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_pdbx_struct_sheet_hbond.range_2_auth_comp_id
_pdbx_struct_sheet_hbond.range_2_auth_asym_id
_pdbx_struct_sheet_hbond.range_2_auth_seq_id
A 1 2 N VAL A 159 ? N VAL A 159 O ILE A 264 ? O ILE A 264
A 2 3 O LEU A 265 ? O LEU A 265 N VAL A 27 ? N VAL A 27
A 3 4 N VAL A 30 ? N VAL A 30 O ILE A 295 ? O ILE A 295
A 4 5 N ASP A 296 ? N ASP A 296 O ILE A 350 ? O ILE A 350
B 1 2 N ASN A 66 ? N ASN A 66 O PHE A 230 ? O PHE A 230
C 1 2 N LYS A 80 ? N LYS A 80 O LYS A 110 ? O LYS A 110
C 2 3 N VAL A 109 ? N VAL A 109 O VAL A 125 ? O VAL A 125
C 3 4 N VAL A 124 ? N VAL A 124 O ILE A 134 ? O ILE A 134
C 4 5 N ARG A 135 ? N ARG A 135 O PHE A 238 ? O PHE A 238
C 5 6 N GLY A 241 ? N GLY A 241 O THR A 250 ? O THR A 250
#
_struct_site.id AC1
_struct_site.pdbx_evidence_code Software
_struct_site.pdbx_auth_asym_id ?
_struct_site.pdbx_auth_comp_id ?
_struct_site.pdbx_auth_seq_id ?
_struct_site.pdbx_auth_ins_code ?
_struct_site.pdbx_num_residues 9
_struct_site.details 'BINDING SITE FOR RESIDUE SO4 A 2847'
#
loop_
_struct_site_gen.id
_struct_site_gen.site_id
_struct_site_gen.pdbx_num_res
_struct_site_gen.label_comp_id
_struct_site_gen.label_asym_id
_struct_site_gen.label_seq_id
_struct_site_gen.pdbx_auth_ins_code
_struct_site_gen.auth_comp_id
_struct_site_gen.auth_asym_id
_struct_site_gen.auth_seq_id
_struct_site_gen.label_atom_id
_struct_site_gen.label_alt_id
_struct_site_gen.symmetry
_struct_site_gen.details
1 AC1 9 SER A 32 ? SER A 32 . ? 1_555 ?
2 AC1 9 GLY A 34 ? GLY A 34 . ? 1_555 ?
3 AC1 9 SER A 35 ? SER A 35 . ? 1_555 ?
4 AC1 9 GLY A 36 ? GLY A 36 . ? 1_555 ?
5 AC1 9 LYS A 37 ? LYS A 37 . ? 1_555 ?
6 AC1 9 SER A 38 ? SER A 38 . ? 1_555 ?
7 AC1 9 ARG A 309 ? ARG A 309 . ? 1_555 ?
8 AC1 9 HOH C . ? HOH A 2857 . ? 1_555 ?
9 AC1 9 HOH C . ? HOH A 3005 . ? 1_555 ?
#
_database_PDB_matrix.entry_id 2GAA
_database_PDB_matrix.origx[1][1] 1.000000
_database_PDB_matrix.origx[1][2] 0.000000
_database_PDB_matrix.origx[1][3] 0.000000
_database_PDB_matrix.origx[2][1] 0.000000
_database_PDB_matrix.origx[2][2] 1.000000
_database_PDB_matrix.origx[2][3] 0.000000
_database_PDB_matrix.origx[3][1] 0.000000
_database_PDB_matrix.origx[3][2] 0.000000
_database_PDB_matrix.origx[3][3] 1.000000
_database_PDB_matrix.origx_vector[1] 0.00000
_database_PDB_matrix.origx_vector[2] 0.00000
_database_PDB_matrix.origx_vector[3] 0.00000
#
_atom_sites.entry_id 2GAA
_atom_sites.fract_transf_matrix[1][1] 0.007421
_atom_sites.fract_transf_matrix[1][2] 0.004284
_atom_sites.fract_transf_matrix[1][3] 0.000000
_atom_sites.fract_transf_matrix[2][1] 0.000000
_atom_sites.fract_transf_matrix[2][2] 0.008569
_atom_sites.fract_transf_matrix[2][3] 0.000000
_atom_sites.fract_transf_matrix[3][1] 0.000000
_atom_sites.fract_transf_matrix[3][2] 0.000000
_atom_sites.fract_transf_matrix[3][3] 0.020543
_atom_sites.fract_transf_vector[1] 0.00000
_atom_sites.fract_transf_vector[2] 0.00000
_atom_sites.fract_transf_vector[3] 0.00000
#
loop_
_atom_type.symbol
C
N
O
S
#
loop_
_atom_site.group_PDB
_atom_site.id
_atom_site.type_symbol
_atom_site.label_atom_id
_atom_site.label_alt_id
_atom_site.label_comp_id
_atom_site.label_asym_id
_atom_site.label_entity_id
_atom_site.label_seq_id
_atom_site.pdbx_PDB_ins_code
_atom_site.Cartn_x
_atom_site.Cartn_y
_atom_site.Cartn_z
_atom_site.occupancy
_atom_site.B_iso_or_equiv
_atom_site.pdbx_formal_charge
_atom_site.auth_seq_id
_atom_site.auth_comp_id
_atom_site.auth_asym_id
_atom_site.auth_atom_id
_atom_site.pdbx_PDB_model_num
ATOM 1 N N . VAL A 1 2 ? 20.864 -2.201 2.638 1.00 37.70 ? 2 VAL A N 1
ATOM 2 C CA . VAL A 1 2 ? 20.651 -2.256 4.114 1.00 36.53 ? 2 VAL A CA 1
ATOM 3 C C . VAL A 1 2 ? 19.173 -2.064 4.445 1.00 35.10 ? 2 VAL A C 1
ATOM 4 O O . VAL A 1 2 ? 18.454 -1.350 3.745 1.00 37.24 ? 2 VAL A O 1
ATOM 5 C CB . VAL A 1 2 ? 21.478 -1.158 4.838 1.00 36.80 ? 2 VAL A CB 1
ATOM 6 C CG1 . VAL A 1 2 ? 21.004 0.222 4.407 1.00 34.55 ? 2 VAL A CG1 1
ATOM 7 C CG2 . VAL A 1 2 ? 21.363 -1.322 6.345 1.00 35.24 ? 2 VAL A CG2 1
ATOM 8 N N . ASP A 1 3 ? 18.725 -2.715 5.510 1.00 34.98 ? 3 ASP A N 1
ATOM 9 C CA . ASP A 1 3 ? 17.336 -2.615 5.945 1.00 34.72 ? 3 ASP A CA 1
ATOM 10 C C . ASP A 1 3 ? 17.249 -1.492 6.982 1.00 32.91 ? 3 ASP A C 1
ATOM 11 O O . ASP A 1 3 ? 17.628 -1.682 8.136 1.00 32.17 ? 3 ASP A O 1
ATOM 12 C CB . ASP A 1 3 ? 16.898 -3.936 6.575 1.00 36.71 ? 3 ASP A CB 1
ATOM 13 C CG . ASP A 1 3 ? 15.397 -4.038 6.731 1.00 38.31 ? 3 ASP A CG 1
ATOM 14 O OD1 . ASP A 1 3 ? 14.777 -3.088 7.247 1.00 42.22 ? 3 ASP A OD1 1
ATOM 15 O OD2 . ASP A 1 3 ? 14.838 -5.080 6.338 1.00 42.12 ? 3 ASP A OD2 1
ATOM 16 N N . THR A 1 4 ? 16.751 -0.330 6.572 1.00 31.80 ? 4 THR A N 1
ATOM 17 C CA . THR A 1 4 ? 16.655 0.811 7.477 1.00 31.89 ? 4 THR A CA 1
ATOM 18 C C . THR A 1 4 ? 15.604 0.650 8.573 1.00 30.07 ? 4 THR A C 1
ATOM 19 O O . THR A 1 4 ? 15.720 1.251 9.640 1.00 27.93 ? 4 THR A O 1
ATOM 20 C CB . THR A 1 4 ? 16.390 2.116 6.699 1.00 32.58 ? 4 THR A CB 1
ATOM 21 O OG1 . THR A 1 4 ? 15.129 2.032 6.025 1.00 34.67 ? 4 THR A OG1 1
ATOM 22 C CG2 . THR A 1 4 ? 17.489 2.347 5.673 1.00 33.72 ? 4 THR A CG2 1
ATOM 23 N N . HIS A 1 5 ? 14.578 -0.156 8.324 1.00 29.53 ? 5 HIS A N 1
ATOM 24 C CA . HIS A 1 5 ? 13.565 -0.362 9.350 1.00 29.09 ? 5 HIS A CA 1
ATOM 25 C C . HIS A 1 5 ? 14.157 -1.225 10.451 1.00 28.81 ? 5 HIS A C 1
ATOM 26 O O . HIS A 1 5 ? 13.807 -1.084 11.623 1.00 29.00 ? 5 HIS A O 1
ATOM 27 C CB . HIS A 1 5 ? 12.314 -1.022 8.768 1.00 29.80 ? 5 HIS A CB 1
ATOM 28 C CG . HIS A 1 5 ? 11.480 -0.096 7.942 1.00 30.10 ? 5 HIS A CG 1
ATOM 29 N ND1 . HIS A 1 5 ? 11.807 0.246 6.647 1.00 30.44 ? 5 HIS A ND1 1
ATOM 30 C CD2 . HIS A 1 5 ? 10.351 0.591 8.239 1.00 30.58 ? 5 HIS A CD2 1
ATOM 31 C CE1 . HIS A 1 5 ? 10.915 1.103 6.182 1.00 31.63 ? 5 HIS A CE1 1
ATOM 32 N NE2 . HIS A 1 5 ? 10.021 1.329 7.127 1.00 31.58 ? 5 HIS A NE2 1
ATOM 33 N N . LYS A 1 6 ? 15.064 -2.118 10.070 1.00 28.73 ? 6 LYS A N 1
ATOM 34 C CA . LYS A 1 6 ? 15.714 -2.982 11.045 1.00 27.94 ? 6 LYS A CA 1
ATOM 35 C C . LYS A 1 6 ? 16.684 -2.137 11.870 1.00 25.58 ? 6 LYS A C 1
ATOM 36 O O . LYS A 1 6 ? 16.854 -2.373 13.063 1.00 25.60 ? 6 LYS A O 1
ATOM 37 C CB . LYS A 1 6 ? 16.468 -4.116 10.347 1.00 30.10 ? 6 LYS A CB 1
ATOM 38 C CG . LYS A 1 6 ? 17.317 -4.969 11.288 1.00 34.68 ? 6 LYS A CG 1
ATOM 39 C CD . LYS A 1 6 ? 16.473 -5.607 12.387 1.00 38.77 ? 6 LYS A CD 1
ATOM 40 C CE . LYS A 1 6 ? 17.345 -6.313 13.420 1.00 39.55 ? 6 LYS A CE 1
ATOM 41 N NZ . LYS A 1 6 ? 18.167 -7.393 12.808 1.00 44.52 ? 6 LYS A NZ 1
ATOM 42 N N . LEU A 1 7 ? 17.327 -1.161 11.232 1.00 25.04 ? 7 LEU A N 1
ATOM 43 C CA . LEU A 1 7 ? 18.250 -0.290 11.956 1.00 23.60 ? 7 LEU A CA 1
ATOM 44 C C . LEU A 1 7 ? 17.419 0.486 12.962 1.00 21.28 ? 7 LEU A C 1
ATOM 45 O O . LEU A 1 7 ? 17.810 0.651 14.108 1.00 21.68 ? 7 LEU A O 1
ATOM 46 C CB . LEU A 1 7 ? 18.952 0.690 11.016 1.00 25.72 ? 7 LEU A CB 1
ATOM 47 C CG . LEU A 1 7 ? 20.021 0.137 10.072 1.00 26.98 ? 7 LEU A CG 1
ATOM 48 C CD1 . LEU A 1 7 ? 20.736 1.293 9.403 1.00 27.98 ? 7 LEU A CD1 1
ATOM 49 C CD2 . LEU A 1 7 ? 21.012 -0.708 10.847 1.00 29.12 ? 7 LEU A CD2 1
ATOM 50 N N . ALA A 1 8 ? 16.263 0.957 12.514 1.00 20.13 ? 8 ALA A N 1
ATOM 51 C CA . ALA A 1 8 ? 15.356 1.696 13.377 1.00 20.65 ? 8 ALA A CA 1
ATOM 52 C C . ALA A 1 8 ? 14.988 0.824 14.577 1.00 18.91 ? 8 ALA A C 1
ATOM 53 O O . ALA A 1 8 ? 14.958 1.298 15.706 1.00 17.30 ? 8 ALA A O 1
ATOM 54 C CB . ALA A 1 8 ? 14.101 2.092 12.604 1.00 18.12 ? 8 ALA A CB 1
ATOM 55 N N . ASP A 1 9 ? 14.718 -0.454 14.331 1.00 21.05 ? 9 ASP A N 1
ATOM 56 C CA . ASP A 1 9 ? 14.360 -1.368 15.415 1.00 22.26 ? 9 ASP A CA 1
ATOM 57 C C . ASP A 1 9 ? 15.513 -1.561 16.388 1.00 21.86 ? 9 ASP A C 1
ATOM 58 O O . ASP A 1 9 ? 15.302 -1.632 17.596 1.00 18.77 ? 9 ASP A O 1
ATOM 59 C CB . ASP A 1 9 ? 13.930 -2.735 14.872 1.00 26.17 ? 9 ASP A CB 1
ATOM 60 C CG . ASP A 1 9 ? 12.561 -2.701 14.205 1.00 28.74 ? 9 ASP A CG 1
ATOM 61 O OD1 . ASP A 1 9 ? 11.800 -1.728 14.410 1.00 27.75 ? 9 ASP A OD1 1
ATOM 62 O OD2 . ASP A 1 9 ? 12.246 -3.666 13.481 1.00 33.68 ? 9 ASP A OD2 1
ATOM 63 N N . ASP A 1 10 ? 16.732 -1.653 15.867 1.00 21.27 ? 10 ASP A N 1
ATOM 64 C CA . ASP A 1 10 ? 17.884 -1.826 16.739 1.00 21.60 ? 10 ASP A CA 1
ATOM 65 C C . ASP A 1 10 ? 18.143 -0.570 17.566 1.00 19.92 ? 10 ASP A C 1
ATOM 66 O O . ASP A 1 10 ? 18.533 -0.659 18.729 1.00 18.54 ? 10 ASP A O 1
ATOM 67 C CB . ASP A 1 10 ? 19.129 -2.200 15.926 1.00 25.15 ? 10 ASP A CB 1
ATOM 68 C CG . ASP A 1 10 ? 19.000 -3.566 15.259 1.00 28.76 ? 10 ASP A CG 1
ATOM 69 O OD1 . ASP A 1 10 ? 18.417 -4.482 15.875 1.00 31.77 ? 10 ASP A OD1 1
ATOM 70 O OD2 . ASP A 1 10 ? 19.487 -3.728 14.127 1.00 29.95 ? 10 ASP A OD2 1
ATOM 71 N N . VAL A 1 11 ? 17.910 0.598 16.971 1.00 19.02 ? 11 VAL A N 1
ATOM 72 C CA . VAL A 1 11 ? 18.113 1.864 17.675 1.00 18.55 ? 11 VAL A CA 1
ATOM 73 C C . VAL A 1 11 ? 17.117 2.007 18.824 1.00 18.28 ? 11 VAL A C 1
ATOM 74 O O . VAL A 1 11 ? 17.482 2.418 19.930 1.00 17.50 ? 11 VAL A O 1
ATOM 75 C CB . VAL A 1 11 ? 17.949 3.063 16.725 1.00 18.83 ? 11 VAL A CB 1
