ALA A 36 0.1907 0.1944 0.1807 -0.0010 0.0308 0.0065 36 ALA A O ? ? ?
462284 N N . SER A 37 0.1802 0.1860 0.1712 -0.0030 0.0437 0.0087 37 SER A N ? ? ?
463285 C CA . SER A 37 0.2079 0.2242 0.2127 -0.0026 0.0426 0.0051 37 SER A CA ? ? ?
464286 C CB . SER A 37 0.2292 0.2503 0.2357 -0.0012 0.0515 0.0047 37 SER A CB ? ? ?
465287 O OG . SER A 37 0.3201 0.3438 0.3347 -0.0066 0.0583 0.0077 37 SER A OG ? ? ?
466288 C C . SER A 37 0.2317 0.2543 0.2520 -0.0078 0.0391 0.0045 37 SER A C ? ? ?
467289 O O . SER A 37 0.2311 0.2623 0.2629 -0.0067 0.0352 0.0023 37 SER A O ? ? ?
468290 N N . LYS A 38 0.2232 0.2412 0.2434 -0.0131 0.0398 0.0062 38 LYS A N ? ? ?
469291 C CA . LYS A 38 0.2467 0.2701 0.2791 -0.0186 0.0350 0.0046 38 LYS A CA ? ? ?
470292 C CB . LYS A 38 0.3776 0.4091 0.4251 -0.0242 0.0405 0.0049 38 LYS A CB ? ? ?
471293 C CG . LYS A 38 0.5514 0.5753 0.5939 -0.0271 0.0502 0.0084 38 LYS A CG ? ? ?
472294 C CD . LYS A 38 0.6917 0.7261 0.7519 -0.0326 0.0573 0.0094 38 LYS A CD ? ? ?
473295 C CE . LYS A 38 0.7999 0.8432 0.8637 -0.0274 0.0644 0.0100 38 LYS A CE ? ? ?
474296 N NZ . LYS A 38 0.9203 0.9746 0.9932 -0.0223 0.0582 0.0064 38 LYS A NZ ? ? ?
475297 C C . LYS A 38 0.2004 0.2137 0.2245 -0.0214 0.0315 0.0044 38 LYS A C ? ? ?
476298 O O . LYS A 38 0.2473 0.2564 0.2740 -0.0273 0.0336 0.0042 38 LYS A O ? ? ?
477299 N N . PRO A 39 0.1688 0.1779 0.1837 -0.0174 0.0262 0.0039 39 PRO A N ? ? ?
478300 C CA . PRO A 39 0.1790 0.1791 0.1861 -0.0188 0.0238 0.0033 39 PRO A CA ? ? ?
479301 C CB . PRO A 39 0.1675 0.1655 0.1660 -0.0126 0.0208 0.0042 39 PRO A CB ? ? ?
480302 C CG . PRO A 39 0.1735 0.1811 0.1787 -0.0101 0.0178 0.0036 39 PRO A CG ? ? ?
481303 C CD . PRO A 39 0.1610 0.1741 0.1743 -0.0116 0.0227 0.0036 39 PRO A CD ? ? ?
482304 C C . PRO A 39 0.1787 0.1831 0.1916 -0.0236 0.0181 -0.0002 39 PRO A C ? ? ?
483305 O O . PRO A 39 0.1895 0.2052 0.2122 -0.0243 0.0139 -0.0010 39 PRO A O ? ? ?
484306 N N . ALA A 40 0.1650 0.1602 0.1717 -0.0266 0.0179 -0.0022 40 ALA A N ? ? ?
485307 C CA . ALA A 40 0.1814 0.1787 0.1875 -0.0301 0.0117 -0.0062 40 ALA A CA ? ? ?
486308 C CB . ALA A 40 0.2034 0.1946 0.2118 -0.0378 0.0129 -0.0101 40 ALA A CB ? ? ?
487309 C C . ALA A 40 0.1733 0.1641 0.1670 -0.0253 0.0105 -0.0062 40 ALA A C ? ? ?
488310 O O . ALA A 40 0.1851 0.1649 0.1714 -0.0231 0.0150 -0.0055 40 ALA A O ? ? ?
489311 N N . VAL A 41 0.1498 0.1478 0.1422 -0.0234 0.0049 -0.0062 41 VAL A N ? ? ?
490312 C CA . VAL A 41 0.1517 0.1456 0.1342 -0.0191 0.0047 -0.0054 41 VAL A CA ? ? ?
491313 C CB . VAL A 41 0.1653 0.1654 0.1503 -0.0138 0.0033 -0.0011 41 VAL A CB ? ? ?
492314 C CG1 . VAL A 41 0.2035 0.2013 0.1808 -0.0104 0.0034 0.0001 41 VAL A CG1 ? ? ?
493315 C CG2 . VAL A 41 0.1728 0.1713 0.1609 -0.0109 0.0071 0.0012 41 VAL A CG2 ? ? ?
494316 C C . VAL A 41 0.1868 0.1815 0.1626 -0.0220 0.0004 -0.0090 41 VAL A C ? ? ?
495317 O O . VAL A 41 0.1737 0.1779 0.1535 -0.0240 -0.0056 -0.0088 41 VAL A O ? ? ?
496318 N N . GLU A 42 0.1638 0.1487 0.1291 -0.0214 0.0035 -0.0120 42 GLU A N ? ? ?
497319 C CA . GLU A 42 0.1873 0.1713 0.1421 -0.0233 0.0007 -0.0161 42 GLU A CA ? ? ?
498320 C CB . GLU A 42 0.2663 0.2391 0.2158 -0.0284 0.0024 -0.0236 42 GLU A CB ? ? ?
499321 C CG . GLU A 42 0.3077 0.2778 0.2430 -0.0303 -0.0002 -0.0297 42 GLU A CG ? ? ?
500322 C CD . GLU A 42 0.4100 0.3676 0.3398 -0.0360 0.0011 -0.0387 42 GLU A CD ? ? ?
501323 O OE1 . GLU A 42 0.4492 0.3947 0.3822 -0.0355 0.0075 -0.0395 42 GLU A OE1 ? ? ?
502324 O OE2 . GLU A 42 0.5607 0.5199 0.4823 -0.0409 -0.0047 -0.0450 42 GLU A OE2 ? ? ?
503325 C C . GLU A 42 0.2055 0.1873 0.1518 -0.0174 0.0041 -0.0139 42 GLU A C ? ? ?
504326 O O . GLU A 42 0.1857 0.1601 0.1310 -0.0136 0.0100 -0.0132 42 GLU A O ? ? ?
505327 N N . ILE A 43 0.1742 0.1634 0.1156 -0.0166 0.0005 -0.0117 43 ILE A N ? ? ?
506328 C CA . ILE A 43 0.1781 0.1668 0.1122 -0.0119 0.0045 -0.0091 43 ILE A CA ? ? ?
507329 C CB . ILE A 43 0.1582 0.1561 0.0999 -0.0089 0.0027 -0.0013 43 ILE A CB ? ? ?
508330 C CG1 . ILE A 43 0.1660 0.1648 0.1208 -0.0071 0.0033 0.0015 43 ILE A CG1 ? ? ?
509331 C CG2 . ILE A 43 0.1682 0.1669 0.1042 -0.0051 0.0072 0.0020 43 ILE A CG2 ? ? ?
510332 C CD1 . ILE A 43 0.1823 0.1878 0.1450 -0.0047 0.0016 0.0075 43 ILE A CD1 ? ? ?
511333 C C . ILE A 43 0.2018 0.1890 0.1204 -0.0137 0.0035 -0.0133 43 ILE A C ? ? ?
512334 O O . ILE A 43 0.2160 0.2091 0.1312 -0.0173 -0.0034 -0.0139 43 ILE A O ? ? ?
513335 N N . LYS A 44 0.2032 0.1829 0.1123 -0.0106 0.0105 -0.0163 44 LYS A N ? ? ?
514336 C CA . LYS A 44 0.2559 0.2338 0.1474 -0.0110 0.0117 -0.0203 44 LYS A CA ? ? ?
515337 C CB . LYS A 44 0.3043 0.2690 0.1856 -0.0130 0.0149 -0.0309 44 LYS A CB ? ? ?
516338 C CG . LYS A 44 0.3923 0.3535 0.2789 -0.0198 0.0088 -0.0362 44 LYS A CG ? ? ?
517339 C CD . LYS A 44 0.6012 0.5480 0.4769 -0.0231 0.0112 -0.0475 44 LYS A CD ? ? ?
518340 C CE . LYS A 44 0.7309 0.6742 0.6157 -0.0306 0.0060 -0.0520 44 LYS A CE ? ? ?
519341 N NZ . LYS A 44 0.8575 0.7843 0.7332 -0.0344 0.0088 -0.0635 44 LYS A NZ ? ? ?
520342 C C . LYS A 44 0.2697 0.2508 0.1592 -0.0051 0.0188 -0.0148 44 LYS A C ? ? ?
521343 O O . LYS A 44 0.2534 0.2310 0.1499 -0.0006 0.0256 -0.0139 44 LYS A O ? ? ?
522344 N N . GLN A 45 0.2940 0.2824 0.1751 -0.0051 0.0170 -0.0103 45 GLN A N ? ? ?
523345 C CA . GLN A 45 0.2818 0.2747 0.1622 -0.0007 0.0240 -0.0039 45 GLN A CA ? ? ?
524346 C CB . GLN A 45 0.2797 0.2824 0.1708 -0.0010 0.0198 0.0065 45 GLN A CB ? ? ?
525347 C CG . GLN A 45 0.2635 0.2714 0.1552 0.0022 0.0270 0.0140 45 GLN A CG ? ? ?
526348 C CD . GLN A 45 0.3114 0.3265 0.2136 0.0012 0.0225 0.0239 45 GLN A CD ? ? ?
527349 O OE1 . GLN A 45 0.3320 0.3484 0.2420 -0.0009 0.0143 0.0250 45 GLN A OE1 ? ? ?
528350 N NE2 . GLN A 45 0.3128 0.3325 0.2166 0.0026 0.0283 0.0313 45 GLN A NE2 ? ? ?
529351 C C . GLN A 45 0.3178 0.3088 0.1759 -0.0004 0.0279 -0.0071 45 GLN A C ? ? ?
530352 O O . GLN A 45 0.3107 0.3029 0.1555 -0.0040 0.0211 -0.0090 45 GLN A O ? ? ?
531353 N N . GLU A 46 0.2865 0.2755 0.1410 0.0043 0.0387 -0.0077 46 GLU A N ? ? ?
532354 C CA . GLU A 46 0.3456 0.3339 0.1789 0.0058 0.0451 -0.0097 46 GLU A CA ? ? ?
533355 C CB . GLU A 46 0.4611 0.4368 0.2809 0.0072 0.0508 -0.0225 46 GLU A CB ? ? ?
534356 C CG . GLU A 46 0.6494 0.6179 0.4530 0.0014 0.0422 -0.0323 46 GLU A CG ? ? ?
535357 C CD . GLU A 46 0.8686 0.8376 0.6443 0.0002 0.0420 -0.0356 46 GLU A CD ? ? ?
536358 O OE1 . GLU A 46 1.0404 1.0049 0.8018 0.0046 0.0531 -0.0397 46 GLU A OE1 ? ? ?
537359 O OE2 . GLU A 46 0.9209 0.8952 0.6886 -0.0047 0.0308 -0.0340 46 GLU A OE2 ? ? ?
538360 C C . GLU A 46 0.3074 0.3034 0.1490 0.0104 0.0548 -0.0007 46 GLU A C ? ? ?
539361 O O . GLU A 46 0.3121 0.3065 0.1623 0.0151 0.0637 -0.0026 46 GLU A O ? ? ?
540362 N N . GLY A 47 0.3095 0.3143 0.1511 0.0090 0.0527 0.0096 47 GLY A N ? ? ?
541363 C CA . GLY A 47 0.3235 0.3365 0.1765 0.0117 0.0612 0.0191 47 GLY A CA ? ? ?
542364 C C . GLY A 47 0.2900 0.3065 0.1708 0.0127 0.0599 0.0222 47 GLY A C ? ? ?
543365 O O . GLY A 47 0.2833 0.3005 0.1749 0.0098 0.0504 0.0243 47 GLY A O ? ? ?
544366 N N . ASP A 48 0.2489 0.2681 0.1410 0.0171 0.0694 0.0220 48 ASP A N ? ? ?
545367 C CA . ASP A 48 0.2402 0.2632 0.1570 0.0185 0.0676 0.0241 48 ASP A CA ? ? ?
546368 C CB . ASP A 48 0.2836 0.3174 0.2154 0.0214 0.0772 0.0309 48 ASP A CB ? ? ?
547369 C CG . ASP A 48 0.3236 0.3656 0.2602 0.0175 0.0771 0.0415 48 ASP A CG ? ? ?
548370 O OD1 . ASP A 48 0.3502 0.3902 0.2864 0.0131 0.0675 0.0446 48 ASP A OD1 ? ? ?
549371 O OD2 . ASP A 48 0.3892 0.4389 0.3297 0.0189 0.0873 0.0469 48 ASP A OD2 ? ? ?
550372 C C . ASP A 48 0.2305 0.2452 0.1501 0.0215 0.0668 0.0155 48 ASP A C ? ? ?
551373 O O . ASP A 48 0.2320 0.2499 0.1698 0.0242 0.0668 0.0170 48 ASP A O ? ? ?
552374 N N . THR A 49 0.2361 0.2400 0.1377 0.0206 0.0655 0.0069 49 THR A N ? ? ?
553375 C CA . THR A 49 0.2352 0.2286 0.1381 0.0224 0.0646 -0.0010 49 THR A CA ? ? ?
554376 C CB . THR A 49 0.2826 0.2655 0.1672 0.0249 0.0720 -0.0104 49 THR A CB ? ? ?
555377 O OG1 . THR A 49 0.2849 0.2728 0.1722 0.0312 0.0840 -0.0085 49 THR A OG1 ? ? ?
556378 C CG2 . THR A 49 0.3054 0.2746 0.1903 0.0260 0.0711 -0.0185 49 THR A CG2 ? ? ?
557379 C C . THR A 49 0.2311 0.2202 0.1343 0.0169 0.0533 -0.0028 49 THR A C ? ? ?
558380 O O . THR A 49 0.2285 0.2172 0.1199 0.0121 0.0475 -0.0040 49 THR A O ? ? ?
559381 N N . PHE A 50 0.1987 0.1852 0.1155 0.0180 0.0506 -0.0026 50 PHE A N ? ? ?
560382 C CA . PHE A 50 0.1942 0.1787 0.1148 0.0134 0.0415 -0.0031 50 PHE A CA ? ? ?
561383 C CB . PHE A 50 0.1843 0.1780 0.1214 0.0133 0.0369 0.0045 50 PHE A CB ? ? ?
562384 C CG . PHE A 50 0.1933 0.1964 0.1319 0.0110 0.0343 0.0107 50 PHE A CG ? ? ?
563385 C CD1 . PHE A 50 0.2075 0.2176 0.1495 0.0133 0.0402 0.0157 50 PHE A CD1 ? ? ?
564386 C CD2 . PHE A 50 0.2141 0.2189 0.1518 0.0066 0.0265 0.0121 50 PHE A CD2 ? ? ?
565387 C CE1 . PHE A 50 0.2087 0.2259 0.1527 0.0108 0.0383 0.0224 50 PHE A CE1 ? ? ?
566388 C CE2 . PHE A 50 0.2169 0.2286 0.1563 0.0050 0.0243 0.0187 50 PHE A CE2 ? ? ?
567389 C CZ . PHE A 50 0.2061 0.2230 0.1480 0.0068 0.0303 0.0240 50 PHE A CZ ? ? ?
568390 C C . PHE A 50 0.2001 0.1727 0.1211 0.0141 0.0421 -0.0089 50 PHE A C ? ? ?
569391 O O . PHE A 50 0.2075 0.1759 0.1334 0.0195 0.0479 -0.0094 50 PHE A O ? ? ?
570392 N N . TYR A 51 0.1963 0.1641 0.1129 0.0084 0.0360 -0.0128 51 TYR A N ? ? ?
571393 C CA . TYR A 51 0.2179 0.1756 0.1379 0.0071 0.0352 -0.0162 51 TYR A CA ? ? ?
572394 C CB . TYR A 51 0.2607 0.2063 0.1678 0.0032 0.0360 -0.0258 51 TYR A CB ? ? ?
573395 C CG . TYR A 51 0.2720 0.2076 0.1832 -0.0010 0.0341 -0.0292 51 TYR A CG ? ? ?
574396 C CD1 . TYR A 51 0.3402 0.2632 0.2549 0.0028 0.0399 -0.0300 51 TYR A CD1 ? ? ?
575397 C CD2 . TYR A 51 0.2876 0.2266 0.2003 -0.0085 0.0268 -0.0307 51 TYR A CD2 ? ? ?
576398 C CE1 . TYR A 51 0.3364 0.2489 0.2547 -0.0015 0.0391 -0.0320 51 TYR A CE1 ? ? ?
577399 C CE2 . TYR A 51 0.2876 0.2181 0.2056 -0.0131 0.0260 -0.0333 51 TYR A CE2 ? ? ?
578400 C CZ . TYR A 51 0.3379 0.2546 0.2581 -0.0099 0.0325 -0.0337 51 TYR A CZ ? ? ?
579401 O OH . TYR A 51 0.3525 0.2599 0.2782 -0.0147 0.0327 -0.0350 51 TYR A OH ? ? ?
580402 C C . TYR A 51 0.1968 0.1607 0.1256 0.0029 0.0278 -0.0125 51 TYR A C ? ? ?
581403 O O . TYR A 51 0.2077 0.1778 0.1340 -0.0016 0.0221 -0.0126 51 TYR A O ? ? ?
582404 N N . ILE A 52 0.1857 0.1480 0.1242 0.0047 0.0279 -0.0093 52 ILE A N ? ? ?
583405 C CA . ILE A 52 0.1738 0.1416 0.1200 0.0016 0.0225 -0.0062 52 ILE A CA ? ? ?
584406 C CB . ILE A 52 0.1614 0.1394 0.1166 0.0047 0.0205 0.0002 52 ILE A CB ? ? ?
585407 C CG1 . ILE A 52 0.1688 0.1552 0.1232 0.0054 0.0198 0.0026 52 ILE A CG1 ? ? ?
586408 C CG2 . ILE A 52 0.1786 0.1605 0.1402 0.0020 0.0159 0.0019 52 ILE A CG2 ? ? ?
587409 C CD1 . ILE A 52 0.1688 0.1637 0.1333 0.0076 0.0180 0.0082 52 ILE A CD1 ? ? ?
588410 C C . ILE A 52 0.1789 0.1373 0.1275 0.0007 0.0243 -0.0072 52 ILE A C ? ? ?
589411 O O . ILE A 52 0.2042 0.1574 0.1548 0.0056 0.0280 -0.0047 52 ILE A O ? ? ?
590412 N N . LYS A 53 0.1732 0.1299 0.1222 -0.0056 0.0216 -0.0103 53 LYS A N ? ? ?
591413 C CA . LYS A 53 0.1833 0.1317 0.1356 -0.0079 0.0238 -0.0104 53 LYS A CA ? ? ?
592414 C CB . LYS A 53 0.2209 0.1596 0.1693 -0.0142 0.0244 -0.0174 53 LYS A CB ? ? ?
593415 C CG . LYS A 53 0.2395 0.1692 0.1930 -0.0181 0.0273 -0.0169 53 LYS A CG ? ? ?
594416 C CD . LYS A 53 0.3298 0.2502 0.2812 -0.0258 0.0270 -0.0248 53 LYS A CD ? ? ?
595417 C CE . LYS A 53 0.4946 0.4018 0.4507 -0.0293 0.0320 -0.0239 53 LYS A CE ? ? ?
596418 N NZ . LYS A 53 0.5398 0.4395 0.4966 -0.0388 0.0305 -0.0324 53 LYS A NZ ? ? ?
597419 C C . LYS A 53 0.1842 0.1419 0.1447 -0.0102 0.0205 -0.0068 53 LYS A C ? ? ?
598420 O O . LYS A 53 0.1679 0.1346 0.1316 -0.0140 0.0158 -0.0081 53 LYS A O ? ? ?
599421 N N . THR A 54 0.1603 0.1156 0.1234 -0.0072 0.0232 -0.0023 54 THR A N ? ? ?
600422 C CA . THR A 54 0.1663 0.1290 0.1355 -0.0083 0.0219 0.0007 54 THR A CA ? ? ?
601423 C CB . THR A 54 0.1789 0.1475 0.1484 -0.0024 0.0206 0.0050 54 THR A CB ? ? ?
602424 O OG1 . THR A 54 0.1812 0.1565 0.1511 -0.0006 0.0172 0.0044 54 THR A OG1 ? ? ?
603425 C CG2 . THR A 54 0.1684 0.1437 0.1423 -0.0032 0.0198 0.0066 54 THR A CG2 ? ? ?
604426 C C . THR A 54 0.1704 0.1244 0.1403 -0.0108 0.0267 0.0021 54 THR A C ? ? ?
605427 O O . THR A 54 0.1822 0.1271 0.1478 -0.0069 0.0306 0.0054 54 THR A O ? ? ?
606428 N N . SER A 55 0.1696 0.1271 0.1460 -0.0173 0.0266 0.0003 55 SER A N ? ? ?
607429 C CA . SER A 55 0.1915 0.1405 0.1702 -0.0215 0.0320 0.0015 55 SER A CA ? ? ?
608430 C CB . SER A 55 0.2655 0.2109 0.2482 -0.0297 0.0308 -0.0046 55 SER A CB ? ? ?
609431 O OG . SER A 55 0.4497 0.3875 0.4374 -0.0351 0.0363 -0.0032 55 SER A OG ? ? ?
610432 C C . SER A 55 0.1797 0.1367 0.1645 -0.0226 0.0343 0.0050 55 SER A C ? ? ?
611433 O O . SER A 55 0.1761 0.1458 0.1681 -0.0240 0.0310 0.0035 55 SER A O ? ? ?
612434 N N . THR A 56 0.1720 0.1210 0.1532 -0.0212 0.0406 0.0103 56 THR A N ? ? ?
613435 C CA . THR A 56 0.1718 0.1262 0.1567 -0.0225 0.0453 0.0139 56 THR A CA ? ? ?
614436 C CB . THR A 56 0.1808 0.1390 0.1573 -0.0149 0.0455 0.0179 56 THR A CB ? ? ?
615437 O OG1 . THR A 56 0.1950 0.1411 0.1605 -0.0103 0.0483 0.0232 56 THR A OG1 ? ? ?
616438 C CG2 . THR A 56 0.1916 0.1588 0.1680 -0.0107 0.0383 0.0147 56 THR A CG2 ? ? ?
617439 C C . THR A 56 0.1797 0.1216 0.1647 -0.0268 0.0530 0.0177 56 THR A C ? ? ?
618440 O O . THR A 56 0.1778 0.1059 0.1589 -0.0273 0.0540 0.0176 56 THR A O ? ? ?
619441 N N . THR A 57 0.1776 0.1236 0.1671 -0.0296 0.0592 0.0213 57 THR A N ? ? ?
620442 C CA . THR A 57 0.1886 0.1230 0.1791 -0.0343 0.0677 0.0264 57 THR A CA ? ? ?
621443 C CB . THR A 57 0.2068 0.1510 0.2054 -0.0382 0.0747 0.0294 57 THR A CB ? ? ?
622444 O OG1 . THR A 57 0.2005 0.1522 0.1896 -0.0305 0.0755 0.0321 57 THR A OG1 ? ? ?
623445 C CG2 . THR A 57 0.2219 0.1807 0.2394 -0.0456 0.0717 0.0231 57 THR A CG2 ? ? ?
624446 C C . THR A 57 0.1947 0.1138 0.1704 -0.0280 0.0715 0.0339 57 THR A C ? ? ?
625447 O O . THR A 57 0.2054 0.1106 0.1810 -0.0315 0.0779 0.0385 57 THR A O ? ? ?
626448 N N . VAL A 58 0.1894 0.1112 0.1537 -0.0189 0.0672 0.0356 58 VAL A N ? ? ?
627449 C CA . VAL A 58 0.2045 0.1151 0.1550 -0.0118 0.0694 0.0435 58 VAL A CA ? ? ?
628450 C CB . VAL A 58 0.2207 0.1393 0.1602 -0.0061 0.0703 0.0481 58 VAL A CB ? ? ?
629451 C CG1 . VAL A 58 0.2393 0.1631 0.1821 -0.0112 0.0787 0.0504 58 VAL A CG1 ? ? ?
630452 C CG2 . VAL A 58 0.2077 0.1396 0.1463 -0.0015 0.0617 0.0422 58 VAL A CG2 ? ? ?
631453 C C . VAL A 58 0.2024 0.1074 0.1483 -0.0053 0.0633 0.0422 58 VAL A C ? ? ?
632454 O O . VAL A 58 0.2080 0.1031 0.1451 0.0009 0.0646 0.0491 58 VAL A O ? ? ?
633455 N N . ARG A 59 0.1949 0.1066 0.1472 -0.0063 0.0572 0.0342 59 ARG A N ? ? ?
634456 C CA . ARG A 59 0.2111 0.1202 0.1603 0.0000 0.0524 0.0328 59 ARG A CA ? ? ?
635457 C CB . ARG A 59 0.2491 0.1671 0.1913 0.0080 0.0478 0.0363 59 ARG A CB ? ? ?
636458 C CG . ARG A 59 0.3000 0.2191 0.2418 0.0147 0.0428 0.0355 59 ARG A CG ? ? ?
637459 C CD . ARG A 59 0.3155 0.2427 0.2511 0.0215 0.0382 0.0399 59 ARG A CD ? ? ?
638460 N NE . ARG A 59 0.3882 0.3225 0.3274 0.0266 0.0324 0.0382 59 ARG A NE ? ? ?
639461 C CZ . ARG A 59 0.3952 0.3241 0.3353 0.0327 0.0323 0.0415 59 ARG A CZ ? ? ?
640462 N NH1 . ARG A 59 0.4180 0.3325 0.3546 0.0352 0.0373 0.0469 59 ARG A NH1 ? ? ?
641463 N NH2 . ARG A 59 0.4713 0.4093 0.4172 0.0367 0.0276 0.0397 59 ARG A NH2 ? ? ?
642464 C C . ARG A 59 0.1970 0.1127 0.1531 -0.0035 0.0477 0.0240 59 ARG A C ? ? ?
643465 O O . ARG A 59 0.1836 0.1122 0.1444 -0.0064 0.0442 0.0203 59 ARG A O ? ? ?
644466 N N . THR A 60 0.2042 0.1103 0.1600 -0.0025 0.0478 0.0210 60 THR A N ? ? ?
645467 C CA . THR A 60 0.2111 0.1226 0.1695 -0.0043 0.0435 0.0134 60 THR A CA ? ? ?
646468 C CB . THR A 60 0.2255 0.1273 0.1867 -0.0121 0.0455 0.0071 60 THR A CB ? ? ?
647469 O OG1 . THR A 60 0.2292 0.1358 0.1972 -0.0200 0.0463 0.0068 60 THR A OG1 ? ? ?
648470 C CG2 . THR A 60 0.2509 0.1567 0.2111 -0.0135 0.0413 -0.0008 60 THR A CG2 ? ? ?
649471 C C . THR A 60 0.2059 0.1164 0.1607 0.0039 0.0421 0.0141 60 THR A C ? ? ?
650472 O O . THR A 60 0.2294 0.1286 0.1814 0.0091 0.0456 0.0179 60 THR A O ? ? ?
651473 N N . THR A 61 0.2065 0.1293 0.1627 0.0052 0.0374 0.0110 61 THR A N ? ? ?
652474 C CA . THR A 61 0.2069 0.1311 0.1623 0.0120 0.0368 0.0111 61 THR A CA ? ? ?
653475 C CB . THR A 61 0.2198 0.1577 0.1775 0.0167 0.0322 0.0151 61 THR A CB ? ? ?
654476 O OG1 . THR A 61 0.2550 0.2045 0.2154 0.0123 0.0280 0.0124 61 THR A OG1 ? ? ?
655477 C CG2 . THR A 61 0.2519 0.1890 0.2074 0.0203 0.0320 0.0218 61 THR A CG2 ? ? ?
656478 C C . THR A 61 0.2023 0.1275 0.1566 0.0089 0.0362 0.0039 61 THR A C ? ? ?
657479 O O . THR A 61 0.1974 0.1298 0.1528 0.0029 0.0329 0.0004 61 THR A O ? ? ?
658480 N N . GLU A 62 0.2246 0.1431 0.1766 0.0136 0.0396 0.0020 62 GLU A N ? ? ?
659481 C CA . GLU A 62 0.2246 0.1447 0.1729 0.0123 0.0399 -0.0044 62 GLU A CA ? ? ?
660482 C CB . GLU A 62 0.2919 0.1957 0.2344 0.0093 0.0441 -0.0115 62 GLU A CB ? ? ?
661483 C CG . GLU A 62 0.3446 0.2423 0.2874 0.0004 0.0427 -0.0144 62 GLU A CG ? ? ?
662484 C CD . GLU A 62 0.5155 0.3954 0.4533 -0.0032 0.0465 -0.0223 62 GLU A CD ? ? ?
663485 O OE1 . GLU A 62 0.4662 0.3460 0.3969 -0.0056 0.0455 -0.0303 62 GLU A OE1 ? ? ?
664486 O OE2 . GLU A 62 0.6125 0.4777 0.5524 -0.0033 0.0508 -0.0205 62 GLU A OE2 ? ? ?
665487 C C . GLU A 62 0.2246 0.1504 0.1750 0.0203 0.0418 -0.0020 62 GLU A C ? ? ?
666488 O O . GLU A 62 0.2471 0.1650 0.1990 0.0269 0.0462 0.0001 62 GLU A O ? ? ?
667489 N N . ILE A 63 0.1951 0.1344 0.1468 0.0199 0.0390 -0.0017 63 ILE A N ? ? ?
668490 C CA . ILE A 63 0.2030 0.1497 0.1587 0.0264 0.0415 0.0006 63 ILE A CA ? ? ?
669491 C CB . ILE A 63 0.1993 0.1608 0.1643 0.0280 0.0365 0.0069 63 ILE A CB ? ? ?
670492 C CG1 . ILE A 63 0.2138 0.1849 0.1786 0.0219 0.0314 0.0066 63 ILE A CG1 ? ? ?
671493 C CG2 . ILE A 63 0.2205 0.1798 0.1890 0.0304 0.0340 0.0116 63 ILE A CG2 ? ? ?
672494 C CD1 . ILE A 63 0.2344 0.2180 0.2086 0.0230 0.0269 0.0116 63 ILE A CD1 ? ? ?
673495 C C . ILE A 63 0.2198 0.1680 0.1687 0.0250 0.0443 -0.0045 63 ILE A C ? ? ?
674496 O O . ILE A 63 0.2045 0.1545 0.1470 0.0186 0.0410 -0.0078 63 ILE A O ? ? ?
675497 N N . ASN A 64 0.2140 0.1615 0.1639 0.0315 0.0507 -0.0049 64 ASN A N ? ? ?
676498 C CA . ASN A 64 0.2583 0.2079 0.2007 0.0318 0.0555 -0.0090 64 ASN A CA ? ? ?
677499 C CB . ASN A 64 0.2961 0.2296 0.2292 0.0345 0.0628 -0.0168 64 ASN A CB ? ? ?
678500 C CG . ASN A 64 0.3660 0.2868 0.2881 0.0272 0.0599 -0.0241 64 ASN A CG ? ? ?
679501 O OD1 . ASN A 64 0.3891 0.3108 0.2999 0.0217 0.0579 -0.0293 64 ASN A OD1 ? ? ?
680502 N ND2 . ASN A 64 0.4422 0.3509 0.3677 0.0267 0.0596 -0.0242 64 ASN A ND2 ? ? ?
681503 C C . ASN A 64 0.2400 0.2033 0.1932 0.0376 0.0585 -0.0032 64 ASN A C ? ? ?
682504 O O . ASN A 64 0.2406 0.2044 0.2038 0.0446 0.0615 0.0000 64 ASN A O ? ? ?
683505 N N . PHE A 65 0.2128 0.1874 0.1648 0.0346 0.0577 -0.0012 65 PHE A N ? ? ?
684506 C CA . PHE A 65 0.2047 0.1931 0.1689 0.0388 0.0612 0.0045 65 PHE A CA ? ? ?
685507 C CB . PHE A 65 0.1845 0.1837 0.1638 0.0377 0.0537 0.0112 65 PHE A CB ? ? ?
686508 C CG . PHE A 65 0.1797 0.1829 0.1568 0.0304 0.0461 0.0129 65 PHE A CG ? ? ?
687509 C CD1 . PHE A 65 0.1968 0.2098 0.1765 0.0275 0.0462 0.0166 65 PHE A CD1 ? ? ?
688510 C CD2 . PHE A 65 0.1869 0.1838 0.1603 0.0267 0.0396 0.0112 65 PHE A CD2 ? ? ?
689511 C CE1 . PHE A 65 0.1904 0.2056 0.1690 0.0216 0.0393 0.0184 65 PHE A CE1 ? ? ?
690512 C CE2 . PHE A 65 0.1806 0.1813 0.1535 0.0211 0.0333 0.0126 65 PHE A CE2 ? ? ?
691513 C CZ . PHE A 65 0.1795 0.1889 0.1553 0.0189 0.0329 0.0161 65 PHE A CZ ? ? ?
692514 C C . PHE A 65 0.1996 0.1949 0.1567 0.0363 0.0650 0.0049 65 PHE A C ? ? ?
693515 O O . PHE A 65 0.2035 0.1957 0.1475 0.0306 0.0615 0.0025 65 PHE A O ? ? ?
694516 N N . LYS A 66 0.1897 0.1951 0.1561 0.0409 0.0721 0.0086 66 LYS A N ? ? ?
695517 C CA . LYS A 66 0.2140 0.2291 0.1779 0.0386 0.0763 0.0121 66 LYS A CA ? ? ?
696518 C CB . LYS A 66 0.2737 0.2885 0.2321 0.0447 0.0894 0.0092 66 LYS A CB ? ? ?
697519 C CG . LYS A 66 0.4020 0.4266 0.3555 0.0427 0.0960 0.0136 66 LYS A CG ? ? ?
698520 C CD . LYS A 66 0.4762 0.4987 0.4193 0.0488 0.1103 0.0091 66 LYS A CD ? ? ?
699521 C CE . LYS A 66 0.6060 0.6411 0.5486 0.0479 0.1189 0.0158 66 LYS A CE ? ? ?
700522 N NZ . LYS A 66 0.5778 0.6114 0.5024 0.0404 0.1134 0.0185 66 LYS A NZ ? ? ?
701523 C C . LYS A 66 0.1924 0.2222 0.1768 0.0372 0.0724 0.0206 66 LYS A C ? ? ?
702524 O O . LYS A 66 0.1704 0.2060 0.1719 0.0412 0.0716 0.0229 66 LYS A O ? ? ?
703525 N N . VAL A 67 0.1837 0.2191 0.1669 0.0313 0.0693 0.0252 67 VAL A N ? ? ?
704526 C CA . VAL A 67 0.1641 0.2119 0.1667 0.0287 0.0658 0.0324 67 VAL A CA ? ? ?
705527 C CB . VAL A 67 0.1594 0.2088 0.1573 0.0220 0.0623 0.0372 67 VAL A CB ? ? ?
706528 C CG1 . VAL A 67 0.1618 0.2215 0.1809 0.0186 0.0584 0.0438 67 VAL A CG1 ? ? ?
707529 C CG2 . VAL A 67 0.1651 0.2042 0.1492 0.0185 0.0536 0.0335 67 VAL A CG2 ? ? ?
708530 C C . VAL A 67 0.1514 0.2113 0.1697 0.0333 0.0750 0.0360 67 VAL A C ? ? ?
709531 O O . VAL A 67 0.1874 0.2479 0.1978 0.0362 0.0856 0.0354 67 VAL A O ? ? ?
710532 N N . GLY A 68 0.1268 0.1965 0.1671 0.0343 0.0708 0.0392 68 GLY A N ? ? ?
711533 C CA . GLY A 68 0.1277 0.2122 0.1884 0.0382 0.0780 0.0433 68 GLY A CA ? ? ?
712534 C C . GLY A 68 0.1347 0.2192 0.2002 0.0477 0.0835 0.0401 68 GLY A C ? ? ?
713535 O O . GLY A 68 0.1299 0.2281 0.2144 0.0521 0.0899 0.0435 68 GLY A O ? ? ?
714536 N N . GLU A 69 0.1386 0.2077 0.1887 0.0509 0.0813 0.0340 69 GLU A N ? ? ?
715537 C CA . GLU A 69 0.1647 0.2302 0.2186 0.0603 0.0863 0.0312 69 GLU A CA ? ? ?
716538 C CB . GLU A 69 0.1916 0.2429 0.2244 0.0635 0.0963 0.0242 69 GLU A CB ? ? ?
717539 C CG . GLU A 69 0.2402 0.2994 0.2700 0.0632 0.1078 0.0255 69 GLU A CG ? ? ?
718540 C CD . GLU A 69 0.3187 0.3659 0.3284 0.0677 0.1194 0.0180 69 GLU A CD ? ? ?
719541 O OE1 . GLU A 69 0.3256 0.3576 0.3264 0.0720 0.1193 0.0111 69 GLU A OE1 ? ? ?
720542 O OE2 . GLU A 69 0.3534 0.4059 0.3555 0.0667 0.1287 0.0189 69 GLU A OE2 ? ? ?
721543 C C . GLU A 69 0.1516 0.2099 0.2068 0.0618 0.0759 0.0303 69 GLU A C ? ? ?
722544 O O . GLU A 69 0.1563 0.2034 0.1975 0.0567 0.0689 0.0276 69 GLU A O ? ? ?
723545 N N . GLU A 70 0.1657 0.2319 0.2387 0.0690 0.0749 0.0334 70 GLU A N ? ? ?
724546 C CA . GLU A 70 0.1839 0.2452 0.2587 0.0711 0.0650 0.0344 70 GLU A CA ? ? ?
725547 C CB . GLU A 70 0.2297 0.3055 0.3280 0.0795 0.0640 0.0396 70 GLU A CB ? ? ?
726548 C CG . GLU A 70 0.3123 0.3869 0.4138 0.0820 0.0526 0.0426 70 GLU A CG ? ? ?
727549 C CD . GLU A 70 0.4249 0.5165 0.5508 0.0905 0.0503 0.0484 70 GLU A CD ? ? ?
728550 O OE1 . GLU A 70 0.4937 0.6053 0.6385 0.0871 0.0459 0.0516 70 GLU A OE1 ? ? ?
729551 O OE2 . GLU A 70 0.5805 0.6656 0.7080 0.1004 0.0530 0.0498 70 GLU A OE2 ? ? ?
730552 C C . GLU A 70 0.1755 0.2150 0.2309 0.0734 0.0670 0.0291 70 GLU A C ? ? ?
731553 O O . GLU A 70 0.1845 0.2149 0.2324 0.0778 0.0769 0.0249 70 GLU A O ? ? ?
732554 N N . PHE A 71 0.1594 0.1902 0.2067 0.0701 0.0580 0.0291 71 PHE A N ? ? ?
733555 C CA . PHE A 71 0.1844 0.1950 0.2162 0.0713 0.0591 0.0252 71 PHE A CA ? ? ?
734556 C CB . PHE A 71 0.1965 0.1958 0.2094 0.0628 0.0596 0.0191 71 PHE A CB ? ? ?
735557 C CG . PHE A 71 0.1917 0.1952 0.2015 0.0542 0.0504 0.0203 71 PHE A CG ? ? ?
736558 C CD1 . PHE A 71 0.1964 0.2140 0.2136 0.0500 0.0477 0.0228 71 PHE A CD1 ? ? ?
737559 C CD2 . PHE A 71 0.1883 0.1809 0.1887 0.0507 0.0454 0.0189 71 PHE A CD2 ? ? ?
738560 C CE1 . PHE A 71 0.1995 0.2192 0.2144 0.0430 0.0398 0.0234 71 PHE A CE1 ? ? ?
739561 C CE2 . PHE A 71 0.1861 0.1828 0.1846 0.0439 0.0381 0.0196 71 PHE A CE2 ? ? ?
740562 C CZ . PHE A 71 0.1715 0.1812 0.1771 0.0404 0.0352 0.0215 71 PHE A CZ ? ? ?
741563 C C . PHE A 71 0.2012 0.2096 0.2348 0.0725 0.0500 0.0294 71 PHE A C ? ? ?
742564 O O . PHE A 71 0.1945 0.2167 0.2386 0.0715 0.0423 0.0339 71 PHE A O ? ? ?
743565 N N . GLU A 72 0.2317 0.2224 0.2548 0.0745 0.0514 0.0280 72 GLU A N ? ? ?
744566 C CA . GLU A 72 0.2467 0.2332 0.2688 0.0764 0.0445 0.0329 72 GLU A CA ? ? ?
745567 C CB . GLU A 72 0.3326 0.3080 0.3576 0.0867 0.0492 0.0359 72 GLU A CB ? ? ?
746568 C CG . GLU A 72 0.5020 0.4778 0.5292 0.0913 0.0418 0.0439 72 GLU A CG ? ? ?
747569 C CD . GLU A 72 0.5253 0.4897 0.5564 0.1025 0.0461 0.0485 72 GLU A CD ? ? ?
748570 O OE1 . GLU A 72 0.4824 0.4545 0.5277 0.1110 0.0503 0.0498 72 GLU A OE1 ? ? ?
749571 O OE2 . GLU A 72 0.5777 0.5256 0.5986 0.1029 0.0457 0.0515 72 GLU A OE2 ? ? ?
750572 C C . GLU A 72 0.2388 0.2141 0.2456 0.0678 0.0416 0.0298 72 GLU A C ? ? ?
751573 O O . GLU A 72 0.2727 0.2357 0.2692 0.0637 0.0465 0.0239 72 GLU A O ? ? ?
752574 N N . GLU A 73 0.2164 0.1972 0.2223 0.0648 0.0334 0.0332 73 GLU A N ? ? ?
753575 C CA . GLU A 73 0.2112 0.1824 0.2047 0.0580 0.0312 0.0314 73 GLU A CA ? ? ?
754576 C CB . GLU A 73 0.2223 0.2003 0.2134 0.0492 0.0289 0.0268 73 GLU A CB ? ? ?
755577 C CG . GLU A 73 0.2030 0.1978 0.2031 0.0478 0.0225 0.0287 73 GLU A CG ? ? ?
756578 C CD . GLU A 73 0.1871 0.1858 0.1845 0.0397 0.0195 0.0253 73 GLU A CD ? ? ?
757579 O OE1 . GLU A 73 0.2537 0.2438 0.2420 0.0351 0.0210 0.0221 73 GLU A OE1 ? ? ?
758580 O OE2 . GLU A 73 0.1629 0.1736 0.1686 0.0380 0.0156 0.0261 73 GLU A OE2 ? ? ?
759581 C C . GLU A 73 0.2042 0.1764 0.1959 0.0605 0.0250 0.0375 73 GLU A C ? ? ?
760582 O O . GLU A 73 0.2054 0.1795 0.2024 0.0684 0.0236 0.0432 73 GLU A O ? ? ?
761583 N N . GLN A 74 0.2014 0.1719 0.1846 0.0541 0.0217 0.0365 74 GLN A N ? ? ?
762584 C CA . GLN A 74 0.2102 0.1824 0.1885 0.0557 0.0161 0.0414 74 GLN A CA ? ? ?
763585 C CB . GLN A 74 0.2690 0.2249 0.2357 0.0548 0.0203 0.0438 74 GLN A CB ? ? ?
764586 C CG . GLN A 74 0.3148 0.2572 0.2820 0.0613 0.0260 0.0477 74 GLN A CG ? ? ?
765587 C CD . GLN A 74 0.3728 0.2984 0.3297 0.0589 0.0305 0.0506 74 GLN A CD ? ? ?
766588 O OE1 . GLN A 74 0.3944 0.3198 0.3445 0.0523 0.0301 0.0494 74 GLN A OE1 ? ? ?
767589 N NE2 . GLN A 74 0.4674 0.3784 0.4241 0.0644 0.0355 0.0548 74 GLN A NE2 ? ? ?
768590 C C . GLN A 74 0.1910 0.1738 0.1684 0.0497 0.0101 0.0383 74 GLN A C ? ? ?
769591 O O . GLN A 74 0.1884 0.1724 0.1663 0.0434 0.0115 0.0331 74 GLN A O ? ? ?
770592 N N . THR A 75 0.1831 0.1732 0.1589 0.0521 0.0032 0.0415 75 THR A N ? ? ?
771593 C CA . THR A 75 0.1876 0.1839 0.1593 0.0470 -0.0021 0.0382 75 THR A CA ? ? ?
772594 C CB . THR A 75 0.1769 0.1817 0.1466 0.0509 -0.0107 0.0413 75 THR A CB ? ? ?
773595 O OG1 . THR A 75 0.2140 0.2102 0.1717 0.0558 -0.0097 0.0475 75 THR A OG1 ? ? ?
774596 C CG2 . THR A 75 0.2024 0.2201 0.1874 0.0549 -0.0157 0.0430 75 THR A CG2 ? ? ?
775597 C C . THR A 75 0.1921 0.1781 0.1522 0.0425 0.0024 0.0366 75 THR A C ? ? ?
776598 O O . THR A 75 0.1975 0.1718 0.1523 0.0433 0.0085 0.0391 75 THR A O ? ? ?
777599 N N . VAL A 76 0.2228 0.2131 0.1799 0.0379 -0.0003 0.0324 76 VAL A N ? ? ?
778600 C CA . VAL A 76 0.2437 0.2273 0.1924 0.0338 0.0041 0.0307 76 VAL A CA ? ? ?
779601 C CB . VAL A 76 0.3152 0.3054 0.2635 0.0301 0.0005 0.0253 76 VAL A CB ? ? ?
780602 C CG1 . VAL A 76 0.4209 0.4060 0.3631 0.0265 0.0061 0.0236 76 VAL A CG1 ? ? ?
781603 C CG2 . VAL A 76 0.4784 0.4754 0.4389 0.0271 -0.0020 0.0211 76 VAL A CG2 ? ? ?
782604 C C . VAL A 76 0.2398 0.2151 0.1762 0.0368 0.0070 0.0364 76 VAL A C ? ? ?
783605 O O . VAL A 76 0.3048 0.2714 0.2370 0.0339 0.0137 0.0372 76 VAL A O ? ? ?
784606 N N . ASP A 77 0.2247 0.2028 0.1556 0.0425 0.0019 0.0409 77 ASP A N ? ? ?
785607 C CA . ASP A 77 0.2443 0.2150 0.1613 0.0462 0.0039 0.0479 77 ASP A CA ? ? ?
786608 C CB . ASP A 77 0.2824 0.2611 0.1897 0.0496 -0.0044 0.0489 77 ASP A CB ? ? ?
787609 C CG . ASP A 77 0.2866 0.2756 0.2025 0.0544 -0.0137 0.0502 77 ASP A CG ? ? ?
788610 O OD1 . ASP A 77 0.2675 0.2627 0.1991 0.0527 -0.0151 0.0463 77 ASP A OD1 ? ? ?
789611 O OD2 . ASP A 77 0.3160 0.3076 0.2230 0.0598 -0.0197 0.0556 77 ASP A OD2 ? ? ?
790612 C C . ASP A 77 0.2395 0.2009 0.1582 0.0514 0.0072 0.0553 77 ASP A C ? ? ?
791613 O O . ASP A 77 0.2805 0.2349 0.1883 0.0557 0.0084 0.0631 77 ASP A O ? ? ?
792614 N N . GLY A 78 0.2386 0.1995 0.1703 0.0516 0.0089 0.0531 78 GLY A N ? ? ?
793615 C CA . GLY A 78 0.2779 0.2270 0.2124 0.0557 0.0143 0.0578 78 GLY A CA ? ? ?
794616 C C . GLY A 78 0.3128 0.2657 0.2541 0.0649 0.0103 0.0632 78 GLY A C ? ? ?
795617 O O . GLY A 78 0.3544 0.2955 0.2962 0.0700 0.0149 0.0685 78 GLY A O ? ? ?
796618 N N . ARG A 79 0.2718 0.2408 0.2201 0.0670 0.0020 0.0618 79 ARG A N ? ? ?