ATOM 76 C CG1 . VAL A 1 11 ? 18.005 4.364 17.514 1.00 19.55 ? 11 VAL A CG1 1
ATOM 77 C CG2 . VAL A 1 11 ? 19.045 3.041 15.675 1.00 19.35 ? 11 VAL A CG2 1
ATOM 78 N N . LEU A 1 12 ? 15.858 1.667 18.559 1.00 17.45 ? 12 LEU A N 1
ATOM 79 C CA . LEU A 1 12 ? 14.827 1.753 19.582 1.00 19.48 ? 12 LEU A CA 1
ATOM 80 C C . LEU A 1 12 ? 15.090 0.738 20.687 1.00 19.28 ? 12 LEU A C 1
ATOM 81 O O . LEU A 1 12 ? 14.778 0.984 21.848 1.00 19.80 ? 12 LEU A O 1
ATOM 82 C CB . LEU A 1 12 ? 13.443 1.526 18.969 1.00 19.04 ? 12 LEU A CB 1
ATOM 83 C CG . LEU A 1 12 ? 12.971 2.637 18.027 1.00 21.93 ? 12 LEU A CG 1
ATOM 84 C CD1 . LEU A 1 12 ? 11.597 2.296 17.485 1.00 21.73 ? 12 LEU A CD1 1
ATOM 85 C CD2 . LEU A 1 12 ? 12.935 3.966 18.769 1.00 21.79 ? 12 LEU A CD2 1
ATOM 86 N N . GLN A 1 13 ? 15.665 -0.405 20.326 1.00 20.68 ? 13 GLN A N 1
ATOM 87 C CA . GLN A 1 13 ? 15.963 -1.418 21.326 1.00 21.51 ? 13 GLN A CA 1
ATOM 88 C C . GLN A 1 13 ? 17.042 -0.923 22.286 1.00 20.94 ? 13 GLN A C 1
ATOM 89 O O . GLN A 1 13 ? 16.956 -1.150 23.492 1.00 19.81 ? 13 GLN A O 1
ATOM 90 C CB . GLN A 1 13 ? 16.414 -2.721 20.663 1.00 23.56 ? 13 GLN A CB 1
ATOM 91 C CG . GLN A 1 13 ? 16.854 -3.775 21.665 1.00 28.21 ? 13 GLN A CG 1
ATOM 92 C CD . GLN A 1 13 ? 16.979 -5.151 21.048 1.00 34.22 ? 13 GLN A CD 1
ATOM 93 O OE1 . GLN A 1 13 ? 17.726 -5.349 20.087 1.00 39.47 ? 13 GLN A OE1 1
ATOM 94 N NE2 . GLN A 1 13 ? 16.245 -6.113 21.597 1.00 36.88 ? 13 GLN A NE2 1
ATOM 95 N N . LEU A 1 14 ? 18.061 -0.250 21.756 1.00 20.43 ? 14 LEU A N 1
ATOM 96 C CA . LEU A 1 14 ? 19.118 0.274 22.616 1.00 19.68 ? 14 LEU A CA 1
ATOM 97 C C . LEU A 1 14 ? 18.561 1.390 23.485 1.00 17.56 ? 14 LEU A C 1
ATOM 98 O O . LEU A 1 14 ? 18.808 1.439 24.685 1.00 18.94 ? 14 LEU A O 1
ATOM 99 C CB . LEU A 1 14 ? 20.286 0.821 21.794 1.00 20.58 ? 14 LEU A CB 1
ATOM 100 C CG . LEU A 1 14 ? 21.439 1.360 22.660 1.00 22.39 ? 14 LEU A CG 1
ATOM 101 C CD1 . LEU A 1 14 ? 21.941 0.257 23.588 1.00 21.55 ? 14 LEU A CD1 1
ATOM 102 C CD2 . LEU A 1 14 ? 22.569 1.855 21.777 1.00 21.71 ? 14 LEU A CD2 1
ATOM 103 N N . LEU A 1 15 ? 17.809 2.296 22.873 1.00 16.34 ? 15 LEU A N 1
ATOM 104 C CA . LEU A 1 15 ? 17.223 3.400 23.619 1.00 16.37 ? 15 LEU A CA 1
ATOM 105 C C . LEU A 1 15 ? 16.365 2.870 24.764 1.00 15.78 ? 15 LEU A C 1
ATOM 106 O O . LEU A 1 15 ? 16.446 3.358 25.895 1.00 16.43 ? 15 LEU A O 1
ATOM 107 C CB . LEU A 1 15 ? 16.366 4.273 22.695 1.00 16.04 ? 15 LEU A CB 1
ATOM 108 C CG . LEU A 1 15 ? 15.657 5.460 23.350 1.00 18.52 ? 15 LEU A CG 1
ATOM 109 C CD1 . LEU A 1 15 ? 16.669 6.337 24.073 1.00 17.06 ? 15 LEU A CD1 1
ATOM 110 C CD2 . LEU A 1 15 ? 14.913 6.270 22.292 1.00 19.66 ? 15 LEU A CD2 1
ATOM 111 N N . ASP A 1 16 ? 15.539 1.872 24.465 1.00 15.59 ? 16 ASP A N 1
ATOM 112 C CA . ASP A 1 16 ? 14.674 1.288 25.484 1.00 17.68 ? 16 ASP A CA 1
ATOM 113 C C . ASP A 1 16 ? 15.506 0.674 26.602 1.00 18.44 ? 16 ASP A C 1
ATOM 114 O O . ASP A 1 16 ? 15.208 0.854 27.776 1.00 17.41 ? 16 ASP A O 1
ATOM 115 C CB . ASP A 1 16 ? 13.772 0.212 24.877 1.00 17.15 ? 16 ASP A CB 1
ATOM 116 C CG . ASP A 1 16 ? 12.776 -0.326 25.877 1.00 19.26 ? 16 ASP A CG 1
ATOM 117 O OD1 . ASP A 1 16 ? 11.881 0.437 26.291 1.00 16.49 ? 16 ASP A OD1 1
ATOM 118 O OD2 . ASP A 1 16 ? 12.898 -1.505 26.260 1.00 19.39 ? 16 ASP A OD2 1
ATOM 119 N N . ASN A 1 17 ? 16.551 -0.055 26.229 1.00 21.55 ? 17 ASN A N 1
ATOM 120 C CA . ASN A 1 17 ? 17.427 -0.687 27.209 1.00 24.82 ? 17 ASN A CA 1
ATOM 121 C C . ASN A 1 17 ? 18.173 0.333 28.075 1.00 24.18 ? 17 ASN A C 1
ATOM 122 O O . ASN A 1 17 ? 18.468 0.066 29.237 1.00 23.01 ? 17 ASN A O 1
ATOM 123 C CB . ASN A 1 17 ? 18.446 -1.585 26.498 1.00 29.08 ? 17 ASN A CB 1
ATOM 124 C CG . ASN A 1 17 ? 17.959 -3.019 26.337 1.00 36.29 ? 17 ASN A CG 1
ATOM 125 O OD1 . ASN A 1 17 ? 18.382 -3.731 25.419 1.00 38.41 ? 17 ASN A OD1 1
ATOM 126 N ND2 . ASN A 1 17 ? 17.079 -3.456 27.238 1.00 36.86 ? 17 ASN A ND2 1
ATOM 127 N N . ARG A 1 18 ? 18.458 1.503 27.512 1.00 22.14 ? 18 ARG A N 1
ATOM 128 C CA . ARG A 1 18 ? 19.204 2.538 28.225 1.00 21.11 ? 18 ARG A CA 1
ATOM 129 C C . ARG A 1 18 ? 18.347 3.695 28.725 1.00 20.28 ? 18 ARG A C 1
ATOM 130 O O . ARG A 1 18 ? 18.871 4.697 29.206 1.00 20.05 ? 18 ARG A O 1
ATOM 131 C CB . ARG A 1 18 ? 20.307 3.086 27.308 1.00 19.04 ? 18 ARG A CB 1
ATOM 132 C CG . ARG A 1 18 ? 21.289 2.029 26.802 1.00 20.86 ? 18 ARG A CG 1
ATOM 133 C CD . ARG A 1 18 ? 22.124 1.445 27.934 1.00 17.22 ? 18 ARG A CD 1
ATOM 134 N NE . ARG A 1 18 ? 22.896 2.489 28.598 1.00 21.54 ? 18 ARG A NE 1
ATOM 135 C CZ . ARG A 1 18 ? 23.779 2.280 29.570 1.00 22.00 ? 18 ARG A CZ 1
ATOM 136 N NH1 . ARG A 1 18 ? 24.015 1.051 30.006 1.00 25.82 ? 18 ARG A NH1 1
ATOM 137 N NH2 . ARG A 1 18 ? 24.432 3.306 30.105 1.00 23.48 ? 18 ARG A NH2 1
ATOM 138 N N . ILE A 1 19 ? 17.032 3.541 28.630 1.00 21.57 ? 19 ILE A N 1
ATOM 139 C CA . ILE A 1 19 ? 16.091 4.578 29.026 1.00 22.52 ? 19 ILE A CA 1
ATOM 140 C C . ILE A 1 19 ? 16.366 5.218 30.388 1.00 22.98 ? 19 ILE A C 1
ATOM 141 O O . ILE A 1 19 ? 16.158 6.416 30.569 1.00 22.41 ? 19 ILE A O 1
ATOM 142 C CB . ILE A 1 19 ? 14.643 4.028 28.998 1.00 24.32 ? 19 ILE A CB 1
ATOM 143 C CG1 . ILE A 1 19 ? 13.653 5.190 29.013 1.00 28.10 ? 19 ILE A CG1 1
ATOM 144 C CG2 . ILE A 1 19 ? 14.406 3.089 30.174 1.00 26.61 ? 19 ILE A CG2 1
ATOM 145 C CD1 . ILE A 1 19 ? 13.695 6.035 27.743 1.00 26.20 ? 19 ILE A CD1 1
ATOM 146 N N . GLU A 1 20 ? 16.840 4.423 31.341 1.00 22.29 ? 20 GLU A N 1
ATOM 147 C CA . GLU A 1 20 ? 17.124 4.933 32.679 1.00 25.26 ? 20 GLU A CA 1
ATOM 148 C C . GLU A 1 20 ? 18.565 5.398 32.884 1.00 24.46 ? 20 GLU A C 1
ATOM 149 O O . GLU A 1 20 ? 18.870 6.040 33.890 1.00 25.38 ? 20 GLU A O 1
ATOM 150 C CB . GLU A 1 20 ? 16.796 3.861 33.720 1.00 27.69 ? 20 GLU A CB 1
ATOM 151 C CG . GLU A 1 20 ? 15.312 3.627 33.940 1.00 35.06 ? 20 GLU A CG 1
ATOM 152 C CD . GLU A 1 20 ? 15.042 2.413 34.807 1.00 38.57 ? 20 GLU A CD 1
ATOM 153 O OE1 . GLU A 1 20 ? 15.602 2.333 35.922 1.00 40.85 ? 20 GLU A OE1 1
ATOM 154 O OE2 . GLU A 1 20 ? 14.269 1.537 34.372 1.00 42.53 ? 20 GLU A OE2 1
ATOM 155 N N . ASP A 1 21 ? 19.442 5.090 31.934 1.00 23.19 ? 21 ASP A N 1
ATOM 156 C CA . ASP A 1 21 ? 20.853 5.453 32.051 1.00 23.84 ? 21 ASP A CA 1
ATOM 157 C C . ASP A 1 21 ? 21.337 6.538 31.090 1.00 23.64 ? 21 ASP A C 1
ATOM 158 O O . ASP A 1 21 ? 22.361 7.185 31.336 1.00 23.85 ? 21 ASP A O 1
ATOM 159 C CB . ASP A 1 21 ? 21.718 4.210 31.850 1.00 25.50 ? 21 ASP A CB 1
ATOM 160 C CG . ASP A 1 21 ? 21.310 3.066 32.752 1.00 28.21 ? 21 ASP A CG 1
ATOM 161 O OD1 . ASP A 1 21 ? 21.288 3.264 33.984 1.00 30.65 ? 21 ASP A OD1 1
ATOM 162 O OD2 . ASP A 1 21 ? 21.012 1.973 32.229 1.00 30.29 ? 21 ASP A OD2 1
ATOM 163 N N . ASN A 1 22 ? 20.614 6.730 29.995 1.00 19.75 ? 22 ASN A N 1
ATOM 164 C CA . ASN A 1 22 ? 21.016 7.725 29.007 1.00 19.93 ? 22 ASN A CA 1
ATOM 165 C C . ASN A 1 22 ? 19.827 8.488 28.462 1.00 17.65 ? 22 ASN A C 1
ATOM 166 O O . ASN A 1 22 ? 18.840 7.893 28.027 1.00 18.55 ? 22 ASN A O 1
ATOM 167 C CB . ASN A 1 22 ? 21.758 7.061 27.836 1.00 17.06 ? 22 ASN A CB 1
ATOM 168 C CG . ASN A 1 22 ? 23.050 6.378 28.263 1.00 18.60 ? 22 ASN A CG 1
ATOM 169 O OD1 . ASN A 1 22 ? 23.065 5.185 28.575 1.00 17.12 ? 22 ASN A OD1 1
ATOM 170 N ND2 . ASN A 1 22 ? 24.143 7.137 28.279 1.00 16.68 ? 22 ASN A ND2 1
ATOM 171 N N . TYR A 1 23 ? 19.934 9.809 28.483 1.00 15.93 ? 23 TYR A N 1
ATOM 172 C CA . TYR A 1 23 ? 18.875 10.662 27.978 1.00 17.91 ? 23 TYR A CA 1
ATOM 173 C C . TYR A 1 23 ? 18.721 10.478 26.462 1.00 18.54 ? 23 TYR A C 1
ATOM 174 O O . TYR A 1 23 ? 17.630 10.613 25.916 1.00 16.88 ? 23 TYR A O 1
ATOM 175 C CB . TYR A 1 23 ? 19.184 12.121 28.290 1.00 16.61 ? 23 TYR A CB 1
ATOM 176 C CG . TYR A 1 23 ? 18.032 13.023 27.949 1.00 19.53 ? 23 TYR A CG 1
ATOM 177 C CD1 . TYR A 1 23 ? 16.885 13.040 28.746 1.00 13.88 ? 23 TYR A CD1 1
ATOM 178 C CD2 . TYR A 1 23 ? 18.062 13.827 26.810 1.00 15.42 ? 23 TYR A CD2 1
ATOM 179 C CE1 . TYR A 1 23 ? 15.806 13.829 28.418 1.00 16.07 ? 23 TYR A CE1 1
ATOM 180 C CE2 . TYR A 1 23 ? 16.975 14.628 26.472 1.00 16.75 ? 23 TYR A CE2 1
ATOM 181 C CZ . TYR A 1 23 ? 15.850 14.619 27.286 1.00 15.14 ? 23 TYR A CZ 1
ATOM 182 O OH . TYR A 1 23 ? 14.768 15.396 26.973 1.00 16.34 ? 23 TYR A OH 1
ATOM 183 N N . ARG A 1 24 ? 19.822 10.179 25.782 1.00 19.06 ? 24 ARG A N 1
ATOM 184 C CA . ARG A 1 24 ? 19.760 9.968 24.342 1.00 21.20 ? 24 ARG A CA 1
ATOM 185 C C . ARG A 1 24 ? 20.767 8.933 23.863 1.00 21.58 ? 24 ARG A C 1
ATOM 186 O O . ARG A 1 24 ? 21.793 8.702 24.503 1.00 22.28 ? 24 ARG A O 1
ATOM 187 C CB . ARG A 1 24 ? 19.956 11.295 23.589 1.00 24.70 ? 24 ARG A CB 1
ATOM 188 C CG . ARG A 1 24 ? 21.053 12.185 24.143 1.00 24.19 ? 24 ARG A CG 1
ATOM 189 C CD . ARG A 1 24 ? 21.242 13.453 23.324 1.00 25.16 ? 24 ARG A CD 1
ATOM 190 N NE . ARG A 1 24 ? 20.014 14.225 23.175 1.00 26.35 ? 24 ARG A NE 1
ATOM 191 C CZ . ARG A 1 24 ? 19.946 15.549 23.278 1.00 21.67 ? 24 ARG A CZ 1
ATOM 192 N NH1 . ARG A 1 24 ? 21.034 16.258 23.538 1.00 20.50 ? 24 ARG A NH1 1