797619 C CA . ARG A 79 0.3002 0.2761 0.2582 0.0757 -0.0024 0.0671 79 ARG A CA ? ? ?
798620 C CB . ARG A 79 0.3705 0.3631 0.3289 0.0774 -0.0141 0.0680 79 ARG A CB ? ? ?
799621 C CG . ARG A 79 0.4541 0.4433 0.3937 0.0790 -0.0183 0.0732 79 ARG A CG ? ? ?
800622 C CD . ARG A 79 0.5166 0.5223 0.4552 0.0805 -0.0311 0.0728 79 ARG A CD ? ? ?
801623 N NE . ARG A 79 0.5999 0.6165 0.5468 0.0730 -0.0347 0.0629 79 ARG A NE ? ? ?
802624 C CZ . ARG A 79 0.6221 0.6427 0.5591 0.0679 -0.0397 0.0571 79 ARG A CZ ? ? ?
803625 N NH1 . ARG A 79 0.6942 0.7128 0.6121 0.0701 -0.0439 0.0601 79 ARG A NH1 ? ? ?
804626 N NH2 . ARG A 79 0.5904 0.6167 0.5363 0.0608 -0.0403 0.0483 79 ARG A NH2 ? ? ?
805627 C C . ARG A 79 0.2566 0.2362 0.2308 0.0762 0.0014 0.0628 79 ARG A C ? ? ?
806628 O O . ARG A 79 0.2259 0.2130 0.2056 0.0699 0.0013 0.0557 79 ARG A O ? ? ?
807629 N N . PRO A 80 0.2465 0.2204 0.2282 0.0839 0.0057 0.0669 80 PRO A N ? ? ?
808630 C CA . PRO A 80 0.2424 0.2209 0.2386 0.0853 0.0103 0.0626 80 PRO A CA ? ? ?
809631 C CB . PRO A 80 0.2709 0.2405 0.2725 0.0960 0.0146 0.0689 80 PRO A CB ? ? ?
810632 C CG . PRO A 80 0.3107 0.2645 0.2979 0.0978 0.0151 0.0755 80 PRO A CG ? ? ?
811633 C CD . PRO A 80 0.2851 0.2465 0.2611 0.0920 0.0074 0.0760 80 PRO A CD ? ? ?
812634 C C . PRO A 80 0.2130 0.2134 0.2235 0.0847 0.0037 0.0606 80 PRO A C ? ? ?
813635 O O . PRO A 80 0.2174 0.2303 0.2329 0.0887 -0.0051 0.0652 80 PRO A O ? ? ?
814636 N N . CYS A 81 0.2074 0.2122 0.2247 0.0796 0.0080 0.0541 81 CYS A N ? ? ?
815637 C CA . CYS A 81 0.1884 0.2125 0.2209 0.0780 0.0038 0.0524 81 CYS A CA ? ? ?
816638 C CB . CYS A 81 0.1759 0.2060 0.2035 0.0687 -0.0026 0.0483 81 CYS A CB ? ? ?
817639 S SG . CYS A 81 0.1843 0.2020 0.1994 0.0593 0.0039 0.0413 81 CYS A SG ? ? ?
818640 C C . CYS A 81 0.2028 0.2287 0.2446 0.0780 0.0127 0.0489 81 CYS A C ? ? ?
819641 O O . CYS A 81 0.1943 0.2058 0.2273 0.0767 0.0210 0.0453 81 CYS A O ? ? ?
820642 N N . LYS A 82 0.1933 0.2373 0.2530 0.0791 0.0108 0.0498 82 LYS A N ? ? ?
821643 C CA . LYS A 82 0.2042 0.2536 0.2730 0.0779 0.0191 0.0468 82 LYS A CA ? ? ?
822644 C CB . LYS A 82 0.2648 0.3315 0.3563 0.0852 0.0202 0.0509 82 LYS A CB ? ? ?
823645 C CG . LYS A 82 0.4578 0.5189 0.5536 0.0970 0.0246 0.0548 82 LYS A CG ? ? ?
824646 C CD . LYS A 82 0.6333 0.6778 0.7206 0.1001 0.0379 0.0505 82 LYS A CD ? ? ?
825647 C CE . LYS A 82 0.6613 0.7016 0.7575 0.1131 0.0430 0.0545 82 LYS A CE ? ? ?
826648 N NZ . LYS A 82 0.7479 0.7711 0.8358 0.1161 0.0564 0.0487 82 LYS A NZ ? ? ?
827649 C C . LYS A 82 0.1829 0.2386 0.2507 0.0676 0.0162 0.0432 82 LYS A C ? ? ?
828650 O O . LYS A 82 0.1847 0.2508 0.2582 0.0639 0.0071 0.0441 82 LYS A O ? ? ?
829651 N N . SER A 83 0.1498 0.1978 0.2092 0.0631 0.0237 0.0389 83 SER A N ? ? ?
830652 C CA . SER A 83 0.1367 0.1875 0.1931 0.0539 0.0217 0.0363 83 SER A CA ? ? ?
831653 C CB . SER A 83 0.1457 0.1807 0.1830 0.0491 0.0221 0.0322 83 SER A CB ? ? ?
832654 O OG . SER A 83 0.1655 0.1962 0.1964 0.0485 0.0150 0.0329 83 SER A OG ? ? ?
833655 C C . SER A 83 0.1461 0.2043 0.2100 0.0525 0.0295 0.0360 83 SER A C ? ? ?
834656 O O . SER A 83 0.1409 0.1962 0.2045 0.0577 0.0385 0.0354 83 SER A O ? ? ?
835657 N N . LEU A 84 0.1419 0.2089 0.2122 0.0456 0.0264 0.0367 84 LEU A N ? ? ?
836658 C CA . LEU A 84 0.1376 0.2119 0.2141 0.0430 0.0336 0.0379 84 LEU A CA ? ? ?
837659 C CB . LEU A 84 0.1567 0.2499 0.2577 0.0449 0.0340 0.0423 84 LEU A CB ? ? ?
838660 C CG . LEU A 84 0.2002 0.3022 0.3092 0.0415 0.0426 0.0450 84 LEU A CG ? ? ?
839661 C CD1 . LEU A 84 0.2436 0.3381 0.3400 0.0459 0.0550 0.0431 84 LEU A CD1 ? ? ?
840662 C CD2 . LEU A 84 0.2442 0.3667 0.3809 0.0421 0.0425 0.0496 84 LEU A CD2 ? ? ?
841663 C C . LEU A 84 0.1218 0.1931 0.1917 0.0343 0.0301 0.0370 84 LEU A C ? ? ?
842664 O O . LEU A 84 0.1305 0.2063 0.2075 0.0300 0.0219 0.0376 84 LEU A O ? ? ?
843665 N N . VAL A 85 0.1125 0.1755 0.1682 0.0322 0.0361 0.0354 85 VAL A N ? ? ?
844666 C CA . VAL A 85 0.1098 0.1695 0.1587 0.0251 0.0336 0.0356 85 VAL A CA ? ? ?
845667 C CB . VAL A 85 0.1188 0.1650 0.1468 0.0242 0.0350 0.0315 85 VAL A CB ? ? ?
846668 C CG1 . VAL A 85 0.1198 0.1638 0.1422 0.0180 0.0315 0.0327 85 VAL A CG1 ? ? ?
847669 C CG2 . VAL A 85 0.1276 0.1646 0.1486 0.0264 0.0307 0.0276 85 VAL A CG2 ? ? ?
848670 C C . VAL A 85 0.1106 0.1794 0.1677 0.0223 0.0395 0.0403 85 VAL A C ? ? ?
849671 O O . VAL A 85 0.1196 0.1919 0.1767 0.0258 0.0488 0.0414 85 VAL A O ? ? ?
850672 N N . LYS A 86 0.1198 0.1916 0.1841 0.0161 0.0347 0.0432 86 LYS A N ? ? ?
851673 C CA . LYS A 86 0.1265 0.2043 0.1970 0.0121 0.0400 0.0489 86 LYS A CA ? ? ?
852674 C CB . LYS A 86 0.1431 0.2347 0.2390 0.0094 0.0385 0.0528 86 LYS A CB ? ? ?
853675 C CG . LYS A 86 0.1736 0.2765 0.2831 0.0151 0.0417 0.0527 86 LYS A CG ? ? ?
854676 C CD . LYS A 86 0.2288 0.3472 0.3654 0.0115 0.0385 0.0563 86 LYS A CD ? ? ?
855677 C CE . LYS A 86 0.2881 0.4197 0.4402 0.0181 0.0410 0.0567 86 LYS A CE ? ? ?
856678 N NZ . LYS A 86 0.3683 0.5178 0.5493 0.0140 0.0385 0.0605 86 LYS A NZ ? ? ?
857679 C C . LYS A 86 0.1237 0.1933 0.1849 0.0067 0.0361 0.0503 86 LYS A C ? ? ?
858680 O O . LYS A 86 0.1117 0.1746 0.1693 0.0052 0.0279 0.0469 86 LYS A O ? ? ?
859681 N N . TRP A 87 0.1221 0.1928 0.1800 0.0042 0.0423 0.0559 87 TRP A N ? ? ?
860682 C CA . TRP A 87 0.1191 0.1837 0.1728 -0.0007 0.0385 0.0596 87 TRP A CA ? ? ?
861683 C CB . TRP A 87 0.1368 0.2006 0.1781 -0.0013 0.0465 0.0658 87 TRP A CB ? ? ?
862684 C CG . TRP A 87 0.1535 0.2116 0.1717 0.0025 0.0495 0.0616 87 TRP A CG ? ? ?
863685 C CD1 . TRP A 87 0.1720 0.2326 0.1803 0.0060 0.0592 0.0611 87 TRP A CD1 ? ? ?
864686 N NE1 . TRP A 87 0.1838 0.2360 0.1702 0.0081 0.0581 0.0553 87 TRP A NE1 ? ? ?
865687 C CE2 . TRP A 87 0.1936 0.2392 0.1772 0.0059 0.0477 0.0529 87 TRP A CE2 ? ? ?
866688 C CZ2 . TRP A 87 0.2020 0.2398 0.1694 0.0060 0.0424 0.0473 87 TRP A CZ2 ? ? ?
867689 C CH2 . TRP A 87 0.1933 0.2277 0.1647 0.0038 0.0330 0.0465 87 TRP A CH2 ? ? ?
868690 C CZ3 . TRP A 87 0.1863 0.2230 0.1751 0.0017 0.0287 0.0501 87 TRP A CZ3 ? ? ?
869691 C CE3 . TRP A 87 0.1596 0.2028 0.1636 0.0010 0.0330 0.0548 87 TRP A CE3 ? ? ?
870692 C CD2 . TRP A 87 0.1582 0.2069 0.1609 0.0029 0.0426 0.0567 87 TRP A CD2 ? ? ?
871693 C C . TRP A 87 0.1123 0.1811 0.1871 -0.0058 0.0341 0.0628 87 TRP A C ? ? ?
872694 O O . TRP A 87 0.1453 0.2228 0.2344 -0.0083 0.0396 0.0684 87 TRP A O ? ? ?
873695 N N . GLU A 88 0.1136 0.1763 0.1906 -0.0076 0.0248 0.0588 88 GLU A N ? ? ?
874696 C CA . GLU A 88 0.1204 0.1833 0.2143 -0.0132 0.0200 0.0606 88 GLU A CA ? ? ?
875697 C CB . GLU A 88 0.1535 0.2094 0.2466 -0.0133 0.0101 0.0533 88 GLU A CB ? ? ?
876698 C CG . GLU A 88 0.1951 0.2497 0.3050 -0.0191 0.0046 0.0529 88 GLU A CG ? ? ?
877699 C CD . GLU A 88 0.2880 0.3357 0.3953 -0.0187 -0.0043 0.0444 88 GLU A CD ? ? ?
878700 O OE1 . GLU A 88 0.3911 0.4436 0.4983 -0.0164 -0.0082 0.0388 88 GLU A OE1 ? ? ?
879701 O OE2 . GLU A 88 0.3376 0.3751 0.4426 -0.0201 -0.0069 0.0438 88 GLU A OE2 ? ? ?
880702 C C . GLU A 88 0.1317 0.1895 0.2241 -0.0169 0.0233 0.0687 88 GLU A C ? ? ?
881703 O O . GLU A 88 0.1401 0.2012 0.2481 -0.0218 0.0257 0.0744 88 GLU A O ? ? ?
882704 N N . SER A 89 0.1201 0.1699 0.1941 -0.0145 0.0233 0.0696 89 SER A N ? ? ?
883705 C CA . SER A 89 0.1362 0.1810 0.2048 -0.0166 0.0261 0.0784 89 SER A CA ? ? ?
884706 C CB . SER A 89 0.1619 0.1970 0.2373 -0.0191 0.0189 0.0789 89 SER A CB ? ? ?
885707 O OG . SER A 89 0.1707 0.2006 0.2370 -0.0157 0.0121 0.0713 89 SER A OG ? ? ?
886708 C C . SER A 89 0.1336 0.1759 0.1789 -0.0124 0.0283 0.0787 89 SER A C ? ? ?
887709 O O . SER A 89 0.1329 0.1764 0.1689 -0.0089 0.0278 0.0715 89 SER A O ? ? ?
888710 N N . GLU A 90 0.1494 0.1878 0.1853 -0.0132 0.0302 0.0870 90 GLU A N ? ? ?
889711 C CA . GLU A 90 0.1716 0.2088 0.1845 -0.0100 0.0316 0.0875 90 GLU A CA ? ? ?
890712 C CB . GLU A 90 0.2105 0.2434 0.2158 -0.0111 0.0319 0.0987 90 GLU A CB ? ? ?
891713 C CG . GLU A 90 0.2472 0.2794 0.2273 -0.0081 0.0315 0.0992 90 GLU A CG ? ? ?
892714 C CD . GLU A 90 0.3077 0.3375 0.2767 -0.0086 0.0333 0.1120 90 GLU A CD ? ? ?
893715 O OE1 . GLU A 90 0.3255 0.3502 0.3061 -0.0103 0.0304 0.1201 90 GLU A OE1 ? ? ?
894716 O OE2 . GLU A 90 0.3861 0.4184 0.3338 -0.0070 0.0377 0.1139 90 GLU A OE2 ? ? ?
895717 C C . GLU A 90 0.1762 0.2098 0.1796 -0.0071 0.0242 0.0781 90 GLU A C ? ? ?
896718 O O . GLU A 90 0.1936 0.2282 0.1816 -0.0047 0.0260 0.0735 90 GLU A O ? ? ?
897719 N N . ASN A 91 0.1536 0.1828 0.1667 -0.0076 0.0165 0.0750 91 ASN A N ? ? ?
898720 C CA . ASN A 91 0.1590 0.1856 0.1651 -0.0053 0.0103 0.0674 91 ASN A CA ? ? ?
899721 C CB . ASN A 91 0.2187 0.2403 0.2262 -0.0050 0.0037 0.0710 91 ASN A CB ? ? ?
900722 C CG . ASN A 91 0.2708 0.2922 0.2666 -0.0047 0.0045 0.0804 91 ASN A CG ? ? ?
901723 O OD1 . ASN A 91 0.3718 0.3899 0.3737 -0.0058 0.0049 0.0896 91 ASN A OD1 ? ? ?
902724 N ND2 . ASN A 91 0.3067 0.3309 0.2851 -0.0035 0.0049 0.0786 91 ASN A ND2 ? ? ?
903725 C C . ASN A 91 0.1352 0.1620 0.1499 -0.0047 0.0078 0.0584 91 ASN A C ? ? ?
904726 O O . ASN A 91 0.1156 0.1398 0.1274 -0.0034 0.0030 0.0528 91 ASN A O ? ? ?
905727 N N . LYS A 92 0.1193 0.1500 0.1444 -0.0056 0.0111 0.0574 92 LYS A N ? ? ?
906728 C CA . LYS A 92 0.1132 0.1445 0.1462 -0.0049 0.0080 0.0502 92 LYS A CA ? ? ?
907729 C CB . LYS A 92 0.1366 0.1661 0.1852 -0.0077 0.0039 0.0505 92 LYS A CB ? ? ?
908730 C CG . LYS A 92 0.1457 0.1759 0.1995 -0.0069 -0.0004 0.0427 92 LYS A CG ? ? ?
909731 C CD . LYS A 92 0.1998 0.2263 0.2660 -0.0098 -0.0053 0.0409 92 LYS A CD ? ? ?
910732 C CE . LYS A 92 0.2569 0.2839 0.3242 -0.0087 -0.0099 0.0329 92 LYS A CE ? ? ?
911733 N NZ . LYS A 92 0.3078 0.3316 0.3870 -0.0123 -0.0147 0.0299 92 LYS A NZ ? ? ?
912734 C C . LYS A 92 0.1158 0.1535 0.1508 -0.0033 0.0127 0.0483 92 LYS A C ? ? ?
913735 O O . LYS A 92 0.1323 0.1759 0.1764 -0.0046 0.0172 0.0527 92 LYS A O ? ? ?
914736 N N . MET A 93 0.1040 0.1404 0.1316 -0.0002 0.0122 0.0422 93 MET A N ? ? ?
915737 C CA . MET A 93 0.1121 0.1534 0.1427 0.0027 0.0159 0.0403 93 MET A CA ? ? ?
916738 C CB . MET A 93 0.1454 0.1828 0.1611 0.0061 0.0198 0.0366 93 MET A CB ? ? ?
917739 C CG . MET A 93 0.1877 0.2179 0.1948 0.0064 0.0153 0.0315 93 MET A CG ? ? ?
918740 S SD . MET A 93 0.2579 0.2820 0.2489 0.0090 0.0200 0.0268 93 MET A SD ? ? ?
919741 C CE . MET A 93 0.3797 0.4020 0.3586 0.0059 0.0193 0.0282 93 MET A CE ? ? ?
920742 C C . MET A 93 0.1092 0.1518 0.1490 0.0033 0.0103 0.0364 93 MET A C ? ? ?
921743 O O . MET A 93 0.1128 0.1501 0.1495 0.0028 0.0050 0.0329 93 MET A O ? ? ?
922744 N N . VAL A 94 0.1035 0.1541 0.1548 0.0046 0.0116 0.0373 94 VAL A N ? ? ?
923745 C CA . VAL A 94 0.1117 0.1651 0.1705 0.0056 0.0056 0.0341 94 VAL A CA ? ? ?
924746 C CB . VAL A 94 0.1529 0.2132 0.2292 0.0013 0.0014 0.0356 94 VAL A CB ? ? ?
925747 C CG1 . VAL A 94 0.2031 0.2670 0.2849 0.0023 -0.0062 0.0315 94 VAL A CG1 ? ? ?
926748 C CG2 . VAL A 94 0.2015 0.2552 0.2780 -0.0036 -0.0008 0.0364 94 VAL A CG2 ? ? ?
927749 C C . VAL A 94 0.1044 0.1621 0.1636 0.0111 0.0086 0.0337 94 VAL A C ? ? ?
928750 O O . VAL A 94 0.1142 0.1780 0.1786 0.0130 0.0152 0.0368 94 VAL A O ? ? ?
929751 N N . CYS A 95 0.1043 0.1586 0.1583 0.0141 0.0042 0.0304 95 CYS A N ? ? ?
930752 C CA . CYS A 95 0.1116 0.1677 0.1653 0.0202 0.0062 0.0306 95 CYS A CA ? ? ?
931753 C CB . CYS A 95 0.1297 0.1738 0.1668 0.0228 0.0085 0.0280 95 CYS A CB ? ? ?
932754 S SG . CYS A 95 0.1625 0.2048 0.1985 0.0310 0.0121 0.0289 95 CYS A SG ? ? ?
933755 C C . CYS A 95 0.1367 0.2000 0.1996 0.0218 -0.0014 0.0305 95 CYS A C ? ? ?
934756 O O . CYS A 95 0.1493 0.2085 0.2063 0.0203 -0.0079 0.0277 95 CYS A O ? ? ?
935757 N N . GLU A 96 0.1234 0.1979 0.2001 0.0254 -0.0003 0.0335 96 GLU A N ? ? ?
936758 C CA . GLU A 96 0.1551 0.2381 0.2405 0.0281 -0.0083 0.0341 96 GLU A CA ? ? ?
937759 C CB . GLU A 96 0.2293 0.3292 0.3380 0.0263 -0.0095 0.0369 96 GLU A CB ? ? ?
938760 C CG . GLU A 96 0.4632 0.5752 0.5838 0.0290 -0.0190 0.0377 96 GLU A CG ? ? ?
939761 C CD . GLU A 96 0.6919 0.8222 0.8386 0.0256 -0.0211 0.0400 96 GLU A CD ? ? ?
940762 O OE1 . GLU A 96 0.7510 0.8888 0.9098 0.0276 -0.0119 0.0439 96 GLU A OE1 ? ? ?
941763 O OE2 . GLU A 96 0.7169 0.8540 0.8722 0.0205 -0.0315 0.0375 96 GLU A OE2 ? ? ?
942764 C C . GLU A 96 0.1443 0.2233 0.2229 0.0365 -0.0062 0.0357 96 GLU A C ? ? ?
943765 O O . GLU A 96 0.1395 0.2165 0.2181 0.0408 0.0023 0.0373 96 GLU A O ? ? ?
944766 N N . GLN A 97 0.1422 0.2189 0.2137 0.0388 -0.0137 0.0353 97 GLN A N ? ? ?
945767 C CA . GLN A 97 0.1487 0.2191 0.2122 0.0466 -0.0123 0.0379 97 GLN A CA ? ? ?
946768 C CB . GLN A 97 0.1707 0.2262 0.2136 0.0455 -0.0131 0.0358 97 GLN A CB ? ? ?
947769 C CG . GLN A 97 0.1799 0.2240 0.2125 0.0406 -0.0064 0.0322 97 GLN A CG ? ? ?
948770 C CD . GLN A 97 0.2121 0.2440 0.2281 0.0393 -0.0068 0.0305 97 GLN A CD ? ? ?
949771 O OE1 . GLN A 97 0.1978 0.2304 0.2081 0.0392 -0.0130 0.0303 97 GLN A OE1 ? ? ?
950772 N NE2 . GLN A 97 0.2208 0.2416 0.2282 0.0383 0.0000 0.0292 97 GLN A NE2 ? ? ?
951773 C C . GLN A 97 0.1839 0.2670 0.2587 0.0519 -0.0203 0.0416 97 GLN A C ? ? ?
952774 O O . GLN A 97 0.1840 0.2762 0.2639 0.0483 -0.0298 0.0402 97 GLN A O ? ? ?
953775 N N . LYS A 98 0.1761 0.2594 0.2548 0.0606 -0.0166 0.0462 98 LYS A N ? ? ?
954776 C CA . LYS A 98 0.2032 0.2984 0.2923 0.0675 -0.0245 0.0511 98 LYS A CA ? ? ?
955777 C CB . LYS A 98 0.2968 0.4092 0.4115 0.0714 -0.0217 0.0542 98 LYS A CB ? ? ?
956778 C CG . LYS A 98 0.4691 0.6000 0.6027 0.0642 -0.0283 0.0525 98 LYS A CG ? ? ?
957779 C CD . LYS A 98 0.6728 0.8024 0.8098 0.0561 -0.0202 0.0491 98 LYS A CD ? ? ?
958780 C CE . LYS A 98 0.8603 1.0060 1.0162 0.0481 -0.0268 0.0479 98 LYS A CE ? ? ?
959781 N NZ . LYS A 98 1.0057 1.1471 1.1510 0.0415 -0.0382 0.0432 98 LYS A NZ ? ? ?
960782 C C . LYS A 98 0.1952 0.2775 0.2710 0.0760 -0.0227 0.0555 98 LYS A C ? ? ?
961783 O O . LYS A 98 0.2048 0.2757 0.2771 0.0799 -0.0126 0.0562 98 LYS A O ? ? ?
962784 N N . LEU A 99 0.1908 0.2742 0.2584 0.0786 -0.0325 0.0585 99 LEU A N ? ? ?
963785 C CA . LEU A 99 0.2327 0.3032 0.2869 0.0865 -0.0312 0.0643 99 LEU A CA ? ? ?
964786 C CB . LEU A 99 0.2623 0.3357 0.3044 0.0876 -0.0431 0.0672 99 LEU A CB ? ? ?
965787 C CG . LEU A 99 0.2891 0.3550 0.3124 0.0789 -0.0453 0.0613 99 LEU A CG ? ? ?
966788 C CD1 . LEU A 99 0.3486 0.4201 0.3603 0.0804 -0.0577 0.0633 99 LEU A CD1 ? ? ?
967789 C CD2 . LEU A 99 0.3226 0.3678 0.3288 0.0775 -0.0349 0.0609 99 LEU A CD2 ? ? ?
968790 C C . LEU A 99 0.2790 0.3536 0.3484 0.0975 -0.0277 0.0708 99 LEU A C ? ? ?
969791 O O . LEU A 99 0.2596 0.3534 0.3496 0.1009 -0.0330 0.0732 99 LEU A O ? ? ?
970792 N N . LEU A 100 0.2874 0.3437 0.3477 0.1029 -0.0185 0.0735 100 LEU A N ? ? ?
971793 C CA . LEU A 100 0.3154 0.3714 0.3884 0.1146 -0.0140 0.0795 100 LEU A CA ? ? ?
972794 C CB . LEU A 100 0.3338 0.3650 0.3946 0.1169 -0.0017 0.0788 100 LEU A CB ? ? ?
973795 C CG . LEU A 100 0.3758 0.3997 0.4351 0.1101 0.0091 0.0700 100 LEU A CG ? ? ?
974796 C CD1 . LEU A 100 0.4551 0.4558 0.5059 0.1140 0.0202 0.0691 100 LEU A CD1 ? ? ?
975797 C CD2 . LEU A 100 0.4090 0.4507 0.4887 0.1111 0.0117 0.0677 100 LEU A CD2 ? ? ?
976798 C C . LEU A 100 0.4080 0.4709 0.4828 0.1237 -0.0245 0.0890 100 LEU A C ? ? ?
977799 O O . LEU A 100 0.3903 0.4672 0.4850 0.1326 -0.0271 0.0941 100 LEU A O ? ? ?
978800 N N . LYS A 101 0.4658 0.5187 0.5191 0.1218 -0.0300 0.0916 101 LYS A N ? ? ?
979801 C CA . LYS A 101 0.5447 0.6026 0.5936 0.1297 -0.0408 0.1011 101 LYS A CA ? ? ?
980802 C CB . LYS A 101 0.6019 0.6370 0.6360 0.1372 -0.0346 0.1093 101 LYS A CB ? ? ?
981803 C CG . LYS A 101 0.7213 0.7487 0.7704 0.1475 -0.0251 0.1133 101 LYS A CG ? ? ?
982804 C CD . LYS A 101 0.8021 0.8061 0.8377 0.1554 -0.0202 0.1228 101 LYS A CD ? ? ?
983805 C CE . LYS A 101 0.8637 0.8734 0.8916 0.1632 -0.0325 0.1348 101 LYS A CE ? ? ?
984806 N NZ . LYS A 101 0.9531 0.9413 0.9741 0.1736 -0.0271 0.1464 101 LYS A NZ ? ? ?
985807 C C . LYS A 101 0.4601 0.5246 0.4935 0.1220 -0.0521 0.0983 101 LYS A C ? ? ?
986808 O O . LYS A 101 0.4819 0.5370 0.5007 0.1124 -0.0483 0.0914 101 LYS A O ? ? ?
987809 N N . GLY A 102 0.4566 0.5374 0.4935 0.1269 -0.0661 0.1036 102 GLY A N ? ? ?
988810 C CA . GLY A 102 0.4459 0.5315 0.4646 0.1215 -0.0777 0.1015 102 GLY A CA ? ? ?
989811 C C . GLY A 102 0.4529 0.5519 0.4792 0.1101 -0.0827 0.0900 102 GLY A C ? ? ?
990812 O O . GLY A 102 0.3991 0.5086 0.4482 0.1071 -0.0796 0.0856 102 GLY A O ? ? ?
991813 N N . GLU A 103 0.4484 0.5463 0.4547 0.1039 -0.0900 0.0855 103 GLU A N ? ? ?
992814 C CA . GLU A 103 0.4813 0.5888 0.4921 0.0930 -0.0953 0.0743 103 GLU A CA ? ? ?
993815 C CB . GLU A 103 0.5976 0.7261 0.6154 0.0933 -0.1131 0.0736 103 GLU A CB ? ? ?
994816 C CG . GLU A 103 0.7025 0.8508 0.7515 0.0992 -0.1177 0.0789 103 GLU A CG ? ? ?
995817 C CD . GLU A 103 0.9004 1.0724 0.9614 0.0975 -0.1361 0.0769 103 GLU A CD ? ? ?
996818 O OE1 . GLU A 103 1.1105 1.2820 1.1517 0.0925 -0.1463 0.0713 103 GLU A OE1 ? ? ?
997819 O OE2 . GLU A 103 1.1081 1.2997 1.1989 0.1011 -0.1402 0.0804 103 GLU A OE2 ? ? ?
998820 C C . GLU A 103 0.3868 0.4783 0.3723 0.0857 -0.0905 0.0678 103 GLU A C ? ? ?
999821 O O . GLU A 103 0.4001 0.4760 0.3642 0.0888 -0.0848 0.0724 103 GLU A O ? ? ?
1000822 N N . GLY A 104 0.3531 0.4487 0.3429 0.0760 -0.0922 0.0573 104 GLY A N ? ? ?
1001823 C CA . GLY A 104 0.3233 0.4053 0.2935 0.0692 -0.0869 0.0502 104 GLY A CA ? ? ?
1002824 C C . GLY A 104 0.2840 0.3708 0.2673 0.0595 -0.0872 0.0398 104 GLY A C ? ? ?
1003825 O O . GLY A 104 0.2803 0.3809 0.2870 0.0576 -0.0914 0.0387 104 GLY A O ? ? ?
1004826 N N . PRO A 105 0.2583 0.3338 0.2279 0.0534 -0.0823 0.0326 105 PRO A N ? ? ?
1005827 C CA . PRO A 105 0.2486 0.3256 0.2297 0.0447 -0.0815 0.0236 105 PRO A CA ? ? ?
1006828 C CB . PRO A 105 0.2798 0.3416 0.2420 0.0416 -0.0737 0.0188 105 PRO A CB ? ? ?
1007829 C CG . PRO A 105 0.2904 0.3463 0.2283 0.0473 -0.0747 0.0231 105 PRO A CG ? ? ?
1008830 C CD . PRO A 105 0.2884 0.3494 0.2318 0.0550 -0.0766 0.0336 105 PRO A CD ? ? ?
1009831 C C . PRO A 105 0.2235 0.3039 0.2275 0.0431 -0.0742 0.0256 105 PRO A C ? ? ?
1010832 O O . PRO A 105 0.2256 0.3008 0.2309 0.0477 -0.0656 0.0318 105 PRO A O ? ? ?
1011833 N N . LYS A 106 0.2066 0.2946 0.2274 0.0363 -0.0773 0.0202 106 LYS A N ? ? ?
1012834 C CA . LYS A 106 0.1961 0.2865 0.2359 0.0337 -0.0694 0.0216 106 LYS A CA ? ? ?
1013835 C CB . LYS A 106 0.2481 0.3504 0.3088 0.0267 -0.0755 0.0175 106 LYS A CB ? ? ?
1014836 C CG . LYS A 106 0.3472 0.4528 0.4268 0.0242 -0.0666 0.0203 106 LYS A CG ? ? ?
1015837 C CD . LYS A 106 0.4125 0.5317 0.5162 0.0175 -0.0717 0.0185 106 LYS A CD ? ? ?
1016838 C CE . LYS A 106 0.5609 0.6818 0.6797 0.0154 -0.0609 0.0223 106 LYS A CE ? ? ?
1017839 N NZ . LYS A 106 0.6224 0.7545 0.7646 0.0074 -0.0643 0.0211 106 LYS A NZ ? ? ?
1018840 C C . LYS A 106 0.1670 0.2421 0.1961 0.0309 -0.0589 0.0193 106 LYS A C ? ? ?
1019841 O O . LYS A 106 0.1594 0.2275 0.1787 0.0265 -0.0601 0.0131 106 LYS A O ? ? ?
1020842 N N . THR A 107 0.1545 0.2248 0.1857 0.0337 -0.0490 0.0238 107 THR A N ? ? ?
1021843 C CA . THR A 107 0.1282 0.1857 0.1501 0.0310 -0.0401 0.0219 107 THR A CA ? ? ?
1022844 C CB . THR A 107 0.1499 0.1967 0.1567 0.0361 -0.0342 0.0255 107 THR A CB ? ? ?
1023845 O OG1 . THR A 107 0.1384 0.1873 0.1528 0.0416 -0.0302 0.0311 107 THR A OG1 ? ? ?
1024846 C CG2 . THR A 107 0.1808 0.2248 0.1716 0.0390 -0.0395 0.0259 107 THR A CG2 ? ? ?
1025847 C C . THR A 107 0.1348 0.1941 0.1700 0.0281 -0.0335 0.0226 107 THR A C ? ? ?
1026848 O O . THR A 107 0.1092 0.1772 0.1581 0.0303 -0.0320 0.0263 107 THR A O ? ? ?
1027849 N N . SER A 108 0.1110 0.1625 0.1417 0.0235 -0.0294 0.0195 108 SER A N ? ? ?
1028850 C CA . SER A 108 0.1256 0.1767 0.1637 0.0208 -0.0228 0.0207 108 SER A CA ? ? ?
1029851 C CB . SER A 108 0.1620 0.2213 0.2159 0.0156 -0.0261 0.0199 108 SER A CB ? ? ?
1030852 O OG . SER A 108 0.2077 0.2634 0.2586 0.0115 -0.0320 0.0147 108 SER A OG ? ? ?
1031853 C C . SER A 108 0.1167 0.1567 0.1433 0.0185 -0.0182 0.0185 108 SER A C ? ? ?
1032854 O O . SER A 108 0.1212 0.1551 0.1371 0.0185 -0.0199 0.0156 108 SER A O ? ? ?
1033855 N N . TRP A 109 0.1161 0.1545 0.1451 0.0168 -0.0125 0.0199 109 TRP A N ? ? ?
1034856 C CA . TRP A 109 0.1125 0.1433 0.1342 0.0140 -0.0099 0.0180 109 TRP A CA ? ? ?
1035857 C CB . TRP A 109 0.1207 0.1437 0.1306 0.0161 -0.0051 0.0179 109 TRP A CB ? ? ?
1036858 C CG . TRP A 109 0.1262 0.1480 0.1349 0.0188 0.0005 0.0201 109 TRP A CG ? ? ?
1037859 C CD1 . TRP A 109 0.1470 0.1668 0.1534 0.0235 0.0025 0.0216 109 TRP A CD1 ? ? ?
1038860 N NE1 . TRP A 109 0.1350 0.1524 0.1405 0.0252 0.0086 0.0222 109 TRP A NE1 ? ? ?
1039861 C CE2 . TRP A 109 0.1316 0.1501 0.1371 0.0212 0.0104 0.0212 109 TRP A CE2 ? ? ?
1040862 C CZ2 . TRP A 109 0.1391 0.1560 0.1412 0.0211 0.0160 0.0209 109 TRP A CZ2 ? ? ?
1041863 C CH2 . TRP A 109 0.1525 0.1714 0.1534 0.0169 0.0159 0.0211 109 TRP A CH2 ? ? ?
1042864 C CZ3 . TRP A 109 0.1476 0.1693 0.1528 0.0133 0.0107 0.0219 109 TRP A CZ3 ? ? ?
1043865 C CE3 . TRP A 109 0.1380 0.1605 0.1472 0.0134 0.0056 0.0210 109 TRP A CE3 ? ? ?
1044866 C CD2 . TRP A 109 0.1460 0.1673 0.1544 0.0173 0.0053 0.0207 109 TRP A CD2 ? ? ?
1045867 C C . TRP A 109 0.1131 0.1463 0.1421 0.0107 -0.0074 0.0201 109 TRP A C ? ? ?
1046868 O O . TRP A 109 0.1207 0.1603 0.1581 0.0110 -0.0053 0.0232 109 TRP A O ? ? ?
1047869 N N . THR A 110 0.0959 0.1244 0.1222 0.0078 -0.0076 0.0190 110 THR A N ? ? ?
1048870 C CA . THR A 110 0.0795 0.1087 0.1097 0.0051 -0.0054 0.0221 110 THR A CA ? ? ?
1049871 C CB . THR A 110 0.0983 0.1286 0.1395 0.0015 -0.0092 0.0225 110 THR A CB ? ? ?
1050872 O OG1 . THR A 110 0.1193 0.1436 0.1577 0.0010 -0.0125 0.0187 110 THR A OG1 ? ? ?
1051873 C CG2 . THR A 110 0.1001 0.1369 0.1519 0.0008 -0.0126 0.0219 110 THR A CG2 ? ? ?
1052874 C C . THR A 110 0.0878 0.1113 0.1086 0.0048 -0.0037 0.0215 110 THR A C ? ? ?
1053875 O O . THR A 110 0.0990 0.1186 0.1148 0.0053 -0.0052 0.0182 110 THR A O ? ? ?
1054876 N N . ARG A 111 0.0834 0.1075 0.1019 0.0037 -0.0007 0.0248 111 ARG A N ? ? ?
1055877 C CA . ARG A 111 0.0972 0.1180 0.1085 0.0028 -0.0009 0.0248 111 ARG A CA ? ? ?
1056878 C CB . ARG A 111 0.1221 0.1407 0.1223 0.0037 0.0024 0.0229 111 ARG A CB ? ? ?
1057879 C CG . ARG A 111 0.1319 0.1468 0.1286 0.0052 0.0027 0.0186 111 ARG A CG ? ? ?
1058880 C CD . ARG A 111 0.1563 0.1669 0.1432 0.0051 0.0059 0.0162 111 ARG A CD ? ? ?
1059881 N NE . ARG A 111 0.1934 0.1992 0.1777 0.0053 0.0062 0.0131 111 ARG A NE ? ? ?
1060882 C CZ . ARG A 111 0.1908 0.1934 0.1745 0.0081 0.0083 0.0128 111 ARG A CZ ? ? ?
1061883 N NH1 . ARG A 111 0.2021 0.2072 0.1890 0.0113 0.0098 0.0148 111 ARG A NH1 ? ? ?
1062884 N NH2 . ARG A 111 0.2191 0.2166 0.1997 0.0078 0.0091 0.0111 111 ARG A NH2 ? ? ?
1063885 C C . ARG A 111 0.1085 0.1306 0.1226 0.0009 -0.0010 0.0301 111 ARG A C ? ? ?
1064886 O O . ARG A 111 0.1039 0.1292 0.1193 0.0005 0.0025 0.0340 111 ARG A O ? ? ?
1065887 N N . GLU A 112 0.1081 0.1281 0.1239 0.0002 -0.0045 0.0309 112 GLU A N ? ? ?
1066888 C CA . GLU A 112 0.1438 0.1636 0.1624 -0.0011 -0.0051 0.0373 112 GLU A CA ? ? ?
1067889 C CB . GLU A 112 0.2190 0.2368 0.2506 -0.0024 -0.0069 0.0388 112 GLU A CB ? ? ?
1068890 C CG . GLU A 112 0.3116 0.3254 0.3487 -0.0014 -0.0108 0.0339 112 GLU A CG ? ? ?
1069891 C CD . GLU A 112 0.4744 0.4850 0.5234 -0.0033 -0.0126 0.0332 112 GLU A CD ? ? ?
1070892 O OE1 . GLU A 112 0.3089 0.3171 0.3647 -0.0052 -0.0123 0.0392 112 GLU A OE1 ? ? ?
1071893 O OE2 . GLU A 112 0.3333 0.3434 0.3841 -0.0031 -0.0143 0.0267 112 GLU A OE2 ? ? ?
1072894 C C . GLU A 112 0.1475 0.1665 0.1615 -0.0005 -0.0083 0.0386 112 GLU A C ? ? ?
1073895 O O . GLU A 112 0.1218 0.1401 0.1373 0.0005 -0.0109 0.0343 112 GLU A O ? ? ?
1074896 N N . LEU A 113 0.1379 0.1580 0.1464 -0.0009 -0.0080 0.0449 113 LEU A N ? ? ?
1075897 C CA . LEU A 113 0.1680 0.1887 0.1730 -0.0001 -0.0124 0.0478 113 LEU A CA ? ? ?
1076898 C CB . LEU A 113 0.2334 0.2567 0.2239 -0.0007 -0.0116 0.0518 113 LEU A CB ? ? ?
1077899 C CG . LEU A 113 0.2651 0.2897 0.2434 -0.0014 -0.0099 0.0453 113 LEU A CG ? ? ?
1078900 C CD1 . LEU A 113 0.3186 0.3448 0.2807 -0.0019 -0.0088 0.0488 113 LEU A CD1 ? ? ?
1079901 C CD2 . LEU A 113 0.2910 0.3169 0.2708 -0.0017 -0.0148 0.0393 113 LEU A CD2 ? ? ?
1080902 C C . LEU A 113 0.1768 0.1943 0.1926 0.0006 -0.0148 0.0540 113 LEU A C ? ? ?
1081903 O O . LEU A 113 0.1952 0.2106 0.2135 -0.0006 -0.0122 0.0602 113 LEU A O ? ? ?
1082904 N N . THR A 114 0.1315 0.1481 0.1547 0.0027 -0.0191 0.0524 114 THR A N ? ? ?
1083905 C CA . THR A 114 0.1532 0.1647 0.1878 0.0044 -0.0212 0.0574 114 THR A CA ? ? ?
1084906 C CB . THR A 114 0.1826 0.1921 0.2277 0.0068 -0.0229 0.0507 114 THR A CB ? ? ?
1085907 O OG1 . THR A 114 0.2106 0.2266 0.2533 0.0085 -0.0256 0.0481 114 THR A OG1 ? ? ?
1086908 C CG2 . THR A 114 0.2802 0.2878 0.3271 0.0053 -0.0201 0.0424 114 THR A CG2 ? ? ?
1087909 C C . THR A 114 0.1627 0.1757 0.1937 0.0063 -0.0249 0.0668 114 THR A C ? ? ?
1088910 O O . THR A 114 0.1689 0.1880 0.1886 0.0062 -0.0270 0.0676 114 THR A O ? ? ?
1089911 N N . ASN A 115 0.1613 0.1680 0.2020 0.0080 -0.0260 0.0736 115 ASN A N ? ? ?
1090912 C CA . ASN A 115 0.2129 0.2195 0.2507 0.0103 -0.0295 0.0848 115 ASN A CA ? ? ?
1091913 C CB . ASN A 115 0.2679 0.2639 0.3184 0.0115 -0.0287 0.0921 115 ASN A CB ? ? ?
1092914 C CG . ASN A 115 0.4787 0.4697 0.5295 0.0066 -0.0227 0.0951 115 ASN A CG ? ? ?
1093915 O OD1 . ASN A 115 0.5266 0.5225 0.5652 0.0038 -0.0192 0.0981 115 ASN A OD1 ? ? ?
1094916 N ND2 . ASN A 115 0.6682 0.6497 0.7337 0.0052 -0.0211 0.0936 115 ASN A ND2 ? ? ?
1095917 C C . ASN A 115 0.1700 0.1835 0.2085 0.0143 -0.0362 0.0843 115 ASN A C ? ? ?
1096918 O O . ASN A 115 0.1966 0.2140 0.2276 0.0160 -0.0405 0.0926 115 ASN A O ? ? ?
1097919 N N . ASP A 116 0.1534 0.1697 0.2005 0.0155 -0.0368 0.0748 116 ASP A N ? ? ?
1098920 C CA . ASP A 116 0.1564 0.1812 0.2081 0.0187 -0.0423 0.0732 116 ASP A CA ? ? ?
1099921 C CB . ASP A 116 0.1578 0.1806 0.2262 0.0220 -0.0409 0.0665 116 ASP A CB ? ? ?
1100922 C CG . ASP A 116 0.2055 0.2253 0.2733 0.0191 -0.0351 0.0557 116 ASP A CG ? ? ?
1101923 O OD1 . ASP A 116 0.3419 0.3619 0.3981 0.0147 -0.0324 0.0532 116 ASP A OD1 ? ? ?
1102924 O OD2 . ASP A 116 0.3382 0.3554 0.4166 0.0218 -0.0331 0.0500 116 ASP A OD2 ? ? ?
1103925 C C . ASP A 116 0.1447 0.1793 0.1856 0.0154 -0.0439 0.0673 116 ASP A C ? ? ?
1104926 O O . ASP A 116 0.1564 0.1998 0.2027 0.0168 -0.0487 0.0653 116 ASP A O ? ? ?
1105927 N N . GLY A 117 0.1449 0.1779 0.1721 0.0111 -0.0398 0.0643 117 GLY A N ? ? ?
1106928 C CA . GLY A 117 0.1400 0.1792 0.1553 0.0077 -0.0407 0.0585 117 GLY A CA ? ? ?
1107929 C C . GLY A 117 0.1344 0.1734 0.1528 0.0056 -0.0365 0.0481 117 GLY A C ? ? ?
1108930 O O . GLY A 117 0.1600 0.2027 0.1709 0.0026 -0.0371 0.0429 117 GLY A O ? ? ?
1109931 N N . GLU A 118 0.1207 0.1544 0.1490 0.0069 -0.0324 0.0453 118 GLU A N ? ? ?
1110932 C CA . GLU A 118 0.1063 0.1391 0.1361 0.0055 -0.0283 0.0368 118 GLU A CA ? ? ?
1111933 C CB . GLU A 118 0.1146 0.1457 0.1583 0.0087 -0.0272 0.0341 118 GLU A CB ? ? ?
1112934 C CG . GLU A 118 0.1241 0.1624 0.1788 0.0116 -0.0314 0.0357 118 GLU A CG ? ? ?
1113935 C CD . GLU A 118 0.1564 0.1929 0.2253 0.0159 -0.0294 0.0331 118 GLU A CD ? ? ?
1114936 O OE1 . GLU A 118 0.1523 0.1809 0.2209 0.0163 -0.0252 0.0292 118 GLU A OE1 ? ? ?
1115937 O OE2 . GLU A 118 0.1975 0.2410 0.2780 0.0192 -0.0323 0.0349 118 GLU A OE2 ? ? ?
1116938 C C . GLU A 118 0.1114 0.1389 0.1328 0.0034 -0.0233 0.0347 118 GLU A C ? ? ?
1117939 O O . GLU A 118 0.1272 0.1523 0.1436 0.0029 -0.0222 0.0396 118 GLU A O ? ? ?
1118940 N N . LEU A 119 0.1153 0.1417 0.1355 0.0024 -0.0199 0.0282 119 LEU A N ? ? ?
1119941 C CA . LEU A 119 0.1117 0.1343 0.1255 0.0013 -0.0157 0.0260 119 LEU A CA ? ? ?
1120942 C CB . LEU A 119 0.1382 0.1614 0.1422 -0.0008 -0.0139 0.0223 119 LEU A CB ? ? ?
1121943 C CG . LEU A 119 0.2061 0.2255 0.2040 -0.0009 -0.0092 0.0200 119 LEU A CG ? ? ?
1122944 C CD1 . LEU A 119 0.2632 0.2824 0.2572 -0.0006 -0.0074 0.0239 119 LEU A CD1 ? ? ?
1123945 C CD2 . LEU A 119 0.2706 0.2882 0.2609 -0.0027 -0.0074 0.0156 119 LEU A CD2 ? ? ?
1124946 C C . LEU A 119 0.1292 0.1489 0.1491 0.0026 -0.0138 0.0220 119 LEU A C ? ? ?
1125947 O O . LEU A 119 0.1236 0.1442 0.1464 0.0033 -0.0133 0.0182 119 LEU A O ? ? ?
1126948 N N . ILE A 120 0.0916 0.1083 0.1134 0.0027 -0.0128 0.0230 120 ILE A N ? ? ?
1127949 C CA . ILE A 120 0.0936 0.1077 0.1184 0.0036 -0.0120 0.0185 120 ILE A CA ? ? ?
1128950 C CB . ILE A 120 0.1076 0.1182 0.1412 0.0037 -0.0138 0.0194 120 ILE A CB ? ? ?
1129951 C CG1 . ILE A 120 0.1397 0.1486 0.1807 0.0054 -0.0158 0.0214 120 ILE A CG1 ? ? ?
1130952 C CG2 . ILE A 120 0.1207 0.1289 0.1547 0.0041 -0.0140 0.0134 120 ILE A CG2 ? ? ?
1131953 C CD1 . ILE A 120 0.1687 0.1715 0.2190 0.0051 -0.0174 0.0227 120 ILE A CD1 ? ? ?
1132954 C C . ILE A 120 0.0972 0.1115 0.1159 0.0031 -0.0096 0.0171 120 ILE A C ? ? ?
1133955 O O . ILE A 120 0.0959 0.1115 0.1142 0.0023 -0.0087 0.0203 120 ILE A O ? ? ?
1134956 N N . LEU A 121 0.0837 0.0970 0.0982 0.0041 -0.0082 0.0131 121 LEU A N ? ? ?
1135957 C CA . LEU A 121 0.0904 0.1034 0.1003 0.0049 -0.0068 0.0121 121 LEU A CA ? ? ?
1136958 C CB . LEU A 121 0.1102 0.1213 0.1126 0.0053 -0.0037 0.0106 121 LEU A CB ? ? ?
1137959 C CG . LEU A 121 0.1397 0.1488 0.1368 0.0074 -0.0023 0.0102 121 LEU A CG ? ? ?
1138960 C CD1 . LEU A 121 0.1542 0.1644 0.1513 0.0084 -0.0012 0.0127 121 LEU A CD1 ? ? ?
1139961 C CD2 . LEU A 121 0.1546 0.1598 0.1453 0.0073 0.0012 0.0091 121 LEU A CD2 ? ? ?
1140962 C C . LEU A 121 0.0963 0.1084 0.1084 0.0060 -0.0090 0.0092 121 LEU A C ? ? ?
1141963 O O . LEU A 121 0.1131 0.1233 0.1246 0.0067 -0.0092 0.0058 121 LEU A O ? ? ?
1142964 N N . THR A 122 0.0954 0.1096 0.1103 0.0059 -0.0108 0.0100 122 THR A N ? ? ?
1143965 C CA . THR A 122 0.1077 0.1219 0.1222 0.0068 -0.0140 0.0064 122 THR A CA ? ? ?
1144966 C CB . THR A 122 0.1420 0.1569 0.1663 0.0044 -0.0183 0.0051 122 THR A CB ? ? ?
1145967 O OG1 . THR A 122 0.1465 0.1671 0.1779 0.0032 -0.0192 0.0085 122 THR A OG1 ? ? ?
1146968 C CG2 . THR A 122 0.1251 0.1365 0.1559 0.0028 -0.0179 0.0059 122 THR A CG2 ? ? ?
1147969 C C . THR A 122 0.1179 0.1345 0.1274 0.0090 -0.0137 0.0077 122 THR A C ? ? ?
1148970 O O . THR A 122 0.1165 0.1357 0.1279 0.0095 -0.0116 0.0113 122 THR A O ? ? ?
1149971 N N . MET A 123 0.1121 0.1274 0.1143 0.0109 -0.0155 0.0049 123 MET A N ? ? ?
1150972 C CA . MET A 123 0.1148 0.1322 0.1121 0.0139 -0.0167 0.0068 123 MET A CA ? ? ?
1151973 C CB . MET A 123 0.1315 0.1435 0.1171 0.0162 -0.0121 0.0080 123 MET A CB ? ? ?
1152974 C CG . MET A 123 0.1556 0.1647 0.1420 0.0153 -0.0065 0.0104 123 MET A CG ? ? ?
1153975 S SD . MET A 123 0.2280 0.2298 0.2035 0.0165 -0.0008 0.0118 123 MET A SD ? ? ?
1154976 C CE . MET A 123 0.2411 0.2420 0.2148 0.0143 0.0006 0.0080 123 MET A CE ? ? ?
1155977 C C . MET A 123 0.1376 0.1577 0.1342 0.0140 -0.0233 0.0031 123 MET A C ? ? ?
1156978 O O . MET A 123 0.1238 0.1402 0.1148 0.0134 -0.0243 -0.0017 123 MET A O ? ? ?
1157979 N N . THR A 124 0.1141 0.1410 0.1164 0.0150 -0.0278 0.0051 124 THR A N ? ? ?
1158980 C CA . THR A 124 0.1265 0.1577 0.1295 0.0143 -0.0359 0.0012 124 THR A CA ? ? ?
1159981 C CB . THR A 124 0.1502 0.1881 0.1709 0.0101 -0.0399 0.0008 124 THR A CB ? ? ?
1160982 O OG1 . THR A 124 0.1450 0.1775 0.1713 0.0063 -0.0365 -0.0007 124 THR A OG1 ? ? ?
1161983 C CG2 . THR A 124 0.1882 0.2309 0.2114 0.0082 -0.0492 -0.0041 124 THR A CG2 ? ? ?
1162984 C C . THR A 124 0.1372 0.1725 0.1330 0.0189 -0.0395 0.0042 124 THR A C ? ? ?
1163985 O O . THR A 124 0.1325 0.1703 0.1313 0.0222 -0.0367 0.0100 124 THR A O ? ? ?
1164986 N N . ALA A 125 0.1431 0.1785 0.1285 0.0196 -0.0457 0.0000 125 ALA A N ? ? ?
1165987 C CA . ALA A 125 0.1565 0.1975 0.1353 0.0238 -0.0520 0.0028 125 ALA A CA ? ? ?
1166988 C CB . ALA A 125 0.1812 0.2148 0.1398 0.0284 -0.0479 0.0056 125 ALA A CB ? ? ?
1167989 C C . ALA A 125 0.1608 0.2071 0.1400 0.0209 -0.0626 -0.0042 125 ALA A C ? ? ?
1168990 O O . ALA A 125 0.1661 0.2058 0.1336 0.0190 -0.0633 -0.0113 125 ALA A O ? ? ?
1169991 N N . ASP A 126 0.1760 0.2341 0.1696 0.0203 -0.0704 -0.0026 126 ASP A N ? ? ?
1170992 C CA . ASP A 126 0.2182 0.2830 0.2180 0.0156 -0.0814 -0.0097 126 ASP A CA ? ? ?
1171993 C CB . ASP A 126 0.2463 0.3127 0.2265 0.0189 -0.0903 -0.0124 126 ASP A CB ? ? ?
1172994 C CG . ASP A 126 0.3086 0.3865 0.2914 0.0250 -0.0960 -0.0039 126 ASP A CG ? ? ?
1173995 O OD1 . ASP A 126 0.2771 0.3652 0.2821 0.0251 -0.0960 0.0013 126 ASP A OD1 ? ? ?
1174996 O OD2 . ASP A 126 0.3305 0.4071 0.2932 0.0301 -0.0996 -0.0018 126 ASP A OD2 ? ? ?
1175997 C C . ASP A 126 0.2257 0.2823 0.2302 0.0091 -0.0789 -0.0175 126 ASP A C ? ? ?
1176998 O O . ASP A 126 0.2332 0.2894 0.2533 0.0061 -0.0734 -0.0150 126 ASP A O ? ? ?
1177999 N N . ASP A 127 0.2470 0.2964 0.2372 0.0074 -0.0825 -0.0266 127 ASP A N ? ? ?
11781000 C CA . ASP A 127 0.3002 0.3406 0.2957 0.0020 -0.0806 -0.0344 127 ASP A CA ? ? ?
11791001 C CB . ASP A 127 0.3613 0.3992 0.3474 -0.0010 -0.0902 -0.0461 127 ASP A CB ? ? ?
11801002 C CG . ASP A 127 0.5593 0.6089 0.5609 -0.0061 -0.1027 -0.0487 127 ASP A CG ? ? ?
11811003 O OD1 . ASP A 127 0.5969 0.6563 0.6205 -0.0081 -0.1024 -0.0415 127 ASP A OD1 ? ? ?
11821004 O OD2 . ASP A 127 0.7768 0.8264 0.7689 -0.0084 -0.1126 -0.0582 127 ASP A OD2 ? ? ?
11831005 C C . ASP A 127 0.2670 0.2953 0.2538 0.0040 -0.0693 -0.0344 127 ASP A C ? ? ?
11841006 O O . ASP A 127 0.3163 0.3375 0.3111 0.0006 -0.0664 -0.0385 127 ASP A O ? ? ?
11851007 N N . VAL A 128 0.2067 0.2332 0.1789 0.0096 -0.0631 -0.0292 128 VAL A N ? ? ?
11861008 C CA . VAL A 128 0.1806 0.1978 0.1438 0.0116 -0.0533 -0.0297 128 VAL A CA ? ? ?
11871009 C CB . VAL A 128 0.1991 0.2144 0.1404 0.0167 -0.0505 -0.0279 128 VAL A CB ? ? ?
11881010 C CG1 . VAL A 128 0.2361 0.2442 0.1715 0.0184 -0.0393 -0.0267 128 VAL A CG1 ? ? ?
11891011 C CG2 . VAL A 128 0.2419 0.2564 0.1670 0.0171 -0.0578 -0.0361 128 VAL A CG2 ? ? ?
11901012 C C . VAL A 128 0.1657 0.1826 0.1415 0.0112 -0.0457 -0.0226 128 VAL A C ? ? ?
11911013 O O . VAL A 128 0.1429 0.1653 0.1237 0.0127 -0.0447 -0.0151 128 VAL A O ? ? ?
11921014 N N . VAL A 129 0.1407 0.1512 0.1212 0.0097 -0.0406 -0.0252 129 VAL A N ? ? ?
11931015 C CA . VAL A 129 0.1356 0.1456 0.1267 0.0090 -0.0345 -0.0193 129 VAL A CA ? ? ?
11941016 C CB . VAL A 129 0.1524 0.1610 0.1596 0.0047 -0.0366 -0.0207 129 VAL A CB ? ? ?
11951017 C CG1 . VAL A 129 0.1869 0.1958 0.2028 0.0043 -0.0311 -0.0138 129 VAL A CG1 ? ? ?
11961018 C CG2 . VAL A 129 0.1715 0.1862 0.1882 0.0013 -0.0444 -0.0215 129 VAL A CG2 ? ? ?
11971019 C C . VAL A 129 0.1305 0.1353 0.1147 0.0113 -0.0267 -0.0192 129 VAL A C ? ? ?
11981020 O O . VAL A 129 0.1589 0.1586 0.1397 0.0119 -0.0251 -0.0251 129 VAL A O ? ? ?
11991021 N N . CYS A 130 0.1319 0.1384 0.1157 0.0124 -0.0217 -0.0127 130 CYS A N ? ? ?
12001022 C CA . CYS A 130 0.1185 0.1223 0.0999 0.0134 -0.0148 -0.0117 130 CYS A CA ? ? ?
12011023 C CB . CYS A 130 0.1404 0.1444 0.1119 0.0153 -0.0108 -0.0072 130 CYS A CB ? ? ?
12021024 S SG . CYS A 130 0.1536 0.1562 0.1267 0.0147 -0.0027 -0.0047 130 CYS A SG ? ? ?
12031025 C C . CYS A 130 0.1208 0.1254 0.1148 0.0113 -0.0134 -0.0085 130 CYS A C ? ? ?
12041026 O O . CYS A 130 0.1184 0.1259 0.1176 0.0101 -0.0145 -0.0041 130 CYS A O ? ? ?
12051027 N N . THR A 131 0.1140 0.1165 0.1125 0.0115 -0.0109 -0.0106 131 THR A N ? ? ?
12061028 C CA . THR A 131 0.0993 0.1026 0.1085 0.0102 -0.0105 -0.0072 131 THR A CA ? ? ?
12071029 C CB . THR A 131 0.1177 0.1171 0.1359 0.0101 -0.0127 -0.0103 131 THR A CB ? ? ?
12081030 O OG1 . THR A 131 0.1291 0.1266 0.1484 0.0084 -0.0173 -0.0130 131 THR A OG1 ? ? ?
12091031 C CG2 . THR A 131 0.1198 0.1199 0.1481 0.0092 -0.0131 -0.0050 131 THR A CG2 ? ? ?
12101032 C C . THR A 131 0.1083 0.1136 0.1172 0.0109 -0.0058 -0.0055 131 THR A C ? ? ?
12111033 O O . THR A 131 0.1110 0.1157 0.1178 0.0127 -0.0024 -0.0088 131 THR A O ? ? ?
12121034 N N . ARG A 132 0.0975 0.1055 0.1086 0.0092 -0.0055 -0.0007 132 ARG A N ? ? ?
12131035 C CA . ARG A 132 0.1319 0.1426 0.1442 0.0086 -0.0025 0.0006 132 ARG A CA ? ? ?
12141036 C CB . ARG A 132 0.1839 0.1942 0.1883 0.0073 0.0003 0.0022 132 ARG A CB ? ? ?
12151037 C CG . ARG A 132 0.3301 0.3371 0.3251 0.0089 0.0014 0.0013 132 ARG A CG ? ? ?
12161038 C CD . ARG A 132 0.3562 0.3619 0.3453 0.0094 0.0065 0.0005 132 ARG A CD ? ? ?
12171039 N NE . ARG A 132 0.2516 0.2560 0.2391 0.0071 0.0096 0.0033 132 ARG A NE ? ? ?
12181040 C CZ . ARG A 132 0.2159 0.2195 0.2014 0.0061 0.0150 0.0037 132 ARG A CZ ? ? ?
12191041 N NH1 . ARG A 132 0.2472 0.2514 0.2297 0.0078 0.0185 0.0020 132 ARG A NH1 ? ? ?
12201042 N NH2 . ARG A 132 0.1987 0.2002 0.1849 0.0029 0.0174 0.0055 132 ARG A NH2 ? ? ?
12211043 C C . ARG A 132 0.1141 0.1276 0.1340 0.0074 -0.0052 0.0042 132 ARG A C ? ? ?
12221044 O O . ARG A 132 0.1323 0.1453 0.1515 0.0062 -0.0074 0.0072 132 ARG A O ? ? ?
12231045 N N . VAL A 133 0.0825 0.0996 0.1094 0.0079 -0.0049 0.0043 133 VAL A N ? ? ?
12241046 C CA . VAL A 133 0.0982 0.1184 0.1317 0.0075 -0.0085 0.0083 133 VAL A CA ? ? ?
12251047 C CB . VAL A 133 0.1043 0.1240 0.1485 0.0107 -0.0101 0.0084 133 VAL A CB ? ? ?
12261048 C CG1 . VAL A 133 0.1218 0.1445 0.1717 0.0109 -0.0145 0.0144 133 VAL A CG1 ? ? ?
12271049 C CG2 . VAL A 133 0.1245 0.1369 0.1682 0.0118 -0.0102 0.0059 133 VAL A CG2 ? ? ?
12281050 C C . VAL A 133 0.0819 0.1081 0.1163 0.0054 -0.0085 0.0091 133 VAL A C ? ? ?
12291051 O O . VAL A 133 0.0814 0.1108 0.1195 0.0054 -0.0055 0.0065 133 VAL A O ? ? ?
12301052 N N . TYR A 134 0.0751 0.1032 0.1064 0.0033 -0.0118 0.0124 134 TYR A N ? ? ?
12311053 C CA . TYR A 134 0.0808 0.1141 0.1117 0.0002 -0.0132 0.0122 134 TYR A CA ? ? ?
12321054 C CB . TYR A 134 0.1013 0.1306 0.1205 -0.0030 -0.0115 0.0107 134 TYR A CB ? ? ?
12331055 C CG . TYR A 134 0.1263 0.1494 0.1401 -0.0026 -0.0062 0.0083 134 TYR A CG ? ? ?
12341056 C CD1 . TYR A 134 0.1489 0.1679 0.1597 -0.0001 -0.0053 0.0091 134 TYR A CD1 ? ? ?
12351057 C CD2 . TYR A 134 0.1702 0.1918 0.1826 -0.0049 -0.0026 0.0057 134 TYR A CD2 ? ? ?
12361058 C CE1 . TYR A 134 0.1826 0.1971 0.1882 0.0009 -0.0019 0.0076 134 TYR A CE1 ? ? ?
12371059 C CE2 . TYR A 134 0.1764 0.1918 0.1826 -0.0037 0.0020 0.0050 134 TYR A CE2 ? ? ?
12381060 C CZ . TYR A 134 0.1969 0.2092 0.1994 -0.0005 0.0018 0.0060 134 TYR A CZ ? ? ?
12391061 O OH . TYR A 134 0.2856 0.2932 0.2819 0.0014 0.0046 0.0059 134 TYR A OH ? ? ?
12401062 C C . TYR A 134 0.0869 0.1257 0.1213 0.0004 -0.0193 0.0164 134 TYR A C ? ? ?
12411063 O O . TYR A 134 0.0739 0.1103 0.1069 0.0023 -0.0214 0.0206 134 TYR A O ? ? ?
12421064 N N . VAL A 135 0.0973 0.1436 0.1358 -0.0020 -0.0223 0.0156 135 VAL A N ? ? ?
12431065 C CA . VAL A 135 0.1066 0.1596 0.1461 -0.0023 -0.0295 0.0195 135 VAL A CA ? ? ?
12441066 C CB . VAL A 135 0.1279 0.1896 0.1844 0.0013 -0.0330 0.0221 135 VAL A CB ? ? ?
12451067 C CG1 . VAL A 135 0.1372 0.2074 0.2055 -0.0009 -0.0315 0.0179 135 VAL A CG1 ? ? ?
12461068 C CG2 . VAL A 135 0.1670 0.2347 0.2236 0.0026 -0.0414 0.0284 135 VAL A CG2 ? ? ?
12471069 C C . VAL A 135 0.1092 0.1650 0.1420 -0.0080 -0.0315 0.0158 135 VAL A C ? ? ?
12481070 O O . VAL A 135 0.0976 0.1523 0.1321 -0.0111 -0.0275 0.0110 135 VAL A O ? ? ?
12491071 N N . ARG A 136 0.1199 0.1782 0.1440 -0.0095 -0.0375 0.0178 136 ARG A N ? ? ?
12501072 C CA . ARG A 136 0.1330 0.1931 0.1498 -0.0153 -0.0402 0.0129 136 ARG A CA ? ? ?
12511073 C CB . ARG A 136 0.1615 0.2223 0.1634 -0.0162 -0.0462 0.0149 136 ARG A CB ? ? ?
12521074 C CG . ARG A 136 0.1841 0.2346 0.1697 -0.0145 -0.0407 0.0162 136 ARG A CG ? ? ?
12531075 C CD . ARG A 136 0.2248 0.2762 0.1930 -0.0158 -0.0455 0.0175 136 ARG A CD ? ? ?
12541076 N NE . ARG A 136 0.2646 0.3081 0.2190 -0.0137 -0.0393 0.0199 136 ARG A NE ? ? ?
12551077 C CZ . ARG A 136 0.3412 0.3841 0.2963 -0.0097 -0.0377 0.0280 136 ARG A CZ ? ? ?
12561078 N NH1 . ARG A 136 0.3776 0.4250 0.3458 -0.0068 -0.0415 0.0344 136 ARG A NH1 ? ? ?
12571079 N NH2 . ARG A 136 0.3275 0.3648 0.2708 -0.0087 -0.0315 0.0298 136 ARG A NH2 ? ? ?
12581080 C C . ARG A 136 0.1357 0.2069 0.1684 -0.0182 -0.0441 0.0105 136 ARG A C ? ? ?
12591081 O O . ARG A 136 0.1225 0.2034 0.1691 -0.0149 -0.0483 0.0146 136 ARG A O ? ? ?
12601082 N N . GLU A 137 0.1669 0.2364 0.1985 -0.0244 -0.0424 0.0041 137 GLU A N ? ? ?
12611083 C CA . GLU A 137 0.2095 0.2899 0.2577 -0.0289 -0.0450 0.0013 137 GLU A CA ? ? ?
12621084 C CB . GLU A 137 0.2463 0.3198 0.2900 -0.0365 -0.0415 -0.0058 137 GLU A CB ? ? ?
12631085 C CG . GLU A 137 0.3899 0.4533 0.4344 -0.0359 -0.0304 -0.0067 137 GLU A CG ? ? ?
12641086 C CD . GLU A 137 0.5323 0.5873 0.5734 -0.0432 -0.0267 -0.0125 137 GLU A CD ? ? ?
12651087 O OE1 . GLU A 137 0.5140 0.5698 0.5511 -0.0493 -0.0328 -0.0173 137 GLU A OE1 ? ? ?
12661088 O OE2 . GLU A 137 0.7558 0.8027 0.7978 -0.0430 -0.0178 -0.0123 137 GLU A OE2 ? ? ?
12671089 C C . GLU A 137 0.2415 0.3356 0.2953 -0.0302 -0.0565 0.0029 137 GLU A C ? ? ?
12681090 O O . GLU A 137 0.2148 0.3073 0.2530 -0.0320 -0.0627 0.0022 137 GLU A O ? ? ?
12691091 O OXT . GLU A 137 0.2738 0.3816 0.3477 -0.0295 -0.0598 0.0047 137 GLU A OXT ? ? ?
1270#
1271loop_
1272_atom_site.id
1273_atom_site.group_PDB
1274_atom_site.type_symbol
1275_atom_site.label_atom_id
1276_atom_site.label_alt_id
1277_atom_site.label_comp_id
1278_atom_site.label_asym_id
1279_atom_site.label_entity_id
1280_atom_site.label_seq_id
1281_atom_site.pdbx_PDB_ins_code
1282_atom_site.Cartn_x
1283_atom_site.Cartn_y
1284_atom_site.Cartn_z
1285_atom_site.occupancy
1286_atom_site.B_iso_or_equiv
1287_atom_site.pdbx_formal_charge
1288_atom_site.auth_seq_id
1289_atom_site.auth_comp_id
1290_atom_site.auth_asym_id
1291_atom_site.auth_atom_id
1292_atom_site.pdbx_PDB_model_num
12931 ATOM N N . PRO A 1 1 ? 16.949 13.324 44.533 1.00 35.75 ? 1 PRO A N 1
12942 ATOM C CA . PRO A 1 1 ? 18.076 13.580 43.637 1.00 38.80 ? 1 PRO A CA 1
12953 ATOM C CB . PRO A 1 1 ? 17.444 13.475 42.247 1.00 36.08 ? 1 PRO A CB 1
12964 ATOM C CG . PRO A 1 1 ? 16.055 13.934 42.454 1.00 34.90 ? 1 PRO A CG 1
12975 ATOM C CD . PRO A 1 1 ? 15.667 13.391 43.808 1.00 35.61 ? 1 PRO A CD 1
12986 ATOM C C . PRO A 1 1 ? 18.675 14.968 43.840 1.00 34.39 ? 1 PRO A C 1
12997 ATOM O O . PRO A 1 1 ? 17.946 15.925 44.096 1.00 32.68 ? 1 PRO A O 1
13008 ATOM N N . ASN A 1 2 ? 20.001 15.069 43.697 1.00 26.37 ? 2 ASN A N 1
13019 ATOM C CA . ASN A 1 2 ? 20.664 16.362 43.687 1.00 24.21 ? 2 ASN A CA 1
130210 ATOM C CB . ASN A 1 2 ? 21.716 16.470 44.767 1.00 30.29 ? 2 ASN A CB 1
130311 ATOM C CG . ASN A 1 2 ? 22.292 17.867 44.814 1.00 36.72 ? 2 ASN A CG 1
130412 ATOM O OD1 . ASN A 1 2 ? 21.684 18.838 44.316 1.00 25.36 ? 2 ASN A OD1 1
130513 ATOM N ND2 . ASN A 1 2 ? 23.463 17.998 45.420 1.00 49.47 ? 2 ASN A ND2 1
130614 ATOM C C . ASN A 1 2 ? 21.301 16.638 42.327 1.00 17.88 ? 2 ASN A C 1
130715 ATOM O O . ASN A 1 2 ? 22.365 16.114 42.002 1.00 18.92 ? 2 ASN A O 1
130816 ATOM N N . PHE A 1 3 ? 20.629 17.475 41.535 1.00 14.34 ? 3 PHE A N 1
130917 ATOM C CA . PHE A 1 3 ? 21.121 17.837 40.217 1.00 13.02 ? 3 PHE A CA 1
131018 ATOM C CB . PHE A 1 3 ? 19.962 18.241 39.296 1.00 12.67 ? 3 PHE A CB 1
131119 ATOM C CG . PHE A 1 3 ? 19.068 17.122 38.801 1.00 13.04 ? 3 PHE A CG 1
131220 ATOM C CD1 . PHE A 1 3 ? 18.095 16.572 39.619 1.00 14.41 ? 3 PHE A CD1 1
131321 ATOM C CD2 . PHE A 1 3 ? 19.191 16.634 37.510 1.00 15.43 ? 3 PHE A CD2 1
131422 ATOM C CE1 . PHE A 1 3 ? 17.257 15.562 39.155 1.00 13.58 ? 3 PHE A CE1 1
131523 ATOM C CE2 . PHE A 1 3 ? 18.345 15.616 37.049 1.00 15.68 ? 3 PHE A CE2 1
131624 ATOM C CZ . PHE A 1 3 ? 17.388 15.092 37.876 1.00 13.88 ? 3 PHE A CZ 1
131725 ATOM C C . PHE A 1 3 ? 22.128 18.985 40.230 1.00 12.70 ? 3 PHE A C 1
131826 ATOM O O . PHE A 1 3 ? 22.676 19.322 39.181 1.00 12.67 ? 3 PHE A O 1
131927 ATOM N N . SER A 1 4 ? 22.345 19.594 41.399 1.00 12.75 ? 4 SER A N 1
132028 ATOM C CA . SER A 1 4 ? 23.170 20.785 41.508 1.00 14.57 ? 4 SER A CA 1
132129 ATOM C CB . SER A 1 4 ? 23.163 21.332 42.938 1.00 17.93 ? 4 SER A CB 1
132230 ATOM O OG . SER A 1 4 ? 21.869 21.814 43.297 1.00 20.21 ? 4 SER A OG 1
132331 ATOM C C . SER A 1 4 ? 24.609 20.532 41.065 1.00 15.68 ? 4 SER A C 1
132432 ATOM O O . SER A 1 4 ? 25.198 19.499 41.384 1.00 13.59 ? 4 SER A O 1
132533 ATOM N N . GLY A 1 5 ? 25.169 21.498 40.332 1.00 15.21 ? 5 GLY A N 1
132634 ATOM C CA . GLY A 1 5 ? 26.594 21.489 40.045 1.00 18.46 ? 5 GLY A CA 1
132735 ATOM C C . GLY A 1 5 ? 26.954 22.235 38.766 1.00 15.32 ? 5 GLY A C 1
132836 ATOM O O . GLY A 1 5 ? 26.083 22.804 38.108 1.00 12.64 ? 5 GLY A O 1
132937 ATOM N N . ASN A 1 6 ? 28.256 22.223 38.464 1.00 13.01 ? 6 ASN A N 1
133038 ATOM C CA . ASN A 1 6 ? 28.804 22.692 37.204 1.00 13.01 ? 6 ASN A CA 1
133139 ATOM C CB . ASN A 1 6 ? 30.050 23.548 37.437 1.00 16.10 ? 6 ASN A CB 1
133240 ATOM C CG . ASN A 1 6 ? 29.709 24.812 38.181 1.00 26.16 ? 6 ASN A CG 1
133341 ATOM O OD1 . ASN A 1 6 ? 28.942 25.639 37.698 1.00 23.90 ? 6 ASN A OD1 1
133442 ATOM N ND2 . ASN A 1 6 ? 30.242 24.981 39.377 1.00 32.20 ? 6 ASN A ND2 1
133543 ATOM C C . ASN A 1 6 ? 29.126 21.456 36.370 1.00 11.84 ? 6 ASN A C 1
133644 ATOM O O . ASN A 1 6 ? 29.959 20.638 36.766 1.00 14.51 ? 6 ASN A O 1
133745 ATOM N N . TRP A 1 7 ? 28.437 21.321 35.238 1.00 10.51 ? 7 TRP A N 1
133846 ATOM C CA . TRP A 1 7 ? 28.491 20.122 34.421 1.00 10.61 ? 7 TRP A CA 1
133947 ATOM C CB . TRP A 1 7 ? 27.056 19.634 34.169 1.00 11.06 ? 7 TRP A CB 1
134048 ATOM C CG . TRP A 1 7 ? 26.271 19.267 35.396 1.00 11.22 ? 7 TRP A CG 1
134149 ATOM C CD1 . TRP A 1 7 ? 25.520 20.091 36.184 1.00 12.03 ? 7 TRP A CD1 1
134250 ATOM N NE1 . TRP A 1 7 ? 24.934 19.370 37.199 1.00 13.80 ? 7 TRP A NE1 1
134351 ATOM C CE2 . TRP A 1 7 ? 25.287 18.050 37.068 1.00 11.73 ? 7 TRP A CE2 1
134452 ATOM C CZ2 . TRP A 1 7 ? 24.948 16.934 37.850 1.00 11.51 ? 7 TRP A CZ2 1
134553 ATOM C CH2 . TRP A 1 7 ? 25.470 15.723 37.482 1.00 10.83 ? 7 TRP A CH2 1
134654 ATOM C CZ3 . TRP A 1 7 ? 26.323 15.597 36.375 1.00 10.68 ? 7 TRP A CZ3 1
134755 ATOM C CE3 . TRP A 1 7 ? 26.654 16.693 35.598 1.00 11.17 ? 7 TRP A CE3 1
134856 ATOM C CD2 . TRP A 1 7 ? 26.128 17.951 35.943 1.00 10.82 ? 7 TRP A CD2 1
134957 ATOM C C . TRP A 1 7 ? 29.243 20.341 33.102 1.00 12.95 ? 7 TRP A C 1
135058 ATOM O O . TRP A 1 7 ? 29.105 21.387 32.458 1.00 12.32 ? 7 TRP A O 1
135159 ATOM N N . LYS A 1 8 ? 30.055 19.347 32.713 1.00 11.40 ? 8 LYS A N 1
135260 ATOM C CA . LYS A 1 8 ? 30.776 19.394 31.449 1.00 14.38 ? 8 LYS A CA 1
135361 ATOM C CB . LYS A 1 8 ? 32.287 19.436 31.665 1.00 21.70 ? 8 LYS A CB 1
135462 ATOM C CG . LYS A 1 8 ? 32.868 18.191 32.279 1.00 26.85 ? 8 LYS A CG 1
135563 ATOM C CD . LYS A 1 8 ? 34.377 18.324 32.631 1.00 40.14 ? 8 LYS A CD 1
135664 ATOM C CE . LYS A 1 8 ? 35.282 18.700 31.473 1.00 46.47 ? 8 LYS A CE 1
135765 ATOM N NZ . LYS A 1 8 ? 35.275 17.673 30.403 1.00 52.86 ? 8 LYS A NZ 1
135866 ATOM C C . LYS A 1 8 ? 30.378 18.190 30.601 1.00 12.98 ? 8 LYS A C 1
135967 ATOM O O . LYS A 1 8 ? 30.120 17.100 31.127 1.00 12.49 ? 8 LYS A O 1
136068 ATOM N N . ILE A 1 9 ? 30.294 18.400 29.284 1.00 10.33 ? 9 ILE A N 1
136169 ATOM C CA . ILE A 1 9 ? 29.797 17.358 28.397 1.00 9.39 ? 9 ILE A CA 1
136270 ATOM C CB . ILE A 1 9 ? 29.283 17.975 27.081 1.00 10.48 ? 9 ILE A CB 1
136371 ATOM C CG1 . ILE A 1 9 ? 28.336 17.024 26.339 1.00 13.01 ? 9 ILE A CG1 1
136472 ATOM C CG2 . ILE A 1 9 ? 30.425 18.418 26.171 1.00 13.86 ? 9 ILE A CG2 1
136573 ATOM C CD1 . ILE A 1 9 ? 27.516 17.751 25.305 1.00 14.88 ? 9 ILE A CD1 1
136674 ATOM C C . ILE A 1 9 ? 30.858 16.290 28.138 1.00 10.02 ? 9 ILE A C 1
136775 ATOM O O . ILE A 1 9 ? 32.046 16.611 28.014 1.00 10.90 ? 9 ILE A O 1
136876 ATOM N N . ILE A 1 10 ? 30.418 15.023 28.051 1.00 9.64 ? 10 ILE A N 1
136977 ATOM C CA . ILE A 1 10 ? 31.298 13.929 27.669 1.00 11.64 ? 10 ILE A CA 1
137078 ATOM C CB . ILE A 1 10 ? 31.570 12.983 28.869 1.00 15.26 ? 10 ILE A CB 1
137179 ATOM C CG1 . ILE A 1 10 ? 30.296 12.350 29.433 1.00 16.89 ? 10 ILE A CG1 1
137280 ATOM C CG2 . ILE A 1 10 ? 32.326 13.700 29.966 1.00 17.53 ? 10 ILE A CG2 1
137381 ATOM C CD1 . ILE A 1 10 ? 30.607 11.170 30.423 1.00 19.17 ? 10 ILE A CD1 1
137482 ATOM C C . ILE A 1 10 ? 30.816 13.145 26.446 1.00 12.11 ? 10 ILE A C 1
137583 ATOM O O . ILE A 1 10 ? 31.596 12.394 25.860 1.00 12.72 ? 10 ILE A O 1
137684 ATOM N N . ARG A 1 11 ? 29.554 13.333 26.053 1.00 10.49 ? 11 ARG A N 1
137785 ATOM C CA . ARG A 1 11 ? 28.994 12.702 24.861 1.00 11.09 ? 11 ARG A CA 1
137886 ATOM C CB . ARG A 1 11 ? 28.457 11.292 25.183 1.00 13.41 ? 11 ARG A CB 1
137987 ATOM C CG . ARG A 1 11 ? 27.777 10.596 24.016 1.00 16.27 ? 11 ARG A CG 1
138088 ATOM C CD . ARG A 1 11 ? 27.188 9.254 24.441 1.00 16.74 ? 11 ARG A CD 1
138189 ATOM N NE . ARG A 1 11 ? 28.208 8.293 24.831 1.00 18.78 ? 11 ARG A NE 1
138290 ATOM C CZ . ARG A 1 11 ? 28.818 7.456 23.997 1.00 23.85 ? 11 ARG A CZ 1
138391 ATOM N NH1 . ARG A 1 11 ? 28.669 7.549 22.684 1.00 22.18 ? 11 ARG A NH1 1
138492 ATOM N NH2 . ARG A 1 11 ? 29.582 6.488 24.494 1.00 23.41 ? 11 ARG A NH2 1
138593 ATOM C C . ARG A 1 11 ? 27.856 13.542 24.294 1.00 10.30 ? 11 ARG A C 1
138694 ATOM O O . ARG A 1 11 ? 27.044 14.067 25.054 1.00 9.66 ? 11 ARG A O 1
138795 ATOM N N . SER A 1 12 ? 27.829 13.682 22.959 1.00 10.71 ? 12 SER A N 1
138896 ATOM C CA . SER A 1 12 ? 26.688 14.256 22.259 1.00 10.46 ? 12 SER A CA 1
138997 ATOM C CB . SER A 1 12 ? 26.976 15.694 21.834 1.00 11.20 ? 12 SER A CB 1
139098 ATOM O OG . SER A 1 12 ? 25.836 16.284 21.220 1.00 10.80 ? 12 SER A OG 1
139199 ATOM C C . SER A 1 12 ? 26.344 13.420 21.028 1.00 11.24 ? 12 SER A C 1
1392100 ATOM O O . SER A 1 12 ? 27.226 13.123 20.231 1.00 12.90 ? 12 SER A O 1
1393101 ATOM N N . GLU A 1 13 ? 25.067 13.037 20.883 1.00 9.30 ? 13 GLU A N 1
1394102 ATOM C CA . GLU A 1 13 ? 24.604 12.279 19.727 1.00 11.59 ? 13 GLU A CA 1
1395103 ATOM C CB . GLU A 1 13 ? 24.176 10.857 20.122 1.00 12.04 ? 13 GLU A CB 1
1396104 ATOM C CG . GLU A 1 13 ? 25.236 10.017 20.782 1.00 15.51 ? 13 GLU A CG 1
1397105 ATOM C CD . GLU A 1 13 ? 26.226 9.336 19.866 1.00 20.15 ? 13 GLU A CD 1
1398106 ATOM O OE1 . GLU A 1 13 ? 26.007 9.313 18.632 1.00 21.36 ? 13 GLU A OE1 1
1399107 ATOM O OE2 . GLU A 1 13 ? 27.235 8.820 20.400 1.00 24.90 ? 13 GLU A OE2 1
1400108 ATOM C C . GLU A 1 13 ? 23.383 12.957 19.109 1.00 10.58 ? 13 GLU A C 1
1401109 ATOM O O . GLU A 1 13 ? 22.455 13.316 19.829 1.00 8.99 ? 13 GLU A O 1
1402110 ATOM N N . ASN A 1 14 ? 23.399 13.094 17.776 1.00 11.14 ? 14 ASN A N 1
1403111 ATOM C CA . ASN A 1 14 ? 22.223 13.448 16.994 1.00 11.92 ? 14 ASN A CA 1
1404112 ATOM C CB . ASN A 1 14 ? 21.044 12.500 17.358 1.00 11.06 ? 14 ASN A CB 1
1405113 ATOM C CG . ASN A 1 14 ? 20.381 11.852 16.142 1.00 13.13 ? 14 ASN A CG 1
1406114 ATOM O OD1 . ASN A 1 14 ? 20.989 11.695 15.057 1.00 13.59 ? 14 ASN A OD1 1
1407115 ATOM N ND2 . ASN A 1 14 ? 19.125 11.441 16.293 1.00 12.41 ? 14 ASN A ND2 1
1408116 ATOM C C . ASN A 1 14 ? 21.785 14.909 17.129 1.00 11.17 ? 14 ASN A C 1
1409117 ATOM O O . ASN A 1 14 ? 20.649 15.244 16.808 1.00 10.70 ? 14 ASN A O 1
1410118 ATOM N N . PHE A 1 15 ? 22.691 15.794 17.563 1.00 10.45 ? 15 PHE A N 1
1411119 ATOM C CA . PHE A 1 15 ? 22.320 17.192 17.727 1.00 10.58 ? 15 PHE A CA 1
1412120 ATOM C CB . PHE A 1 15 ? 23.418 17.964 18.468 1.00 11.54 ? 15 PHE A CB 1
1413121 ATOM C CG . PHE A 1 15 ? 23.065 19.392 18.793 1.00 11.86 ? 15 PHE A CG 1
1414122 ATOM C CD1 . PHE A 1 15 ? 22.018 19.688 19.648 1.00 17.16 ? 15 PHE A CD1 1
1415123 ATOM C CD2 . PHE A 1 15 ? 23.776 20.443 18.239 1.00 13.97 ? 15 PHE A CD2 1
1416124 ATOM C CE1 . PHE A 1 15 ? 21.696 21.009 19.946 1.00 18.04 ? 15 PHE A CE1 1
1417125 ATOM C CE2 . PHE A 1 15 ? 23.456 21.756 18.545 1.00 15.20 ? 15 PHE A CE2 1
1418126 ATOM C CZ . PHE A 1 15 ? 22.418 22.032 19.391 1.00 16.19 ? 15 PHE A CZ 1
1419127 ATOM C C . PHE A 1 15 ? 22.015 17.855 16.382 1.00 11.62 ? 15 PHE A C 1
1420128 ATOM O O . PHE A 1 15 ? 21.022 18.563 16.244 1.00 12.03 ? 15 PHE A O 1
1421129 ATOM N N . GLU A 1 16 ? 22.859 17.628 15.374 1.00 12.94 ? 16 GLU A N 1
1422130 ATOM C CA . GLU A 1 16 ? 22.608 18.227 14.072 1.00 15.47 ? 16 GLU A CA 1
1423131 ATOM C CB . GLU A 1 16 ? 23.747 17.967 13.081 1.00 19.63 ? 16 GLU A CB 1
1424132 ATOM C CG . GLU A 1 16 ? 23.419 18.579 11.730 1.00 23.32 ? 16 GLU A CG 1
1425133 ATOM C CD . GLU A 1 16 ? 24.569 18.926 10.814 1.00 27.25 ? 16 GLU A CD 1
1426134 ATOM O OE1 . GLU A 1 16 ? 25.713 18.501 11.086 1.00 29.13 ? 16 GLU A OE1 1
1427135 ATOM O OE2 . GLU A 1 16 ? 24.317 19.639 9.817 1.00 30.41 ? 16 GLU A OE2 1
1428136 ATOM C C . GLU A 1 16 ? 21.285 17.755 13.469 1.00 14.68 ? 16 GLU A C 1
1429137 ATOM O O . GLU A 1 16 ? 20.543 18.546 12.880 1.00 14.29 ? 16 GLU A O 1
1430138 ATOM N N . GLU A 1 17 ? 20.999 16.456 13.612 1.00 13.64 ? 17 GLU A N 1
1431139 ATOM C CA . GLU A 1 17 ? 19.764 15.881 13.101 1.00 15.61 ? 17 GLU A CA 1
1432140 ATOM C CB . GLU A 1 17 ? 19.794 14.347 13.282 1.00 18.55 ? 17 GLU A CB 1
1433141 ATOM C CG . GLU A 1 17 ? 20.842 13.634 12.431 1.00 23.86 ? 17 GLU A CG 1
1434142 ATOM C CD . GLU A 1 17 ? 22.318 13.697 12.830 1.00 30.32 ? 17 GLU A CD 1
1435143 ATOM O OE1 . GLU A 1 17 ? 22.686 14.323 13.855 1.00 21.67 ? 17 GLU A OE1 1
1436144 ATOM O OE2 . GLU A 1 17 ? 23.124 13.099 12.080 1.00 42.45 ? 17 GLU A OE2 1
1437145 ATOM C C . GLU A 1 17 ? 18.521 16.482 13.765 1.00 13.46 ? 17 GLU A C 1
1438146 ATOM O O . GLU A 1 17 ? 17.490 16.689 13.112 1.00 14.05 ? 17 GLU A O 1
1439147 ATOM N N . LEU A 1 18 ? 18.628 16.789 15.062 1.00 11.98 ? 18 LEU A N 1
1440148 ATOM C CA . LEU A 1 18 ? 17.569 17.478 15.783 1.00 11.81 ? 18 LEU A CA 1
1441149 ATOM C CB . LEU A 1 18 ? 17.964 17.642 17.239 1.00 12.20 ? 18 LEU A CB 1
1442150 ATOM C CG . LEU A 1 18 ? 16.976 18.368 18.144 1.00 14.47 ? 18 LEU A CG 1
1443151 ATOM C CD1 . LEU A 1 18 ? 15.853 17.481 18.511 1.00 16.84 ? 18 LEU A CD1 1
1444152 ATOM C CD2 . LEU A 1 18 ? 17.638 18.853 19.410 1.00 16.00 ? 18 LEU A CD2 1
1445153 ATOM C C . LEU A 1 18 ? 17.289 18.850 15.167 1.00 12.51 ? 18 LEU A C 1
1446154 ATOM O O . LEU A 1 18 ? 16.136 19.202 14.928 1.00 12.51 ? 18 LEU A O 1
1447155 ATOM N N . LEU A 1 19 ? 18.357 19.609 14.885 1.00 13.60 ? 19 LEU A N 1
1448156 ATOM C CA . LEU A 1 19 ? 18.214 20.927 14.273 1.00 14.43 ? 19 LEU A CA 1
1449157 ATOM C CB . LEU A 1 19 ? 19.577 21.635 14.253 1.00 15.35 ? 19 LEU A CB 1
1450158 ATOM C CG . LEU A 1 19 ? 20.218 21.914 15.611 1.00 15.98 ? 19 LEU A CG 1
1451159 ATOM C CD1 . LEU A 1 19 ? 21.517 22.689 15.444 1.00 18.98 ? 19 LEU A CD1 1
1452160 ATOM C CD2 . LEU A 1 19 ? 19.266 22.641 16.542 1.00 16.64 ? 19 LEU A CD2 1
1453161 ATOM C C . LEU A 1 19 ? 17.620 20.864 12.864 1.00 15.61 ? 19 LEU A C 1
1454162 ATOM O O . LEU A 1 19 ? 16.878 21.756 12.459 1.00 15.54 ? 19 LEU A O 1
1455163 ATOM N N . LYS A 1 20 ? 17.940 19.803 12.120 1.00 16.15 ? 20 LYS A N 1
1456164 ATOM C CA . LYS A 1 20 ? 17.395 19.601 10.786 1.00 19.45 ? 20 LYS A CA 1
1457165 ATOM C CB . LYS A 1 20 ? 18.031 18.360 10.147 1.00 24.44 ? 20 LYS A CB 1
1458166 ATOM C CG . LYS A 1 20 ? 18.073 18.399 8.636 1.00 34.20 ? 20 LYS A CG 1
1459167 ATOM C CD . LYS A 1 20 ? 18.493 17.062 7.980 1.00 42.16 ? 20 LYS A CD 1
1460168 ATOM C CE . LYS A 1 20 ? 19.821 16.528 8.460 1.00 53.73 ? 20 LYS A CE 1
1461169 ATOM N NZ . LYS A 1 20 ? 20.915 17.507 8.266 1.00 54.49 ? 20 LYS A NZ 1
1462170 ATOM C C . LYS A 1 20 ? 15.867 19.484 10.822 1.00 18.24 ? 20 LYS A C 1
1463171 ATOM O O . LYS A 1 20 ? 15.167 20.129 10.039 1.00 17.95 ? 20 LYS A O 1
1464172 ATOM N N . VAL A 1 21 ? 15.345 18.661 11.735 1.00 17.04 ? 21 VAL A N 1
1465173 ATOM C CA . VAL A 1 21 ? 13.908 18.509 11.910 1.00 18.11 ? 21 VAL A CA 1
1466174 ATOM C CB . VAL A 1 21 ? 13.613 17.414 12.956 1.00 23.37 ? 21 VAL A CB 1
1467175 ATOM C CG1 . VAL A 1 21 ? 12.146 17.431 13.401 1.00 29.22 ? 21 VAL A CG1 1
1468176 ATOM C CG2 . VAL A 1 21 ? 14.016 16.054 12.420 1.00 25.60 ? 21 VAL A CG2 1
1469177 ATOM C C . VAL A 1 21 ? 13.234 19.828 12.283 1.00 16.81 ? 21 VAL A C 1
1470178 ATOM O O . VAL A 1 21 ? 12.104 20.104 11.876 1.00 14.99 ? 21 VAL A O 1
1471179 ATOM N N . LEU A 1 22 ? 13.943 20.654 13.054 1.00 16.33 ? 22 LEU A N 1
1472180 ATOM C CA . LEU A 1 22 ? 13.401 21.933 13.487 1.00 17.68 ? 22 LEU A CA 1
1473181 ATOM C CB . LEU A 1 22 ? 14.130 22.382 14.747 1.00 16.24 ? 22 LEU A CB 1
1474182 ATOM C CG . LEU A 1 22 ? 13.868 21.512 15.994 1.00 18.46 ? 22 LEU A CG 1
1475183 ATOM C CD1 . LEU A 1 22 ? 14.726 21.948 17.168 1.00 19.54 ? 22 LEU A CD1 1
1476184 ATOM C CD2 . LEU A 1 22 ? 12.407 21.548 16.379 1.00 21.14 ? 22 LEU A CD2 1
1477185 ATOM C C . LEU A 1 22 ? 13.498 23.000 12.399 1.00 19.07 ? 22 LEU A C 1
1478186 ATOM O O . LEU A 1 22 ? 13.016 24.109 12.592 1.00 19.56 ? 22 LEU A O 1
1479187 ATOM N N . GLY A 1 23 ? 14.138 22.662 11.272 1.00 18.89 ? 23 GLY A N 1
1480188 ATOM C CA . GLY A 1 23 ? 14.147 23.496 10.082 1.00 21.08 ? 23 GLY A CA 1
1481189 ATOM C C . GLY A 1 23 ? 15.258 24.543 10.038 1.00 20.88 ? 23 GLY A C 1