ATOM 193 N NH2 . ARG A 1 24 ? 18.789 16.168 23.106 1.00 22.56 ? 24 ARG A NH2 1
ATOM 194 N N . VAL A 1 25 ? 20.438 8.273 22.757 1.00 20.47 ? 25 VAL A N 1
ATOM 195 C CA . VAL A 1 25 ? 21.323 7.281 22.178 1.00 19.25 ? 25 VAL A CA 1
ATOM 196 C C . VAL A 1 25 ? 21.928 7.915 20.940 1.00 17.53 ? 25 VAL A C 1
ATOM 197 O O . VAL A 1 25 ? 21.270 8.694 20.242 1.00 17.24 ? 25 VAL A O 1
ATOM 198 C CB . VAL A 1 25 ? 20.568 5.991 21.747 1.00 21.59 ? 25 VAL A CB 1
ATOM 199 C CG1 . VAL A 1 25 ? 19.876 5.361 22.946 1.00 26.23 ? 25 VAL A CG1 1
ATOM 200 C CG2 . VAL A 1 25 ? 19.561 6.313 20.662 1.00 25.38 ? 25 VAL A CG2 1
ATOM 201 N N . CYS A 1 26 ? 23.186 7.600 20.680 1.00 17.08 ? 26 CYS A N 1
ATOM 202 C CA . CYS A 1 26 ? 23.859 8.123 19.508 1.00 17.11 ? 26 CYS A CA 1
ATOM 203 C C . CYS A 1 26 ? 24.088 6.999 18.516 1.00 16.98 ? 26 CYS A C 1
ATOM 204 O O . CYS A 1 26 ? 24.270 5.841 18.896 1.00 15.61 ? 26 CYS A O 1
ATOM 205 C CB . CYS A 1 26 ? 25.201 8.745 19.882 1.00 18.74 ? 26 CYS A CB 1
ATOM 206 S SG . CYS A 1 26 ? 25.058 10.234 20.896 1.00 20.22 ? 26 CYS A SG 1
ATOM 207 N N . VAL A 1 27 ? 24.065 7.356 17.241 1.00 14.34 ? 27 VAL A N 1
ATOM 208 C CA . VAL A 1 27 ? 24.304 6.408 16.180 1.00 15.37 ? 27 VAL A CA 1
ATOM 209 C C . VAL A 1 27 ? 25.410 6.993 15.313 1.00 14.15 ? 27 VAL A C 1
ATOM 210 O O . VAL A 1 27 ? 25.340 8.149 14.908 1.00 15.50 ? 27 VAL A O 1
ATOM 211 C CB . VAL A 1 27 ? 23.049 6.194 15.306 1.00 16.88 ? 27 VAL A CB 1
ATOM 212 C CG1 . VAL A 1 27 ? 23.378 5.269 14.145 1.00 16.27 ? 27 VAL A CG1 1
ATOM 213 C CG2 . VAL A 1 27 ? 21.912 5.619 16.150 1.00 19.57 ? 27 VAL A CG2 1
ATOM 214 N N . ILE A 1 28 ? 26.450 6.209 15.071 1.00 14.23 ? 28 ILE A N 1
ATOM 215 C CA . ILE A 1 28 ? 27.534 6.656 14.205 1.00 15.29 ? 28 ILE A CA 1
ATOM 216 C C . ILE A 1 28 ? 27.353 5.894 12.899 1.00 16.05 ? 28 ILE A C 1
ATOM 217 O O . ILE A 1 28 ? 27.153 4.679 12.914 1.00 17.27 ? 28 ILE A O 1
ATOM 218 C CB . ILE A 1 28 ? 28.919 6.329 14.798 1.00 13.57 ? 28 ILE A CB 1
ATOM 219 C CG1 . ILE A 1 28 ? 29.276 7.359 15.872 1.00 13.94 ? 28 ILE A CG1 1
ATOM 220 C CG2 . ILE A 1 28 ? 29.976 6.313 13.687 1.00 15.01 ? 28 ILE A CG2 1
ATOM 221 C CD1 . ILE A 1 28 ? 30.620 7.098 16.539 1.00 16.90 ? 28 ILE A CD1 1
ATOM 222 N N . LEU A 1 29 ? 27.390 6.618 11.782 1.00 15.04 ? 29 LEU A N 1
ATOM 223 C CA . LEU A 1 29 ? 27.238 6.030 10.455 1.00 15.69 ? 29 LEU A CA 1
ATOM 224 C C . LEU A 1 29 ? 28.359 6.572 9.570 1.00 14.66 ? 29 LEU A C 1
ATOM 225 O O . LEU A 1 29 ? 28.380 7.757 9.232 1.00 16.14 ? 29 LEU A O 1
ATOM 226 C CB . LEU A 1 29 ? 25.881 6.407 9.852 1.00 17.33 ? 29 LEU A CB 1
ATOM 227 C CG . LEU A 1 29 ? 25.632 5.889 8.431 1.00 21.06 ? 29 LEU A CG 1
ATOM 228 C CD1 . LEU A 1 29 ? 25.682 4.361 8.424 1.00 21.03 ? 29 LEU A CD1 1
ATOM 229 C CD2 . LEU A 1 29 ? 24.284 6.385 7.927 1.00 22.62 ? 29 LEU A CD2 1
ATOM 230 N N . VAL A 1 30 ? 29.291 5.705 9.206 1.00 13.32 ? 30 VAL A N 1
ATOM 231 C CA . VAL A 1 30 ? 30.422 6.108 8.381 1.00 13.71 ? 30 VAL A CA 1
ATOM 232 C C . VAL A 1 30 ? 30.383 5.499 6.990 1.00 14.82 ? 30 VAL A C 1
ATOM 233 O O . VAL A 1 30 ? 30.011 4.337 6.811 1.00 15.45 ? 30 VAL A O 1
ATOM 234 C CB . VAL A 1 30 ? 31.766 5.715 9.048 1.00 15.18 ? 30 VAL A CB 1
ATOM 235 C CG1 . VAL A 1 30 ? 32.922 5.911 8.071 1.00 12.89 ? 30 VAL A CG1 1
ATOM 236 C CG2 . VAL A 1 30 ? 31.987 6.557 10.290 1.00 12.67 ? 30 VAL A CG2 1
ATOM 237 N N . GLY A 1 31 ? 30.783 6.304 6.010 1.00 16.91 ? 31 GLY A N 1
ATOM 238 C CA . GLY A 1 31 ? 30.829 5.855 4.632 1.00 16.27 ? 31 GLY A CA 1
ATOM 239 C C . GLY A 1 31 ? 31.756 6.755 3.837 1.00 16.39 ? 31 GLY A C 1
ATOM 240 O O . GLY A 1 31 ? 31.880 7.946 4.136 1.00 13.70 ? 31 GLY A O 1
ATOM 241 N N . SER A 1 32 ? 32.415 6.194 2.828 1.00 15.62 ? 32 SER A N 1
ATOM 242 C CA . SER A 1 32 ? 33.309 6.983 1.995 1.00 18.04 ? 32 SER A CA 1
ATOM 243 C C . SER A 1 32 ? 32.415 7.743 1.017 1.00 18.65 ? 32 SER A C 1
ATOM 244 O O . SER A 1 32 ? 31.203 7.517 0.984 1.00 18.67 ? 32 SER A O 1
ATOM 245 C CB . SER A 1 32 ? 34.290 6.068 1.251 1.00 18.07 ? 32 SER A CB 1
ATOM 246 O OG . SER A 1 32 ? 33.613 5.124 0.446 1.00 21.62 ? 32 SER A OG 1
ATOM 247 N N . PRO A 1 33 ? 32.991 8.662 0.224 1.00 18.64 ? 33 PRO A N 1
ATOM 248 C CA . PRO A 1 33 ? 32.189 9.428 -0.733 1.00 19.87 ? 33 PRO A CA 1
ATOM 249 C C . PRO A 1 33 ? 31.344 8.543 -1.654 1.00 21.79 ? 33 PRO A C 1
ATOM 250 O O . PRO A 1 33 ? 31.833 7.562 -2.213 1.00 22.60 ? 33 PRO A O 1
ATOM 251 C CB . PRO A 1 33 ? 33.242 10.230 -1.497 1.00 19.94 ? 33 PRO A CB 1
ATOM 252 C CG . PRO A 1 33 ? 34.297 10.463 -0.455 1.00 17.31 ? 33 PRO A CG 1
ATOM 253 C CD . PRO A 1 33 ? 34.401 9.100 0.191 1.00 18.51 ? 33 PRO A CD 1
ATOM 254 N N . GLY A 1 34 ? 30.067 8.892 -1.790 1.00 22.50 ? 34 GLY A N 1
ATOM 255 C CA . GLY A 1 34 ? 29.173 8.133 -2.644 1.00 21.59 ? 34 GLY A CA 1
ATOM 256 C C . GLY A 1 34 ? 28.627 6.853 -2.040 1.00 19.97 ? 34 GLY A C 1
ATOM 257 O O . GLY A 1 34 ? 27.990 6.071 -2.731 1.00 18.96 ? 34 GLY A O 1
ATOM 258 N N . SER A 1 35 ? 28.869 6.640 -0.751 1.00 18.91 ? 35 SER A N 1
ATOM 259 C CA . SER A 1 35 ? 28.397 5.438 -0.070 1.00 18.71 ? 35 SER A CA 1
ATOM 260 C C . SER A 1 35 ? 26.914 5.504 0.260 1.00 18.42 ? 35 SER A C 1
ATOM 261 O O . SER A 1 35 ? 26.293 4.482 0.537 1.00 19.98 ? 35 SER A O 1
ATOM 262 C CB . SER A 1 35 ? 29.175 5.236 1.229 1.00 20.23 ? 35 SER A CB 1
ATOM 263 O OG . SER A 1 35 ? 28.959 6.333 2.103 1.00 18.62 ? 35 SER A OG 1
ATOM 264 N N . GLY A 1 36 ? 26.346 6.706 0.243 1.00 19.97 ? 36 GLY A N 1
ATOM 265 C CA . GLY A 1 36 ? 24.934 6.852 0.555 1.00 21.57 ? 36 GLY A CA 1
ATOM 266 C C . GLY A 1 36 ? 24.624 6.987 2.044 1.00 22.20 ? 36 GLY A C 1
ATOM 267 O O . GLY A 1 36 ? 23.503 6.713 2.471 1.00 23.00 ? 36 GLY A O 1
ATOM 268 N N . LYS A 1 37 ? 25.605 7.405 2.840 1.00 22.08 ? 37 LYS A N 1
ATOM 269 C CA . LYS A 1 37 ? 25.396 7.574 4.279 1.00 22.08 ? 37 LYS A CA 1
ATOM 270 C C . LYS A 1 37 ? 24.376 8.678 4.557 1.00 20.82 ? 37 LYS A C 1
ATOM 271 O O . LYS A 1 37 ? 23.652 8.647 5.552 1.00 20.50 ? 37 LYS A O 1
ATOM 272 C CB . LYS A 1 37 ? 26.721 7.908 4.967 1.00 21.74 ? 37 LYS A CB 1
ATOM 273 C CG . LYS A 1 37 ? 27.467 9.069 4.339 1.00 20.55 ? 37 LYS A CG 1
ATOM 274 C CD . LYS A 1 37 ? 28.786 9.322 5.042 1.00 20.90 ? 37 LYS A CD 1
ATOM 275 C CE . LYS A 1 37 ? 29.577 10.418 4.342 1.00 20.33 ? 37 LYS A CE 1
ATOM 276 N NZ . LYS A 1 37 ? 30.007 9.991 2.978 1.00 20.59 ? 37 LYS A NZ 1
ATOM 277 N N . SER A 1 38 ? 24.318 9.648 3.660 1.00 22.34 ? 38 SER A N 1
ATOM 278 C CA . SER A 1 38 ? 23.395 10.764 3.796 1.00 25.21 ? 38 SER A CA 1
ATOM 279 C C . SER A 1 38 ? 21.938 10.293 3.719 1.00 25.32 ? 38 SER A C 1
ATOM 280 O O . SER A 1 38 ? 21.117 10.650 4.567 1.00 25.84 ? 38 SER A O 1
ATOM 281 C CB . SER A 1 38 ? 23.684 11.793 2.697 1.00 29.01 ? 38 SER A CB 1
ATOM 282 O OG . SER A 1 38 ? 22.962 12.992 2.907 1.00 35.07 ? 38 SER A OG 1
ATOM 283 N N . THR A 1 39 ? 21.625 9.478 2.714 1.00 25.21 ? 39 THR A N 1
ATOM 284 C CA . THR A 1 39 ? 20.267 8.973 2.530 1.00 26.66 ? 39 THR A CA 1
ATOM 285 C C . THR A 1 39 ? 19.875 7.922 3.567 1.00 25.12 ? 39 THR A C 1
ATOM 286 O O . THR A 1 39 ? 18.722 7.856 3.985 1.00 25.83 ? 39 THR A O 1
ATOM 287 C CB . THR A 1 39 ? 20.070 8.375 1.107 1.00 28.17 ? 39 THR A CB 1
ATOM 288 O OG1 . THR A 1 39 ? 20.914 7.232 0.934 1.00 31.97 ? 39 THR A OG1 1
ATOM 289 C CG2 . THR A 1 39 ? 20.423 9.404 0.049 1.00 29.49 ? 39 THR A CG2 1
ATOM 290 N N . ILE A 1 40 ? 20.826 7.091 3.974 1.00 23.16 ? 40 ILE A N 1
ATOM 291 C CA . ILE A 1 40 ? 20.535 6.077 4.974 1.00 21.97 ? 40 ILE A CA 1
ATOM 292 C C . ILE A 1 40 ? 20.187 6.781 6.285 1.00 22.37 ? 40 ILE A C 1
ATOM 293 O O . ILE A 1 40 ? 19.205 6.437 6.946 1.00 20.99 ? 40 ILE A O 1
ATOM 294 C CB . ILE A 1 40 ? 21.749 5.144 5.192 1.00 23.10 ? 40 ILE A CB 1
ATOM 295 C CG1 . ILE A 1 40 ? 22.022 4.344 3.912 1.00 24.13 ? 40 ILE A CG1 1
ATOM 296 C CG2 . ILE A 1 40 ? 21.479 4.185 6.349 1.00 22.58 ? 40 ILE A CG2 1
ATOM 297 C CD1 . ILE A 1 40 ? 23.245 3.445 3.997 1.00 23.01 ? 40 ILE A CD1 1
ATOM 298 N N . ALA A 1 41 ? 20.987 7.782 6.642 1.00 19.98 ? 41 ALA A N 1
ATOM 299 C CA . ALA A 1 41 ? 20.771 8.536 7.873 1.00 21.06 ? 41 ALA A CA 1
ATOM 300 C C . ALA A 1 41 ? 19.419 9.245 7.881 1.00 22.27 ? 41 ALA A C 1
ATOM 301 O O . ALA A 1 41 ? 18.692 9.208 8.875 1.00 22.40 ? 41 ALA A O 1
ATOM 302 C CB . ALA A 1 41 ? 21.898 9.556 8.059 1.00 17.59 ? 41 ALA A CB 1
ATOM 303 N N . GLU A 1 42 ? 19.080 9.887 6.768 1.00 23.90 ? 42 GLU A N 1
ATOM 304 C CA . GLU A 1 42 ? 17.816 10.608 6.671 1.00 24.36 ? 42 GLU A CA 1
ATOM 305 C C . GLU A 1 42 ? 16.639 9.653 6.728 1.00 23.63 ? 42 GLU A C 1
ATOM 306 O O . GLU A 1 42 ? 15.635 9.936 7.378 1.00 21.18 ? 42 GLU A O 1
ATOM 307 C CB . GLU A 1 42 ? 17.774 11.430 5.378 1.00 28.59 ? 42 GLU A CB 1
ATOM 308 C CG . GLU A 1 42 ? 18.896 12.456 5.288 1.00 35.56 ? 42 GLU A CG 1
ATOM 309 C CD . GLU A 1 42 ? 18.804 13.339 4.059 1.00 40.73 ? 42 GLU A CD 1
ATOM 310 O OE1 . GLU A 1 42 ? 18.796 12.801 2.931 1.00 44.65 ? 42 GLU A OE1 1
ATOM 311 O OE2 . GLU A 1 42 ? 18.746 14.577 4.223 1.00 44.49 ? 42 GLU A OE2 1
ATOM 312 N N . GLU A 1 43 ? 16.773 8.516 6.054 1.00 24.03 ? 43 GLU A N 1