1482190 ATOM O O . GLY A 1 23 ? 15.153 25.522 9.305 1.00 22.02 ? 23 GLY A O 1
1483191 ATOM N N . VAL A 1 24 ? 16.321 24.336 10.824 1.00 17.91 ? 24 VAL A N 1
1484192 ATOM C CA . VAL A 1 24 ? 17.467 25.229 10.799 1.00 17.52 ? 24 VAL A CA 1
1485193 ATOM C CB . VAL A 1 24 ? 18.321 25.079 12.076 1.00 16.50 ? 24 VAL A CB 1
1486194 ATOM C CG1 . VAL A 1 24 ? 19.494 26.059 12.055 1.00 15.85 ? 24 VAL A CG1 1
1487195 ATOM C CG2 . VAL A 1 24 ? 17.478 25.243 13.326 1.00 16.00 ? 24 VAL A CG2 1
1488196 ATOM C C . VAL A 1 24 ? 18.309 24.954 9.557 1.00 19.26 ? 24 VAL A C 1
1489197 ATOM O O . VAL A 1 24 ? 18.654 23.805 9.291 1.00 18.31 ? 24 VAL A O 1
1490198 ATOM N N . ASN A 1 25 ? 18.669 26.017 8.825 1.00 18.62 ? 25 ASN A N 1
1491199 ATOM C CA . ASN A 1 25 ? 19.370 25.864 7.562 1.00 22.39 ? 25 ASN A CA 1
1492200 ATOM C CB . ASN A 1 25 ? 19.268 27.137 6.690 1.00 25.23 ? 25 ASN A CB 1
1493201 ATOM C CG . ASN A 1 25 ? 20.079 28.351 7.138 1.00 29.95 ? 25 ASN A CG 1
1494202 ATOM O OD1 . ASN A 1 25 ? 21.200 28.250 7.651 1.00 28.96 ? 25 ASN A OD1 1
1495203 ATOM N ND2 . ASN A 1 25 ? 19.542 29.556 6.897 1.00 32.03 ? 25 ASN A ND2 1
1496204 ATOM C C . ASN A 1 25 ? 20.826 25.457 7.786 1.00 21.34 ? 25 ASN A C 1
1497205 ATOM O O . ASN A 1 25 ? 21.337 25.562 8.893 1.00 19.71 ? 25 ASN A O 1
1498206 ATOM N N . VAL A 1 26 ? 21.479 25.007 6.707 1.00 23.47 ? 26 VAL A N 1
1499207 ATOM C CA . VAL A 1 26 ? 22.802 24.400 6.772 1.00 24.10 ? 26 VAL A CA 1
1500208 ATOM C CB . VAL A 1 26 ? 23.258 24.015 5.348 1.00 30.42 ? 26 VAL A CB 1
1501209 ATOM C CG1 . VAL A 1 26 ? 24.725 23.591 5.335 1.00 33.81 ? 26 VAL A CG1 1
1502210 ATOM C CG2 . VAL A 1 26 ? 22.359 22.928 4.765 1.00 32.15 ? 26 VAL A CG2 1
1503211 ATOM C C . VAL A 1 26 ? 23.861 25.270 7.449 1.00 21.81 ? 26 VAL A C 1
1504212 ATOM O O . VAL A 1 26 ? 24.595 24.789 8.311 1.00 21.03 ? 26 VAL A O 1
1505213 ATOM N N . MET A 1 27 ? 23.949 26.544 7.048 1.00 21.77 ? 27 MET A N 1
1506214 ATOM C CA . MET A 1 27 ? 24.975 27.431 7.576 1.00 22.29 ? 27 MET A CA 1
1507215 ATOM C CB . MET A 1 27 ? 25.042 28.742 6.769 1.00 25.80 ? 27 MET A CB 1
1508216 ATOM C CG . MET A 1 27 ? 25.974 28.691 5.550 1.00 34.01 ? 27 MET A CG 1
1509217 ATOM S SD . MET A 1 27 ? 25.118 28.424 3.978 1.00 45.83 ? 27 MET A SD 1
1510218 ATOM C CE . MET A 1 27 ? 26.515 28.372 2.850 1.00 41.63 ? 27 MET A CE 1
1511219 ATOM C C . MET A 1 27 ? 24.760 27.728 9.063 1.00 21.77 ? 27 MET A C 1
1512220 ATOM O O . MET A 1 27 ? 25.717 27.759 9.835 1.00 20.72 ? 27 MET A O 1
1513221 ATOM N N . LEU A 1 28 ? 23.504 27.917 9.491 1.00 19.53 ? 28 LEU A N 1
1514222 ATOM C CA . LEU A 1 28 ? 23.236 28.148 10.902 1.00 17.72 ? 28 LEU A CA 1
1515223 ATOM C CB . LEU A 1 28 ? 21.797 28.650 11.129 1.00 17.88 ? 28 LEU A CB 1
1516224 ATOM C CG . LEU A 1 28 ? 21.550 30.095 10.742 1.00 20.00 ? 28 LEU A CG 1
1517225 ATOM C CD1 . LEU A 1 28 ? 20.066 30.451 10.854 1.00 20.82 ? 28 LEU A CD1 1
1518226 ATOM C CD2 . LEU A 1 28 ? 22.375 31.042 11.593 1.00 18.30 ? 28 LEU A CD2 1
1519227 ATOM C C . LEU A 1 28 ? 23.487 26.887 11.725 1.00 17.11 ? 28 LEU A C 1
1520228 ATOM O O . LEU A 1 28 ? 23.932 26.973 12.867 1.00 16.01 ? 28 LEU A O 1
1521229 ATOM N N . ARG A 1 29 ? 23.193 25.714 11.148 1.00 17.26 ? 29 ARG A N 1
1522230 ATOM C CA . ARG A 1 29 ? 23.490 24.458 11.819 1.00 18.29 ? 29 ARG A CA 1
1523231 ATOM C CB . ARG A 1 29 ? 23.042 23.245 11.000 1.00 22.12 ? 29 ARG A CB 1
1524232 ATOM C CG . ARG A 1 29 ? 21.618 22.837 11.237 1.00 25.22 ? 29 ARG A CG 1
1525233 ATOM C CD . ARG A 1 29 ? 21.396 21.406 10.808 1.00 33.00 ? 29 ARG A CD 1
1526234 ATOM N NE . ARG A 1 29 ? 20.515 21.333 9.659 1.00 45.68 ? 29 ARG A NE 1
1527235 ATOM C CZ . ARG A 1 29 ? 20.900 21.255 8.398 1.00 35.38 ? 29 ARG A CZ 1
1528236 ATOM N NH1 . ARG A 1 29 ? 21.949 20.539 8.025 1.00 41.89 ? 29 ARG A NH1 1
1529237 ATOM N NH2 . ARG A 1 29 ? 20.176 21.872 7.478 1.00 30.70 ? 29 ARG A NH2 1
1530238 ATOM C C . ARG A 1 29 ? 24.988 24.332 12.096 1.00 20.21 ? 29 ARG A C 1
1531239 ATOM O O . ARG A 1 29 ? 25.388 23.910 13.178 1.00 17.16 ? 29 ARG A O 1
1532240 ATOM N N . LYS A 1 30 ? 25.798 24.700 11.102 1.00 20.12 ? 30 LYS A N 1
1533241 ATOM C CA . LYS A 1 30 ? 27.248 24.668 11.220 1.00 26.22 ? 30 LYS A CA 1
1534242 ATOM C CB . LYS A 1 30 ? 27.868 25.244 9.933 1.00 31.27 ? 30 LYS A CB 1
1535243 ATOM C CG . LYS A 1 30 ? 29.344 24.955 9.727 1.00 39.87 ? 30 LYS A CG 1
1536244 ATOM C CD . LYS A 1 30 ? 29.782 25.300 8.301 1.00 45.37 ? 30 LYS A CD 1
1537245 ATOM C CE . LYS A 1 30 ? 31.220 24.940 8.002 1.00 56.20 ? 30 LYS A CE 1
1538246 ATOM N NZ . LYS A 1 30 ? 32.173 25.844 8.696 1.00 63.05 ? 30 LYS A NZ 1
1539247 ATOM C C . LYS A 1 30 ? 27.704 25.441 12.457 1.00 23.65 ? 30 LYS A C 1
1540248 ATOM O O . LYS A 1 30 ? 28.455 24.913 13.277 1.00 25.03 ? 30 LYS A O 1
1541249 ATOM N N . ILE A 1 31 ? 27.206 26.677 12.594 1.00 21.76 ? 31 ILE A N 1
1542250 ATOM C CA . ILE A 1 31 ? 27.529 27.549 13.711 1.00 20.15 ? 31 ILE A CA 1
1543251 ATOM C CB . ILE A 1 31 ? 26.851 28.939 13.502 1.00 20.86 ? 31 ILE A CB 1
1544252 ATOM C CG1 . ILE A 1 31 ? 27.421 29.640 12.252 1.00 22.14 ? 31 ILE A CG1 1
1545253 ATOM C CG2 . ILE A 1 31 ? 26.965 29.830 14.747 1.00 20.08 ? 31 ILE A CG2 1
1546254 ATOM C CD1 . ILE A 1 31 ? 26.672 30.939 11.810 1.00 24.07 ? 31 ILE A CD1 1
1547255 ATOM C C . ILE A 1 31 ? 27.124 26.909 15.035 1.00 20.87 ? 31 ILE A C 1
1548256 ATOM O O . ILE A 1 31 ? 27.919 26.856 15.973 1.00 17.77 ? 31 ILE A O 1
1549257 ATOM N N . ALA A 1 32 ? 25.870 26.438 15.098 1.00 16.07 ? 32 ALA A N 1
1550258 ATOM C CA . ALA A 1 32 ? 25.305 25.906 16.322 1.00 15.30 ? 32 ALA A CA 1
1551259 ATOM C CB . ALA A 1 32 ? 23.818 25.615 16.126 1.00 15.97 ? 32 ALA A CB 1
1552260 ATOM C C . ALA A 1 32 ? 26.039 24.653 16.796 1.00 14.69 ? 32 ALA A C 1
1553261 ATOM O O . ALA A 1 32 ? 26.324 24.529 17.977 1.00 13.26 ? 32 ALA A O 1
1554262 ATOM N N . VAL A 1 33 ? 26.341 23.733 15.873 1.00 16.21 ? 33 VAL A N 1
1555263 ATOM C CA . VAL A 1 33 ? 26.962 22.467 16.244 1.00 16.96 ? 33 VAL A CA 1
1556264 ATOM C CB . VAL A 1 33 ? 27.040 21.485 15.049 1.00 18.93 ? 33 VAL A CB 1
1557265 ATOM C CG1 . VAL A 1 33 ? 27.905 20.273 15.377 1.00 24.17 ? 33 VAL A CG1 1
1558266 ATOM C CG2 . VAL A 1 33 ? 25.645 21.049 14.607 1.00 21.24 ? 33 VAL A CG2 1
1559267 ATOM C C . VAL A 1 33 ? 28.349 22.701 16.846 1.00 16.45 ? 33 VAL A C 1
1560268 ATOM O O . VAL A 1 33 ? 28.700 22.084 17.847 1.00 18.49 ? 33 VAL A O 1
1561269 ATOM N N . ALA A 1 34 ? 29.118 23.613 16.251 1.00 16.53 ? 34 ALA A N 1
1562270 ATOM C CA . ALA A 1 34 ? 30.451 23.913 16.752 1.00 17.77 ? 34 ALA A CA 1
1563271 ATOM C CB . ALA A 1 34 ? 31.170 24.876 15.826 1.00 19.76 ? 34 ALA A CB 1
1564272 ATOM C C . ALA A 1 34 ? 30.375 24.477 18.170 1.00 20.37 ? 34 ALA A C 1
1565273 ATOM O O . ALA A 1 34 ? 31.106 24.032 19.054 1.00 19.53 ? 34 ALA A O 1
1566274 ATOM N N . ALA A 1 35 ? 29.468 25.439 18.389 1.00 15.32 ? 35 ALA A N 1
1567275 ATOM C CA . ALA A 1 35 ? 29.377 26.107 19.675 1.00 15.01 ? 35 ALA A CA 1
1568276 ATOM C CB . ALA A 1 35 ? 28.514 27.358 19.587 1.00 16.23 ? 35 ALA A CB 1
1569277 ATOM C C . ALA A 1 35 ? 28.824 25.171 20.746 1.00 14.54 ? 35 ALA A C 1
1570278 ATOM O O . ALA A 1 35 ? 29.225 25.254 21.904 1.00 13.61 ? 35 ALA A O 1
1571279 ATOM N N . ALA A 1 36 ? 27.875 24.305 20.361 1.00 12.27 ? 36 ALA A N 1
1572280 ATOM C CA . ALA A 1 36 ? 27.245 23.408 21.314 1.00 13.95 ? 36 ALA A CA 1
1573281 ATOM C CB . ALA A 1 36 ? 25.937 22.863 20.746 1.00 13.67 ? 36 ALA A CB 1
1574282 ATOM C C . ALA A 1 36 ? 28.147 22.255 21.748 1.00 13.51 ? 36 ALA A C 1
1575283 ATOM O O . ALA A 1 36 ? 27.767 21.487 22.622 1.00 14.89 ? 36 ALA A O 1
1576284 ATOM N N . SER A 1 37 ? 29.330 22.128 21.138 1.00 14.15 ? 37 SER A N 1
1577285 ATOM C CA . SER A 1 37 ? 30.232 21.040 21.479 1.00 16.97 ? 37 SER A CA 1
1578286 ATOM C CB . SER A 1 37 ? 31.205 20.782 20.335 1.00 18.82 ? 37 SER A CB 1
1579287 ATOM O OG . SER A 1 37 ? 32.194 21.792 20.308 1.00 26.28 ? 37 SER A OG 1
1580288 ATOM C C . SER A 1 37 ? 30.996 21.271 22.782 1.00 19.42 ? 37 SER A C 1
1581289 ATOM O O . SER A 1 37 ? 31.512 20.319 23.358 1.00 19.91 ? 37 SER A O 1
1582290 ATOM N N . LYS A 1 38 ? 31.043 22.518 23.272 1.00 18.63 ? 38 LYS A N 1
1583291 ATOM C CA . LYS A 1 38 ? 31.680 22.793 24.553 1.00 20.95 ? 38 LYS A CA 1
1584292 ATOM C CB . LYS A 1 38 ? 33.126 23.288 24.351 1.00 31.89 ? 38 LYS A CB 1
1585293 ATOM C CG . LYS A 1 38 ? 33.292 24.414 23.342 1.00 45.28 ? 38 LYS A CG 1
1586294 ATOM C CD . LYS A 1 38 ? 34.769 24.711 22.992 1.00 57.10 ? 38 LYS A CD 1
1587295 ATOM C CE . LYS A 1 38 ? 35.347 23.809 21.917 1.00 65.98 ? 38 LYS A CE 1
1588296 ATOM N NZ . LYS A 1 38 ? 35.558 22.410 22.380 1.00 76.01 ? 38 LYS A NZ 1
1589297 ATOM C C . LYS A 1 38 ? 30.859 23.764 25.401 1.00 16.81 ? 38 LYS A C 1
1590298 ATOM O O . LYS A 1 38 ? 31.270 24.887 25.679 1.00 20.47 ? 38 LYS A O 1
1591299 ATOM N N . PRO A 1 39 ? 29.678 23.335 25.886 1.00 13.96 ? 39 PRO A N 1
1592300 ATOM C CA . PRO A 1 39 ? 28.833 24.185 26.722 1.00 14.32 ? 39 PRO A CA 1
1593301 ATOM C CB . PRO A 1 39 ? 27.496 23.454 26.684 1.00 13.13 ? 39 PRO A CB 1
1594302 ATOM C CG . PRO A 1 39 ? 27.875 22.029 26.575 1.00 14.04 ? 39 PRO A CG 1
1595303 ATOM C CD . PRO A 1 39 ? 29.127 21.981 25.727 1.00 13.41 ? 39 PRO A CD 1
1596304 ATOM C C . PRO A 1 39 ? 29.353 24.278 28.153 1.00 14.57 ? 39 PRO A C 1
1597305 ATOM O O . PRO A 1 39 ? 30.126 23.430 28.596 1.00 15.97 ? 39 PRO A O 1
1598306 ATOM N N . ALA A 1 40 ? 28.948 25.338 28.852 1.00 13.08 ? 40 ALA A N 1
1599307 ATOM C CA . ALA A 1 40 ? 29.078 25.416 30.297 1.00 14.41 ? 40 ALA A CA 1
1600308 ATOM C CB . ALA A 1 40 ? 29.748 26.717 30.683 1.00 16.05 ? 40 ALA A CB 1
1601309 ATOM C C . ALA A 1 40 ? 27.673 25.325 30.885 1.00 13.27 ? 40 ALA A C 1
1602310 ATOM O O . ALA A 1 40 ? 26.812 26.114 30.513 1.00 13.72 ? 40 ALA A O 1
1603311 ATOM N N . VAL A 1 41 ? 27.434 24.353 31.775 1.00 11.57 ? 41 VAL A N 1
1604312 ATOM C CA . VAL A 1 41 ? 26.113 24.158 32.355 1.00 11.36 ? 41 VAL A CA 1
1605313 ATOM C CB . VAL A 1 41 ? 25.503 22.801 31.959 1.00 12.66 ? 41 VAL A CB 1
1606314 ATOM C CG1 . VAL A 1 41 ? 24.175 22.570 32.657 1.00 15.41 ? 41 VAL A CG1 1
1607315 ATOM C CG2 . VAL A 1 41 ? 25.338 22.687 30.442 1.00 13.29 ? 41 VAL A CG2 1
1608316 ATOM C C . VAL A 1 41 ? 26.200 24.298 33.873 1.00 13.97 ? 41 VAL A C 1
1609317 ATOM O O . VAL A 1 41 ? 26.992 23.601 34.512 1.00 13.29 ? 41 VAL A O 1
1610318 ATOM N N . GLU A 1 42 ? 25.377 25.200 34.431 1.00 11.62 ? 42 GLU A N 1
1611319 ATOM C CA . GLU A 1 42 ? 25.261 25.396 35.867 1.00 13.18 ? 42 GLU A CA 1
1612320 ATOM C CB . GLU A 1 42 ? 25.629 26.847 36.239 1.00 18.98 ? 42 GLU A CB 1
1613321 ATOM C CG . GLU A 1 42 ? 25.465 27.159 37.719 1.00 21.81 ? 42 GLU A CG 1
1614322 ATOM C CD . GLU A 1 42 ? 25.846 28.570 38.115 1.00 29.41 ? 42 GLU A CD 1
1615323 ATOM O OE1 . GLU A 1 42 ? 25.571 29.513 37.336 1.00 32.27 ? 42 GLU A OE1 1
1616324 ATOM O OE2 . GLU A 1 42 ? 26.396 28.731 39.225 1.00 41.13 ? 42 GLU A OE2 1
1617325 ATOM C C . GLU A 1 42 ? 23.827 25.091 36.302 1.00 14.33 ? 42 GLU A C 1
1618326 ATOM O O . GLU A 1 42 ? 22.884 25.652 35.747 1.00 12.55 ? 42 GLU A O 1
1619327 ATOM N N . ILE A 1 43 ? 23.671 24.166 37.259 1.00 11.93 ? 43 ILE A N 1
1620328 ATOM C CA . ILE A 1 43 ? 22.367 23.835 37.817 1.00 12.03 ? 43 ILE A CA 1
1621329 ATOM C CB . ILE A 1 43 ? 21.977 22.355 37.566 1.00 10.90 ? 43 ILE A CB 1
1622330 ATOM C CG1 . ILE A 1 43 ? 21.948 22.042 36.055 1.00 11.89 ? 43 ILE A CG1 1
1623331 ATOM C CG2 . ILE A 1 43 ? 20.663 21.999 38.219 1.00 11.56 ? 43 ILE A CG2 1
1624332 ATOM C CD1 . ILE A 1 43 ? 21.545 20.633 35.706 1.00 13.56 ? 43 ILE A CD1 1
1625333 ATOM C C . ILE A 1 43 ? 22.383 24.144 39.308 1.00 13.46 ? 43 ILE A C 1
1626334 ATOM O O . ILE A 1 43 ? 23.316 23.747 40.014 1.00 14.64 ? 43 ILE A O 1
1627335 ATOM N N . LYS A 1 44 ? 21.340 24.855 39.765 1.00 13.12 ? 44 LYS A N 1
1628336 ATOM C CA . LYS A 1 44 ? 21.092 25.074 41.180 1.00 16.76 ? 44 LYS A CA 1
1629337 ATOM C CB . LYS A 1 44 ? 21.202 26.564 41.545 1.00 19.97 ? 44 LYS A CB 1
1630338 ATOM C CG . LYS A 1 44 ? 22.529 27.187 41.150 1.00 26.97 ? 44 LYS A CG 1
1631339 ATOM C CD . LYS A 1 44 ? 22.692 28.601 41.677 1.00 42.80 ? 44 LYS A CD 1
1632340 ATOM C CE . LYS A 1 44 ? 23.945 29.251 41.147 1.00 53.19 ? 44 LYS A CE 1
1633341 ATOM N NZ . LYS A 1 44 ? 24.055 30.662 41.593 1.00 62.51 ? 44 LYS A NZ 1
1634342 ATOM C C . LYS A 1 44 ? 19.699 24.528 41.482 1.00 17.89 ? 44 LYS A C 1
1635343 ATOM O O . LYS A 1 44 ? 18.724 24.914 40.837 1.00 16.69 ? 44 LYS A O 1
1636344 ATOM N N . GLN A 1 45 ? 19.626 23.606 42.448 1.00 19.78 ? 45 GLN A N 1
1637345 ATOM C CA . GLN A 1 45 ? 18.380 22.966 42.824 1.00 18.92 ? 45 GLN A CA 1
1638346 ATOM C CB . GLN A 1 45 ? 18.439 21.461 42.572 1.00 19.29 ? 45 GLN A CB 1
1639347 ATOM C CG . GLN A 1 45 ? 17.196 20.707 43.035 1.00 18.16 ? 45 GLN A CG 1
1640348 ATOM C CD . GLN A 1 45 ? 17.330 19.220 42.841 1.00 22.41 ? 45 GLN A CD 1
1641349 ATOM O OE1 . GLN A 1 45 ? 18.310 18.716 42.286 1.00 24.28 ? 45 GLN A OE1 1
1642350 ATOM N NE2 . GLN A 1 45 ? 16.349 18.479 43.296 1.00 22.68 ? 45 GLN A NE2 1
1643351 ATOM C C . GLN A 1 45 ? 18.124 23.236 44.301 1.00 21.12 ? 45 GLN A C 1
1644352 ATOM O O . GLN A 1 45 ? 19.031 23.099 45.117 1.00 20.24 ? 45 GLN A O 1
1645353 ATOM N N . GLU A 1 46 ? 16.882 23.614 44.619 1.00 18.50 ? 46 GLU A N 1
1646354 ATOM C CA . GLU A 1 46 ? 16.420 23.746 45.991 1.00 22.59 ? 46 GLU A CA 1
1647355 ATOM C CB . GLU A 1 46 ? 16.295 25.228 46.385 1.00 31.02 ? 46 GLU A CB 1
1648356 ATOM C CG . GLU A 1 46 ? 17.565 25.867 46.925 1.00 45.28 ? 46 GLU A CG 1
1649357 ATOM C CD . GLU A 1 46 ? 17.731 25.765 48.433 1.00 61.86 ? 46 GLU A CD 1
1650358 ATOM O OE1 . GLU A 1 46 ? 16.823 26.228 49.164 1.00 74.93 ? 46 GLU A OE1 1
1651359 ATOM O OE2 . GLU A 1 46 ? 18.771 25.234 48.886 1.00 65.92 ? 46 GLU A OE2 1
1652360 ATOM C C . GLU A 1 46 ? 15.069 23.045 46.050 1.00 20.00 ? 46 GLU A C 1
1653361 ATOM O O . GLU A 1 46 ? 14.061 23.632 45.676 1.00 20.55 ? 46 GLU A O 1
1654362 ATOM N N . GLY A 1 47 ? 15.061 21.772 46.457 1.00 20.39 ? 47 GLY A N 1
1655363 ATOM C CA . GLY A 1 47 ? 13.837 20.986 46.454 1.00 22.02 ? 47 GLY A CA 1
1656364 ATOM C C . GLY A 1 47 ? 13.360 20.737 45.025 1.00 20.19 ? 47 GLY A C 1
1657365 ATOM O O . GLY A 1 47 ? 14.109 20.205 44.215 1.00 19.97 ? 47 GLY A O 1
1658366 ATOM N N . ASP A 1 48 ? 12.130 21.167 44.718 1.00 17.32 ? 48 ASP A N 1
1659367 ATOM C CA . ASP A 1 48 ? 11.594 21.074 43.367 1.00 17.38 ? 48 ASP A CA 1
1660368 ATOM C CB . ASP A 1 48 ? 10.118 20.625 43.438 1.00 21.49 ? 48 ASP A CB 1
1661369 ATOM C CG . ASP A 1 48 ? 9.923 19.176 43.862 1.00 24.99 ? 48 ASP A CG 1
1662370 ATOM O OD1 . ASP A 1 48 ? 10.839 18.356 43.627 1.00 27.02 ? 48 ASP A OD1 1
1663371 ATOM O OD2 . ASP A 1 48 ? 8.885 18.877 44.475 1.00 30.47 ? 48 ASP A OD2 1
1664372 ATOM C C . ASP A 1 48 ? 11.730 22.370 42.561 1.00 16.47 ? 48 ASP A C 1
1665373 ATOM O O . ASP A 1 48 ? 11.100 22.508 41.508 1.00 17.15 ? 48 ASP A O 1
1666374 ATOM N N . THR A 1 49 ? 12.574 23.301 43.044 1.00 16.16 ? 49 THR A N 1
1667375 ATOM C CA . THR A 1 49 ? 12.866 24.545 42.349 1.00 15.84 ? 49 THR A CA 1
1668376 ATOM C CB . THR A 1 49 ? 12.778 25.715 43.315 1.00 18.83 ? 49 THR A CB 1
1669377 ATOM O OG1 . THR A 1 49 ? 11.427 25.815 43.798 1.00 19.21 ? 49 THR A OG1 1
1670378 ATOM C CG2 . THR A 1 49 ? 13.178 27.017 42.696 1.00 20.27 ? 49 THR A CG2 1
1671379 ATOM C C . THR A 1 49 ? 14.241 24.466 41.688 1.00 15.41 ? 49 THR A C 1
1672380 ATOM O O . THR A 1 49 ? 15.232 24.115 42.334 1.00 14.89 ? 49 THR A O 1
1673381 ATOM N N . PHE A 1 50 ? 14.282 24.832 40.406 1.00 13.14 ? 50 PHE A N 1
1674382 ATOM C CA . PHE A 1 50 ? 15.476 24.680 39.592 1.00 12.84 ? 50 PHE A CA 1
1675383 ATOM C CB . PHE A 1 50 ? 15.277 23.584 38.526 1.00 12.73 ? 50 PHE A CB 1
1676384 ATOM C CG . PHE A 1 50 ? 15.271 22.179 39.057 1.00 13.73 ? 50 PHE A CG 1
1677385 ATOM C CD1 . PHE A 1 50 ? 14.116 21.629 39.593 1.00 15.12 ? 50 PHE A CD1 1
1678386 ATOM C CD2 . PHE A 1 50 ? 16.428 21.405 39.039 1.00 15.39 ? 50 PHE A CD2 1
1679387 ATOM C CE1 . PHE A 1 50 ? 14.107 20.328 40.068 1.00 15.46 ? 50 PHE A CE1 1
1680388 ATOM C CE2 . PHE A 1 50 ? 16.419 20.107 39.538 1.00 15.84 ? 50 PHE A CE2 1
1681389 ATOM C CZ . PHE A 1 50 ? 15.265 19.580 40.055 1.00 15.19 ? 50 PHE A CZ 1
1682390 ATOM C C . PHE A 1 50 ? 15.843 25.984 38.894 1.00 13.00 ? 50 PHE A C 1
1683391 ATOM O O . PHE A 1 50 ? 14.964 26.738 38.491 1.00 13.60 ? 50 PHE A O 1
1684392 ATOM N N . TYR A 1 51 ? 17.157 26.227 38.801 1.00 12.46 ? 51 TYR A N 1
1685393 ATOM C CA . TYR A 1 51 ? 17.755 27.214 37.924 1.00 13.99 ? 51 TYR A CA 1
1686394 ATOM C CB . TYR A 1 51 ? 18.451 28.321 38.756 1.00 16.71 ? 51 TYR A CB 1
1687395 ATOM C CG . TYR A 1 51 ? 19.393 29.225 37.982 1.00 17.44 ? 51 TYR A CG 1
1688396 ATOM C CD1 . TYR A 1 51 ? 18.918 30.334 37.288 1.00 22.59 ? 51 TYR A CD1 1
1689397 ATOM C CD2 . TYR A 1 51 ? 20.762 28.973 37.943 1.00 18.80 ? 51 TYR A CD2 1
1690398 ATOM C CE1 . TYR A 1 51 ? 19.781 31.184 36.598 1.00 22.11 ? 51 TYR A CE1 1
1691399 ATOM C CE2 . TYR A 1 51 ? 21.633 29.809 37.245 1.00 18.72 ? 51 TYR A CE2 1
1692400 ATOM C CZ . TYR A 1 51 ? 21.137 30.913 36.571 1.00 22.39 ? 51 TYR A CZ 1
1693401 ATOM O OH . TYR A 1 51 ? 21.985 31.740 35.865 1.00 23.44 ? 51 TYR A OH 1
1694402 ATOM C C . TYR A 1 51 ? 18.764 26.482 37.041 1.00 12.72 ? 51 TYR A C 1
1695403 ATOM O O . TYR A 1 51 ? 19.621 25.771 37.559 1.00 13.67 ? 51 TYR A O 1
1696404 ATOM N N . ILE A 1 52 ? 18.687 26.673 35.718 1.00 12.05 ? 52 ILE A N 1
1697405 ATOM C CA . ILE A 1 52 ? 19.593 26.001 34.794 1.00 11.46 ? 52 ILE A CA 1
1698406 ATOM C CB . ILE A 1 52 ? 18.954 24.801 34.046 1.00 10.99 ? 52 ILE A CB 1
1699407 ATOM C CG1 . ILE A 1 52 ? 18.356 23.757 35.024 1.00 11.77 ? 52 ILE A CG1 1
1700408 ATOM C CG2 . ILE A 1 52 ? 19.961 24.169 33.071 1.00 12.62 ? 52 ILE A CG2 1
1701409 ATOM C CD1 . ILE A 1 52 ? 17.636 22.610 34.343 1.00 12.26 ? 52 ILE A CD1 1
1702410 ATOM C C . ILE A 1 52 ? 20.092 27.034 33.790 1.00 11.68 ? 52 ILE A C 1
1703411 ATOM O O . ILE A 1 52 ? 19.295 27.597 33.042 1.00 13.59 ? 52 ILE A O 1
1704412 ATOM N N . LYS A 1 53 ? 21.409 27.268 33.793 1.00 11.19 ? 53 LYS A N 1
1705413 ATOM C CA . LYS A 1 53 ? 22.054 28.173 32.855 1.00 11.86 ? 53 LYS A CA 1
1706414 ATOM C CB . LYS A 1 53 ? 22.872 29.239 33.575 1.00 14.47 ? 53 LYS A CB 1
1707415 ATOM C CG . LYS A 1 53 ? 23.652 30.179 32.641 1.00 15.84 ? 53 LYS A CG 1
1708416 ATOM C CD . LYS A 1 53 ? 24.489 31.166 33.427 1.00 22.67 ? 53 LYS A CD 1
1709417 ATOM C CE . LYS A 1 53 ? 24.975 32.319 32.595 1.00 35.46 ? 53 LYS A CE 1
1710418 ATOM N NZ . LYS A 1 53 ? 25.933 33.162 33.360 1.00 38.85 ? 53 LYS A NZ 1
1711419 ATOM C C . LYS A 1 53 ? 22.948 27.342 31.941 1.00 12.39 ? 53 LYS A C 1
1712420 ATOM O O . LYS A 1 53 ? 23.796 26.586 32.416 1.00 11.42 ? 53 LYS A O 1
1713421 ATOM N N . THR A 1 54 ? 22.735 27.492 30.633 1.00 10.51 ? 54 THR A N 1
1714422 ATOM C CA . THR A 1 54 ? 23.498 26.779 29.623 1.00 11.34 ? 54 THR A CA 1
1715423 ATOM C CB . THR A 1 54 ? 22.608 25.846 28.801 1.00 12.49 ? 54 THR A CB 1
1716424 ATOM O OG1 . THR A 1 54 ? 21.911 24.968 29.682 1.00 12.87 ? 54 THR A OG1 1
1717425 ATOM C CG2 . THR A 1 54 ? 23.411 25.058 27.769 1.00 11.96 ? 54 THR A CG2 1
1718426 ATOM C C . THR A 1 54 ? 24.149 27.822 28.728 1.00 11.45 ? 54 THR A C 1
1719427 ATOM O O . THR A 1 54 ? 23.443 28.578 28.068 1.00 12.03 ? 54 THR A O 1
1720428 ATOM N N . SER A 1 55 ? 25.490 27.866 28.729 1.00 11.65 ? 55 SER A N 1
1721429 ATOM C CA . SER A 1 55 ? 26.225 28.930 28.074 1.00 13.22 ? 55 SER A CA 1
1722430 ATOM C CB . SER A 1 55 ? 27.069 29.677 29.103 1.00 19.07 ? 55 SER A CB 1
1723431 ATOM O OG . SER A 1 55 ? 27.863 30.651 28.460 1.00 33.54 ? 55 SER A OG 1
1724432 ATOM C C . SER A 1 55 ? 27.114 28.406 26.948 1.00 12.65 ? 55 SER A C 1
1725433 ATOM O O . SER A 1 55 ? 27.821 27.413 27.116 1.00 12.90 ? 55 SER A O 1
1726434 ATOM N N . THR A 1 56 ? 27.049 29.080 25.794 1.00 11.74 ? 56 THR A N 1
1727435 ATOM C CA . THR A 1 56 ? 27.938 28.831 24.667 1.00 11.97 ? 56 THR A CA 1
1728436 ATOM C CB . THR A 1 56 ? 27.270 28.017 23.532 1.00 12.56 ? 56 THR A CB 1
1729437 ATOM O OG1 . THR A 1 56 ? 26.304 28.850 22.877 1.00 13.07 ? 56 THR A OG1 1
1730438 ATOM C CG2 . THR A 1 56 ? 26.610 26.757 24.021 1.00 13.64 ? 56 THR A CG2 1
1731439 ATOM C C . THR A 1 56 ? 28.382 30.192 24.138 1.00 12.27 ? 56 THR A C 1
1732440 ATOM O O . THR A 1 56 ? 27.851 31.218 24.544 1.00 11.65 ? 56 THR A O 1
1733441 ATOM N N . THR A 1 57 ? 29.335 30.188 23.203 1.00 12.33 ? 57 THR A N 1
1734442 ATOM C CA . THR A 1 57 ? 29.833 31.416 22.609 1.00 12.92 ? 57 THR A CA 1
1735443 ATOM C CB . THR A 1 57 ? 31.057 31.140 21.744 1.00 14.82 ? 57 THR A CB 1
1736444 ATOM O OG1 . THR A 1 57 ? 30.726 30.160 20.763 1.00 14.27 ? 57 THR A OG1 1
1737445 ATOM C CG2 . THR A 1 57 ? 32.255 30.691 22.563 1.00 16.90 ? 57 THR A CG2 1
1738446 ATOM C C . THR A 1 57 ? 28.799 32.175 21.777 1.00 12.60 ? 57 THR A C 1
1739447 ATOM O O . THR A 1 57 ? 29.005 33.348 21.499 1.00 13.08 ? 57 THR A O 1
1740448 ATOM N N . VAL A 1 58 ? 27.705 31.496 21.380 1.00 11.95 ? 58 VAL A N 1
1741449 ATOM C CA . VAL A 1 58 ? 26.710 32.085 20.489 1.00 12.49 ? 58 VAL A CA 1
1742450 ATOM C CB . VAL A 1 58 ? 26.574 31.279 19.163 1.00 13.69 ? 58 VAL A CB 1
1743451 ATOM C CG1 . VAL A 1 58 ? 27.904 31.183 18.419 1.00 15.38 ? 58 VAL A CG1 1
1744452 ATOM C CG2 . VAL A 1 58 ? 25.972 29.894 19.405 1.00 12.99 ? 58 VAL A CG2 1
1745453 ATOM C C . VAL A 1 58 ? 25.320 32.247 21.101 1.00 12.05 ? 58 VAL A C 1
1746454 ATOM O O . VAL A 1 58 ? 24.477 32.897 20.502 1.00 12.01 ? 58 VAL A O 1
1747455 ATOM N N . ARG A 1 59 ? 25.090 31.687 22.293 1.00 11.81 ? 59 ARG A N 1
1748456 ATOM C CA . ARG A 1 59 ? 23.769 31.721 22.904 1.00 12.94 ? 59 ARG A CA 1
1749457 ATOM C CB . ARG A 1 59 ? 22.794 30.837 22.086 1.00 15.99 ? 59 ARG A CB 1
1750458 ATOM C CG . ARG A 1 59 ? 21.363 30.728 22.629 1.00 20.03 ? 59 ARG A CG 1
1751459 ATOM C CD . ARG A 1 59 ? 20.503 30.029 21.578 1.00 21.30 ? 59 ARG A CD 1
1752460 ATOM N NE . ARG A 1 59 ? 19.235 29.531 22.092 1.00 27.32 ? 59 ARG A NE 1
1753461 ATOM C CZ . ARG A 1 59 ? 18.154 30.279 22.274 1.00 27.75 ? 59 ARG A CZ 1
1754462 ATOM N NH1 . ARG A 1 59 ? 18.144 31.565 21.964 1.00 29.08 ? 59 ARG A NH1 1
1755463 ATOM N NH2 . ARG A 1 59 ? 17.054 29.721 22.770 1.00 34.16 ? 59 ARG A NH2 1
1756464 ATOM C C . ARG A 1 59 ? 23.846 31.212 24.334 1.00 12.18 ? 59 ARG A C 1
1757465 ATOM O O . ARG A 1 59 ? 24.432 30.160 24.581 1.00 11.58 ? 59 ARG A O 1
1758466 ATOM N N . THR A 1 60 ? 23.230 31.960 25.254 1.00 12.49 ? 60 THR A N 1
1759467 ATOM C CA . THR A 1 60 ? 23.075 31.513 26.627 1.00 13.24 ? 60 THR A CA 1
1760468 ATOM C CB . THR A 1 60 ? 23.882 32.423 27.557 1.00 14.20 ? 60 THR A CB 1
1761469 ATOM O OG1 . THR A 1 60 ? 25.277 32.311 27.224 1.00 14.79 ? 60 THR A OG1 1
1762470 ATOM C CG2 . THR A 1 60 ? 23.665 32.090 29.020 1.00 16.28 ? 60 THR A CG2 1
1763471 ATOM C C . THR A 1 60 ? 21.588 31.494 26.966 1.00 12.71 ? 60 THR A C 1
1764472 ATOM O O . THR A 1 60 ? 20.868 32.413 26.600 1.00 14.20 ? 60 THR A O 1
1765473 ATOM N N . THR A 1 61 ? 21.145 30.442 27.662 1.00 13.12 ? 61 THR A N 1
1766474 ATOM C CA . THR A 1 61 ? 19.780 30.363 28.154 1.00 13.17 ? 61 THR A CA 1
1767475 ATOM C CB . THR A 1 61 ? 18.995 29.189 27.527 1.00 14.61 ? 61 THR A CB 1
1768476 ATOM O OG1 . THR A 1 61 ? 19.612 27.946 27.851 1.00 17.76 ? 61 THR A OG1 1
1769477 ATOM C CG2 . THR A 1 61 ? 18.873 29.294 26.002 1.00 17.06 ? 61 THR A CG2 1
1770478 ATOM C C . THR A 1 61 ? 19.839 30.247 29.672 1.00 12.80 ? 61 THR A C 1
1771479 ATOM O O . THR A 1 61 ? 20.727 29.582 30.204 1.00 12.63 ? 61 THR A O 1
1772480 ATOM N N . GLU A 1 62 ? 18.879 30.893 30.345 1.00 14.32 ? 62 GLU A N 1
1773481 ATOM C CA . GLU A 1 62 ? 18.681 30.748 31.779 1.00 14.27 ? 62 GLU A CA 1
1774482 ATOM C CB . GLU A 1 62 ? 19.068 32.010 32.541 1.00 19.00 ? 62 GLU A CB 1
1775483 ATOM C CG . GLU A 1 62 ? 20.500 32.437 32.372 1.00 23.01 ? 62 GLU A CG 1
1776484 ATOM C CD . GLU A 1 62 ? 20.802 33.732 33.098 1.00 35.91 ? 62 GLU A CD 1
1777485 ATOM O OE1 . GLU A 1 62 ? 20.845 33.717 34.349 1.00 31.82 ? 62 GLU A OE1 1
1778486 ATOM O OE2 . GLU A 1 62 ? 20.965 34.768 32.414 1.00 43.23 ? 62 GLU A OE2 1
1779487 ATOM C C . GLU A 1 62 ? 17.202 30.478 32.030 1.00 14.48 ? 62 GLU A C 1
1780488 ATOM O O . GLU A 1 62 ? 16.373 31.330 31.716 1.00 16.09 ? 62 GLU A O 1
1781489 ATOM N N . ILE A 1 63 ? 16.883 29.321 32.615 1.00 12.53 ? 63 ILE A N 1
1782490 ATOM C CA . ILE A 1 63 ? 15.507 28.999 32.952 1.00 13.46 ? 63 ILE A CA 1
1783491 ATOM C CB . ILE A 1 63 ? 14.964 27.783 32.162 1.00 13.80 ? 63 ILE A CB 1
1784492 ATOM C CG1 . ILE A 1 63 ? 15.671 26.467 32.502 1.00 15.19 ? 63 ILE A CG1 1
1785493 ATOM C CG2 . ILE A 1 63 ? 15.002 28.077 30.658 1.00 15.51 ? 63 ILE A CG2 1
1786494 ATOM C CD1 . ILE A 1 63 ? 15.077 25.247 31.802 1.00 17.40 ? 63 ILE A CD1 1
1787495 ATOM C C . ILE A 1 63 ? 15.368 28.819 34.459 1.00 14.65 ? 63 ILE A C 1
1788496 ATOM O O . ILE A 1 63 ? 16.296 28.358 35.123 1.00 13.32 ? 63 ILE A O 1
1789497 ATOM N N . ASN A 1 64 ? 14.208 29.247 34.962 1.00 14.20 ? 64 ASN A N 1
1790498 ATOM C CA . ASN A 1 64 ? 13.823 29.116 36.354 1.00 17.55 ? 64 ASN A CA 1
1791499 ATOM C CB . ASN A 1 64 ? 13.732 30.480 37.038 1.00 19.87 ? 64 ASN A CB 1
1792500 ATOM C CG . ASN A 1 64 ? 15.057 31.095 37.327 1.00 24.76 ? 64 ASN A CG 1
1793501 ATOM O OD1 . ASN A 1 64 ? 15.689 30.799 38.333 1.00 26.31 ? 64 ASN A OD1 1
1794502 ATOM N ND2 . ASN A 1 64 ? 15.501 31.977 36.459 1.00 30.55 ? 64 ASN A ND2 1
1795503 ATOM C C . ASN A 1 64 ? 12.457 28.442 36.371 1.00 16.75 ? 64 ASN A C 1
1796504 ATOM O O . ASN A 1 64 ? 11.524 28.937 35.743 1.00 17.08 ? 64 ASN A O 1
1797505 ATOM N N . PHE A 1 65 ? 12.330 27.332 37.103 1.00 14.87 ? 65 PHE A N 1
1798506 ATOM C CA . PHE A 1 65 ? 11.042 26.661 37.177 1.00 14.91 ? 65 PHE A CA 1
1799507 ATOM C CB . PHE A 1 65 ? 10.826 25.726 35.982 1.00 14.00 ? 65 PHE A CB 1
1800508 ATOM C CG . PHE A 1 65 ? 11.762 24.545 35.885 1.00 13.67 ? 65 PHE A CG 1
1801509 ATOM C CD1 . PHE A 1 65 ? 11.490 23.362 36.557 1.00 15.35 ? 65 PHE A CD1 1
1802510 ATOM C CD2 . PHE A 1 65 ? 12.912 24.615 35.122 1.00 13.98 ? 65 PHE A CD2 1
1803511 ATOM C CE1 . PHE A 1 65 ? 12.364 22.274 36.465 1.00 14.87 ? 65 PHE A CE1 1
1804512 ATOM C CE2 . PHE A 1 65 ? 13.777 23.528 35.028 1.00 13.56 ? 65 PHE A CE2 1
1805513 ATOM C CZ . PHE A 1 65 ? 13.490 22.361 35.691 1.00 13.78 ? 65 PHE A CZ 1
1806514 ATOM C C . PHE A 1 65 ? 10.876 25.880 38.474 1.00 14.51 ? 65 PHE A C 1
1807515 ATOM O O . PHE A 1 65 ? 11.862 25.521 39.111 1.00 14.39 ? 65 PHE A O 1
1808516 ATOM N N . LYS A 1 66 ? 9.610 25.645 38.832 1.00 14.23 ? 66 LYS A N 1
1809517 ATOM C CA . LYS A 1 66 ? 9.235 24.689 39.860 1.00 16.35 ? 66 LYS A CA 1
1810518 ATOM C CB . LYS A 1 66 ? 8.326 25.381 40.904 1.00 20.90 ? 66 LYS A CB 1
1811519 ATOM C CG . LYS A 1 66 ? 7.877 24.479 42.064 1.00 31.17 ? 66 LYS A CG 1
1812520 ATOM C CD . LYS A 1 66 ? 7.138 25.254 43.192 1.00 36.70 ? 66 LYS A CD 1
1813521 ATOM C CE . LYS A 1 66 ? 6.426 24.330 44.175 1.00 47.26 ? 66 LYS A CE 1
1814522 ATOM N NZ . LYS A 1 66 ? 7.369 23.422 44.886 1.00 44.52 ? 66 LYS A NZ 1
1815523 ATOM C C . LYS A 1 66 ? 8.551 23.524 39.146 1.00 15.57 ? 66 LYS A C 1
1816524 ATOM O O . LYS A 1 66 ? 7.761 23.737 38.224 1.00 14.43 ? 66 LYS A O 1
1817525 ATOM N N . VAL A 1 67 ? 8.870 22.289 39.551 1.00 14.99 ? 67 VAL A N 1
1818526 ATOM C CA . VAL A 1 67 ? 8.239 21.114 38.966 1.00 14.28 ? 67 VAL A CA 1
1819527 ATOM C CB . VAL A 1 67 ? 8.834 19.790 39.511 1.00 13.83 ? 67 VAL A CB 1
1820528 ATOM C CG1 . VAL A 1 67 ? 8.197 18.573 38.842 1.00 14.85 ? 67 VAL A CG1 1
1821529 ATOM C CG2 . VAL A 1 67 ? 10.345 19.761 39.338 1.00 13.65 ? 67 VAL A CG2 1
1822530 ATOM C C . VAL A 1 67 ? 6.730 21.219 39.197 1.00 14.01 ? 67 VAL A C 1
1823531 ATOM O O . VAL A 1 67 ? 6.296 21.600 40.285 1.00 16.66 ? 67 VAL A O 1
1824532 ATOM N N . GLY A 1 68 ? 5.947 20.954 38.139 1.00 12.91 ? 68 GLY A N 1
1825533 ATOM C CA . GLY A 1 68 ? 4.496 20.965 38.222 1.00 13.90 ? 68 GLY A CA 1
1826534 ATOM C C . GLY A 1 68 ? 3.820 22.318 38.009 1.00 14.58 ? 68 GLY A C 1
1827535 ATOM O O . GLY A 1 68 ? 2.592 22.409 38.079 1.00 15.06 ? 68 GLY A O 1
1828536 ATOM N N . GLU A 1 69 ? 4.613 23.366 37.734 1.00 14.08 ? 69 GLU A N 1
1829537 ATOM C CA . GLU A 1 69 ? 4.065 24.694 37.491 1.00 16.15 ? 69 GLU A CA 1
1830538 ATOM C CB . GLU A 1 69 ? 4.468 25.659 38.605 1.00 17.34 ? 69 GLU A CB 1
1831539 ATOM C CG . GLU A 1 69 ? 3.902 25.212 39.933 1.00 21.31 ? 69 GLU A CG 1
1832540 ATOM C CD . GLU A 1 69 ? 4.024 26.180 41.086 1.00 26.66 ? 69 GLU A CD 1
1833541 ATOM O OE1 . GLU A 1 69 ? 4.432 27.342 40.865 1.00 26.57 ? 69 GLU A OE1 1
1834542 ATOM O OE2 . GLU A 1 69 ? 3.710 25.761 42.223 1.00 29.34 ? 69 GLU A OE2 1
1835543 ATOM C C . GLU A 1 69 ? 4.532 25.206 36.132 1.00 14.96 ? 69 GLU A C 1
1836544 ATOM O O . GLU A 1 69 ? 5.706 25.115 35.799 1.00 14.66 ? 69 GLU A O 1
1837545 ATOM N N . GLU A 1 70 ? 3.586 25.708 35.339 1.00 16.75 ? 70 GLU A N 1
1838546 ATOM C CA . GLU A 1 70 ? 3.876 26.145 33.981 1.00 18.10 ? 70 GLU A CA 1
1839547 ATOM C CB . GLU A 1 70 ? 2.543 26.486 33.284 1.00 22.72 ? 70 GLU A CB 1
1840548 ATOM C CG . GLU A 1 70 ? 2.631 26.786 31.799 1.00 29.29 ? 70 GLU A CG 1
1841549 ATOM C CD . GLU A 1 70 ? 1.273 27.054 31.176 1.00 39.27 ? 70 GLU A CD 1
1842550 ATOM O OE1 . GLU A 1 70 ? 0.493 26.088 31.013 1.00 45.73 ? 70 GLU A OE1 1
1843551 ATOM O OE2 . GLU A 1 70 ? 0.972 28.237 30.895 1.00 51.43 ? 70 GLU A OE2 1
1844552 ATOM C C . GLU A 1 70 ? 4.834 27.335 33.995 1.00 16.36 ? 70 GLU A C 1
1845553 ATOM O O . GLU A 1 70 ? 4.761 28.181 34.885 1.00 16.63 ? 70 GLU A O 1
1846554 ATOM N N . PHE A 1 71 ? 5.744 27.378 33.015 1.00 14.64 ? 71 PHE A N 1
1847555 ATOM C CA . PHE A 1 71 ? 6.667 28.492 32.844 1.00 15.68 ? 71 PHE A CA 1
1848556 ATOM C CB . PHE A 1 71 ? 8.001 28.280 33.598 1.00 15.83 ? 71 PHE A CB 1
1849557 ATOM C CG . PHE A 1 71 ? 8.879 27.168 33.074 1.00 15.49 ? 71 PHE A CG 1
1850558 ATOM C CD1 . PHE A 1 71 ? 8.564 25.848 33.312 1.00 16.42 ? 71 PHE A CD1 1
1851559 ATOM C CD2 . PHE A 1 71 ? 10.018 27.449 32.341 1.00 14.68 ? 71 PHE A CD2 1
1852560 ATOM C CE1 . PHE A 1 71 ? 9.369 24.826 32.833 1.00 16.66 ? 71 PHE A CE1 1
1853561 ATOM C CE2 . PHE A 1 71 ? 10.818 26.432 31.870 1.00 14.57 ? 71 PHE A CE2 1
1854562 ATOM C CZ . PHE A 1 71 ? 10.489 25.120 32.116 1.00 13.94 ? 71 PHE A CZ 1
1855563 ATOM C C . PHE A 1 71 ? 6.917 28.684 31.353 1.00 16.99 ? 71 PHE A C 1
1856564 ATOM O O . PHE A 1 71 ? 6.473 27.876 30.540 1.00 17.10 ? 71 PHE A O 1
1857565 ATOM N N . GLU A 1 72 ? 7.593 29.785 31.009 1.00 18.66 ? 72 GLU A N 1
1858566 ATOM C CA . GLU A 1 72 ? 7.840 30.127 29.621 1.00 19.71 ? 72 GLU A CA 1
1859567 ATOM C CB . GLU A 1 72 ? 7.310 31.549 29.326 1.00 26.27 ? 72 GLU A CB 1
1860568 ATOM C CG . GLU A 1 72 ? 7.140 31.851 27.851 1.00 39.72 ? 72 GLU A CG 1
1861569 ATOM C CD . GLU A 1 72 ? 6.573 33.225 27.550 1.00 41.36 ? 72 GLU A CD 1
1862570 ATOM O OE1 . GLU A 1 72 ? 5.439 33.511 28.000 1.00 38.55 ? 72 GLU A OE1 1
1863571 ATOM O OE2 . GLU A 1 72 ? 7.259 34.010 26.854 1.00 44.79 ? 72 GLU A OE2 1
1864572 ATOM C C . GLU A 1 72 ? 9.338 29.989 29.365 1.00 18.39 ? 72 GLU A C 1
1865573 ATOM O O . GLU A 1 72 ? 10.158 30.403 30.183 1.00 20.47 ? 72 GLU A O 1
1866574 ATOM N N . GLU A 1 73 ? 9.685 29.343 28.249 1.00 16.74 ? 73 GLU A N 1
1867575 ATOM C CA . GLU A 1 73 ? 11.062 29.300 27.792 1.00 15.75 ? 73 GLU A CA 1
1868576 ATOM C CB . GLU A 1 73 ? 11.789 28.072 28.390 1.00 16.74 ? 73 GLU A CB 1
1869577 ATOM C CG . GLU A 1 73 ? 11.180 26.716 28.059 1.00 15.89 ? 73 GLU A CG 1
1870578 ATOM C CD . GLU A 1 73 ? 12.037 25.502 28.392 1.00 14.67 ? 73 GLU A CD 1
1871579 ATOM O OE1 . GLU A 1 73 ? 13.244 25.662 28.659 1.00 19.46 ? 73 GLU A OE1 1
1872580 ATOM O OE2 . GLU A 1 73 ? 11.501 24.377 28.379 1.00 13.30 ? 73 GLU A OE2 1
1873581 ATOM C C . GLU A 1 73 ? 11.066 29.340 26.262 1.00 15.17 ? 73 GLU A C 1
1874582 ATOM O O . GLU A 1 73 ? 10.147 29.887 25.653 1.00 15.46 ? 73 GLU A O 1
1875583 ATOM N N . GLN A 1 74 ? 12.138 28.823 25.662 1.00 14.68 ? 74 GLN A N 1
1876584 ATOM C CA . GLN A 1 74 ? 12.228 28.702 24.222 1.00 15.29 ? 74 GLN A CA 1
1877585 ATOM C CB . GLN A 1 74 ? 13.247 29.704 23.650 1.00 19.20 ? 74 GLN A CB 1
1878586 ATOM C CG . GLN A 1 74 ? 12.840 31.153 23.790 1.00 22.48 ? 74 GLN A CG 1
1879587 ATOM C CD . GLN A 1 74 ? 13.895 32.077 23.217 1.00 26.35 ? 74 GLN A CD 1
1880588 ATOM O OE1 . GLN A 1 74 ? 14.961 31.644 22.768 1.00 27.86 ? 74 GLN A OE1 1
1881589 ATOM N NE2 . GLN A 1 74 ? 13.615 33.364 23.210 1.00 33.42 ? 74 GLN A NE2 1
1882590 ATOM C C . GLN A 1 74 ? 12.636 27.280 23.862 1.00 14.03 ? 74 GLN A C 1
1883591 ATOM O O . GLN A 1 74 ? 13.321 26.601 24.637 1.00 13.87 ? 74 GLN A O 1
1884592 ATOM N N . THR A 1 75 ? 12.208 26.854 22.670 1.00 13.56 ? 75 THR A N 1
1885593 ATOM C CA . THR A 1 75 ? 12.731 25.653 22.044 1.00 13.97 ? 75 THR A CA 1
1886594 ATOM C CB . THR A 1 75 ? 11.947 25.319 20.773 1.00 13.30 ? 75 THR A CB 1
1887595 ATOM O OG1 . THR A 1 75 ? 12.133 26.353 19.791 1.00 15.68 ? 75 THR A OG1 1
1888596 ATOM C CG2 . THR A 1 75 ? 10.453 25.127 21.051 1.00 16.05 ? 75 THR A CG2 1
1889597 ATOM C C . THR A 1 75 ? 14.221 25.832 21.754 1.00 13.75 ? 75 THR A C 1
1890598 ATOM O O . THR A 1 75 ? 14.750 26.947 21.818 1.00 13.73 ? 75 THR A O 1
1891599 ATOM N N . VAL A 1 76 ? 14.875 24.734 21.368 1.00 16.21 ? 76 VAL A N 1
1892600 ATOM C CA . VAL A 1 76 ? 16.297 24.746 21.044 1.00 17.46 ? 76 VAL A CA 1
1893601 ATOM C CB . VAL A 1 76 ? 16.793 23.330 20.666 1.00 23.27 ? 76 VAL A CB 1
1894602 ATOM C CG1 . VAL A 1 76 ? 18.290 23.346 20.358 1.00 31.32 ? 76 VAL A CG1 1
1895603 ATOM C CG2 . VAL A 1 76 ? 16.480 22.332 21.758 1.00 36.66 ? 76 VAL A CG2 1
1896604 ATOM C C . VAL A 1 76 ? 16.636 25.734 19.932 1.00 16.61 ? 76 VAL A C 1
1897605 ATOM O O . VAL A 1 76 ? 17.691 26.366 19.961 1.00 21.40 ? 76 VAL A O 1
1898606 ATOM N N . ASP A 1 77 ? 15.716 25.896 18.974 1.00 15.35 ? 77 ASP A N 1
1899607 ATOM C CA . ASP A 1 77 ? 15.924 26.767 17.828 1.00 16.33 ? 77 ASP A CA 1
1900608 ATOM C CB . ASP A 1 77 ? 15.307 26.135 16.576 1.00 19.30 ? 77 ASP A CB 1
1901609 ATOM C CG . ASP A 1 77 ? 13.809 25.943 16.604 1.00 20.13 ? 77 ASP A CG 1
1902610 ATOM O OD1 . ASP A 1 77 ? 13.285 25.501 17.650 1.00 19.19 ? 77 ASP A OD1 1
1903611 ATOM O OD2 . ASP A 1 77 ? 13.167 26.214 15.584 1.00 22.28 ? 77 ASP A OD2 1
1904612 ATOM C C . ASP A 1 77 ? 15.387 28.180 18.056 1.00 15.75 ? 77 ASP A C 1
1905613 ATOM O O . ASP A 1 77 ? 15.366 28.985 17.129 1.00 18.52 ? 77 ASP A O 1
1906614 ATOM N N . GLY A 1 78 ? 14.931 28.455 19.287 1.00 16.01 ? 78 GLY A N 1
1907615 ATOM C CA . GLY A 1 78 ? 14.633 29.810 19.744 1.00 18.88 ? 78 GLY A CA 1
1908616 ATOM C C . GLY A 1 78 ? 13.187 30.302 19.686 1.00 21.91 ? 78 GLY A C 1
1909617 ATOM O O . GLY A 1 78 ? 12.948 31.504 19.789 1.00 24.90 ? 78 GLY A O 1
1910618 ATOM N N . ARG A 1 79 ? 12.214 29.391 19.557 1.00 19.28 ? 79 ARG A N 1
1911619 ATOM C CA . ARG A 1 79 ? 10.819 29.799 19.473 1.00 21.96 ? 79 ARG A CA 1
1912620 ATOM C CB . ARG A 1 79 ? 10.038 28.872 18.541 1.00 27.96 ? 79 ARG A CB 1
1913621 ATOM C CG . ARG A 1 79 ? 10.455 28.979 17.065 1.00 33.98 ? 79 ARG A CG 1
1914622 ATOM C CD . ARG A 1 79 ? 9.630 28.086 16.143 1.00 39.32 ? 79 ARG A CD 1
1915623 ATOM N NE . ARG A 1 79 ? 9.634 26.698 16.594 1.00 46.41 ? 79 ARG A NE 1
1916624 ATOM C CZ . ARG A 1 79 ? 10.072 25.657 15.895 1.00 48.00 ? 79 ARG A CZ 1
1917625 ATOM N NH1 . ARG A 1 79 ? 10.321 25.742 14.597 1.00 53.14 ? 79 ARG A NH1 1
1918626 ATOM N NH2 . ARG A 1 79 ? 10.240 24.491 16.513 1.00 45.88 ? 79 ARG A NH2 1
1919627 ATOM C C . ARG A 1 79 ? 10.203 29.807 20.870 1.00 19.05 ? 79 ARG A C 1
1920628 ATOM O O . ARG A 1 79 ? 10.373 28.848 21.617 1.00 16.96 ? 79 ARG A O 1
1921629 ATOM N N . PRO A 1 80 ? 9.495 30.882 21.291 1.00 18.30 ? 80 PRO A N 1
1922630 ATOM C CA . PRO A 1 80 ? 8.822 30.885 22.592 1.00 18.47 ? 80 PRO A CA 1
1923631 ATOM C CB . PRO A 1 80 ? 8.097 32.236 22.621 1.00 20.63 ? 80 PRO A CB 1
1924632 ATOM C CG . PRO A 1 80 ? 8.787 33.083 21.610 1.00 22.98 ? 80 PRO A CG 1
1925633 ATOM C CD . PRO A 1 80 ? 9.349 32.157 20.568 1.00 20.86 ? 80 PRO A CD 1
1926634 ATOM C C . PRO A 1 80 ? 7.831 29.736 22.780 1.00 17.10 ? 80 PRO A C 1
1927635 ATOM O O . PRO A 1 80 ? 7.041 29.438 21.886 1.00 17.91 ? 80 PRO A O 1
1928636 ATOM N N . CYS A 1 81 ? 7.850 29.133 23.977 1.00 16.95 ? 81 CYS A N 1
1929637 ATOM C CA . CYS A 1 81 ? 6.942 28.051 24.327 1.00 16.37 ? 81 CYS A CA 1
1930638 ATOM C CB . CYS A 1 81 ? 7.556 26.696 23.974 1.00 15.41 ? 81 CYS A CB 1
1931639 ATOM S SG . CYS A 1 81 ? 9.088 26.303 24.870 1.00 15.42 ? 81 CYS A SG 1
1932640 ATOM C C . CYS A 1 81 ? 6.548 28.100 25.800 1.00 17.79 ? 81 CYS A C 1
1933641 ATOM O O . CYS A 1 81 ? 7.242 28.721 26.608 1.00 16.51 ? 81 CYS A O 1
1934642 ATOM N N . LYS A 1 82 ? 5.424 27.442 26.109 1.00 17.99 ? 82 LYS A N 1
1935643 ATOM C CA . LYS A 1 82 ? 4.991 27.178 27.472 1.00 19.23 ? 82 LYS A CA 1
1936644 ATOM C CB . LYS A 1 82 ? 3.471 27.277 27.646 1.00 25.07 ? 82 LYS A CB 1
1937645 ATOM C CG . LYS A 1 82 ? 2.906 28.663 27.504 1.00 40.27 ? 82 LYS A CG 1
1938646 ATOM C CD . LYS A 1 82 ? 3.252 29.620 28.644 1.00 53.47 ? 82 LYS A CD 1
1939647 ATOM C CE . LYS A 1 82 ? 2.469 30.917 28.543 1.00 55.80 ? 82 LYS A CE 1
1940648 ATOM N NZ . LYS A 1 82 ? 2.746 31.830 29.686 1.00 61.97 ? 82 LYS A NZ 1
1941649 ATOM C C . LYS A 1 82 ? 5.440 25.765 27.820 1.00 17.69 ? 82 LYS A C 1
1942650 ATOM O O . LYS A 1 82 ? 5.228 24.835 27.042 1.00 18.26 ? 82 LYS A O 1
1943651 ATOM N N . SER A 1 83 ? 6.090 25.637 28.979 1.00 14.65 ? 83 SER A N 1
1944652 ATOM C CA . SER A 1 83 ? 6.680 24.384 29.406 1.00 13.61 ? 83 SER A CA 1
1945653 ATOM C CB . SER A 1 83 ? 8.194 24.530 29.491 1.00 13.40 ? 83 SER A CB 1
1946654 ATOM O OG . SER A 1 83 ? 8.783 24.567 28.197 1.00 14.69 ? 83 SER A OG 1
1947655 ATOM C C . SER A 1 83 ? 6.104 23.950 30.751 1.00 14.75 ? 83 SER A C 1
1948656 ATOM O O . SER A 1 83 ? 5.711 24.793 31.558 1.00 14.25 ? 83 SER A O 1
1949657 ATOM N N . LEU A 1 84 ? 6.044 22.626 30.950 1.00 14.82 ? 84 LEU A N 1
1950658 ATOM C CA . LEU A 1 84 ? 5.566 22.029 32.184 1.00 14.83 ? 84 LEU A CA 1
1951659 ATOM C CB . LEU A 1 84 ? 4.078 21.633 32.088 1.00 17.48 ? 84 LEU A CB 1
1952660 ATOM C CG . LEU A 1 84 ? 3.522 20.905 33.334 1.00 21.36 ? 84 LEU A CG 1
1953661 ATOM C CD1 . LEU A 1 84 ? 3.638 21.774 34.556 1.00 24.26 ? 84 LEU A CD1 1
1954662 ATOM C CD2 . LEU A 1 84 ? 2.086 20.456 33.132 1.00 26.10 ? 84 LEU A CD2 1
1955663 ATOM C C . LEU A 1 84 ? 6.436 20.805 32.452 1.00 13.33 ? 84 LEU A C 1
1956664 ATOM O O . LEU A 1 84 ? 6.455 19.872 31.647 1.00 14.33 ? 84 LEU A O 1
1957665 ATOM N N . VAL A 1 85 ? 7.170 20.848 33.569 1.00 12.01 ? 85 VAL A N 1
1958666 ATOM C CA . VAL A 1 85 ? 8.023 19.757 34.013 1.00 11.53 ? 85 VAL A CA 1
1959667 ATOM C CB . VAL A 1 85 ? 9.353 20.299 34.605 1.00 11.34 ? 85 VAL A CB 1
1960668 ATOM C CG1 . VAL A 1 85 ? 10.262 19.160 35.048 1.00 11.21 ? 85 VAL A CG1 1
1961669 ATOM C CG2 . VAL A 1 85 ? 10.081 21.192 33.611 1.00 11.60 ? 85 VAL A CG2 1
1962670 ATOM C C . VAL A 1 85 ? 7.302 18.899 35.049 1.00 12.05 ? 85 VAL A C 1
1963671 ATOM O O . VAL A 1 85 ? 6.635 19.432 35.934 1.00 12.85 ? 85 VAL A O 1
1964672 ATOM N N . LYS A 1 86 ? 7.427 17.570 34.909 1.00 13.04 ? 86 LYS A N 1
1965673 ATOM C CA . LYS A 1 86 ? 6.944 16.615 35.892 1.00 13.89 ? 86 LYS A CA 1
1966674 ATOM C CB . LYS A 1 86 ? 5.695 15.844 35.387 1.00 16.23 ? 86 LYS A CB 1
1967675 ATOM C CG . LYS A 1 86 ? 4.526 16.711 35.069 1.00 19.30 ? 86 LYS A CG 1
1968676 ATOM C CD . LYS A 1 86 ? 3.345 15.917 34.535 1.00 24.78 ? 86 LYS A CD 1
1969677 ATOM C CE . LYS A 1 86 ? 2.192 16.825 34.211 1.00 30.21 ? 86 LYS A CE 1
1970678 ATOM N NZ . LYS A 1 86 ? 0.980 16.057 33.862 1.00 37.78 ? 86 LYS A NZ 1
1971679 ATOM C C . LYS A 1 86 ? 8.035 15.597 36.217 1.00 13.21 ? 86 LYS A C 1
1972680 ATOM O O . LYS A 1 86 ? 8.921 15.341 35.402 1.00 11.99 ? 86 LYS A O 1
1973681 ATOM N N . TRP A 1 87 ? 7.941 14.989 37.404 1.00 13.02 ? 87 TRP A N 1
1974682 ATOM C CA . TRP A 1 87 ? 8.759 13.830 37.724 1.00 12.52 ? 87 TRP A CA 1
1975683 ATOM C CB . TRP A 1 87 ? 8.829 13.594 39.246 1.00 13.57 ? 87 TRP A CB 1
1976684 ATOM C CG . TRP A 1 87 ? 9.530 14.673 40.013 1.00 14.13 ? 87 TRP A CG 1
1977685 ATOM C CD1 . TRP A 1 87 ? 8.989 15.515 40.940 1.00 15.39 ? 87 TRP A CD1 1
1978686 ATOM N NE1 . TRP A 1 87 ? 9.961 16.365 41.430 1.00 15.53 ? 87 TRP A NE1 1
1979687 ATOM C CE2 . TRP A 1 87 ? 11.157 16.066 40.832 1.00 16.05 ? 87 TRP A CE2 1
1980688 ATOM C CZ2 . TRP A 1 87 ? 12.420 16.643 40.987 1.00 16.09 ? 87 TRP A CZ2 1
1981689 ATOM C CH2 . TRP A 1 87 ? 13.447 16.122 40.243 1.00 15.42 ? 87 TRP A CH2 1
1982690 ATOM C CZ3 . TRP A 1 87 ? 13.246 15.066 39.349 1.00 15.38 ? 87 TRP A CZ3 1
1983691 ATOM C CE3 . TRP A 1 87 ? 11.995 14.502 39.182 1.00 13.84 ? 87 TRP A CE3 1
1984692 ATOM C CD2 . TRP A 1 87 ? 10.923 15.005 39.930 1.00 13.84 ? 87 TRP A CD2 1
1985693 ATOM C C . TRP A 1 87 ? 8.178 12.596 37.031 1.00 12.65 ? 87 TRP A C 1
1986694 ATOM O O . TRP A 1 87 ? 7.115 12.120 37.408 1.00 15.86 ? 87 TRP A O 1
1987695 ATOM N N . GLU A 1 88 ? 8.882 12.084 36.017 1.00 12.65 ? 88 GLU A N 1
1988696 ATOM C CA . GLU A 1 88 ? 8.559 10.785 35.442 1.00 13.63 ? 88 GLU A CA 1
1989697 ATOM C CB . GLU A 1 88 ? 9.345 10.536 34.151 1.00 16.04 ? 88 GLU A CB 1
1990698 ATOM C CG . GLU A 1 88 ? 8.979 9.235 33.449 1.00 19.73 ? 88 GLU A CG 1
1991699 ATOM C CD . GLU A 1 88 ? 9.688 9.020 32.126 1.00 26.82 ? 88 GLU A CD 1
1992700 ATOM O OE1 . GLU A 1 88 ? 9.367 9.732 31.153 1.00 35.08 ? 88 GLU A OE1 1
1993701 ATOM O OE2 . GLU A 1 88 ? 10.571 8.136 32.061 1.00 30.41 ? 88 GLU A OE2 1
1994702 ATOM C C . GLU A 1 88 ? 8.870 9.711 36.480 1.00 14.35 ? 88 GLU A C 1
1995703 ATOM O O . GLU A 1 88 ? 8.085 8.794 36.677 1.00 15.51 ? 88 GLU A O 1
1996704 ATOM N N . SER A 1 89 ? 10.026 9.846 37.131 1.00 12.74 ? 89 SER A N 1
1997705 ATOM C CA . SER A 1 89 ? 10.430 8.967 38.217 1.00 13.74 ? 89 SER A CA 1
1998706 ATOM C CB . SER A 1 89 ? 11.173 7.752 37.675 1.00 15.69 ? 89 SER A CB 1
1999707 ATOM O OG . SER A 1 89 ? 12.340 8.172 36.993 1.00 16.01 ? 89 SER A OG 1
2000708 ATOM C C . SER A 1 89 ? 11.289 9.774 39.184 1.00 12.86 ? 89 SER A C 1
2001709 ATOM O O . SER A 1 89 ? 11.543 10.949 38.946 1.00 12.59 ? 89 SER A O 1
2002710 ATOM N N . GLU A 1 90 ? 11.748 9.135 40.265 1.00 13.75 ? 90 GLU A N 1
2003711 ATOM C CA . GLU A 1 90 ? 12.481 9.835 41.300 1.00 14.87 ? 90 GLU A CA 1
2004712 ATOM C CB . GLU A 1 90 ? 12.939 8.824 42.354 1.00 17.63 ? 90 GLU A CB 1
2005713 ATOM C CG . GLU A 1 90 ? 13.769 9.457 43.447 1.00 19.84 ? 90 GLU A CG 1
2006714 ATOM C CD . GLU A 1 90 ? 13.982 8.591 44.668 1.00 24.26 ? 90 GLU A CD 1
2007715 ATOM O OE1 . GLU A 1 90 ? 14.149 7.360 44.522 1.00 25.84 ? 90 GLU A OE1 1
2008716 ATOM O OE2 . GLU A 1 90 ? 13.979 9.160 45.780 1.00 29.96 ? 90 GLU A OE2 1
2009717 ATOM C C . GLU A 1 90 ? 13.660 10.644 40.759 1.00 14.89 ? 90 GLU A C 1
2010718 ATOM O O . GLU A 1 90 ? 13.917 11.753 41.231 1.00 15.88 ? 90 GLU A O 1
2011719 ATOM N N . ASN A 1 91 ? 14.373 10.097 39.761 1.00 13.24 ? 91 ASN A N 1
2012720 ATOM C CA . ASN A 1 91 ? 15.572 10.746 39.253 1.00 13.42 ? 91 ASN A CA 1
2013721 ATOM C CB . ASN A 1 91 ? 16.746 9.758 39.310 1.00 18.03 ? 91 ASN A CB 1
2014722 ATOM C CG . ASN A 1 91 ? 17.039 9.323 40.716 1.00 21.83 ? 91 ASN A CG 1
2015723 ATOM O OD1 . ASN A 1 91 ? 16.881 8.159 41.082 1.00 29.88 ? 91 ASN A OD1 1
2016724 ATOM N ND2 . ASN A 1 91 ? 17.434 10.246 41.532 1.00 24.28 ? 91 ASN A ND2 1
2017725 ATOM C C . ASN A 1 91 ? 15.470 11.298 37.835 1.00 11.77 ? 91 ASN A C 1
2018726 ATOM O O . ASN A 1 91 ? 16.491 11.647 37.247 1.00 10.08 ? 91 ASN A O 1
2019727 ATOM N N . LYS A 1 92 ? 14.245 11.402 37.305 1.00 10.89 ? 92 LYS A N 1
2020728 ATOM C CA . LYS A 1 92 ? 14.030 11.789 35.922 1.00 10.63 ? 92 LYS A CA 1
2021729 ATOM C CB . LYS A 1 92 ? 13.746 10.567 35.053 1.00 12.84 ? 92 LYS A CB 1
2022730 ATOM C CG . LYS A 1 92 ? 13.588 10.923 33.584 1.00 13.71 ? 92 LYS A CG 1
2023731 ATOM C CD . LYS A 1 92 ? 13.489 9.694 32.707 1.00 18.21 ? 92 LYS A CD 1
2024732 ATOM C CE . LYS A 1 92 ? 13.406 10.058 31.258 1.00 22.77 ? 92 LYS A CE 1
2025733 ATOM N NZ . LYS A 1 92 ? 13.067 8.872 30.426 1.00 27.01 ? 92 LYS A NZ 1
2026734 ATOM C C . LYS A 1 92 ? 12.879 12.785 35.794 1.00 11.06 ? 92 LYS A C 1
2027735 ATOM O O . LYS A 1 92 ? 11.746 12.480 36.158 1.00 12.75 ? 92 LYS A O 1
2028736 ATOM N N . MET A 1 93 ? 13.188 13.983 35.282 1.00 9.89 ? 93 MET A N 1
2029737 ATOM C CA . MET A 1 93 ? 12.170 14.980 34.996 1.00 10.74 ? 93 MET A CA 1
2030738 ATOM C CB . MET A 1 93 ? 12.579 16.381 35.502 1.00 12.88 ? 93 MET A CB 1
2031739 ATOM C CG . MET A 1 93 ? 13.823 16.924 34.903 1.00 15.80 ? 93 MET A CG 1
2032740 ATOM S SD . MET A 1 93 ? 14.257 18.554 35.593 1.00 20.76 ? 93 MET A SD 1
2033741 ATOM C CE . MET A 1 93 ? 15.214 18.096 36.951 1.00 30.01 ? 93 MET A CE 1
2034742 ATOM C C . MET A 1 93 ? 11.907 14.998 33.491 1.00 10.79 ? 93 MET A C 1
2035743 ATOM O O . MET A 1 93 ? 12.821 14.774 32.692 1.00 10.85 ? 93 MET A O 1
2036744 ATOM N N . VAL A 1 94 ? 10.639 15.222 33.127 1.00 10.85 ? 94 VAL A N 1
2037745 ATOM C CA . VAL A 1 94 ? 10.231 15.318 31.736 1.00 11.77 ? 94 VAL A CA 1
2038746 ATOM C CB . VAL A 1 94 ? 9.381 14.117 31.296 1.00 15.67 ? 94 VAL A CB 1
2039747 ATOM C CG1 . VAL A 1 94 ? 8.954 14.241 29.838 1.00 19.87 ? 94 VAL A CG1 1
2040748 ATOM C CG2 . VAL A 1 94 ? 10.123 12.813 31.535 1.00 19.34 ? 94 VAL A CG2 1
2041749 ATOM C C . VAL A 1 94 ? 9.477 16.626 31.539 1.00 11.32 ? 94 VAL A C 1
2042750 ATOM O O . VAL A 1 94 ? 8.621 16.989 32.354 1.00 12.39 ? 94 VAL A O 1
2043751 ATOM N N . CYS A 1 95 ? 9.790 17.300 30.424 1.00 11.09 ? 95 CYS A N 1
2044752 ATOM C CA . CYS A 1 95 ? 9.183 18.575 30.088 1.00 11.70 ? 95 CYS A CA 1
2045753 ATOM C CB . CYS A 1 95 ? 10.245 19.660 30.046 1.00 12.38 ? 95 CYS A CB 1
2046754 ATOM S SG . CYS A 1 95 ? 9.578 21.320 29.713 1.00 14.89 ? 95 CYS A SG 1
2047755 ATOM C C . CYS A 1 95 ? 8.445 18.498 28.756 1.00 14.11 ? 95 CYS A C 1
2048756 ATOM O O . CYS A 1 95 ? 9.051 18.148 27.738 1.00 14.85 ? 95 CYS A O 1
2049757 ATOM N N . GLU A 1 96 ? 7.156 18.859 28.780 1.00 13.72 ? 96 GLU A N 1
2050758 ATOM C CA . GLU A 1 96 ? 6.362 18.988 27.570 1.00 16.68 ? 96 GLU A CA 1
2051759 ATOM C CB . GLU A 1 96 ? 4.987 18.347 27.795 1.00 23.59 ? 96 GLU A CB 1
2052760 ATOM C CG . GLU A 1 96 ? 4.039 18.472 26.625 1.00 42.69 ? 96 GLU A CG 1
2053761 ATOM C CD . GLU A 1 96 ? 2.739 17.720 26.834 1.00 61.92 ? 96 GLU A CD 1
2054762 ATOM O OE1 . GLU A 1 96 ? 2.060 17.990 27.852 1.00 67.10 ? 96 GLU A OE1 1
2055763 ATOM O OE2 . GLU A 1 96 ? 2.398 16.862 25.986 1.00 64.30 ? 96 GLU A OE2 1
2056764 ATOM C C . GLU A 1 96 ? 6.271 20.467 27.201 1.00 15.54 ? 96 GLU A C 1
2057765 ATOM O O . GLU A 1 96 ? 6.050 21.314 28.067 1.00 15.11 ? 96 GLU A O 1
2058766 ATOM N N . GLN A 1 97 ? 6.466 20.767 25.909 1.00 15.13 ? 97 GLN A N 1
2059767 ATOM C CA . GLN A 1 97 ? 6.502 22.137 25.428 1.00 15.27 ? 97 GLN A CA 1
2060768 ATOM C CB . GLN A 1 97 ? 7.836 22.452 24.741 1.00 16.07 ? 97 GLN A CB 1
2061769 ATOM C CG . GLN A 1 97 ? 9.063 22.313 25.643 1.00 16.22 ? 97 GLN A CG 1
2062770 ATOM C CD . GLN A 1 97 ? 10.350 22.628 24.921 1.00 18.01 ? 97 GLN A CD 1
2063771 ATOM O OE1 . GLN A 1 97 ? 10.528 22.332 23.730 1.00 16.75 ? 97 GLN A OE1 1
2064772 ATOM N NE2 . GLN A 1 97 ? 11.278 23.275 25.615 1.00 18.18 ? 97 GLN A NE2 1
2065773 ATOM C C . GLN A 1 97 ? 5.349 22.370 24.458 1.00 18.68 ? 97 GLN A C 1
2066774 ATOM O O . GLN A 1 97 ? 5.008 21.483 23.676 1.00 19.06 ? 97 GLN A O 1
2067775 ATOM N N . LYS A 1 98 ? 4.753 23.565 24.526 1.00 18.17 ? 98 LYS A N 1
2068776 ATOM C CA . LYS A 1 98 ? 3.705 23.974 23.603 1.00 20.89 ? 98 LYS A CA 1
2069777 ATOM C CB . LYS A 1 98 ? 2.333 24.012 24.301 1.00 29.41 ? 98 LYS A CB 1
2070778 ATOM C CG . LYS A 1 98 ? 1.576 22.686 24.310 1.00 44.00 ? 98 LYS A CG 1
2071779 ATOM C CD . LYS A 1 98 ? 1.866 21.810 25.516 1.00 60.14 ? 98 LYS A CD 1
2072780 ATOM C CE . LYS A 1 98 ? 1.172 20.470 25.426 1.00 75.86 ? 98 LYS A CE 1
2073781 ATOM N NZ . LYS A 1 98 ? 1.772 19.601 24.374 1.00 86.95 ? 98 LYS A NZ 1
2074782 ATOM C C . LYS A 1 98 ? 4.035 25.351 23.036 1.00 19.57 ? 98 LYS A C 1
2075783 ATOM O O . LYS A 1 98 ? 4.291 26.282 23.791 1.00 19.94 ? 98 LYS A O 1
2076784 ATOM N N . LEU A 1 99 ? 4.020 25.480 21.704 1.00 19.04 ? 99 LEU A N 1
2077785 ATOM C CA . LEU A 1 99 ? 4.335 26.746 21.057 1.00 21.65 ? 99 LEU A CA 1
2078786 ATOM C CB . LEU A 1 99 ? 4.381 26.581 19.536 1.00 23.75 ? 99 LEU A CB 1
2079787 ATOM C CG . LEU A 1 99 ? 5.530 25.752 19.000 1.00 25.18 ? 99 LEU A CG 1
2080788 ATOM C CD1 . LEU A 1 99 ? 5.359 25.497 17.512 1.00 29.71 ? 99 LEU A CD1 1
2081789 ATOM C CD2 . LEU A 1 99 ? 6.841 26.427 19.258 1.00 26.83 ? 99 LEU A CD2 1
2082790 ATOM C C . LEU A 1 99 ? 3.299 27.815 21.385 1.00 25.82 ? 99 LEU A C 1
2083791 ATOM O O . LEU A 1 99 ? 2.101 27.539 21.367 1.00 25.33 ? 99 LEU A O 1
2084792 ATOM N N . LEU A 1 100 ? 3.778 29.030 21.675 1.00 25.76 ? 100 LEU A N 1
2085793 ATOM C CA . LEU A 1 100 ? 2.904 30.161 21.942 1.00 28.30 ? 100 LEU A CA 1
2086794 ATOM C CB . LEU A 1 100 ? 3.711 31.319 22.533 1.00 28.78 ? 100 LEU A CB 1
2087795 ATOM C CG . LEU A 1 100 ? 4.268 31.103 23.918 1.00 31.86 ? 100 LEU A CG 1
2088796 ATOM C CD1 . LEU A 1 100 ? 4.810 32.401 24.487 1.00 37.29 ? 100 LEU A CD1 1
2089797 ATOM C CD2 . LEU A 1 100 ? 3.243 30.552 24.819 1.00 35.49 ? 100 LEU A CD2 1
2090798 ATOM C C . LEU A 1 100 ? 2.220 30.644 20.669 1.00 35.84 ? 100 LEU A C 1
2091799 ATOM O O . LEU A 1 100 ? 1.035 30.963 20.681 1.00 35.33 ? 100 LEU A O 1
2092800 ATOM N N . LYS A 1 101 ? 3.007 30.720 19.593 1.00 39.57 ? 101 LYS A N 1
2093801 ATOM C CA . LYS A 1 101 ? 2.520 31.125 18.287 1.00 45.82 ? 101 LYS A CA 1
2094802 ATOM C CB . LYS A 1 101 ? 3.059 32.508 17.903 1.00 49.34 ? 101 LYS A CB 1
2095803 ATOM C CG . LYS A 1 101 ? 2.471 33.659 18.699 1.00 58.96 ? 101 LYS A CG 1
2096804 ATOM C CD . LYS A 1 101 ? 2.910 35.028 18.172 1.00 64.37 ? 101 LYS A CD 1
2097805 ATOM C CE . LYS A 1 101 ? 2.490 35.272 16.741 1.00 69.19 ? 101 LYS A CE 1
2098806 ATOM N NZ . LYS A 1 101 ? 2.609 36.706 16.368 1.00 75.49 ? 101 LYS A NZ 1
2099807 ATOM C C . LYS A 1 101 ? 2.956 30.111 17.235 1.00 38.91 ? 101 LYS A C 1
2100808 ATOM O O . LYS A 1 101 ? 4.036 29.535 17.336 1.00 39.99 ? 101 LYS A O 1
2101809 ATOM N N . GLY A 1 102 ? 2.099 29.918 16.227 1.00 39.15 ? 102 GLY A N 1
2102810 ATOM C CA . GLY A 1 102 ? 2.435 29.124 15.060 1.00 37.95 ? 102 GLY A CA 1
2103811 ATOM C C . GLY A 1 102 ? 2.392 27.621 15.319 1.00 39.06 ? 102 GLY A C 1
2104812 ATOM O O . GLY A 1 102 ? 1.835 27.164 16.315 1.00 35.69 ? 102 GLY A O 1
2105813 ATOM N N . GLU A 1 103 ? 2.979 26.869 14.385 1.00 38.15 ? 103 GLU A N 1
2106814 ATOM C CA . GLU A 1 103 ? 3.025 25.422 14.476 1.00 41.12 ? 103 GLU A CA 1
2107815 ATOM C CB . GLU A 1 103 ? 1.972 24.790 13.567 1.00 51.03 ? 103 GLU A CB 1
2108816 ATOM C CG . GLU A 1 103 ? 0.562 25.083 14.028 1.00 60.66 ? 103 GLU A CG 1
2109817 ATOM C CD . GLU A 1 103 ? -0.508 24.344 13.261 1.00 77.22 ? 103 GLU A CD 1
2110818 ATOM O OE1 . GLU A 1 103 ? -0.169 23.668 12.262 1.00 93.28 ? 103 GLU A OE1 1
2111819 ATOM O OE2 . GLU A 1 103 ? -1.688 24.434 13.665 1.00 94.92 ? 103 GLU A OE2 1
2112820 ATOM C C . GLU A 1 103 ? 4.421 24.925 14.124 1.00 32.57 ? 103 GLU A C 1
2113821 ATOM O O . GLU A 1 103 ? 5.273 25.675 13.649 1.00 32.64 ? 103 GLU A O 1
2114822 ATOM N N . GLY A 1 104 ? 4.645 23.644 14.393 1.00 30.13 ? 104 GLY A N 1
2115823 ATOM C CA . GLY A 1 104 ? 5.953 23.056 14.190 1.00 26.90 ? 104 GLY A CA 1
2116824 ATOM C C . GLY A 1 104 ? 6.010 21.694 14.858 1.00 24.27 ? 104 GLY A C 1
2117825 ATOM O O . GLY A 1 104 ? 5.019 21.244 15.426 1.00 24.96 ? 104 GLY A O 1
2118826 ATOM N N . PRO A 1 105 ? 7.171 21.010 14.790 1.00 21.58 ? 105 PRO A N 1
2119827 ATOM C CA . PRO A 1 105 ? 7.348 19.716 15.446 1.00 21.16 ? 105 PRO A CA 1
2120828 ATOM C CB . PRO A 1 105 ? 8.843 19.433 15.261 1.00 22.72 ? 105 PRO A CB 1
2121829 ATOM C CG . PRO A 1 105 ? 9.242 20.250 14.058 1.00 22.77 ? 105 PRO A CG 1
2122830 ATOM C CD . PRO A 1 105 ? 8.369 21.465 14.069 1.00 22.89 ? 105 PRO A CD 1
2123831 ATOM C C . PRO A 1 105 ? 6.981 19.752 16.926 1.00 19.87 ? 105 PRO A C 1
2124832 ATOM O O . PRO A 1 105 ? 7.129 20.782 17.583 1.00 19.93 ? 105 PRO A O 1
2125833 ATOM N N . LYS A 1 106 ? 6.531 18.606 17.441 1.00 19.17 ? 106 LYS A N 1
2126834 ATOM C CA . LYS A 1 106 ? 6.299 18.443 18.864 1.00 18.91 ? 106 LYS A CA 1
2127835 ATOM C CB . LYS A 1 106 ? 5.443 17.208 19.149 1.00 23.88 ? 106 LYS A CB 1
2128836 ATOM C CG . LYS A 1 106 ? 5.121 17.041 20.632 1.00 32.29 ? 106 LYS A CG 1
2129837 ATOM C CD . LYS A 1 106 ? 4.091 15.969 20.936 1.00 38.44 ? 106 LYS A CD 1
2130838 ATOM C CE . LYS A 1 106 ? 3.892 15.824 22.430 1.00 50.59 ? 106 LYS A CE 1
2131839 ATOM N NZ . LYS A 1 106 ? 3.023 14.669 22.764 1.00 56.36 ? 106 LYS A NZ 1
2132840 ATOM C C . LYS A 1 106 ? 7.661 18.315 19.540 1.00 15.93 ? 106 LYS A C 1
2133841 ATOM O O . LYS A 1 106 ? 8.475 17.494 19.127 1.00 14.89 ? 106 LYS A O 1
2134842 ATOM N N . THR A 1 107 ? 7.912 19.141 20.560 1.00 14.87 ? 107 THR A N 1
2135843 ATOM C CA . THR A 1 107 ? 9.197 19.117 21.237 1.00 12.21 ? 107 THR A CA 1
2136844 ATOM C CB . THR A 1 107 ? 9.947 20.431 21.028 1.00 13.25 ? 107 THR A CB 1
2137845 ATOM O OG1 . THR A 1 107 ? 9.208 21.506 21.632 1.00 12.59 ? 107 THR A OG1 1
2138846 ATOM C CG2 . THR A 1 107 ? 10.193 20.725 19.549 1.00 15.19 ? 107 THR A CG2 1
2139847 ATOM C C . THR A 1 107 ? 9.035 18.816 22.722 1.00 13.13 ? 107 THR A C 1
2140848 ATOM O O . THR A 1 107 ? 8.016 19.145 23.328 1.00 11.70 ? 107 THR A O 1
2141849 ATOM N N . SER A 1 108 ? 10.071 18.190 23.289 1.00 10.93 ? 108 SER A N 1
2142850 ATOM C CA . SER A 1 108 ? 10.161 17.923 24.712 1.00 12.26 ? 108 SER A CA 1
2143851 ATOM C CB . SER A 1 108 ? 9.425 16.632 25.060 1.00 15.77 ? 108 SER A CB 1
2144852 ATOM O OG . SER A 1 108 ? 9.935 15.562 24.277 1.00 19.20 ? 108 SER A OG 1
2145853 ATOM C C . SER A 1 108 ? 11.634 17.828 25.104 1.00 10.97 ? 108 SER A C 1
2146854 ATOM O O . SER A 1 108 ? 12.525 17.790 24.242 1.00 10.88 ? 108 SER A O 1
2147855 ATOM N N . TRP A 1 109 ? 11.889 17.769 26.411 1.00 10.94 ? 109 TRP A N 1
2148856 ATOM C CA . TRP A 1 109 ? 13.219 17.441 26.907 1.00 10.26 ? 109 TRP A CA 1
2149857 ATOM C CB . TRP A 1 109 ? 14.138 18.675 27.077 1.00 10.40 ? 109 TRP A CB 1
2150858 ATOM C CG . TRP A 1 109 ? 13.679 19.796 27.994 1.00 10.77 ? 109 TRP A CG 1
2151859 ATOM C CD1 . TRP A 1 109 ? 13.169 20.998 27.614 1.00 12.30 ? 109 TRP A CD1 1
2152860 ATOM N NE1 . TRP A 1 109 ? 12.902 21.777 28.719 1.00 11.26 ? 109 TRP A NE1 1
2153861 ATOM C CE2 . TRP A 1 109 ? 13.275 21.092 29.851 1.00 11.02 ? 109 TRP A CE2 1
2154862 ATOM C CZ2 . TRP A 1 109 ? 13.205 21.459 31.195 1.00 11.49 ? 109 TRP A CZ2 1
2155863 ATOM C CH2 . TRP A 1 109 ? 13.645 20.547 32.126 1.00 12.56 ? 109 TRP A CH2 1
2156864 ATOM C CZ3 . TRP A 1 109 ? 14.123 19.294 31.751 1.00 12.36 ? 109 TRP A CZ3 1
2157865 ATOM C CE3 . TRP A 1 109 ? 14.202 18.929 30.416 1.00 11.73 ? 109 TRP A CE3 1
2158866 ATOM C CD2 . TRP A 1 109 ? 13.762 19.836 29.438 1.00 12.31 ? 109 TRP A CD2 1
2159867 ATOM C C . TRP A 1 109 ? 13.074 16.641 28.195 1.00 10.57 ? 109 TRP A C 1
2160868 ATOM O O . TRP A 1 109 ? 12.016 16.672 28.820 1.00 11.56 ? 109 TRP A O 1
2161869 ATOM N N . THR A 1 110 ? 14.130 15.894 28.534 1.00 9.01 ? 110 THR A N 1
2162870 ATOM C CA . THR A 1 110 ? 14.207 15.163 29.787 1.00 7.84 ? 110 THR A CA 1
2163871 ATOM C CB . THR A 1 110 ? 13.903 13.643 29.596 1.00 9.64 ? 110 THR A CB 1
2164872 ATOM O OG1 . THR A 1 110 ? 14.996 13.006 28.920 1.00 11.07 ? 110 THR A OG1 1
2165873 ATOM C CG2 . THR A 1 110 ? 12.612 13.403 28.843 1.00 10.23 ? 110 THR A CG2 1
2166874 ATOM C C . THR A 1 110 ? 15.591 15.391 30.388 1.00 8.10 ? 110 THR A C 1
2167875 ATOM O O . THR A 1 110 ? 16.573 15.586 29.662 1.00 8.75 ? 110 THR A O 1
2168876 ATOM N N . ARG A 1 111 ? 15.666 15.338 31.726 1.00 7.71 ? 111 ARG A N 1
2169877 ATOM C CA . ARG A 1 111 ? 16.938 15.331 32.425 1.00 8.52 ? 111 ARG A CA 1
2170878 ATOM C CB . ARG A 1 111 ? 17.290 16.706 33.050 1.00 10.14 ? 111 ARG A CB 1
2171879 ATOM C CG . ARG A 1 111 ? 17.697 17.774 32.031 1.00 10.72 ? 111 ARG A CG 1
2172880 ATOM C CD . ARG A 1 111 ? 18.092 19.078 32.716 1.00 12.28 ? 111 ARG A CD 1
2173881 ATOM N NE . ARG A 1 111 ? 18.779 19.989 31.804 1.00 15.01 ? 111 ARG A NE 1
2174882 ATOM C CZ . ARG A 1 111 ? 18.183 20.806 30.946 1.00 14.70 ? 111 ARG A CZ 1
2175883 ATOM N NH1 . ARG A 1 111 ? 16.868 20.900 30.878 1.00 15.74 ? 111 ARG A NH1 1
2176884 ATOM N NH2 . ARG A 1 111 ? 18.930 21.561 30.144 1.00 16.72 ? 111 ARG A NH2 1
2177885 ATOM C C . ARG A 1 111 ? 16.885 14.263 33.509 1.00 9.52 ? 111 ARG A C 1