ATOM 313 C CA . GLU A 1 43 ? 15.722 7.506 6.022 1.00 24.17 ? 43 GLU A CA 1
ATOM 314 C C . GLU A 1 43 ? 15.495 6.940 7.425 1.00 23.17 ? 43 GLU A C 1
ATOM 315 O O . GLU A 1 43 ? 14.357 6.832 7.895 1.00 20.45 ? 43 GLU A O 1
ATOM 316 C CB . GLU A 1 43 ? 16.116 6.391 5.051 1.00 26.67 ? 43 GLU A CB 1
ATOM 317 C CG . GLU A 1 43 ? 15.024 5.392 4.749 1.00 32.59 ? 43 GLU A CG 1
ATOM 318 C CD . GLU A 1 43 ? 15.375 4.499 3.572 1.00 37.76 ? 43 GLU A CD 1
ATOM 319 O OE1 . GLU A 1 43 ? 15.680 5.038 2.485 1.00 41.48 ? 43 GLU A OE1 1
ATOM 320 O OE2 . GLU A 1 43 ? 15.343 3.260 3.730 1.00 40.84 ? 43 GLU A OE2 1
ATOM 321 N N . LEU A 1 44 ? 16.584 6.586 8.095 1.00 20.53 ? 44 LEU A N 1
ATOM 322 C CA . LEU A 1 44 ? 16.506 6.047 9.448 1.00 19.58 ? 44 LEU A CA 1
ATOM 323 C C . LEU A 1 44 ? 15.817 7.033 10.395 1.00 19.61 ? 44 LEU A C 1
ATOM 324 O O . LEU A 1 44 ? 14.911 6.667 11.143 1.00 18.83 ? 44 LEU A O 1
ATOM 325 C CB . LEU A 1 44 ? 17.918 5.737 9.959 1.00 19.34 ? 44 LEU A CB 1
ATOM 326 C CG . LEU A 1 44 ? 18.087 5.336 11.430 1.00 18.80 ? 44 LEU A CG 1
ATOM 327 C CD1 . LEU A 1 44 ? 17.248 4.111 11.755 1.00 19.29 ? 44 LEU A CD1 1
ATOM 328 C CD2 . LEU A 1 44 ? 19.559 5.061 11.697 1.00 19.18 ? 44 LEU A CD2 1
HETATM 329 N N . CME A 1 45 ? 16.227 8.277 10.197 1.00 21.17 ? 45 CME A N 1
HETATM 330 C CA . CME A 1 45 ? 15.710 9.350 11.042 1.00 22.60 ? 45 CME A CA 1
HETATM 331 C CB . CME A 1 45 ? 16.478 10.629 10.733 1.00 26.47 ? 45 CME A CB 1
HETATM 332 S SG . CME A 1 45 ? 15.880 12.103 11.604 1.00 27.64 ? 45 CME A SG 1
HETATM 333 S SD . CME A 1 45 ? 14.641 12.986 10.255 1.00 40.89 ? 45 CME A SD 1
HETATM 334 C CE . CME A 1 45 ? 15.137 14.738 10.296 1.00 42.58 ? 45 CME A CE 1
HETATM 335 C CZ . CME A 1 45 ? 16.469 14.971 9.616 1.00 45.56 ? 45 CME A CZ 1
HETATM 336 O OH . CME A 1 45 ? 16.752 16.204 9.441 1.00 49.77 ? 45 CME A OH 1
HETATM 337 C C . CME A 1 45 ? 14.211 9.610 10.883 1.00 24.58 ? 45 CME A C 1
HETATM 338 O O . CME A 1 45 ? 13.414 9.447 11.809 1.00 22.88 ? 45 CME A O 1
ATOM 339 N N . GLN A 1 46 ? 14.041 9.307 9.461 1.00 32.96 ? 46 GLN A N 1
ATOM 340 C CA . GLN A 1 46 ? 12.615 9.538 9.305 1.00 30.18 ? 46 GLN A CA 1
ATOM 341 C C . GLN A 1 46 ? 11.801 8.387 9.879 1.00 27.07 ? 46 GLN A C 1
ATOM 342 O O . GLN A 1 46 ? 10.644 8.563 10.264 1.00 24.93 ? 46 GLN A O 1
ATOM 343 C CB . GLN A 1 46 ? 12.293 9.728 7.824 1.00 33.13 ? 46 GLN A CB 1
ATOM 344 C CG . GLN A 1 46 ? 12.739 11.072 7.297 1.00 38.36 ? 46 GLN A CG 1
ATOM 345 C CD . GLN A 1 46 ? 11.926 12.208 7.883 1.00 41.03 ? 46 GLN A CD 1
ATOM 346 O OE1 . GLN A 1 46 ? 12.312 13.374 7.798 1.00 43.44 ? 46 GLN A OE1 1
ATOM 347 N NE2 . GLN A 1 46 ? 10.782 11.872 8.475 1.00 43.87 ? 46 GLN A NE2 1
ATOM 348 N N . ILE A 1 47 ? 11.937 7.304 9.438 1.00 25.03 ? 47 ILE A N 1
ATOM 349 C CA . ILE A 1 47 ? 11.258 6.138 9.985 1.00 24.19 ? 47 ILE A CA 1
ATOM 350 C C . ILE A 1 47 ? 10.979 6.229 11.483 1.00 22.85 ? 47 ILE A C 1
ATOM 351 O O . ILE A 1 47 ? 9.853 6.004 11.927 1.00 20.38 ? 47 ILE A O 1
ATOM 352 C CB . ILE A 1 47 ? 12.066 4.861 9.702 1.00 23.46 ? 47 ILE A CB 1
ATOM 353 C CG1 . ILE A 1 47 ? 12.126 4.628 8.190 1.00 25.60 ? 47 ILE A CG1 1
ATOM 354 C CG2 . ILE A 1 47 ? 11.439 3.667 10.418 1.00 25.94 ? 47 ILE A CG2 1
ATOM 355 C CD1 . ILE A 1 47 ? 12.889 3.384 7.782 1.00 24.98 ? 47 ILE A CD1 1
ATOM 356 N N . ILE A 1 48 ? 12.003 6.555 12.263 1.00 22.27 ? 48 ILE A N 1
ATOM 357 C CA . ILE A 1 48 ? 11.833 6.660 13.707 1.00 20.44 ? 48 ILE A CA 1
ATOM 358 C C . ILE A 1 48 ? 10.824 7.740 14.080 1.00 21.22 ? 48 ILE A C 1
ATOM 359 O O . ILE A 1 48 ? 9.934 7.504 14.900 1.00 18.61 ? 48 ILE A O 1
ATOM 360 C CB . ILE A 1 48 ? 13.174 6.944 14.409 1.00 19.70 ? 48 ILE A CB 1
ATOM 361 C CG1 . ILE A 1 48 ? 14.076 5.709 14.292 1.00 20.29 ? 48 ILE A CG1 1
ATOM 362 C CG2 . ILE A 1 48 ? 12.929 7.321 15.881 1.00 16.36 ? 48 ILE A CG2 1
ATOM 363 C CD1 . ILE A 1 48 ? 15.540 5.954 14.654 1.00 20.27 ? 48 ILE A CD1 1
ATOM 364 N N . ASN A 1 49 ? 10.955 8.921 13.485 1.00 20.28 ? 49 ASN A N 1
ATOM 365 C CA . ASN A 1 49 ? 10.021 9.996 13.792 1.00 21.80 ? 49 ASN A CA 1
ATOM 366 C C . ASN A 1 49 ? 8.589 9.632 13.387 1.00 22.02 ? 49 ASN A C 1
ATOM 367 O O . ASN A 1 49 ? 7.643 9.932 14.113 1.00 21.23 ? 49 ASN A O 1
ATOM 368 C CB . ASN A 1 49 ? 10.452 11.302 13.120 1.00 19.06 ? 49 ASN A CB 1
ATOM 369 C CG . ASN A 1 49 ? 11.682 11.917 13.771 1.00 20.49 ? 49 ASN A CG 1
ATOM 370 O OD1 . ASN A 1 49 ? 11.847 11.863 14.991 1.00 20.96 ? 49 ASN A OD1 1
ATOM 371 N ND2 . ASN A 1 49 ? 12.542 12.521 12.959 1.00 20.81 ? 49 ASN A ND2 1
ATOM 372 N N . GLU A 1 50 ? 8.428 8.983 12.236 1.00 22.23 ? 50 GLU A N 1
ATOM 373 C CA . GLU A 1 50 ? 7.099 8.570 11.776 1.00 23.23 ? 50 GLU A CA 1
ATOM 374 C C . GLU A 1 50 ? 6.460 7.633 12.794 1.00 22.64 ? 50 GLU A C 1
ATOM 375 O O . GLU A 1 50 ? 5.274 7.750 13.111 1.00 23.35 ? 50 GLU A O 1
ATOM 376 C CB . GLU A 1 50 ? 7.193 7.845 10.430 1.00 24.50 ? 50 GLU A CB 1
ATOM 377 C CG . GLU A 1 50 ? 7.226 8.753 9.217 1.00 33.22 ? 50 GLU A CG 1
ATOM 378 C CD . GLU A 1 50 ? 7.555 7.995 7.936 1.00 37.95 ? 50 GLU A CD 1
ATOM 379 O OE1 . GLU A 1 50 ? 7.057 6.858 7.773 1.00 37.20 ? 50 GLU A OE1 1
ATOM 380 O OE2 . GLU A 1 50 ? 8.305 8.541 7.094 1.00 40.31 ? 50 GLU A OE2 1
ATOM 381 N N . LYS A 1 51 ? 7.250 6.683 13.284 1.00 21.70 ? 51 LYS A N 1
ATOM 382 C CA . LYS A 1 51 ? 6.777 5.732 14.273 1.00 19.43 ? 51 LYS A CA 1
ATOM 383 C C . LYS A 1 51 ? 6.290 6.467 15.517 1.00 20.37 ? 51 LYS A C 1
ATOM 384 O O . LYS A 1 51 ? 5.259 6.121 16.100 1.00 18.20 ? 51 LYS A O 1
ATOM 385 C CB . LYS A 1 51 ? 7.904 4.779 14.666 1.00 20.84 ? 51 LYS A CB 1
ATOM 386 C CG . LYS A 1 51 ? 8.139 3.629 13.706 1.00 24.17 ? 51 LYS A CG 1
ATOM 387 C CD . LYS A 1 51 ? 9.351 2.823 14.153 1.00 28.20 ? 51 LYS A CD 1
ATOM 388 C CE . LYS A 1 51 ? 9.410 1.457 13.487 1.00 29.98 ? 51 LYS A CE 1
ATOM 389 N NZ . LYS A 1 51 ? 8.282 0.579 13.934 1.00 32.17 ? 51 LYS A NZ 1
ATOM 390 N N . TYR A 1 52 ? 7.037 7.485 15.926 1.00 17.99 ? 52 TYR A N 1
ATOM 391 C CA . TYR A 1 52 ? 6.662 8.237 17.112 1.00 20.24 ? 52 TYR A CA 1
ATOM 392 C C . TYR A 1 52 ? 5.365 9.013 16.899 1.00 20.49 ? 52 TYR A C 1
ATOM 393 O O . TYR A 1 52 ? 4.505 9.049 17.777 1.00 20.46 ? 52 TYR A O 1
ATOM 394 C CB . TYR A 1 52 ? 7.787 9.195 17.519 1.00 19.56 ? 52 TYR A CB 1
ATOM 395 C CG . TYR A 1 52 ? 7.559 9.846 18.867 1.00 19.45 ? 52 TYR A CG 1
ATOM 396 C CD1 . TYR A 1 52 ? 7.395 9.073 20.021 1.00 19.20 ? 52 TYR A CD1 1
ATOM 397 C CD2 . TYR A 1 52 ? 7.479 11.231 18.987 1.00 19.72 ? 52 TYR A CD2 1
ATOM 398 C CE1 . TYR A 1 52 ? 7.151 9.668 21.261 1.00 14.92 ? 52 TYR A CE1 1
ATOM 399 C CE2 . TYR A 1 52 ? 7.237 11.832 20.221 1.00 19.30 ? 52 TYR A CE2 1
ATOM 400 C CZ . TYR A 1 52 ? 7.074 11.046 21.347 1.00 17.41 ? 52 TYR A CZ 1
ATOM 401 O OH . TYR A 1 52 ? 6.827 11.645 22.556 1.00 20.71 ? 52 TYR A OH 1
ATOM 402 N N . HIS A 1 53 ? 5.224 9.627 15.730 1.00 20.21 ? 53 HIS A N 1
ATOM 403 C CA . HIS A 1 53 ? 4.021 10.394 15.424 1.00 21.18 ? 53 HIS A CA 1
ATOM 404 C C . HIS A 1 53 ? 2.801 9.474 15.426 1.00 21.43 ? 53 HIS A C 1
ATOM 405 O O . HIS A 1 53 ? 1.734 9.843 15.915 1.00 22.55 ? 53 HIS A O 1
ATOM 406 C CB . HIS A 1 53 ? 4.184 11.084 14.069 1.00 19.26 ? 53 HIS A CB 1
ATOM 407 C CG . HIS A 1 53 ? 5.285 12.100 14.047 1.00 21.41 ? 53 HIS A CG 1
ATOM 408 N ND1 . HIS A 1 53 ? 5.959 12.446 12.896 1.00 21.78 ? 53 HIS A ND1 1
ATOM 409 C CD2 . HIS A 1 53 ? 5.841 12.834 15.041 1.00 19.13 ? 53 HIS A CD2 1
ATOM 410 C CE1 . HIS A 1 53 ? 6.885 13.344 13.181 1.00 20.79 ? 53 HIS A CE1 1
ATOM 411 N NE2 . HIS A 1 53 ? 6.834 13.597 14.477 1.00 20.93 ? 53 HIS A NE2 1
ATOM 412 N N . THR A 1 54 ? 2.973 8.271 14.892 1.00 22.47 ? 54 THR A N 1
ATOM 413 C CA . THR A 1 54 ? 1.898 7.292 14.847 1.00 23.08 ? 54 THR A CA 1
ATOM 414 C C . THR A 1 54 ? 1.511 6.905 16.276 1.00 23.32 ? 54 THR A C 1
ATOM 415 O O . THR A 1 54 ? 0.340 6.709 16.584 1.00 23.72 ? 54 THR A O 1
ATOM 416 C CB . THR A 1 54 ? 2.345 6.047 14.054 1.00 23.45 ? 54 THR A CB 1
ATOM 417 O OG1 . THR A 1 54 ? 2.676 6.443 12.719 1.00 22.69 ? 54 THR A OG1 1
ATOM 418 C CG2 . THR A 1 54 ? 1.232 4.994 14.002 1.00 24.95 ? 54 THR A CG2 1
ATOM 419 N N . PHE A 1 55 ? 2.506 6.803 17.151 1.00 24.05 ? 55 PHE A N 1
ATOM 420 C CA . PHE A 1 55 ? 2.257 6.468 18.545 1.00 22.71 ? 55 PHE A CA 1
ATOM 421 C C . PHE A 1 55 ? 1.497 7.610 19.217 1.00 22.89 ? 55 PHE A C 1
ATOM 422 O O . PHE A 1 55 ? 0.556 7.378 19.974 1.00 22.44 ? 55 PHE A O 1
ATOM 423 C CB . PHE A 1 55 ? 3.579 6.236 19.281 1.00 21.89 ? 55 PHE A CB 1
ATOM 424 C CG . PHE A 1 55 ? 3.453 6.281 20.779 1.00 21.22 ? 55 PHE A CG 1
ATOM 425 C CD1 . PHE A 1 55 ? 2.945 5.196 21.484 1.00 19.45 ? 55 PHE A CD1 1
ATOM 426 C CD2 . PHE A 1 55 ? 3.829 7.421 21.481 1.00 20.35 ? 55 PHE A CD2 1
ATOM 427 C CE1 . PHE A 1 55 ? 2.813 5.244 22.872 1.00 21.58 ? 55 PHE A CE1 1
ATOM 428 C CE2 . PHE A 1 55 ? 3.700 7.480 22.866 1.00 20.37 ? 55 PHE A CE2 1
ATOM 429 C CZ . PHE A 1 55 ? 3.191 6.389 23.562 1.00 20.77 ? 55 PHE A CZ 1
ATOM 430 N N . LEU A 1 56 ? 1.922 8.841 18.946 1.00 23.31 ? 56 LEU A N 1