2178886 ATOM O O . ARG A 1 111 ? 15.905 14.182 34.255 1.00 9.27 ? 111 ARG A O 1
2179887 ATOM N N . GLU A 1 112 ? 17.927 13.427 33.557 1.00 9.48 ? 112 GLU A N 1
2180888 ATOM C CA . GLU A 1 112 ? 17.961 12.331 34.514 1.00 12.36 ? 112 GLU A CA 1
2181889 ATOM C CB . GLU A 1 112 ? 17.454 11.040 33.893 1.00 18.59 ? 112 GLU A CB 1
2182890 ATOM C CG . GLU A 1 112 ? 18.245 10.483 32.746 1.00 25.94 ? 112 GLU A CG 1
2183891 ATOM C CD . GLU A 1 112 ? 17.518 9.351 32.039 1.00 39.02 ? 112 GLU A CD 1
2184892 ATOM O OE1 . GLU A 1 112 ? 17.186 8.342 32.716 1.00 26.07 ? 112 GLU A OE1 1
2185893 ATOM O OE2 . GLU A 1 112 ? 17.272 9.489 30.812 1.00 27.92 ? 112 GLU A OE2 1
2186894 ATOM C C . GLU A 1 112 ? 19.353 12.135 35.103 1.00 12.52 ? 112 GLU A C 1
2187895 ATOM O O . GLU A 1 112 ? 20.358 12.296 34.416 1.00 10.51 ? 112 GLU A O 1
2188896 ATOM N N . LEU A 1 113 ? 19.388 11.815 36.397 1.00 11.64 ? 113 LEU A N 1
2189897 ATOM C CA . LEU A 1 113 ? 20.628 11.483 37.082 1.00 13.94 ? 113 LEU A CA 1
2190898 ATOM C CB . LEU A 1 113 ? 20.597 11.928 38.536 1.00 18.79 ? 113 LEU A CB 1
2191899 ATOM C CG . LEU A 1 113 ? 20.685 13.388 38.802 1.00 21.01 ? 113 LEU A CG 1
2192900 ATOM C CD1 . LEU A 1 113 ? 20.558 13.667 40.281 1.00 24.85 ? 113 LEU A CD1 1
2193901 ATOM C CD2 . LEU A 1 113 ? 22.023 13.961 38.303 1.00 23.13 ? 113 LEU A CD2 1
2194902 ATOM C C . LEU A 1 113 ? 20.773 9.968 37.051 1.00 14.83 ? 113 LEU A C 1
2195903 ATOM O O . LEU A 1 113 ? 19.872 9.255 37.493 1.00 16.30 ? 113 LEU A O 1
2196904 ATOM N N . THR A 1 114 ? 21.901 9.480 36.526 1.00 11.43 ? 114 THR A N 1
2197905 ATOM C CA . THR A 1 114 ? 22.137 8.048 36.421 1.00 13.31 ? 114 THR A CA 1
2198906 ATOM C CB . THR A 1 114 ? 22.963 7.745 35.168 1.00 15.86 ? 114 THR A CB 1
2199907 ATOM O OG1 . THR A 1 114 ? 24.202 8.429 35.268 1.00 18.17 ? 114 THR A OG1 1
2200908 ATOM C CG2 . THR A 1 114 ? 22.267 8.139 33.898 1.00 23.56 ? 114 THR A CG2 1
2201909 ATOM C C . THR A 1 114 ? 22.825 7.513 37.673 1.00 14.00 ? 114 THR A C 1
2202910 ATOM O O . THR A 1 114 ? 23.328 8.274 38.500 1.00 14.36 ? 114 THR A O 1
2203911 ATOM N N . ASN A 1 115 ? 22.869 6.185 37.773 1.00 13.98 ? 115 ASN A N 1
2204912 ATOM C CA . ASN A 1 115 ? 23.378 5.499 38.944 1.00 17.98 ? 115 ASN A CA 1
2205913 ATOM C CB . ASN A 1 115 ? 23.067 4.011 38.845 1.00 22.38 ? 115 ASN A CB 1
2206914 ATOM C CG . ASN A 1 115 ? 21.585 3.727 38.935 1.00 38.90 ? 115 ASN A CG 1
2207915 ATOM O OD1 . ASN A 1 115 ? 20.859 4.363 39.710 1.00 42.49 ? 115 ASN A OD1 1
2208916 ATOM N ND2 . ASN A 1 115 ? 21.096 2.779 38.136 1.00 54.00 ? 115 ASN A ND2 1
2209917 ATOM C C . ASN A 1 115 ? 24.874 5.714 39.152 1.00 14.79 ? 115 ASN A C 1
2210918 ATOM O O . ASN A 1 115 ? 25.352 5.577 40.272 1.00 16.80 ? 115 ASN A O 1
2211919 ATOM N N . ASP A 1 116 ? 25.578 6.092 38.077 1.00 13.78 ? 116 ASP A N 1
2212920 ATOM C CA . ASP A 1 116 ? 27.010 6.361 38.117 1.00 14.36 ? 116 ASP A CA 1
2213921 ATOM C CB . ASP A 1 116 ? 27.659 5.926 36.795 1.00 14.86 ? 116 ASP A CB 1
2214922 ATOM C CG . ASP A 1 116 ? 27.081 6.541 35.518 1.00 18.53 ? 116 ASP A CG 1
2215923 ATOM O OD1 . ASP A 1 116 ? 26.199 7.401 35.618 1.00 29.00 ? 116 ASP A OD1 1
2216924 ATOM O OD2 . ASP A 1 116 ? 27.513 6.150 34.438 1.00 29.22 ? 116 ASP A OD2 1
2217925 ATOM C C . ASP A 1 116 ? 27.395 7.813 38.396 1.00 13.41 ? 116 ASP A C 1
2218926 ATOM O O . ASP A 1 116 ? 28.581 8.133 38.421 1.00 14.71 ? 116 ASP A O 1
2219927 ATOM N N . GLY A 1 117 ? 26.400 8.676 38.608 1.00 13.03 ? 117 GLY A N 1
2220928 ATOM C CA . GLY A 1 117 ? 26.626 10.063 38.977 1.00 12.49 ? 117 GLY A CA 1
2221929 ATOM C C . GLY A 1 117 ? 26.629 11.050 37.815 1.00 12.12 ? 117 GLY A C 1
2222930 ATOM O O . GLY A 1 117 ? 26.928 12.224 38.016 1.00 14.04 ? 117 GLY A O 1
2223931 ATOM N N . GLU A 1 118 ? 26.256 10.577 36.619 1.00 11.16 ? 118 GLU A N 1
2224932 ATOM C CA . GLU A 1 118 ? 26.212 11.418 35.436 1.00 10.04 ? 118 GLU A CA 1
2225933 ATOM C CB . GLU A 1 118 ? 26.736 10.636 34.221 1.00 11.01 ? 118 GLU A CB 1
2226934 ATOM C CG . GLU A 1 118 ? 28.193 10.240 34.393 1.00 12.25 ? 118 GLU A CG 1
2227935 ATOM C CD . GLU A 1 118 ? 28.774 9.362 33.308 1.00 15.12 ? 118 GLU A CD 1
2228936 ATOM O OE1 . GLU A 1 118 ? 28.052 9.032 32.335 1.00 14.58 ? 118 GLU A OE1 1
2229937 ATOM O OE2 . GLU A 1 118 ? 29.965 8.991 33.456 1.00 18.86 ? 118 GLU A OE2 1
2230938 ATOM C C . GLU A 1 118 ? 24.799 11.953 35.203 1.00 10.08 ? 118 GLU A C 1
2231939 ATOM O O . GLU A 1 118 ? 23.856 11.590 35.906 1.00 11.14 ? 118 GLU A O 1
2232940 ATOM N N . LEU A 1 119 ? 24.687 12.850 34.223 1.00 10.33 ? 119 LEU A N 1
2233941 ATOM C CA . LEU A 1 119 ? 23.436 13.505 33.879 1.00 9.78 ? 119 LEU A CA 1
2234942 ATOM C CB . LEU A 1 119 ? 23.537 15.005 34.188 1.00 11.63 ? 119 LEU A CB 1
2235943 ATOM C CG . LEU A 1 119 ? 22.374 15.910 33.825 1.00 16.73 ? 119 LEU A CG 1
2236944 ATOM C CD1 . LEU A 1 119 ? 21.202 15.653 34.668 1.00 21.13 ? 119 LEU A CD1 1
2237945 ATOM C CD2 . LEU A 1 119 ? 22.771 17.396 33.965 1.00 21.57 ? 119 LEU A CD2 1
2238946 ATOM C C . LEU A 1 119 ? 23.190 13.259 32.395 1.00 11.25 ? 119 LEU A C 1
2239947 ATOM O O . LEU A 1 119 ? 24.085 13.518 31.578 1.00 10.90 ? 119 LEU A O 1
2240948 ATOM N N . ILE A 1 120 ? 22.006 12.710 32.078 1.00 8.25 ? 120 ILE A N 1
2241949 ATOM C CA . ILE A 1 120 ? 21.584 12.564 30.691 1.00 8.41 ? 120 ILE A CA 1
2242950 ATOM C CB . ILE A 1 120 ? 21.073 11.144 30.382 1.00 9.66 ? 120 ILE A CB 1
2243951 ATOM C CG1 . ILE A 1 120 ? 22.127 10.073 30.690 1.00 12.34 ? 120 ILE A CG1 1
2244952 ATOM C CG2 . ILE A 1 120 ? 20.546 11.075 28.921 1.00 10.64 ? 120 ILE A CG2 1
2245953 ATOM C CD1 . ILE A 1 120 ? 21.591 8.640 30.538 1.00 14.72 ? 120 ILE A CD1 1
2246954 ATOM C C . ILE A 1 120 ? 20.509 13.599 30.364 1.00 8.54 ? 120 ILE A C 1
2247955 ATOM O O . ILE A 1 120 ? 19.466 13.657 31.024 1.00 8.46 ? 120 ILE A O 1
2248956 ATOM N N . LEU A 1 121 ? 20.771 14.404 29.326 1.00 7.34 ? 121 LEU A N 1
2249957 ATOM C CA . LEU A 1 121 ? 19.773 15.280 28.741 1.00 7.74 ? 121 LEU A CA 1
2250958 ATOM C CB . LEU A 1 121 ? 20.382 16.652 28.465 1.00 9.05 ? 121 LEU A CB 1
2251959 ATOM C CG . LEU A 1 121 ? 19.600 17.601 27.562 1.00 11.19 ? 121 LEU A CG 1
2252960 ATOM C CD1 . LEU A 1 121 ? 18.360 18.132 28.258 1.00 12.37 ? 121 LEU A CD1 1
2253961 ATOM C CD2 . LEU A 1 121 ? 20.509 18.749 27.106 1.00 12.10 ? 121 LEU A CD2 1
2254962 ATOM C C . LEU A 1 121 ? 19.299 14.658 27.432 1.00 8.24 ? 121 LEU A C 1
2255963 ATOM O O . LEU A 1 121 ? 20.126 14.285 26.609 1.00 9.50 ? 121 LEU A O 1
2256964 ATOM N N . THR A 1 122 ? 17.981 14.546 27.241 1.00 8.30 ? 122 THR A N 1
2257965 ATOM C CA . THR A 1 122 ? 17.465 14.244 25.917 1.00 9.26 ? 122 THR A CA 1
2258966 ATOM C CB . THR A 1 122 ? 16.719 12.891 25.797 1.00 12.24 ? 122 THR A CB 1
2259967 ATOM O OG1 . THR A 1 122 ? 15.393 13.002 26.280 1.00 12.93 ? 122 THR A OG1 1
2260968 ATOM C CG2 . THR A 1 122 ? 17.439 11.779 26.516 1.00 10.99 ? 122 THR A CG2 1
2261969 ATOM C C . THR A 1 122 ? 16.613 15.420 25.463 1.00 10.00 ? 122 THR A C 1
2262970 ATOM O O . THR A 1 122 ? 15.958 16.087 26.273 1.00 10.00 ? 122 THR A O 1
2263971 ATOM N N . MET A 1 123 ? 16.676 15.668 24.152 1.00 9.31 ? 123 MET A N 1
2264972 ATOM C CA . MET A 1 123 ? 15.838 16.653 23.493 1.00 9.45 ? 123 MET A CA 1
2265973 ATOM C CB . MET A 1 123 ? 16.693 17.853 23.049 1.00 10.32 ? 123 MET A CB 1
2266974 ATOM C CG . MET A 1 123 ? 17.285 18.622 24.221 1.00 12.17 ? 123 MET A CG 1
2267975 ATOM S SD . MET A 1 123 ? 18.290 20.048 23.693 1.00 17.40 ? 123 MET A SD 1
2268976 ATOM C CE . MET A 1 123 ? 19.742 19.276 23.144 1.00 18.37 ? 123 MET A CE 1
2269977 ATOM C C . MET A 1 123 ? 15.194 15.952 22.304 1.00 11.30 ? 123 MET A C 1
2270978 ATOM O O . MET A 1 123 ? 15.892 15.287 21.535 1.00 9.97 ? 123 MET A O 1
2271979 ATOM N N . THR A 1 124 ? 13.875 16.130 22.148 1.00 9.78 ? 124 THR A N 1
2272980 ATOM C CA . THR A 1 124 ? 13.128 15.462 21.099 1.00 10.89 ? 124 THR A CA 1
2273981 ATOM C CB . THR A 1 124 ? 12.113 14.486 21.711 1.00 13.40 ? 124 THR A CB 1
2274982 ATOM O OG1 . THR A 1 124 ? 12.822 13.513 22.524 1.00 13.00 ? 124 THR A OG1 1
2275983 ATOM C CG2 . THR A 1 124 ? 11.326 13.794 20.685 1.00 16.59 ? 124 THR A CG2 1
2276984 ATOM C C . THR A 1 124 ? 12.424 16.479 20.207 1.00 11.65 ? 124 THR A C 1
2277985 ATOM O O . THR A 1 124 ? 11.943 17.502 20.691 1.00 11.43 ? 124 THR A O 1
2278986 ATOM N N . ALA A 1 125 ? 12.374 16.168 18.905 1.00 11.84 ? 125 ALA A N 1
2279987 ATOM C CA . ALA A 1 125 ? 11.554 16.889 17.946 1.00 12.88 ? 125 ALA A CA 1
2280988 ATOM C CB . ALA A 1 125 ? 12.360 17.870 17.129 1.00 14.10 ? 125 ALA A CB 1
2281989 ATOM C C . ALA A 1 125 ? 10.936 15.829 17.047 1.00 13.37 ? 125 ALA A C 1
2282990 ATOM O O . ALA A 1 125 ? 11.660 15.118 16.343 1.00 13.30 ? 125 ALA A O 1
2283991 ATOM N N . ASP A 1 126 ? 9.606 15.738 17.107 1.00 15.26 ? 126 ASP A N 1
2284992 ATOM C CA . ASP A 1 126 ? 8.854 14.662 16.486 1.00 18.93 ? 126 ASP A CA 1
2285993 ATOM C CB . ASP A 1 126 ? 8.711 14.926 14.984 1.00 20.67 ? 126 ASP A CB 1
2286994 ATOM C CG . ASP A 1 126 ? 7.695 16.026 14.679 1.00 25.96 ? 126 ASP A CG 1
2287995 ATOM O OD1 . ASP A 1 126 ? 6.786 16.256 15.525 1.00 24.33 ? 126 ASP A OD1 1
2288996 ATOM O OD2 . ASP A 1 126 ? 7.818 16.671 13.615 1.00 27.13 ? 126 ASP A OD2 1
2289997 ATOM C C . ASP A 1 126 ? 9.500 13.330 16.865 1.00 19.43 ? 126 ASP A C 1
2290998 ATOM O O . ASP A 1 126 ? 9.500 12.987 18.043 1.00 20.42 ? 126 ASP A O 1
2291999 ATOM N N . ASP A 1 127 ? 10.057 12.593 15.893 1.00 20.54 ? 127 ASP A N 1
22921000 ATOM C CA . ASP A 1 127 ? 10.622 11.274 16.166 1.00 24.65 ? 127 ASP A CA 1
22931001 ATOM C CB . ASP A 1 127 ? 10.420 10.365 14.940 1.00 29.16 ? 127 ASP A CB 1
22941002 ATOM C CG . ASP A 1 127 ? 8.992 9.907 14.744 1.00 45.51 ? 127 ASP A CG 1
22951003 ATOM O OD1 . ASP A 1 127 ? 8.170 10.088 15.680 1.00 49.31 ? 127 ASP A OD1 1
22961004 ATOM O OD2 . ASP A 1 127 ? 8.688 9.373 13.657 1.00 62.43 ? 127 ASP A OD2 1
22971005 ATOM C C . ASP A 1 127 ? 12.106 11.264 16.543 1.00 21.48 ? 127 ASP A C 1
22981006 ATOM O O . ASP A 1 127 ? 12.608 10.253 17.034 1.00 25.40 ? 127 ASP A O 1
22991007 ATOM N N . VAL A 1 128 ? 12.787 12.394 16.335 1.00 16.29 ? 128 VAL A N 1
23001008 ATOM C CA . VAL A 1 128 ? 14.232 12.474 16.456 1.00 13.74 ? 128 VAL A CA 1
23011009 ATOM C CB . VAL A 1 128 ? 14.769 13.471 15.438 1.00 14.58 ? 128 VAL A CB 1
23021010 ATOM C CG1 . VAL A 1 128 ? 16.236 13.758 15.652 1.00 17.15 ? 128 VAL A CG1 1
23031011 ATOM C CG2 . VAL A 1 128 ? 14.501 12.973 14.019 1.00 17.51 ? 128 VAL A CG2 1
23041012 ATOM C C . VAL A 1 128 ? 14.631 12.838 17.880 1.00 12.89 ? 128 VAL A C 1
23051013 ATOM O O . VAL A 1 128 ? 14.076 13.772 18.469 1.00 11.37 ? 128 VAL A O 1
23061014 ATOM N N . VAL A 1 129 ? 15.600 12.088 18.410 1.00 10.87 ? 129 VAL A N 1
23071015 ATOM C CA . VAL A 1 129 ? 16.080 12.259 19.768 1.00 10.73 ? 129 VAL A CA 1
23081016 ATOM C CB . VAL A 1 129 ? 15.768 10.991 20.574 1.00 12.45 ? 129 VAL A CB 1
23091017 ATOM C CG1 . VAL A 1 129 ? 16.199 11.168 22.030 1.00 15.41 ? 129 VAL A CG1 1
23101018 ATOM C CG2 . VAL A 1 129 ? 14.290 10.602 20.436 1.00 14.37 ? 129 VAL A CG2 1
23111019 ATOM C C . VAL A 1 129 ? 17.577 12.546 19.825 1.00 10.01 ? 129 VAL A C 1
23121020 ATOM O O . VAL A 1 129 ? 18.383 11.797 19.273 1.00 12.03 ? 129 VAL A O 1
23131021 ATOM N N . CYS A 1 130 ? 17.935 13.628 20.526 1.00 10.16 ? 130 CYS A N 1
23141022 ATOM C CA . CYS A 1 130 ? 19.315 13.988 20.780 1.00 8.97 ? 130 CYS A CA 1
23151023 ATOM C CB . CYS A 1 130 ? 19.513 15.475 20.493 1.00 10.44 ? 130 CYS A CB 1
23161024 ATOM S SG . CYS A 1 130 ? 21.062 16.171 21.118 1.00 11.49 ? 130 CYS A SG 1
23171025 ATOM C C . CYS A 1 130 ? 19.652 13.627 22.225 1.00 9.50 ? 130 CYS A C 1
23181026 ATOM O O . CYS A 1 130 ? 18.897 13.970 23.138 1.00 9.52 ? 130 CYS A O 1
23191027 ATOM N N . THR A 1 131 ? 20.774 12.917 22.413 1.00 9.03 ? 131 THR A N 1
23201028 ATOM C CA . THR A 1 131 ? 21.211 12.470 23.727 1.00 8.17 ? 131 THR A CA 1
23211029 ATOM C CB . THR A 1 131 ? 21.361 10.940 23.763 1.00 9.76 ? 131 THR A CB 1
23221030 ATOM O OG1 . THR A 1 131 ? 20.164 10.332 23.310 1.00 10.64 ? 131 THR A OG1 1
23231031 ATOM C CG2 . THR A 1 131 ? 21.684 10.441 25.135 1.00 10.21 ? 131 THR A CG2 1
23241032 ATOM C C . THR A 1 131 ? 22.542 13.129 24.067 1.00 8.93 ? 131 THR A C 1
23251033 ATOM O O . THR A 1 131 ? 23.477 13.067 23.270 1.00 9.07 ? 131 THR A O 1
23261034 ATOM N N . ARG A 1 132 ? 22.605 13.782 25.238 1.00 8.20 ? 132 ARG A N 1
23271035 ATOM C CA . ARG A 1 132 ? 23.811 14.456 25.694 1.00 11.02 ? 132 ARG A CA 1
23281036 ATOM C CB . ARG A 1 132 ? 23.646 15.985 25.682 1.00 14.91 ? 132 ARG A CB 1
23291037 ATOM C CG . ARG A 1 132 ? 22.858 16.541 24.509 1.00 26.12 ? 132 ARG A CG 1
23301038 ATOM C CD . ARG A 1 132 ? 23.687 17.305 23.564 1.00 27.99 ? 132 ARG A CD 1
23311039 ATOM N NE . ARG A 1 132 ? 24.056 18.624 24.063 1.00 19.65 ? 132 ARG A NE 1
23321040 ATOM C CZ . ARG A 1 132 ? 24.983 19.378 23.482 1.00 16.76 ? 132 ARG A CZ 1
23331041 ATOM N NH1 . ARG A 1 132 ? 25.534 19.025 22.334 1.00 19.17 ? 132 ARG A NH1 1
23341042 ATOM N NH2 . ARG A 1 132 ? 25.373 20.503 24.068 1.00 15.37 ? 132 ARG A NH2 1
23351043 ATOM C C . ARG A 1 132 ? 24.098 13.984 27.113 1.00 9.89 ? 132 ARG A C 1
23361044 ATOM O O . ARG A 1 132 ? 23.180 13.897 27.934 1.00 11.30 ? 132 ARG A O 1
23371045 ATOM N N . VAL A 1 133 ? 25.372 13.689 27.393 1.00 7.67 ? 133 VAL A N 1
23381046 ATOM C CA . VAL A 1 133 ? 25.758 13.140 28.680 1.00 9.17 ? 133 VAL A CA 1
23391047 ATOM C CB . VAL A 1 133 ? 26.304 11.712 28.567 1.00 9.92 ? 133 VAL A CB 1
23401048 ATOM C CG1 . VAL A 1 133 ? 26.630 11.136 29.936 1.00 11.53 ? 133 VAL A CG1 1
23411049 ATOM C CG2 . VAL A 1 133 ? 25.328 10.813 27.815 1.00 11.31 ? 133 VAL A CG2 1
23421050 ATOM C C . VAL A 1 133 ? 26.798 14.064 29.305 1.00 8.06 ? 133 VAL A C 1
23431051 ATOM O O . VAL A 1 133 ? 27.740 14.470 28.635 1.00 8.20 ? 133 VAL A O 1
23441052 ATOM N N . TYR A 1 134 ? 26.622 14.350 30.600 1.00 7.49 ? 134 TYR A N 1
23451053 ATOM C CA . TYR A 1 134 ? 27.500 15.247 31.328 1.00 8.07 ? 134 TYR A CA 1
23461054 ATOM C CB . TYR A 1 134 ? 26.805 16.557 31.721 1.00 9.27 ? 134 TYR A CB 1
23471055 ATOM C CG . TYR A 1 134 ? 26.100 17.265 30.600 1.00 10.94 ? 134 TYR A CG 1
23481056 ATOM C CD1 . TYR A 1 134 ? 24.887 16.792 30.114 1.00 12.54 ? 134 TYR A CD1 1
23491057 ATOM C CD2 . TYR A 1 134 ? 26.630 18.416 30.029 1.00 14.33 ? 134 TYR A CD2 1
23501058 ATOM C CE1 . TYR A 1 134 ? 24.229 17.425 29.086 1.00 14.95 ? 134 TYR A CE1 1
23511059 ATOM C CE2 . TYR A 1 134 ? 25.958 19.077 28.991 1.00 14.50 ? 134 TYR A CE2 1
23521060 ATOM C CZ . TYR A 1 134 ? 24.761 18.561 28.523 1.00 15.94 ? 134 TYR A CZ 1
23531061 ATOM O OH . TYR A 1 134 ? 24.015 19.108 27.506 1.00 22.65 ? 134 TYR A OH 1
23541062 ATOM C C . TYR A 1 134 ? 27.991 14.612 32.621 1.00 8.79 ? 134 TYR A C 1
23551063 ATOM O O . TYR A 1 134 ? 27.336 13.721 33.163 1.00 7.66 ? 134 TYR A O 1
23561064 ATOM N N . VAL A 1 135 ? 29.112 15.149 33.119 1.00 9.92 ? 135 VAL A N 1
23571065 ATOM C CA . VAL A 1 135 ? 29.672 14.802 34.414 1.00 10.85 ? 135 VAL A CA 1
23581066 ATOM C CB . VAL A 1 135 ? 30.867 13.830 34.272 1.00 13.21 ? 135 VAL A CB 1
23591067 ATOM C CG1 . VAL A 1 135 ? 32.078 14.518 33.654 1.00 14.48 ? 135 VAL A CG1 1
23601068 ATOM C CG2 . VAL A 1 135 ? 31.235 13.196 35.614 1.00 16.46 ? 135 VAL A CG2 1
23611069 ATOM C C . VAL A 1 135 ? 30.060 16.128 35.064 1.00 10.95 ? 135 VAL A C 1
23621070 ATOM O O . VAL A 1 135 ? 30.359 17.100 34.371 1.00 10.06 ? 135 VAL A O 1
23631071 ATOM N N . ARG A 1 136 ? 30.049 16.182 36.395 1.00 11.64 ? 136 ARG A N 1
23641072 ATOM C CA . ARG A 1 136 ? 30.445 17.410 37.066 1.00 12.53 ? 136 ARG A CA 1
23651073 ATOM C CB . ARG A 1 136 ? 30.170 17.370 38.553 1.00 14.40 ? 136 ARG A CB 1
23661074 ATOM C CG . ARG A 1 136 ? 28.673 17.401 38.900 1.00 15.49 ? 136 ARG A CG 1
23671075 ATOM C CD . ARG A 1 136 ? 28.474 17.503 40.401 1.00 18.26 ? 136 ARG A CD 1
23681076 ATOM N NE . ARG A 1 136 ? 27.077 17.404 40.796 1.00 20.84 ? 136 ARG A NE 1
23691077 ATOM C CZ . ARG A 1 136 ? 26.405 16.271 40.942 1.00 26.89 ? 136 ARG A CZ 1
23701078 ATOM N NH1 . ARG A 1 136 ? 26.949 15.100 40.652 1.00 30.22 ? 136 ARG A NH1 1
23711079 ATOM N NH2 . ARG A 1 136 ? 25.155 16.316 41.390 1.00 25.35 ? 136 ARG A NH2 1
23721080 ATOM C C . ARG A 1 136 ? 31.922 17.681 36.816 1.00 13.45 ? 136 ARG A C 1
23731081 ATOM O O . ARG A 1 136 ? 32.735 16.756 36.795 1.00 13.03 ? 136 ARG A O 1
23741082 ATOM N N . GLU A 1 137 ? 32.249 18.973 36.674 1.00 15.84 ? 137 GLU A N 1
23751083 ATOM C CA . GLU A 1 137 ? 33.608 19.422 36.416 1.00 19.93 ? 137 GLU A CA 1
23761084 ATOM C CB . GLU A 1 137 ? 33.657 20.949 36.276 1.00 22.53 ? 137 GLU A CB 1
23771085 ATOM C CG . GLU A 1 137 ? 33.185 21.471 34.945 1.00 33.63 ? 137 GLU A CG 1
23781086 ATOM C CD . GLU A 1 137 ? 33.271 22.982 34.817 1.00 44.56 ? 137 GLU A CD 1
23791087 ATOM O OE1 . GLU A 1 137 ? 33.621 23.652 35.817 1.00 43.03 ? 137 GLU A OE1 1
23801088 ATOM O OE2 . GLU A 1 137 ? 32.996 23.496 33.709 1.00 62.02 ? 137 GLU A OE2 1
23811089 ATOM C C . GLU A 1 137 ? 34.552 19.056 37.517 1.00 22.96 ? 137 GLU A C 1
23821090 ATOM O O . GLU A 1 137 ? 34.224 19.246 38.687 1.00 20.40 ? 137 GLU A O 1
23831091 ATOM O OXT . GLU A 1 137 ? 35.680 18.631 37.244 1.00 26.40 ? 137 GLU A OXT 1
23841092 HETATM C C1 . REA B 2 . ? 21.991 29.785 16.697 1.00 17.82 ? 200 REA A C1 1
23851093 HETATM C C2 . REA B 2 . ? 20.990 30.477 15.765 1.00 20.31 ? 200 REA A C2 1
23861094 HETATM C C3 . REA B 2 . ? 20.298 29.535 14.844 1.00 17.46 ? 200 REA A C3 1
23871095 HETATM C C4 . REA B 2 . ? 19.583 28.449 15.628 1.00 16.95 ? 200 REA A C4 1
23881096 HETATM C C5 . REA B 2 . ? 20.445 27.793 16.664 1.00 15.44 ? 200 REA A C5 1
23891097 HETATM C C6 . REA B 2 . ? 21.483 28.454 17.227 1.00 13.94 ? 200 REA A C6 1
23901098 HETATM C C7 . REA B 2 . ? 22.282 27.891 18.302 1.00 15.07 ? 200 REA A C7 1
23911099 HETATM C C8 . REA B 2 . ? 21.888 27.041 19.281 1.00 12.78 ? 200 REA A C8 1
23921100 HETATM C C9 . REA B 2 . ? 22.721 26.474 20.257 1.00 12.56 ? 200 REA A C9 1
23931101 HETATM C C10 . REA B 2 . ? 22.201 25.597 21.223 1.00 13.35 ? 200 REA A C10 1
23941102 HETATM C C11 . REA B 2 . ? 22.862 24.936 22.249 1.00 12.66 ? 200 REA A C11 1
23951103 HETATM C C12 . REA B 2 . ? 22.321 24.007 23.106 1.00 13.96 ? 200 REA A C12 1
23961104 HETATM C C13 . REA B 2 . ? 22.920 23.314 24.176 1.00 12.73 ? 200 REA A C13 1
23971105 HETATM C C14 . REA B 2 . ? 22.147 22.474 24.951 1.00 14.07 ? 200 REA A C14 1
23981106 HETATM C C15 . REA B 2 . ? 22.580 21.651 26.108 1.00 16.38 ? 200 REA A C15 1
23991107 HETATM C C16 . REA B 2 . ? 22.270 30.746 17.864 1.00 22.29 ? 200 REA A C16 1
24001108 HETATM C C17 . REA B 2 . ? 23.311 29.581 15.931 1.00 17.07 ? 200 REA A C17 1
24011109 HETATM C C18 . REA B 2 . ? 20.034 26.378 16.965 1.00 17.45 ? 200 REA A C18 1
24021110 HETATM C C19 . REA B 2 . ? 24.195 26.711 20.265 1.00 12.79 ? 200 REA A C19 1
24031111 HETATM C C20 . REA B 2 . ? 24.325 23.643 24.499 1.00 14.50 ? 200 REA A C20 1
24041112 HETATM O O1 . REA B 2 . ? 23.706 21.159 26.108 1.00 17.64 ? 200 REA A O1 1
24051113 HETATM O O2 . REA B 2 . ? 21.851 21.679 27.082 1.00 14.21 ? 200 REA A O2 1
24061114 HETATM O O . HOH C 3 . ? 21.763 19.795 31.173 1.00 19.51 ? 300 HOH A O 1
24071115 HETATM O O . HOH C 3 . ? 7.613 26.972 37.072 1.00 16.86 ? 301 HOH A O 1
24081116 HETATM O O . HOH C 3 . ? 22.950 27.659 25.122 1.00 21.71 ? 302 HOH A O 1
24091117 HETATM O O . HOH C 3 . ? 30.697 27.415 22.930 1.00 15.67 ? 303 HOH A O 1
24101118 HETATM O O . HOH C 3 . ? 29.940 20.909 40.373 1.00 20.53 ? 304 HOH A O 1
24111119 HETATM O O . HOH C 3 . ? 31.430 21.098 28.412 1.00 17.81 ? 305 HOH A O 1
24121120 HETATM O O . HOH C 3 . ? 19.419 26.564 30.241 1.00 12.22 ? 306 HOH A O 1
24131121 HETATM O O . HOH C 3 . ? 19.070 26.773 22.824 1.00 29.17 ? 307 HOH A O 1
24141122 HETATM O O . HOH C 3 . ? 16.101 22.470 28.626 1.00 33.13 ? 308 HOH A O 1
24151123 HETATM O O . HOH C 3 . ? 21.848 22.000 29.779 1.00 14.89 ? 309 HOH A O 1
24161124 HETATM O O . HOH C 3 . ? 13.144 22.230 22.060 1.00 23.32 ? 310 HOH A O 1
24171125 HETATM O O . HOH C 3 . ? 30.129 22.867 12.552 1.00 33.32 ? 311 HOH A O 1
24181126 HETATM O O . HOH C 3 . ? 7.348 23.015 35.524 1.00 12.73 ? 312 HOH A O 1
24191127 HETATM O O . HOH C 3 . ? 7.289 23.004 20.032 1.00 31.88 ? 313 HOH A O 1
24201128 HETATM O O . HOH C 3 . ? 18.076 24.702 29.123 1.00 25.01 ? 314 HOH A O 1
24211129 HETATM O O . HOH C 3 . ? 37.045 16.599 38.632 1.00 23.09 ? 315 HOH A O 1
24221130 HETATM O O . HOH C 3 . ? 28.716 7.455 30.024 1.00 18.52 ? 316 HOH A O 1
24231131 HETATM O O . HOH C 3 . ? 13.145 14.376 25.173 1.00 23.00 ? 317 HOH A O 1
24241132 HETATM O O . HOH C 3 . ? 6.141 9.796 39.181 1.00 19.55 ? 318 HOH A O 1
24251133 HETATM O O . HOH C 3 . ? 19.582 10.374 13.112 1.00 30.23 ? 319 HOH A O 1
24261134 HETATM O O . HOH C 3 . ? 25.376 11.045 16.638 1.00 19.83 ? 320 HOH A O 1
24271135 HETATM O O . HOH C 3 . ? 25.218 34.341 18.254 1.00 12.92 ? 321 HOH A O 1
24281136 HETATM O O . HOH C 3 . ? 23.487 10.711 14.473 1.00 13.89 ? 322 HOH A O 1
24291137 HETATM O O . HOH C 3 . ? 17.092 12.218 30.323 1.00 14.03 ? 323 HOH A O 1
24301138 HETATM O O . HOH C 3 . ? 27.757 12.073 42.037 1.00 23.26 ? 324 HOH A O 1
24311139 HETATM O O . HOH C 3 . ? 30.109 12.550 21.413 1.00 30.99 ? 325 HOH A O 1
24321140 HETATM O O . HOH C 3 . ? 25.737 15.515 18.470 1.00 13.63 ? 326 HOH A O 1
24331141 HETATM O O . HOH C 3 . ? 4.569 21.780 18.437 1.00 35.00 ? 327 HOH A O 1
24341142 HETATM O O . HOH C 3 . ? 8.134 23.281 17.554 1.00 28.67 ? 328 HOH A O 1
24351143 HETATM O O . HOH C 3 . ? 13.412 28.679 14.556 1.00 42.08 ? 329 HOH A O 1
24361144 HETATM O O . HOH C 3 . ? 10.413 18.706 10.303 1.00 35.58 ? 330 HOH A O 1
24371145 HETATM O O . HOH C 3 . ? 10.697 13.517 25.923 1.00 32.59 ? 331 HOH A O 1
24381146 HETATM O O . HOH C 3 . ? 5.177 17.363 31.549 1.00 37.40 ? 332 HOH A O 1
24391147 HETATM O O . HOH C 3 . ? 0.745 25.860 36.357 1.00 27.59 ? 333 HOH A O 1
24401148 HETATM O O . HOH C 3 . ? 3.183 28.912 36.963 1.00 37.23 ? 334 HOH A O 1
24411149 HETATM O O . HOH C 3 . ? 6.339 28.605 39.122 1.00 32.60 ? 335 HOH A O 1
24421150 HETATM O O . HOH C 3 . ? 12.491 30.518 32.666 1.00 32.00 ? 336 HOH A O 1
24431151 HETATM O O . HOH C 3 . ? 14.906 30.286 27.671 1.00 38.00 ? 337 HOH A O 1
24441152 HETATM O O . HOH C 3 . ? 17.389 32.791 28.789 1.00 25.17 ? 338 HOH A O 1
24451153 HETATM O O . HOH C 3 . ? 29.453 25.862 34.697 1.00 30.87 ? 339 HOH A O 1
24461154 HETATM O O . HOH C 3 . ? 30.304 23.860 33.499 1.00 27.90 ? 340 HOH A O 1
24471155 HETATM O O . HOH C 3 . ? 30.214 28.444 16.166 1.00 20.38 ? 342 HOH A O 1
24481156 HETATM O O . HOH C 3 . ? 19.680 23.552 27.036 1.00 24.07 ? 343 HOH A O 1
24491157 HETATM O O . HOH C 3 . ? 18.216 25.037 24.399 1.00 45.96 ? 344 HOH A O 1
24501158 HETATM O O . HOH C 3 . ? 14.151 24.156 25.249 1.00 22.51 ? 345 HOH A O 1
24511159 HETATM O O . HOH C 3 . ? 15.061 27.996 26.925 1.00 26.92 ? 346 HOH A O 1
24521160 HETATM O O . HOH C 3 . ? 29.890 5.157 27.019 1.00 30.20 ? 350 HOH A O 1
24531161 HETATM O O . HOH C 3 . ? 14.126 5.410 42.766 1.00 30.55 ? 351 HOH A O 1
24541162 HETATM O O . HOH C 3 . ? 8.873 5.714 35.416 1.00 38.27 ? 352 HOH A O 1
24551163 HETATM O O . HOH C 3 . ? 14.525 29.102 39.937 1.00 31.13 ? 353 HOH A O 1
24561164 HETATM O O . HOH C 3 . ? 17.368 20.121 47.156 1.00 34.92 ? 354 HOH A O 1
24571165 HETATM O O . HOH C 3 . ? 25.316 15.987 15.315 1.00 26.18 ? 357 HOH A O 1
24581166 HETATM O O . HOH C 3 . ? 27.244 17.440 18.043 1.00 32.39 ? 358 HOH A O 1
24591167 HETATM O O . HOH C 3 . ? 27.565 19.854 19.346 1.00 32.04 ? 359 HOH A O 1
24601168 HETATM O O . HOH C 3 . ? 11.374 8.712 18.916 1.00 26.87 ? 360 HOH A O 1
24611169 HETATM O O . HOH C 3 . ? 16.232 27.235 24.326 1.00 29.59 ? 361 HOH A O 1
24621170 HETATM O O . HOH C 3 . ? 21.843 27.886 4.468 1.00 32.73 ? 362 HOH A O 1
24631171 HETATM O O . HOH C 3 . ? 11.591 6.865 34.577 1.00 35.36 ? 363 HOH A O 1
24641172 HETATM O O . HOH C 3 . ? 13.208 4.636 36.800 1.00 38.83 ? 364 HOH A O 1
24651173 HETATM O O . HOH C 3 . ? 23.122 9.158 41.175 1.00 36.26 ? 365 HOH A O 1
24661174 HETATM O O . HOH C 3 . ? 21.142 12.691 43.959 1.00 36.88 ? 366 HOH A O 1
24671175 HETATM O O . HOH C 3 . ? 12.072 13.374 42.636 1.00 24.48 ? 367 HOH A O 1
24681176 HETATM O O . HOH C 3 . ? 30.845 17.790 22.310 1.00 36.27 ? 369 HOH A O 1
24691177 HETATM O O . HOH C 3 . ? 25.471 10.771 9.660 1.00 42.41 ? 371 HOH A O 1
24701178 HETATM O O . HOH C 3 . ? 26.578 13.514 16.542 1.00 48.29 ? 372 HOH A O 1
24711179 HETATM O O . HOH C 3 . ? 26.884 17.086 12.962 1.00 37.88 ? 373 HOH A O 1
24721180 HETATM O O . HOH C 3 . ? 16.978 28.523 9.405 1.00 20.93 ? 375 HOH A O 1
24731181 HETATM O O . HOH C 3 . ? 16.665 32.292 11.315 1.00 21.54 ? 376 HOH A O 1
24741182 HETATM O O . HOH C 3 . ? 5.938 30.507 19.704 1.00 31.27 ? 377 HOH A O 1
24751183 HETATM O O . HOH C 3 . ? 9.007 15.971 11.492 1.00 40.08 ? 378 HOH A O 1
24761184 HETATM O O . HOH C 3 . ? 7.863 13.935 19.946 1.00 34.62 ? 379 HOH A O 1
24771185 HETATM O O . HOH C 3 . ? 11.943 11.011 23.375 1.00 30.32 ? 380 HOH A O 1
24781186 HETATM O O . HOH C 3 . ? 5.541 15.907 25.608 1.00 47.34 ? 381 HOH A O 1
24791187 HETATM O O . HOH C 3 . ? 33.718 18.863 27.669 1.00 33.62 ? 383 HOH A O 1
24801188 HETATM O O . HOH C 3 . ? 17.070 26.934 42.731 1.00 36.17 ? 384 HOH A O 1
24811189 HETATM O O . HOH C 3 . ? 25.455 24.899 41.287 1.00 36.08 ? 385 HOH A O 1
24821190 HETATM O O . HOH C 3 . ? 31.283 7.516 31.898 1.00 22.50 ? 386 HOH A O 1
24831191 HETATM O O . HOH C 3 . ? 15.167 27.585 7.684 1.00 35.29 ? 388 HOH A O 1
24841192 HETATM O O . HOH C 3 . ? 3.023 23.145 20.177 1.00 31.29 ? 389 HOH A O 1
24851193 HETATM O O . HOH C 3 . ? 3.421 22.717 28.311 1.00 36.04 ? 390 HOH A O 1
24861194 HETATM O O . HOH C 3 . ? 13.626 19.692 21.460 1.00 30.78 ? 391 HOH A O 1
24871195 HETATM O O . HOH C 3 . ? 26.649 28.428 32.268 1.00 29.36 ? 392 HOH A O 1
24881196 HETATM O O . HOH C 3 . ? 20.442 26.163 25.771 1.00 25.71 ? 393 HOH A O 1
24891197 HETATM O O . HOH C 3 . ? 24.009 13.973 42.862 1.00 40.72 ? 395 HOH A O 1
24901198 HETATM O O . HOH C 3 . ? 11.583 12.542 44.984 1.00 38.51 ? 396 HOH A O 1
24911199 HETATM O O . HOH C 3 . ? 1.946 27.630 43.390 1.00 43.83 ? 397 HOH A O 1
24921200 HETATM O O . HOH C 3 . ? 32.165 22.939 40.339 1.00 46.76 ? 398 HOH A O 1
24931201 HETATM O O . HOH C 3 . ? 32.443 20.099 40.063 1.00 28.79 ? 399 HOH A O 1
2494#
2495_symmetry.entry_id 1CBS
2496_symmetry.space_group_name_H-M 'P 21 21 21'
2497_symmetry.Int_Tables_number 19
2498#
2499_cell.entry_id 1CBS
2500_cell.length_a 45.650
2501_cell.length_b 47.560
2502_cell.length_c 77.610
2503_cell.angle_alpha 90.00
2504_cell.angle_beta 90.00
2505_cell.angle_gamma 90.00
2506_cell.Z_PDB 0
2507#
2508loop_
2509_chem_comp.id
2510_chem_comp.name
2511_chem_comp.formula
2512_chem_comp.formula_weight
2513_chem_comp.mon_nstd_flag
2514_chem_comp.type
2515ALA ALANINE ? 89.094025 y 'L-peptide linking'
2516ARG ARGININE ? 175.211945 y 'L-peptide linking'
2517ASN ASPARAGINE ? 132.118988 y 'L-peptide linking'
2518ASP ASPARTICACID ? 132.094986 y 'L-peptide linking'
2519CYS CYSTEINE ? 121.154022 y 'L-peptide linking'
2520GLN GLUTAMINE ? 146.145950 y 'L-peptide linking'
2521GLU GLUTAMICACID ? 146.121964 y 'L-peptide linking'
2522GLY GLYCINE ? 75.067017 y 'peptide linking'
2523HOH WATER 88() 18.014999 . non-polymer
2524ILE ISOLEUCINE ? 131.175018 y 'L-peptide linking'
2525LEU LEUCINE ? 131.175018 y 'L-peptide linking'
2526LYS LYSINE ? 147.197937 y 'L-peptide linking'
2527MET METHIONINE ? 149.207947 y 'L-peptide linking'
2528PHE PHENYLALANINE ? 165.191956 y 'L-peptide linking'
2529PRO PROLINE ? 114.124031 y 'L-peptide linking'
2530REA RETINOICACID ? 299.433899 . non-polymer
2531SER SERINE ? 105.093025 y 'L-peptide linking'
2532THR THREONINE ? 119.120033 y 'L-peptide linking'
2533TRP TRYPTOPHAN ? 204.228958 y 'L-peptide linking'
2534TYR TYROSINE ? 181.190948 y 'L-peptide linking'
2535VAL VALINE ? 117.148041 y 'L-peptide linking'
2536#
2537loop_
2538_pdbx_nonpoly_scheme.asym_id
2539_pdbx_nonpoly_scheme.ndb_seq_num
2540_pdbx_nonpoly_scheme.entity_id
2541_pdbx_nonpoly_scheme.mon_id
2542_pdbx_nonpoly_scheme.pdb_seq_num
2543_pdbx_nonpoly_scheme.auth_seq_num
2544_pdbx_nonpoly_scheme.pdb_mon_id
2545_pdbx_nonpoly_scheme.auth_mon_id
2546_pdbx_nonpoly_scheme.pdb_strand_id
2547_pdbx_nonpoly_scheme.pdb_ins_code
2548B 1 2 REA 200 1 REA REA A .
2549C 1 3 HOH 300 1 HOH HOH A .
2550C 2 3 HOH 301 2 HOH HOH A .
2551C 3 3 HOH 302 3 HOH HOH A .
2552C 4 3 HOH 303 4 HOH HOH A .
2553C 5 3 HOH 304 5 HOH HOH A .
2554C 6 3 HOH 305 6 HOH HOH A .
2555C 7 3 HOH 306 7 HOH HOH A .
2556C 8 3 HOH 307 8 HOH HOH A .
2557C 9 3 HOH 308 9 HOH HOH A .
2558C 10 3 HOH 309 10 HOH HOH A .
2559C 11 3 HOH 310 11 HOH HOH A .
2560C 12 3 HOH 311 12 HOH HOH A .
2561C 13 3 HOH 312 13 HOH HOH A .
2562C 14 3 HOH 313 14 HOH HOH A .
2563C 15 3 HOH 314 15 HOH HOH A .
2564C 16 3 HOH 315 16 HOH HOH A .
2565C 17 3 HOH 316 17 HOH HOH A .
2566C 18 3 HOH 317 18 HOH HOH A .
2567C 19 3 HOH 318 19 HOH HOH A .
2568C 20 3 HOH 319 20 HOH HOH A .
2569C 21 3 HOH 320 21 HOH HOH A .
2570C 22 3 HOH 321 22 HOH HOH A .
2571C 23 3 HOH 322 23 HOH HOH A .
2572C 24 3 HOH 323 24 HOH HOH A .
2573C 25 3 HOH 324 25 HOH HOH A .
2574C 26 3 HOH 325 26 HOH HOH A .
2575C 27 3 HOH 326 27 HOH HOH A .
2576C 28 3 HOH 327 28 HOH HOH A .
2577C 29 3 HOH 328 29 HOH HOH A .
2578C 30 3 HOH 329 30 HOH HOH A .
2579C 31 3 HOH 330 31 HOH HOH A .
2580C 32 3 HOH 331 32 HOH HOH A .
2581C 33 3 HOH 332 33 HOH HOH A .
2582C 34 3 HOH 333 34 HOH HOH A .
2583C 35 3 HOH 334 35 HOH HOH A .
2584C 36 3 HOH 335 36 HOH HOH A .
2585C 37 3 HOH 336 37 HOH HOH A .
2586C 38 3 HOH 337 38 HOH HOH A .
2587C 39 3 HOH 338 39 HOH HOH A .
2588C 40 3 HOH 339 40 HOH HOH A .
2589C 41 3 HOH 340 41 HOH HOH A .
2590C 42 3 HOH 342 42 HOH HOH A .
2591C 43 3 HOH 343 43 HOH HOH A .
2592C 44 3 HOH 344 44 HOH HOH A .
2593C 45 3 HOH 345 45 HOH HOH A .
2594C 46 3 HOH 346 46 HOH HOH A .
2595C 47 3 HOH 350 47 HOH HOH A .
2596C 48 3 HOH 351 48 HOH HOH A .
2597C 49 3 HOH 352 49 HOH HOH A .
2598C 50 3 HOH 353 50 HOH HOH A .
2599C 51 3 HOH 354 51 HOH HOH A .
2600C 52 3 HOH 357 52 HOH HOH A .
2601C 53 3 HOH 358 53 HOH HOH A .
2602C 54 3 HOH 359 54 HOH HOH A .
2603C 55 3 HOH 360 55 HOH HOH A .
2604C 56 3 HOH 361 56 HOH HOH A .
2605C 57 3 HOH 362 57 HOH HOH A .
2606C 58 3 HOH 363 58 HOH HOH A .
2607C 59 3 HOH 364 59 HOH HOH A .
2608C 60 3 HOH 365 60 HOH HOH A .
2609C 61 3 HOH 366 61 HOH HOH A .
2610C 62 3 HOH 367 62 HOH HOH A .
2611C 63 3 HOH 369 63 HOH HOH A .
2612C 64 3 HOH 371 64 HOH HOH A .
2613C 65 3 HOH 372 65 HOH HOH A .
2614C 66 3 HOH 373 66 HOH HOH A .
2615C 67 3 HOH 375 67 HOH HOH A .
2616C 68 3 HOH 376 68 HOH HOH A .
2617C 69 3 HOH 377 69 HOH HOH A .
2618C 70 3 HOH 378 70 HOH HOH A .
2619C 71 3 HOH 379 71 HOH HOH A .
2620C 72 3 HOH 380 72 HOH HOH A .
2621C 73 3 HOH 381 73 HOH HOH A .
2622C 74 3 HOH 383 74 HOH HOH A .
2623C 75 3 HOH 384 75 HOH HOH A .
2624C 76 3 HOH 385 76 HOH HOH A .
2625C 77 3 HOH 386 77 HOH HOH A .
2626C 78 3 HOH 388 78 HOH HOH A .
2627C 79 3 HOH 389 79 HOH HOH A .
2628C 80 3 HOH 390 80 HOH HOH A .
2629C 81 3 HOH 391 81 HOH HOH A .
2630C 82 3 HOH 392 82 HOH HOH A .
2631C 83 3 HOH 393 83 HOH HOH A .
2632C 84 3 HOH 395 84 HOH HOH A .
2633C 85 3 HOH 396 85 HOH HOH A .
2634C 86 3 HOH 397 86 HOH HOH A .
2635C 87 3 HOH 398 87 HOH HOH A .
2636C 88 3 HOH 399 88 HOH HOH A .
2637#
2638loop_
2639_entity_poly_seq.entity_id
2640_entity_poly_seq.num
2641_entity_poly_seq.mon_id
2642_entity_poly_seq.hetero
26431 1 PRO n
26441 2 ASN n
26451 3 PHE n
26461 4 SER n
26471 5 GLY n
26481 6 ASN n
26491 7 TRP n
26501 8 LYS n
26511 9 ILE n
26521 10 ILE n
26531 11 ARG n
26541 12 SER n
26551 13 GLU n
26561 14 ASN n
26571 15 PHE n
26581 16 GLU n
26591 17 GLU n
26601 18 LEU n
26611 19 LEU n
26621 20 LYS n
26631 21 VAL n
26641 22 LEU n
26651 23 GLY n
26661 24 VAL n
26671 25 ASN n
26681 26 VAL n
26691 27 MET n
26701 28 LEU n
26711 29 ARG n
26721 30 LYS n
26731 31 ILE n
26741 32 ALA n
26751 33 VAL n
26761 34 ALA n
26771 35 ALA n
26781 36 ALA n
26791 37 SER n
26801 38 LYS n
26811 39 PRO n
26821 40 ALA n
26831 41 VAL n
26841 42 GLU n
26851 43 ILE n
26861 44 LYS n
26871 45 GLN n
26881 46 GLU n
26891 47 GLY n
26901 48 ASP n
26911 49 THR n
26921 50 PHE n
26931 51 TYR n
26941 52 ILE n
26951 53 LYS n
26961 54 THR n
26971 55 SER n
26981 56 THR n
26991 57 THR n
27001 58 VAL n
27011 59 ARG n
27021 60 THR n
27031 61 THR n
27041 62 GLU n
27051 63 ILE n
27061 64 ASN n
27071 65 PHE n
27081 66 LYS n
27091 67 VAL n
27101 68 GLY n
27111 69 GLU n
27121 70 GLU n
27131 71 PHE n
27141 72 GLU n
27151 73 GLU n
27161 74 GLN n
27171 75 THR n
27181 76 VAL n
27191 77 ASP n
27201 78 GLY n
27211 79 ARG n
27221 80 PRO n
27231 81 CYS n
27241 82 LYS n
27251 83 SER n
27261 84 LEU n
27271 85 VAL n
27281 86 LYS n
27291 87 TRP n
27301 88 GLU n
27311 89 SER n
27321 90 GLU n
27331 91 ASN n
27341 92 LYS n
27351 93 MET n
27361 94 VAL n
27371 95 CYS n
27381 96 GLU n
27391 97 GLN n
27401 98 LYS n
27411 99 LEU n
27421 100 LEU n
27431 101 LYS n
27441 102 GLY n
27451 103 GLU n
27461 104 GLY n
27471 105 PRO n
27481 106 LYS n
27491 107 THR n
27501 108 SER n
27511 109 TRP n
27521 110 THR n
27531 111 ARG n
27541 112 GLU n
27551 113 LEU n
27561 114 THR n
27571 115 ASN n
27581 116 ASP n
27591 117 GLY n
27601 118 GLU n
27611 119 LEU n
27621 120 ILE n
27631 121 LEU n
27641 122 THR n
27651 123 MET n
27661 124 THR n
27671 125 ALA n
27681 126 ASP n
27691 127 ASP n
27701 128 VAL n
27711 129 VAL n
27721 130 CYS n
27731 131 THR n
27741 132 ARG n
27751 133 VAL n
27761 134 TYR n
27771 135 VAL n
27781 136 ARG n
27791 137 GLU n
2780#
2781loop_
2782_entity.id
2783_entity.type
2784_entity.src_method
2785_entity.pdbx_description
2786_entity.pdbx_number_of_molecules
2787_entity.details
2788_entity.pdbx_mutation
2789_entity.pdbx_fragment
2790_entity.pdbx_ec
2791_entity.pdbx_parent_entity_id
27921 polymer ? ? 1 ? ? ? ? ?
27932 non-polymer syn RETINOICACID 1 ? ? ? ? ?
27943 water nat water 88 ? ? ? ? ?
2795#
2796loop_
2797_struct_asym.id
2798_struct_asym.pdbx_blank_PDB_chainid_flag
2799_struct_asym.entity_id
2800A N 1
2801B N 2
2802C N 3
2803#
2804loop_
2805_pdbx_poly_seq_scheme.asym_id
2806_pdbx_poly_seq_scheme.entity_id
2807_pdbx_poly_seq_scheme.seq_id
2808_pdbx_poly_seq_scheme.mon_id
2809_pdbx_poly_seq_scheme.ndb_seq_num
2810_pdbx_poly_seq_scheme.pdb_seq_num
2811_pdbx_poly_seq_scheme.auth_seq_num
2812_pdbx_poly_seq_scheme.pdb_mon_id
2813_pdbx_poly_seq_scheme.auth_mon_id
2814_pdbx_poly_seq_scheme.pdb_strand_id
2815_pdbx_poly_seq_scheme.pdb_ins_code
2816_pdbx_poly_seq_scheme.hetero
2817A 1 1 PRO 1 1 1 PRO PRO A . n
2818A 1 2 ASN 2 2 2 ASN ASN A . n
2819A 1 3 PHE 3 3 3 PHE PHE A . n
2820A 1 4 SER 4 4 4 SER SER A . n
2821A 1 5 GLY 5 5 5 GLY GLY A . n
2822A 1 6 ASN 6 6 6 ASN ASN A . n
2823A 1 7 TRP 7 7 7 TRP TRP A . n
2824A 1 8 LYS 8 8 8 LYS LYS A . n
2825A 1 9 ILE 9 9 9 ILE ILE A . n
2826A 1 10 ILE 10 10 10 ILE ILE A . n
2827A 1 11 ARG 11 11 11 ARG ARG A . n
2828A 1 12 SER 12 12 12 SER SER A . n
2829A 1 13 GLU 13 13 13 GLU GLU A . n
2830A 1 14 ASN 14 14 14 ASN ASN A . n
2831A 1 15 PHE 15 15 15 PHE PHE A . n
2832A 1 16 GLU 16 16 16 GLU GLU A . n
2833A 1 17 GLU 17 17 17 GLU GLU A . n
2834A 1 18 LEU 18 18 18 LEU LEU A . n
2835A 1 19 LEU 19 19 19 LEU LEU A . n
2836A 1 20 LYS 20 20 20 LYS LYS A . n
2837A 1 21 VAL 21 21 21 VAL VAL A . n
2838A 1 22 LEU 22 22 22 LEU LEU A . n
2839A 1 23 GLY 23 23 23 GLY GLY A . n
2840A 1 24 VAL 24 24 24 VAL VAL A . n
2841A 1 25 ASN 25 25 25 ASN ASN A . n
2842A 1 26 VAL 26 26 26 VAL VAL A . n
2843A 1 27 MET 27 27 27 MET MET A . n
2844A 1 28 LEU 28 28 28 LEU LEU A . n
2845A 1 29 ARG 29 29 29 ARG ARG A . n
2846A 1 30 LYS 30 30 30 LYS LYS A . n
2847A 1 31 ILE 31 31 31 ILE ILE A . n
2848A 1 32 ALA 32 32 32 ALA ALA A . n
2849A 1 33 VAL 33 33 33 VAL VAL A . n
2850A 1 34 ALA 34 34 34 ALA ALA A . n
2851A 1 35 ALA 35 35 35 ALA ALA A . n
2852A 1 36 ALA 36 36 36 ALA ALA A . n
2853A 1 37 SER 37 37 37 SER SER A . n
2854A 1 38 LYS 38 38 38 LYS LYS A . n
2855A 1 39 PRO 39 39 39 PRO PRO A . n
2856A 1 40 ALA 40 40 40 ALA ALA A . n
2857A 1 41 VAL 41 41 41 VAL VAL A . n
2858A 1 42 GLU 42 42 42 GLU GLU A . n
2859A 1 43 ILE 43 43 43 ILE ILE A . n
2860A 1 44 LYS 44 44 44 LYS LYS A . n
2861A 1 45 GLN 45 45 45 GLN GLN A . n
2862A 1 46 GLU 46 46 46 GLU GLU A . n
2863A 1 47 GLY 47 47 47 GLY GLY A . n
2864A 1 48 ASP 48 48 48 ASP ASP A . n
2865A 1 49 THR 49 49 49 THR THR A . n
2866A 1 50 PHE 50 50 50 PHE PHE A . n
2867A 1 51 TYR 51 51 51 TYR TYR A . n
2868A 1 52 ILE 52 52 52 ILE ILE A . n
2869A 1 53 LYS 53 53 53 LYS LYS A . n
2870A 1 54 THR 54 54 54 THR THR A . n
2871A 1 55 SER 55 55 55 SER SER A . n
2872A 1 56 THR 56 56 56 THR THR A . n
2873A 1 57 THR 57 57 57 THR THR A . n
2874A 1 58 VAL 58 58 58 VAL VAL A . n
2875A 1 59 ARG 59 59 59 ARG ARG A . n
2876A 1 60 THR 60 60 60 THR THR A . n
2877A 1 61 THR 61 61 61 THR THR A . n
2878A 1 62 GLU 62 62 62 GLU GLU A . n
2879A 1 63 ILE 63 63 63 ILE ILE A . n
2880A 1 64 ASN 64 64 64 ASN ASN A . n
2881A 1 65 PHE 65 65 65 PHE PHE A . n
2882A 1 66 LYS 66 66 66 LYS LYS A . n
2883A 1 67 VAL 67 67 67 VAL VAL A . n
2884A 1 68 GLY 68 68 68 GLY GLY A . n
2885A 1 69 GLU 69 69 69 GLU GLU A . n
2886A 1 70 GLU 70 70 70 GLU GLU A . n
2887A 1 71 PHE 71 71 71 PHE PHE A . n
2888A 1 72 GLU 72 72 72 GLU GLU A . n
2889A 1 73 GLU 73 73 73 GLU GLU A . n
2890A 1 74 GLN 74 74 74 GLN GLN A . n
2891A 1 75 THR 75 75 75 THR THR A . n
2892A 1 76 VAL 76 76 76 VAL VAL A . n
2893A 1 77 ASP 77 77 77 ASP ASP A . n
2894A 1 78 GLY 78 78 78 GLY GLY A . n
2895A 1 79 ARG 79 79 79 ARG ARG A . n
2896A 1 80 PRO 80 80 80 PRO PRO A . n
2897A 1 81 CYS 81 81 81 CYS CYS A . n
2898A 1 82 LYS 82 82 82 LYS LYS A . n
2899A 1 83 SER 83 83 83 SER SER A . n
2900A 1 84 LEU 84 84 84 LEU LEU A . n
2901A 1 85 VAL 85 85 85 VAL VAL A . n
2902A 1 86 LYS 86 86 86 LYS LYS A . n
2903A 1 87 TRP 87 87 87 TRP TRP A . n
2904A 1 88 GLU 88 88 88 GLU GLU A . n
2905A 1 89 SER 89 89 89 SER SER A . n
2906A 1 90 GLU 90 90 90 GLU GLU A . n
2907A 1 91 ASN 91 91 91 ASN ASN A . n
2908A 1 92 LYS 92 92 92 LYS LYS A . n
2909A 1 93 MET 93 93 93 MET MET A . n
2910A 1 94 VAL 94 94 94 VAL VAL A . n
2911A 1 95 CYS 95 95 95 CYS CYS A . n
2912A 1 96 GLU 96 96 96 GLU GLU A . n
2913A 1 97 GLN 97 97 97 GLN GLN A . n
2914A 1 98 LYS 98 98 98 LYS LYS A . n
2915A 1 99 LEU 99 99 99 LEU LEU A . n
2916A 1 100 LEU 100 100 100 LEU LEU A . n
2917A 1 101 LYS 101 101 101 LYS LYS A . n
2918A 1 102 GLY 102 102 102 GLY GLY A . n
2919A 1 103 GLU 103 103 103 GLU GLU A . n
2920A 1 104 GLY 104 104 104 GLY GLY A . n
2921A 1 105 PRO 105 105 105 PRO PRO A . n
2922A 1 106 LYS 106 106 106 LYS LYS A . n
2923A 1 107 THR 107 107 107 THR THR A . n
2924A 1 108 SER 108 108 108 SER SER A . n
2925A 1 109 TRP 109 109 109 TRP TRP A . n
2926A 1 110 THR 110 110 110 THR THR A . n
2927A 1 111 ARG 111 111 111 ARG ARG A . n
2928A 1 112 GLU 112 112 112 GLU GLU A . n
2929A 1 113 LEU 113 113 113 LEU LEU A . n
2930A 1 114 THR 114 114 114 THR THR A . n
2931A 1 115 ASN 115 115 115 ASN ASN A . n
2932A 1 116 ASP 116 116 116 ASP ASP A . n
2933A 1 117 GLY 117 117 117 GLY GLY A . n
2934A 1 118 GLU 118 118 118 GLU GLU A . n
2935A 1 119 LEU 119 119 119 LEU LEU A . n
2936A 1 120 ILE 120 120 120 ILE ILE A . n
2937A 1 121 LEU 121 121 121 LEU LEU A . n
2938A 1 122 THR 122 122 122 THR THR A . n
2939A 1 123 MET 123 123 123 MET MET A . n
2940A 1 124 THR 124 124 124 THR THR A . n
2941A 1 125 ALA 125 125 125 ALA ALA A . n
2942A 1 126 ASP 126 126 126 ASP ASP A . n
2943A 1 127 ASP 127 127 127 ASP ASP A . n
2944A 1 128 VAL 128 128 128 VAL VAL A . n
2945A 1 129 VAL 129 129 129 VAL VAL A . n
2946A 1 130 CYS 130 130 130 CYS CYS A . n
2947A 1 131 THR 131 131 131 THR THR A . n
2948A 1 132 ARG 132 132 132 ARG ARG A . n
2949A 1 133 VAL 133 133 133 VAL VAL A . n
2950A 1 134 TYR 134 134 134 TYR TYR A . n
2951A 1 135 VAL 135 135 135 VAL VAL A . n
2952A 1 136 ARG 136 136 136 ARG ARG A . n
2953A 1 137 GLU 137 137 137 GLU GLU A . n
2954#
2955_exptl.entry_id 1CBS
2956_exptl.method 'X-RAY DIFFRACTION'
2957_exptl.crystals_number ?
2958#
2959loop_
2960_dssp_struct_bridge_pairs.id
2961_dssp_struct_bridge_pairs.label_comp_id
2962_dssp_struct_bridge_pairs.label_seq_id
2963_dssp_struct_bridge_pairs.label_asym_id
2964_dssp_struct_bridge_pairs.auth_seq_id
2965_dssp_struct_bridge_pairs.auth_asym_id
2966_dssp_struct_bridge_pairs.pdbx_PDB_ins_code
2967_dssp_struct_bridge_pairs.acceptor_1_label_comp_id
2968_dssp_struct_bridge_pairs.acceptor_1_label_seq_id
2969_dssp_struct_bridge_pairs.acceptor_1_label_asym_id
2970_dssp_struct_bridge_pairs.acceptor_1_auth_seq_id
2971_dssp_struct_bridge_pairs.acceptor_1_auth_asym_id
2972_dssp_struct_bridge_pairs.acceptor_1_pdbx_PDB_ins_code
2973_dssp_struct_bridge_pairs.acceptor_1_energy
2974_dssp_struct_bridge_pairs.acceptor_2_label_comp_id
2975_dssp_struct_bridge_pairs.acceptor_2_label_seq_id
2976_dssp_struct_bridge_pairs.acceptor_2_label_asym_id
2977_dssp_struct_bridge_pairs.acceptor_2_auth_seq_id
2978_dssp_struct_bridge_pairs.acceptor_2_auth_asym_id
2979_dssp_struct_bridge_pairs.acceptor_2_pdbx_PDB_ins_code
2980_dssp_struct_bridge_pairs.acceptor_2_energy
2981_dssp_struct_bridge_pairs.donor_1_label_comp_id
2982_dssp_struct_bridge_pairs.donor_1_label_seq_id
2983_dssp_struct_bridge_pairs.donor_1_label_asym_id
2984_dssp_struct_bridge_pairs.donor_1_auth_seq_id
2985_dssp_struct_bridge_pairs.donor_1_auth_asym_id
2986_dssp_struct_bridge_pairs.donor_1_pdbx_PDB_ins_code
2987_dssp_struct_bridge_pairs.donor_1_energy
2988_dssp_struct_bridge_pairs.donor_2_label_comp_id
2989_dssp_struct_bridge_pairs.donor_2_label_seq_id
2990_dssp_struct_bridge_pairs.donor_2_label_asym_id
2991_dssp_struct_bridge_pairs.donor_2_auth_seq_id
2992_dssp_struct_bridge_pairs.donor_2_auth_asym_id
2993_dssp_struct_bridge_pairs.donor_2_pdbx_PDB_ins_code
2994_dssp_struct_bridge_pairs.donor_2_energy
29951 PRO 1 A 1 A ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? PHE 3 A 3 A ? -0.6 GLY 47 A 47 A ? -0.1
29962 ASN 2 A 2 A ? PHE 3 A 3 A ? -0.1 SER 4 A 4 A ? -0.1 ASN 91 A 91 A ? -0.0 GLU 46 A 46 A ? -0.0
29973 PHE 3 A 3 A ? PRO 1 A 1 A ? -0.6 LEU 113 A 113 A ? -0.0 ASN 2 A 2 A ? -0.1 ILE 43 A 43 A ? -0.1
29984 SER 4 A 4 A ? GLN 45 A 45 A ? -0.1 GLU 42 A 42 A ? -0.1 ASN 6 A 6 A ? -0.3 LYS 44 A 44 A ? -0.2
29995 GLY 5 A 5 A ? ILE 43 A 43 A ? -2.4 TRP 7 A 7 A ? -0.1 ILE 43 A 43 A ? -2.7 TRP 7 A 7 A ? -0.6
30006 ASN 6 A 6 A ? SER 4 A 4 A ? -0.3 GLU 42 A 42 A ? -0.2 GLU 137 A 137 A ? -2.8 LYS 8 A 8 A ? -0.4
30017 TRP 7 A 7 A ? VAL 41 A 41 A ? -2.9 GLY 5 A 5 A ? -0.6 VAL 41 A 41 A ? -1.4 ILE 9 A 9 A ? -0.4
30028 LYS 8 A 8 A ? VAL 135 A 135 A ? -3.1 ASN 6 A 6 A ? -0.4 VAL 135 A 135 A ? -2.3 ILE 10 A 10 A ? -0.2
30039 ILE 9 A 9 A ? PRO 39 A 39 A ? -0.4 TRP 7 A 7 A ? -0.4 TYR 134 A 134 A ? -0.3 SER 12 A 12 A ? -0.1
300410 ILE 10 A 10 A ? VAL 133 A 133 A ? -3.2 ARG 11 A 11 A ? -0.4 SER 12 A 12 A ? -0.3 TYR 134 A 134 A ? -0.2
300511 ARG 11 A 11 A ? VAL 133 A 133 A ? -1.4 GLU 13 A 13 A ? -0.0 VAL 133 A 133 A ? -2.5 ILE 10 A 10 A ? -0.4
300612 SER 12 A 12 A ? ILE 10 A 10 A ? -0.3 ARG 132 A 132 A ? -0.2 ASN 14 A 14 A ? -0.4 ARG 132 A 132 A ? -0.2
300713 GLU 13 A 13 A ? THR 131 A 131 A ? -2.5 ARG 11 A 11 A ? -0.3 THR 131 A 131 A ? -1.6 ARG 11 A 11 A ? -0.0
300814 ASN 14 A 14 A ? SER 12 A 12 A ? -0.4 CYS 130 A 130 A ? -0.2 LEU 18 A 18 A ? -1.8 LEU 19 A 19 A ? -0.1
300915 PHE 15 A 15 A ? GLU 16 A 16 A ? -0.2 GLU 17 A 17 A ? -0.2 LEU 19 A 19 A ? -1.9 LYS 20 A 20 A ? -0.2
301016 GLU 16 A 16 A ? GLU 17 A 17 A ? -0.2 LEU 18 A 18 A ? -0.2 LYS 20 A 20 A ? -1.9 PHE 15 A 15 A ? -0.2
301117 GLU 17 A 17 A ? LEU 18 A 18 A ? -0.2 LEU 19 A 19 A ? -0.2 VAL 21 A 21 A ? -1.8 GLU 16 A 16 A ? -0.2
301218 LEU 18 A 18 A ? ASN 14 A 14 A ? -1.8 LEU 19 A 19 A ? -0.2 LEU 22 A 22 A ? -1.4 GLU 17 A 17 A ? -0.2
301319 LEU 19 A 19 A ? PHE 15 A 15 A ? -1.9 LYS 20 A 20 A ? -0.2 VAL 24 A 24 A ? -2.3 GLY 23 A 23 A ? -0.3
301420 LYS 20 A 20 A ? GLU 16 A 16 A ? -1.9 VAL 21 A 21 A ? -0.2 GLY 23 A 23 A ? -1.4 LEU 19 A 19 A ? -0.2
301521 VAL 21 A 21 A ? GLU 17 A 17 A ? -1.8 LEU 22 A 22 A ? -0.3 LYS 20 A 20 A ? -0.2 LEU 19 A 19 A ? -0.2
301622 LEU 22 A 22 A ? LEU 18 A 18 A ? -1.4 GLU 17 A 17 A ? -0.2 VAL 21 A 21 A ? -0.3 LYS 20 A 20 A ? -0.2
301723 GLY 23 A 23 A ? LYS 20 A 20 A ? -1.4 LEU 19 A 19 A ? -0.3 ASN 25 A 25 A ? -0.4 LYS 20 A 20 A ? -0.2
301824 VAL 24 A 24 A ? LEU 19 A 19 A ? -2.3 ASN 25 A 25 A ? -0.1 GLY 23 A 23 A ? -0.3 LEU 22 A 22 A ? -0.1
301925 ASN 25 A 25 A ? GLY 23 A 23 A ? -0.4 VAL 26 A 26 A ? -0.1 ARG 29 A 29 A ? -2.4 LYS 30 A 30 A ? -0.2
302026 VAL 26 A 26 A ? MET 27 A 27 A ? -0.2 LEU 28 A 28 A ? -0.2 LYS 30 A 30 A ? -2.0 ILE 31 A 31 A ? -0.1
302127 MET 27 A 27 A ? LEU 28 A 28 A ? -0.2 ARG 29 A 29 A ? -0.2 ILE 31 A 31 A ? -1.6 VAL 26 A 26 A ? -0.2
302228 LEU 28 A 28 A ? ARG 29 A 29 A ? -0.2 LYS 30 A 30 A ? -0.2 ALA 32 A 32 A ? -2.4 MET 27 A 27 A ? -0.2
302329 ARG 29 A 29 A ? ASN 25 A 25 A ? -2.4 ILE 31 A 31 A ? -0.2 VAL 33 A 33 A ? -2.9 ALA 34 A 34 A ? -0.3
302430 LYS 30 A 30 A ? VAL 26 A 26 A ? -2.0 ILE 31 A 31 A ? -0.2 ALA 34 A 34 A ? -1.7 LEU 28 A 28 A ? -0.2
302531 ILE 31 A 31 A ? MET 27 A 27 A ? -1.6 ALA 32 A 32 A ? -0.2 ALA 35 A 35 A ? -2.0 LYS 30 A 30 A ? -0.2
302632 ALA 32 A 32 A ? LEU 28 A 28 A ? -2.4 VAL 33 A 33 A ? -0.2 ALA 36 A 36 A ? -2.6 LYS 30 A 30 A ? -0.2
302733 VAL 33 A 33 A ? ARG 29 A 29 A ? -2.9 ALA 34 A 34 A ? -0.2 SER 37 A 37 A ? -0.5 ALA 32 A 32 A ? -0.2
302834 ALA 34 A 34 A ? LYS 30 A 30 A ? -1.7 ARG 29 A 29 A ? -0.3 SER 37 A 37 A ? -0.9 LYS 38 A 38 A ? -0.3
302935 ALA 35 A 35 A ? ILE 31 A 31 A ? -2.0 ALA 36 A 36 A ? -0.2 LYS 38 A 38 A ? -1.1 THR 57 A 57 A ? -0.2
303036 ALA 36 A 36 A ? ALA 32 A 32 A ? -2.6 SER 37 A 37 A ? -0.2 ALA 35 A 35 A ? -0.2 ALA 34 A 34 A ? -0.2
303137 SER 37 A 37 A ? ALA 34 A 34 A ? -0.9 VAL 33 A 33 A ? -0.5 ALA 36 A 36 A ? -0.2 ALA 35 A 35 A ? -0.2
303238 LYS 38 A 38 A ? ALA 35 A 35 A ? -1.1 ALA 34 A 34 A ? -0.3 SER 37 A 37 A ? -0.2 ALA 36 A 36 A ? -0.1
303339 PRO 39 A 39 A ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? VAL 41 A 41 A ? -0.5 ILE 9 A 9 A ? -0.4
303440 ALA 40 A 40 A ? SER 55 A 55 A ? -2.2 LYS 8 A 8 A ? -0.1 SER 55 A 55 A ? -2.9 GLU 42 A 42 A ? -0.5
303541 VAL 41 A 41 A ? TRP 7 A 7 A ? -1.4 PRO 39 A 39 A ? -0.5 TRP 7 A 7 A ? -2.9 ILE 43 A 43 A ? -0.5
303642 GLU 42 A 42 A ? LYS 53 A 53 A ? -2.5 ALA 40 A 40 A ? -0.5 LYS 53 A 53 A ? -2.6 LYS 44 A 44 A ? -0.4
303743 ILE 43 A 43 A ? GLY 5 A 5 A ? -2.7 VAL 41 A 41 A ? -0.5 GLY 5 A 5 A ? -2.4 GLN 45 A 45 A ? -0.4
303844 LYS 44 A 44 A ? TYR 51 A 51 A ? -2.4 GLU 42 A 42 A ? -0.4 TYR 51 A 51 A ? -2.1 GLU 46 A 46 A ? -0.4
303945 GLN 45 A 45 A ? ILE 43 A 43 A ? -0.4 PHE 50 A 50 A ? -0.2 GLY 47 A 47 A ? -0.4 PHE 50 A 50 A ? -0.2
304046 GLU 46 A 46 A ? THR 49 A 49 A ? -2.7 LYS 44 A 44 A ? -0.4 THR 49 A 49 A ? -1.9 ASP 48 A 48 A ? -0.3
304147 GLY 47 A 47 A ? GLN 45 A 45 A ? -0.4 ASP 48 A 48 A ? -0.3 GLU 46 A 46 A ? -0.0 LYS 66 A 66 A ? -0.0
304248 ASP 48 A 48 A ? GLU 46 A 46 A ? -0.3 GLN 45 A 45 A ? -0.1 VAL 67 A 67 A ? -2.3 PHE 50 A 50 A ? -0.5
304349 THR 49 A 49 A ? GLU 46 A 46 A ? -1.9 LYS 66 A 66 A ? -0.2 GLU 46 A 46 A ? -2.7 TYR 51 A 51 A ? -0.3
304450 PHE 50 A 50 A ? PHE 65 A 65 A ? -3.1 ASP 48 A 48 A ? -0.5 PHE 65 A 65 A ? -2.2 ILE 52 A 52 A ? -0.4
304551 TYR 51 A 51 A ? LYS 44 A 44 A ? -2.1 THR 49 A 49 A ? -0.3 LYS 44 A 44 A ? -2.4 LYS 53 A 53 A ? -0.4
304652 ILE 52 A 52 A ? ILE 63 A 63 A ? -2.3 PHE 50 A 50 A ? -0.4 ILE 63 A 63 A ? -2.3 THR 54 A 54 A ? -0.5
304753 LYS 53 A 53 A ? GLU 42 A 42 A ? -2.6 TYR 51 A 51 A ? -0.4 GLU 42 A 42 A ? -2.5 SER 55 A 55 A ? -0.5
304854 THR 54 A 54 A ? THR 61 A 61 A ? -2.4 ILE 52 A 52 A ? -0.5 THR 61 A 61 A ? -2.2 THR 56 A 56 A ? -0.4
304955 SER 55 A 55 A ? ALA 40 A 40 A ? -2.9 LYS 53 A 53 A ? -0.5 ALA 40 A 40 A ? -2.2 THR 57 A 57 A ? -0.3
305056 THR 56 A 56 A ? ARG 59 A 59 A ? -1.1 THR 54 A 54 A ? -0.4 ARG 59 A 59 A ? -0.3 ALA 36 A 36 A ? -0.1
305157 THR 57 A 57 A ? SER 55 A 55 A ? -0.3 ALA 35 A 35 A ? -0.2 THR 60 A 60 A ? -0.1 ALA 36 A 36 A ? -0.0
305258 VAL 58 A 58 A ? ARG 59 A 59 A ? -0.3 ALA 32 A 32 A ? -0.1 THR 60 A 60 A ? -0.3 THR 57 A 57 A ? -0.2
305359 ARG 59 A 59 A ? THR 56 A 56 A ? -0.3 ALA 35 A 35 A ? -0.1 THR 56 A 56 A ? -1.1 THR 61 A 61 A ? -0.4
305460 THR 60 A 60 A ? VAL 58 A 58 A ? -0.3 SER 55 A 55 A ? -0.2 GLU 62 A 62 A ? -0.4 SER 55 A 55 A ? -0.2
305561 THR 61 A 61 A ? THR 54 A 54 A ? -2.2 ARG 59 A 59 A ? -0.4 THR 54 A 54 A ? -2.4 ILE 63 A 63 A ? -0.4
305662 GLU 62 A 62 A ? THR 60 A 60 A ? -0.4 LYS 53 A 53 A ? -0.2 ASN 64 A 64 A ? -0.4 LYS 53 A 53 A ? -0.2
305763 ILE 63 A 63 A ? ILE 52 A 52 A ? -2.3 THR 61 A 61 A ? -0.4 ILE 52 A 52 A ? -2.3 PHE 65 A 65 A ? -0.4
305864 ASN 64 A 64 A ? GLU 62 A 62 A ? -0.4 TYR 51 A 51 A ? -0.2 LYS 66 A 66 A ? -0.3 TYR 51 A 51 A ? -0.2
305965 PHE 65 A 65 A ? PHE 50 A 50 A ? -2.2 ILE 63 A 63 A ? -0.4 PHE 50 A 50 A ? -3.1 VAL 67 A 67 A ? -0.4
306066 LYS 66 A 66 A ? GLU 69 A 69 A ? -0.3 ASN 64 A 64 A ? -0.3 GLU 69 A 69 A ? -1.8 VAL 85 A 85 A ? -0.3
306167 VAL 67 A 67 A ? ASP 48 A 48 A ? -2.3 PHE 65 A 65 A ? -0.4 LYS 86 A 86 A ? -0.2 GLU 70 A 70 A ? -0.1
306268 GLY 68 A 68 A ? VAL 85 A 85 A ? -2.9 GLU 69 A 69 A ? -0.2 GLU 70 A 70 A ? -0.4 VAL 67 A 67 A ? -0.2
306369 GLU 69 A 69 A ? LYS 66 A 66 A ? -1.8 VAL 85 A 85 A ? -0.1 VAL 85 A 85 A ? -0.4 LYS 66 A 66 A ? -0.3
306470 GLU 70 A 70 A ? GLY 68 A 68 A ? -0.4 LEU 84 A 84 A ? -0.1 GLU 72 A 72 A ? -0.3 LEU 84 A 84 A ? -0.2
306571 PHE 71 A 71 A ? SER 83 A 83 A ? -2.2 PHE 65 A 65 A ? -0.1 SER 83 A 83 A ? -3.3 GLU 73 A 73 A ? -0.4
306672 GLU 72 A 72 A ? GLU 70 A 70 A ? -0.3 LYS 82 A 82 A ? -0.2 LYS 82 A 82 A ? -0.2 GLN 74 A 74 A ? -0.2
306773 GLU 73 A 73 A ? CYS 81 A 81 A ? -2.3 PHE 71 A 71 A ? -0.4 CYS 81 A 81 A ? -2.4 THR 75 A 75 A ? -0.3
306874 GLN 74 A 74 A ? PRO 80 A 80 A ? -0.3 GLU 72 A 72 A ? -0.2 LEU 99 A 99 A ? -0.0 VAL 76 A 76 A ? -0.0
306975 THR 75 A 75 A ? ARG 79 A 79 A ? -2.3 GLU 73 A 73 A ? -0.3 GLY 78 A 78 A ? -1.9 CYS 81 A 81 A ? -0.0
307076 VAL 76 A 76 A ? ASP 77 A 77 A ? -0.3 GLY 78 A 78 A ? -0.1 THR 75 A 75 A ? -0.1 LEU 19 A 19 A ? -0.1
307177 ASP 77 A 77 A ? ARG 79 A 79 A ? -0.1 LEU 22 A 22 A ? -0.0 VAL 76 A 76 A ? -0.3 THR 75 A 75 A ? -0.0
307278 GLY 78 A 78 A ? THR 75 A 75 A ? -1.9 ARG 79 A 79 A ? -0.3 VAL 76 A 76 A ? -0.1 ASP 77 A 77 A ? -0.0
307379 ARG 79 A 79 A ? PRO 80 A 80 A ? -0.1 LEU 100 A 100 A ? -0.0 THR 75 A 75 A ? -2.3 GLY 78 A 78 A ? -0.3
307480 PRO 80 A 80 A ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? LEU 100 A 100 A ? -1.7 LYS 101 A 101 A ? -0.5