ATOM 431 C CA . LEU A 1 56 ? 1.278 10.022 19.519 1.00 24.09 ? 56 LEU A CA 1
ATOM 432 C C . LEU A 1 56 ? -0.183 10.139 19.106 1.00 24.02 ? 56 LEU A C 1
ATOM 433 O O . LEU A 1 56 ? -1.007 10.644 19.867 1.00 24.08 ? 56 LEU A O 1
ATOM 434 C CB . LEU A 1 56 ? 2.007 11.293 19.092 1.00 23.21 ? 56 LEU A CB 1
ATOM 435 C CG . LEU A 1 56 ? 3.354 11.554 19.754 1.00 23.54 ? 56 LEU A CG 1
ATOM 436 C CD1 . LEU A 1 56 ? 3.944 12.840 19.195 1.00 20.42 ? 56 LEU A CD1 1
ATOM 437 C CD2 . LEU A 1 56 ? 3.172 11.645 21.273 1.00 23.81 ? 56 LEU A CD2 1
ATOM 438 N N . SER A 1 57 ? -0.490 9.687 17.894 1.00 21.99 ? 57 SER A N 1
ATOM 439 C CA . SER A 1 57 ? -1.853 9.737 17.379 1.00 24.53 ? 57 SER A CA 1
ATOM 440 C C . SER A 1 57 ? -2.864 9.167 18.377 1.00 23.60 ? 57 SER A C 1
ATOM 441 O O . SER A 1 57 ? -3.924 9.753 18.597 1.00 24.26 ? 57 SER A O 1
ATOM 442 C CB . SER A 1 57 ? -1.944 8.959 16.060 1.00 25.38 ? 57 SER A CB 1
ATOM 443 O OG . SER A 1 57 ? -3.294 8.819 15.653 1.00 29.75 ? 57 SER A OG 1
ATOM 444 N N . GLU A 1 58 ? -2.525 8.035 18.990 1.00 23.58 ? 58 GLU A N 1
ATOM 445 C CA . GLU A 1 58 ? -3.411 7.386 19.947 1.00 24.81 ? 58 GLU A CA 1
ATOM 446 C C . GLU A 1 58 ? -3.058 7.595 21.417 1.00 24.19 ? 58 GLU A C 1
ATOM 447 O O . GLU A 1 58 ? -3.733 7.075 22.308 1.00 23.68 ? 58 GLU A O 1
ATOM 448 C CB . GLU A 1 58 ? -3.510 5.894 19.613 1.00 28.87 ? 58 GLU A CB 1
ATOM 449 C CG . GLU A 1 58 ? -4.341 5.658 18.359 1.00 34.18 ? 58 GLU A CG 1
ATOM 450 C CD . GLU A 1 58 ? -4.364 4.210 17.906 1.00 38.43 ? 58 GLU A CD 1
ATOM 451 O OE1 . GLU A 1 58 ? -4.458 3.312 18.769 1.00 41.11 ? 58 GLU A OE1 1
ATOM 452 O OE2 . GLU A 1 58 ? -4.309 3.977 16.680 1.00 38.30 ? 58 GLU A OE2 1
ATOM 453 N N . HIS A 1 59 ? -1.994 8.354 21.661 1.00 22.91 ? 59 HIS A N 1
ATOM 454 C CA . HIS A 1 59 ? -1.554 8.695 23.012 1.00 21.63 ? 59 HIS A CA 1
ATOM 455 C C . HIS A 1 59 ? -1.302 10.193 22.931 1.00 22.50 ? 59 HIS A C 1
ATOM 456 O O . HIS A 1 59 ? -0.203 10.655 23.217 1.00 22.28 ? 59 HIS A O 1
ATOM 457 C CB . HIS A 1 59 ? -0.253 7.970 23.367 1.00 21.09 ? 59 HIS A CB 1
ATOM 458 C CG . HIS A 1 59 ? -0.349 6.483 23.279 1.00 19.75 ? 59 HIS A CG 1
ATOM 459 N ND1 . HIS A 1 59 ? -0.340 5.806 22.078 1.00 21.64 ? 59 HIS A ND1 1
ATOM 460 C CD2 . HIS A 1 59 ? -0.510 5.543 24.240 1.00 20.33 ? 59 HIS A CD2 1
ATOM 461 C CE1 . HIS A 1 59 ? -0.492 4.514 22.302 1.00 21.05 ? 59 HIS A CE1 1
ATOM 462 N NE2 . HIS A 1 59 ? -0.598 4.327 23.606 1.00 21.66 ? 59 HIS A NE2 1
ATOM 463 N N . PRO A 1 60 ? -2.342 10.968 22.549 1.00 22.91 ? 60 PRO A N 1
ATOM 464 C CA . PRO A 1 60 ? -2.401 12.425 22.360 1.00 23.54 ? 60 PRO A CA 1
ATOM 465 C C . PRO A 1 60 ? -1.764 13.345 23.391 1.00 24.12 ? 60 PRO A C 1
ATOM 466 O O . PRO A 1 60 ? -1.156 14.352 23.031 1.00 25.64 ? 60 PRO A O 1
ATOM 467 C CB . PRO A 1 60 ? -3.902 12.705 22.239 1.00 21.93 ? 60 PRO A CB 1
ATOM 468 C CG . PRO A 1 60 ? -4.472 11.420 21.771 1.00 21.78 ? 60 PRO A CG 1
ATOM 469 C CD . PRO A 1 60 ? -3.712 10.420 22.582 1.00 22.72 ? 60 PRO A CD 1
ATOM 470 N N . ASN A 1 61 ? -1.910 13.015 24.667 1.00 25.20 ? 61 ASN A N 1
ATOM 471 C CA . ASN A 1 61 ? -1.382 13.869 25.721 1.00 24.58 ? 61 ASN A CA 1
ATOM 472 C C . ASN A 1 61 ? -0.410 13.168 26.648 1.00 23.82 ? 61 ASN A C 1
ATOM 473 O O . ASN A 1 61 ? -0.330 13.484 27.833 1.00 22.45 ? 61 ASN A O 1
ATOM 474 C CB . ASN A 1 61 ? -2.556 14.428 26.517 1.00 26.35 ? 61 ASN A CB 1
ATOM 475 C CG . ASN A 1 61 ? -3.553 15.137 25.629 1.00 26.81 ? 61 ASN A CG 1
ATOM 476 O OD1 . ASN A 1 61 ? -3.237 16.165 25.036 1.00 26.67 ? 61 ASN A OD1 1
ATOM 477 N ND2 . ASN A 1 61 ? -4.757 14.581 25.514 1.00 25.05 ? 61 ASN A ND2 1
ATOM 478 N N . VAL A 1 62 ? 0.343 12.228 26.094 1.00 23.79 ? 62 VAL A N 1
ATOM 479 C CA . VAL A 1 62 ? 1.303 11.455 26.870 1.00 23.17 ? 62 VAL A CA 1
ATOM 480 C C . VAL A 1 62 ? 2.583 12.223 27.192 1.00 24.53 ? 62 VAL A C 1
ATOM 481 O O . VAL A 1 62 ? 3.248 11.937 28.191 1.00 24.00 ? 62 VAL A O 1
ATOM 482 C CB . VAL A 1 62 ? 1.683 10.168 26.118 1.00 22.67 ? 62 VAL A CB 1
ATOM 483 C CG1 . VAL A 1 62 ? 2.473 10.522 24.861 1.00 20.15 ? 62 VAL A CG1 1
ATOM 484 C CG2 . VAL A 1 62 ? 2.474 9.233 27.025 1.00 20.81 ? 62 VAL A CG2 1
ATOM 485 N N . ILE A 1 63 ? 2.927 13.199 26.356 1.00 24.86 ? 63 ILE A N 1
ATOM 486 C CA . ILE A 1 63 ? 4.152 13.952 26.575 1.00 27.00 ? 63 ILE A CA 1
ATOM 487 C C . ILE A 1 63 ? 4.131 14.837 27.808 1.00 29.12 ? 63 ILE A C 1
ATOM 488 O O . ILE A 1 63 ? 3.170 15.567 28.065 1.00 29.42 ? 63 ILE A O 1
ATOM 489 C CB . ILE A 1 63 ? 4.516 14.838 25.366 1.00 25.23 ? 63 ILE A CB 1
ATOM 490 C CG1 . ILE A 1 63 ? 4.784 13.968 24.139 1.00 24.39 ? 63 ILE A CG1 1
ATOM 491 C CG2 . ILE A 1 63 ? 5.755 15.663 25.690 1.00 24.46 ? 63 ILE A CG2 1
ATOM 492 C CD1 . ILE A 1 63 ? 5.091 14.767 22.880 1.00 21.65 ? 63 ILE A CD1 1
ATOM 493 N N . GLU A 1 64 ? 5.219 14.759 28.560 1.00 31.76 ? 64 GLU A N 1
ATOM 494 C CA . GLU A 1 64 ? 5.403 15.543 29.769 1.00 33.85 ? 64 GLU A CA 1
ATOM 495 C C . GLU A 1 64 ? 6.883 15.882 29.868 1.00 34.09 ? 64 GLU A C 1
ATOM 496 O O . GLU A 1 64 ? 7.741 15.054 29.543 1.00 34.43 ? 64 GLU A O 1
ATOM 497 C CB . GLU A 1 64 ? 4.985 14.743 30.999 1.00 36.86 ? 64 GLU A CB 1
ATOM 498 C CG . GLU A 1 64 ? 3.552 14.263 30.972 1.00 42.10 ? 64 GLU A CG 1
ATOM 499 C CD . GLU A 1 64 ? 3.102 13.739 32.316 1.00 45.48 ? 64 GLU A CD 1
ATOM 500 O OE1 . GLU A 1 64 ? 3.064 14.541 33.274 1.00 48.63 ? 64 GLU A OE1 1
ATOM 501 O OE2 . GLU A 1 64 ? 2.790 12.531 32.418 1.00 46.94 ? 64 GLU A OE2 1
ATOM 502 N N . VAL A 1 65 ? 7.180 17.102 30.296 1.00 32.53 ? 65 VAL A N 1
ATOM 503 C CA . VAL A 1 65 ? 8.559 17.531 30.447 1.00 32.11 ? 65 VAL A CA 1
ATOM 504 C C . VAL A 1 65 ? 8.857 17.609 31.938 1.00 32.46 ? 65 VAL A C 1
ATOM 505 O O . VAL A 1 65 ? 8.194 18.339 32.678 1.00 33.36 ? 65 VAL A O 1
ATOM 506 C CB . VAL A 1 65 ? 8.796 18.907 29.786 1.00 31.08 ? 65 VAL A CB 1
ATOM 507 C CG1 . VAL A 1 65 ? 10.252 19.310 29.932 1.00 31.12 ? 65 VAL A CG1 1
ATOM 508 C CG2 . VAL A 1 65 ? 8.418 18.844 28.315 1.00 29.86 ? 65 VAL A CG2 1
ATOM 509 N N . ASN A 1 66 ? 9.845 16.837 32.376 1.00 31.50 ? 66 ASN A N 1
ATOM 510 C CA . ASN A 1 66 ? 10.227 16.796 33.781 1.00 31.30 ? 66 ASN A CA 1
ATOM 511 C C . ASN A 1 66 ? 11.372 17.740 34.116 1.00 29.05 ? 66 ASN A C 1
ATOM 512 O O . ASN A 1 66 ? 11.747 18.593 33.312 1.00 26.31 ? 66 ASN A O 1
ATOM 513 C CB . ASN A 1 66 ? 10.642 15.379 34.163 1.00 35.66 ? 66 ASN A CB 1
ATOM 514 C CG . ASN A 1 66 ? 9.609 14.358 33.784 1.00 40.48 ? 66 ASN A CG 1
ATOM 515 O OD1 . ASN A 1 66 ? 8.513 14.324 34.349 1.00 45.24 ? 66 ASN A OD1 1
ATOM 516 N ND2 . ASN A 1 66 ? 9.944 13.518 32.814 1.00 42.90 ? 66 ASN A ND2 1
ATOM 517 N N . ASP A 1 67 ? 11.913 17.565 35.320 1.00 27.59 ? 67 ASP A N 1
ATOM 518 C CA . ASP A 1 67 ? 13.028 18.358 35.823 1.00 30.27 ? 67 ASP A CA 1
ATOM 519 C C . ASP A 1 67 ? 12.775 19.853 35.745 1.00 30.41 ? 67 ASP A C 1
ATOM 520 O O . ASP A 1 67 ? 13.701 20.642 35.568 1.00 30.70 ? 67 ASP A O 1
ATOM 521 C CB . ASP A 1 67 ? 14.299 18.005 35.051 1.00 30.58 ? 67 ASP A CB 1
ATOM 522 C CG . ASP A 1 67 ? 14.539 16.511 34.990 1.00 31.91 ? 67 ASP A CG 1
ATOM 523 O OD1 . ASP A 1 67 ? 14.366 15.841 36.030 1.00 31.36 ? 67 ASP A OD1 1
ATOM 524 O OD2 . ASP A 1 67 ? 14.902 16.009 33.906 1.00 33.53 ? 67 ASP A OD2 1
ATOM 525 N N . ARG A 1 68 ? 11.515 20.239 35.892 1.00 33.05 ? 68 ARG A N 1
ATOM 526 C CA . ARG A 1 68 ? 11.136 21.642 35.824 1.00 35.05 ? 68 ARG A CA 1
ATOM 527 C C . ARG A 1 68 ? 11.785 22.497 36.917 1.00 34.96 ? 68 ARG A C 1
ATOM 528 O O . ARG A 1 68 ? 12.000 23.691 36.719 1.00 36.75 ? 68 ARG A O 1
ATOM 529 C CB . ARG A 1 68 ? 9.612 21.769 35.899 1.00 37.39 ? 68 ARG A CB 1
ATOM 530 C CG . ARG A 1 68 ? 8.870 20.802 34.979 1.00 42.20 ? 68 ARG A CG 1
ATOM 531 C CD . ARG A 1 68 ? 8.302 19.618 35.759 1.00 46.76 ? 68 ARG A CD 1
ATOM 532 N NE . ARG A 1 68 ? 9.264 19.044 36.699 1.00 48.12 ? 68 ARG A NE 1
ATOM 533 C CZ . ARG A 1 68 ? 8.971 18.080 37.567 1.00 50.28 ? 68 ARG A CZ 1
ATOM 534 N NH1 . ARG A 1 68 ? 7.744 17.578 37.613 1.00 52.26 ? 68 ARG A NH1 1
ATOM 535 N NH2 . ARG A 1 68 ? 9.898 17.622 38.397 1.00 50.88 ? 68 ARG A NH2 1
ATOM 536 N N . LEU A 1 69 ? 12.102 21.890 38.058 1.00 34.11 ? 69 LEU A N 1
ATOM 537 C CA . LEU A 1 69 ? 12.716 22.628 39.166 1.00 34.93 ? 69 LEU A CA 1
ATOM 538 C C . LEU A 1 69 ? 14.227 22.435 39.259 1.00 34.98 ? 69 LEU A C 1
ATOM 539 O O . LEU A 1 69 ? 14.846 22.804 40.257 1.00 33.89 ? 69 LEU A O 1
ATOM 540 C CB . LEU A 1 69 ? 12.084 22.219 40.500 1.00 34.43 ? 69 LEU A CB 1
ATOM 541 C CG . LEU A 1 69 ? 10.556 22.256 40.609 1.00 35.56 ? 69 LEU A CG 1
ATOM 542 C CD1 . LEU A 1 69 ? 10.159 22.046 42.059 1.00 35.48 ? 69 LEU A CD1 1
ATOM 543 C CD2 . LEU A 1 69 ? 10.018 23.585 40.100 1.00 35.70 ? 69 LEU A CD2 1
ATOM 544 N N . LYS A 1 70 ? 14.819 21.854 38.222 1.00 34.15 ? 70 LYS A N 1
ATOM 545 C CA . LYS A 1 70 ? 16.257 21.629 38.209 1.00 34.26 ? 70 LYS A CA 1
ATOM 546 C C . LYS A 1 70 ? 16.943 22.657 37.325 1.00 32.74 ? 70 LYS A C 1
ATOM 547 O O . LYS A 1 70 ? 16.334 23.205 36.412 1.00 33.19 ? 70 LYS A O 1
ATOM 548 C CB . LYS A 1 70 ? 16.571 20.218 37.704 1.00 34.40 ? 70 LYS A CB 1