307581 CYS 81 A 81 A ? GLU 73 A 73 A ? -2.4 LEU 99 A 99 A ? -0.2 GLU 73 A 73 A ? -2.3 SER 83 A 83 A ? -0.5
307682 LYS 82 A 82 A ? LYS 98 A 98 A ? -2.8 PRO 80 A 80 A ? -0.3 LYS 98 A 98 A ? -2.3 LEU 84 A 84 A ? -0.3
307783 SER 83 A 83 A ? PHE 71 A 71 A ? -3.3 CYS 81 A 81 A ? -0.5 PHE 71 A 71 A ? -2.2 VAL 85 A 85 A ? -0.4
307884 LEU 84 A 84 A ? GLU 96 A 96 A ? -1.4 LYS 82 A 82 A ? -0.3 GLU 96 A 96 A ? -2.0 LYS 86 A 86 A ? -0.4
307985 VAL 85 A 85 A ? GLU 69 A 69 A ? -0.4 SER 83 A 83 A ? -0.4 GLY 68 A 68 A ? -2.9 TRP 87 A 87 A ? -0.3
308086 LYS 86 A 86 A ? VAL 94 A 94 A ? -2.4 LEU 84 A 84 A ? -0.4 VAL 94 A 94 A ? -2.7 GLU 88 A 88 A ? -0.8
308187 TRP 87 A 87 A ? VAL 85 A 85 A ? -0.3 MET 93 A 93 A ? -0.2 MET 93 A 93 A ? -0.2 GLU 90 A 90 A ? -0.1
308288 GLU 88 A 88 A ? LYS 92 A 92 A ? -2.0 LYS 86 A 86 A ? -0.8 GLU 90 A 90 A ? -0.3 TRP 87 A 87 A ? -0.2
308389 SER 89 A 89 A ? LYS 92 A 92 A ? -1.7 LYS 86 A 86 A ? -0.2 LYS 92 A 92 A ? -1.4 GLU 88 A 88 A ? -0.3
308490 GLU 90 A 90 A ? ASN 91 A 91 A ? -0.3 GLU 88 A 88 A ? -0.3 MET 93 A 93 A ? -0.0 GLU 88 A 88 A ? -0.0
308591 ASN 91 A 91 A ? LYS 92 A 92 A ? -0.1 LEU 113 A 113 A ? -0.1 LEU 113 A 113 A ? -2.1 MET 93 A 93 A ? -0.4
308692 LYS 92 A 92 A ? SER 89 A 89 A ? -1.4 GLU 112 A 112 A ? -0.2 GLU 88 A 88 A ? -2.0 SER 89 A 89 A ? -1.7
308793 MET 93 A 93 A ? ARG 111 A 111 A ? -2.7 ASN 91 A 91 A ? -0.4 ARG 111 A 111 A ? -2.0 CYS 95 A 95 A ? -0.4
308894 VAL 94 A 94 A ? LYS 86 A 86 A ? -2.7 LYS 92 A 92 A ? -0.3 LYS 86 A 86 A ? -2.4 GLU 96 A 96 A ? -0.5
308995 CYS 95 A 95 A ? TRP 109 A 109 A ? -3.1 MET 93 A 93 A ? -0.4 TRP 109 A 109 A ? -1.7 GLN 97 A 97 A ? -0.4
309096 GLU 96 A 96 A ? LEU 84 A 84 A ? -2.0 VAL 94 A 94 A ? -0.5 LEU 84 A 84 A ? -1.4 LYS 98 A 98 A ? -0.4
309197 GLN 97 A 97 A ? THR 107 A 107 A ? -1.5 CYS 95 A 95 A ? -0.4 THR 107 A 107 A ? -0.4 LEU 99 A 99 A ? -0.4
309298 LYS 98 A 98 A ? LYS 82 A 82 A ? -2.3 GLU 96 A 96 A ? -0.4 LYS 82 A 82 A ? -2.8 LEU 100 A 100 A ? -0.1
309399 LEU 99 A 99 A ? GLN 97 A 97 A ? -0.4 CYS 81 A 81 A ? -0.2 CYS 81 A 81 A ? -0.2 GLY 102 A 102 A ? -0.1
3094100 LEU 100 A 100 A ? PRO 80 A 80 A ? -1.7 LYS 101 A 101 A ? -0.2 GLY 102 A 102 A ? -0.3 LEU 99 A 99 A ? -0.1
3095101 LYS 101 A 101 A ? PRO 80 A 80 A ? -0.5 GLU 103 A 103 A ? -0.0 LEU 100 A 100 A ? -0.2 ? ? ? ? ? ? ?
3096102 GLY 102 A 102 A ? LEU 100 A 100 A ? -0.3 LEU 99 A 99 A ? -0.1 GLY 104 A 104 A ? -0.3 LEU 99 A 99 A ? -0.1
3097103 GLU 103 A 103 A ? LYS 106 A 106 A ? -0.0 LEU 100 A 100 A ? -0.0 LEU 100 A 100 A ? -0.0 LYS 101 A 101 A ? -0.0
3098104 GLY 104 A 104 A ? GLY 102 A 102 A ? -0.3 LEU 99 A 99 A ? -0.0 LEU 99 A 99 A ? -0.1 LEU 22 A 22 A ? -0.1
3099105 PRO 105 A 105 A ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? THR 107 A 107 A ? -0.4 LEU 22 A 22 A ? -0.0
3100106 LYS 106 A 106 A ? LYS 98 A 98 A ? -0.1 GLU 103 A 103 A ? -0.0 ASP 126 A 126 A ? -2.5 SER 108 A 108 A ? -0.3
3101107 THR 107 A 107 A ? GLN 97 A 97 A ? -0.4 PRO 105 A 105 A ? -0.4 GLN 97 A 97 A ? -1.5 TRP 109 A 109 A ? -0.3
3102108 SER 108 A 108 A ? THR 124 A 124 A ? -1.4 LYS 106 A 106 A ? -0.3 THR 124 A 124 A ? -2.4 THR 110 A 110 A ? -0.3
3103109 TRP 109 A 109 A ? CYS 95 A 95 A ? -1.7 THR 107 A 107 A ? -0.3 CYS 95 A 95 A ? -3.1 ARG 111 A 111 A ? -0.3
3104110 THR 110 A 110 A ? THR 122 A 122 A ? -2.2 SER 108 A 108 A ? -0.3 THR 122 A 122 A ? -2.2 GLU 112 A 112 A ? -0.4
3105111 ARG 111 A 111 A ? MET 93 A 93 A ? -2.0 TRP 109 A 109 A ? -0.3 MET 93 A 93 A ? -2.7 LEU 113 A 113 A ? -0.3
3106112 GLU 112 A 112 A ? ILE 120 A 120 A ? -2.0 THR 110 A 110 A ? -0.4 ILE 120 A 120 A ? -2.6 THR 114 A 114 A ? -0.5
3107113 LEU 113 A 113 A ? ASN 91 A 91 A ? -2.1 ARG 111 A 111 A ? -0.3 LEU 119 A 119 A ? -0.2 ASN 115 A 115 A ? -0.1
3108114 THR 114 A 114 A ? GLU 118 A 118 A ? -2.4 GLU 112 A 112 A ? -0.5 GLY 117 A 117 A ? -1.8 LYS 92 A 92 A ? -0.0
3109115 ASN 115 A 115 A ? ASP 116 A 116 A ? -0.3 GLY 117 A 117 A ? -0.1 THR 114 A 114 A ? -0.1 LEU 113 A 113 A ? -0.0
3110116 ASP 116 A 116 A ? GLU 118 A 118 A ? -0.0 ? ? ? ? ? ? ? ASN 115 A 115 A ? -0.3 LEU 113 A 113 A ? -0.0
3111117 GLY 117 A 117 A ? THR 114 A 114 A ? -1.8 GLU 118 A 118 A ? -0.3 ARG 136 A 136 A ? -0.3 ASN 115 A 115 A ? -0.1
3112118 GLU 118 A 118 A ? VAL 135 A 135 A ? -0.1 VAL 133 A 133 A ? -0.0 THR 114 A 114 A ? -2.4 ILE 120 A 120 A ? -0.4
3113119 LEU 119 A 119 A ? TYR 134 A 134 A ? -2.3 LEU 113 A 113 A ? -0.2 TYR 134 A 134 A ? -2.7 LEU 121 A 121 A ? -0.5
3114120 ILE 120 A 120 A ? GLU 112 A 112 A ? -2.6 GLU 118 A 118 A ? -0.4 GLU 112 A 112 A ? -2.0 THR 122 A 122 A ? -0.5
3115121 LEU 121 A 121 A ? ARG 132 A 132 A ? -3.0 LEU 119 A 119 A ? -0.5 ARG 132 A 132 A ? -2.7 MET 123 A 123 A ? -0.4
3116122 THR 122 A 122 A ? THR 110 A 110 A ? -2.2 ILE 120 A 120 A ? -0.5 THR 110 A 110 A ? -2.2 THR 124 A 124 A ? -0.4
3117123 MET 123 A 123 A ? CYS 130 A 130 A ? -2.0 LEU 121 A 121 A ? -0.4 CYS 130 A 130 A ? -3.0 ALA 125 A 125 A ? -0.4
3118124 THR 124 A 124 A ? SER 108 A 108 A ? -2.4 THR 122 A 122 A ? -0.4 SER 108 A 108 A ? -1.4 ASP 126 A 126 A ? -0.3
3119125 ALA 125 A 125 A ? VAL 128 A 128 A ? -2.2 MET 123 A 123 A ? -0.4 VAL 128 A 128 A ? -2.3 THR 107 A 107 A ? -0.2
3120126 ASP 126 A 126 A ? LYS 106 A 106 A ? -2.5 THR 124 A 124 A ? -0.3 SER 108 A 108 A ? -0.0 VAL 21 A 21 A ? -0.0
3121127 ASP 127 A 127 A ? ALA 125 A 125 A ? -0.2 THR 124 A 124 A ? -0.1 VAL 129 A 129 A ? -0.3 ASP 126 A 126 A ? -0.3
3122128 VAL 128 A 128 A ? ALA 125 A 125 A ? -2.3 GLU 17 A 17 A ? -0.1 ALA 125 A 125 A ? -2.2 CYS 130 A 130 A ? -0.4
3123129 VAL 129 A 129 A ? ASP 127 A 127 A ? -0.3 THR 124 A 124 A ? -0.2 THR 131 A 131 A ? -0.5 THR 124 A 124 A ? -0.2
3124130 CYS 130 A 130 A ? MET 123 A 123 A ? -3.0 VAL 128 A 128 A ? -0.4 MET 123 A 123 A ? -2.0 ARG 132 A 132 A ? -0.5
3125131 THR 131 A 131 A ? GLU 13 A 13 A ? -1.6 VAL 129 A 129 A ? -0.5 GLU 13 A 13 A ? -2.5 VAL 133 A 133 A ? -0.4
3126132 ARG 132 A 132 A ? LEU 121 A 121 A ? -2.7 CYS 130 A 130 A ? -0.5 LEU 121 A 121 A ? -3.0 TYR 134 A 134 A ? -0.4
3127133 VAL 133 A 133 A ? ARG 11 A 11 A ? -2.5 THR 131 A 131 A ? -0.4 ILE 10 A 10 A ? -3.2 ARG 11 A 11 A ? -1.4
3128134 TYR 134 A 134 A ? LEU 119 A 119 A ? -2.7 ARG 132 A 132 A ? -0.4 LEU 119 A 119 A ? -2.3 ARG 136 A 136 A ? -0.3
3129135 VAL 135 A 135 A ? LYS 8 A 8 A ? -2.3 VAL 133 A 133 A ? -0.3 LYS 8 A 8 A ? -3.1 GLU 118 A 118 A ? -0.1
3130136 ARG 136 A 136 A ? GLY 117 A 117 A ? -0.3 TYR 134 A 134 A ? -0.3 TRP 7 A 7 A ? -0.3 GLY 5 A 5 A ? -0.0
3131137 GLU 137 A 137 A ? ASN 6 A 6 A ? -2.8 VAL 135 A 135 A ? -0.1 ASN 6 A 6 A ? -0.1 ARG 136 A 136 A ? -0.1
3132#
3133_struct_sheet.id A
3134_struct_sheet.number_strands 10
3135#
3136loop_
3137_struct_sheet_range.sheet_id
3138_struct_sheet_range.id
3139_struct_sheet_range.beg_label_comp_id
3140_struct_sheet_range.beg_label_asym_id
3141_struct_sheet_range.beg_label_seq_id
3142_struct_sheet_range.pdbx_beg_PDB_ins_code
3143_struct_sheet_range.end_label_comp_id
3144_struct_sheet_range.end_label_asym_id
3145_struct_sheet_range.end_label_seq_id
3146_struct_sheet_range.pdbx_end_PDB_ins_code
3147_struct_sheet_range.beg_auth_comp_id
3148_struct_sheet_range.beg_auth_asym_id
3149_struct_sheet_range.beg_auth_seq_id
3150_struct_sheet_range.end_auth_comp_id
3151_struct_sheet_range.end_auth_asym_id
3152_struct_sheet_range.end_auth_seq_id
3153A A GLY A 5 ? GLU A 13 ? GLY A 5 GLU A 13
3154A B ALA A 40 ? GLU A 46 ? ALA A 40 GLU A 46
3155A C THR A 49 ? SER A 55 ? THR A 49 SER A 55
3156A D THR A 60 ? LYS A 66 ? THR A 60 LYS A 66
3157A E PHE A 71 ? GLN A 74 ? PHE A 71 GLN A 74
3158A F PRO A 80 ? SER A 89 ? PRO A 80 SER A 89
3159A G LYS A 92 ? LEU A 99 ? LYS A 92 LEU A 99
3160A H THR A 107 ? LEU A 113 ? THR A 107 LEU A 113
3161A I LEU A 119 ? ALA A 125 ? LEU A 119 ALA A 125
3162A J VAL A 128 ? ARG A 136 ? VAL A 128 ARG A 136
3163#
3164loop_
3165_dssp_struct_ladder.id
3166_dssp_struct_ladder.sheet_id
3167_dssp_struct_ladder.range_id_1
3168_dssp_struct_ladder.range_id_2
3169_dssp_struct_ladder.type
3170_dssp_struct_ladder.beg_1_label_comp_id
3171_dssp_struct_ladder.beg_1_label_asym_id
3172_dssp_struct_ladder.beg_1_label_seq_id
3173_dssp_struct_ladder.pdbx_beg_1_PDB_ins_code
3174_dssp_struct_ladder.end_1_label_comp_id
3175_dssp_struct_ladder.end_1_label_asym_id
3176_dssp_struct_ladder.end_1_label_seq_id
3177_dssp_struct_ladder.pdbx_end_1_PDB_ins_code
3178_dssp_struct_ladder.beg_1_auth_comp_id
3179_dssp_struct_ladder.beg_1_auth_asym_id
3180_dssp_struct_ladder.beg_1_auth_seq_id
3181_dssp_struct_ladder.end_1_auth_comp_id
3182_dssp_struct_ladder.end_1_auth_asym_id
3183_dssp_struct_ladder.end_1_auth_seq_id
3184_dssp_struct_ladder.beg_2_label_comp_id
3185_dssp_struct_ladder.beg_2_label_asym_id
3186_dssp_struct_ladder.beg_2_label_seq_id
3187_dssp_struct_ladder.pdbx_beg_2_PDB_ins_code
3188_dssp_struct_ladder.end_2_label_comp_id
3189_dssp_struct_ladder.end_2_label_asym_id
3190_dssp_struct_ladder.end_2_label_seq_id
3191_dssp_struct_ladder.pdbx_end_2_PDB_ins_code
3192_dssp_struct_ladder.beg_2_auth_comp_id
3193_dssp_struct_ladder.beg_2_auth_asym_id
3194_dssp_struct_ladder.beg_2_auth_seq_id
3195_dssp_struct_ladder.end_2_auth_comp_id
3196_dssp_struct_ladder.end_2_auth_asym_id
3197_dssp_struct_ladder.end_2_auth_seq_id
3198A A A B anti-parallel GLY A 5 ? TRP A 7 ? GLY A 5 TRP A 7 ILE A 43 ? VAL A 41 ? ILE A 43 VAL A 41
3199B A A J anti-parallel TRP A 7 ? GLU A 13 ? TRP A 7 GLU A 13 ARG A 136 ? THR A 131 ? ARG A 136 THR A 131
3200C A B C anti-parallel ALA A 40 ? GLU A 46 ? ALA A 40 GLU A 46 SER A 55 ? THR A 49 ? SER A 55 THR A 49
3201D A C D anti-parallel THR A 49 ? SER A 55 ? THR A 49 SER A 55 LYS A 66 ? THR A 60 ? LYS A 66 THR A 60
3202E A E F anti-parallel PHE A 71 ? GLN A 74 ? PHE A 71 GLN A 74 SER A 83 ? PRO A 80 ? SER A 83 PRO A 80
3203F A F G anti-parallel CYS A 81 ? SER A 89 ? CYS A 81 SER A 89 LEU A 99 ? LYS A 92 ? LEU A 99 LYS A 92
3204G A G H anti-parallel LYS A 92 ? GLU A 96 ? LYS A 92 GLU A 96 GLU A 112 ? SER A 108 ? GLU A 112 SER A 108
3205H A H I anti-parallel THR A 107 ? LEU A 113 ? THR A 107 LEU A 113 ALA A 125 ? LEU A 119 ? ALA A 125 LEU A 119
3206I A I J anti-parallel LEU A 119 ? ALA A 125 ? LEU A 119 ALA A 125 TYR A 134 ? VAL A 128 ? TYR A 134 VAL A 128
3207#
3208_dssp_statistics.entry_id 1CBS
3209_dssp_statistics.nr_of_residues 137
3210_dssp_statistics.nr_of_chains 1
3211_dssp_statistics.nr_of_ss_bridges_total 0
3212_dssp_statistics.nr_of_ss_bridges_intra_chain 0
3213_dssp_statistics.nr_of_ss_bridges_inter_chain 0
3214#
3215loop_
3216_dssp_statistics_hbond.entry_id
3217_dssp_statistics_hbond.type
3218_dssp_statistics_hbond.count
3219_dssp_statistics_hbond.count_per_100
32201CBS O(I)-->H-N(J) 92 67.2
32211CBS 'PARALLEL BRIDGES' 0 0.0
32221CBS 'ANTIPARALLEL BRIDGES' 65 47.4
32231CBS O(I)-->H-N(I-5) 0 0.0
32241CBS O(I)-->H-N(I-4) 3 2.2
32251CBS O(I)-->H-N(I-3) 4 2.9
32261CBS O(I)-->H-N(I-2) 0 0.0
32271CBS O(I)-->H-N(I-1) 0 0.0
32281CBS O(I)-->H-N(I+0) 0 0.0
32291CBS O(I)-->H-N(I+1) 0 0.0
32301CBS O(I)-->H-N(I+2) 5 3.6
32311CBS O(I)-->H-N(I+3) 9 6.6
32321CBS O(I)-->H-N(I+4) 14 10.2
32331CBS O(I)-->H-N(I+5) 1 0.7
3234#
3235loop_
3236_dssp_statistics_histogram.entry_id
3237_dssp_statistics_histogram.type
3238_dssp_statistics_histogram.1
3239_dssp_statistics_histogram.2
3240_dssp_statistics_histogram.3
3241_dssp_statistics_histogram.4
3242_dssp_statistics_histogram.5
3243_dssp_statistics_histogram.6
3244_dssp_statistics_histogram.7
3245_dssp_statistics_histogram.8
3246_dssp_statistics_histogram.9
3247_dssp_statistics_histogram.10
3248_dssp_statistics_histogram.11
3249_dssp_statistics_histogram.12
3250_dssp_statistics_histogram.13
3251_dssp_statistics_histogram.14
3252_dssp_statistics_histogram.15
3253_dssp_statistics_histogram.16
3254_dssp_statistics_histogram.17
3255_dssp_statistics_histogram.18
3256_dssp_statistics_histogram.19
3257_dssp_statistics_histogram.20
3258_dssp_statistics_histogram.21
3259_dssp_statistics_histogram.22
3260_dssp_statistics_histogram.23
3261_dssp_statistics_histogram.24
3262_dssp_statistics_histogram.25
3263_dssp_statistics_histogram.26
3264_dssp_statistics_histogram.27
3265_dssp_statistics_histogram.28
3266_dssp_statistics_histogram.29
3267_dssp_statistics_histogram.30
32681CBS residues_per_alpha_helix 0 0 0 0 0 0 1 0 0 0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0
32691CBS parallel_bridges_per_ladder 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0
32701CBS antiparallel_bridges_per_ladder 0 0 1 1 1 1 4 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0
32711CBS ladders_per_sheet 0 0 0 0 0 0 0 0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0
3272#
3273loop_
3274_dssp_struct_summary.entry_id
3275_dssp_struct_summary.label_asym_id
3276_dssp_struct_summary.label_seq_id
3277_dssp_struct_summary.label_comp_id
3278_dssp_struct_summary.secondary_structure
3279_dssp_struct_summary.ss_bridge
3280_dssp_struct_summary.helix_3_10
3281_dssp_struct_summary.helix_alpha
3282_dssp_struct_summary.helix_pi
3283_dssp_struct_summary.helix_pp
3284_dssp_struct_summary.bend
3285_dssp_struct_summary.chirality
3286_dssp_struct_summary.sheet
3287_dssp_struct_summary.strand
3288_dssp_struct_summary.ladder_1
3289_dssp_struct_summary.ladder_2
3290_dssp_struct_summary.accessibility
3291_dssp_struct_summary.TCO
3292_dssp_struct_summary.kappa
3293_dssp_struct_summary.alpha
3294_dssp_struct_summary.phi
3295_dssp_struct_summary.psi
3296_dssp_struct_summary.x_ca
3297_dssp_struct_summary.y_ca
3298_dssp_struct_summary.z_ca
32991CBS A 1 PRO . . . . . . . . . . . . ? . . . . 144.4 18.1 13.6 43.6
33001CBS A 2 ASN . . . . . . . + . . . . ? -0.899 . 168.9 -115.0 102.2 20.7 16.4 43.7
33011CBS A 3 PHE . . . . . . . + . . . . ? 0.494 37.1 125.8 -84.3 -5.9 21.1 17.8 40.2
33021CBS A 4 SER . . . . . . . + . . . . ? -0.238 38.2 71.9 -61.3 138.6 23.2 20.8 41.5
33031CBS A 5 GLY E . . . . . S - A A A . ? -0.865 80.9 -69.0 154.4 -178.9 26.6 21.5 40.0
33041CBS A 6 ASN E . . . . . . - A A A . ? -0.956 54.4 -160.0 -102.6 116.3 28.8 22.7 37.2
33051CBS A 7 TRP E . . . . . . - A A A B ? -0.804 12.7 -164.3 -109.1 139.3 28.5 20.1 34.4
33061CBS A 8 LYS E . . . . . . - A A . B ? -0.944 27.8 -111.1 -121.2 143.9 30.8 19.4 31.4
33071CBS A 9 ILE E . . . . . . + A A . B ? -0.471 33.8 168.5 -77.5 142.7 29.8 17.4 28.4
33081CBS A 10 ILE E . . . . . . + A A . . ? 0.498 70.0 22.8 -123.1 -14.3 31.3 13.9 27.7
33091CBS A 11 ARG E . . . . . . - A A . B ? -0.973 53.7 -179.1 -153.2 137.5 29.0 12.7 24.9
33101CBS A 12 SER E . . . . . . - A A . B ? -0.981 9.3 -179.7 -135.3 129.1 26.7 14.3 22.3
33111CBS A 13 GLU E . . . . . . - A A . B ? -0.996 62.2 -4.4 -128.5 133.5 24.6 12.3 19.7
33121CBS A 14 ASN S . . > . . S + . . . . ? 0.626 75.5 136.3 73.0 20.6 22.2 13.4 17.0
33131CBS A 15 PHE H . . > . . S + . . . . ? 0.936 74.0 47.5 -66.8 -45.2 22.3 17.2 17.7
33141CBS A 16 GLU H . . > . . S + . . . . ? 0.910 110.4 52.8 -61.5 -41.3 22.6 18.2 14.1
33151CBS A 17 GLU H . . > . . S + . . . . ? 0.860 105.9 54.5 -62.5 -36.0 19.8 15.9 13.1
33161CBS A 18 LEU H . . X . . S + . . . . ? 0.932 108.5 48.4 -60.5 -46.4 17.6 17.5 15.8
33171CBS A 19 LEU H . . < > . S + . . . . ? 0.838 106.3 58.1 -64.4 -33.9 18.2 20.9 14.3
33181CBS A 20 LYS H . > < 5 . S + . . . . ? 0.932 105.7 48.5 -60.9 -47.7 17.4 19.6 10.8
33191CBS A 21 VAL H . 3 < 5 . S + . . . . ? 0.848 107.5 56.1 -60.0 -34.5 13.9 18.5 11.9
33201CBS A 22 LEU T . 3 < 5 . S - . . . . ? 0.512 120.1 -112.5 -79.7 -4.9 13.4 21.9 13.5
33211CBS A 23 GLY T . < . 5 . . + . . . . ? 0.662 58.0 158.8 87.6 20.5 14.1 23.5 10.1
33221CBS A 24 VAL . . . . < . . - . . . . ? -0.641 41.3 -118.8 -76.4 131.5 17.5 25.2 10.8
33231CBS A 25 ASN . . . > . . . - . . . . ? -0.159 25.3 -100.3 -73.7 165.9 19.4 25.9 7.6
33241CBS A 26 VAL H . . > . . S + . . . . ? 0.850 117.5 46.8 -55.2 -48.6 22.8 24.4 6.8
33251CBS A 27 MET H . . > . . S + . . . . ? 0.894 114.3 47.0 -67.2 -39.5 25.0 27.4 7.6
33261CBS A 28 LEU H . . > . . S + . . . . ? 0.867 109.6 54.9 -69.6 -34.9 23.2 28.1 10.9
33271CBS A 29 ARG H . . X . . S + . . . . ? 0.913 104.2 55.3 -59.9 -43.2 23.5 24.5 11.8
33281CBS A 30 LYS H . . X . . S + . . . . ? 0.933 110.6 44.6 -53.3 -50.4 27.2 24.7 11.2
33291CBS A 31 ILE H . . X . . S + . . . . ? 0.920 115.2 47.3 -59.6 -50.2 27.5 27.5 13.7
33301CBS A 32 ALA H . . X . . S + . . . . ? 0.892 109.4 51.7 -63.7 -44.2 25.3 25.9 16.3
33311CBS A 33 VAL H . . X . . S + . . . . ? 0.907 110.6 48.5 -63.7 -41.8 27.0 22.5 16.2
33321CBS A 34 ALA H . > < . . S + . . . . ? 0.938 115.9 42.9 -62.5 -46.7 30.5 23.9 16.8
33331CBS A 35 ALA H . > < . . S + . . . . ? 0.847 109.7 56.7 -70.4 -36.3 29.4 26.1 19.7
33341CBS A 36 ALA H . 3 < . . S + . . . . ? 0.529 88.4 78.9 -74.0 -5.7 27.2 23.4 21.3
33351CBS A 37 SER T . < < . . S + . . . . ? 0.692 103.0 32.0 -77.9 -16.9 30.2 21.0 21.5
33361CBS A 38 LYS S . < . . . S + . . . . ? -0.463 81.7 165.7 -137.1 68.4 31.7 22.8 24.6
33371CBS A 39 PRO . . . . . . . - . . . . ? -0.339 32.0 -137.2 -76.9 158.3 28.8 24.2 26.7
33381CBS A 40 ALA E . . . . . . - A B . C ? -0.995 24.8 -169.2 -109.9 123.6 29.1 25.4 30.3
33391CBS A 41 VAL E . . . . . . - A B A C ? -0.972 9.0 -176.3 -120.7 125.0 26.1 24.2 32.4
33401CBS A 42 GLU E . . . . . . - A B A C ? -0.984 4.5 -174.0 -118.7 124.2 25.3 25.4 35.9
33411CBS A 43 ILE E . . . . . . - A B A C ? -0.984 6.4 -174.9 -118.9 131.6 22.4 23.8 37.8
33421CBS A 44 LYS E . . . . . . - A B . C ? -0.998 10.4 -173.8 -122.2 123.9 21.1 25.1 41.2
33431CBS A 45 GLN E . . . . . . + A B . C ? -0.968 16.7 176.1 -121.4 134.4 18.4 23.0 42.8
33441CBS A 46 GLU E . > . . . S - A B . C ? -0.864 71.2 -60.4 -133.3 95.2 16.4 23.7 46.0
33451CBS A 47 GLY T . 3 . . . S - . . . . ? -0.509 121.1 -15.2 67.1 -121.9 13.8 21.0 46.5
33461CBS A 48 ASP T . 3 . . . S + . . . . ? 0.203 117.7 100.7 -97.2 15.1 11.6 21.1 43.4
33471CBS A 49 THR E . < . . . . - A C C D ? -0.888 54.3 -172.0 -103.7 130.7 12.9 24.5 42.3
33481CBS A 50 PHE E . . . . . . - A C C D ? -0.923 22.4 -171.2 -128.3 142.8 15.5 24.7 39.6
33491CBS A 51 TYR E . . . . . . - A C C D ? -0.995 15.6 -178.3 -123.4 129.1 17.8 27.2 37.9
33501CBS A 52 ILE E . . . . . . - A C C D ? -0.974 6.1 -175.0 -134.4 117.5 19.6 26.0 34.8
33511CBS A 53 LYS E . . . . . . - A C C D ? -0.962 1.6 -173.2 -113.1 125.5 22.1 28.2 32.9
33521CBS A 54 THR E . . . . . . - A C C D ? -0.982 11.3 -168.8 -122.0 116.1 23.5 26.8 29.6
33531CBS A 55 SER E . . . . . . + A C C D ? -0.901 15.8 158.0 -118.1 133.2 26.2 28.9 28.1
33541CBS A 56 THR . . . . . . . - . . . . ? -0.880 54.6 -99.2 -135.9 172.0 27.9 28.8 24.7
33551CBS A 57 THR S . . . . . S + . . . . ? 0.655 122.3 34.9 -65.6 -17.5 29.8 31.4 22.6
33561CBS A 58 VAL S . . . . . S + . . . . ? 0.506 126.3 13.6 -116.7 -8.8 26.7 32.1 20.5
33571CBS A 59 ARG . . . . . . . - . . . . ? -0.883 51.8 -165.5 -171.1 132.5 23.8 31.7 22.9
33581CBS A 60 THR E . . . . . . - A D D . ? -0.983 10.0 -166.8 -122.1 137.7 23.1 31.5 26.6
33591CBS A 61 THR E . . . . . . - A D D . ? -0.960 4.4 -171.3 -120.0 143.0 19.8 30.4 28.2
33601CBS A 62 GLU E . . . . . . - A D D . ? -0.972 9.5 -177.0 -131.1 118.9 18.7 30.7 31.8
33611CBS A 63 ILE E . . . . . . - A D D . ? -0.906 10.0 -168.4 -118.2 144.7 15.5 29.0 33.0
33621CBS A 64 ASN E . . . . . . + A D D . ? -0.999 24.3 150.7 -127.3 125.5 13.8 29.1 36.4
33631CBS A 65 PHE E . . . . . . - A D D . ? -0.993 39.0 -139.6 -152.9 157.3 11.0 26.7 37.2
33641CBS A 66 LYS E . > . . . . - A D D . ? -0.953 44.4 -103.7 -110.1 137.5 9.2 24.7 39.9
33651CBS A 67 VAL T . 3 . . . S + . . . . ? -0.381 107.1 20.5 -59.3 133.9 8.2 21.1 39.0
33661CBS A 68 GLY T . 3 . . . S + . . . . ? 0.424 102.9 100.6 86.8 1.5 4.5 21.0 38.2
33671CBS A 69 GLU S . < . . . S - . . . . ? -0.976 75.1 -115.1 -123.9 131.6 4.1 24.7 37.5
33681CBS A 70 GLU . . . . . . . + . . . . ? -0.305 39.9 169.7 -64.6 143.3 3.9 26.1 34.0
33691CBS A 71 PHE E . . . . . . - A E E . ? -0.909 30.6 -111.6 -146.0 170.9 6.7 28.5 32.8
33701CBS A 72 GLU E . . . . . . + A E E . ? -0.902 45.7 136.3 -112.0 134.1 7.8 30.1 29.6
33711CBS A 73 GLU E . . . . . . - A E E . ? -0.677 45.0 -94.5 -144.5 -155.8 11.1 29.3 27.8
33721CBS A 74 GLN E . . . . . . - A E E . ? -0.967 28.4 -112.5 -129.5 151.9 12.2 28.7 24.2
33731CBS A 75 THR . . > . . . . - . . . . ? -0.226 47.7 -92.8 -63.2 170.1 12.7 25.7 22.0
33741CBS A 76 VAL T . 3 . . . S + . . . . ? 0.832 129.4 50.4 -57.6 -34.3 16.3 24.7 21.0
33751CBS A 77 ASP T . 3 . . . S - . . . . ? 0.304 126.6 -98.8 -92.9 6.2 15.9 26.8 17.8
33761CBS A 78 GLY S . < . . . S + . . . . ? 0.581 71.5 141.9 97.1 17.1 14.6 29.8 19.7
33771CBS A 79 ARG . . . . . . . - . . . . ? -0.740 55.6 -109.6 -92.1 131.2 10.8 29.8 19.5
33781CBS A 80 PRO E . . . . . . + A F E . ? -0.342 47.3 169.9 -56.7 137.7 8.8 30.9 22.6
33791CBS A 81 CYS E . . . . . . - A F E F ? -0.960 37.6 -118.7 -145.5 159.5 6.9 28.1 24.3
33801CBS A 82 LYS E . . . . . . - A F E F ? -0.892 38.0 -164.1 -97.0 130.4 5.0 27.2 27.5
33811CBS A 83 SER E . . . . . . - A F E F ? -0.876 16.8 -170.9 -122.1 149.5 6.7 24.4 29.4
33821CBS A 84 LEU E . . . . . . - A F . F ? -0.951 10.7 -158.6 -142.3 116.9 5.6 22.0 32.2
33831CBS A 85 VAL E . . . . . . + A F . F ? -0.807 13.9 175.8 -97.0 136.6 8.0 19.8 34.0
33841CBS A 86 LYS E . . . . . . - A F . F ? -0.957 37.8 -105.8 -131.0 156.2 6.9 16.6 35.9
33851CBS A 87 TRP E . . . . . . - A F . F ? -0.748 28.6 -178.5 -77.2 109.8 8.8 13.8 37.7
33861CBS A 88 GLU E . . . . . S - A F . . ? 0.898 77.6 -16.5 -67.9 -44.2 8.6 10.8 35.4
33871CBS A 89 SER E . > . . . S - A F . F ? -0.883 89.1 -77.0 -148.9 179.3 10.4 9.0 38.2
33881CBS A 90 GLU T . 3 . . . S + . . . . ? 0.832 130.3 26.4 -52.4 -38.7 12.5 9.8 41.3
33891CBS A 91 ASN T . 3 . . . S + . . . . ? 0.246 112.1 74.9 -111.7 14.1 15.6 10.7 39.3
33901CBS A 92 LYS E . < . . . . - A G F G ? -0.979 53.5 -168.1 -137.3 119.2 14.0 11.8 35.9
33911CBS A 93 MET E . . . . . . - A G F G ? -0.830 8.3 -160.7 -102.7 144.3 12.2 15.0 35.0
33921CBS A 94 VAL E . . . . . . - A G F G ? -0.992 1.0 -158.4 -126.6 137.1 10.2 15.3 31.7
33931CBS A 95 CYS E . . . . . . - A G F G ? -0.966 1.9 -160.4 -120.1 124.7 9.2 18.6 30.1
33941CBS A 96 GLU E . . . . . . - A G F G ? -0.862 15.1 -156.7 -100.3 135.1 6.4 19.0 27.6
33951CBS A 97 GLN E . . . . . . - A G F . ? -0.893 10.2 -168.8 -116.7 142.1 6.5 22.1 25.4
33961CBS A 98 LYS E . . . . . . - A G F . ? -0.997 27.4 -118.4 -130.1 127.8 3.7 24.0 23.6
33971CBS A 99 LEU E . . . . . . - A G F . ? -0.383 10.6 -151.5 -65.3 136.8 4.3 26.7 21.1
33981CBS A 100 LEU S . . . . . S + . . . . ? 0.882 83.1 18.2 -71.8 -43.3 2.9 30.2 21.9
33991CBS A 101 LYS S . . . . . S - . . . . ? -0.970 114.0 -6.0 -129.5 146.4 2.5 31.1 18.3
34001CBS A 102 GLY S . . . . . S - . . . . ? -0.157 77.5 -78.8 76.5 -165.4 2.4 29.1 15.1
34011CBS A 103 GLU . . . . . . . + . . . . ? -0.853 51.4 130.6 -135.5 169.0 3.0 25.4 14.5
34021CBS A 104 GLY . . . . . . . - . . . . ? -0.961 57.3 -26.8 167.4 -178.8 6.0 23.1 14.2
34031CBS A 105 PRO . . . . . . . - . . . . ? -0.157 67.3 -102.8 -52.8 150.8 7.3 19.7 15.4
34041CBS A 106 LYS . . . . . . . - . . . . ? -0.660 47.8 -165.0 -74.4 127.1 6.3 18.4 18.9
34051CBS A 107 THR E . . . . . . + A H . H ? -0.894 19.1 154.5 -121.3 150.9 9.2 19.1 21.2
34061CBS A 108 SER E . . . . . . - A H G H ? -0.945 19.4 -152.3 -153.6 171.1 10.2 17.9 24.7
34071CBS A 109 TRP E . . . . . . - A H G H ? -0.972 4.2 -162.3 -145.6 158.5 13.2 17.4 26.9
34081CBS A 110 THR E . . . . . . - A H G H ? -0.978 2.1 -164.3 -134.9 150.9 14.2 15.2 29.8
34091CBS A 111 ARG E . . . . . . + A H G H ? -0.996 15.8 174.3 -135.0 131.5 16.9 15.3 32.4
34101CBS A 112 GLU E . . . . . . - A H G H ? -0.997 28.4 -136.5 -140.6 141.9 18.0 12.3 34.5
34111CBS A 113 LEU E . . . . . . - A H . H ? -0.876 30.3 -145.7 -94.4 124.5 20.6 11.5 37.1
34121CBS A 114 THR . . > . . . . - . . . . ? -0.416 25.3 -104.8 -89.9 168.6 22.1 8.0 36.4
34131CBS A 115 ASN T . 3 . . . S + . . . . ? 0.704 118.5 57.5 -66.5 -21.0 23.4 5.5 38.9
34141CBS A 116 ASP T . 3 . . . S - . . . . ? 0.366 122.7 -99.7 -91.5 1.7 27.0 6.4 38.1
34151CBS A 117 GLY S . < . . . S + . . . . ? 0.487 82.3 123.9 95.0 8.4 26.6 10.1 39.0
34161CBS A 118 GLU . . . . . . . - . . . . ? -0.375 55.2 -126.9 -95.9 173.1 26.2 11.4 35.4
34171CBS A 119 LEU E . . . . . . - A I H I ? -0.991 14.4 -159.2 -125.0 125.7 23.4 13.5 33.9
34181CBS A 120 ILE E . . . . . . - A I H I ? -0.952 6.1 -169.8 -105.7 124.0 21.6 12.6 30.7
34191CBS A 121 LEU E . . . . . . - A I H I ? -0.943 4.1 -172.1 -103.7 129.9 19.8 15.3 28.7
34201CBS A 122 THR E . . . . . . - A I H I ? -0.962 4.4 -170.0 -117.1 145.2 17.5 14.2 25.9
34211CBS A 123 MET E . . . . . . - A I H I ? -0.999 9.9 -164.1 -128.9 132.9 15.8 16.7 23.5
34221CBS A 124 THR E . . . . . . - A I H I ? -0.915 17.9 -179.5 -122.3 143.3 13.1 15.5 21.1
34231CBS A 125 ALA E . > . . . S - A I H I ? -0.933 72.5 -52.9 -138.4 116.1 11.6 16.9 17.9
34241CBS A 126 ASP T . 3 . . . S - . . . . ? -0.386 125.0 -17.0 48.4 -114.8 8.9 14.7 16.5
34251CBS A 127 ASP T . 3 . . . S + . . . . ? 0.613 115.6 98.4 -90.4 -12.6 10.6 11.3 16.2
34261CBS A 128 VAL E . < . . . . - A J . I ? -0.614 53.0 -164.9 -90.0 132.7 14.2 12.5 16.5
34271CBS A 129 VAL E . . . . . . - A J . I ? -0.968 7.9 -160.0 -122.2 127.7 16.1 12.3 19.8
34281CBS A 130 CYS E . . . . . . - A J . I ? -0.902 11.3 -160.6 -103.8 130.3 19.3 14.0 20.8
34291CBS A 131 THR E . . . . . . + A J B I ? -0.959 10.5 179.0 -116.5 126.7 21.2 12.5 23.7
34301CBS A 132 ARG E . . . . . . - A J B I ? -0.992 9.6 -159.6 -129.2 136.4 23.8 14.5 25.7
34311CBS A 133 VAL E . . . . . . - A J B I ? -0.959 11.2 -177.0 -122.7 135.1 25.8 13.1 28.7
34321CBS A 134 TYR E . . . . . . - A J B I ? -0.889 13.2 -165.2 -129.1 158.8 27.5 15.2 31.3
34331CBS A 135 VAL E . . . . . . - A J B . ? -0.949 40.7 -92.0 -135.4 151.8 29.7 14.8 34.4
34341CBS A 136 ARG E . . . . . . . A J B . ? -0.423 . . -66.1 143.8 30.4 17.4 37.1
34351CBS A 137 GLU . . . . . . . . . . . . ? -0.308 . . -61.6 . 33.6 19.4 36.4
3436#
3437loop_
3438_struct_conf_type.id
3439_struct_conf_type.criteria
3440STRN DSSP
3441BEND DSSP
3442HELX_RH_AL_P DSSP
3443TURN_TY1_P DSSP
3444#
3445loop_
3446_struct_conf.id
3447_struct_conf.conf_type_id
3448_struct_conf.beg_label_comp_id
3449_struct_conf.beg_label_asym_id
3450_struct_conf.beg_label_seq_id
3451_struct_conf.pdbx_beg_PDB_ins_code
3452_struct_conf.end_label_comp_id
3453_struct_conf.end_label_asym_id
3454_struct_conf.end_label_seq_id
3455_struct_conf.pdbx_end_PDB_ins_code
3456_struct_conf.beg_auth_comp_id
3457_struct_conf.beg_auth_asym_id
3458_struct_conf.beg_auth_seq_id
3459_struct_conf.end_auth_comp_id
3460_struct_conf.end_auth_asym_id
3461_struct_conf.end_auth_seq_id
3462STRN1 STRN GLY A 5 ? GLU A 13 ? GLY A 5 GLU A 13
3463BEND1 BEND ASN A 14 ? ASN A 14 ? ASN A 14 ASN A 14
3464HELX_RH_AL_P1 HELX_RH_AL_P PHE A 15 ? VAL A 21 ? PHE A 15 VAL A 21
3465TURN_TY1_P1 TURN_TY1_P LEU A 22 ? GLY A 23 ? LEU A 22 GLY A 23
3466HELX_RH_AL_P2 HELX_RH_AL_P VAL A 26 ? ALA A 36 ? VAL A 26 ALA A 36
3467TURN_TY1_P2 TURN_TY1_P SER A 37 ? SER A 37 ? SER A 37 SER A 37
3468BEND2 BEND LYS A 38 ? LYS A 38 ? LYS A 38 LYS A 38
3469STRN2 STRN ALA A 40 ? GLU A 46 ? ALA A 40 GLU A 46
3470TURN_TY1_P3 TURN_TY1_P GLY A 47 ? ASP A 48 ? GLY A 47 ASP A 48
3471STRN3 STRN THR A 49 ? SER A 55 ? THR A 49 SER A 55
3472BEND3 BEND THR A 57 ? VAL A 58 ? THR A 57 VAL A 58
3473STRN4 STRN THR A 60 ? LYS A 66 ? THR A 60 LYS A 66
3474TURN_TY1_P4 TURN_TY1_P VAL A 67 ? GLY A 68 ? VAL A 67 GLY A 68
3475BEND4 BEND GLU A 69 ? GLU A 69 ? GLU A 69 GLU A 69
3476STRN5 STRN PHE A 71 ? GLN A 74 ? PHE A 71 GLN A 74
3477TURN_TY1_P5 TURN_TY1_P VAL A 76 ? ASP A 77 ? VAL A 76 ASP A 77
3478BEND5 BEND GLY A 78 ? GLY A 78 ? GLY A 78 GLY A 78
3479STRN6 STRN PRO A 80 ? SER A 89 ? PRO A 80 SER A 89
3480TURN_TY1_P6 TURN_TY1_P GLU A 90 ? ASN A 91 ? GLU A 90 ASN A 91
3481STRN7 STRN LYS A 92 ? LEU A 99 ? LYS A 92 LEU A 99
3482BEND6 BEND LEU A 100 ? GLY A 102 ? LEU A 100 GLY A 102
3483STRN8 STRN THR A 107 ? LEU A 113 ? THR A 107 LEU A 113
3484TURN_TY1_P7 TURN_TY1_P ASN A 115 ? ASP A 116 ? ASN A 115 ASP A 116
3485BEND7 BEND GLY A 117 ? GLY A 117 ? GLY A 117 GLY A 117
3486STRN9 STRN LEU A 119 ? ALA A 125 ? LEU A 119 ALA A 125
3487TURN_TY1_P8 TURN_TY1_P ASP A 126 ? ASP A 127 ? ASP A 126 ASP A 127
3488STRN10 STRN VAL A 128 ? ARG A 136 ? VAL A 128 ARG A 136
3489#