ATOM 549 C CG . LYS A 1 70 ? 16.138 19.118 38.643 1.00 36.36 ? 70 LYS A CG 1
ATOM 550 C CD . LYS A 1 70 ? 16.717 17.785 38.212 1.00 40.93 ? 70 LYS A CD 1
ATOM 551 C CE . LYS A 1 70 ? 16.439 16.701 39.241 1.00 42.14 ? 70 LYS A CE 1
ATOM 552 N NZ . LYS A 1 70 ? 17.051 15.400 38.844 1.00 45.36 ? 70 LYS A NZ 1
ATOM 553 N N . PRO A 1 71 ? 18.224 22.947 37.596 1.00 32.85 ? 71 PRO A N 1
ATOM 554 C CA . PRO A 1 71 ? 18.947 23.926 36.782 1.00 33.18 ? 71 PRO A CA 1
ATOM 555 C C . PRO A 1 71 ? 19.334 23.333 35.430 1.00 33.78 ? 71 PRO A C 1
ATOM 556 O O . PRO A 1 71 ? 19.417 22.114 35.278 1.00 33.96 ? 71 PRO A O 1
ATOM 557 C CB . PRO A 1 71 ? 20.161 24.248 37.642 1.00 32.60 ? 71 PRO A CB 1
ATOM 558 C CG . PRO A 1 71 ? 20.444 22.933 38.296 1.00 33.08 ? 71 PRO A CG 1
ATOM 559 C CD . PRO A 1 71 ? 19.065 22.460 38.704 1.00 32.39 ? 71 PRO A CD 1
ATOM 560 N N . MET A 1 72 ? 19.562 24.195 34.448 1.00 33.87 ? 72 MET A N 1
ATOM 561 C CA . MET A 1 72 ? 19.949 23.744 33.119 1.00 34.14 ? 72 MET A CA 1
ATOM 562 C C . MET A 1 72 ? 21.289 23.027 33.178 1.00 33.21 ? 72 MET A C 1
ATOM 563 O O . MET A 1 72 ? 22.140 23.357 34.000 1.00 32.59 ? 72 MET A O 1
ATOM 564 C CB . MET A 1 72 ? 20.070 24.935 32.168 1.00 35.63 ? 72 MET A CB 1
ATOM 565 C CG . MET A 1 72 ? 18.780 25.689 31.951 1.00 38.16 ? 72 MET A CG 1
ATOM 566 S SD . MET A 1 72 ? 17.520 24.641 31.201 1.00 41.27 ? 72 MET A SD 1
ATOM 567 C CE . MET A 1 72 ? 18.110 24.585 29.499 1.00 36.82 ? 72 MET A CE 1
ATOM 568 N N . VAL A 1 73 ? 21.470 22.038 32.311 1.00 31.50 ? 73 VAL A N 1
ATOM 569 C CA . VAL A 1 73 ? 22.731 21.313 32.255 1.00 31.00 ? 73 VAL A CA 1
ATOM 570 C C . VAL A 1 73 ? 23.732 22.304 31.666 1.00 31.94 ? 73 VAL A C 1
ATOM 571 O O . VAL A 1 73 ? 23.497 22.850 30.587 1.00 31.93 ? 73 VAL A O 1
ATOM 572 C CB . VAL A 1 73 ? 22.633 20.081 31.321 1.00 31.10 ? 73 VAL A CB 1
ATOM 573 C CG1 . VAL A 1 73 ? 23.979 19.374 31.241 1.00 32.53 ? 73 VAL A CG1 1
ATOM 574 C CG2 . VAL A 1 73 ? 21.563 19.125 31.827 1.00 31.15 ? 73 VAL A CG2 1
ATOM 575 N N . ASN A 1 74 ? 24.829 22.560 32.373 1.00 33.16 ? 74 ASN A N 1
ATOM 576 C CA . ASN A 1 74 ? 25.835 23.492 31.867 1.00 35.46 ? 74 ASN A CA 1
ATOM 577 C C . ASN A 1 74 ? 26.745 22.695 30.944 1.00 34.16 ? 74 ASN A C 1
ATOM 578 O O . ASN A 1 74 ? 27.442 21.787 31.382 1.00 33.87 ? 74 ASN A O 1
ATOM 579 C CB . ASN A 1 74 ? 26.653 24.097 33.012 1.00 37.35 ? 74 ASN A CB 1
ATOM 580 C CG . ASN A 1 74 ? 27.445 25.319 32.576 1.00 40.16 ? 74 ASN A CG 1
ATOM 581 O OD1 . ASN A 1 74 ? 28.071 25.321 31.515 1.00 40.85 ? 74 ASN A OD1 1
ATOM 582 N ND2 . ASN A 1 74 ? 27.424 26.362 33.396 1.00 40.40 ? 74 ASN A ND2 1
ATOM 583 N N . LEU A 1 75 ? 26.738 23.033 29.662 1.00 32.71 ? 75 LEU A N 1
ATOM 584 C CA . LEU A 1 75 ? 27.543 22.291 28.705 1.00 32.73 ? 75 LEU A CA 1
ATOM 585 C C . LEU A 1 75 ? 28.897 22.915 28.386 1.00 34.00 ? 75 LEU A C 1
ATOM 586 O O . LEU A 1 75 ? 29.820 22.219 27.964 1.00 36.05 ? 75 LEU A O 1
ATOM 587 C CB . LEU A 1 75 ? 26.736 22.109 27.417 1.00 30.12 ? 75 LEU A CB 1
ATOM 588 C CG . LEU A 1 75 ? 25.366 21.461 27.648 1.00 29.54 ? 75 LEU A CG 1
ATOM 589 C CD1 . LEU A 1 75 ? 24.559 21.444 26.359 1.00 27.79 ? 75 LEU A CD1 1
ATOM 590 C CD2 . LEU A 1 75 ? 25.568 20.050 28.192 1.00 26.88 ? 75 LEU A CD2 1
ATOM 591 N N . VAL A 1 76 ? 29.018 24.216 28.616 1.00 33.37 ? 76 VAL A N 1
ATOM 592 C CA . VAL A 1 76 ? 30.241 24.946 28.303 1.00 35.22 ? 76 VAL A CA 1
ATOM 593 C C . VAL A 1 76 ? 31.118 25.362 29.483 1.00 35.20 ? 76 VAL A C 1
ATOM 594 O O . VAL A 1 76 ? 32.191 25.928 29.284 1.00 34.73 ? 76 VAL A O 1
ATOM 595 C CB . VAL A 1 76 ? 29.896 26.211 27.500 1.00 35.90 ? 76 VAL A CB 1
ATOM 596 C CG1 . VAL A 1 76 ? 29.201 25.823 26.207 1.00 33.94 ? 76 VAL A CG1 1
ATOM 597 C CG2 . VAL A 1 76 ? 28.997 27.116 28.330 1.00 35.23 ? 76 VAL A CG2 1
ATOM 598 N N . ASP A 1 77 ? 30.670 25.078 30.702 1.00 35.36 ? 77 ASP A N 1
ATOM 599 C CA . ASP A 1 77 ? 31.416 25.441 31.908 1.00 37.08 ? 77 ASP A CA 1
ATOM 600 C C . ASP A 1 77 ? 32.903 25.067 31.881 1.00 35.10 ? 77 ASP A C 1
ATOM 601 O O . ASP A 1 77 ? 33.735 25.785 32.426 1.00 33.75 ? 77 ASP A O 1
ATOM 602 C CB . ASP A 1 77 ? 30.761 24.793 33.133 1.00 40.07 ? 77 ASP A CB 1
ATOM 603 C CG . ASP A 1 77 ? 30.764 23.272 33.060 1.00 44.13 ? 77 ASP A CG 1
ATOM 604 O OD1 . ASP A 1 77 ? 31.857 22.671 33.132 1.00 46.42 ? 77 ASP A OD1 1
ATOM 605 O OD2 . ASP A 1 77 ? 29.673 22.676 32.923 1.00 46.01 ? 77 ASP A OD2 1
ATOM 606 N N . SER A 1 78 ? 33.232 23.945 31.248 1.00 34.47 ? 78 SER A N 1
ATOM 607 C CA . SER A 1 78 ? 34.614 23.474 31.184 1.00 33.85 ? 78 SER A CA 1
ATOM 608 C C . SER A 1 78 ? 35.489 24.204 30.169 1.00 32.38 ? 78 SER A C 1
ATOM 609 O O . SER A 1 78 ? 36.707 24.017 30.152 1.00 30.89 ? 78 SER A O 1
ATOM 610 C CB . SER A 1 78 ? 34.639 21.974 30.871 1.00 37.28 ? 78 SER A CB 1
ATOM 611 O OG . SER A 1 78 ? 33.944 21.233 31.860 1.00 43.08 ? 78 SER A OG 1
ATOM 612 N N . LEU A 1 79 ? 34.879 25.030 29.323 1.00 28.80 ? 79 LEU A N 1
ATOM 613 C CA . LEU A 1 79 ? 35.640 25.754 28.314 1.00 27.23 ? 79 LEU A CA 1
ATOM 614 C C . LEU A 1 79 ? 36.025 27.152 28.768 1.00 26.06 ? 79 LEU A C 1
ATOM 615 O O . LEU A 1 79 ? 35.341 27.773 29.575 1.00 25.47 ? 79 LEU A O 1
ATOM 616 C CB . LEU A 1 79 ? 34.849 25.859 27.004 1.00 26.51 ? 79 LEU A CB 1
ATOM 617 C CG . LEU A 1 79 ? 34.420 24.560 26.315 1.00 25.14 ? 79 LEU A CG 1
ATOM 618 C CD1 . LEU A 1 79 ? 33.754 24.904 24.989 1.00 25.81 ? 79 LEU A CD1 1
ATOM 619 C CD2 . LEU A 1 79 ? 35.626 23.655 26.092 1.00 24.39 ? 79 LEU A CD2 1
ATOM 620 N N . LYS A 1 80 ? 37.139 27.629 28.239 1.00 26.45 ? 80 LYS A N 1
ATOM 621 C CA . LYS A 1 80 ? 37.639 28.959 28.536 1.00 26.81 ? 80 LYS A CA 1
ATOM 622 C C . LYS A 1 80 ? 36.783 29.950 27.753 1.00 26.52 ? 80 LYS A C 1
ATOM 623 O O . LYS A 1 80 ? 36.347 29.668 26.635 1.00 24.23 ? 80 LYS A O 1
ATOM 624 C CB . LYS A 1 80 ? 39.107 29.050 28.108 1.00 29.65 ? 80 LYS A CB 1
ATOM 625 C CG . LYS A 1 80 ? 39.588 30.435 27.722 1.00 34.28 ? 80 LYS A CG 1
ATOM 626 C CD . LYS A 1 80 ? 40.974 30.362 27.091 1.00 37.16 ? 80 LYS A CD 1
ATOM 627 C CE . LYS A 1 80 ? 41.337 31.665 26.406 1.00 38.86 ? 80 LYS A CE 1
ATOM 628 N NZ . LYS A 1 80 ? 41.268 32.806 27.358 1.00 40.94 ? 80 LYS A NZ 1
ATOM 629 N N . THR A 1 81 ? 36.523 31.105 28.347 1.00 26.15 ? 81 THR A N 1
ATOM 630 C CA . THR A 1 81 ? 35.718 32.114 27.684 1.00 26.58 ? 81 THR A CA 1
ATOM 631 C C . THR A 1 81 ? 36.600 32.999 26.819 1.00 27.45 ? 81 THR A C 1
ATOM 632 O O . THR A 1 81 ? 37.638 33.484 27.269 1.00 28.06 ? 81 THR A O 1
ATOM 633 C CB . THR A 1 81 ? 34.976 33.014 28.699 1.00 27.08 ? 81 THR A CB 1
ATOM 634 O OG1 . THR A 1 81 ? 34.081 32.220 29.483 1.00 28.84 ? 81 THR A OG1 1
ATOM 635 C CG2 . THR A 1 81 ? 34.183 34.089 27.977 1.00 27.76 ? 81 THR A CG2 1
ATOM 636 N N . LEU A 1 82 ? 36.190 33.194 25.571 1.00 26.37 ? 82 LEU A N 1
ATOM 637 C CA . LEU A 1 82 ? 36.933 34.056 24.669 1.00 29.27 ? 82 LEU A CA 1
ATOM 638 C C . LEU A 1 82 ? 36.571 35.452 25.154 1.00 29.62 ? 82 LEU A C 1
ATOM 639 O O . LEU A 1 82 ? 35.439 35.896 24.976 1.00 30.16 ? 82 LEU A O 1
ATOM 640 C CB . LEU A 1 82 ? 36.462 33.866 23.223 1.00 25.59 ? 82 LEU A CB 1
ATOM 641 C CG . LEU A 1 82 ? 37.238 34.656 22.164 1.00 25.99 ? 82 LEU A CG 1
ATOM 642 C CD1 . LEU A 1 82 ? 38.696 34.234 22.181 1.00 24.93 ? 82 LEU A CD1 1
ATOM 643 C CD2 . LEU A 1 82 ? 36.639 34.412 20.790 1.00 25.61 ? 82 LEU A CD2 1
ATOM 644 N N . GLN A 1 83 ? 37.520 36.131 25.787 1.00 32.82 ? 83 GLN A N 1
ATOM 645 C CA . GLN A 1 83 ? 37.261 37.468 26.311 1.00 35.12 ? 83 GLN A CA 1
ATOM 646 C C . GLN A 1 83 ? 36.736 38.410 25.228 1.00 34.53 ? 83 GLN A C 1
ATOM 647 O O . GLN A 1 83 ? 37.117 38.307 24.063 1.00 32.59 ? 83 GLN A O 1
ATOM 648 C CB . GLN A 1 83 ? 38.529 38.036 26.948 1.00 37.87 ? 83 GLN A CB 1
ATOM 649 C CG . GLN A 1 83 ? 39.064 37.197 28.107 1.00 40.59 ? 83 GLN A CG 1
ATOM 650 C CD . GLN A 1 83 ? 38.013 36.923 29.175 1.00 43.70 ? 83 GLN A CD 1
ATOM 651 O OE1 . GLN A 1 83 ? 37.327 37.836 29.641 1.00 44.30 ? 83 GLN A OE1 1
ATOM 652 N NE2 . GLN A 1 83 ? 37.892 35.660 29.575 1.00 43.50 ? 83 GLN A NE2 1
ATOM 653 N N . PRO A 1 84 ? 35.853 39.348 25.609 1.00 35.99 ? 84 PRO A N 1
ATOM 654 C CA . PRO A 1 84 ? 35.252 40.322 24.693 1.00 36.02 ? 84 PRO A CA 1
ATOM 655 C C . PRO A 1 84 ? 36.200 40.943 23.671 1.00 35.54 ? 84 PRO A C 1
ATOM 656 O O . PRO A 1 84 ? 35.831 41.128 22.514 1.00 35.57 ? 84 PRO A O 1
ATOM 657 C CB . PRO A 1 84 ? 34.655 41.351 25.645 1.00 36.33 ? 84 PRO A CB 1
ATOM 658 C CG . PRO A 1 84 ? 34.202 40.491 26.781 1.00 36.00 ? 84 PRO A CG 1
ATOM 659 C CD . PRO A 1 84 ? 35.410 39.606 26.992 1.00 35.88 ? 84 PRO A CD 1
ATOM 660 N N . ASN A 1 85 ? 37.421 41.260 24.088 1.00 36.95 ? 85 ASN A N 1
ATOM 661 C CA . ASN A 1 85 ? 38.375 41.860 23.166 1.00 38.01 ? 85 ASN A CA 1
ATOM 662 C C . ASN A 1 85 ? 38.786 40.888 22.064 1.00 37.94 ? 85 ASN A C 1
ATOM 663 O O . ASN A 1 85 ? 38.902 41.278 20.899 1.00 38.00 ? 85 ASN A O 1
ATOM 664 C CB . ASN A 1 85 ? 39.611 42.376 23.920 1.00 40.52 ? 85 ASN A CB 1
ATOM 665 C CG . ASN A 1 85 ? 40.321 41.291 24.708 1.00 42.99 ? 85 ASN A CG 1
ATOM 666 O OD1 . ASN A 1 85 ? 39.739 40.664 25.594 1.00 44.79 ? 85 ASN A OD1 1
ATOM 667 N ND2 . ASN A 1 85 ? 41.594 41.071 24.392 1.00 44.55 ? 85 ASN A ND2 1
ATOM 668 N N . LYS A 1 86 ? 38.998 39.626 22.430 1.00 35.43 ? 86 LYS A N 1
ATOM 669 C CA . LYS A 1 86 ? 39.386 38.609 21.455 1.00 34.59 ? 86 LYS A CA 1
ATOM 670 C C . LYS A 1 86 ? 38.224 38.278 20.518 1.00 32.49 ? 86 LYS A C 1
ATOM 671 O O . LYS A 1 86 ? 38.434 37.982 19.344 1.00 32.10 ? 86 LYS A O 1
ATOM 672 C CB . LYS A 1 86 ? 39.861 37.344 22.170 1.00 35.31 ? 86 LYS A CB 1
ATOM 673 C CG . LYS A 1 86 ? 41.134 37.535 22.988 1.00 38.83 ? 86 LYS A CG 1
ATOM 674 C CD . LYS A 1 86 ? 41.517 36.261 23.741 1.00 40.23 ? 86 LYS A CD 1
ATOM 675 C CE . LYS A 1 86 ? 40.427 35.842 24.725 1.00 41.58 ? 86 LYS A CE 1
ATOM 676 N NZ . LYS A 1 86 ? 40.759 34.582 25.447 1.00 38.67 ? 86 LYS A NZ 1
ATOM 677 N N . VAL A 1 87 ? 37.000 38.325 21.036 1.00 31.43 ? 87 VAL A N 1
ATOM 678 C CA . VAL A 1 87 ? 35.827 38.059 20.214 1.00 31.55 ? 87 VAL A CA 1
ATOM 679 C C . VAL A 1 87 ? 35.808 39.092 19.092 1.00 32.48 ? 87 VAL A C 1
ATOM 680 O O . VAL A 1 87 ? 35.587 38.764 17.925 1.00 30.53 ? 87 VAL A O 1
ATOM 681 C CB . VAL A 1 87 ? 34.510 38.182 21.030 1.00 31.10 ? 87 VAL A CB 1
ATOM 682 C CG1 . VAL A 1 87 ? 33.312 37.965 20.120 1.00 28.76 ? 87 VAL A CG1 1
ATOM 683 C CG2 . VAL A 1 87 ? 34.496 37.169 22.160 1.00 31.45 ? 87 VAL A CG2 1
ATOM 684 N N . ALA A 1 88 ? 36.056 40.346 19.456 1.00 33.41 ? 88 ALA A N 1
ATOM 685 C CA . ALA A 1 88 ? 36.075 41.435 18.489 1.00 32.82 ? 88 ALA A CA 1
ATOM 686 C C . ALA A 1 88 ? 37.178 41.212 17.454 1.00 33.20 ? 88 ALA A C 1
ATOM 687 O O . ALA A 1 88 ? 36.959 41.375 16.255 1.00 32.59 ? 88 ALA A O 1
ATOM 688 C CB . ALA A 1 88 ? 36.285 42.767 19.213 1.00 33.98 ? 88 ALA A CB 1
ATOM 689 N N . GLU A 1 89 ? 38.364 40.839 17.923 1.00 33.50 ? 89 GLU A N 1
ATOM 690 C CA . GLU A 1 89 ? 39.490 40.588 17.029 1.00 35.73 ? 89 GLU A CA 1
ATOM 691 C C . GLU A 1 89 ? 39.119 39.495 16.021 1.00 36.18 ? 89 GLU A C 1
ATOM 692 O O . GLU A 1 89 ? 39.332 39.650 14.819 1.00 34.97 ? 89 GLU A O 1
ATOM 693 C CB . GLU A 1 89 ? 40.717 40.148 17.835 1.00 37.91 ? 89 GLU A CB 1
ATOM 694 C CG . GLU A 1 89 ? 41.992 40.037 17.012 1.00 41.83 ? 89 GLU A CG 1
ATOM 695 C CD . GLU A 1 89 ? 43.132 39.397 17.781 1.00 44.86 ? 89 GLU A CD 1
ATOM 696 O OE1 . GLU A 1 89 ? 43.399 39.827 18.924 1.00 46.54 ? 89 GLU A OE1 1
ATOM 697 O OE2 . GLU A 1 89 ? 43.769 38.467 17.239 1.00 47.86 ? 89 GLU A OE2 1
ATOM 698 N N . MET A 1 90 ? 38.567 38.391 16.523 1.00 35.57 ? 90 MET A N 1
ATOM 699 C CA . MET A 1 90 ? 38.159 37.273 15.672 1.00 34.09 ? 90 MET A CA 1
ATOM 700 C C . MET A 1 90 ? 37.141 37.727 14.639 1.00 33.35 ? 90 MET A C 1
ATOM 701 O O . MET A 1 90 ? 37.290 37.459 13.445 1.00 32.50 ? 90 MET A O 1
ATOM 702 C CB . MET A 1 90 ? 37.544 36.152 16.516 1.00 34.09 ? 90 MET A CB 1
ATOM 703 C CG . MET A 1 90 ? 36.837 35.072 15.695 1.00 32.88 ? 90 MET A CG 1
ATOM 704 S SD . MET A 1 90 ? 35.856 33.977 16.734 1.00 35.50 ? 90 MET A SD 1
ATOM 705 C CE . MET A 1 90 ? 34.384 34.984 16.986 1.00 36.25 ? 90 MET A CE 1
ATOM 706 N N . ILE A 1 91 ? 36.096 38.399 15.109 1.00 33.11 ? 91 ILE A N 1
ATOM 707 C CA . ILE A 1 91 ? 35.052 38.898 14.226 1.00 35.23 ? 91 ILE A CA 1
ATOM 708 C C . ILE A 1 91 ? 35.677 39.806 13.179 1.00 35.48 ? 91 ILE A C 1
ATOM 709 O O . ILE A 1 91 ? 35.290 39.786 12.012 1.00 35.65 ? 91 ILE A O 1
ATOM 710 C CB . ILE A 1 91 ? 33.986 39.709 14.998 1.00 35.73 ? 91 ILE A CB 1
ATOM 711 C CG1 . ILE A 1 91 ? 33.237 38.798 15.975 1.00 36.61 ? 91 ILE A CG1 1
ATOM 712 C CG2 . ILE A 1 91 ? 33.022 40.370 14.015 1.00 35.48 ? 91 ILE A CG2 1
ATOM 713 C CD1 . ILE A 1 91 ? 32.534 37.627 15.313 1.00 36.88 ? 91 ILE A CD1 1
ATOM 714 N N . GLU A 1 92 ? 36.651 40.598 13.610 1.00 37.20 ? 92 GLU A N 1
ATOM 715 C CA . GLU A 1 92 ? 37.337 41.521 12.718 1.00 38.83 ? 92 GLU A CA 1
ATOM 716 C C . GLU A 1 92 ? 38.112 40.758 11.649 1.00 36.82 ? 92 GLU A C 1
ATOM 717 O O . GLU A 1 92 ? 38.160 41.171 10.492 1.00 35.81 ? 92 GLU A O 1
ATOM 718 C CB . GLU A 1 92 ? 38.278 42.413 13.528 1.00 41.97 ? 92 GLU A CB 1
ATOM 719 C CG . GLU A 1 92 ? 38.928 43.529 12.735 1.00 47.41 ? 92 GLU A CG 1
ATOM 720 C CD . GLU A 1 92 ? 39.451 44.634 13.629 1.00 49.78 ? 92 GLU A CD 1
ATOM 721 O OE1 . GLU A 1 92 ? 38.625 45.279 14.310 1.00 51.73 ? 92 GLU A OE1 1
ATOM 722 O OE2 . GLU A 1 92 ? 40.680 44.858 13.657 1.00 51.90 ? 92 GLU A OE2 1
ATOM 723 N N . ASN A 1 93 ? 38.713 39.638 12.039 1.00 35.34 ? 93 ASN A N 1
ATOM 724 C CA . ASN A 1 93 ? 39.466 38.819 11.096 1.00 32.90 ? 93 ASN A CA 1
ATOM 725 C C . ASN A 1 93 ? 38.558 37.825 10.381 1.00 32.00 ? 93 ASN A C 1
ATOM 726 O O . ASN A 1 93 ? 38.918 36.662 10.204 1.00 30.21 ? 93 ASN A O 1
ATOM 727 C CB . ASN A 1 93 ? 40.586 38.064 11.814 1.00 33.71 ? 93 ASN A CB 1
ATOM 728 C CG . ASN A 1 93 ? 41.631 38.990 12.389 1.00 35.22 ? 93 ASN A CG 1
ATOM 729 O OD1 . ASN A 1 93 ? 42.101 39.905 11.715 1.00 35.94 ? 93 ASN A OD1 1
ATOM 730 N ND2 . ASN A 1 93 ? 42.011 38.753 13.634 1.00 35.10 ? 93 ASN A ND2 1
ATOM 731 N N . GLN A 1 94 ? 37.376 38.291 9.986 1.00 29.98 ? 94 GLN A N 1
ATOM 732 C CA . GLN A 1 94 ? 36.407 37.467 9.268 1.00 31.57 ? 94 GLN A CA 1
ATOM 733 C C . GLN A 1 94 ? 35.957 36.206 10.022 1.00 31.08 ? 94 GLN A C 1
ATOM 734 O O . GLN A 1 94 ? 35.611 35.197 9.400 1.00 30.74 ? 94 GLN A O 1
ATOM 735 C CB . GLN A 1 94 ? 36.983 37.058 7.908 1.00 33.39 ? 94 GLN A CB 1
ATOM 736 C CG . GLN A 1 94 ? 37.626 38.191 7.115 1.00 34.60 ? 94 GLN A CG 1
ATOM 737 C CD . GLN A 1 94 ? 36.721 39.401 6.961 1.00 36.43 ? 94 GLN A CD 1
ATOM 738 O OE1 . GLN A 1 94 ? 36.576 40.205 7.879 1.00 38.50 ? 94 GLN A OE1 1
ATOM 739 N NE2 . GLN A 1 94 ? 36.103 39.529 5.798 1.00 38.88 ? 94 GLN A NE2 1
ATOM 740 N N . GLY A 1 95 ? 35.962 36.270 11.350 1.00 29.81 ? 95 GLY A N 1
ATOM 741 C CA . GLY A 1 95 ? 35.553 35.135 12.163 1.00 28.83 ? 95 GLY A CA 1
ATOM 742 C C . GLY A 1 95 ? 36.567 34.003 12.144 1.00 29.50 ? 95 GLY A C 1
ATOM 743 O O . GLY A 1 95 ? 36.199 32.830 12.237 1.00 29.44 ? 95 GLY A O 1
ATOM 744 N N . LEU A 1 96 ? 37.846 34.358 12.044 1.00 28.23 ? 96 LEU A N 1
ATOM 745 C CA . LEU A 1 96 ? 38.919 33.375 11.988 1.00 28.43 ? 96 LEU A CA 1
ATOM 746 C C . LEU A 1 96 ? 40.031 33.575 13.013 1.00 28.91 ? 96 LEU A C 1
ATOM 747 O O . LEU A 1 96 ? 40.226 34.676 13.530 1.00 26.11 ? 96 LEU A O 1
ATOM 748 C CB . LEU A 1 96 ? 39.532 33.387 10.592 1.00 30.37 ? 96 LEU A CB 1
ATOM 749 C CG . LEU A 1 96 ? 38.589 32.962 9.469 1.00 30.84 ? 96 LEU A CG 1
ATOM 750 C CD1 . LEU A 1 96 ? 39.194 33.311 8.127 1.00 34.72 ? 96 LEU A CD1 1
ATOM 751 C CD2 . LEU A 1 96 ? 38.324 31.473 9.577 1.00 32.43 ? 96 LEU A CD2 1
ATOM 752 N N . PHE A 1 97 ? 40.747 32.488 13.298 1.00 30.72 ? 97 PHE A N 1
ATOM 753 C CA . PHE A 1 97 ? 41.887 32.488 14.218 1.00 30.84 ? 97 PHE A CA 1
ATOM 754 C C . PHE A 1 97 ? 43.086 32.194 13.321 1.00 32.15 ? 97 PHE A C 1
ATOM 755 O O . PHE A 1 97 ? 43.454 31.037 13.121 1.00 32.83 ? 97 PHE A O 1
ATOM 756 C CB . PHE A 1 97 ? 41.764 31.373 15.260 1.00 30.14 ? 97 PHE A CB 1
ATOM 757 C CG . PHE A 1 97 ? 40.611 31.536 16.205 1.00 29.22 ? 97 PHE A CG 1
ATOM 758 C CD1 . PHE A 1 97 ? 40.536 32.636 17.053 1.00 30.29 ? 97 PHE A CD1 1
ATOM 759 C CD2 . PHE A 1 97 ? 39.611 30.571 16.269 1.00 28.85 ? 97 PHE A CD2 1
ATOM 760 C CE1 . PHE A 1 97 ? 39.479 32.773 17.957 1.00 30.19 ? 97 PHE A CE1 1
ATOM 761 C CE2 . PHE A 1 97 ? 38.552 30.695 17.166 1.00 30.52 ? 97 PHE A CE2 1
ATOM 762 C CZ . PHE A 1 97 ? 38.487 31.802 18.015 1.00 29.36 ? 97 PHE A CZ 1
ATOM 763 N N . LYS A 1 98 ? 43.689 33.249 12.788 1.00 33.47 ? 98 LYS A N 1
ATOM 764 C CA . LYS A 1 98 ? 44.815 33.127 11.869 1.00 35.64 ? 98 LYS A CA 1
ATOM 765 C C . LYS A 1 98 ? 45.921 32.131 12.207 1.00 34.96 ? 98 LYS A C 1
ATOM 766 O O . LYS A 1 98 ? 46.340 31.358 11.349 1.00 35.84 ? 98 LYS A O 1
ATOM 767 C CB . LYS A 1 98 ? 45.448 34.502 11.641 1.00 39.05 ? 98 LYS A CB 1
ATOM 768 C CG . LYS A 1 98 ? 46.556 34.498 10.597 1.00 42.98 ? 98 LYS A CG 1
ATOM 769 C CD . LYS A 1 98 ? 47.094 35.900 10.347 1.00 46.11 ? 98 LYS A CD 1
ATOM 770 C CE . LYS A 1 98 ? 48.195 35.887 9.299 1.00 47.14 ? 98 LYS A CE 1
ATOM 771 N NZ . LYS A 1 98 ? 49.329 35.015 9.715 1.00 49.65 ? 98 LYS A NZ 1
ATOM 772 N N . ASP A 1 99 ? 46.387 32.137 13.450 1.00 33.88 ? 99 ASP A N 1
ATOM 773 C CA . ASP A 1 99 ? 47.488 31.263 13.839 1.00 33.51 ? 99 ASP A CA 1
ATOM 774 C C . ASP A 1 99 ? 47.164 29.835 14.266 1.00 31.63 ? 99 ASP A C 1
ATOM 775 O O . ASP A 1 99 ? 48.068 29.096 14.656 1.00 31.33 ? 99 ASP A O 1
ATOM 776 C CB . ASP A 1 99 ? 48.301 31.936 14.950 1.00 37.13 ? 99 ASP A CB 1
ATOM 777 C CG . ASP A 1 99 ? 48.777 33.327 14.563 1.00 40.45 ? 99 ASP A CG 1
ATOM 778 O OD1 . ASP A 1 99 ? 49.335 33.482 13.452 1.00 42.89 ? 99 ASP A OD1 1
ATOM 779 O OD2 . ASP A 1 99 ? 48.597 34.262 15.371 1.00 41.62 ? 99 ASP A OD2 1
ATOM 780 N N . HIS A 1 100 ? 45.901 29.430 14.183 1.00 29.10 ? 100 HIS A N 1
ATOM 781 C CA . HIS A 1 100 ? 45.536 28.083 14.609 1.00 27.59 ? 100 HIS A CA 1
ATOM 782 C C . HIS A 1 100 ? 44.725 27.244 13.623 1.00 25.40 ? 100 HIS A C 1
ATOM 783 O O . HIS A 1 100 ? 44.268 26.160 13.975 1.00 25.10 ? 100 HIS A O 1
ATOM 784 C CB . HIS A 1 100 ? 44.768 28.160 15.933 1.00 28.68 ? 100 HIS A CB 1
ATOM 785 C CG . HIS A 1 100 ? 45.576 28.695 17.075 1.00 29.13 ? 100 HIS A CG 1
ATOM 786 N ND1 . HIS A 1 100 ? 46.619 27.995 17.641 1.00 30.28 ? 100 HIS A ND1 1
ATOM 787 C CD2 . HIS A 1 100 ? 45.496 29.864 17.753 1.00 29.69 ? 100 HIS A CD2 1
ATOM 788 C CE1 . HIS A 1 100 ? 47.147 28.709 18.619 1.00 30.63 ? 100 HIS A CE1 1
ATOM 789 N NE2 . HIS A 1 100 ? 46.484 29.848 18.709 1.00 31.30 ? 100 HIS A NE2 1
ATOM 790 N N . VAL A 1 101 ? 44.558 27.713 12.393 1.00 23.98 ? 101 VAL A N 1
ATOM 791 C CA . VAL A 1 101 ? 43.759 26.971 11.424 1.00 22.42 ? 101 VAL A CA 1
ATOM 792 C C . VAL A 1 101 ? 44.153 25.512 11.177 1.00 22.44 ? 101 VAL A C 1
ATOM 793 O O . VAL A 1 101 ? 43.325 24.719 10.742 1.00 21.97 ? 101 VAL A O 1
ATOM 794 C CB . VAL A 1 101 ? 43.686 27.720 10.070 1.00 22.08 ? 101 VAL A CB 1
ATOM 795 C CG1 . VAL A 1 101 ? 43.038 29.082 10.281 1.00 22.18 ? 101 VAL A CG1 1
ATOM 796 C CG2 . VAL A 1 101 ? 45.077 27.862 9.456 1.00 22.17 ? 101 VAL A CG2 1
ATOM 797 N N . GLU A 1 102 ? 45.403 25.150 11.456 1.00 24.23 ? 102 GLU A N 1
ATOM 798 C CA . GLU A 1 102 ? 45.859 23.772 11.258 1.00 22.58 ? 102 GLU A CA 1
ATOM 799 C C . GLU A 1 102 ? 46.260 23.137 12.593 1.00 24.22 ? 102 GLU A C 1
ATOM 800 O O . GLU A 1 102 ? 46.838 22.050 12.633 1.00 24.09 ? 102 GLU A O 1
ATOM 801 C CB . GLU A 1 102 ? 47.051 23.738 10.293 1.00 24.97 ? 102 GLU A CB 1
ATOM 802 C CG . GLU A 1 102 ? 46.770 24.352 8.927 1.00 24.06 ? 102 GLU A CG 1
ATOM 803 C CD . GLU A 1 102 ? 47.999 24.377 8.031 1.00 24.50 ? 102 GLU A CD 1
ATOM 804 O OE1 . GLU A 1 102 ? 48.427 23.304 7.560 1.00 27.94 ? 102 GLU A OE1 1
ATOM 805 O OE2 . GLU A 1 102 ? 48.544 25.473 7.803 1.00 24.45 ? 102 GLU A OE2 1
ATOM 806 N N . ASP A 1 103 ? 45.943 23.821 13.685 1.00 21.79 ? 103 ASP A N 1
ATOM 807 C CA . ASP A 1 103 ? 46.272 23.335 15.019 1.00 20.95 ? 103 ASP A CA 1
ATOM 808 C C . ASP A 1 103 ? 45.168 22.438 15.580 1.00 20.87 ? 103 ASP A C 1
ATOM 809 O O . ASP A 1 103 ? 44.147 22.923 16.076 1.00 21.27 ? 103 ASP A O 1
ATOM 810 C CB . ASP A 1 103 ? 46.501 24.529 15.943 1.00 21.06 ? 103 ASP A CB 1
ATOM 811 C CG . ASP A 1 103 ? 46.908 24.118 17.336 1.00 21.76 ? 103 ASP A CG 1
ATOM 812 O OD1 . ASP A 1 103 ? 47.244 22.933 17.538 1.00 24.64 ? 103 ASP A OD1 1
ATOM 813 O OD2 . ASP A 1 103 ? 46.899 24.990 18.227 1.00 26.32 ? 103 ASP A OD2 1
ATOM 814 N N . VAL A 1 104 ? 45.382 21.128 15.517 1.00 19.37 ? 104 VAL A N 1
ATOM 815 C CA . VAL A 1 104 ? 44.389 20.182 16.002 1.00 19.56 ? 104 VAL A CA 1
ATOM 816 C C . VAL A 1 104 ? 44.254 20.174 17.520 1.00 19.84 ? 104 VAL A C 1
ATOM 817 O O . VAL A 1 104 ? 43.287 19.634 18.059 1.00 21.38 ? 104 VAL A O 1
ATOM 818 C CB . VAL A 1 104 ? 44.684 18.747 15.478 1.00 19.70 ? 104 VAL A CB 1
ATOM 819 C CG1 . VAL A 1 104 ? 44.787 18.776 13.946 1.00 20.04 ? 104 VAL A CG1 1
ATOM 820 C CG2 . VAL A 1 104 ? 45.980 18.201 16.081 1.00 19.55 ? 104 VAL A CG2 1
ATOM 821 N N . ASN A 1 105 ? 45.210 20.791 18.209 1.00 21.01 ? 105 ASN A N 1
ATOM 822 C CA . ASN A 1 105 ? 45.174 20.852 19.671 1.00 21.91 ? 105 ASN A CA 1
ATOM 823 C C . ASN A 1 105 ? 44.602 22.162 20.213 1.00 21.54 ? 105 ASN A C 1
ATOM 824 O O . ASN A 1 105 ? 44.542 22.367 21.425 1.00 20.77 ? 105 ASN A O 1
ATOM 825 C CB . ASN A 1 105 ? 46.572 20.618 20.264 1.00 24.93 ? 105 ASN A CB 1
ATOM 826 C CG . ASN A 1 105 ? 46.852 19.149 20.544 1.00 28.10 ? 105 ASN A CG 1
ATOM 827 O OD1 . ASN A 1 105 ? 47.814 18.811 21.235 1.00 33.27 ? 105 ASN A OD1 1
ATOM 828 N ND2 . ASN A 1 105 ? 46.016 18.271 20.006 1.00 29.03 ? 105 ASN A ND2 1
ATOM 829 N N . PHE A 1 106 ? 44.190 23.055 19.320 1.00 20.08 ? 106 PHE A N 1
ATOM 830 C CA . PHE A 1 106 ? 43.591 24.309 19.744 1.00 21.01 ? 106 PHE A CA 1
ATOM 831 C C . PHE A 1 106 ? 42.290 23.935 20.442 1.00 21.12 ? 106 PHE A C 1
ATOM 832 O O . PHE A 1 106 ? 41.438 23.274 19.854 1.00 23.05 ? 106 PHE A O 1
ATOM 833 C CB . PHE A 1 106 ? 43.297 25.192 18.530 1.00 23.03 ? 106 PHE A CB 1
ATOM 834 C CG . PHE A 1 106 ? 42.666 26.512 18.872 1.00 24.63 ? 106 PHE A CG 1
ATOM 835 C CD1 . PHE A 1 106 ? 43.357 27.454 19.629 1.00 25.69 ? 106 PHE A CD1 1
ATOM 836 C CD2 . PHE A 1 106 ? 41.386 26.821 18.425 1.00 25.56 ? 106 PHE A CD2 1
ATOM 837 C CE1 . PHE A 1 106 ? 42.784 28.683 19.932 1.00 28.52 ? 106 PHE A CE1 1
ATOM 838 C CE2 . PHE A 1 106 ? 40.802 28.047 18.722 1.00 28.13 ? 106 PHE A CE2 1
ATOM 839 C CZ . PHE A 1 106 ? 41.502 28.982 19.477 1.00 28.84 ? 106 PHE A CZ 1
ATOM 840 N N . GLN A 1 107 ? 42.135 24.342 21.697 1.00 21.88 ? 107 GLN A N 1
ATOM 841 C CA . GLN A 1 107 ? 40.928 24.014 22.445 1.00 21.85 ? 107 GLN A CA 1
ATOM 842 C C . GLN A 1 107 ? 39.778 24.952 22.115 1.00 21.69 ? 107 GLN A C 1
ATOM 843 O O . GLN A 1 107 ? 39.983 26.138 21.888 1.00 20.72 ? 107 GLN A O 1
ATOM 844 C CB . GLN A 1 107 ? 41.201 24.054 23.953 1.00 25.83 ? 107 GLN A CB 1
ATOM 845 C CG . GLN A 1 107 ? 42.185 22.997 24.445 1.00 28.15 ? 107 GLN A CG 1
ATOM 846 C CD . GLN A 1 107 ? 41.755 21.589 24.079 1.00 31.56 ? 107 GLN A CD 1
ATOM 847 O OE1 . GLN A 1 107 ? 40.644 21.162 24.400 1.00 33.35 ? 107 GLN A OE1 1
ATOM 848 N NE2 . GLN A 1 107 ? 42.636 20.859 23.404 1.00 32.61 ? 107 GLN A NE2 1
ATOM 849 N N . PRO A 1 108 ? 38.544 24.422 22.079 1.00 21.54 ? 108 PRO A N 1
ATOM 850 C CA . PRO A 1 108 ? 37.365 25.234 21.775 1.00 22.05 ? 108 PRO A CA 1
ATOM 851 C C . PRO A 1 108 ? 37.168 26.290 22.856 1.00 21.38 ? 108 PRO A C 1
ATOM 852 O O . PRO A 1 108 ? 37.507 26.071 24.015 1.00 21.34 ? 108 PRO A O 1
ATOM 853 C CB . PRO A 1 108 ? 36.226 24.213 21.780 1.00 20.00 ? 108 PRO A CB 1
ATOM 854 C CG . PRO A 1 108 ? 36.905 22.927 21.442 1.00 22.30 ? 108 PRO A CG 1
ATOM 855 C CD . PRO A 1 108 ? 38.169 23.010 22.250 1.00 22.74 ? 108 PRO A CD 1
ATOM 856 N N . VAL A 1 109 ? 36.626 27.434 22.471 1.00 22.12 ? 109 VAL A N 1
ATOM 857 C CA . VAL A 1 109 ? 36.368 28.503 23.421 1.00 22.47 ? 109 VAL A CA 1
ATOM 858 C C . VAL A 1 109 ? 34.920 28.950 23.251 1.00 24.24 ? 109 VAL A C 1
ATOM 859 O O . VAL A 1 109 ? 34.312 28.720 22.206 1.00 23.32 ? 109 VAL A O 1
ATOM 860 C CB . VAL A 1 109 ? 37.321 29.692 23.196 1.00 21.32 ? 109 VAL A CB 1
ATOM 861 C CG1 . VAL A 1 109 ? 38.758 29.260 23.488 1.00 19.10 ? 109 VAL A CG1 1
ATOM 862 C CG2 . VAL A 1 109 ? 37.200 30.197 21.766 1.00 18.68 ? 109 VAL A CG2 1
ATOM 863 N N . LYS A 1 110 ? 34.367 29.572 24.286 1.00 24.75 ? 110 LYS A N 1
ATOM 864 C CA . LYS A 1 110 ? 32.984 30.027 24.254 1.00 26.28 ? 110 LYS A CA 1
ATOM 865 C C . LYS A 1 110 ? 32.881 31.534 24.457 1.00 26.55 ? 110 LYS A C 1
ATOM 866 O O . LYS A 1 110 ? 33.825 32.175 24.917 1.00 24.64 ? 110 LYS A O 1
ATOM 867 C CB . LYS A 1 110 ? 32.187 29.337 25.359 1.00 27.41 ? 110 LYS A CB 1
ATOM 868 C CG . LYS A 1 110 ? 32.618 29.772 26.753 1.00 27.80 ? 110 LYS A CG 1
ATOM 869 C CD . LYS A 1 110 ? 31.844 29.058 27.832 1.00 31.68 ? 110 LYS A CD 1
ATOM 870 C CE . LYS A 1 110 ? 32.383 29.413 29.205 1.00 33.95 ? 110 LYS A CE 1
ATOM 871 N NZ . LYS A 1 110 ? 31.791 28.544 30.258 1.00 39.09 ? 110 LYS A NZ 1
ATOM 872 N N . TYR A 1 111 ? 31.719 32.081 24.114 1.00 28.40 ? 111 TYR A N 1
ATOM 873 C CA . TYR A 1 111 ? 31.438 33.505 24.271 1.00 31.13 ? 111 TYR A CA 1
ATOM 874 C C . TYR A 1 111 ? 29.960 33.764 23.994 1.00 33.79 ? 111 TYR A C 1
ATOM 875 O O . TYR A 1 111 ? 29.332 33.051 23.211 1.00 31.85 ? 111 TYR A O 1
ATOM 876 C CB . TYR A 1 111 ? 32.324 34.346 23.338 1.00 29.13 ? 111 TYR A CB 1
ATOM 877 C CG . TYR A 1 111 ? 32.050 34.192 21.855 1.00 28.50 ? 111 TYR A CG 1
ATOM 878 C CD1 . TYR A 1 111 ? 31.041 34.922 21.228 1.00 27.03 ? 111 TYR A CD1 1
ATOM 879 C CD2 . TYR A 1 111 ? 32.814 33.326 21.076 1.00 28.38 ? 111 TYR A CD2 1
ATOM 880 C CE1 . TYR A 1 111 ? 30.802 34.794 19.864 1.00 26.14 ? 111 TYR A CE1 1
ATOM 881 C CE2 . TYR A 1 111 ? 32.583 33.187 19.714 1.00 26.85 ? 111 TYR A CE2 1
ATOM 882 C CZ . TYR A 1 111 ? 31.578 33.922 19.114 1.00 27.64 ? 111 TYR A CZ 1
ATOM 883 O OH . TYR A 1 111 ? 31.342 33.766 17.769 1.00 27.72 ? 111 TYR A OH 1
ATOM 884 N N . SER A 1 112 ? 29.408 34.775 24.656 1.00 38.13 ? 112 SER A N 1
ATOM 885 C CA . SER A 1 112 ? 28.004 35.130 24.492 1.00 42.77 ? 112 SER A CA 1
ATOM 886 C C . SER A 1 112 ? 27.781 35.946 23.230 1.00 45.36 ? 112 SER A C 1
ATOM 887 O O . SER A 1 112 ? 28.313 37.047 23.090 1.00 47.50 ? 112 SER A O 1
ATOM 888 C CB . SER A 1 112 ? 27.514 35.921 25.705 1.00 42.81 ? 112 SER A CB 1
ATOM 889 O OG . SER A 1 112 ? 27.537 35.116 26.871 1.00 45.90 ? 112 SER A OG 1
ATOM 890 N N . ALA A 1 113 ? 26.987 35.399 22.316 1.00 47.86 ? 113 ALA A N 1
ATOM 891 C CA . ALA A 1 113 ? 26.688 36.069 21.058 1.00 49.45 ? 113 ALA A CA 1
ATOM 892 C C . ALA A 1 113 ? 25.368 36.826 21.155 1.00 50.27 ? 113 ALA A C 1
ATOM 893 O O . ALA A 1 113 ? 24.705 36.808 22.193 1.00 51.68 ? 113 ALA A O 1
ATOM 894 C CB . ALA A 1 113 ? 26.629 35.043 19.922 1.00 49.49 ? 113 ALA A CB 1
ATOM 895 N N . GLU A 1 119 ? 17.059 36.895 23.201 1.00 62.70 ? 119 GLU A N 1